]> http://creativecommons.org/licenses/by/3.0/ OTCS is a biological ontology of Two Component Systems. Hsin-Hui Huang mailto:yongqunh@med.umich.edu 5-15-2019 A biological ontology in the area of Two Component Systems. Yongqun "Oliver" He (YH) Vision Release: 1.0.01 Meng Liu OTCS: Ontology of Two Component Systems OWL-DL obo:bfo/axiom/165 obo:bfo/axiom/0000568 obo:bfo/axiom/567 obo:bfo/axiom/564 obo:bfo/axiom/566 obo:bfo/axiom/565 obo:bfo/axiom/565 obo:bfo/axiom/567 obo:bfo/axiom/566 obo:bfo/axiom/170 obo:bfo/axiom/539 obo:bfo/axiom/593 obo:bfo/axiom/589 obo:bfo/axiom/589 obo:bfo/axiom/585 obo:bfo/axiom/585 obo:bfo/axiom/585 obo:bfo/axiom/585 obo:bfo/axiom/575 obo:bfo/axiom/576 obo:bfo/axiom/109 obo:bfo/axiom/109 obo:bfo/axiom/163 obo:bfo/axiom/164 obo:bfo/axiom/592 obo:bfo/axiom/592 obo:bfo/axiom/590 obo:bfo/axiom/108 obo:bfo/axiom/108 obo:bfo/axiom/166 obo:bfo/axiom/165 obo:bfo/axiom/111 obo:bfo/axiom/110 obo:bfo/axiom/579 obo:bfo/axiom/579 obo:bfo/axiom/578 obo:bfo/axiom/578 obo:bfo/axiom/583 obo:bfo/axiom/583 obo:bfo/axiom/577 obo:bfo/axiom/0000601 obo:bfo/axiom/577 obo:bfo/axiom/548 obo:bfo/axiom/0000602 obo:bfo/axiom/587 obo:bfo/axiom/587 obo:bfo/axiom/580 obo:bfo/axiom/580 obo:bfo/axiom/584 obo:bfo/axiom/584 obo:bfo/axiom/557 obo:bfo/axiom/588 obo:bfo/axiom/588 obo:bfo/axiom/171 obo:bfo/axiom/113 obo:bfo/axiom/151 obo:bfo/axiom/112 obo:bfo/axiom/595 obo:bfo/axiom/596 obo:bfo/axiom/597 obo:bfo/axiom/029-001 obo:bfo/axiom/029-001 obo:bfo/axiom/586 obo:bfo/axiom/029-001 obo:bfo/axiom/586 obo:bfo/axiom/581 obo:bfo/axiom/028-001 obo:bfo/axiom/581 obo:bfo/axiom/028-001 obo:bfo/axiom/582 obo:bfo/axiom/582 obo:bfo/axiom/_ obo:bfo/axiom/591 obo:bfo/axiom/591 obo:bfo/axiom/121 obo:bfo/axiom/177 obo:bfo/axiom/175 obo:bfo/axiom/175 obo:bfo/axiom/177 obo:bfo/axiom/106 obo:bfo/axiom/117 obo:bfo/axiom/129 obo:bfo/axiom/106 obo:bfo/axiom/138 obo:bfo/axiom/117 obo:bfo/axiom/129 obo:bfo/axiom/138 obo:bfo/axiom/501 obo:bfo/axiom/501 obo:bfo/axiom/517 obo:bfo/axiom/518 obo:bfo/axiom/157 obo:bfo/axiom/156 obo:bfo/axiom/538 obo:bfo/axiom/537 obo:bfo/axiom/534 obo:bfo/axiom/533 obo:bfo/axiom/178 obo:bfo/axiom/180 obo:bfo/axiom/521 obo:bfo/axiom/519 obo:bfo/axiom/523 obo:bfo/axiom/041-002 obo:bfo/axiom/529 obo:bfo/axiom/530 obo:bfo/axiom/525 obo:bfo/axiom/101 obo:bfo/axiom/531 obo:bfo/axiom/509 obo:bfo/axiom/105 obo:bfo/axiom/115 obo:bfo/axiom/154 obo:bfo/axiom/128 obo:bfo/axiom/516 obo:bfo/axiom/513 obo:bfo/axiom/528 obo:bfo/axiom/148 obo:bfo/axiom/532 obo:bfo/axiom/508 obo:bfo/axiom/147 obo:bfo/axiom/104 obo:bfo/axiom/153 obo:bfo/axiom/136 obo:bfo/axiom/114 obo:bfo/axiom/127 obo:bfo/axiom/535 obo:bfo/axiom/536 obo:bfo/axiom/159 obo:bfo/axiom/160 obo:bfo/axiom/539 obo:bfo/axiom/540 obo:bfo/axiom/102 obo:bfo/axiom/518 obo:bfo/axiom/532 obo:bfo/axiom/527 obo:bfo/axiom/512 obo:bfo/axiom/507 obo:bfo/axiom/506 obo:bfo/axiom/502 obo:bfo/axiom/503 obo:bfo/axiom/137 obo:bfo/axiom/173 obo:bfo/axiom/172 obo:bfo/axiom/502 obo:bfo/axiom/503 obo:bfo/axiom/518 obo:bfo/axiom/517 obo:bfo/axiom/156 obo:bfo/axiom/157 obo:bfo/axiom/537 obo:bfo/axiom/538 obo:bfo/axiom/533 obo:bfo/axiom/534 obo:bfo/axiom/180 obo:bfo/axiom/178 obo:bfo/axiom/516 obo:bfo/axiom/530 obo:bfo/axiom/521 obo:bfo/axiom/519 obo:bfo/axiom/523 obo:bfo/axiom/529 obo:bfo/axiom/102 obo:bfo/axiom/525 obo:bfo/axiom/532 obo:bfo/axiom/508 obo:bfo/axiom/104 obo:bfo/axiom/114 obo:bfo/axiom/153 obo:bfo/axiom/127 obo:bfo/axiom/0000601 obo:bfo/axiom/041-002 obo:bfo/axiom/512 obo:bfo/axiom/527 obo:bfo/axiom/147 obo:bfo/axiom/531 obo:bfo/axiom/509 obo:bfo/axiom/148 obo:bfo/axiom/105 obo:bfo/axiom/154 obo:bfo/axiom/137 obo:bfo/axiom/115 obo:bfo/axiom/128 obo:bfo/axiom/536 obo:bfo/axiom/535 obo:bfo/axiom/160 obo:bfo/axiom/159 obo:bfo/axiom/540 obo:bfo/axiom/539 obo:bfo/axiom/101 obo:bfo/axiom/517 obo:bfo/axiom/519 obo:bfo/axiom/521 obo:bfo/axiom/523 obo:bfo/axiom/525 obo:bfo/axiom/531 obo:bfo/axiom/528 obo:bfo/axiom/513 obo:bfo/axiom/506 obo:bfo/axiom/507 obo:bfo/axiom/503 obo:bfo/axiom/502 obo:bfo/axiom/136 obo:bfo/axiom/172 obo:bfo/axiom/173 obo:bfo/axiom/503 obo:bfo/axiom/502 obo:bfo/axiom/106-002 obo:bfo/axiom/573 http://example.com/bfo-spec-label Person:Alan Ruttenberg obo:ARO_0000000 Macrolides are a group of drugs (typically antibiotics) that have a large macrocyclic lactone ring of 12-16 carbons to which one or more deoxy sugars, usually cladinose and desosamine, may be attached. Macrolides bind to the 50S-subunit of bacterial ribosomes, inhibiting the synthesis of vital proteins. obo:ARO_0000000 obo:aro.owl obo:ARO_0000000 antibiotic_resistance obo:ARO_0000000 ARO:0000000 obo:ARO_0000000 macrolide antibiotic obo:ARO_0000001 The fluoroquinolones are a family of synthetic broad-spectrum antibiotics that are 4-quinolone-3-carboxylates. These compounds interact with topoisomerase II (DNA gyrase) to disrupt bacterial DNA replication, damage DNA, and cause cell death. obo:ARO_0000001 obo:aro.owl obo:ARO_0000001 quinolone obo:ARO_0000001 antibiotic_resistance obo:ARO_0000001 ARO:0000001 obo:ARO_0000001 fluoroquinolone antibiotic obo:ARO_0000003 Astromicin is an aminoglycoside antibiotic used to treat different types of bacterial infections. Astromicin works by binding to the bacterial 30S ribosomal subunit, causing misreading of mRNA and leaving the bacterium unable to synthesize proteins vital to its growth. obo:ARO_0000003 obo:aro.owl obo:ARO_0000003 PubChem:5284517 obo:ARO_0000003 Astromicina obo:ARO_0000003 Astromicine obo:ARO_0000003 Astromicinum obo:ARO_0000003 fortimicin A obo:ARO_0000003 antibiotic_resistance obo:ARO_0000003 ARO:0000003 obo:ARO_0000003 astromicin obo:ARO_0000004 Monobactams are a class of beta-lactam antibiotics with a broad spectrum of antibacterial activity, and have a structure which renders them highly resistant to beta-lactamases. Unlike penams and cephems, monobactams do not have any ring fused to its four-member lactam structure. Monobactam antibiotics are bactericidal, and act by inhibiting the synthesis of the peptidoglycan layer of bacterial cell walls. The peptidoglycan layer is important for cell wall structural integrity, especially in Gram-positive organisms. obo:ARO_0000004 obo:aro.owl obo:ARO_0000004 antibiotic_resistance obo:ARO_0000004 ARO:0000004 obo:ARO_0000004 monobactam obo:ARO_0000005 Neomycin is an aminoglycoside antibiotic used to treat different types of bacterial infections. Neomycin works by binding to the bacterial 30S ribosomal subunit, causing misreading of mRNA and leaving the bacterium unable to synthesize proteins vital to its growth. obo:ARO_0000005 obo:aro.owl obo:ARO_0000005 PubChem:8378 obo:ARO_0000005 Fradiomycin obo:ARO_0000005 Fradiomycinum obo:ARO_0000005 Framycetinum obo:ARO_0000005 Mycifradin obo:ARO_0000005 Neomas obo:ARO_0000005 Soframycin obo:ARO_0000005 framycetin obo:ARO_0000005 neomycin B obo:ARO_0000005 antibiotic_resistance obo:ARO_0000005 ARO:0000005 obo:ARO_0000005 neomycin obo:ARO_0000006 Erythromycin is a macrolide antibiotic with a 14-carbon ring that has an antimicrobial spectrum similar to or slightly wider than that of penicillin, and is often used for people that have an allergy to penicillins. Erythromycin may possess bacteriocidal activity, particularly at higher concentrations by binding to the 50S subunit of the bacterial 70S rRNA complex, inhibiting peptidyl-tRNA translocation. Thus, protein synthesis and subsequently structure/function processes critical for life or replication are inhibited. obo:ARO_0000006 obo:aro.owl obo:ARO_0000006 PubChem:12560 obo:ARO_0000006 Abomacetin obo:ARO_0000006 Emgel obo:ARO_0000006 Eritromicina obo:ARO_0000006 Erymax obo:ARO_0000006 Erythrocin obo:ARO_0000006 Erythromycin A obo:ARO_0000006 Erythromycine obo:ARO_0000006 Erythromycinum obo:ARO_0000006 N-methylerythromycin A obo:ARO_0000006 antibiotic_resistance obo:ARO_0000006 ARO:0000006 obo:ARO_0000006 erythromycin obo:ARO_0000007 Dibekacin is an aminoglycoside antibiotic used to treat different types of bacterial infections. Dibekacin works by binding to the bacterial 30S ribosomal subunit, causing misreading of mRNA and leaving the bacterium unable to synthesize proteins vital to its growth. obo:ARO_0000007 obo:aro.owl obo:ARO_0000007 PubChem:470999 obo:ARO_0000007 Debecacin obo:ARO_0000007 Dibekacina obo:ARO_0000007 Dibekacine obo:ARO_0000007 Dibekacinum obo:ARO_0000007 Dideoxykanamycin B obo:ARO_0000007 Icacine obo:ARO_0000007 Kappati obo:ARO_0000007 Orbicin obo:ARO_0000007 Panamicin obo:ARO_0000007 antibiotic_resistance obo:ARO_0000007 ARO:0000007 obo:ARO_0000007 dibekacin obo:ARO_0000008 Cefoxitin is a cephamycin antibiotic often grouped with the second generation cephalosporins. Cefoxitin is bactericidal and acts by inhibiting the synthesis of the peptidoglycan layer of bacterial cell walls. The peptidoglycan layer is important for cell wall structural integrity, especially in Gram-positive organisms. Cefoxitin's 7-alpha-methoxy group and 3' leaving group make it a poor substrate for most beta-lactamases. obo:ARO_0000008 obo:aro.owl obo:ARO_0000008 PubChem:441199 obo:ARO_0000008 Cefoxitin obo:ARO_0000008 FOX obo:ARO_0000008 Mefoxitin obo:ARO_0000008 mefoxin obo:ARO_0000008 antibiotic_resistance obo:ARO_0000008 ARO:0000008 obo:ARO_0000008 cefoxitin obo:ARO_0000011 Cloxacillin is a semisynthetic, isoxazolyl penicillin derivative in the beta-lactam class of antibiotics. It interferes with peptidogylcan synthesis and is commonly used for treating penicillin-resistant Staphylococcus aureus infections. obo:ARO_0000011 obo:aro.owl obo:ARO_0000011 PubChem:6098 obo:ARO_0000011 Chloroxacillin obo:ARO_0000011 Clossacillina obo:ARO_0000011 Cloxacilina obo:ARO_0000011 Cloxacilline obo:ARO_0000011 Cloxacillinum obo:ARO_0000011 Cloxapen obo:ARO_0000011 Methocillin S obo:ARO_0000011 Orbenin obo:ARO_0000011 Syntarpen obo:ARO_0000011 Tegopen obo:ARO_0000011 antibiotic_resistance obo:ARO_0000011 ARO:0000011 obo:ARO_0000011 cloxacillin obo:ARO_0000013 Amikacin is an aminoglycoside antibiotic that works by binding to the bacterial 30S ribosomal subunit, causing misreading of mRNA and leaving the bacterium unable to synthesize proteins vital to its growth. obo:ARO_0000013 obo:aro.owl obo:ARO_0000013 PubChem:37768 obo:ARO_0000013 AMK obo:ARO_0000013 Amicacin obo:ARO_0000013 Amikacina obo:ARO_0000013 Amikacinum obo:ARO_0000013 Amikavet obo:ARO_0000013 Arikace obo:ARO_0000013 Kaminax obo:ARO_0000013 Lukadin obo:ARO_0000013 Mikavir obo:ARO_0000013 amikacine obo:ARO_0000013 mikacin obo:ARO_0000013 antibiotic_resistance obo:ARO_0000013 ARO:0000013 obo:ARO_0000013 amikacin obo:ARO_0000014 Gentamicin C is a mixture of gentamicin C1, gentamicin C1a, and gentamicin C2 (these differ in substituents at position C6'). Gentamicin works by binding to the bacterial 30S ribosomal subunit, causing misreading of mRNA and leaving the bacterium unable to synthesize proteins vital to its growth. obo:ARO_0000014 obo:aro.owl obo:ARO_0000014 PubChem:3084091 obo:ARO_0000014 Cidomycin obo:ARO_0000014 Garamycin obo:ARO_0000014 Gentacycol obo:ARO_0000014 Gentamicins obo:ARO_0000014 Gentamycinum obo:ARO_0000014 Gentavet obo:ARO_0000014 Gentocin obo:ARO_0000014 Refobacin obo:ARO_0000014 Uromycine obo:ARO_0000014 antibiotic_resistance obo:ARO_0000014 ARO:0000014 obo:ARO_0000014 gentamicin C obo:ARO_0000015 Derived from penicillin to combat penicillin-resistance, methicillin is insensitive to beta-lactamases (also known as penicillinases) secreted by many penicillin-resistant bacteria. Methicillin is bactericidal, and acts by inhibiting the synthesis of the peptidoglycan layer of bacterial cell walls. The peptidoglycan layer is important for cell wall structural integrity, especially in Gram-positive organisms. obo:ARO_0000015 obo:aro.owl obo:ARO_0000015 PubChem:6087 obo:ARO_0000015 Dimocillin obo:ARO_0000015 Metacillin obo:ARO_0000015 Methicillinum obo:ARO_0000015 Methycillin obo:ARO_0000015 Meticilina obo:ARO_0000015 Meticilline obo:ARO_0000015 Meticillinum obo:ARO_0000015 Staphcillin obo:ARO_0000015 meticillin obo:ARO_0000015 antibiotic_resistance obo:ARO_0000015 ARO:0000015 obo:ARO_0000015 methicillin obo:ARO_0000016 Aminoglycosides are a group of antibiotics that are mostly effective against Gram-negative bacteria. These molecules consist of aminated sugars attached to a dibasic cyclitol. Aminoglycosides work by binding to the bacterial 30S ribosomal subunit (some work by binding to the 50S subunit), inhibiting the translocation of the peptidyl-tRNA from the A-site to the P-site and also causing misreading of mRNA, leaving the bacterium unable to synthesize proteins vital to its growth. obo:ARO_0000016 obo:aro.owl obo:ARO_0000016 antibiotic_resistance obo:ARO_0000016 ARO:0000016 obo:ARO_0000016 aminoglycoside antibiotic obo:ARO_0000020 Carbapenems are a class of beta-lactam antibiotics with a broad spectrum of antibacterial activity, and have a structure which renders them highly resistant to beta-lactamases. Carbapenem antibiotics are bactericidal, and act by inhibiting the synthesis of the peptidoglycan layer of bacterial cell walls. The peptidoglycan layer is important for cell wall structural integrity, especially in Gram-positive organisms. obo:ARO_0000020 obo:aro.owl obo:ARO_0000020 antibiotic_resistance obo:ARO_0000020 ARO:0000020 obo:ARO_0000020 carbapenem obo:ARO_0000021 Ribostamycin is an aminoglycoside antibiotic used to treat different types of bacterial infections. Ribostamycin works by binding to the bacterial 30S ribosomal subunit, causing misreading of mRNA and leaving the bacterium unable to synthesize proteins vital to its growth. obo:ARO_0000021 obo:aro.owl obo:ARO_0000021 PubChem:33042 obo:ARO_0000021 dekamycin IV obo:ARO_0000021 hetangmycin obo:ARO_0000021 ribastamin obo:ARO_0000021 ribostamycin obo:ARO_0000021 vistamycin obo:ARO_0000021 xylostatin obo:ARO_0000021 antibiotic_resistance obo:ARO_0000021 ARO:0000021 obo:ARO_0000021 ribostamycin obo:ARO_0000022 Polymyxins are cationic detergent antibiotics, with a general structure of a cyclic peptide with a long hydrophobic tail. They disrupt the structure of the bacterial cell membrane by interacting with its phospholipids. Polymyxins have a bactericidal effect on Gram-negative bacilli, especially on Pseudomonas and coliform organisms. obo:ARO_0000022 obo:aro.owl obo:ARO_0000022 antibiotic_resistance obo:ARO_0000022 ARO:0000022 obo:ARO_0000022 polymyxin antibiotic obo:ARO_0000023 Enoxacin belongs to a group called fluoroquinolones. Its mode of action depends upon blocking bacterial DNA replication by binding itself to DNA gyrase and causing double-stranded breaks in the bacterial chromosome. obo:ARO_0000023 obo:aro.owl obo:ARO_0000023 PubChem:3229 obo:ARO_0000023 Enroxil obo:ARO_0000023 Penetrex obo:ARO_0000023 antibiotic_resistance obo:ARO_0000023 ARO:0000023 obo:ARO_0000023 enoxacin obo:ARO_0000024 Butirosin is an aminoglycoside antibiotic used to treat different types of bacterial infections. Butirosin works by binding to the bacterial 30S ribosomal subunit, causing misreading of mRNA and leaving the bacterium unable to synthesize proteins vital to its growth. obo:ARO_0000024 obo:aro.owl obo:ARO_0000024 PubChem:72393 obo:ARO_0000024 ambutyrosin sulfate obo:ARO_0000024 butirosin sulphate obo:ARO_0000024 antibiotic_resistance obo:ARO_0000024 ARO:0000024 obo:ARO_0000024 butirosin obo:ARO_0000027 Roxithromycin is a semi-synthetic, 14-carbon ring macrolide antibiotic derived from erythromycin. It is used to treat respiratory tract, urinary and soft tissue infections. Roxithromycin may possess bacteriocidal activity, particularly at higher concentrations by binding to the 50S subunit of the bacterial 70S rRNA complex, protein synthesis and subsequently structure/function processes critical for life or replication are inhibited. obo:ARO_0000027 obo:aro.owl obo:ARO_0000027 PubChem:6915744 obo:ARO_0000027 antibiotic_resistance obo:ARO_0000027 ARO:0000027 obo:ARO_0000027 roxithromycin obo:ARO_0000028 Vancomycin is a glycopeptide antibiotic used in the prophylaxis and treatment of infections caused by Gram-positive bacteria. Vancomycin inhibits the synthesis of peptidoglycan, the major component of the cell wall of gram-positive bacteria. Its mechanism of action is unusual in that it acts by binding precursors of peptidoglycan, rather than by interacting with an enzyme. obo:ARO_0000028 obo:aro.owl obo:ARO_0000028 PubChem:14969 obo:ARO_0000028 Vancocin obo:ARO_0000028 antibiotic_resistance obo:ARO_0000028 ARO:0000028 obo:ARO_0000028 vancomycin obo:ARO_0000029 Teicoplanin is a glycopeptide antibiotic used in the prophylaxis and treatment of serious infections caused by Gram-positive bacteria. Teicoplanin has a unique acyl-aliphatic chain, and binds to cell wall precursors to inhibit transglycosylation and transpeptidation. obo:ARO_0000029 obo:aro.owl obo:ARO_0000029 PubChem:16129712 obo:ARO_0000029 targocid obo:ARO_0000029 teichomycin obo:ARO_0000029 antibiotic_resistance obo:ARO_0000029 ARO:0000029 obo:ARO_0000029 teicoplanin obo:ARO_0000030 Tigecycline is an glycylcycline antibiotic. It works by inhibiting action of the prokaryotic 30S ribosome. obo:ARO_0000030 obo:aro.owl obo:ARO_0000030 PubChem:54686904 obo:ARO_0000030 Tygacil obo:ARO_0000030 antibiotic_resistance obo:ARO_0000030 ARO:0000030 obo:ARO_0000030 tigecycline obo:ARO_0000032 Cephalosporins are a class of beta-lactam antibiotics, containing the beta-lactam ring fused with a dihydrothiazolidine ring. Together with cephamycins they belong to a sub-group called cephems. Cephalosporin are bactericidal, and act by inhibiting the synthesis of the peptidoglycan layer of bacterial cell walls. The peptidoglycan layer is important for cell wall structural integrity, especially in Gram-positive organisms. obo:ARO_0000032 obo:aro.owl obo:ARO_0000032 Cephems obo:ARO_0000032 antibiotic_resistance obo:ARO_0000032 ARO:0000032 obo:ARO_0000032 cephalosporin obo:ARO_0000035 Sisomicin is an aminoglycoside antibiotic used to treat different types of bacterial infections. Sisomicin works by binding to the bacterial 30S ribosomal subunit, causing misreading of mRNA and leaving the bacterium unable to synthesize proteins vital to its growth. obo:ARO_0000035 obo:aro.owl obo:ARO_0000035 PubChem:36119 obo:ARO_0000035 antibiotic 6640 obo:ARO_0000035 dehydrogentamicin obo:ARO_0000035 rickamicin obo:ARO_0000035 sisomycin obo:ARO_0000035 sissomicin obo:ARO_0000035 antibiotic_resistance obo:ARO_0000035 ARO:0000035 obo:ARO_0000035 sisomicin obo:ARO_0000036 Ciprofloxacin is a bacteriocidal fluoroquinolone. It blocks bacterial DNA replication by binding to the toposiomerase II or IV-DNA complex (or cleavable complex), thereby causing double-stranded breaks in the bacterial chromosome. obo:ARO_0000036 obo:aro.owl obo:ARO_0000036 PubChem:2764 obo:ARO_0000036 CIP obo:ARO_0000036 Cipro obo:ARO_0000036 Ciprobay obo:ARO_0000036 Ciproxan obo:ARO_0000036 antibiotic_resistance obo:ARO_0000036 ARO:0000036 obo:ARO_0000036 ciprofloxacin obo:ARO_0000037 Apramycin is an aminoglycoside antibiotic used to treat different types of bacterial infections in animals. Apramycin works by binding to the bacterial 30S ribosomal subunit, causing misreading of mRNA and leaving the bacterium unable to synthesize proteins vital to its growth. obo:ARO_0000037 obo:aro.owl obo:ARO_0000037 PubChem:3081545 obo:ARO_0000037 ambylan obo:ARO_0000037 apralan obo:ARO_0000037 nebramycin II obo:ARO_0000037 antibiotic_resistance obo:ARO_0000037 ARO:0000037 obo:ARO_0000037 apramycin obo:ARO_0000038 Netilmicin is a member of the aminoglycoside family of antibiotics. These antibiotics have the ability to kill a wide variety of bacteria by binding to the bacterial 30S ribosomal subunit, causing misreading of mRNA and leaving the bacterium unable to synthesize proteins vital to its growth. Netilmicin is not absorbed from the gut and is therefore only given by injection or infusion. It is only used in the treatment of serious infections particularly those resistant to gentamicin. obo:ARO_0000038 obo:aro.owl obo:ARO_0000038 PubChem:441306 obo:ARO_0000038 1-N-aethylsisomicin obo:ARO_0000038 netilyn obo:ARO_0000038 netromycin obo:ARO_0000038 vectacin obo:ARO_0000038 antibiotic_resistance obo:ARO_0000038 ARO:0000038 obo:ARO_0000038 netilmicin obo:ARO_0000039 Spectinomycin is an aminoglycoside antibiotic used to treat different types of bacterial infections. Spectinomycin works by binding to the bacterial 30S ribosomal subunit inhibiting translation. obo:ARO_0000039 obo:aro.owl obo:ARO_0000039 PubChem:15541 obo:ARO_0000039 Actinospectacin obo:ARO_0000039 Spectam obo:ARO_0000039 Togamycin obo:ARO_0000039 Trobicin obo:ARO_0000039 antibiotic_resistance obo:ARO_0000039 ARO:0000039 obo:ARO_0000039 spectinomycin obo:ARO_0000040 Streptomycin is an aminoglycoside antibiotic used to treat different types of bacterial infections. Streptomycin works by binding to the bacterial 30S ribosomal subunit, causing misreading of mRNA and leaving the bacterium unable to synthesize proteins vital to its growth. obo:ARO_0000040 obo:aro.owl obo:ARO_0000040 PubChem:19649 obo:ARO_0000040 streptomycin A obo:ARO_0000040 streptomycin A sulfate obo:ARO_0000040 streptomycin sulfate obo:ARO_0000040 streptomycin sulphate obo:ARO_0000040 antibiotic_resistance obo:ARO_0000040 ARO:0000040 obo:ARO_0000040 streptomycin obo:ARO_0000042 Glycylcyclines are a new class of antibiotics derived from tetracycline. These tetracycline analogues are specifically designed to overcome two common mechanisms of tetracycline resistance. Presently, there is only one glycylcycline antibiotic for clinical use: tigecycline. It works by inhibiting action of the prokaryotic 30S ribosome, preventing the binding of aminoacyl-tRNA. obo:ARO_0000042 obo:aro.owl obo:ARO_0000042 antibiotic_resistance obo:ARO_0000042 ARO:0000042 obo:ARO_0000042 glycylcycline obo:ARO_0000043 Carbenicillin is a semi-synthetic antibiotic belonging to the carboxypenicillin subgroup of the penicillins. It has gram-negative coverage which includes Pseudomonas aeruginosa but limited gram-positive coverage. The carboxypenicillins are susceptible to degradation by beta-lactamase enzymes. Carbenicillin antibiotics are bactericidal, and act by inhibiting the synthesis of the peptidoglycan layer of bacterial cell walls. The peptidoglycan layer is important for cell wall structural integrity, especially in Gram-positive organisms. obo:ARO_0000043 obo:aro.owl obo:ARO_0000043 PubChem:20824 obo:ARO_0000043 Anabactyl obo:ARO_0000043 CAR obo:ARO_0000043 Carbecin obo:ARO_0000043 Carbenicilina obo:ARO_0000043 Carbenicillina obo:ARO_0000043 Carbenicilline obo:ARO_0000043 Carbenicillinum obo:ARO_0000043 Geopen obo:ARO_0000043 Microcillin obo:ARO_0000043 Pyopen obo:ARO_0000043 antibiotic_resistance obo:ARO_0000043 ARO:0000043 obo:ARO_0000043 carbenicillin obo:ARO_0000044 Cephamycins are a group of beta-lactam antibiotics, very similar to cephalosporins. Together with cephalosporins, they form a sub-group of antibiotics known as cephems. Cephamycins are bactericidal, and act by inhibiting the synthesis of the peptidoglycan layer of bacterial cell walls. The peptidoglycan layer is important for cell wall structural integrity, especially in Gram-positive organisms. The 7-alpha-methoxy group increases resistance to beta-lactamases. obo:ARO_0000044 obo:aro.owl obo:ARO_0000044 cephems obo:ARO_0000044 PubChem:123731 obo:ARO_0000044 antibiotic_resistance obo:ARO_0000044 ARO:0000044 obo:ARO_0000044 cephamycin obo:ARO_0000049 Kanamycin is an aminoglycoside antibiotic used to treat different types of bacterial infections. Kanamycin works by binding to the bacterial 30S ribosomal subunit, causing misreading of mRNA and leaving the bacterium unable to synthesize proteins vital to its growth. obo:ARO_0000049 obo:aro.owl obo:ARO_0000049 PubChem:6032 obo:ARO_0000049 Aminodeoxykanamycin obo:ARO_0000049 Aspidium obo:ARO_0000049 Kanamicina obo:ARO_0000049 Kanamycin sulfate obo:ARO_0000049 Kanamycine obo:ARO_0000049 Kanamycinum obo:ARO_0000049 Kantrex obo:ARO_0000049 kanamycin A obo:ARO_0000049 antibiotic_resistance obo:ARO_0000049 ARO:0000049 obo:ARO_0000049 kanamycin A obo:ARO_0000051 Tetracycline is a broad-spectrum polyketide antibiotic produced by many Streptomyces. It works by inhibiting action of the prokaryotic 30S ribosome. obo:ARO_0000051 obo:aro.owl obo:ARO_0000051 PubChem:54675776 obo:ARO_0000051 Abricycline obo:ARO_0000051 Achromycin obo:ARO_0000051 Agromicina obo:ARO_0000051 Ambramicina obo:ARO_0000051 Ambramycin obo:ARO_0000051 Biocycline obo:ARO_0000051 Criseociclina obo:ARO_0000051 Enterocycline obo:ARO_0000051 Sumycin obo:ARO_0000051 Tsiklomistsin obo:ARO_0000051 antibiotic_resistance obo:ARO_0000051 ARO:0000051 obo:ARO_0000051 tetracycline obo:ARO_0000052 Tobramycin is an aminoglycoside antibiotic used to treat different types of bacterial infections. Tobramycin works by binding to the bacterial 30S ribosomal subunit, causing misreading of mRNA and leaving the bacterium unable to synthesize proteins vital to its growth. obo:ARO_0000052 obo:aro.owl obo:ARO_0000052 PubChem:36294 obo:ARO_0000052 Gotabiotic obo:ARO_0000052 Nebcin obo:ARO_0000052 Tenebrimycin obo:ARO_0000052 Tobracin obo:ARO_0000052 Tobradistin obo:ARO_0000052 Tobramaxin obo:ARO_0000052 Tobramicin obo:ARO_0000052 Tobramitsetin obo:ARO_0000052 Tobramycetin obo:ARO_0000052 Tobrex obo:ARO_0000052 antibiotic_resistance obo:ARO_0000052 ARO:0000052 obo:ARO_0000052 tobramycin obo:ARO_0000053 Bleomycin is a family of glycopeptide antibiotics produced by the bacterium Streptomyces verticillus. Bleomycins, taken as a mixture, act by the induction of DNA and RNA strand breaks. In addition to its antibacterial activity, bleomycin is also used as an anticancer agent. obo:ARO_0000053 obo:aro.owl obo:ARO_0000053 Blenoxane obo:ARO_0000053 Bleocin obo:ARO_0000053 Bleomicin obo:ARO_0000053 Bleomycin sulfate obo:ARO_0000053 Isobleomycin A2 obo:ARO_0000053 cu-blenoxane obo:ARO_0000053 antibiotic_resistance obo:ARO_0000053 ARO:0000053 obo:ARO_0000053 bleomycin obo:ARO_0000054 Penicillin (sometimes abbreviated PCN) is a beta-lactam antibiotic used in the treatment of bacterial infections caused by susceptible, usually Gram-positive, organisms. It works by inhibiting the synthesis of the peptidoglycan layer of bacterial cell walls. The peptidoglycan layer is important for cell wall structural integrity, especially in Gram-positive organisms. obo:ARO_0000054 obo:aro.owl obo:ARO_0000054 PubChem:2349 obo:ARO_0000054 Benzopenicillin obo:ARO_0000054 Benzylpenicillin obo:ARO_0000054 Cilopen obo:ARO_0000054 Dropcillin obo:ARO_0000054 Gelacillin obo:ARO_0000054 Liquacillin obo:ARO_0000054 PCN obo:ARO_0000054 Pharmacillin obo:ARO_0000054 Pradupen obo:ARO_0000054 Specilline G obo:ARO_0000054 penicillin g obo:ARO_0000054 antibiotic_resistance obo:ARO_0000054 ARO:0000054 obo:ARO_0000054 penicillin obo:ARO_0000056 Oxacillin is a penicillinase-resistant beta-lactam. It is similar to methicillin, and has replaced methicillin in clinical use. Oxacillin, especially in combination with other antibiotics, is effective against many penicillinase-producing strains of Staphylococcus aureus and Staphylococcus epidermidis. obo:ARO_0000056 obo:aro.owl obo:ARO_0000056 PubChem:6196 obo:ARO_0000056 MPI-penicillin obo:ARO_0000056 Ossacillina obo:ARO_0000056 Oxacilina obo:ARO_0000056 Oxacilline obo:ARO_0000056 Oxacillinum obo:ARO_0000056 Oxazocillin obo:ARO_0000056 Oxazocilline obo:ARO_0000056 Prostaphlin obo:ARO_0000056 Prostaphlyn obo:ARO_0000056 antibiotic_resistance obo:ARO_0000056 ARO:0000056 obo:ARO_0000056 oxacillin obo:ARO_0000057 Telithromycin is a semi-synthetic derivative of erythromycin. It is a 14-membered macrolide and is the first ketolide antibiotic to be used in clinics. Telithromycin binds the 50S subunit of the bacterial ribosome to inhibit protein synthesis. obo:ARO_0000057 obo:aro.owl obo:ARO_0000057 PubChem:3002190 obo:ARO_0000057 HMR-3647 obo:ARO_0000057 HMR3647 obo:ARO_0000057 Ketek obo:ARO_0000057 Levviax obo:ARO_0000057 antibiotic_resistance obo:ARO_0000057 ARO:0000057 obo:ARO_0000057 telithromycin obo:ARO_0000058 Cefazolin (INN), also known as cefazoline or cephazolin, is a first generation cephalosporin antibiotic. It is administered parenterally, and is active against a broad spectrum of bacteria. obo:ARO_0000058 obo:aro.owl obo:ARO_0000058 PubChem:33255 obo:ARO_0000058 CFZ obo:ARO_0000058 Cefamezin obo:ARO_0000058 Cefazolina obo:ARO_0000058 Cefazoline obo:ARO_0000058 Cefazolinum obo:ARO_0000058 Cephamezine obo:ARO_0000058 Cephazolidin obo:ARO_0000058 Cephazolin obo:ARO_0000058 Cephazoline obo:ARO_0000058 Elzogram obo:ARO_0000058 antibiotic_resistance obo:ARO_0000058 ARO:0000058 obo:ARO_0000058 cefazolin obo:ARO_0000059 Cefepime (INN) is a fourth-generation cephalosporin antibiotic developed in 1994. It contains an aminothiazolyl group that decreases its affinity with beta-lactamases. Cefepime shows high binding affinity with penicillin-binding proteins and has an extended spectrum of activity against Gram-positive and Gram-negative bacteria, with greater activity against both Gram-negative and Gram-positive organisms than third-generation agents. obo:ARO_0000059 obo:aro.owl obo:ARO_0000059 PubChem:5479537 obo:ARO_0000059 Axepim obo:ARO_0000059 Cefepima obo:ARO_0000059 Cefepimum obo:ARO_0000059 FEP obo:ARO_0000059 Maxipime obo:ARO_0000059 antibiotic_resistance obo:ARO_0000059 ARO:0000059 obo:ARO_0000059 cefepime obo:ARO_0000060 Ceftazidime is a third-generation cephalosporin antibiotic. Like other third-generation cephalosporins, it has broad spectrum activity against Gram-positive and Gram-negative bacteria. Unlike most third-generation agents, it is active against Pseudomonas aeruginosa, however it has weaker activity against Gram-positive microorganisms and is not used for such infections. obo:ARO_0000060 obo:aro.owl obo:ARO_0000060 PubChem:5481173 obo:ARO_0000060 CAZ obo:ARO_0000060 Ceftazidim obo:ARO_0000060 Ceptaz obo:ARO_0000060 Fortaz obo:ARO_0000060 Pentacef obo:ARO_0000060 Tazicef obo:ARO_0000060 Tazidime obo:ARO_0000060 avibactam obo:ARO_0000060 caftazidime obo:ARO_0000060 ceftazidima obo:ARO_0000060 ceftazidimum obo:ARO_0000060 antibiotic_resistance obo:ARO_0000060 ARO:0000060 obo:ARO_0000060 ceftazidime obo:ARO_0000061 Ceftobiprole (Zeftera/Zevtera) is a next generation (5th generation) cephalosporin antibiotic with activity against methicillin-resistant Staphylococcus aureus, penicillin-resistant Streptococcus pneumoniae, Pseudomonas aeruginosa, and Enterococci. Ceftobiprole inhibits transpeptidases essential to building cell walls, and is a poor substrate for most beta-lactamases. obo:ARO_0000061 obo:aro.owl obo:ARO_0000061 PubChem:135413542 obo:ARO_0000061 Ceftobiprole medocaril obo:ARO_0000061 Zeftera obo:ARO_0000061 Zevtera obo:ARO_0000061 antibiotic_resistance obo:ARO_0000061 ARO:0000061 obo:ARO_0000061 ceftobiprole obo:ARO_0000062 Ceftriaxone is a third-generation cephalosporin antibiotic. The presence of an aminothiazolyl sidechain increases ceftriazone's resistance to beta-lactamases. Like other third-generation cephalosporins, it has broad spectrum activity against Gram-positive and Gram-negative bacteria. obo:ARO_0000062 obo:aro.owl obo:ARO_0000062 PubChem:5479530 obo:ARO_0000062 Biotrakson obo:ARO_0000062 CRO obo:ARO_0000062 Cefatriaxone obo:ARO_0000062 Ceftriaxon obo:ARO_0000062 Ceftriaxona obo:ARO_0000062 Ceftriaxonum obo:ARO_0000062 Ceftriazone obo:ARO_0000062 Longacef obo:ARO_0000062 Longaceph obo:ARO_0000062 Rocephin obo:ARO_0000062 antibiotic_resistance obo:ARO_0000062 ARO:0000062 obo:ARO_0000062 ceftriaxone obo:ARO_0000063 Cefuroxime is a second-generation cephalosporin antibiotic with increased stability with beta-lactamases than first-generation cephalosporins. Cefuroxime is active against Gram-positive organisms but less active against methicillin-resistant strains. obo:ARO_0000063 obo:aro.owl obo:ARO_0000063 PubChem:5479529 obo:ARO_0000063 Biofuroksym obo:ARO_0000063 CXM obo:ARO_0000063 Cefuril obo:ARO_0000063 Cefuroxim obo:ARO_0000063 Cefuroximo obo:ARO_0000063 Cefuroximum obo:ARO_0000063 Cephuroxime obo:ARO_0000063 Sharox obo:ARO_0000063 Zinacef obo:ARO_0000063 antibiotic_resistance obo:ARO_0000063 ARO:0000063 obo:ARO_0000063 cefuroxime obo:ARO_0000064 Amoxicillin is a moderate-spectrum, bacteriolytic, beta-lactam antibiotic used to treat bacterial infections caused by susceptible microorganisms. A derivative of penicillin, it has a wider range of treatment but remains relatively ineffective against Gram-negative bacteria. It is commonly taken with clavulanic acid, a beta-lactamase inhibitor. Like other beta-lactams, amoxicillin interferes with the synthesis of peptidoglycan. obo:ARO_0000064 obo:aro.owl obo:ARO_0000064 PubChem:33613 obo:ARO_0000064 AMX obo:ARO_0000064 Amolin obo:ARO_0000064 Amopenixin obo:ARO_0000064 Amoxicilina obo:ARO_0000064 Amoxicilline obo:ARO_0000064 Amoxicillinum obo:ARO_0000064 Amoxycillin obo:ARO_0000064 Clamoxyl obo:ARO_0000064 D-Amoxicillin obo:ARO_0000064 Moxal obo:ARO_0000064 antibiotic_resistance obo:ARO_0000064 ARO:0000064 obo:ARO_0000064 amoxicillin obo:ARO_0000065 Clarithromycin is a methyl derivative of erythromycin, sharing the 14-carbon macrolide ring. The antibiotic binds to the 50S subunit of the ribosome and is used to treat pharyngitis, tonsillitis, acute maxillary sinusitis, acute bacterial exacerbation of chronic bronchitis, pneumonia (especially atypical pneumonias associated with Chlamydia pneumoniae or TWAR), and skin structure infections. obo:ARO_0000065 obo:aro.owl obo:ARO_0000065 PubChem:84029 obo:ARO_0000065 Biaxin obo:ARO_0000065 CLR obo:ARO_0000065 Clambiotic obo:ARO_0000065 Clarith obo:ARO_0000065 Clathromycin obo:ARO_0000065 Klacid obo:ARO_0000065 Klaricid obo:ARO_0000065 Macladin obo:ARO_0000065 Naxy obo:ARO_0000065 Veclam obo:ARO_0000065 antibiotic_resistance obo:ARO_0000065 ARO:0000065 obo:ARO_0000065 clarithromycin obo:ARO_0000067 Colistins are polymyxin antibiotics produced by certain strains of Bacillus polymyxa var. colistinus. Colistin, also referred to as polymyxin E, is a mixture of cyclic polypeptides colistin A and B which disrupt the bacterial cell membrane and is effective against Gram-negative bacteria. obo:ARO_0000067 obo:aro.owl obo:ARO_0000067 CST obo:ARO_0000067 Colomycin obo:ARO_0000067 polymyxin E obo:ARO_0000067 antibiotic_resistance obo:ARO_0000067 ARO:0000067 obo:ARO_0000067 colistin obo:ARO_0000069 Doxycycline is second generation semi-synthetic derivative of the tetracycline group of antibiotics. It inhibits bacterial protein synthesis by binding to the 30S subunit of the bacterial ribosome and preventing the aminotransferase-tRNA from associating with the ribosome. obo:ARO_0000069 obo:aro.owl obo:ARO_0000069 PubChem:54671203 obo:ARO_0000069 Azudoxat obo:ARO_0000069 Deoxymykoin obo:ARO_0000069 Doxiciclina obo:ARO_0000069 Doxitard obo:ARO_0000069 Doxycyclinum obo:ARO_0000069 Doxytetracycline obo:ARO_0000069 Vibramycin obo:ARO_0000069 Vibramycine obo:ARO_0000069 Vibravenos obo:ARO_0000069 antibiotic_resistance obo:ARO_0000069 ARO:0000069 obo:ARO_0000069 doxycycline obo:ARO_0000070 Ertapenem is a carbapenem antibiotic and is highly resistant to beta-lactamases like other carbapenems. It inhibits bacterial cell wall synthesis. obo:ARO_0000070 obo:aro.owl obo:ARO_0000070 PubChem:150610 obo:ARO_0000070 Invanz obo:ARO_0000070 antibiotic_resistance obo:ARO_0000070 ARO:0000070 obo:ARO_0000070 ertapenem obo:ARO_0000071 Levofloxacin is a synthetic chemotherapeutic antibiotic of the fluoroquinolone drug class. Its main target is topoisomerase IV, inhibiting its function and disrupting DNA replication. obo:ARO_0000071 obo:aro.owl obo:ARO_0000071 PubChem:149096 obo:ARO_0000071 Levaquin obo:ARO_0000071 Tavanic obo:ARO_0000071 antibiotic_resistance obo:ARO_0000071 ARO:0000071 obo:ARO_0000071 levofloxacin obo:ARO_0000073 Meropenem is an ultra-broad spectrum injectable antibiotic used to treat a wide variety of infections, including meningitis and pneumonia. It is a beta-lactam and belongs to the subgroup of carbapenem, similar to imipenem and ertapenem. obo:ARO_0000073 obo:aro.owl obo:ARO_0000073 PubChem:441130 obo:ARO_0000073 Meronem obo:ARO_0000073 Meropen obo:ARO_0000073 Meropenem anhydrous obo:ARO_0000073 Meropenemum obo:ARO_0000073 Merrem obo:ARO_0000073 meropenem obo:ARO_0000073 antibiotic_resistance obo:ARO_0000073 ARO:0000073 obo:ARO_0000073 meropenem obo:ARO_0000074 Moxifloxacin is a fourth generation synthetic fluoroquinolone chemotherapeutic agent, and has been shown to be significantly more active than levofloxacin (4 to 8 times more) against Streptococcus pneumoniae. It acts by inhibiting bacterial DNA topoisomerases. obo:ARO_0000074 obo:aro.owl obo:ARO_0000074 PubChem:152946 obo:ARO_0000074 Actira (hydrochloride) obo:ARO_0000074 Avelox obo:ARO_0000074 Avelox (hydrochloride) obo:ARO_0000074 MXFX obo:ARO_0000074 Moxifloxacin hydrochloride obo:ARO_0000074 Vigamox obo:ARO_0000074 antibiotic_resistance obo:ARO_0000074 ARO:0000074 obo:ARO_0000074 moxifloxacin obo:ARO_0000078 Piperacillin is an acetylureidopenicillin and has an extended spectrum of targets relative to other beta-lactam antibiotics. It inhibits cell wall synthesis in bacteria, and is usually taken with the beta-lactamase inhibitor tazobactam to overcome penicillin-resistant bacteria. obo:ARO_0000078 obo:aro.owl obo:ARO_0000078 PubChem:43672 obo:ARO_0000078 Piperacillin anhydrous obo:ARO_0000078 Piperacillin sodium obo:ARO_0000078 Pipercillin obo:ARO_0000078 Pipracil obo:ARO_0000078 Pipril obo:ARO_0000078 antibiotic_resistance obo:ARO_0000078 ARO:0000078 obo:ARO_0000078 piperacillin obo:ARO_0001001 Mutational alteration or enzymatic modification of antibiotic target which results in antibiotic resistance. obo:ARO_0001001 obo:aro.owl obo:ARO_0001001 antibiotic target alteration obo:ARO_0001001 antibiotic_resistance obo:ARO_0001001 ARO:0001001 obo:ARO_0001001 antibiotic target alteration obo:ARO_0001003 Protection of antibiotic action target from antibiotic binding, which process will result in antibiotic resistance. obo:ARO_0001003 obo:aro.owl obo:ARO_0001003 antibiotic_resistance obo:ARO_0001003 ARO:0001003 obo:ARO_0001003 antibiotic target protection obo:ARO_0001004 Enzymatic inactivation of antibiotic to confer drug resistance. obo:ARO_0001004 obo:aro.owl obo:ARO_0001004 drug enzymatic inactivation obo:ARO_0001004 drug enzymatic modification obo:ARO_0001004 antibiotic_resistance obo:ARO_0001004 ARO:0001004 obo:ARO_0001004 antibiotic inactivation obo:ARO_0010000 Antibiotic resistance via the transport of antibiotics out of the cell. obo:ARO_0010000 obo:aro.owl obo:ARO_0010000 antibiotic_resistance obo:ARO_0010000 ARO:0010000 obo:ARO_0010000 antibiotic efflux obo:ARO_3000007 Beta-lactam antibiotics are a broad class of antibiotics that include penams (penicillin derivatives), cephems (cephalosporins), monobactams, and carbapenems. These antibiotic agents contain a beta-lactam nucleus in its molecular structure. They are the most widely-used group of antibiotics. obo:ARO_3000007 obo:aro.owl obo:ARO_3000007 antibiotic_resistance obo:ARO_3000007 ARO:3000007 obo:ARO_3000007 beta-lactam antibiotic obo:ARO_3000008 Penams, often referred to as penicillins, are a group of antibiotics derived from Penicillium fungi. Penicillin antibiotics are historically significant because they are the first drugs that were effective against many previously serious diseases such as syphilis and Staphylococcus infections. Penicillins are still widely used today, though many types of bacteria are now resistant. All penicillins are beta-lactam antibiotics in the penam sub-group, and are used in the treatment of bacterial infections caused by susceptible, usually Gram-positive, organisms. obo:ARO_3000008 obo:aro.owl obo:ARO_3000008 penams obo:ARO_3000008 antibiotic_resistance obo:ARO_3000008 ARO:3000008 obo:ARO_3000008 penicilllin obo:ARO_3000022 Ristocetin is a glycopeptide antibiotic similar to vancomycin but positively charged. It is not used clinically because it induces platelet agglutination. obo:ARO_3000022 obo:aro.owl obo:ARO_3000022 PubChem:16204749 obo:ARO_3000022 antibiotic_resistance obo:ARO_3000022 ARO:3000022 obo:ARO_3000022 ristocetin obo:ARO_3000050 These antibiotics are derived from tetracycline, a polyketide antibiotic that inhibits the 30S subunit of bacterial ribosomes. obo:ARO_3000050 obo:aro.owl obo:ARO_3000050 antibiotic_resistance obo:ARO_3000050 ARO:3000050 obo:ARO_3000050 tetracycline antibiotic obo:ARO_3000081 Glycopeptide antibiotics are natural products produced non-ribosomally by Actinomycetales bacteria. With the exception of bleomycins, they act by binding the terminal D-Ala-D-Ala in peptidoglycan precursors of the growing bacterial cell wall and are generally active against Gram-positive bacteria. This inhibits transglycosylation leading to cell death due to osmotic stress. obo:ARO_3000081 obo:aro.owl obo:ARO_3000081 antibiotic_resistance obo:ARO_3000081 ARO:3000081 obo:ARO_3000081 glycopeptide antibiotic obo:ARO_3000117 A47934 is an 'aglycone' glycopeptide antibiotic produced by Streptomyces toyocaensis. It is a teicoplanin-like glycopeptide. obo:ARO_3000117 obo:aro.owl obo:ARO_3000117 PubChem:16131155 obo:ARO_3000117 antibiotic_resistance obo:ARO_3000117 ARO:3000117 obo:ARO_3000117 antibiotic A47934 obo:ARO_3000120 Balhimycin is a vancomycin-like glycopeptide antibiotic produced by Amycolatopsis balhimycina. It binds to the terminal Lys-D-Ala-D-Ala of peptidoglycan precursors. obo:ARO_3000120 obo:aro.owl obo:ARO_3000120 PubChem:16134543 obo:ARO_3000120 antibiotic_resistance obo:ARO_3000120 ARO:3000120 obo:ARO_3000120 balhimycin obo:ARO_3000145 Tylosin is a 16-membered macrolide, naturally produced by Streptomyces fradiae. It interacts with the bacterial ribosome 50S subunit to inhibit protein synthesis. obo:ARO_3000145 obo:aro.owl obo:ARO_3000145 PubChem:5280440 obo:ARO_3000145 antibiotic_resistance obo:ARO_3000145 ARO:3000145 obo:ARO_3000145 tylosin obo:ARO_3000152 Minocycline is second generation semi-synthetic derivative of the tetracycline group of antibiotics. It inhibits bacterial protein synthesis by binding to the 30S subunit of the bacterial ribosome and preventing the aminotransferase-tRNA from associating with the ribosome. obo:ARO_3000152 obo:aro.owl obo:ARO_3000152 PubChem:54675783 obo:ARO_3000152 antibiotic_resistance obo:ARO_3000152 ARO:3000152 obo:ARO_3000152 minocycline obo:ARO_3000156 Spiramycin is a 16-membered macrolide and is natural product produced by Streptomyces ambofaciens. It binds to the 50S subunit of bacterial ribosomes and inhibits peptidyl transfer activity to disrupt protein synthesis. obo:ARO_3000156 obo:aro.owl obo:ARO_3000156 PubChem:6419898 obo:ARO_3000156 rovamycin obo:ARO_3000156 antibiotic_resistance obo:ARO_3000156 ARO:3000156 obo:ARO_3000156 spiramycin obo:ARO_3000157 Rifamycin antibiotics are a group of broad-spectrum ansamycin antibiotics that inhibit bacterial RNA polymerase by binding to a highly conserved region, blocking the oligonucleotide exit tunnel, and preventing the extension of nascent mRNAs. obo:ARO_3000157 obo:aro.owl obo:ARO_3000157 antibiotic_resistance obo:ARO_3000157 ARO:3000157 obo:ARO_3000157 rifamycin antibiotic obo:ARO_3000158 Azithromycin is a 15-membered macrolide and falls under the subclass of azalide. Like other macrolides, azithromycin binds bacterial ribosomes to inhibit protein synthesis. The nitrogen substitution at the C-9a position prevents its degradation. obo:ARO_3000158 obo:aro.owl obo:ARO_3000158 PubChem:447043 obo:ARO_3000158 AZM obo:ARO_3000158 antibiotic_resistance obo:ARO_3000158 ARO:3000158 obo:ARO_3000158 azithromycin obo:ARO_3000169 Rifampin is a semi-synthetic rifamycin, and inhibits RNA synthesis by binding to RNA polymerase. Rifampin is the mainstay agent for the treatment of tuberculosis, leprosy and complicated Gram-positive infections. obo:ARO_3000169 obo:aro.owl obo:ARO_3000169 PubChem:135398735 obo:ARO_3000169 rifampicin obo:ARO_3000169 antibiotic_resistance obo:ARO_3000169 ARO:3000169 obo:ARO_3000169 rifampin obo:ARO_3000170 Imipenem is a broad-spectrum antibiotic and is usually taken with cilastatin, which prevents hydrolysis of imipenem by renal dehydropeptidase-I. It is resistant to hydrolysis by most other beta-lactamases. Notable exceptions are the KPC beta-lactamases and Ambler Class B enzymes. obo:ARO_3000170 obo:aro.owl obo:ARO_3000170 PubChem:104838 obo:ARO_3000170 antibiotic_resistance obo:ARO_3000170 ARO:3000170 obo:ARO_3000170 imipenem obo:ARO_3000171 Diaminopyrimidines are a class of organic compounds containing a pyrimidine ring substituted by two amine groups. They are inhibitors of dihydrofolate reductase, an enzyme critical for DNA synthesis. obo:ARO_3000171 obo:aro.owl obo:ARO_3000171 antibiotic_resistance obo:ARO_3000171 ARO:3000171 obo:ARO_3000171 diaminopyrimidine antibiotic obo:ARO_3000176 Dirithromycin is an oxazine derivative of erythromycin, sharing the 14-carbon macrolide ring. The antibiotic binds to the 50S subunit of the ribosome to inhibit bacterial protein synthesis. obo:ARO_3000176 obo:aro.owl obo:ARO_3000176 PubChem:6473883 obo:ARO_3000176 antibiotic_resistance obo:ARO_3000176 ARO:3000176 obo:ARO_3000176 dirithromycin obo:ARO_3000184 Chloroeremomycin is a vancomycin-like glycopeptide, with three sugars instead of two in vancomycin and balhimycin. Chloroeremomycin dimerizes and binds to the terminus of peptidoglycan precursors. obo:ARO_3000184 obo:aro.owl obo:ARO_3000184 PubChem:445806 obo:ARO_3000184 antibiotic_resistance obo:ARO_3000184 ARO:3000184 obo:ARO_3000184 chloroeremomycin obo:ARO_3000188 Trimethoprim is a synthetic 5-(3,4,5- trimethoxybenzyl) pyrimidine inhibitor of dihydrofolate reductase, inhibiting synthesis of tetrahydrofolic acid. Tetrahydrofolic acid is an essential precursor in the de novo synthesis of the DNA nucleotide thymidine. Trimethoprim is a bacteriostatic antibiotic mainly used in the prophylaxis and treatment of urinary tract infections in combination with sulfamethoxazole, a sulfonamide antibiotic. obo:ARO_3000188 obo:aro.owl obo:ARO_3000188 PubChem:5578 obo:ARO_3000188 antibiotic_resistance obo:ARO_3000188 ARO:3000188 obo:ARO_3000188 trimethoprim obo:ARO_3000189 Oritavancin is a semi-synthetic derivative of chloroeremomycin, a vancomycin-like glycopeptide. Oritavancin inhibits both transglycosylation and transpeptidation, by binding both the D-Ala-D-Ala and pentaglycine bridge segments of peptidoglycan to inhibit cell wall formation. obo:ARO_3000189 obo:aro.owl obo:ARO_3000189 PubChem:16136912 obo:ARO_3000189 antibiotic_resistance obo:ARO_3000189 ARO:3000189 obo:ARO_3000189 oritavancin obo:ARO_3000214 Hygromycin B is an aminoglycoside antibiotic used to treat different types of bacterial infections. Hygromycin B works by binding to the bacterial 30S ribosomal subunit, causing misreading of mRNA and leaving the bacterium unable to synthesize proteins vital to its growth. Hygromycin B has also been shown to interact with eukaryotic cells. obo:ARO_3000214 obo:aro.owl obo:ARO_3000214 PubChem:35766 obo:ARO_3000214 antibiotic_resistance obo:ARO_3000214 ARO:3000214 obo:ARO_3000214 hygromycin B obo:ARO_3000244 Reduction in permeability to antibiotic, generally through reduced production of porins, can provide resistance. obo:ARO_3000244 obo:aro.owl obo:ARO_3000244 antibiotic_resistance obo:ARO_3000244 ARO:3000244 obo:ARO_3000244 reduced permeability to antibiotic obo:ARO_3000269 Brodimoprim is a structural derivative of trimethoprim and an inhibitor of bacterial dihydrofolate reductase. The 4-methoxy group of trimethoprim is replaced with a bromine atom. obo:ARO_3000269 obo:aro.owl obo:ARO_3000269 PubChem:68760 obo:ARO_3000269 antibiotic_resistance obo:ARO_3000269 ARO:3000269 obo:ARO_3000269 brodimoprim obo:ARO_3000282 Sulfonamides are broad spectrum, synthetic antibiotics that contain the sulfonamide group. Sulfonamides inhibit dihydropteroate synthase, which catalyzes the conversion of p-aminobenzoic acid to dihydropteroic acid as part of the tetrahydrofolic acid biosynthetic pathway. Tetrahydrofolic acid is essential for folate synthesis, a precursor of many nucleotides and amino acids. Many sulfamides are taken with trimethoprim, an inhibitor of dihydrofolate reductase, also disturbing the trihydrofolic acid synthesis pathway. obo:ARO_3000282 obo:aro.owl obo:ARO_3000282 antibiotic_resistance obo:ARO_3000282 ARO:3000282 obo:ARO_3000282 sulfonamide antibiotic obo:ARO_3000284 Tetroxoprim is a trimethoprim derivative that inhibits bacterial dihydrofolate reductase. obo:ARO_3000284 obo:aro.owl obo:ARO_3000284 PubChem:65450 obo:ARO_3000284 antibiotic_resistance obo:ARO_3000284 ARO:3000284 obo:ARO_3000284 tetroxoprim obo:ARO_3000324 Sulfadiazine is a potent inhibitor of dihydropteroate synthase, interfering with the tetrahydrofolic biosynthesis pathway. Tetrahydrofolic acid is essential for folate synthesis, a precursor to many nucleotides and amino acids. obo:ARO_3000324 obo:aro.owl obo:ARO_3000324 PubChem:5215 obo:ARO_3000324 antibiotic_resistance obo:ARO_3000324 ARO:3000324 obo:ARO_3000324 sulfadiazine obo:ARO_3000325 Sulfadimidine is an alkaline sulfonamide antibiotic that inhibits dihydropteroate synthase, and enzyme in the tetrahydrofolic acid biosynthesis pathway. This interferes with the production of folate, which is a precursor to many amino acids and nucleotides. obo:ARO_3000325 obo:aro.owl obo:ARO_3000325 PubChem:5327 obo:ARO_3000325 sulfamethazine obo:ARO_3000325 antibiotic_resistance obo:ARO_3000325 ARO:3000325 obo:ARO_3000325 sulfadimidine obo:ARO_3000327 Sulfadoxine is an inhibitor of dihydropteroate synthase, interfering with the tetrahydrofolic biosynthesis pathway. Tetrahydrofolic acid is essential for folate synthesis, a precursor to many nucleotides and amino acids. obo:ARO_3000327 obo:aro.owl obo:ARO_3000327 PubChem:17134 obo:ARO_3000327 antibiotic_resistance obo:ARO_3000327 ARO:3000327 obo:ARO_3000327 sulfadoxine obo:ARO_3000329 Sulfamethoxazole is a sulfonamide antibiotic usually taken with trimethoprim, a diaminopyrimidine antibiotic. Sulfamethoxazole inhibits dihydropteroate synthase, essential to tetrahydrofolic acid biosynthesis. This pathway generates compounds used in the synthesis of many amino acids and nucleotides. obo:ARO_3000329 obo:aro.owl obo:ARO_3000329 PubChem:5329 obo:ARO_3000329 antibiotic_resistance obo:ARO_3000329 ARO:3000329 obo:ARO_3000329 sulfamethoxazole obo:ARO_3000330 Sulfisoxazole is an inhibitor of dihydropteroate synthase, interfering with the tetrahydrofolic biosynthesis pathway. Tetrahydrofolic acid is essential for folate synthesis, a precursor to many nucleotides and amino acids. obo:ARO_3000330 obo:aro.owl obo:ARO_3000330 PubChem:5344 obo:ARO_3000330 antibiotic_resistance obo:ARO_3000330 ARO:3000330 obo:ARO_3000330 sulfisoxazole obo:ARO_3000337 Iclaprim is a bactericidal compound that inhibits dihydrofolate reductase. It is used against clinically important Gram-positive pathogens, including methicillin-sensitive Staphylococcus aureus and methicillin-resistant S. aureus. obo:ARO_3000337 obo:aro.owl obo:ARO_3000337 PubChem:213043 obo:ARO_3000337 AR-100 obo:ARO_3000337 RO-48-2622 obo:ARO_3000337 antibiotic_resistance obo:ARO_3000337 ARO:3000337 obo:ARO_3000337 iclaprim obo:ARO_3000385 Chloramphenicol is a bacteriostatic antimicrobial originally derived from the bacterium Streptomyces venezuelae. It was the first antibiotic to be manufactured synthetically on a large scale. It functions by inhibiting peptidyl transferase activity of the bacterial ribosome, binding to A2451 and A2452 residues in the 23S rRNA of the 50S ribosomal subunit and preventing peptide bond formation. obo:ARO_3000385 obo:aro.owl obo:ARO_3000385 PubChem:5959 obo:ARO_3000385 CHL obo:ARO_3000385 antibiotic_resistance obo:ARO_3000385 ARO:3000385 obo:ARO_3000385 chloramphenicol obo:ARO_3000454 Polymyxin B is mixture of mostly polymyxins B1 and B2, mainly used for resistant gram-negative infections. They are polypeptides with cationic detergent action on cell membranes. obo:ARO_3000454 obo:aro.owl obo:ARO_3000454 antibiotic_resistance obo:ARO_3000454 ARO:3000454 obo:ARO_3000454 polymyxin B obo:ARO_3000466 Dalbavancin is a semisynthetic second-generation lipoglycopeptide derived from teicoplanin. It binds to the D-Ala-D-Ala terminus of peptidoglycan precursors. It is used to treat Gram-positive bacteria and can be used to treat methicillin-resistant Staphylococcus aureus and vancomycin-resistant enterococci. obo:ARO_3000466 obo:aro.owl obo:ARO_3000466 PubChem:23724878 obo:ARO_3000466 Zeven obo:ARO_3000466 antibiotic_resistance obo:ARO_3000466 ARO:3000466 obo:ARO_3000466 dalbavancin obo:ARO_3000488 Telavancin is a semi-synthetic derivative of vancomycin and is a second-generation lipoglycopeptide antibiotic. Telavancin inhibits cell wall synthesis by forming a complex with the D-Ala-D-Ala terminus of peptidoglycan precursors and preventing transglycosylation. obo:ARO_3000488 obo:aro.owl obo:ARO_3000488 PubChem:3081362 obo:ARO_3000488 antibiotic_resistance obo:ARO_3000488 ARO:3000488 obo:ARO_3000488 telavancin obo:ARO_3000517 Rifaximin is a semi-synthetic rifamycin used to treat traveller's diarrhea. Rifaximin inhibits RNA synthesis by binding to the beta subunit of bacterial RNA polymerase. obo:ARO_3000517 obo:aro.owl obo:ARO_3000517 PubChem:6436173 obo:ARO_3000517 antibiotic_resistance obo:ARO_3000517 ARO:3000517 obo:ARO_3000517 rifaximin obo:ARO_3000525 A40926 is a glycopeptide antibiotic produced by Nonomuraea sp. ATCC 39727. It is precusor of the second-generation glycopeptide antibiotic dalbavancin. obo:ARO_3000525 obo:aro.owl obo:ARO_3000525 PubChem:16133962 obo:ARO_3000525 antibiotic_resistance obo:ARO_3000525 ARO:3000525 obo:ARO_3000525 antibiotic A40926 obo:ARO_3000528 Chlortetracycline was an early, first-generation tetracycline antibiotic developed in the 1940's. It inhibits bacterial protein synthesis by binding to the 30S subunit of bacterial ribosomes, preventing the aminoacyl-tRNA from binding to the ribosome. obo:ARO_3000528 obo:aro.owl obo:ARO_3000528 PubChem:54675777 obo:ARO_3000528 Aureomycin obo:ARO_3000528 antibiotic_resistance obo:ARO_3000528 ARO:3000528 obo:ARO_3000528 chlortetracycline obo:ARO_3000530 Rifabutin is a semisynthetic rifamycin used in tuberculosis therapy. It inhibits DNA-dependent RNA synthesis. obo:ARO_3000530 obo:aro.owl obo:ARO_3000530 PubChem:135398743 obo:ARO_3000530 antibiotic_resistance obo:ARO_3000530 ARO:3000530 obo:ARO_3000530 rifabutin obo:ARO_3000534 Rifapentine is a semisynthetic rifamycin that inhibits DNA-dependent RNA synthesis. It is often used in the treatment of tuberculosis and leprosy. obo:ARO_3000534 obo:aro.owl obo:ARO_3000534 PubChem:135403821 obo:ARO_3000534 priftin obo:ARO_3000534 antibiotic_resistance obo:ARO_3000534 ARO:3000534 obo:ARO_3000534 rifapentine obo:ARO_3000550 Aztreonam was the first monobactam discovered, and is greatly effective against Gram-negative bacteria while inactive against Gram-positive bacteria. Artreonam is a poor substrate for beta-lactamases, and may even act as an inhibitor. In Gram-negative bacteria, Aztreonam interferes with filamentation, inhibiting cell division and leading to cell death. obo:ARO_3000550 obo:aro.owl obo:ARO_3000550 PubChem:5742832 obo:ARO_3000550 ATM obo:ARO_3000550 Primbactam obo:ARO_3000550 antibiotic_resistance obo:ARO_3000550 ARO:3000550 obo:ARO_3000550 aztreonam obo:ARO_3000622 Colistin A, or polymyxin E1, has a 6-octanoic acid lipid tail. Polymyxins disrupt the cell membrane of Gram-negative bacteria. obo:ARO_3000622 obo:aro.owl obo:ARO_3000622 PubChem:202195 obo:ARO_3000622 polymyxin E1 obo:ARO_3000622 antibiotic_resistance obo:ARO_3000622 ARO:3000622 obo:ARO_3000622 colistin A obo:ARO_3000624 Colistin B, or polymyxin E2, has a 6-heptanoic acid lipid tail. Polymyxins disrupt the cell membrane of Gram-negative bacteria. obo:ARO_3000624 obo:aro.owl obo:ARO_3000624 PubChem:25138298 obo:ARO_3000624 polymyxin E2 obo:ARO_3000624 antibiotic_resistance obo:ARO_3000624 ARO:3000624 obo:ARO_3000624 colistin B obo:ARO_3000625 Polymyxin B1 is in the family of polymyxin lipopeptides with a 6-methyloctanoic acid acyl group. These antibiotics disrupt the cell membrane of Gram-negative bacteria. obo:ARO_3000625 obo:aro.owl obo:ARO_3000625 PubChem:199402 obo:ARO_3000625 antibiotic_resistance obo:ARO_3000625 ARO:3000625 obo:ARO_3000625 polymyxin B1 obo:ARO_3000626 Polymyxin B2 is in the family of polymyxin lipopeptides with a 6-methylheptanoic acid acyl group. These antibiotics disrupt the cell membrane of Gram-negative bacteria. obo:ARO_3000626 obo:aro.owl obo:ARO_3000626 PubChem:11982455 obo:ARO_3000626 antibiotic_resistance obo:ARO_3000626 ARO:3000626 obo:ARO_3000626 polymyxin B2 obo:ARO_3000627 Polymyxin B3 is in the family of polymyxin lipopeptides with an octanoic acid acyl group. These antibiotics disrupt the cell membrane of Gram-negative bacteria. obo:ARO_3000627 obo:aro.owl obo:ARO_3000627 PubChem:46883542 obo:ARO_3000627 antibiotic_resistance obo:ARO_3000627 ARO:3000627 obo:ARO_3000627 polymyxin B3 obo:ARO_3000628 Polymyxin B4 is in the family of polymyxin lipopeptides with a heptanoic acid acyl group. These antibiotics disrupt the cell membrane of Gram-negative bacteria. obo:ARO_3000628 obo:aro.owl obo:ARO_3000628 PubChem:46883543 obo:ARO_3000628 antibiotic_resistance obo:ARO_3000628 ARO:3000628 obo:ARO_3000628 polymyxin B4 obo:ARO_3000632 Benzylpenicillin, commonly referred to as penicillin G, is effective against both Gram-positive and Gram-negative bacteria. It is unstable in acid. obo:ARO_3000632 obo:aro.owl obo:ARO_3000632 PubChem:5904 obo:ARO_3000632 Penicillin G obo:ARO_3000632 benzopenicillin obo:ARO_3000632 antibiotic_resistance obo:ARO_3000632 ARO:3000632 obo:ARO_3000632 benzylpenicillin obo:ARO_3000633 Phenoxymethylpenicillin, or penicillin V, is a penicillin derivative that is acid stable but less active than benzylpenicillin (penicillin G). obo:ARO_3000633 obo:aro.owl obo:ARO_3000633 PubChem:6869 obo:ARO_3000633 penicillin V obo:ARO_3000633 phenomycilline obo:ARO_3000633 phenopenicillin obo:ARO_3000633 antibiotic_resistance obo:ARO_3000633 ARO:3000633 obo:ARO_3000633 phenoxymethylpenicillin obo:ARO_3000634 Propicillin is an orally taken penicillin derivative that has high absorption but poor activity. obo:ARO_3000634 obo:aro.owl obo:ARO_3000634 PubChem:92879 obo:ARO_3000634 levopropicillin obo:ARO_3000634 antibiotic_resistance obo:ARO_3000634 ARO:3000634 obo:ARO_3000634 propicillin obo:ARO_3000635 Dicloxacillin is a penicillin derivative that has an extra chlorine atom in comparison to cloxacillin. While more active than cloxacillin, its high affinity for serum protein reduces its activity in human serum in vitro. obo:ARO_3000635 obo:aro.owl obo:ARO_3000635 PubChem:18381 obo:ARO_3000635 dicloxacilin obo:ARO_3000635 dicloxacycline obo:ARO_3000635 antibiotic_resistance obo:ARO_3000635 ARO:3000635 obo:ARO_3000635 dicloxacillin obo:ARO_3000636 Flucloxacillin is similar to cloxacillin, with an extra additional fluorine atom. obo:ARO_3000636 obo:aro.owl obo:ARO_3000636 PubChem:21319 obo:ARO_3000636 floxacillin obo:ARO_3000636 floxapen obo:ARO_3000636 antibiotic_resistance obo:ARO_3000636 ARO:3000636 obo:ARO_3000636 flucloxacillin obo:ARO_3000637 Ampicillin is a penicillin derivative that is highly acid stable, with its activity similar to benzylpenicillin. obo:ARO_3000637 obo:aro.owl obo:ARO_3000637 PubChem:6249 obo:ARO_3000637 AMP obo:ARO_3000637 Principen obo:ARO_3000637 ampicillin acid obo:ARO_3000637 antibiotic_resistance obo:ARO_3000637 ARO:3000637 obo:ARO_3000637 ampicillin obo:ARO_3000638 Azlocillin is a semisynthetic derivative of penicillin that is notably active against Ps. aeruginosa and other Gram-negative bacteria. obo:ARO_3000638 obo:aro.owl obo:ARO_3000638 PubChem:6479523 obo:ARO_3000638 AZL obo:ARO_3000638 antibiotic_resistance obo:ARO_3000638 ARO:3000638 obo:ARO_3000638 azlocillin obo:ARO_3000639 Mezlocillin is a penicillin derivative taken parenterally. obo:ARO_3000639 obo:aro.owl obo:ARO_3000639 PubChem:656511 obo:ARO_3000639 mezlin obo:ARO_3000639 mezlocillin obo:ARO_3000639 antibiotic_resistance obo:ARO_3000639 ARO:3000639 obo:ARO_3000639 mezlocillin obo:ARO_3000640 Doripenem is a carbapenem with a broad range of activity against Gram-positive and Gram-negative bacteria, and along with meropenem, it is the most active beta-lactam antibiotic against Pseudomonas aeruginosa. It inhibits bacterial cell wall synthesis. obo:ARO_3000640 obo:aro.owl obo:ARO_3000640 PubChem:73303 obo:ARO_3000640 doribax obo:ARO_3000640 antibiotic_resistance obo:ARO_3000640 ARO:3000640 obo:ARO_3000640 doripenem obo:ARO_3000641 Cefalexin is a cephalosporin antibiotic that causes filamentation. It is resistant to staphylococcal beta-lactamase, but degraded by enterobacterial beta-lactamases. obo:ARO_3000641 obo:aro.owl obo:ARO_3000641 PubChem:27447 obo:ARO_3000641 LEX obo:ARO_3000641 cephalexin obo:ARO_3000641 antibiotic_resistance obo:ARO_3000641 ARO:3000641 obo:ARO_3000641 cefalexin obo:ARO_3000642 Cefadroxil, or p-hydroxycephalexin, is an cephalosporin antibiotic similar to cefalexin. obo:ARO_3000642 obo:aro.owl obo:ARO_3000642 PubChem:47965 obo:ARO_3000642 CFR obo:ARO_3000642 p-hydroxycephalexin obo:ARO_3000642 antibiotic_resistance obo:ARO_3000642 ARO:3000642 obo:ARO_3000642 cefadroxil obo:ARO_3000643 Cefotiam is a cephalosporin antibiotic with similar activity to cefuroxime but more active against enterobacteria. It is consumed orally as the prodrug cefotiam hexetil. obo:ARO_3000643 obo:aro.owl obo:ARO_3000643 PubChem:43708 obo:ARO_3000643 cefotiamum obo:ARO_3000643 antibiotic_resistance obo:ARO_3000643 ARO:3000643 obo:ARO_3000643 cefotiam obo:ARO_3000644 Cefaclor is a semisynthetic cephalosporin derived from cephalexin. It has broad-spectrum antibiotic activity. obo:ARO_3000644 obo:aro.owl obo:ARO_3000644 PubChem:51039 obo:ARO_3000644 CEC obo:ARO_3000644 ceclor obo:ARO_3000644 cephaclor obo:ARO_3000644 antibiotic_resistance obo:ARO_3000644 ARO:3000644 obo:ARO_3000644 cefaclor obo:ARO_3000645 Cefotaxime is a semisynthetic cephalosporin taken parenterally. It is resistant to most beta-lactamases and active against Gram-negative rods and cocci due to its aminothiazoyl and methoximino functional groups. obo:ARO_3000645 obo:aro.owl obo:ARO_3000645 PubChem:5742673 obo:ARO_3000645 CTX obo:ARO_3000645 cefotaxime acid obo:ARO_3000645 antibiotic_resistance obo:ARO_3000645 ARO:3000645 obo:ARO_3000645 cefotaxime obo:ARO_3000646 Cefixime is a cephalosporin resistant to most beta-lactamases. It is active against many enterobacteria, but activity against staphylococci is poor. obo:ARO_3000646 obo:aro.owl obo:ARO_3000646 PubChem:5362065 obo:ARO_3000646 CFM obo:ARO_3000646 necopen obo:ARO_3000646 antibiotic_resistance obo:ARO_3000646 ARO:3000646 obo:ARO_3000646 cefixime obo:ARO_3000647 Cefpodoxime is a semisynthetic cephalosporin that acts similarly to cefotaxime with broad-spectrum activity. It is stable to many plasmid-mediated beta-lactamses. Cefpodoxime is consumed as the prodrug cefpodoxime proxetil. obo:ARO_3000647 obo:aro.owl obo:ARO_3000647 PubChem:6335986 obo:ARO_3000647 CPD obo:ARO_3000647 antibiotic_resistance obo:ARO_3000647 ARO:3000647 obo:ARO_3000647 cefpodoxime obo:ARO_3000648 Ceftibuten is a semisynthetic cephalosporin active against Gram-negative bacilli. It is resistant against many plasmid-mediated beta-lactamases. obo:ARO_3000648 obo:aro.owl obo:ARO_3000648 PubChem:5282242 obo:ARO_3000648 CTB obo:ARO_3000648 Cedax obo:ARO_3000648 antibiotic_resistance obo:ARO_3000648 ARO:3000648 obo:ARO_3000648 ceftibuten obo:ARO_3000649 Cefditoren is a semisynthetic cephalosporin active against staphylococci, streptococci, and and most enterobacteria. It is resistant to staphylococcal and most enterobacterial beta-lactamases, and is usually taken as the prodrug cefditoren pivoxil. obo:ARO_3000649 obo:aro.owl obo:ARO_3000649 PubChem:9571074 obo:ARO_3000649 CDN obo:ARO_3000649 antibiotic_resistance obo:ARO_3000649 ARO:3000649 obo:ARO_3000649 cefditoren obo:ARO_3000650 Cefdinir is similar to cefixime with a modified side-chain at its 7-amino position. It also shares similar activity with cefixime but is more active against staphylococci. It has also be shown to enhance phagocytosis. obo:ARO_3000650 obo:aro.owl obo:ARO_3000650 PubChem:6915944 obo:ARO_3000650 CDR obo:ARO_3000650 antibiotic_resistance obo:ARO_3000650 ARO:3000650 obo:ARO_3000650 cefdinir obo:ARO_3000651 Ceftaroline is a novel cephalosporin active against methicillin resistant Staphylococcus aureus. Like other cephalosporins it binds penicillin-binding proteins to inhibit cell wall synthesis. It strongly binds with PBP2a, associated with methicillin resistance. It is taken orally as the prodrug ceftaroline fosamil. obo:ARO_3000651 obo:aro.owl obo:ARO_3000651 PubChem:9852982 obo:ARO_3000651 CPT obo:ARO_3000651 T91825 obo:ARO_3000651 antibiotic_resistance obo:ARO_3000651 ARO:3000651 obo:ARO_3000651 ceftaroline obo:ARO_3000652 A semi-synthetic derivative of gentamicin B (hydroxyamino propionyl genamicin B). It is modified to combat microbial inactivation and has a slightly larger spectrum of activity compared to other aminoglycosides, including Ser marcescens, Enterobacteria, and K pneumoniae. obo:ARO_3000652 obo:aro.owl obo:ARO_3000652 PubChem:3037209 obo:ARO_3000652 isepamicine obo:ARO_3000652 isepamicinum obo:ARO_3000652 antibiotic_resistance obo:ARO_3000652 ARO:3000652 obo:ARO_3000652 isepamicin obo:ARO_3000653 A gentamicin class aminoglycoside antibiotic often used in mammalian cell culture work as a selectable marker for the neo cassette (APH3'). obo:ARO_3000653 obo:aro.owl obo:ARO_3000653 PubChem:123865 obo:ARO_3000653 geneticin obo:ARO_3000653 antibiotic_resistance obo:ARO_3000653 ARO:3000653 obo:ARO_3000653 G418 obo:ARO_3000654 A synthetic derivative (1-N-(4-amino-2-hydroxybutyryl) of dibekacin used in Japan. It is active against methicillin-resistant Staph. aureus and shows synergy with ampicillin when treating gentamicin and vancomycin resistant enterocci. obo:ARO_3000654 obo:aro.owl obo:ARO_3000654 PubChem:68682 obo:ARO_3000654 habekacin obo:ARO_3000654 haberacin obo:ARO_3000654 antibiotic_resistance obo:ARO_3000654 ARO:3000654 obo:ARO_3000654 arbekacin obo:ARO_3000655 Gentamicin B is a semisynthetic aminoglycoside antibacterial. obo:ARO_3000655 obo:aro.owl obo:ARO_3000655 PubChem:11754987 obo:ARO_3000655 betamicin obo:ARO_3000655 antibiotic_resistance obo:ARO_3000655 ARO:3000655 obo:ARO_3000655 gentamicin B obo:ARO_3000657 An aminoglycoside antibiotic used for the treatment of parasitic infections. It is similar to neomycin sharing a similar spectrum of activity, but its hydroxyl group at the 6'-position instead of an amino group makes it resistant to AAC(6') modifying enzymes. obo:ARO_3000657 obo:aro.owl obo:ARO_3000657 PubChem:165580 obo:ARO_3000657 Gabbomycin obo:ARO_3000657 Humagel obo:ARO_3000657 Humatin obo:ARO_3000657 aminosidin obo:ARO_3000657 aminosidine obo:ARO_3000657 catenulin obo:ARO_3000657 crestomycin obo:ARO_3000657 estomycin obo:ARO_3000657 hydroxymycin obo:ARO_3000657 monomycin A obo:ARO_3000657 neomycin E obo:ARO_3000657 paucimycin obo:ARO_3000657 antibiotic_resistance obo:ARO_3000657 ARO:3000657 obo:ARO_3000657 paromomycin obo:ARO_3000658 Lividomycins are aminoglycosidic antibiotics produced by Streptomyces lividus. They contain 2-amino-2,3-dideoxy-D-glucose. obo:ARO_3000658 obo:aro.owl obo:ARO_3000658 antibiotic_resistance obo:ARO_3000658 ARO:3000658 obo:ARO_3000658 lividomycin obo:ARO_3000659 Gatifloxacin is an 8-methoxy, 7-piperazinyl, 6-fluoroquinolone that can be taken orally or by intravenous administration. It is active against most Gram-positive and Gram-negative bacteria, but inactive against non-fermenting Gram-negative rods including Pseudomonas aeruginosa. obo:ARO_3000659 obo:aro.owl obo:ARO_3000659 PubChem:5379 obo:ARO_3000659 AM-1155 obo:ARO_3000659 Tequin obo:ARO_3000659 antibiotic_resistance obo:ARO_3000659 ARO:3000659 obo:ARO_3000659 gatifloxacin obo:ARO_3000660 Lomefloxacin is a difluoropiperazinyl quinolone, sharing similar activities with other fluoroquinolones. It is used to treat urinary tract infections. Relative to other fluoroquinolones, it has a longer half life and has higher serum concentrations. obo:ARO_3000660 obo:aro.owl obo:ARO_3000660 PubChem:3948 obo:ARO_3000660 antibiotic_resistance obo:ARO_3000660 ARO:3000660 obo:ARO_3000660 lomefloxacin obo:ARO_3000661 Nalidixic acid is a quinolone derivative of naphthyridine active against many enterobacteria, but ineffective against Ps aeruginosa, Gram-positive bacteria, and anaerobes. Acquired resistance is common in nalidixic acid treatments. obo:ARO_3000661 obo:aro.owl obo:ARO_3000661 PubChem:4421 obo:ARO_3000661 nalidixin obo:ARO_3000661 antibiotic_resistance obo:ARO_3000661 ARO:3000661 obo:ARO_3000661 nalidixic acid obo:ARO_3000662 Norfloxacin is a 6-fluoro, 7-piperazinyl quinolone with a wide range of activity against Gram-negative bacteria. It is inactive against most anaerobes. obo:ARO_3000662 obo:aro.owl obo:ARO_3000662 PubChem:4539 obo:ARO_3000662 antibiotic_resistance obo:ARO_3000662 ARO:3000662 obo:ARO_3000662 norfloxacin obo:ARO_3000663 Ofloxacin is a 6-fluoro, 7-piperazinyl quinolone with a methyl-substituted oxazine ring. It has a broad spectrum of activity including many enterobacteria and mycoplasma but most anaerobes are resistant. obo:ARO_3000663 obo:aro.owl obo:ARO_3000663 PubChem:4583 obo:ARO_3000663 Tarivid obo:ARO_3000663 floxin obo:ARO_3000663 antibiotic_resistance obo:ARO_3000663 ARO:3000663 obo:ARO_3000663 ofloxacin obo:ARO_3000664 Trovafloxacin is a trifluoroquinalone with a broad spectrum of activity that acts by inhibiting the uncoiling of supercoiled DNA. While potent against many Gram-positive and Gram-negative bacteria, it is less active against pseudomonads and Cl. difficile. It is usually taken as the prodrug trovafloxacin mesylate or alatrofloxacin mesylate for oral or intravenous administration, respectively. obo:ARO_3000664 obo:aro.owl obo:ARO_3000664 PubChem:62959 obo:ARO_3000664 Trovan obo:ARO_3000664 alatrofloxacin obo:ARO_3000664 antibiotic_resistance obo:ARO_3000664 ARO:3000664 obo:ARO_3000664 trovafloxacin obo:ARO_3000665 Grepafloxacin is a broad-spectrum antibacterial quinoline. It is no longer taken due to its high toxicity. obo:ARO_3000665 obo:aro.owl obo:ARO_3000665 PubChem:72474 obo:ARO_3000665 Raxar obo:ARO_3000665 antibiotic_resistance obo:ARO_3000665 ARO:3000665 obo:ARO_3000665 grepafloxacin obo:ARO_3000666 Sparfloxacin is a dimethylpiperazinyl difluoroquinolone that acts by inhibiting DNA gyrase. It is active against aerobic Gram-positive and Gram-negative bacteria, as well as some mycobacteria. It has moderate activity against some anaerobes. obo:ARO_3000666 obo:aro.owl obo:ARO_3000666 PubChem:60464 obo:ARO_3000666 Zagam obo:ARO_3000666 antibiotic_resistance obo:ARO_3000666 ARO:3000666 obo:ARO_3000666 sparfloxacin obo:ARO_3000667 Demeclocycline is a tetracycline analog with 7-chloro and 6-methyl groups. Due to its fast absorption and slow excretion, it maintains higher effective blood levels compared to other tetracyclines. obo:ARO_3000667 obo:aro.owl obo:ARO_3000667 PubChem:54680690 obo:ARO_3000667 DMCTC obo:ARO_3000667 declomycin obo:ARO_3000667 antibiotic_resistance obo:ARO_3000667 ARO:3000667 obo:ARO_3000667 demeclocycline obo:ARO_3000668 Oxytetracycline is a derivative of tetracycline with a 5-hydroxyl group. Its activity is similar to other tetracyclines. obo:ARO_3000668 obo:aro.owl obo:ARO_3000668 PubChem:54675779 obo:ARO_3000668 antibiotic_resistance obo:ARO_3000668 ARO:3000668 obo:ARO_3000668 oxytetracycline obo:ARO_3000683 Sulfacetamide is a very soluable sulfonamide antibiotic previously used to treat urinary tract infections. Its relatively low activity and toxicity to those with Stevens-Johnson syndrome have reduced its use and availability. obo:ARO_3000683 obo:aro.owl obo:ARO_3000683 PubChem:5320 obo:ARO_3000683 antibiotic_resistance obo:ARO_3000683 ARO:3000683 obo:ARO_3000683 sulfacetamide obo:ARO_3000684 Mafenide is a sulfonamide used topically for treating burns. obo:ARO_3000684 obo:aro.owl obo:ARO_3000684 PubChem:3998 obo:ARO_3000684 ambamide obo:ARO_3000684 maphenide obo:ARO_3000684 sulfamylon obo:ARO_3000684 antibiotic_resistance obo:ARO_3000684 ARO:3000684 obo:ARO_3000684 mafenide obo:ARO_3000690 Bleomycinic acid is a glycopeptide antibiotic produced by Streptomyces verticillus taken as a mixture of bleomycins. It induces stand breaks in bacterial nucleic acids. obo:ARO_3000690 obo:aro.owl obo:ARO_3000690 PubChem:2410 obo:ARO_3000690 antibiotic_resistance obo:ARO_3000690 ARO:3000690 obo:ARO_3000690 bleomycinic acid obo:ARO_3000691 Bleomycin A2 is a glycopeptide antibiotic produced by Streptomyces verticillus taken as a mixture of bleomycins. It induces stand breaks in bacterial nucleic acids. obo:ARO_3000691 obo:aro.owl obo:ARO_3000691 PubChem:5460769 obo:ARO_3000691 antibiotic_resistance obo:ARO_3000691 ARO:3000691 obo:ARO_3000691 bleomycin A2 obo:ARO_3000692 Bleomycin B2 is a glycopeptide antibiotic produced by Streptomyces verticillus taken as a mixture of bleomycins. It induces stand breaks in bacterial nucleic acids. obo:ARO_3000692 obo:aro.owl obo:ARO_3000692 PubChem:5496540 obo:ARO_3000692 antibiotic_resistance obo:ARO_3000692 ARO:3000692 obo:ARO_3000692 bleomycin B2 obo:ARO_3000698 Sulfasalazine is a derivative of the early sulfonamide sulfapyridine (salicylazosulfapyridine). It was developed to increase water solubility and is taken orally for ulcerative colitis. obo:ARO_3000698 obo:aro.owl obo:ARO_3000698 PubChem:5339 obo:ARO_3000698 salicylazosulfapyridine obo:ARO_3000698 antibiotic_resistance obo:ARO_3000698 ARO:3000698 obo:ARO_3000698 sulfasalazine obo:ARO_3000699 Sulfamethizole is a short-acting sulfonamide that inhibits dihydropteroate synthetase. obo:ARO_3000699 obo:aro.owl obo:ARO_3000699 PubChem:5328 obo:ARO_3000699 Urolucosil obo:ARO_3000699 sulfamethizol obo:ARO_3000699 sulphamethizole obo:ARO_3000699 antibiotic_resistance obo:ARO_3000699 ARO:3000699 obo:ARO_3000699 sulfamethizole obo:ARO_3000700 Lividomycin A is a pentasaccharide antibiotic which interferes with bacterial protein synthesis. obo:ARO_3000700 obo:aro.owl obo:ARO_3000700 PubChem:72394 obo:ARO_3000700 antibiotic_resistance obo:ARO_3000700 ARO:3000700 obo:ARO_3000700 lividomycin A obo:ARO_3000701 Lividomycin B is a derivative of lividomycin A with a removed mannose group (demannosyllividomycin A). Livodomycins interfere with bacterial protein synthesis. obo:ARO_3000701 obo:aro.owl obo:ARO_3000701 PubChem:46174031 obo:ARO_3000701 antibiotic_resistance obo:ARO_3000701 ARO:3000701 obo:ARO_3000701 lividomycin B obo:ARO_3000704 Cefalotin is a semisynthetic cephalosporin antibiotic activate against staphylococci. It is resistant to staphylococci beta-lactamases but hydrolyzed by enterobacterial beta-lactamases. obo:ARO_3000704 obo:aro.owl obo:ARO_3000704 PubChem:6024 obo:ARO_3000704 CEF obo:ARO_3000704 cephalothin obo:ARO_3000704 antibiotic_resistance obo:ARO_3000704 ARO:3000704 obo:ARO_3000704 cefalotin obo:ARO_3000705 Isopenicillin N is a natural penicillin derivative produced by Penicillium chrysogenum with activity similar to penicillin N. obo:ARO_3000705 obo:aro.owl obo:ARO_3000705 PubChem:440723 obo:ARO_3000705 antibiotic_resistance obo:ARO_3000705 ARO:3000705 obo:ARO_3000705 isopenicillin N obo:ARO_3000706 Penicillin N is a penicillin derivative produced by Cephalosporium acremonium. obo:ARO_3000706 obo:aro.owl obo:ARO_3000706 PubChem:71724 obo:ARO_3000706 antibiotic_resistance obo:ARO_3000706 ARO:3000706 obo:ARO_3000706 penicillin N obo:ARO_3000761 Mecillinam is a broad-spectrum beta-lactam antibiotic that was semi-synthetically derived to have a different drug centre, being a 6-alpha-amidinopenicillanate instead of a 6-alpha-acylaminopenicillanate. Contrasting most beta-lactam drugs, mecillinam is most active against Gram-negative bacteria. It binds specifically to penicillin binding protein 2 (PBP2). obo:ARO_3000761 obo:aro.owl obo:ARO_3000761 PubChem:36273 obo:ARO_3000761 Selexid obo:ARO_3000761 Selexidin obo:ARO_3000761 amdinocillin obo:ARO_3000761 antibiotic_resistance obo:ARO_3000761 ARO:3000761 obo:ARO_3000761 mecillinam obo:ARO_3000762 Pefloxacin is structurally and functionally similar to norfloxacin. It is poorly active against mycobacteria, while anaerobes are resistant. obo:ARO_3000762 obo:aro.owl obo:ARO_3000762 PubChem:51081 obo:ARO_3000762 antibiotic_resistance obo:ARO_3000762 ARO:3000762 obo:ARO_3000762 pefloxacin obo:ARO_3000767 Avoparcin is a glycopeptide antibiotic that is an analog of vancomycin. It was formally used to treat animals, but has since been banned because of its selection for vancomycin-resistant enterococci. obo:ARO_3000767 obo:aro.owl obo:ARO_3000767 PubChem:16132294 obo:ARO_3000767 antibiotic_resistance obo:ARO_3000767 ARO:3000767 obo:ARO_3000767 avoparcin obo:ARO_3000842 EBR-1 is an Ambler class B beta-lactamase found in Empedobacter brevis and is known to mediate the hydrolysis of penicillins, cephalosporins, and carbapenems efficiently but not aztreonam. obo:ARO_3000842 obo:aro.owl obo:ARO_3000842 antibiotic_resistance obo:ARO_3000842 ARO:3000842 obo:ARO_3000842 EBR-1 beta-lactamase obo:ARO_3000867 Oleandomycin is a 14-membered macrolide produced by Streptomyces antibioticus. It is ssimilar to erythromycin, and contains a desosamine amino sugar and an oleandrose sugar. It targets the 50S ribosomal subunit to prevent protein synthesis. obo:ARO_3000867 obo:aro.owl obo:ARO_3000867 PubChem:72493 obo:ARO_3000867 Amimycin obo:ARO_3000867 Matromycin obo:ARO_3000867 antibiotic_resistance obo:ARO_3000867 ARO:3000867 obo:ARO_3000867 oleandomycin obo:ARO_3001221 A macrolide antibiotic from Streptomyces narbonensis subsp. josamyceticus. The drug has antimicrobial activity against a wide spectrum of pathogens. obo:ARO_3001221 obo:aro.owl obo:ARO_3001221 PubChem:5284579 obo:ARO_3001221 antibiotic_resistance obo:ARO_3001221 ARO:3001221 obo:ARO_3001221 josamycin obo:ARO_3001222 Produced by Streptomyces bikiniensis obo:ARO_3001222 obo:aro.owl obo:ARO_3001222 PubChem:6436271 obo:ARO_3001222 antibiotic_resistance obo:ARO_3001222 ARO:3001222 obo:ARO_3001222 chalcomycin obo:ARO_3001223 Produced by Streptomyces mycarofaciens. obo:ARO_3001223 obo:aro.owl obo:ARO_3001223 PubChem:5282169 obo:ARO_3001223 antibiotic_resistance obo:ARO_3001223 ARO:3001223 obo:ARO_3001223 midecamycin obo:ARO_3001224 Produced by Micromonospora griseorubida. obo:ARO_3001224 obo:aro.owl obo:ARO_3001224 PubChem:6447311 obo:ARO_3001224 antibiotic_resistance obo:ARO_3001224 ARO:3001224 obo:ARO_3001224 mycinamicin obo:ARO_3001225 Produced by Micromonospora megalomicia. obo:ARO_3001225 obo:aro.owl obo:ARO_3001225 PubChem:474871 obo:ARO_3001225 antibiotic_resistance obo:ARO_3001225 ARO:3001225 obo:ARO_3001225 megalomycin obo:ARO_3001226 Produced by Streptomyces narbonensis. obo:ARO_3001226 obo:aro.owl obo:ARO_3001226 PubChem:5282036 obo:ARO_3001226 antibiotic_resistance obo:ARO_3001226 ARO:3001226 obo:ARO_3001226 narbomycin obo:ARO_3001227 Kitasamycin is a macrolide antibiotic and is produced by Streptoverticillium kitasatoense. The drug has antimicrobial activity against a wide spectrum of pathogens. obo:ARO_3001227 obo:aro.owl obo:ARO_3001227 PubChem:5282189 obo:ARO_3001227 antibiotic_resistance obo:ARO_3001227 ARO:3001227 obo:ARO_3001227 kitasamycin obo:ARO_3001228 Produced by Streptomyces halstedii and Streptomyces thermotolerans. obo:ARO_3001228 obo:aro.owl obo:ARO_3001228 PubChem:5287879 obo:ARO_3001228 antibiotic_resistance obo:ARO_3001228 ARO:3001228 obo:ARO_3001228 carbomycin obo:ARO_3001229 Produced by Micromonospora rosaria. obo:ARO_3001229 obo:aro.owl obo:ARO_3001229 PubChem:6537204 obo:ARO_3001229 antibiotic_resistance obo:ARO_3001229 ARO:3001229 obo:ARO_3001229 rosaramicin obo:ARO_3001230 Produced by Streptomyces caelestis. obo:ARO_3001230 obo:aro.owl obo:ARO_3001230 PubChem:6440864 obo:ARO_3001230 antibiotic_resistance obo:ARO_3001230 ARO:3001230 obo:ARO_3001230 niddamycin obo:ARO_3001232 Produced by Streptomyces venezuelae ATCC 15439. obo:ARO_3001232 obo:aro.owl obo:ARO_3001232 PubChem:5282034 obo:ARO_3001232 antibiotic_resistance obo:ARO_3001232 ARO:3001232 obo:ARO_3001232 methymycin obo:ARO_3001233 Produced by Streptomyces venezuelae ATCC 15439. obo:ARO_3001233 obo:aro.owl obo:ARO_3001233 PubChem:5282037 obo:ARO_3001233 antibiotic_resistance obo:ARO_3001233 ARO:3001233 obo:ARO_3001233 pikromycin obo:ARO_3001294 A gentamicin-group aminoglycoside isolated from Micromonospora. obo:ARO_3001294 obo:aro.owl obo:ARO_3001294 PubChem:512877 obo:ARO_3001294 antibiotic_resistance obo:ARO_3001294 ARO:3001294 obo:ARO_3001294 verdamicin obo:ARO_3001295 A semisynthetic genamicin-group aminoglycoside, derived from verdamicin. obo:ARO_3001295 obo:aro.owl obo:ARO_3001295 PubChem:52948322 obo:ARO_3001295 antibiotic_resistance obo:ARO_3001295 ARO:3001295 obo:ARO_3001295 vertilimicin obo:ARO_3001296 An unusual aminoglycoside because the cyclitol ring is not amino substituted; it was discovered as a fermentation product of Streptomyces kasugaensis. obo:ARO_3001296 obo:aro.owl obo:ARO_3001296 PubChem:65174 obo:ARO_3001296 antibiotic_resistance obo:ARO_3001296 ARO:3001296 obo:ARO_3001296 kasugamycin obo:ARO_3001878 CTX-M-15 is a beta-lactamase found in the Enterobacteriaceae family obo:ARO_3001878 obo:aro.owl obo:ARO_3001878 UOE-1 obo:ARO_3001878 antibiotic_resistance obo:ARO_3001878 ARO:3001878 obo:ARO_3001878 CTX-M-15 obo:ARO_3003675 Plazomicin is a neoglycoside, or next-generation, aminoglycoside, that has been identified as a potentially useful agent to combat drug-resistant bacteria, such as Acinetobacter baumannii and Pseudomonas aeruginosa. obo:ARO_3003675 obo:aro.owl obo:ARO_3003675 PubChem:42613186 obo:ARO_3003675 ACHN-490 obo:ARO_3003675 antibiotic_resistance obo:ARO_3003675 ARO:3003675 obo:ARO_3003675 plazomicin obo:ARO_3003690 Sitafloxacin is a fluoroquinolone active against multi-resistant Gram-positive and negative pathogens. Sitafloxacin shows inhibitory activity against DNA gyrase and topoisomerase IV, which blocks bacterial DNA replication, thereby causing double-stranded breaks in the bacterial chromosome. obo:ARO_3003690 obo:aro.owl obo:ARO_3003690 PubChem:461399 obo:ARO_3003690 Gracevit obo:ARO_3003690 antibiotic_resistance obo:ARO_3003690 ARO:3003690 obo:ARO_3003690 sitafloxacin obo:ARO_3003701 Rokitamycin is a macrolide antibiotic. Synthesized from strains of Streptomyces kitasatoensis. obo:ARO_3003701 obo:aro.owl obo:ARO_3003701 PubChem:5282211 obo:ARO_3003701 antibiotic_resistance obo:ARO_3003701 ARO:3003701 obo:ARO_3003701 rokitamycin obo:ARO_3003706 Penems are a class of unsaturated beta-lactam antibiotics with a broad spectrum of antibacterial activity and have a structure which renders them highly resistant to beta-lactamases. All penems are all synthetically made and act by inhibiting the synthesis of the peptidoglycan layer of bacterial cell walls. They are structurally similar to carbapenems, however, where carbapenems have a carbon, penems have a sulfur. obo:ARO_3003706 obo:aro.owl obo:ARO_3003706 antibiotic_resistance obo:ARO_3003706 ARO:3003706 obo:ARO_3003706 penem obo:ARO_3003707 Faropenem is an orally active beta-lactam antibiotic belonging to the penem group. obo:ARO_3003707 obo:aro.owl obo:ARO_3003707 PubChem:65894 obo:ARO_3003707 antibiotic_resistance obo:ARO_3003707 ARO:3003707 obo:ARO_3003707 faropenem obo:ARO_3003708 Panipenem is a carbapenem antibacterial agent with a broad spectrum of in vitro activity covering a wide range of Gram-negative and Gram-positive aerobic and anaerobic bacterial. It is used in combination with betamipron to inhibit panipenem uptake into the renal tubule and prevent nephrotoxicity. obo:ARO_3003708 obo:aro.owl obo:ARO_3003708 PubChem:72015 obo:ARO_3003708 antibiotic_resistance obo:ARO_3003708 ARO:3003708 obo:ARO_3003708 panipenem obo:ARO_3003821 BAL30072 is a monocyclic beta-lactam antibiotic belonging to the sulfactams. BAL30072 was found to trigger the spheroplasting and lysis of Escherichia coli rather than the formation of extensive filaments. obo:ARO_3003821 obo:aro.owl obo:ARO_3003821 PubChem:52942440 obo:ARO_3003821 antibiotic_resistance obo:ARO_3003821 ARO:3003821 obo:ARO_3003821 BAL30072 obo:ARO_3003831 Temocillin is a beta-lactamase resistant carboxypenicillin. It is primarily used for the treatment of multiple drug resistant, Gram-negative bacteria, specifically Enterobacteriaceae. obo:ARO_3003831 obo:aro.owl obo:ARO_3003831 PubChem:171758 obo:ARO_3003831 BRL 17421 obo:ARO_3003831 Temocilline obo:ARO_3003831 Temocillinum obo:ARO_3003831 antibiotic_resistance obo:ARO_3003831 ARO:3003831 obo:ARO_3003831 temocillin obo:ARO_3003832 Ticarcillin is a carboxypenicillin used for the treatment of Gram-negative bacteria, particularly P. aeruginosa. Ticarcillin's antibiotic properties arise from its ability to prevent cross-linking of peptidoglycan during cell wall synthesis, when the bacteria try to divide, causing cell death. obo:ARO_3003832 obo:aro.owl obo:ARO_3003832 PubChem:36921 obo:ARO_3003832 Ticarcilina obo:ARO_3003832 Ticarcilline obo:ARO_3003832 Ticarcillinum obo:ARO_3003832 antibiotic_resistance obo:ARO_3003832 ARO:3003832 obo:ARO_3003832 ticarcillin obo:ARO_3003927 a 5th generation cephalosporin antibiotic obo:ARO_3003927 obo:aro.owl obo:ARO_3003927 PubChem:53234134 obo:ARO_3003927 Zerbaxa obo:ARO_3003927 antibiotic_resistance obo:ARO_3003927 ARO:3003927 obo:ARO_3003927 ceftolozane obo:ARO_3003936 a aminomethylcycline antibiotic that targets 16s rRNA in gram positive and gram negative bacteria obo:ARO_3003936 obo:aro.owl obo:ARO_3003936 PubChem:54697325 obo:ARO_3003936 antibiotic_resistance obo:ARO_3003936 ARO:3003936 obo:ARO_3003936 omadacycline obo:ARO_3003972 A clinically developed Macrolide antibiotic targeting gram positive and gram negative bacteria. obo:ARO_3003972 obo:aro.owl obo:ARO_3003972 PubChem:72734351 obo:ARO_3003972 CEM-101 obo:ARO_3003972 antibiotic_resistance obo:ARO_3003972 ARO:3003972 obo:ARO_3003972 Solithromycin obo:ARO_3003979 A fluorocycline that acts to inhibit the bacterial ribosome. obo:ARO_3003979 obo:aro.owl obo:ARO_3003979 PubChem:54726192 obo:ARO_3003979 7-fluoro-9-pyrrolidinoacetamido-6-demethyl-6-deoxytetracycline obo:ARO_3003979 TP-434 obo:ARO_3003979 antibiotic_resistance obo:ARO_3003979 ARO:3003979 obo:ARO_3003979 Eravacycline obo:ARO_3003993 Capreomycin is an aminoglycoside antibiotic, capable of treating a large number of infections but in particular used for killing bacteria causing tuberculosis. obo:ARO_3003993 obo:aro.owl obo:ARO_3003993 PubChem:122130878 obo:ARO_3003993 antibiotic_resistance obo:ARO_3003993 ARO:3003993 obo:ARO_3003993 capreomycin obo:ARO_3003999 Cefamandole is a second-generation cephalosporin-class beta-lactam antibiotic. obo:ARO_3003999 obo:aro.owl obo:ARO_3003999 PubChem:456255 obo:ARO_3003999 FAM obo:ARO_3003999 antibiotic_resistance obo:ARO_3003999 ARO:3003999 obo:ARO_3003999 cefamandole obo:ARO_3004000 Cefetamet is a third-generation semi-synthetic beta-lactam antibiotic that inactivates inner cell wall PBPs through targeting binding, resulting in cell lysis. obo:ARO_3004000 obo:aro.owl obo:ARO_3004000 PubChem:5487888 obo:ARO_3004000 FET obo:ARO_3004000 cefetametum obo:ARO_3004000 antibiotic_resistance obo:ARO_3004000 ARO:3004000 obo:ARO_3004000 cefetamet obo:ARO_3004001 Cefmetazole is a semi-synthetic cephamycin antibiotic with broad spectrum antibiotic activity against both gram-positive and gram-negative bacteria, that disrupt cell wall synthesis through binding to PBPs causing cell lysis. obo:ARO_3004001 obo:aro.owl obo:ARO_3004001 PubChem:42008 obo:ARO_3004001 CMZ obo:ARO_3004001 antibiotic_resistance obo:ARO_3004001 ARO:3004001 obo:ARO_3004001 cefmetazole obo:ARO_3004002 Cefonicid is a second-generation cephalosporin-class beta-lactam antibiotic with broad spectrum activity. Particularly used against urinary tract infections and lower respiratory infections. Causes cell lysis by inactivation of PBPs through binding, inhibiting peptidoglycan synthesis. obo:ARO_3004002 obo:aro.owl obo:ARO_3004002 PubChem:43594 obo:ARO_3004002 CID obo:ARO_3004002 cefonicide obo:ARO_3004002 antibiotic_resistance obo:ARO_3004002 ARO:3004002 obo:ARO_3004002 cefonicid obo:ARO_3004003 Cefoperazone is a semi-synthetic cephalosporin containing a tetrazolyl moiety that is resistant to beta-lactamases. Particularly used for treatment of Pseudomonas spp. infections. obo:ARO_3004003 obo:aro.owl obo:ARO_3004003 PubChem:44187 obo:ARO_3004003 CFP obo:ARO_3004003 cefoperazine obo:ARO_3004003 antibiotic_resistance obo:ARO_3004003 ARO:3004003 obo:ARO_3004003 cefoperazone obo:ARO_3004004 Cefotetan is a cephamycin-class beta-lactam antibiotic that is highly resistant to beta-lactamases and effective against a wide range of gram-negative and gram-positive bacteria. obo:ARO_3004004 obo:aro.owl obo:ARO_3004004 PubChem:53025 obo:ARO_3004004 CTT obo:ARO_3004004 Cefotetanum obo:ARO_3004004 antibiotic_resistance obo:ARO_3004004 ARO:3004004 obo:ARO_3004004 cefotetan obo:ARO_3004005 Cefprozil is a cephalosporin and beta-lactam antibiotic with bactericidal activity. It selectively binds to PBPs and inhibits peptidoglycan synthesis, a major cell wall component, resulting in cell lysis. obo:ARO_3004005 obo:aro.owl obo:ARO_3004005 PubChem:5281006 obo:ARO_3004005 Brisoral obo:ARO_3004005 CPR obo:ARO_3004005 Cefzil obo:ARO_3004005 antibiotic_resistance obo:ARO_3004005 ARO:3004005 obo:ARO_3004005 cefprozil obo:ARO_3004006 Ceftiofur is a third-generation broad spectrum cephalosporin and beta-lactam antibiotic. It causes cell lysis by disrupting peptidoglycan cross-linkage and cell wall formation by binding to PBPs. obo:ARO_3004006 obo:aro.owl obo:ARO_3004006 PubChem:6328657 obo:ARO_3004006 Excenel obo:ARO_3004006 Naxcel obo:ARO_3004006 antibiotic_resistance obo:ARO_3004006 ARO:3004006 obo:ARO_3004006 ceftiofur obo:ARO_3004007 Ceftizoxime is a third-generation cephalosporin and broad spectrum beta-lactam antibiotic. Ceftizoxime causes bacterial cell lysis through peptidoglycan cross-linking inhibition by binding to PBPs. obo:ARO_3004007 obo:aro.owl obo:ARO_3004007 PubChem:6533629 obo:ARO_3004007 ZOX obo:ARO_3004007 antibiotic_resistance obo:ARO_3004007 ARO:3004007 obo:ARO_3004007 ceftizoxime obo:ARO_3004008 Cephapirin is a first-generation cephalosporin and broad spectrum beta-lactam antibiotic. Inactivation of penicillin-binding proteins through cephapirin binding disrupts peptidoglycan cross-linking, resulting in cell lysis. obo:ARO_3004008 obo:aro.owl obo:ARO_3004008 PubChem:30699 obo:ARO_3004008 HAP obo:ARO_3004008 cefadyl obo:ARO_3004008 cefapirin obo:ARO_3004008 antibiotic_resistance obo:ARO_3004008 ARO:3004008 obo:ARO_3004008 cephapirin obo:ARO_3004009 Cefradine is a first-generation cephalosporin and broad spectrum beta-lactam antibiotic. Cefradine binding to penicillin-binding proteins disrupts cell wall peptidoglycan cross-linkage, resulting in cell lysis. obo:ARO_3004009 obo:aro.owl obo:ARO_3004009 PubChem:38103 obo:ARO_3004009 Cephradine obo:ARO_3004009 RAD obo:ARO_3004009 antibiotic_resistance obo:ARO_3004009 ARO:3004009 obo:ARO_3004009 cefradine obo:ARO_3004010 Cinoxacin is a fluoroquinolone antibiotic primarily used for the treatment of urinary tract infections in adults. Cinoxacin binds to DNA gyrase, resulting in double-stranded DNA breaks and cell death. obo:ARO_3004010 obo:aro.owl obo:ARO_3004010 PubChem:2762 obo:ARO_3004010 Azolinic acid obo:ARO_3004010 CIN obo:ARO_3004010 antibiotic_resistance obo:ARO_3004010 ARO:3004010 obo:ARO_3004010 cinoxacin obo:ARO_3004011 Clinafloxacin is a fluoroquinolone antibiotic and gyrase (DNA topoisomerase II) inhibitor. It binds to DNA gyrase and disrupts replication by causing double-stranded DNA breaks, resulting in cell death. obo:ARO_3004011 obo:aro.owl obo:ARO_3004011 PubChem:60063 obo:ARO_3004011 CLX obo:ARO_3004011 antibiotic_resistance obo:ARO_3004011 ARO:3004011 obo:ARO_3004011 clinafloxacin obo:ARO_3004012 Clofazimine is a fluoroquinolone-class phenazine dye used for the treatment of leprosy. Clofazimine binds to DNA and disrupts bacterial DNA gyrase, thereby causing double-stranded DNA breaks, and subsequent cell death. obo:ARO_3004012 obo:aro.owl obo:ARO_3004012 PubChem:2794 obo:ARO_3004012 Lampren obo:ARO_3004012 Lamprene obo:ARO_3004012 antibiotic_resistance obo:ARO_3004012 ARO:3004012 obo:ARO_3004012 Clofazimine obo:ARO_3004013 Fleroxacin is a broad spectrum fluoroquinolone antibiotic that inhibits the DNA supercoiling activity of bacterial DNA gyrase, resulting in double-stranded DNA breaks and subsequent cell death. obo:ARO_3004013 obo:aro.owl obo:ARO_3004013 PubChem:3357 obo:ARO_3004013 Megalocin obo:ARO_3004013 Quinodis obo:ARO_3004013 antibiotic_resistance obo:ARO_3004013 ARO:3004013 obo:ARO_3004013 fleroxacin obo:ARO_3004014 Flomoxef is a second-generation cephamycin (oxacephem) and beta-lactam antibiotic. obo:ARO_3004014 obo:aro.owl obo:ARO_3004014 PubChem:65864 obo:ARO_3004014 antibiotic_resistance obo:ARO_3004014 ARO:3004014 obo:ARO_3004014 flomoxef obo:ARO_3004015 Gentamicin A is part of a complex of broad spectrum aminoglycoside antibiotics. Gentamicin inhibits protein synthesis, resulting in bacterial cell death. obo:ARO_3004015 obo:aro.owl obo:ARO_3004015 PubChem:12810388 obo:ARO_3004015 Garamycin obo:ARO_3004015 Gentamicin obo:ARO_3004015 antibiotic_resistance obo:ARO_3004015 ARO:3004015 obo:ARO_3004015 gentamicin A obo:ARO_3004016 Loracarbef is a second-generation cephalosporin (carbacephem) and broad spectrum beta-lactam antibiotic. Loracarbef inhibits PBPs through binding, disrupting peptidoglycan cell wall cross-linkage and resulting in cell death. obo:ARO_3004016 obo:aro.owl obo:ARO_3004016 PubChem:5284585 obo:ARO_3004016 Lorabid obo:ARO_3004016 Loracarbefum obo:ARO_3004016 antibiotic_resistance obo:ARO_3004016 ARO:3004016 obo:ARO_3004016 loracarbef obo:ARO_3004017 Moxalactam (Latamoxef) is a broad spectrum cephalosporin (oxacephem) and beta-lactam antibiotic. Moxalactam binding to PBPs inhibits peptidoglycan cross-linkage in the cell wall, resulting in cell death. Moxalactam is proposed to be effective against meningitides as it passes the blood-brain barrier. obo:ARO_3004017 obo:aro.owl obo:ARO_3004017 PubChem:47499 obo:ARO_3004017 Latamoxef obo:ARO_3004017 antibiotic_resistance obo:ARO_3004017 ARO:3004017 obo:ARO_3004017 moxalactam obo:ARO_3004018 Nafcillin is a penicillin-class narrow-spectrum beta-lactam antibiotic. It inhibits cell wall synthesis and peptidoglycan cross-linkage through binding to PBPs, similarly to other penicillin-like antibiotics. obo:ARO_3004018 obo:aro.owl obo:ARO_3004018 PubChem:8982 obo:ARO_3004018 Nafcil obo:ARO_3004018 antibiotic_resistance obo:ARO_3004018 ARO:3004018 obo:ARO_3004018 nafcillin obo:ARO_3004120 CBP C1-aminomethylene vancomycin is a synthetic vancomycin derivative which exhibits multiple synergistic mechanisms of action, allowing it to effectively inhibit otherwise-glycopeptide resistant Gram-positive bacteria (notably those with functioning VanA clusters). obo:ARO_3004120 obo:aro.owl obo:ARO_3004120 antibiotic_resistance obo:ARO_3004120 ARO:3004120 obo:ARO_3004120 CBP C1-aminomethylene vancomycin obo:ARO_3004129 Cephaloridine is a semisynthetic, broad-spectrum, first-generation cephalosporin with antibacterial activity. Cephaloridine binds to and inactivates penicillin-binding proteins (PBPs) located on the inner membrane of the bacterial cell wall. PBPs are enzymes involved in the terminal stages of assembling the bacterial cell wall and in reshaping the cell wall during growth and division. Inactivation of PBPs interferes with the cross-linkage of peptidoglycan chains necessary for bacterial cell wall strength and rigidity. This results in the weakening of the bacterial cell wall and causes cell lysis. obo:ARO_3004129 obo:aro.owl obo:ARO_3004129 PubChem:5773 obo:ARO_3004129 Cefaloridin obo:ARO_3004129 Cefaloridine obo:ARO_3004129 Cefalorizin obo:ARO_3004129 Cephalomycine obo:ARO_3004129 Cephaloridin obo:ARO_3004129 Cephaloridinum obo:ARO_3004129 Ceporin obo:ARO_3004129 antibiotic_resistance obo:ARO_3004129 ARO:3004129 obo:ARO_3004129 cephaloridine obo:ARO_3004130 Balofloxacin is an 8-methoxy fluoroquinolone antibiotic. It shows potent bactericidal activity and inhibits the supercoiling activity of DNA gyrase of S. aureus, E. coli, and P. aeruginosa. obo:ARO_3004130 obo:aro.owl obo:ARO_3004130 PubChem:65958 obo:ARO_3004130 1-cyclopropyl-6-fluoro-1,4-dihydro-8-methoxy-7-(3-methylaminopiperidine-1-yl)-4-oxoquinoline-3-carboxylic acid obo:ARO_3004130 Q 35 obo:ARO_3004130 Q-35 obo:ARO_3004130 antibiotic_resistance obo:ARO_3004130 ARO:3004130 obo:ARO_3004130 balofloxacin obo:ARO_3004204 EBR beta-lactamases are Class B beta-lactamases first isolated from Empedobacter brevis and are able to hydrolyze penicillins, cephalosporins, and carbapenems. obo:ARO_3004204 obo:aro.owl obo:ARO_3004204 antibiotic_resistance obo:ARO_3004204 ARO:3004204 obo:ARO_3004204 EBR beta-lactamase obo:ARO_3004295 A ribosomally synthesized cyclic peptide antibiotic. Lassomycin has been shown to be effective against drug-resistant mycobacteria but shows little activity against other bacteria. Lassomycin targets and binds to a region of the ClpC1 ATPase complex and uncouples ATPase from proteolytic activity, an essential function for mycobacterial viability, causing cell death. obo:ARO_3004295 obo:aro.owl obo:ARO_3004295 PubChem:132528125 obo:ARO_3004295 antibiotic_resistance obo:ARO_3004295 ARO:3004295 obo:ARO_3004295 lassomycin obo:ARO_3004462 Delafloxacin is a novel fluoroquinolone antibiotic, differentiated from other on-market fluoroquinolones by the absence of a protonatable substituent conferring a weakly acidic character to the molecule. This property results in increased intracellular penetration and enhanced bactericidal activity under acidic conditions. obo:ARO_3004462 obo:aro.owl obo:ARO_3004462 PubChem:487101 obo:ARO_3004462 antibiotic_resistance obo:ARO_3004462 ARO:3004462 obo:ARO_3004462 delafloxacin obo:ARO_3004463 EBR-2 is a novel EBR-like class B beta-lactamase isolated from an extensively drug-resistant strain of Empedobacter falsenii obo:ARO_3004463 obo:aro.owl obo:ARO_3004463 antibiotic_resistance obo:ARO_3004463 ARO:3004463 obo:ARO_3004463 EBR-2 obo:ARO_3004473 A carbapenem antibiotic, administered as the oral drug tebipenem-pivoxil, shown to be effective at treating bacterial infections. obo:ARO_3004473 obo:aro.owl obo:ARO_3004473 PubChem:9800194 obo:ARO_3004473 antibiotic_resistance obo:ARO_3004473 ARO:3004473 obo:ARO_3004473 tebipenem obo:ARO_3004474 A siderophore cephalosporin with antibiotic activity against Gram-negative pathogens including and specifically Pseudomonas aeruginosa. obo:ARO_3004474 obo:aro.owl obo:ARO_3004474 PubChem:77843966 obo:ARO_3004474 antibiotic_resistance obo:ARO_3004474 ARO:3004474 obo:ARO_3004474 cefiderocol obo:ARO_3004477 Eremomycin pyrrolidide (5) is a semisynthetic glycopeptides 3-6 that is derived from vancomycin or eremomycin. It has high activity against staphylococci and enterococci, including vancomycin-resistant strains. obo:ARO_3004477 obo:aro.owl obo:ARO_3004477 antibiotic_resistance obo:ARO_3004477 ARO:3004477 obo:ARO_3004477 eremomycin pyrrolidide obo:ARO_3004499 Tosufloxacin is a fluoroquinolone antibiotic with an extended spectrum of activity. obo:ARO_3004499 obo:aro.owl obo:ARO_3004499 PubChem:5517 obo:ARO_3004499 antibiotic_resistance obo:ARO_3004499 ARO:3004499 obo:ARO_3004499 Tosufloxacin obo:ARO_3004566 Rifalazil is a rifamycin derivative antibiotic, sometimes used for treating Clostridioides difficile infections. obo:ARO_3004566 obo:aro.owl obo:ARO_3004566 PubChem:135431094 obo:ARO_3004566 antibiotic_resistance obo:ARO_3004566 ARO:3004566 obo:ARO_3004566 Rifalazil obo:BFO_0000001 entity obo:BFO_0000001 Entity obo:BFO_0000001 Julius Caesar obo:BFO_0000001 Verdi’s Requiem obo:BFO_0000001 the Second World War obo:BFO_0000001 your body mass index obo:BFO_0000001 BFO 2 Reference: In all areas of empirical inquiry we encounter general terms of two sorts. First are general terms which refer to universals or types:animaltuberculosissurgical procedurediseaseSecond, are general terms used to refer to groups of entities which instantiate a given universal but do not correspond to the extension of any subuniversal of that universal because there is nothing intrinsic to the entities in question by virtue of which they – and only they – are counted as belonging to the given group. Examples are: animal purchased by the Emperortuberculosis diagnosed on a Wednesdaysurgical procedure performed on a patient from Stockholmperson identified as candidate for clinical trial #2056-555person who is signatory of Form 656-PPVpainting by Leonardo da VinciSuch terms, which represent what are called ‘specializations’ in [81 obo:bfo/axiom/0000004 per discussion with Barry Smith http://www.referent-tracking.com/_RTU/papers/CeustersICbookRevised.pdf obo:BFO_0000001 Entity doesn't have a closure axiom because the subclasses don't necessarily exhaust all possibilites. For example Werner Ceusters 'portions of reality' include 4 sorts, entities (as BFO construes them), universals, configurations, and relations. It is an open question as to whether entities as construed in BFO will at some point also include these other portions of reality. See, for example, 'How to track absolutely everything' at http://www.referent-tracking.com/_RTU/papers/CeustersICbookRevised.pdf obo:BFO_0000001 obo:ogg.owl obo:bfo/axiom/001-001 obo:BFO_0000001 An entity is anything that exists or has existed or will exist. (axiom label in BFO2 Reference: [001-001]) obo:BFO_0000001 obo:bfo.owl obo:BFO_0000001 entity obo:BFO_0000002 continuant obo:BFO_0000002 Continuant obo:BFO_0000002 BFO 2 Reference: Continuant entities are entities which can be sliced to yield parts only along the spatial dimension, yielding for example the parts of your table which we call its legs, its top, its nails. ‘My desk stretches from the window to the door. It has spatial parts, and can be sliced (in space) in two. With respect to time, however, a thing is a continuant.’ [60, p. 240 obo:bfo/axiom/0000007 obo:BFO_0000002 Continuant doesn't have a closure axiom because the subclasses don't necessarily exhaust all possibilites. For example, in an expansion involving bringing in some of Ceuster's other portions of reality, questions are raised as to whether universals are continuants obo:BFO_0000002 obo:ogg.owl obo:bfo/axiom/008-002 obo:BFO_0000002 A continuant is an entity that persists, endures, or continues to exist through time while maintaining its identity. (axiom label in BFO2 Reference: [008-002]) obo:bfo/axiom/126-001 obo:BFO_0000002 if b is a continuant and if, for some t, c has_continuant_part b at t, then c is a continuant. (axiom label in BFO2 Reference: [126-001]) obo:bfo/axiom/009-002 obo:BFO_0000002 if b is a continuant and if, for some t, cis continuant_part of b at t, then c is a continuant. (axiom label in BFO2 Reference: [009-002]) obo:bfo/axiom/011-002 obo:BFO_0000002 if b is a material entity, then there is some temporal interval (referred to below as a one-dimensional temporal region) during which b exists. (axiom label in BFO2 Reference: [011-002]) obo:bfo/axiom/009-002 obo:BFO_0000002 (forall (x y) (if (and (Continuant x) (exists (t) (continuantPartOfAt y x t))) (Continuant y))) // axiom label in BFO2 CLIF: [009-002] obo:bfo/axiom/126-001 obo:BFO_0000002 (forall (x y) (if (and (Continuant x) (exists (t) (hasContinuantPartOfAt y x t))) (Continuant y))) // axiom label in BFO2 CLIF: [126-001] obo:bfo/axiom/008-002 obo:BFO_0000002 (forall (x) (if (Continuant x) (Entity x))) // axiom label in BFO2 CLIF: [008-002] obo:bfo/axiom/011-002 obo:BFO_0000002 (forall (x) (if (Material Entity x) (exists (t) (and (TemporalRegion t) (existsAt x t))))) // axiom label in BFO2 CLIF: [011-002] obo:BFO_0000002 obo:bfo.owl obo:BFO_0000002 continuant obo:BFO_0000003 occurrent obo:BFO_0000003 Occurrent obo:BFO_0000003 BFO 2 Reference: every occurrent that is not a temporal or spatiotemporal region is s-dependent on some independent continuant that is not a spatial region obo:BFO_0000003 BFO 2 Reference: s-dependence obtains between every process and its participants in the sense that, as a matter of necessity, this process could not have existed unless these or those participants existed also. A process may have a succession of participants at different phases of its unfolding. Thus there may be different players on the field at different times during the course of a football game; but the process which is the entire game s-depends_on all of these players nonetheless. Some temporal parts of this process will s-depend_on on only some of the players. obo:bfo/axiom/0000006 per discussion with Barry Smith obo:BFO_0000003 Occurrent doesn't have a closure axiom because the subclasses don't necessarily exhaust all possibilites. An example would be the sum of a process and the process boundary of another process. obo:bfo/axiom/0000012 obo:BFO_0000003 Simons uses different terminology for relations of occurrents to regions: Denote the spatio-temporal location of a given occurrent e by 'spn[e]' and call this region its span. We may say an occurrent is at its span, in any larger region, and covers any smaller region. Now suppose we have fixed a frame of reference so that we can speak not merely of spatio-temporal but also of spatial regions (places) and temporal regions (times). The spread of an occurrent, (relative to a frame of reference) is the space it exactly occupies, and its spell is likewise the time it exactly occupies. We write 'spr[e]' and `spl[e]' respectively for the spread and spell of e, omitting mention of the frame. obo:BFO_0000003 obo:ogg.owl obo:bfo/axiom/077-002 obo:BFO_0000003 An occurrent is an entity that unfolds itself in time or it is the instantaneous boundary of such an entity (for example a beginning or an ending) or it is a temporal or spatiotemporal region which such an entity occupies_temporal_region or occupies_spatiotemporal_region. (axiom label in BFO2 Reference: [077-002]) obo:bfo/axiom/108-001 obo:BFO_0000003 Every occurrent occupies_spatiotemporal_region some spatiotemporal region. (axiom label in BFO2 Reference: [108-001]) obo:bfo/axiom/079-001 obo:BFO_0000003 b is an occurrent entity iff b is an entity that has temporal parts. (axiom label in BFO2 Reference: [079-001]) obo:bfo/axiom/108-001 obo:BFO_0000003 (forall (x) (if (Occurrent x) (exists (r) (and (SpatioTemporalRegion r) (occupiesSpatioTemporalRegion x r))))) // axiom label in BFO2 CLIF: [108-001] obo:bfo/axiom/079-001 obo:BFO_0000003 (forall (x) (iff (Occurrent x) (and (Entity x) (exists (y) (temporalPartOf y x))))) // axiom label in BFO2 CLIF: [079-001] obo:BFO_0000003 obo:bfo.owl obo:BFO_0000003 occurrent obo:BFO_0000004 ic obo:BFO_0000004 IndependentContinuant obo:BFO_0000004 a chair obo:BFO_0000004 a heart obo:BFO_0000004 a leg obo:BFO_0000004 a molecule obo:BFO_0000004 a spatial region obo:BFO_0000004 an atom obo:BFO_0000004 an orchestra. obo:BFO_0000004 an organism obo:BFO_0000004 the bottom right portion of a human torso obo:BFO_0000004 the interior of your mouth obo:bfo/axiom/017-002 obo:BFO_0000004 b is an independent continuant = Def. b is a continuant which is such that there is no c and no t such that b s-depends_on c at t. (axiom label in BFO2 Reference: [017-002]) obo:BFO_0000004 obo:ogg.owl obo:bfo/axiom/134-001 obo:BFO_0000004 For any independent continuant b and any time t there is some spatial region r such that b is located_in r at t. (axiom label in BFO2 Reference: [134-001]) obo:bfo/axiom/018-002 obo:BFO_0000004 For every independent continuant b and time t during the region of time spanned by its life, there are entities which s-depends_on b during t. (axiom label in BFO2 Reference: [018-002]) obo:bfo/axiom/134-001 obo:BFO_0000004 (forall (x t) (if (IndependentContinuant x) (exists (r) (and (SpatialRegion r) (locatedInAt x r t))))) // axiom label in BFO2 CLIF: [134-001] obo:bfo/axiom/018-002 obo:BFO_0000004 (forall (x t) (if (and (IndependentContinuant x) (existsAt x t)) (exists (y) (and (Entity y) (specificallyDependsOnAt y x t))))) // axiom label in BFO2 CLIF: [018-002] obo:bfo/axiom/017-002 obo:BFO_0000004 (iff (IndependentContinuant a) (and (Continuant a) (not (exists (b t) (specificallyDependsOnAt a b t))))) // axiom label in BFO2 CLIF: [017-002] obo:BFO_0000004 obo:bfo.owl obo:BFO_0000004 independent continuant obo:BFO_0000006 s-region obo:BFO_0000006 SpatialRegion obo:BFO_0000006 BFO 2 Reference: Spatial regions do not participate in processes. obo:bfo/axiom/0000002 per discussion with Barry Smith obo:BFO_0000006 Spatial region doesn't have a closure axiom because the subclasses don't exhaust all possibilites. An example would be the union of a spatial point and a spatial line that doesn't overlap the point, or two spatial lines that intersect at a single point. In both cases the resultant spatial region is neither 0-dimensional, 1-dimensional, 2-dimensional, or 3-dimensional. obo:BFO_0000006 obo:ogg.owl obo:bfo/axiom/035-001 obo:BFO_0000006 A spatial region is a continuant entity that is a continuant_part_of spaceR as defined relative to some frame R. (axiom label in BFO2 Reference: [035-001]) obo:bfo/axiom/036-001 obo:BFO_0000006 All continuant parts of spatial regions are spatial regions. (axiom label in BFO2 Reference: [036-001]) obo:bfo/axiom/036-001 obo:BFO_0000006 (forall (x y t) (if (and (SpatialRegion x) (continuantPartOfAt y x t)) (SpatialRegion y))) // axiom label in BFO2 CLIF: [036-001] obo:bfo/axiom/035-001 obo:BFO_0000006 (forall (x) (if (SpatialRegion x) (Continuant x))) // axiom label in BFO2 CLIF: [035-001] obo:BFO_0000006 obo:bfo.owl obo:BFO_0000006 spatial region obo:BFO_0000008 t-region obo:BFO_0000008 TemporalRegion obo:bfo/axiom/0000003 per discussion with Barry Smith obo:BFO_0000008 Temporal region doesn't have a closure axiom because the subclasses don't exhaust all possibilites. An example would be the mereological sum of a temporal instant and a temporal interval that doesn't overlap the instant. In this case the resultant temporal region is neither 0-dimensional nor 1-dimensional obo:BFO_0000008 obo:ogg.owl obo:bfo/axiom/100-001 obo:BFO_0000008 A temporal region is an occurrent entity that is part of time as defined relative to some reference frame. (axiom label in BFO2 Reference: [100-001]) obo:bfo/axiom/101-001 obo:BFO_0000008 All parts of temporal regions are temporal regions. (axiom label in BFO2 Reference: [101-001]) obo:bfo/axiom/119-002 obo:BFO_0000008 Every temporal region t is such that t occupies_temporal_region t. (axiom label in BFO2 Reference: [119-002]) obo:bfo/axiom/119-002 obo:BFO_0000008 (forall (r) (if (TemporalRegion r) (occupiesTemporalRegion r r))) // axiom label in BFO2 CLIF: [119-002] obo:bfo/axiom/101-001 obo:BFO_0000008 (forall (x y) (if (and (TemporalRegion x) (occurrentPartOf y x)) (TemporalRegion y))) // axiom label in BFO2 CLIF: [101-001] obo:bfo/axiom/100-001 obo:BFO_0000008 (forall (x) (if (TemporalRegion x) (Occurrent x))) // axiom label in BFO2 CLIF: [100-001] obo:BFO_0000008 obo:bfo.owl obo:BFO_0000008 temporal region obo:BFO_0000009 2d-s-region obo:BFO_0000009 TwoDimensionalSpatialRegion obo:BFO_0000009 an infinitely thin plane in space. obo:BFO_0000009 the surface of a sphere-shaped part of space obo:bfo/axiom/039-001 obo:BFO_0000009 A two-dimensional spatial region is a spatial region that is of two dimensions. (axiom label in BFO2 Reference: [039-001]) obo:bfo/axiom/039-001 obo:BFO_0000009 (forall (x) (if (TwoDimensionalSpatialRegion x) (SpatialRegion x))) // axiom label in BFO2 CLIF: [039-001] obo:BFO_0000009 obo:bfo.owl obo:BFO_0000009 two-dimensional spatial region obo:BFO_0000011 st-region obo:BFO_0000011 SpatiotemporalRegion obo:BFO_0000011 the spatiotemporal region occupied by a human life obo:BFO_0000011 the spatiotemporal region occupied by a process of cellular meiosis. obo:BFO_0000011 the spatiotemporal region occupied by the development of a cancer tumor obo:BFO_0000011 obo:ogg.owl obo:bfo/axiom/095-001 obo:BFO_0000011 A spatiotemporal region is an occurrent entity that is part of spacetime. (axiom label in BFO2 Reference: [095-001]) obo:bfo/axiom/096-001 obo:BFO_0000011 All parts of spatiotemporal regions are spatiotemporal regions. (axiom label in BFO2 Reference: [096-001]) obo:bfo/axiom/099-001 obo:BFO_0000011 Each spatiotemporal region at any time t projects_onto some spatial region at t. (axiom label in BFO2 Reference: [099-001]) obo:bfo/axiom/098-001 obo:BFO_0000011 Each spatiotemporal region projects_onto some temporal region. (axiom label in BFO2 Reference: [098-001]) obo:BFO_0000011 Every spatiotemporal region occupies_spatiotemporal_region itself. obo:bfo/axiom/107-002 obo:BFO_0000011 Every spatiotemporal region s is such that s occupies_spatiotemporal_region s. (axiom label in BFO2 Reference: [107-002]) obo:bfo/axiom/107-002 obo:BFO_0000011 (forall (r) (if (SpatioTemporalRegion r) (occupiesSpatioTemporalRegion r r))) // axiom label in BFO2 CLIF: [107-002] obo:bfo/axiom/099-001 obo:BFO_0000011 (forall (x t) (if (SpatioTemporalRegion x) (exists (y) (and (SpatialRegion y) (spatiallyProjectsOntoAt x y t))))) // axiom label in BFO2 CLIF: [099-001] obo:bfo/axiom/096-001 obo:BFO_0000011 (forall (x y) (if (and (SpatioTemporalRegion x) (occurrentPartOf y x)) (SpatioTemporalRegion y))) // axiom label in BFO2 CLIF: [096-001] obo:bfo/axiom/095-001 obo:BFO_0000011 (forall (x) (if (SpatioTemporalRegion x) (Occurrent x))) // axiom label in BFO2 CLIF: [095-001] obo:bfo/axiom/098-001 obo:BFO_0000011 (forall (x) (if (SpatioTemporalRegion x) (exists (y) (and (TemporalRegion y) (temporallyProjectsOnto x y))))) // axiom label in BFO2 CLIF: [098-001] obo:BFO_0000011 obo:bfo.owl obo:BFO_0000011 spatiotemporal region obo:BFO_0000015 process obo:BFO_0000015 Process obo:BFO_0000015 a process of cell-division, \ a beating of the heart obo:BFO_0000015 a process of meiosis obo:BFO_0000015 a process of sleeping obo:BFO_0000015 the course of a disease obo:BFO_0000015 the flight of a bird obo:BFO_0000015 the life of an organism obo:BFO_0000015 your process of aging. obo:bfo/axiom/083-003 obo:BFO_0000015 p is a process = Def. p is an occurrent that has temporal proper parts and for some time t, p s-depends_on some material entity at t. (axiom label in BFO2 Reference: [083-003]) obo:BFO_0000015 BFO 2 Reference: The realm of occurrents is less pervasively marked by the presence of natural units than is the case in the realm of independent continuants. Thus there is here no counterpart of ‘object’. In BFO 1.0 ‘process’ served as such a counterpart. In BFO 2.0 ‘process’ is, rather, the occurrent counterpart of ‘material entity’. Those natural – as contrasted with engineered, which here means: deliberately executed – units which do exist in the realm of occurrents are typically either parasitic on the existence of natural units on the continuant side, or they are fiat in nature. Thus we can count lives; we can count football games; we can count chemical reactions performed in experiments or in chemical manufacturing. We cannot count the processes taking place, for instance, in an episode of insect mating behavior.Even where natural units are identifiable, for example cycles in a cyclical process such as the beating of a heart or an organism’s sleep/wake cycle, the processes in question form a sequence with no discontinuities (temporal gaps) of the sort that we find for instance where billiard balls or zebrafish or planets are separated by clear spatial gaps. Lives of organisms are process units, but they too unfold in a continuous series from other, prior processes such as fertilization, and they unfold in turn in continuous series of post-life processes such as post-mortem decay. Clear examples of boundaries of processes are almost always of the fiat sort (midnight, a time of death as declared in an operating theater or on a death certificate, the initiation of a state of war) obo:BFO_0000015 obo:ogg.owl obo:bfo/axiom/083-003 obo:BFO_0000015 (iff (Process a) (and (Occurrent a) (exists (b) (properTemporalPartOf b a)) (exists (c t) (and (MaterialEntity c) (specificallyDependsOnAt a c t))))) // axiom label in BFO2 CLIF: [083-003] obo:BFO_0000015 obo:bfo.owl obo:BFO_0000015 process obo:BFO_0000016 disposition obo:BFO_0000016 Disposition obo:BFO_0000016 an atom of element X has the disposition to decay to an atom of element Y obo:BFO_0000016 certain people have a predisposition to colon cancer obo:BFO_0000016 children are innately disposed to categorize objects in certain ways. obo:BFO_0000016 the cell wall is disposed to filter chemicals in endocitosis and exocitosis obo:BFO_0000016 BFO 2 Reference: Dispositions exist along a strength continuum. Weaker forms of disposition are realized in only a fraction of triggering cases. These forms occur in a significant number of cases of a similar type [89 obo:BFO_0000016 obo:ogg.owl obo:bfo/axiom/062-002 obo:BFO_0000016 b is a disposition means: b is a realizable entity & b’s bearer is some material entity & b is such that if it ceases to exist, then its bearer is physically changed, & b’s realization occurs when and because this bearer is in some special physical circumstances, & this realization occurs in virtue of the bearer’s physical make-up. (axiom label in BFO2 Reference: [062-002]) obo:bfo/axiom/063-002 obo:BFO_0000016 If b is a realizable entity then for all t at which b exists, b s-depends_on some material entity at t. (axiom label in BFO2 Reference: [063-002]) obo:bfo/axiom/063-002 obo:BFO_0000016 (forall (x t) (if (and (RealizableEntity x) (existsAt x t)) (exists (y) (and (MaterialEntity y) (specificallyDepends x y t))))) // axiom label in BFO2 CLIF: [063-002] obo:bfo/axiom/062-002 obo:BFO_0000016 (forall (x) (if (Disposition x) (and (RealizableEntity x) (exists (y) (and (MaterialEntity y) (bearerOfAt x y t)))))) // axiom label in BFO2 CLIF: [062-002] obo:BFO_0000016 obo:bfo.owl obo:BFO_0000016 disposition obo:BFO_0000017 realizable obo:BFO_0000017 RealizableEntity obo:BFO_0000017 the disposition of this piece of metal to conduct electricity. obo:BFO_0000017 the disposition of your blood to coagulate obo:BFO_0000017 the function of your reproductive organs obo:BFO_0000017 the role of being a doctor obo:BFO_0000017 the role of this boundary to delineate where Utah and Colorado meet obo:BFO_0000017 obo:ogg.owl obo:bfo/axiom/058-002 obo:BFO_0000017 To say that b is a realizable entity is to say that b is a specifically dependent continuant that inheres in some independent continuant which is not a spatial region and is of a type instances of which are realized in processes of a correlated type. (axiom label in BFO2 Reference: [058-002]) obo:bfo/axiom/060-002 obo:BFO_0000017 All realizable dependent continuants have independent continuants that are not spatial regions as their bearers. (axiom label in BFO2 Reference: [060-002]) obo:bfo/axiom/060-002 obo:BFO_0000017 (forall (x t) (if (RealizableEntity x) (exists (y) (and (IndependentContinuant y) (not (SpatialRegion y)) (bearerOfAt y x t))))) // axiom label in BFO2 CLIF: [060-002] obo:bfo/axiom/058-002 obo:BFO_0000017 (forall (x) (if (RealizableEntity x) (and (SpecificallyDependentContinuant x) (exists (y) (and (IndependentContinuant y) (not (SpatialRegion y)) (inheresIn x y)))))) // axiom label in BFO2 CLIF: [058-002] obo:BFO_0000017 obo:bfo.owl obo:BFO_0000017 realizable entity obo:BFO_0000018 0d-s-region obo:BFO_0000018 ZeroDimensionalSpatialRegion obo:bfo/axiom/037-001 obo:BFO_0000018 A zero-dimensional spatial region is a point in space. (axiom label in BFO2 Reference: [037-001]) obo:bfo/axiom/037-001 obo:BFO_0000018 (forall (x) (if (ZeroDimensionalSpatialRegion x) (SpatialRegion x))) // axiom label in BFO2 CLIF: [037-001] obo:BFO_0000018 obo:bfo.owl obo:BFO_0000018 zero-dimensional spatial region obo:BFO_0000019 quality obo:BFO_0000019 Quality obo:BFO_0000019 the ambient temperature of this portion of air obo:BFO_0000019 the color of a tomato obo:BFO_0000019 the length of the circumference of your waist obo:BFO_0000019 the mass of this piece of gold. obo:BFO_0000019 the shape of your nose obo:BFO_0000019 the shape of your nostril obo:BFO_0000019 obo:ogg.owl obo:bfo/axiom/055-001 obo:BFO_0000019 a quality is a specifically dependent continuant that, in contrast to roles and dispositions, does not require any further process in order to be realized. (axiom label in BFO2 Reference: [055-001]) obo:bfo/axiom/105-001 obo:BFO_0000019 If an entity is a quality at any time that it exists, then it is a quality at every time that it exists. (axiom label in BFO2 Reference: [105-001]) obo:bfo/axiom/055-001 obo:BFO_0000019 (forall (x) (if (Quality x) (SpecificallyDependentContinuant x))) // axiom label in BFO2 CLIF: [055-001] obo:bfo/axiom/105-001 obo:BFO_0000019 (forall (x) (if (exists (t) (and (existsAt x t) (Quality x))) (forall (t_1) (if (existsAt x t_1) (Quality x))))) // axiom label in BFO2 CLIF: [105-001] obo:BFO_0000019 obo:bfo.owl obo:BFO_0000019 quality obo:BFO_0000020 sdc obo:BFO_0000020 SpecificallyDependentContinuant obo:BFO_0000020 Reciprocal specifically dependent continuants: the function of this key to open this lock and the mutually dependent disposition of this lock: to be opened by this key obo:BFO_0000020 of one-sided specifically dependent continuants: the mass of this tomato obo:BFO_0000020 of relational dependent continuants (multiple bearers): John’s love for Mary, the ownership relation between John and this statue, the relation of authority between John and his subordinates. obo:BFO_0000020 the disposition of this fish to decay obo:BFO_0000020 the function of this heart: to pump blood obo:BFO_0000020 the mutual dependence of proton donors and acceptors in chemical reactions [79 obo:BFO_0000020 the mutual dependence of the role predator and the role prey as played by two organisms in a given interaction obo:BFO_0000020 the pink color of a medium rare piece of grilled filet mignon at its center obo:BFO_0000020 the role of being a doctor obo:BFO_0000020 the shape of this hole. obo:BFO_0000020 the smell of this portion of mozzarella obo:bfo/axiom/131-004 obo:BFO_0000020 b is a relational specifically dependent continuant = Def. b is a specifically dependent continuant and there are n &gt; 1 independent continuants c1, … cn which are not spatial regions are such that for all 1 i &lt; j n, ci and cj share no common parts, are such that for each 1 i n, b s-depends_on ci at every time t during the course of b’s existence (axiom label in BFO2 Reference: [131-004]) obo:bfo/axiom/050-003 obo:BFO_0000020 b is a specifically dependent continuant = Def. b is a continuant & there is some independent continuant c which is not a spatial region and which is such that b s-depends_on c at every time t during the course of b’s existence. (axiom label in BFO2 Reference: [050-003]) obo:bfo/axiom/0000005 per discussion with Barry Smith obo:BFO_0000020 Specifically dependent continuant doesn't have a closure axiom because the subclasses don't necessarily exhaust all possibilites. We're not sure what else will develop here, but for example there are questions such as what are promises, obligation, etc. obo:BFO_0000020 obo:ogg.owl obo:bfo/axiom/131-004 obo:BFO_0000020 (iff (RelationalSpecificallyDependentContinuant a) (and (SpecificallyDependentContinuant a) (forall (t) (exists (b c) (and (not (SpatialRegion b)) (not (SpatialRegion c)) (not (= b c)) (not (exists (d) (and (continuantPartOfAt d b t) (continuantPartOfAt d c t)))) (specificallyDependsOnAt a b t) (specificallyDependsOnAt a c t)))))) // axiom label in BFO2 CLIF: [131-004] obo:bfo/axiom/050-003 obo:BFO_0000020 (iff (SpecificallyDependentContinuant a) (and (Continuant a) (forall (t) (if (existsAt a t) (exists (b) (and (IndependentContinuant b) (not (SpatialRegion b)) (specificallyDependsOnAt a b t))))))) // axiom label in BFO2 CLIF: [050-003] obo:BFO_0000020 obo:bfo.owl obo:BFO_0000020 specifically dependent continuant obo:BFO_0000023 role obo:BFO_0000023 Role obo:BFO_0000023 John’s role of husband to Mary is dependent on Mary’s role of wife to John, and both are dependent on the object aggregate comprising John and Mary as member parts joined together through the relational quality of being married. obo:BFO_0000023 the priest role obo:BFO_0000023 the role of a boundary to demarcate two neighboring administrative territories obo:BFO_0000023 the role of a building in serving as a military target obo:BFO_0000023 the role of a stone in marking a property boundary obo:BFO_0000023 the role of subject in a clinical trial obo:BFO_0000023 the student role obo:BFO_0000023 BFO 2 Reference: One major family of examples of non-rigid universals involves roles, and ontologies developed for corresponding administrative purposes may consist entirely of representatives of entities of this sort. Thus ‘professor’, defined as follows,b instance_of professor at t =Def. there is some c, c instance_of professor role & c inheres_in b at t.denotes a non-rigid universal and so also do ‘nurse’, ‘student’, ‘colonel’, ‘taxpayer’, and so forth. (These terms are all, in the jargon of philosophy, phase sortals.) By using role terms in definitions, we can create a BFO conformant treatment of such entities drawing on the fact that, while an instance of professor may be simultaneously an instance of trade union member, no instance of the type professor role is also (at any time) an instance of the type trade union member role (any more than any instance of the type color is at any time an instance of the type length).If an ontology of employment positions should be defined in terms of roles following the above pattern, this enables the ontology to do justice to the fact that individuals instantiate the corresponding universals – professor, sergeant, nurse – only during certain phases in their lives. obo:BFO_0000023 obo:ogg.owl obo:bfo/axiom/061-001 obo:BFO_0000023 b is a role means: b is a realizable entity & b exists because there is some single bearer that is in some special physical, social, or institutional set of circumstances in which this bearer does not have to be& b is not such that, if it ceases to exist, then the physical make-up of the bearer is thereby changed. (axiom label in BFO2 Reference: [061-001]) obo:bfo/axiom/061-001 obo:BFO_0000023 (forall (x) (if (Role x) (RealizableEntity x))) // axiom label in BFO2 CLIF: [061-001] obo:BFO_0000023 obo:bfo.owl obo:BFO_0000023 role obo:BFO_0000026 1d-s-region obo:BFO_0000026 OneDimensionalSpatialRegion obo:BFO_0000026 an edge of a cube-shaped portion of space. obo:bfo/axiom/038-001 obo:BFO_0000026 A one-dimensional spatial region is a line or aggregate of lines stretching from one point in space to another. (axiom label in BFO2 Reference: [038-001]) obo:bfo/axiom/038-001 obo:BFO_0000026 (forall (x) (if (OneDimensionalSpatialRegion x) (SpatialRegion x))) // axiom label in BFO2 CLIF: [038-001] obo:BFO_0000026 obo:bfo.owl obo:BFO_0000026 one-dimensional spatial region obo:BFO_0000028 3d-s-region obo:BFO_0000028 ThreeDimensionalSpatialRegion obo:BFO_0000028 a cube-shaped region of space obo:BFO_0000028 a sphere-shaped region of space, obo:BFO_0000028 obo:ogg.owl obo:bfo/axiom/040-001 obo:BFO_0000028 A three-dimensional spatial region is a spatial region that is of three dimensions. (axiom label in BFO2 Reference: [040-001]) obo:bfo/axiom/040-001 obo:BFO_0000028 (forall (x) (if (ThreeDimensionalSpatialRegion x) (SpatialRegion x))) // axiom label in BFO2 CLIF: [040-001] obo:BFO_0000028 obo:bfo.owl obo:BFO_0000028 three-dimensional spatial region obo:BFO_0000029 site obo:BFO_0000029 Site obo:BFO_0000029 Manhattan Canyon) obo:BFO_0000029 a hole in the interior of a portion of cheese obo:BFO_0000029 a rabbit hole obo:BFO_0000029 an air traffic control region defined in the airspace above an airport obo:BFO_0000029 the Grand Canyon obo:BFO_0000029 the Piazza San Marco obo:BFO_0000029 the cockpit of an aircraft obo:BFO_0000029 the hold of a ship obo:BFO_0000029 the interior of a kangaroo pouch obo:BFO_0000029 the interior of the trunk of your car obo:BFO_0000029 the interior of your bedroom obo:BFO_0000029 the interior of your office obo:BFO_0000029 the interior of your refrigerator obo:BFO_0000029 the lumen of your gut obo:BFO_0000029 your left nostril (a fiat part – the opening – of your left nasal cavity) obo:bfo/axiom/034-002 obo:BFO_0000029 b is a site means: b is a three-dimensional immaterial entity that is (partially or wholly) bounded by a material entity or it is a three-dimensional immaterial part thereof. (axiom label in BFO2 Reference: [034-002]) obo:bfo/axiom/034-002 obo:BFO_0000029 (forall (x) (if (Site x) (ImmaterialEntity x))) // axiom label in BFO2 CLIF: [034-002] obo:BFO_0000029 obo:bfo.owl obo:BFO_0000029 site obo:BFO_0000031 gdc obo:BFO_0000031 GenericallyDependentContinuant obo:BFO_0000031 The entries in your database are patterns instantiated as quality instances in your hard drive. The database itself is an aggregate of such patterns. When you create the database you create a particular instance of the generically dependent continuant type database. Each entry in the database is an instance of the generically dependent continuant type IAO: information content entity. obo:BFO_0000031 the pdf file on your laptop, the pdf file that is a copy thereof on my laptop obo:BFO_0000031 the sequence of this protein molecule; the sequence that is a copy thereof in that protein molecule. obo:bfo/axiom/074-001 obo:BFO_0000031 b is a generically dependent continuant = Def. b is a continuant that g-depends_on one or more other entities. (axiom label in BFO2 Reference: [074-001]) obo:BFO_0000031 obo:ogg.owl obo:bfo/axiom/074-001 obo:BFO_0000031 (iff (GenericallyDependentContinuant a) (and (Continuant a) (exists (b t) (genericallyDependsOnAt a b t)))) // axiom label in BFO2 CLIF: [074-001] obo:BFO_0000031 obo:bfo.owl obo:BFO_0000031 generically dependent continuant obo:BFO_0000034 function obo:BFO_0000034 Function obo:BFO_0000034 the function of a hammer to drive in nails obo:BFO_0000034 the function of a heart pacemaker to regulate the beating of a heart through electricity obo:BFO_0000034 the function of amylase in saliva to break down starch into sugar obo:BFO_0000034 BFO 2 Reference: In the past, we have distinguished two varieties of function, artifactual function and biological function. These are not asserted subtypes of BFO:function however, since the same function – for example: to pump, to transport – can exist both in artifacts and in biological entities. The asserted subtypes of function that would be needed in order to yield a separate monoheirarchy are not artifactual function, biological function, etc., but rather transporting function, pumping function, etc. obo:bfo/axiom/064-001 obo:BFO_0000034 A function is a disposition that exists in virtue of the bearer’s physical make-up and this physical make-up is something the bearer possesses because it came into being, either through evolution (in the case of natural biological entities) or through intentional design (in the case of artifacts), in order to realize processes of a certain sort. (axiom label in BFO2 Reference: [064-001]) obo:bfo/axiom/064-001 obo:BFO_0000034 (forall (x) (if (Function x) (Disposition x))) // axiom label in BFO2 CLIF: [064-001] obo:BFO_0000034 obo:bfo.owl obo:BFO_0000034 function obo:BFO_0000035 p-boundary obo:BFO_0000035 ProcessBoundary obo:BFO_0000035 the boundary between the 2nd and 3rd year of your life. obo:bfo/axiom/084-001 obo:BFO_0000035 p is a process boundary =Def. p is a temporal part of a process & p has no proper temporal parts. (axiom label in BFO2 Reference: [084-001]) obo:BFO_0000035 obo:ogg.owl obo:bfo/axiom/085-002 obo:BFO_0000035 Every process boundary occupies_temporal_region a zero-dimensional temporal region. (axiom label in BFO2 Reference: [085-002]) obo:bfo/axiom/085-002 obo:BFO_0000035 (forall (x) (if (ProcessBoundary x) (exists (y) (and (ZeroDimensionalTemporalRegion y) (occupiesTemporalRegion x y))))) // axiom label in BFO2 CLIF: [085-002] obo:bfo/axiom/084-001 obo:BFO_0000035 (iff (ProcessBoundary a) (exists (p) (and (Process p) (temporalPartOf a p) (not (exists (b) (properTemporalPartOf b a)))))) // axiom label in BFO2 CLIF: [084-001] obo:BFO_0000035 obo:bfo.owl obo:BFO_0000035 process boundary obo:BFO_0000038 1d-t-region obo:BFO_0000038 OneDimensionalTemporalRegion obo:BFO_0000038 the temporal region during which a process occurs. obo:BFO_0000038 BFO 2 Reference: A temporal interval is a special kind of one-dimensional temporal region, namely one that is self-connected (is without gaps or breaks). obo:bfo/axiom/103-001 obo:BFO_0000038 A one-dimensional temporal region is a temporal region that is extended. (axiom label in BFO2 Reference: [103-001]) obo:bfo/axiom/103-001 obo:BFO_0000038 (forall (x) (if (OneDimensionalTemporalRegion x) (TemporalRegion x))) // axiom label in BFO2 CLIF: [103-001] obo:BFO_0000038 obo:bfo.owl obo:BFO_0000038 one-dimensional temporal region obo:BFO_0000040 material obo:BFO_0000040 MaterialEntity obo:BFO_0000040 a flame obo:BFO_0000040 a forest fire obo:BFO_0000040 a human being obo:BFO_0000040 a hurricane obo:BFO_0000040 a photon obo:BFO_0000040 a puff of smoke obo:BFO_0000040 a sea wave obo:BFO_0000040 a tornado obo:BFO_0000040 an aggregate of human beings. obo:BFO_0000040 an energy wave obo:BFO_0000040 an epidemic obo:BFO_0000040 the undetached arm of a human being obo:BFO_0000040 BFO 2 Reference: Material entities (continuants) can preserve their identity even while gaining and losing material parts. Continuants are contrasted with occurrents, which unfold themselves in successive temporal parts or phases [60 obo:BFO_0000040 BFO 2 Reference: Object, Fiat Object Part and Object Aggregate are not intended to be exhaustive of Material Entity. Users are invited to propose new subcategories of Material Entity. obo:BFO_0000040 BFO 2 Reference: ‘Matter’ is intended to encompass both mass and energy (we will address the ontological treatment of portions of energy in a later version of BFO). A portion of matter is anything that includes elementary particles among its proper or improper parts: quarks and leptons, including electrons, as the smallest particles thus far discovered; baryons (including protons and neutrons) at a higher level of granularity; atoms and molecules at still higher levels, forming the cells, organs, organisms and other material entities studied by biologists, the portions of rock studied by geologists, the fossils studied by paleontologists, and so on.Material entities are three-dimensional entities (entities extended in three spatial dimensions), as contrasted with the processes in which they participate, which are four-dimensional entities (entities extended also along the dimension of time).According to the FMA, material entities may have immaterial entities as parts – including the entities identified below as sites; for example the interior (or ‘lumen’) of your small intestine is a part of your body. BFO 2.0 embodies a decision to follow the FMA here. obo:BFO_0000040 obo:ogg.owl obo:bfo/axiom/019-002 obo:BFO_0000040 A material entity is an independent continuant that has some portion of matter as proper or improper continuant part. (axiom label in BFO2 Reference: [019-002]) obo:bfo/axiom/020-002 obo:BFO_0000040 Every entity which has a material entity as continuant part is a material entity. (axiom label in BFO2 Reference: [020-002]) obo:bfo/axiom/021-002 obo:BFO_0000040 every entity of which a material entity is continuant part is also a material entity. (axiom label in BFO2 Reference: [021-002]) obo:bfo/axiom/019-002 obo:BFO_0000040 (forall (x) (if (MaterialEntity x) (IndependentContinuant x))) // axiom label in BFO2 CLIF: [019-002] obo:bfo/axiom/021-002 obo:BFO_0000040 (forall (x) (if (and (Entity x) (exists (y t) (and (MaterialEntity y) (continuantPartOfAt x y t)))) (MaterialEntity x))) // axiom label in BFO2 CLIF: [021-002] obo:bfo/axiom/020-002 obo:BFO_0000040 (forall (x) (if (and (Entity x) (exists (y t) (and (MaterialEntity y) (continuantPartOfAt y x t)))) (MaterialEntity x))) // axiom label in BFO2 CLIF: [020-002] obo:BFO_0000040 obo:bfo.owl obo:BFO_0000040 material entity obo:BFO_0000050 part of obo:BFO_0000050 part of obo:BFO_0000051 has part obo:BFO_0000051 has_part obo:BFO_0000051 obo:ogg.owl obo:BFO_0000051 obo:ro.owl obo:BFO_0000051 obo:RO_0001901 obo:BFO_0000051 has part obo:BFO_0000051 has part obo:BFO_0000052 inheres-in_at obo:BFO_0000052 inheresInAt obo:bfo/axiom/051-002 obo:BFO_0000052 b inheres_in c at t =Def. b is a dependent continuant & c is an independent continuant that is not a spatial region & b s-depends_on c at t. (axiom label in BFO2 Reference: [051-002]) obo:BFO_0000052 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance-level, relation. The BFO reading of the binary relation 'inheres in at all times@en' is: forall(t) exists_at(x,t) -> exists_at(y,t) and 'inheres in@en(x,y,t)'. obo:BFO_0000052 BFO 2 Reference: Inherence is a subrelation of s-depends_on which holds between a dependent continuant and an independent continuant that is not a spatial region. Since dependent continuants cannot migrate from one independent continuant bearer to another, it follows that if b s-depends_on independent continuant c at some time, then b s-depends_on c at all times at which a exists. Inherence is in this sense redundantly time-indexed.For example, consider the particular instance of openness inhering in my mouth at t as I prepare to take a bite out of a donut, followed by a closedness at t+1 when I bite the donut and start chewing. The openness instance is then shortlived, and to say that it s-depends_on my mouth at all times at which this openness exists, means: at all times during this short life. Every time you make a fist, you make a new (instance of the universal) fist. (Every time your hand has the fist-shaped quality, there is created a new instance of the universal fist-shaped quality.) obo:BFO_0000052 BFO2 Reference: independent continuant that is not a spatial region obo:BFO_0000052 BFO2 Reference: specifically dependent continuant obo:BFO_0000052 obo:ogg.owl obo:bfo/axiom/051-002 obo:BFO_0000052 (iff (inheresInAt a b t) (and (DependentContinuant a) (IndependentContinuant b) (not (SpatialRegion b)) (specificallyDependsOnAt a b t))) // axiom label in BFO2 CLIF: [051-002] obo:BFO_0000052 obo:bfo.owl obo:BFO_0000052 inheres in at all times obo:BFO_0000053 bearer-of_st obo:BFO_0000053 bearerOfAt obo:bfo/axiom/053-004 obo:BFO_0000053 b bearer_of c at t =Def. c s-depends_on b at t & b is an independent continuant that is not a spatial region. (axiom label in BFO2 Reference: [053-004]) obo:BFO_0000053 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance level, relation. The BFO reading of the binary relation 'bearer of at some time@en' is: exists t, exists_at(x,t) & exists_at(y,t) & 'bearer of@en'(x,y,t) obo:BFO_0000053 BFO2 Reference: independent continuant that is not a spatial region obo:BFO_0000053 BFO2 Reference: specifically dependent continuant obo:bfo/axiom/053-004 obo:BFO_0000053 (iff (bearerOfAt a b t) (and (specificallyDependsOnAt b a t) (IndependentContinuant a) (not (SpatialRegion a)) (existsAt b t))) // axiom label in BFO2 CLIF: [053-004] obo:BFO_0000053 obo:bfo.owl obo:BFO_0000053 bearer of at some time obo:BFO_0000054 realized-in obo:BFO_0000054 realizedIn obo:BFO_0000054 [copied from inverse property 'realizes'] to say that b realizes c at t is to assert that there is some material entity d & b is a process which has participant d at t & c is a disposition or role of which d is bearer_of at t& the type instantiated by b is correlated with the type instantiated by c. (axiom label in BFO2 Reference: [059-003]) obo:bfo/axiom/106-002 obo:BFO_0000054 if a realizable entity b is realized in a process p, then p stands in the has_participant relation to the bearer of b. (axiom label in BFO2 Reference: [106-002]) obo:bfo/axiom/106-002 obo:BFO_0000054 (forall (x y z t) (if (and (RealizableEntity x) (Process y) (realizesAt y x t) (bearerOfAt z x t)) (hasParticipantAt y z t))) // axiom label in BFO2 CLIF: [106-002] obo:BFO_0000054 obo:bfo.owl obo:BFO_0000054 realized in obo:BFO_0000055 realizes obo:BFO_0000055 realizes obo:bfo/axiom/059-003 obo:BFO_0000055 to say that b realizes c at t is to assert that there is some material entity d & b is a process which has participant d at t & c is a disposition or role of which d is bearer_of at t& the type instantiated by b is correlated with the type instantiated by c. (axiom label in BFO2 Reference: [059-003]) obo:bfo/axiom/059-003 obo:BFO_0000055 (forall (x y t) (if (realizesAt x y t) (and (Process x) (or (Disposition y) (Role y)) (exists (z) (and (MaterialEntity z) (hasParticipantAt x z t) (bearerOfAt z y t)))))) // axiom label in BFO2 CLIF: [059-003] obo:BFO_0000055 obo:bfo.owl obo:BFO_0000055 realizes obo:BFO_0000056 participates-in_st obo:BFO_0000056 participatesInAt obo:BFO_0000056 [copied from inverse property 'has participant at some time'] Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance level, relation. The BFO reading of the binary relation 'has participant at some time@en' is: exists t, exists_at(x,t) & exists_at(y,t) & 'has participant@en'(x,y,t) obo:BFO_0000056 [copied from inverse property 'has participant at some time'] BFO 2 Reference: Spatial regions do not participate in processes. obo:BFO_0000056 [copied from inverse property 'has participant at some time'] BFO2 Reference: independent continuant that is not a spatial region, specifically dependent continuant, generically dependent continuant obo:BFO_0000056 [copied from inverse property 'has participant at some time'] BFO2 Reference: process obo:BFO_0000056 [copied from inverse property 'has participant at some time'] has_participant is an instance-level relation between a process, a continuant, and a temporal region at which the continuant participates in some way in the process. (axiom label in BFO2 Reference: [086-003]) obo:BFO_0000056 obo:bfo.owl obo:BFO_0000056 participates in at some time obo:BFO_0000057 has-participant_st obo:BFO_0000057 hasParticipantAt obo:BFO_0000057 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance level, relation. The BFO reading of the binary relation 'has participant at some time@en' is: exists t, exists_at(x,t) & exists_at(y,t) & 'has participant@en'(x,y,t) obo:BFO_0000057 BFO 2 Reference: Spatial regions do not participate in processes. obo:BFO_0000057 BFO2 Reference: independent continuant that is not a spatial region, specifically dependent continuant, generically dependent continuant obo:BFO_0000057 BFO2 Reference: process obo:bfo/axiom/086-003 obo:BFO_0000057 has_participant is an instance-level relation between a process, a continuant, and a temporal region at which the continuant participates in some way in the process. (axiom label in BFO2 Reference: [086-003]) obo:bfo/axiom/091-003 obo:BFO_0000057 if b has_participant c at t & c is a generically dependent continuant, then there is some independent continuant that is not a spatial region d, and which is such that c g-depends on d at t & b s-depends_on d at t. (axiom label in BFO2 Reference: [091-003]) obo:bfo/axiom/090-003 obo:BFO_0000057 if b has_participant c at t & c is a specifically dependent continuant, then there is some independent continuant that is not a spatial region d, c s-depends_on d at t & b s-depends_on d at t. (axiom label in BFO2 Reference: [090-003]) obo:bfo/axiom/087-001 obo:BFO_0000057 if b has_participant c at t then b is an occurrent. (axiom label in BFO2 Reference: [087-001]) obo:bfo/axiom/089-001 obo:BFO_0000057 if b has_participant c at t then c exists at t. (axiom label in BFO2 Reference: [089-001]) obo:bfo/axiom/088-001 obo:BFO_0000057 if b has_participant c at t then c is a continuant. (axiom label in BFO2 Reference: [088-001]) obo:bfo/axiom/091-003 obo:BFO_0000057 (forall (x y t) (if (and (hasParticipantAt x y t) (GenericallyDependentContinuant y)) (exists (z) (and (IndependentContinuant z) (not (SpatialRegion z)) (genericallyDependsOn y z t) (specificallyDependsOnAt x z t))))) // axiom label in BFO2 CLIF: [091-003] obo:bfo/axiom/090-003 obo:BFO_0000057 (forall (x y t) (if (and (hasParticipantAt x y t) (SpecificallyDependentContinuant y)) (exists (z) (and (IndependentContinuant z) (not (SpatialRegion z)) (specificallyDependsOnAt x z t) (specificallyDependsOnAt y z t))))) // axiom label in BFO2 CLIF: [090-003] obo:bfo/axiom/088-001 obo:BFO_0000057 (forall (x y t) (if (hasParticipantAt x y t) (Continuant y))) // axiom label in BFO2 CLIF: [088-001] obo:bfo/axiom/087-001 obo:BFO_0000057 (forall (x y t) (if (hasParticipantAt x y t) (Occurrent x))) // axiom label in BFO2 CLIF: [087-001] obo:bfo/axiom/089-001 obo:BFO_0000057 (forall (x y t) (if (hasParticipantAt x y t) (existsAt y t))) // axiom label in BFO2 CLIF: [089-001] obo:BFO_0000057 obo:bfo.owl obo:BFO_0000057 has participant at some time obo:BFO_0000058 concretized-by_st obo:BFO_0000058 [copied from inverse property 'concretizes at some time'] You may concretize a piece of software by installing it in your computer obo:BFO_0000058 [copied from inverse property 'concretizes at some time'] You may concretize a recipe that you find in a cookbook by turning it into a plan which exists as a realizable dependent continuant in your head. obo:BFO_0000058 [copied from inverse property 'concretizes at some time'] you may concretize a poem as a pattern of memory traces in your head obo:BFO_0000058 [copied from inverse property 'concretizes at some time'] Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance level, relation. The BFO reading of the binary relation 'concretizes at some time@en' is: exists t, exists_at(x,t) & exists_at(y,t) & 'concretizes@en'(x,y,t) obo:BFO_0000058 obo:ogg.owl obo:BFO_0000058 [copied from inverse property 'concretizes at some time'] b concretizes c at t means: b is a specifically dependent continuant & c is a generically dependent continuant & for some independent continuant that is not a spatial region d, b s-depends_on d at t & c g-depends on d at t & if c migrates from bearer d to another bearer e than a copy of b will be created in e. (axiom label in BFO2 Reference: [075-002]) obo:BFO_0000058 obo:bfo.owl obo:BFO_0000058 concretized by at some time obo:BFO_0000059 concretizes_st obo:BFO_0000059 concretizesAt obo:BFO_0000059 You may concretize a piece of software by installing it in your computer obo:BFO_0000059 You may concretize a recipe that you find in a cookbook by turning it into a plan which exists as a realizable dependent continuant in your head. obo:BFO_0000059 you may concretize a poem as a pattern of memory traces in your head obo:BFO_0000059 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance level, relation. The BFO reading of the binary relation 'concretizes at some time@en' is: exists t, exists_at(x,t) & exists_at(y,t) & 'concretizes@en'(x,y,t) obo:BFO_0000059 obo:ogg.owl obo:bfo/axiom/075-002 obo:BFO_0000059 b concretizes c at t means: b is a specifically dependent continuant & c is a generically dependent continuant & for some independent continuant that is not a spatial region d, b s-depends_on d at t & c g-depends on d at t & if c migrates from bearer d to another bearer e than a copy of b will be created in e. (axiom label in BFO2 Reference: [075-002]) obo:bfo/axiom/076-001 obo:BFO_0000059 if b g-depends on c at some time t, then there is some d, such that d concretizes b at t and d s-depends_on c at t. (axiom label in BFO2 Reference: [076-001]) obo:bfo/axiom/075-002 obo:BFO_0000059 (forall (x y t) (if (concretizesAt x y t) (and (SpecificallyDependentContinuant x) (GenericallyDependentContinuant y) (exists (z) (and (IndependentContinuant z) (specificallyDependsOnAt x z t) (genericallyDependsOnAt y z t)))))) // axiom label in BFO2 CLIF: [075-002] obo:bfo/axiom/076-001 obo:BFO_0000059 (forall (x y t) (if (genericallyDependsOnAt x y t) (exists (z) (and (concretizesAt z x t) (specificallyDependsOnAt z y t))))) // axiom label in BFO2 CLIF: [076-001] obo:BFO_0000059 obo:bfo.owl obo:BFO_0000059 concretizes at some time obo:BFO_0000066 occurs-in obo:BFO_0000066 occursIn obo:BFO_0000066 b occurs_in c =def b is a process and c is a material entity or immaterial entity& there exists a spatiotemporal region r and b occupies_spatiotemporal_region r.& forall(t) if b exists_at t then c exists_at t & there exist spatial regions s and s’ where & b spatially_projects_onto s at t& c is occupies_spatial_region s’ at t& s is a proper_continuant_part_of s’ at t [XXX-001 obo:BFO_0000066 obo:bfo.owl obo:BFO_0000066 occurs in obo:BFO_0000066 occurs in obo:BFO_0000067 contains-process obo:BFO_0000067 containsProcess obo:BFO_0000067 [copied from inverse property 'occurs in'] b occurs_in c =def b is a process and c is a material entity or immaterial entity& there exists a spatiotemporal region r and b occupies_spatiotemporal_region r.& forall(t) if b exists_at t then c exists_at t & there exist spatial regions s and s’ where & b spatially_projects_onto s at t& c is occupies_spatial_region s’ at t& s is a proper_continuant_part_of s’ at t [XXX-001 obo:BFO_0000067 obo:bfo.owl obo:BFO_0000067 contains process obo:BFO_0000070 s-depends-on_at obo:BFO_0000070 specificallyDependsOn obo:BFO_0000070 A pain s-depends_on the organism that is experiencing the pain obo:BFO_0000070 a gait s-depends_on the walking object. (All at some specific time.) obo:BFO_0000070 a shape s-depends_on the shaped object obo:BFO_0000070 one-sided s-dependence of a dependent continuant on an independent continuant: an instance of headache s-depends_on some head obo:BFO_0000070 one-sided s-dependence of a dependent continuant on an independent continuant: an instance of temperature s-depends_on some organism obo:BFO_0000070 one-sided s-dependence of a process on something: a process of cell death s-depends_on a cell obo:BFO_0000070 one-sided s-dependence of a process on something: an instance of seeing (a relational process) s-depends_on some organism and on some seen entity, which may be an occurrent or a continuant obo:BFO_0000070 one-sided s-dependence of one occurrent on another: a process of answering a question is dependent on a prior process of asking a question obo:BFO_0000070 one-sided s-dependence of one occurrent on another: a process of obeying a command is dependent on a prior process of issuing a command obo:BFO_0000070 one-sided s-dependence of one occurrent on multiple independent continuants: a relational process of hitting a ball with a cricket bat obo:BFO_0000070 one-sided s-dependence of one occurrent on multiple independent continuants: a relational process of paying cash to a merchant in exchange for a bag of figs obo:BFO_0000070 reciprocal s-dependence between occurrents: a process of buying and the associated process of selling obo:BFO_0000070 reciprocal s-dependence between occurrents: a process of increasing the volume of a portion of gas while temperature remains constant and the associated process of decreasing the pressure exerted by the gas obo:BFO_0000070 reciprocal s-dependence between occurrents: in a game of chess the process of playing with the white pieces is mutually dependent on the process of playing with the black pieces obo:BFO_0000070 the one-sided dependence of an occurrent on an independent continuant: football match on the players, the ground, the ball obo:BFO_0000070 the one-sided dependence of an occurrent on an independent continuant: handwave on a hand obo:BFO_0000070 the three-sided reciprocal s-dependence of the hue, saturation and brightness of a color [45 obo:BFO_0000070 the three-sided reciprocal s-dependence of the pitch, timbre and volume of a tone [45 obo:BFO_0000070 the two-sided reciprocal s-dependence of the roles of husband and wife [20 obo:BFO_0000070 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance-level, relation. The BFO reading of the binary relation 'specifically depends on at all times@en' is: forall(t) exists_at(x,t) -> exists_at(y,t) and 'specifically depends on@en(x,y,t)'. obo:BFO_0000070 BFO 2 Reference: An entity – for example an act of communication or a game of football – can s-depends_on more than one entity. Complex phenomena for example in the psychological and social realms (such as inferring, commanding and requesting) or in the realm of multi-organismal biological processes (such as infection and resistance), will involve multiple families of dependence relations, involving both continuants and occurrents [1, 4, 28 obo:BFO_0000070 BFO 2 Reference: S-dependence is just one type of dependence among many; it is what, in the literature, is referred to as ‘existential dependence’ [87, 46, 65, 20 obo:BFO_0000070 BFO 2 Reference: the relation of s-depends_on does not in every case require simultaneous existence of its relata. Note the difference between such cases and the cases of continuant universals defined historically: the act of answering depends existentially on the prior act of questioning; the human being who was baptized or who answered a question does not himself depend existentially on the prior act of baptism or answering. He would still exist even if these acts had never taken place. obo:BFO_0000070 BFO2 Reference: specifically dependent continuant\; process; process boundary obo:BFO_0000070 obo:ogg.owl obo:BFO_0000070 To say that b s-depends_on a at t is to say that b and c do not share common parts & b is of its nature such that it cannot exist unless c exists & b is not a boundary of c and b is not a site of which c is the host [64 obo:bfo/axiom/052-001 obo:BFO_0000070 If b is s-depends_on something at some time, then b is not a material entity. (axiom label in BFO2 Reference: [052-001]) obo:bfo/axiom/136-001 obo:BFO_0000070 If b s-depends_on something at t, then there is some c, which is an independent continuant and not a spatial region, such that b s-depends_on c at t. (axiom label in BFO2 Reference: [136-001]) obo:bfo/axiom/015-002 obo:BFO_0000070 If occurrent b s-depends_on some independent continuant c at t, then b s-depends_on c at every time at which b exists. (axiom label in BFO2 Reference: [015-002]) obo:bfo/axiom/013-002 obo:BFO_0000070 an entity does not s-depend_on any of its (continuant or occurrent) parts or on anything it is part of. (axiom label in BFO2 Reference: [013-002]) obo:bfo/axiom/054-002 obo:BFO_0000070 if b s-depends_on c at t & c s-depends_on d at t then b s-depends_on d at t. (axiom label in BFO2 Reference: [054-002]) obo:bfo/axiom/013-002 obo:BFO_0000070 (forall (x y t) (if (and (Entity x) (or (continuantPartOfAt y x t) (continuantPartOfAt x y t) (occurrentPartOf x y) (occurrentPartOf y x))) (not (specificallyDependsOnAt x y t)))) // axiom label in BFO2 CLIF: [013-002] obo:bfo/axiom/015-002 obo:BFO_0000070 (forall (x y t) (if (and (Occurrent x) (IndependentContinuant y) (specificallyDependsOnAt x y t)) (forall (t_1) (if (existsAt x t_1) (specificallyDependsOnAt x y t_1))))) // axiom label in BFO2 CLIF: [015-002] obo:bfo/axiom/136-001 obo:BFO_0000070 (forall (x y t) (if (specificallyDependsOnAt x y t) (exists (z) (and (IndependentContinuant z) (not (SpatialRegion z)) (specificallyDependsOnAt x z t))))) // axiom label in BFO2 CLIF: [136-001] obo:bfo/axiom/054-002 obo:BFO_0000070 (forall (x y z t) (if (and (specificallyDependsOnAt x y t) (specificallyDependsOnAt y z t)) (specificallyDependsOnAt x z t))) // axiom label in BFO2 CLIF: [054-002] obo:bfo/axiom/052-001 obo:BFO_0000070 (forall (x) (if (exists (y t) (specificallyDependsOnAt x y t)) (not (MaterialEntity x)))) // axiom label in BFO2 CLIF: [052-001] obo:BFO_0000070 obo:bfo.owl obo:BFO_0000070 specifically depends on at all times obo:BFO_0000079 f-of_at obo:BFO_0000079 functionOfAt obo:bfo/axiom/067-001 obo:BFO_0000079 a function_of b at t =Def. a is a function and a inheres_in b at t. (axiom label in BFO2 Reference: [067-001]) obo:BFO_0000079 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance-level, relation. The BFO reading of the binary relation 'function of at all times@en' is: forall(t) exists_at(x,t) -> exists_at(y,t) and 'function of@en(x,y,t)'. obo:bfo/axiom/067-001 obo:BFO_0000079 (iff (functionOf a b t) (and (Function a) (inheresInAt a b t))) // axiom label in BFO2 CLIF: [067-001] obo:BFO_0000079 obo:bfo.owl obo:BFO_0000079 function of at all times obo:BFO_0000080 q-of_at obo:BFO_0000080 qualityOfAt obo:bfo/axiom/056-002 obo:BFO_0000080 b quality_of c at t = Def. b is a quality & c is an independent continuant that is not a spatial region & b s-depends_on c at t. (axiom label in BFO2 Reference: [056-002]) obo:BFO_0000080 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance-level, relation. The BFO reading of the binary relation 'quality of at all times@en' is: forall(t) exists_at(x,t) -> exists_at(y,t) and 'quality of@en(x,y,t)'. obo:bfo/axiom/056-002 obo:BFO_0000080 (iff (qualityOfAt a b t) (and (Quality a) (IndependentContinuant b) (not (SpatialRegion b)) (specificallyDependsOnAt a b t))) // axiom label in BFO2 CLIF: [056-002] obo:BFO_0000080 obo:bfo.owl obo:BFO_0000080 quality of at all times obo:BFO_0000081 r-of_at obo:BFO_0000081 roleOfAt obo:bfo/axiom/065-001 obo:BFO_0000081 a role_of b at t =Def. a is a role and a inheres_in b at t. (axiom label in BFO2 Reference: [065-001]) obo:BFO_0000081 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance-level, relation. The BFO reading of the binary relation 'role of at all times@en' is: forall(t) exists_at(x,t) -> exists_at(y,t) and 'role of@en(x,y,t)'. obo:bfo/axiom/065-001 obo:BFO_0000081 (iff (roleOfAt a b t) (and (Role a) (inheresInAt a b t))) // axiom label in BFO2 CLIF: [065-001] obo:BFO_0000081 obo:bfo.owl obo:BFO_0000081 role of at all times obo:BFO_0000082 located-in_at obo:BFO_0000082 locatedInAt obo:BFO_0000082 Mary located_in Salzburg obo:BFO_0000082 the Empire State Building located_in New York. obo:BFO_0000082 this portion of cocaine located_in this portion of blood obo:BFO_0000082 this stem cell located_in this portion of bone marrow obo:BFO_0000082 your arm located_in your body obo:bfo/axiom/045-001 obo:BFO_0000082 b located_in c at t = Def. b and c are independent continuants, and the region at which b is located at t is a (proper or improper) continuant_part_of the region at which c is located at t. (axiom label in BFO2 Reference: [045-001]) obo:BFO_0000082 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance-level, relation. The BFO reading of the binary relation 'located in at all times@en' is: forall(t) exists_at(x,t) -> exists_at(y,t) and 'located in@en(x,y,t)'. obo:BFO_0000082 BFO2 Reference: independent continuant obo:bfo/axiom/046-001 obo:BFO_0000082 Located_in is transitive. (axiom label in BFO2 Reference: [046-001]) obo:bfo/axiom/048-001 obo:BFO_0000082 for all independent continuants b, c, and d: if b continuant_part_of c at t & c located_in d at t, then b located_in d at t. (axiom label in BFO2 Reference: [048-001]) obo:bfo/axiom/049-001 obo:BFO_0000082 for all independent continuants b, c, and d: if b located_in c at t & c continuant_part_of d at t, then b located_in d at t. (axiom label in BFO2 Reference: [049-001]) obo:bfo/axiom/048-001 obo:BFO_0000082 (forall (x y z t) (if (and (IndependentContinuant x) (IndependentContinuant y) (IndependentContinuant z) (continuantPartOfAt x y t) (locatedInAt y z t)) (locatedInAt x z t))) // axiom label in BFO2 CLIF: [048-001] obo:bfo/axiom/049-001 obo:BFO_0000082 (forall (x y z t) (if (and (IndependentContinuant x) (IndependentContinuant y) (IndependentContinuant z) (locatedInAt x y t) (continuantPartOfAt y z t)) (locatedInAt x z t))) // axiom label in BFO2 CLIF: [049-001] obo:bfo/axiom/046-001 obo:BFO_0000082 (forall (x y z t) (if (and (locatedInAt x y t) (locatedInAt y z t)) (locatedInAt x z t))) // axiom label in BFO2 CLIF: [046-001] obo:bfo/axiom/045-001 obo:BFO_0000082 (iff (locatedInAt a b t) (and (IndependentContinuant a) (IndependentContinuant b) (exists (r_1 r_2) (and (occupiesSpatialRegionAt a r_1 t) (occupiesSpatialRegionAt b r_2 t) (continuantPartOfAt r_1 r_2 t))))) // axiom label in BFO2 CLIF: [045-001] obo:BFO_0000082 obo:bfo.owl obo:BFO_0000082 located in at all times obo:BFO_0000083 located-at-r_st obo:BFO_0000083 occupiesSpatialRegionAt obo:BFO_0000083 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance level, relation. The BFO reading of the binary relation 'occupies spatial region at some time@en' is: exists t, exists_at(x,t) & exists_at(y,t) & 'occupies spatial region@en'(x,y,t) obo:BFO_0000083 BFO2 Reference: independent continuant obo:BFO_0000083 BFO2 Reference: spatial region obo:BFO_0000083 obo:ogg.owl obo:bfo/axiom/041-002 obo:BFO_0000083 b occupies_spatial_region r at t means that r is a spatial region in which independent continuant b is exactly located (axiom label in BFO2 Reference: [041-002]) obo:bfo/axiom/042-002 obo:BFO_0000083 every region r is occupies_spatial_region r at all times. (axiom label in BFO2 Reference: [042-002]) obo:bfo/axiom/043-001 obo:BFO_0000083 if b occupies_spatial_region r at t & b continuant_part_of b at t, then there is some r which is continuant_part_of r at t such that b occupies_spatial_region r at t. (axiom label in BFO2 Reference: [043-001]) obo:bfo/axiom/042-002 obo:BFO_0000083 (forall (r t) (if (Region r) (occupiesSpatialRegionAt r r t))) // axiom label in BFO2 CLIF: [042-002] obo:bfo/axiom/041-002 obo:BFO_0000083 (forall (x r t) (if (occupiesSpatialRegionAt x r t) (and (SpatialRegion r) (IndependentContinuant x)))) // axiom label in BFO2 CLIF: [041-002] obo:bfo/axiom/043-001 obo:BFO_0000083 (forall (x y r_1 t) (if (and (occupiesSpatialRegionAt x r_1 t) (continuantPartOfAt y x t)) (exists (r_2) (and (continuantPartOfAt r_2 r_1 t) (occupiesSpatialRegionAt y r_2 t))))) // axiom label in BFO2 CLIF: [043-001] obo:BFO_0000083 obo:bfo.owl obo:BFO_0000083 occupies spatial region at some time obo:BFO_0000084 g-depends-on_st obo:BFO_0000084 genericallyDependsOn obo:BFO_0000084 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance level, relation. The BFO reading of the binary relation 'generically depends on at some time@en' is: exists t, exists_at(x,t) & exists_at(y,t) & 'generically depends on@en'(x,y,t) obo:BFO_0000084 BFO2 Reference: generically dependent continuant obo:BFO_0000084 BFO2 Reference: independent continuant obo:bfo/axiom/072-002 obo:BFO_0000084 b g-depends on c at t1 means: b exists at t1 and c exists at t1 & for some type B it holds that (c instantiates B at t1) & necessarily, for all t (if b exists at t then some instance_of B exists at t) & not (b s-depends_on c at t1). (axiom label in BFO2 Reference: [072-002]) obo:bfo/axiom/073-001 obo:BFO_0000084 if b g-depends_on c at some time t, then b g-depends_on something at all times at which b exists. (axiom label in BFO2 Reference: [073-001]) obo:bfo/axiom/073-001 obo:BFO_0000084 (forall (x y) (if (exists (t) (genericallyDependsOnAt x y t)) (forall (t_1) (if (existsAt x t_1) (exists (z) (genericallyDependsOnAt x z t_1)))))) // axiom label in BFO2 CLIF: [073-001] obo:BFO_0000084 obo:bfo.owl obo:BFO_0000084 generically depends on at some time obo:BFO_0000085 has-f_st obo:BFO_0000085 hasFunctionAt obo:bfo/axiom/070-001 obo:BFO_0000085 a has_function b at t =Def. b function_of a at t. (axiom label in BFO2 Reference: [070-001]) obo:BFO_0000085 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance level, relation. The BFO reading of the binary relation 'has function at some time@en' is: exists t, exists_at(x,t) & exists_at(y,t) & 'has function@en'(x,y,t) obo:bfo/axiom/070-001 obo:BFO_0000085 (iff (hasFunctionAt a b t) (functionOf b a t)) // axiom label in BFO2 CLIF: [070-001] obo:BFO_0000085 obo:bfo.owl obo:BFO_0000085 has function at some time obo:BFO_0000086 has-q_st obo:BFO_0000086 obo:bfo.owl obo:BFO_0000086 has quality at some time obo:BFO_0000087 has-r_st obo:BFO_0000087 hasRoleAt obo:bfo/axiom/068-001 obo:BFO_0000087 a has_role b at t =Def. b role_of a at t. (axiom label in BFO2 Reference: [068-001]) obo:BFO_0000087 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance level, relation. The BFO reading of the binary relation 'has role at some time@en' is: exists t, exists_at(x,t) & exists_at(y,t) & 'has role@en'(x,y,t) obo:bfo/axiom/068-001 obo:BFO_0000087 (iff (hasRoleAt a b t) (roleOfAt b a t)) // axiom label in BFO2 CLIF: [068-001] obo:BFO_0000087 obo:bfo.owl obo:BFO_0000087 has role at some time obo:BFO_0000101 has-g-dep_st obo:BFO_0000101 [copied from inverse property 'generically depends on at some time'] Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance level, relation. The BFO reading of the binary relation 'generically depends on at some time@en' is: exists t, exists_at(x,t) & exists_at(y,t) & 'generically depends on@en'(x,y,t) obo:BFO_0000101 [copied from inverse property 'generically depends on at some time'] BFO2 Reference: generically dependent continuant obo:BFO_0000101 [copied from inverse property 'generically depends on at some time'] BFO2 Reference: independent continuant obo:BFO_0000101 [copied from inverse property 'generically depends on at some time'] b g-depends on c at t1 means: b exists at t1 and c exists at t1 & for some type B it holds that (c instantiates B at t1) & necessarily, for all t (if b exists at t then some instance_of B exists at t) & not (b s-depends_on c at t1). (axiom label in BFO2 Reference: [072-002]) obo:BFO_0000101 obo:bfo.owl obo:BFO_0000101 has generic dependent at some time obo:BFO_0000107 d-of_at obo:BFO_0000107 dispositionOfAt obo:bfo/axiom/066-001 obo:BFO_0000107 a disposition_of b at t =Def. a is a disposition and a inheres_in b at t. (axiom label in BFO2 Reference: [066-001]) obo:BFO_0000107 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance-level, relation. The BFO reading of the binary relation 'disposition of at all times@en' is: forall(t) exists_at(x,t) -> exists_at(y,t) and 'disposition of@en(x,y,t)'. obo:bfo/axiom/066-001 obo:BFO_0000107 (iff (dispositionOf a b t) (and (Disposition a) (inheresInAt a b t))) // axiom label in BFO2 CLIF: [066-001] obo:BFO_0000107 obo:bfo.owl obo:BFO_0000107 disposition of at all times obo:BFO_0000108 exists-at obo:BFO_0000108 existsAt obo:BFO_0000108 BFO2 Reference: entity obo:BFO_0000108 BFO2 Reference: temporal region obo:BFO_0000108 obo:ogg.owl obo:bfo/axiom/118-002 obo:BFO_0000108 b exists_at t means: b is an entity which exists at some temporal region t. (axiom label in BFO2 Reference: [118-002]) obo:BFO_0000108 obo:bfo.owl obo:BFO_0000108 exists at obo:BFO_0000110 c-has-part_at obo:BFO_0000110 hasContinuantPartAt obo:BFO_0000110 [copied from inverse property 'part of continuant at all times that whole exists'] forall(t) exists_at(y,t) -> exists_at(x,t) and 'part of continuant'(x,y,t) obo:bfo/axiom/006-001 obo:BFO_0000110 b has_continuant_part c at t = Def. c continuant_part_of b at t. (axiom label in BFO2 Reference: [006-001]) obo:BFO_0000110 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance-level, relation. The BFO reading of the binary relation 'has continuant part at all times@en' is: forall(t) exists_at(x,t) -> exists_at(y,t) and 'has continuant part@en(x,y,t)'. obo:BFO_0000110 [copied from inverse property 'part of continuant at all times that whole exists'] This is a binary version of a ternary time-indexed, instance level, relation. Unlike the rest of the temporalized relations which temporally quantify over existence of the subject of the relation, this relation temporally quantifies over the existence of the object of the relation. The relation is provided tentatively, to assess whether the GO needs such a relation. It is inverse of 'has continuant part at all times' obo:bfo/axiom/0000602 obo:bfo/axiom/006-001 obo:BFO_0000110 (iff (hasContinuantPartAt a b t) (continuantPartOfAt b a t)) // axiom label in BFO2 CLIF: [006-001] obo:BFO_0000110 obo:bfo.owl obo:BFO_0000110 has continuant part at all times obo:BFO_0000111 c-has-ppart_at obo:BFO_0000111 hasProperContinuantPartAt obo:BFO_0000111 b has_proper_continuant_part c at t = Def. c proper_continuant_part_of b at t. [XXX-001 obo:BFO_0000111 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance-level, relation. The BFO reading of the binary relation 'has proper continuant part at all times@en' is: forall(t) exists_at(x,t) -> exists_at(y,t) and 'has proper continuant part@en(x,y,t)'. obo:BFO_0000111 obo:bfo.owl obo:BFO_0000111 has proper continuant part at all times obo:BFO_0000112 has-d_st obo:BFO_0000112 hasDispositionAt obo:bfo/axiom/069-001 obo:BFO_0000112 a has_disposition b at t =Def. b disposition_of a at t. (axiom label in BFO2 Reference: [069-001]) obo:BFO_0000112 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance level, relation. The BFO reading of the binary relation 'has disposition at some time@en' is: exists t, exists_at(x,t) & exists_at(y,t) & 'has disposition@en'(x,y,t) obo:bfo/axiom/069-001 obo:BFO_0000112 (iff (hasDispositionAt a b t) (dispositionOf b a t)) // axiom label in BFO2 CLIF: [069-001] obo:BFO_0000112 obo:bfo.owl obo:BFO_0000112 has disposition at some time obo:BFO_0000113 has-material-basis_at obo:BFO_0000113 hasMaterialBasisAt obo:BFO_0000113 the material basis of John’s disposition to cough is the viral infection in John’s upper respiratory tract obo:BFO_0000113 the material basis of the disposition to wear unevenly of John’s tires is the worn suspension of his car. obo:BFO_0000113 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance-level, relation. The BFO reading of the binary relation 'has material basis at all times@en' is: forall(t) exists_at(x,t) -> exists_at(y,t) and 'has material basis@en(x,y,t)'. obo:bfo/axiom/071-002 obo:BFO_0000113 b has_material_basis c at t means: b is a disposition & c is a material entity & there is some d bearer_of b at t& c continuant_part_of d at t& d has_disposition b at t because c continuant_part_of d at t. (axiom label in BFO2 Reference: [071-002]) obo:bfo/axiom/071-002 obo:BFO_0000113 (forall (x y t) (if (hasMaterialBasisAt x y t) (and (Disposition x) (MaterialEntity y) (exists (z) (and (bearerOfAt z x t) (continuantPartOfAt y z t) (exists (w) (and (Disposition w) (if (hasDisposition z w) (continuantPartOfAt y z t))))))))) // axiom label in BFO2 CLIF: [071-002] obo:BFO_0000113 obo:bfo.owl obo:BFO_0000113 has material basis at all times obo:BFO_0000115 has-member-part_st obo:BFO_0000115 [copied from inverse property 'member part of at some time'] each piece in a chess set is a member part of the chess set; each Beatle in the collection called The Beatles is a member part of The Beatles. obo:BFO_0000115 [copied from inverse property 'member part of at some time'] each tree in a forest is a member_part of the forest obo:BFO_0000115 [copied from inverse property 'member part of at some time'] b member_part_of c at t =Def. b is an object & there is at t a mutually exhaustive and pairwise disjoint partition of c into objects x1, …, xn (for some n &gt; 1) with b = xi for some 1 ? i ? n. (axiom label in BFO2 Reference: [026-004]) obo:BFO_0000115 [copied from inverse property 'member part of at some time'] Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance level, relation. The BFO reading of the binary relation 'member part of at some time@en' is: exists t, exists_at(x,t) & exists_at(y,t) & 'member part of@en'(x,y,t) obo:BFO_0000115 [copied from inverse property 'member part of at some time'] BFO2 Reference: object obo:BFO_0000115 [copied from inverse property 'member part of at some time'] BFO2 Reference: object aggregate obo:BFO_0000115 obo:bfo.owl obo:BFO_0000115 has member part at some time obo:BFO_0000117 o-has-part obo:BFO_0000117 hasOccurrentPart obo:BFO_0000117 [copied from inverse property 'part of occurrent'] Mary’s 5th birthday occurrent_part_of Mary’s life obo:BFO_0000117 [copied from inverse property 'part of occurrent'] The process of a footballer’s heart beating once is an occurrent part but not a temporal_part of a game of football. obo:BFO_0000117 [copied from inverse property 'part of occurrent'] the first set of the tennis match occurrent_part_of the tennis match. obo:bfo/axiom/007-001 obo:BFO_0000117 b has_occurrent_part c = Def. c occurrent_part_of b. (axiom label in BFO2 Reference: [007-001]) obo:BFO_0000117 [copied from inverse property 'part of occurrent'] BFO 2 Reference: a (continuant or occurrent) part of itself. We appreciate that this is counterintuitive for some users, since it implies for example that President Obama is a part of himself. However it brings benefits in simplifying the logical formalism, and it captures an important feature of identity, namely that it is the limit case of mereological inclusion. obo:BFO_0000117 [copied from inverse property 'part of occurrent'] BFO2 Reference: occurrent obo:BFO_0000117 obo:ogg.owl obo:BFO_0000117 [copied from inverse property 'part of occurrent'] b occurrent_part_of c =Def. b is a part of c & b and c are occurrents. (axiom label in BFO2 Reference: [003-002]) obo:bfo/axiom/007-001 obo:BFO_0000117 (iff (hasOccurrentPart a b) (occurrentPartOf b a)) // axiom label in BFO2 CLIF: [007-001] obo:BFO_0000117 obo:bfo.owl obo:BFO_0000117 has occurrent part obo:BFO_0000118 o-has-ppart obo:BFO_0000118 hasProperOccurrentPart obo:BFO_0000118 [copied from inverse property 'proper part of occurrent'] b proper_occurrent_part_of c =Def. b occurrent_part_of c & b and c are not identical. (axiom label in BFO2 Reference: [005-001]) obo:BFO_0000118 b has_proper_occurrent_part c = Def. c proper_occurrent_part_of b. [XXX-001 obo:BFO_0000118 obo:ogg.owl obo:BFO_0000118 obo:bfo.owl obo:BFO_0000118 has proper occurrent part obo:BFO_0000119 has-profile obo:BFO_0000119 obo:bfo.owl obo:BFO_0000119 has profile obo:BFO_0000121 has-t-part obo:BFO_0000121 [copied from inverse property 'temporal part of'] the 4th year of your life is a temporal part of your life\. The first quarter of a game of football is a temporal part of the whole game\. The process of your heart beating from 4pm to 5pm today is a temporal part of the entire process of your heart beating.\ The 4th year of your life is a temporal part of your life obo:BFO_0000121 [copied from inverse property 'temporal part of'] the process boundary which separates the 3rd and 4th years of your life. obo:BFO_0000121 [copied from inverse property 'temporal part of'] your heart beating from 4pm to 5pm today is a temporal part of the process of your heart beating obo:BFO_0000121 [copied from inverse property 'temporal part of'] b proper_temporal_part_of c =Def. b temporal_part_of c & not (b = c). (axiom label in BFO2 Reference: [116-001]) obo:BFO_0000121 [copied from inverse property 'temporal part of'] b temporal_part_of c =Def.b occurrent_part_of c & & for some temporal region t, b occupies_temporal_region t & for all occurrents d, t (if d occupies_temporal_region t & t? occurrent_part_of t then (d occurrent_part_of a iff d occurrent_part_of b)). (axiom label in BFO2 Reference: [078-003]) obo:BFO_0000121 obo:bfo.owl obo:BFO_0000121 has temporal part obo:BFO_0000123 r-location-of_st obo:BFO_0000123 [copied from inverse property 'occupies spatial region at some time'] Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance level, relation. The BFO reading of the binary relation 'occupies spatial region at some time@en' is: exists t, exists_at(x,t) & exists_at(y,t) & 'occupies spatial region@en'(x,y,t) obo:BFO_0000123 [copied from inverse property 'occupies spatial region at some time'] BFO2 Reference: independent continuant obo:BFO_0000123 [copied from inverse property 'occupies spatial region at some time'] BFO2 Reference: spatial region obo:BFO_0000123 obo:ogg.owl obo:BFO_0000123 [copied from inverse property 'occupies spatial region at some time'] b occupies_spatial_region r at t means that r is a spatial region in which independent continuant b is exactly located (axiom label in BFO2 Reference: [041-002]) obo:BFO_0000123 obo:bfo.owl obo:BFO_0000123 has spatial occupant at some time obo:BFO_0000124 has-location_st obo:BFO_0000124 [copied from inverse property 'located in at some time'] Mary located_in Salzburg obo:BFO_0000124 [copied from inverse property 'located in at some time'] the Empire State Building located_in New York. obo:BFO_0000124 [copied from inverse property 'located in at some time'] this portion of cocaine located_in this portion of blood obo:BFO_0000124 [copied from inverse property 'located in at some time'] this stem cell located_in this portion of bone marrow obo:BFO_0000124 [copied from inverse property 'located in at some time'] your arm located_in your body obo:BFO_0000124 [copied from inverse property 'located in at some time'] b located_in c at t = Def. b and c are independent continuants, and the region at which b is located at t is a (proper or improper) continuant_part_of the region at which c is located at t. (axiom label in BFO2 Reference: [045-001]) obo:BFO_0000124 [copied from inverse property 'located in at some time'] Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance level, relation. The BFO reading of the binary relation 'located in at some time@en' is: exists t, exists_at(x,t) & exists_at(y,t) & 'located in@en'(x,y,t) obo:BFO_0000124 [copied from inverse property 'located in at some time'] BFO2 Reference: independent continuant obo:BFO_0000124 obo:bfo.owl obo:BFO_0000124 has location at some time obo:BFO_0000125 has-s-dep_st obo:BFO_0000125 [copied from inverse property 'specifically depends on at some time'] A pain s-depends_on the organism that is experiencing the pain obo:BFO_0000125 [copied from inverse property 'specifically depends on at some time'] a gait s-depends_on the walking object. (All at some specific time.) obo:BFO_0000125 [copied from inverse property 'specifically depends on at some time'] a shape s-depends_on the shaped object obo:BFO_0000125 [copied from inverse property 'specifically depends on at some time'] one-sided s-dependence of a dependent continuant on an independent continuant: an instance of headache s-depends_on some head obo:BFO_0000125 [copied from inverse property 'specifically depends on at some time'] one-sided s-dependence of a dependent continuant on an independent continuant: an instance of temperature s-depends_on some organism obo:BFO_0000125 [copied from inverse property 'specifically depends on at some time'] one-sided s-dependence of a process on something: a process of cell death s-depends_on a cell obo:BFO_0000125 [copied from inverse property 'specifically depends on at some time'] one-sided s-dependence of a process on something: an instance of seeing (a relational process) s-depends_on some organism and on some seen entity, which may be an occurrent or a continuant obo:BFO_0000125 [copied from inverse property 'specifically depends on at some time'] one-sided s-dependence of one occurrent on another: a process of answering a question is dependent on a prior process of asking a question obo:BFO_0000125 [copied from inverse property 'specifically depends on at some time'] one-sided s-dependence of one occurrent on another: a process of obeying a command is dependent on a prior process of issuing a command obo:BFO_0000125 [copied from inverse property 'specifically depends on at some time'] one-sided s-dependence of one occurrent on multiple independent continuants: a relational process of hitting a ball with a cricket bat obo:BFO_0000125 [copied from inverse property 'specifically depends on at some time'] one-sided s-dependence of one occurrent on multiple independent continuants: a relational process of paying cash to a merchant in exchange for a bag of figs obo:BFO_0000125 [copied from inverse property 'specifically depends on at some time'] reciprocal s-dependence between occurrents: a process of buying and the associated process of selling obo:BFO_0000125 [copied from inverse property 'specifically depends on at some time'] reciprocal s-dependence between occurrents: a process of increasing the volume of a portion of gas while temperature remains constant and the associated process of decreasing the pressure exerted by the gas obo:BFO_0000125 [copied from inverse property 'specifically depends on at some time'] reciprocal s-dependence between occurrents: in a game of chess the process of playing with the white pieces is mutually dependent on the process of playing with the black pieces obo:BFO_0000125 [copied from inverse property 'specifically depends on at some time'] the one-sided dependence of an occurrent on an independent continuant: football match on the players, the ground, the ball obo:BFO_0000125 [copied from inverse property 'specifically depends on at some time'] the one-sided dependence of an occurrent on an independent continuant: handwave on a hand obo:BFO_0000125 [copied from inverse property 'specifically depends on at some time'] the three-sided reciprocal s-dependence of the hue, saturation and brightness of a color [45 obo:BFO_0000125 [copied from inverse property 'specifically depends on at some time'] the three-sided reciprocal s-dependence of the pitch, timbre and volume of a tone [45 obo:BFO_0000125 [copied from inverse property 'specifically depends on at some time'] the two-sided reciprocal s-dependence of the roles of husband and wife [20 obo:BFO_0000125 [copied from inverse property 'specifically depends on at some time'] Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance level, relation. The BFO reading of the binary relation 'specifically depends on at some time@en' is: exists t, exists_at(x,t) & exists_at(y,t) & 'specifically depends on@en'(x,y,t) obo:BFO_0000125 [copied from inverse property 'specifically depends on at some time'] BFO 2 Reference: An entity – for example an act of communication or a game of football – can s-depends_on more than one entity. Complex phenomena for example in the psychological and social realms (such as inferring, commanding and requesting) or in the realm of multi-organismal biological processes (such as infection and resistance), will involve multiple families of dependence relations, involving both continuants and occurrents [1, 4, 28 obo:BFO_0000125 [copied from inverse property 'specifically depends on at some time'] BFO 2 Reference: S-dependence is just one type of dependence among many; it is what, in the literature, is referred to as ‘existential dependence’ [87, 46, 65, 20 obo:BFO_0000125 [copied from inverse property 'specifically depends on at some time'] BFO 2 Reference: the relation of s-depends_on does not in every case require simultaneous existence of its relata. Note the difference between such cases and the cases of continuant universals defined historically: the act of answering depends existentially on the prior act of questioning; the human being who was baptized or who answered a question does not himself depend existentially on the prior act of baptism or answering. He would still exist even if these acts had never taken place. obo:BFO_0000125 [copied from inverse property 'specifically depends on at some time'] BFO2 Reference: specifically dependent continuant\; process; process boundary obo:BFO_0000125 obo:ogg.owl obo:BFO_0000125 [copied from inverse property 'specifically depends on at some time'] To say that b s-depends_on a at t is to say that b and c do not share common parts & b is of its nature such that it cannot exist unless c exists & b is not a boundary of c and b is not a site of which c is the host [64 obo:BFO_0000125 obo:bfo.owl obo:BFO_0000125 has specific dependent at some time obo:BFO_0000126 occupied-by obo:BFO_0000126 [copied from inverse property 'occupies spatiotemporal region'] BFO 2 Reference: The occupies_spatiotemporal_region and occupies_temporal_region relations are the counterpart, on the occurrent side, of the relation occupies_spatial_region. obo:BFO_0000126 obo:ogg.owl obo:BFO_0000126 [copied from inverse property 'occupies spatiotemporal region'] p occupies_spatiotemporal_region s. This is a primitive relation between an occurrent p and the spatiotemporal region s which is its spatiotemporal extent. (axiom label in BFO2 Reference: [082-003]) obo:BFO_0000126 obo:bfo.owl obo:BFO_0000126 has spatiotemporal occupant obo:BFO_0000127 material-basis-of_st obo:BFO_0000127 obo:bfo.owl obo:BFO_0000127 material basis of at some time obo:BFO_0000129 member-part-of_st obo:BFO_0000129 memberPartOfAt obo:BFO_0000129 each piece in a chess set is a member part of the chess set; each Beatle in the collection called The Beatles is a member part of The Beatles. obo:BFO_0000129 each tree in a forest is a member_part of the forest obo:bfo/axiom/026-004 obo:BFO_0000129 b member_part_of c at t =Def. b is an object & there is at t a mutually exhaustive and pairwise disjoint partition of c into objects x1, …, xn (for some n &gt; 1) with b = xi for some 1 ? i ? n. (axiom label in BFO2 Reference: [026-004]) obo:BFO_0000129 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance level, relation. The BFO reading of the binary relation 'member part of at some time@en' is: exists t, exists_at(x,t) & exists_at(y,t) & 'member part of@en'(x,y,t) obo:BFO_0000129 BFO2 Reference: object obo:BFO_0000129 BFO2 Reference: object aggregate obo:bfo/axiom/104-001 obo:BFO_0000129 if b member_part_of c at t then b continuant_part_of c at t. (axiom label in BFO2 Reference: [104-001]) obo:bfo/axiom/104-001 obo:BFO_0000129 (forall (x y t) (if (memberPartOfAt x y t) (continuantPartOfAt x y t))) // axiom label in BFO2 CLIF: [104-001] obo:BFO_0000129 obo:bfo.owl obo:BFO_0000129 member part of at some time obo:BFO_0000130 occupies obo:BFO_0000130 occupiesSpatiotemporalRegion obo:BFO_0000130 BFO 2 Reference: The occupies_spatiotemporal_region and occupies_temporal_region relations are the counterpart, on the occurrent side, of the relation occupies_spatial_region. obo:BFO_0000130 obo:ogg.owl obo:bfo/axiom/082-003 obo:BFO_0000130 p occupies_spatiotemporal_region s. This is a primitive relation between an occurrent p and the spatiotemporal region s which is its spatiotemporal extent. (axiom label in BFO2 Reference: [082-003]) obo:BFO_0000130 obo:bfo.owl obo:BFO_0000130 occupies spatiotemporal region obo:BFO_0000132 o-part-of obo:BFO_0000132 occurrentPartOf obo:BFO_0000132 Mary’s 5th birthday occurrent_part_of Mary’s life obo:BFO_0000132 The process of a footballer’s heart beating once is an occurrent part but not a temporal_part of a game of football. obo:BFO_0000132 the first set of the tennis match occurrent_part_of the tennis match. obo:BFO_0000132 [copied from inverse property 'has occurrent part'] b has_occurrent_part c = Def. c occurrent_part_of b. (axiom label in BFO2 Reference: [007-001]) obo:BFO_0000132 BFO 2 Reference: a (continuant or occurrent) part of itself. We appreciate that this is counterintuitive for some users, since it implies for example that President Obama is a part of himself. However it brings benefits in simplifying the logical formalism, and it captures an important feature of identity, namely that it is the limit case of mereological inclusion. obo:BFO_0000132 BFO2 Reference: occurrent obo:BFO_0000132 obo:ogg.owl obo:bfo/axiom/003-002 obo:BFO_0000132 b occurrent_part_of c =Def. b is a part of c & b and c are occurrents. (axiom label in BFO2 Reference: [003-002]) obo:bfo/axiom/123-001 obo:BFO_0000132 occurrent_part_of is antisymmetric. (axiom label in BFO2 Reference: [123-001]) obo:bfo/axiom/113-002 obo:BFO_0000132 occurrent_part_of is reflexive (every occurrent entity is an occurrent_part_of itself). (axiom label in BFO2 Reference: [113-002]) obo:bfo/axiom/112-001 obo:BFO_0000132 occurrent_part_of is transitive. (axiom label in BFO2 Reference: [112-001]) obo:bfo/axiom/125-001 obo:BFO_0000132 occurrent_part_of satisfies unique product. (axiom label in BFO2 Reference: [125-001]) obo:bfo/axiom/124-001 obo:BFO_0000132 occurrent_part_of satisfies weak supplementation. (axiom label in BFO2 Reference: [124-001]) obo:bfo/axiom/124-001 obo:BFO_0000132 (forall (x y t) (if (and (occurrentPartOf x y t) (not (= x y))) (exists (z) (and (occurrentPartOf z y t) (not (exists (w) (and (occurrentPartOf w x t) (occurrentPartOf w z t)))))))) // axiom label in BFO2 CLIF: [124-001] obo:bfo/axiom/123-001 obo:BFO_0000132 (forall (x y t) (if (and (occurrentPartOf x y t) (occurrentPartOf y x t)) (= x y))) // axiom label in BFO2 CLIF: [123-001] obo:bfo/axiom/125-001 obo:BFO_0000132 (forall (x y t) (if (exists (v) (and (occurrentPartOf v x t) (occurrentPartOf v y t))) (exists (z) (forall (u w) (iff (iff (occurrentPartOf w u t) (and (occurrentPartOf w x t) (occurrentPartOf w y t))) (= z u)))))) // axiom label in BFO2 CLIF: [125-001] obo:bfo/axiom/112-001 obo:BFO_0000132 (forall (x y z) (if (and (occurrentPartOf x y) (occurrentPartOf y z)) (occurrentPartOf x z))) // axiom label in BFO2 CLIF: [112-001] obo:bfo/axiom/113-002 obo:BFO_0000132 (forall (x) (if (Occurrent x) (occurrentPartOf x x))) // axiom label in BFO2 CLIF: [113-002] obo:BFO_0000132 obo:bfo.owl obo:BFO_0000132 part of occurrent obo:BFO_0000133 profile-of obo:BFO_0000133 processProfileOf obo:BFO_0000133 obo:bfo.owl obo:BFO_0000133 process profile of obo:bfo/axiom/080-003 obo:BFO_0000134 To say that each spatiotemporal region s temporally_projects_onto some temporal region t is to say that t is the temporal extension of s. (axiom label in BFO2 Reference: [080-003]) obo:bfo/axiom/081-003 obo:BFO_0000134 To say that spatiotemporal region s spatially_projects_onto spatial region r at t is to say that r is the spatial extent of s at t. (axiom label in BFO2 Reference: [081-003]) obo:BFO_0000136 t-ppart-of obo:BFO_0000136 properTemporalPartOf obo:BFO_0000136 obo:bfo.owl obo:BFO_0000136 proper temporal part of obo:BFO_0000137 c-ppart-of_at obo:BFO_0000137 properContinuantPartOfAt obo:bfo/axiom/004-001 obo:BFO_0000137 b proper_continuant_part_of c at t =Def. b continuant_part_of c at t & b and c are not identical. (axiom label in BFO2 Reference: [004-001]) obo:BFO_0000137 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance-level, relation. The BFO reading of the binary relation 'proper part of continuant at all times@en' is: forall(t) exists_at(x,t) -> exists_at(y,t) and 'proper part of continuant@en(x,y,t)'. obo:bfo/axiom/004-001 obo:BFO_0000137 (iff (properContinuantPartOfAt a b t) (and (continuantPartOfAt a b t) (not (= a b)))) // axiom label in BFO2 CLIF: [004-001] obo:BFO_0000137 obo:bfo.owl obo:BFO_0000137 proper part of continuant at all times obo:BFO_0000138 o-ppart-of obo:BFO_0000138 properOccurrentPartOf obo:BFO_0000138 [copied from inverse property 'has proper occurrent part'] b has_proper_occurrent_part c = Def. c proper_occurrent_part_of b. [XXX-001 obo:bfo/axiom/005-001 obo:BFO_0000138 b proper_occurrent_part_of c =Def. b occurrent_part_of c & b and c are not identical. (axiom label in BFO2 Reference: [005-001]) obo:BFO_0000138 obo:ogg.owl obo:bfo/axiom/005-001 obo:BFO_0000138 (iff (properOccurrentPartOf a b) (and (occurrentPartOf a b) (not (= a b)))) // axiom label in BFO2 CLIF: [005-001] obo:BFO_0000138 obo:bfo.owl obo:BFO_0000138 proper part of occurrent obo:BFO_0000139 t-part-of obo:BFO_0000139 temporalPartOf obo:BFO_0000139 the 4th year of your life is a temporal part of your life\. The first quarter of a game of football is a temporal part of the whole game\. The process of your heart beating from 4pm to 5pm today is a temporal part of the entire process of your heart beating.\ The 4th year of your life is a temporal part of your life obo:BFO_0000139 the process boundary which separates the 3rd and 4th years of your life. obo:BFO_0000139 your heart beating from 4pm to 5pm today is a temporal part of the process of your heart beating obo:bfo/axiom/116-001 obo:BFO_0000139 b proper_temporal_part_of c =Def. b temporal_part_of c & not (b = c). (axiom label in BFO2 Reference: [116-001]) obo:bfo/axiom/078-003 obo:BFO_0000139 b temporal_part_of c =Def.b occurrent_part_of c & & for some temporal region t, b occupies_temporal_region t & for all occurrents d, t (if d occupies_temporal_region t & t? occurrent_part_of t then (d occurrent_part_of a iff d occurrent_part_of b)). (axiom label in BFO2 Reference: [078-003]) obo:BFO_0000139 obo:ogg.owl obo:bfo/axiom/117-002 obo:BFO_0000139 if b proper_temporal_part_of c, then there is some d which is a proper_temporal_part_of c and which shares no parts with b. (axiom label in BFO2 Reference: [117-002]) obo:bfo/axiom/117-002 obo:BFO_0000139 (forall (x y) (if (properTemporalPartOf x y) (exists (z) (and (properTemporalPartOf z y) (not (exists (w) (and (temporalPartOf w x) (temporalPartOf w z)))))))) // axiom label in BFO2 CLIF: [117-002] obo:bfo/axiom/116-001 obo:BFO_0000139 (iff (properTemporalPartOf a b) (and (temporalPartOf a b) (not (= a b)))) // axiom label in BFO2 CLIF: [116-001] obo:bfo/axiom/078-003 obo:BFO_0000139 (iff (temporalPartOf a b) (and (occurrentPartOf a b) (exists (t) (and (TemporalRegion t) (occupiesSpatioTemporalRegion a t))) (forall (c t_1) (if (and (Occurrent c) (occupiesSpatioTemporalRegion c t_1) (occurrentPartOf t_1 r)) (iff (occurrentPartOf c a) (occurrentPartOf c b)))))) // axiom label in BFO2 CLIF: [078-003] obo:BFO_0000139 obo:bfo.owl obo:BFO_0000139 temporal part of obo:BFO_0000140 cf-boundary obo:BFO_0000140 ContinuantFiatBoundary obo:bfo/axiom/029-001 obo:BFO_0000140 b is a continuant fiat boundary = Def. b is an immaterial entity that is of zero, one or two dimensions and does not include a spatial region as part. (axiom label in BFO2 Reference: [029-001]) obo:BFO_0000140 BFO 2 Reference: In BFO 1.1 the assumption was made that the external surface of a material entity such as a cell could be treated as if it were a boundary in the mathematical sense. The new document propounds the view that when we talk about external surfaces of material objects in this way then we are talking about something fiat. To be dealt with in a future version: fiat boundaries at different levels of granularity.More generally, the focus in discussion of boundaries in BFO 2.0 is now on fiat boundaries, which means: boundaries for which there is no assumption that they coincide with physical discontinuities. The ontology of boundaries becomes more closely allied with the ontology of regions. obo:BFO_0000140 BFO 2 Reference: a continuant fiat boundary is a boundary of some material entity (for example: the plane separating the Northern and Southern hemispheres; the North Pole), or it is a boundary of some immaterial entity (for example of some portion of airspace). Three basic kinds of continuant fiat boundary can be distinguished (together with various combination kinds [29 obo:bfo/axiom/0000008 obo:BFO_0000140 Continuant fiat boundary doesn't have a closure axiom because the subclasses don't necessarily exhaust all possibilites. An example would be the mereological sum of two-dimensional continuant fiat boundary and a one dimensional continuant fiat boundary that doesn't overlap it. The situation is analogous to temporal and spatial regions. obo:BFO_0000140 Every continuant fiat boundary is located at some spatial region at every time at which it exists obo:bfo/axiom/029-001 obo:BFO_0000140 (iff (ContinuantFiatBoundary a) (and (ImmaterialEntity a) (exists (b) (and (or (ZeroDimensionalSpatialRegion b) (OneDimensionalSpatialRegion b) (TwoDimensionalSpatialRegion b)) (forall (t) (locatedInAt a b t)))) (not (exists (c t) (and (SpatialRegion c) (continuantPartOfAt c a t)))))) // axiom label in BFO2 CLIF: [029-001] obo:BFO_0000140 obo:bfo.owl obo:BFO_0000140 continuant fiat boundary obo:BFO_0000141 immaterial obo:BFO_0000141 ImmaterialEntity obo:BFO_0000141 BFO 2 Reference: Immaterial entities are divided into two subgroups:boundaries and sites, which bound, or are demarcated in relation, to material entities, and which can thus change location, shape and size and as their material hosts move or change shape or size (for example: your nasal passage; the hold of a ship; the boundary of Wales (which moves with the rotation of the Earth) [38, 7, 10 obo:BFO_0000141 obo:ogg.owl obo:BFO_0000141 obo:bfo.owl obo:BFO_0000141 immaterial entity obo:BFO_0000142 1d-cf-boundary obo:BFO_0000142 OneDimensionalContinuantFiatBoundary obo:BFO_0000142 The Equator obo:BFO_0000142 all geopolitical boundaries obo:BFO_0000142 all lines of latitude and longitude obo:BFO_0000142 the line separating the outer surface of the mucosa of the lower lip from the outer surface of the skin of the chin. obo:BFO_0000142 the median sulcus of your tongue obo:bfo/axiom/032-001 obo:BFO_0000142 a one-dimensional continuant fiat boundary is a continuous fiat line whose location is defined in relation to some material entity. (axiom label in BFO2 Reference: [032-001]) obo:bfo/axiom/032-001 obo:BFO_0000142 (iff (OneDimensionalContinuantFiatBoundary a) (and (ContinuantFiatBoundary a) (exists (b) (and (OneDimensionalSpatialRegion b) (forall (t) (locatedInAt a b t)))))) // axiom label in BFO2 CLIF: [032-001] obo:BFO_0000142 obo:bfo.owl obo:BFO_0000142 one-dimensional continuant fiat boundary obo:BFO_0000144 process-profile obo:BFO_0000144 ProcessProfile obo:BFO_0000144 On a somewhat higher level of complexity are what we shall call rate process profiles, which are the targets of selective abstraction focused not on determinate quality magnitudes plotted over time, but rather on certain ratios between these magnitudes and elapsed times. A speed process profile, for example, is represented by a graph plotting against time the ratio of distance covered per unit of time. Since rates may change, and since such changes, too, may have rates of change, we have to deal here with a hierarchy of process profile universals at successive levels obo:BFO_0000144 One important sub-family of rate process profiles is illustrated by the beat or frequency profiles of cyclical processes, illustrated by the 60 beats per minute beating process of John’s heart, or the 120 beats per minute drumming process involved in one of John’s performances in a rock band, and so on. Each such process includes what we shall call a beat process profile instance as part, a subtype of rate process profile in which the salient ratio is not distance covered but rather number of beat cycles per unit of time. Each beat process profile instance instantiates the determinable universal beat process profile. But it also instantiates multiple more specialized universals at lower levels of generality, selected from rate process profilebeat process profileregular beat process profile3 bpm beat process profile4 bpm beat process profileirregular beat process profileincreasing beat process profileand so on.In the case of a regular beat process profile, a rate can be assigned in the simplest possible fashion by dividing the number of cycles by the length of the temporal region occupied by the beating process profile as a whole. Irregular process profiles of this sort, for example as identified in the clinic, or in the readings on an aircraft instrument panel, are often of diagnostic significance. obo:BFO_0000144 The simplest type of process profiles are what we shall call ‘quality process profiles’, which are the process profiles which serve as the foci of the sort of selective abstraction that is involved when measurements are made of changes in single qualities, as illustrated, for example, by process profiles of mass, temperature, aortic pressure, and so on. obo:bfo/axiom/093-002 obo:BFO_0000144 b is a process_profile =Def. there is some process c such that b process_profile_of c (axiom label in BFO2 Reference: [093-002]) obo:bfo/axiom/094-005 obo:BFO_0000144 b process_profile_of c holds when b proper_occurrent_part_of c& there is some proper_occurrent_part d of c which has no parts in common with b & is mutually dependent on b& is such that b, c and d occupy the same temporal region (axiom label in BFO2 Reference: [094-005]) obo:bfo/axiom/094-005 obo:BFO_0000144 (forall (x y) (if (processProfileOf x y) (and (properContinuantPartOf x y) (exists (z t) (and (properOccurrentPartOf z y) (TemporalRegion t) (occupiesSpatioTemporalRegion x t) (occupiesSpatioTemporalRegion y t) (occupiesSpatioTemporalRegion z t) (not (exists (w) (and (occurrentPartOf w x) (occurrentPartOf w z))))))))) // axiom label in BFO2 CLIF: [094-005] obo:bfo/axiom/093-002 obo:BFO_0000144 (iff (ProcessProfile a) (exists (b) (and (Process b) (processProfileOf a b)))) // axiom label in BFO2 CLIF: [093-002] obo:BFO_0000144 obo:bfo.owl obo:BFO_0000144 process profile obo:BFO_0000145 r-quality obo:BFO_0000145 RelationalQuality obo:BFO_0000145 John’s role of husband to Mary is dependent on Mary’s role of wife to John, and both are dependent on the object aggregate comprising John and Mary as member parts joined together through the relational quality of being married. obo:BFO_0000145 a marriage bond, an instance of love, an obligation between one person and another. obo:bfo/axiom/057-001 obo:BFO_0000145 b is a relational quality = Def. for some independent continuants c, d and for some time t: b quality_of c at t & b quality_of d at t. (axiom label in BFO2 Reference: [057-001]) obo:bfo/axiom/057-001 obo:BFO_0000145 (iff (RelationalQuality a) (exists (b c t) (and (IndependentContinuant b) (IndependentContinuant c) (qualityOfAt a b t) (qualityOfAt a c t)))) // axiom label in BFO2 CLIF: [057-001] obo:BFO_0000145 obo:bfo.owl obo:BFO_0000145 relational quality obo:BFO_0000146 2d-cf-boundary obo:BFO_0000146 TwoDimensionalContinuantFiatBoundary obo:bfo/axiom/033-001 obo:BFO_0000146 a two-dimensional continuant fiat boundary (surface) is a self-connected fiat surface whose location is defined in relation to some material entity. (axiom label in BFO2 Reference: [033-001]) obo:bfo/axiom/033-001 obo:BFO_0000146 (iff (TwoDimensionalContinuantFiatBoundary a) (and (ContinuantFiatBoundary a) (exists (b) (and (TwoDimensionalSpatialRegion b) (forall (t) (locatedInAt a b t)))))) // axiom label in BFO2 CLIF: [033-001] obo:BFO_0000146 obo:bfo.owl obo:BFO_0000146 two-dimensional continuant fiat boundary obo:BFO_0000147 0d-cf-boundary obo:BFO_0000147 ZeroDimensionalContinuantFiatBoundary obo:BFO_0000147 the geographic North Pole obo:BFO_0000147 the point of origin of some spatial coordinate system. obo:BFO_0000147 the quadripoint where the boundaries of Colorado, Utah, New Mexico, and Arizona meet obo:bfo/axiom/0000001 requested by Melanie Courtot https://groups.google.com/d/msg/bfo-owl-devel/s9Uug5QmAws/ZDRnpiIi_TUJ obo:BFO_0000147 zero dimension continuant fiat boundaries are not spatial points. Considering the example 'the quadripoint where the boundaries of Colorado, Utah, New Mexico, and Arizona meet' : There are many frames in which that point is zooming through many points in space. Whereas, no matter what the frame, the quadripoint is always in the same relation to the boundaries of Colorado, Utah, New Mexico, and Arizona. obo:bfo/axiom/031-001 obo:BFO_0000147 a zero-dimensional continuant fiat boundary is a fiat point whose location is defined in relation to some material entity. (axiom label in BFO2 Reference: [031-001]) obo:bfo/axiom/031-001 obo:BFO_0000147 (iff (ZeroDimensionalContinuantFiatBoundary a) (and (ContinuantFiatBoundary a) (exists (b) (and (ZeroDimensionalSpatialRegion b) (forall (t) (locatedInAt a b t)))))) // axiom label in BFO2 CLIF: [031-001] obo:BFO_0000147 obo:bfo.owl obo:BFO_0000147 zero-dimensional continuant fiat boundary obo:BFO_0000148 0d-t-region obo:BFO_0000148 ZeroDimensionalTemporalRegion obo:BFO_0000148 a temporal region that is occupied by a process boundary obo:BFO_0000148 right now obo:BFO_0000148 the moment at which a child is born obo:BFO_0000148 the moment at which a finger is detached in an industrial accident obo:BFO_0000148 the moment of death. obo:BFO_0000148 temporal instant. obo:BFO_0000148 obo:ogg.owl obo:bfo/axiom/102-001 obo:BFO_0000148 A zero-dimensional temporal region is a temporal region that is without extent. (axiom label in BFO2 Reference: [102-001]) obo:bfo/axiom/102-001 obo:BFO_0000148 (forall (x) (if (ZeroDimensionalTemporalRegion x) (TemporalRegion x))) // axiom label in BFO2 CLIF: [102-001] obo:BFO_0000148 obo:bfo.owl obo:BFO_0000148 zero-dimensional temporal region obo:BFO_0000151 st-projects-onto-s_st obo:BFO_0000151 obo:ogg.owl obo:BFO_0000151 obo:bfo.owl obo:BFO_0000151 projects onto spatial region at some time obo:BFO_0000152 s-projection-of-st_st obo:BFO_0000152 obo:ogg.owl obo:BFO_0000152 obo:bfo.owl obo:BFO_0000152 spatial projection of spatiotemporal at some time obo:BFO_0000153 st-projects-onto-t obo:BFO_0000153 obo:ogg.owl obo:BFO_0000153 obo:bfo.owl obo:BFO_0000153 projects onto temporal region obo:BFO_0000154 t-projection-of-st obo:BFO_0000154 obo:ogg.owl obo:BFO_0000154 obo:bfo.owl obo:BFO_0000154 temporal projection of spatiotemporal obo:BFO_0000155 spans obo:BFO_0000155 occupiesTemporalRegion obo:BFO_0000155 obo:ogg.owl obo:bfo/axiom/132-001 obo:BFO_0000155 p occupies_temporal_region t. This is a primitive relation between an occurrent p and the temporal region t upon which the spatiotemporal region p occupies_spatiotemporal_region projects. (axiom label in BFO2 Reference: [132-001]) obo:BFO_0000155 obo:bfo.owl obo:BFO_0000155 occupies temporal region obo:BFO_0000156 span-of obo:BFO_0000156 spanOf obo:BFO_0000156 obo:ogg.owl obo:BFO_0000156 [copied from inverse property 'occupies temporal region'] p occupies_temporal_region t. This is a primitive relation between an occurrent p and the temporal region t upon which the spatiotemporal region p occupies_spatiotemporal_region projects. (axiom label in BFO2 Reference: [132-001]) obo:BFO_0000156 obo:bfo.owl obo:BFO_0000156 has temporal occupant obo:BFO_0000157 during-which-exists obo:BFO_0000157 [copied from inverse property 'exists at'] BFO2 Reference: entity obo:BFO_0000157 [copied from inverse property 'exists at'] BFO2 Reference: temporal region obo:BFO_0000157 obo:ogg.owl obo:BFO_0000157 [copied from inverse property 'exists at'] b exists_at t means: b is an entity which exists at some temporal region t. (axiom label in BFO2 Reference: [118-002]) obo:BFO_0000157 obo:bfo.owl obo:BFO_0000157 during which exists obo:BFO_0000158 bearer-of_at obo:BFO_0000158 bearerOfAt obo:bfo/axiom/053-004 obo:BFO_0000158 b bearer_of c at t =Def. c s-depends_on b at t & b is an independent continuant that is not a spatial region. (axiom label in BFO2 Reference: [053-004]) obo:BFO_0000158 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance-level, relation. The BFO reading of the binary relation 'bearer of at all times@en' is: forall(t) exists_at(x,t) -> exists_at(y,t) and 'bearer of@en(x,y,t)'. obo:BFO_0000158 BFO2 Reference: independent continuant that is not a spatial region obo:BFO_0000158 BFO2 Reference: specifically dependent continuant obo:BFO_0000158 obo:ogg.owl obo:bfo/axiom/053-004 obo:BFO_0000158 (iff (bearerOfAt a b t) (and (specificallyDependsOnAt b a t) (IndependentContinuant a) (not (SpatialRegion a)) (existsAt b t))) // axiom label in BFO2 CLIF: [053-004] obo:BFO_0000158 obo:bfo.owl obo:BFO_0000158 bearer of at all times obo:BFO_0000159 has-q_at obo:BFO_0000159 obo:bfo.owl obo:BFO_0000159 has quality at all times obo:BFO_0000160 has-f_at obo:BFO_0000160 hasFunctionAt obo:bfo/axiom/070-001 obo:BFO_0000160 a has_function b at t =Def. b function_of a at t. (axiom label in BFO2 Reference: [070-001]) obo:BFO_0000160 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance-level, relation. The BFO reading of the binary relation 'has function at all times@en' is: forall(t) exists_at(x,t) -> exists_at(y,t) and 'has function@en(x,y,t)'. obo:bfo/axiom/070-001 obo:BFO_0000160 (iff (hasFunctionAt a b t) (functionOf b a t)) // axiom label in BFO2 CLIF: [070-001] obo:BFO_0000160 obo:bfo.owl obo:BFO_0000160 has function at all times obo:BFO_0000161 has-r_at obo:BFO_0000161 hasRoleAt obo:bfo/axiom/068-001 obo:BFO_0000161 a has_role b at t =Def. b role_of a at t. (axiom label in BFO2 Reference: [068-001]) obo:BFO_0000161 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance-level, relation. The BFO reading of the binary relation 'has role at all times@en' is: forall(t) exists_at(x,t) -> exists_at(y,t) and 'has role@en(x,y,t)'. obo:bfo/axiom/068-001 obo:BFO_0000161 (iff (hasRoleAt a b t) (roleOfAt b a t)) // axiom label in BFO2 CLIF: [068-001] obo:BFO_0000161 obo:bfo.owl obo:BFO_0000161 has role at all times obo:BFO_0000162 has-d_at obo:BFO_0000162 hasDispositionAt obo:bfo/axiom/069-001 obo:BFO_0000162 a has_disposition b at t =Def. b disposition_of a at t. (axiom label in BFO2 Reference: [069-001]) obo:BFO_0000162 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance-level, relation. The BFO reading of the binary relation 'has disposition at all times@en' is: forall(t) exists_at(x,t) -> exists_at(y,t) and 'has disposition@en(x,y,t)'. obo:BFO_0000162 obo:ogg.owl obo:bfo/axiom/069-001 obo:BFO_0000162 (iff (hasDispositionAt a b t) (dispositionOf b a t)) // axiom label in BFO2 CLIF: [069-001] obo:BFO_0000162 obo:bfo.owl obo:BFO_0000162 has disposition at all times obo:BFO_0000163 material-basis-of_at obo:BFO_0000163 obo:bfo.owl obo:BFO_0000163 material basis of at all times obo:BFO_0000164 concretizes_at obo:BFO_0000164 concretizesAt obo:BFO_0000164 You may concretize a piece of software by installing it in your computer obo:BFO_0000164 You may concretize a recipe that you find in a cookbook by turning it into a plan which exists as a realizable dependent continuant in your head. obo:BFO_0000164 you may concretize a poem as a pattern of memory traces in your head obo:BFO_0000164 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance-level, relation. The BFO reading of the binary relation 'concretizes at all times@en' is: forall(t) exists_at(x,t) -> exists_at(y,t) and 'concretizes@en(x,y,t)'. obo:bfo/axiom/075-002 obo:BFO_0000164 b concretizes c at t means: b is a specifically dependent continuant & c is a generically dependent continuant & for some independent continuant that is not a spatial region d, b s-depends_on d at t & c g-depends on d at t & if c migrates from bearer d to another bearer e than a copy of b will be created in e. (axiom label in BFO2 Reference: [075-002]) obo:bfo/axiom/076-001 obo:BFO_0000164 if b g-depends on c at some time t, then there is some d, such that d concretizes b at t and d s-depends_on c at t. (axiom label in BFO2 Reference: [076-001]) obo:bfo/axiom/075-002 obo:BFO_0000164 (forall (x y t) (if (concretizesAt x y t) (and (SpecificallyDependentContinuant x) (GenericallyDependentContinuant y) (exists (z) (and (IndependentContinuant z) (specificallyDependsOnAt x z t) (genericallyDependsOnAt y z t)))))) // axiom label in BFO2 CLIF: [075-002] obo:bfo/axiom/076-001 obo:BFO_0000164 (forall (x y t) (if (genericallyDependsOnAt x y t) (exists (z) (and (concretizesAt z x t) (specificallyDependsOnAt z y t))))) // axiom label in BFO2 CLIF: [076-001] obo:BFO_0000164 obo:bfo.owl obo:BFO_0000164 concretizes at all times obo:BFO_0000165 concretized-by_at obo:BFO_0000165 obo:bfo.owl obo:BFO_0000165 concretized by at all times obo:BFO_0000166 participates-in_at obo:BFO_0000166 participatesInAt obo:BFO_0000166 obo:bfo.owl obo:BFO_0000166 participates in at all times obo:BFO_0000167 has-participant_at obo:BFO_0000167 hasParticipantAt obo:BFO_0000167 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance-level, relation. The BFO reading of the binary relation 'has participant at all times@en' is: forall(t) exists_at(x,t) -> exists_at(y,t) and 'has participant@en(x,y,t)'. obo:BFO_0000167 BFO 2 Reference: Spatial regions do not participate in processes. obo:BFO_0000167 BFO2 Reference: independent continuant that is not a spatial region, specifically dependent continuant, generically dependent continuant obo:BFO_0000167 BFO2 Reference: process obo:bfo/axiom/086-003 obo:BFO_0000167 has_participant is an instance-level relation between a process, a continuant, and a temporal region at which the continuant participates in some way in the process. (axiom label in BFO2 Reference: [086-003]) obo:bfo/axiom/091-003 obo:BFO_0000167 if b has_participant c at t & c is a generically dependent continuant, then there is some independent continuant that is not a spatial region d, and which is such that c g-depends on d at t & b s-depends_on d at t. (axiom label in BFO2 Reference: [091-003]) obo:bfo/axiom/090-003 obo:BFO_0000167 if b has_participant c at t & c is a specifically dependent continuant, then there is some independent continuant that is not a spatial region d, c s-depends_on d at t & b s-depends_on d at t. (axiom label in BFO2 Reference: [090-003]) obo:bfo/axiom/087-001 obo:BFO_0000167 if b has_participant c at t then b is an occurrent. (axiom label in BFO2 Reference: [087-001]) obo:bfo/axiom/089-001 obo:BFO_0000167 if b has_participant c at t then c exists at t. (axiom label in BFO2 Reference: [089-001]) obo:bfo/axiom/088-001 obo:BFO_0000167 if b has_participant c at t then c is a continuant. (axiom label in BFO2 Reference: [088-001]) obo:bfo/axiom/091-003 obo:BFO_0000167 (forall (x y t) (if (and (hasParticipantAt x y t) (GenericallyDependentContinuant y)) (exists (z) (and (IndependentContinuant z) (not (SpatialRegion z)) (genericallyDependsOn y z t) (specificallyDependsOnAt x z t))))) // axiom label in BFO2 CLIF: [091-003] obo:bfo/axiom/090-003 obo:BFO_0000167 (forall (x y t) (if (and (hasParticipantAt x y t) (SpecificallyDependentContinuant y)) (exists (z) (and (IndependentContinuant z) (not (SpatialRegion z)) (specificallyDependsOnAt x z t) (specificallyDependsOnAt y z t))))) // axiom label in BFO2 CLIF: [090-003] obo:bfo/axiom/088-001 obo:BFO_0000167 (forall (x y t) (if (hasParticipantAt x y t) (Continuant y))) // axiom label in BFO2 CLIF: [088-001] obo:bfo/axiom/087-001 obo:BFO_0000167 (forall (x y t) (if (hasParticipantAt x y t) (Occurrent x))) // axiom label in BFO2 CLIF: [087-001] obo:bfo/axiom/089-001 obo:BFO_0000167 (forall (x y t) (if (hasParticipantAt x y t) (existsAt y t))) // axiom label in BFO2 CLIF: [089-001] obo:BFO_0000167 obo:bfo.owl obo:BFO_0000167 has participant at all times obo:BFO_0000168 has-s-dep_at obo:BFO_0000168 obo:ogg.owl obo:BFO_0000168 obo:bfo.owl obo:BFO_0000168 has specific dependent at all times obo:BFO_0000169 s-depends-on_st obo:BFO_0000169 specificallyDependsOn obo:BFO_0000169 A pain s-depends_on the organism that is experiencing the pain obo:BFO_0000169 a gait s-depends_on the walking object. (All at some specific time.) obo:BFO_0000169 a shape s-depends_on the shaped object obo:BFO_0000169 one-sided s-dependence of a dependent continuant on an independent continuant: an instance of headache s-depends_on some head obo:BFO_0000169 one-sided s-dependence of a dependent continuant on an independent continuant: an instance of temperature s-depends_on some organism obo:BFO_0000169 one-sided s-dependence of a process on something: a process of cell death s-depends_on a cell obo:BFO_0000169 one-sided s-dependence of a process on something: an instance of seeing (a relational process) s-depends_on some organism and on some seen entity, which may be an occurrent or a continuant obo:BFO_0000169 one-sided s-dependence of one occurrent on another: a process of answering a question is dependent on a prior process of asking a question obo:BFO_0000169 one-sided s-dependence of one occurrent on another: a process of obeying a command is dependent on a prior process of issuing a command obo:BFO_0000169 one-sided s-dependence of one occurrent on multiple independent continuants: a relational process of hitting a ball with a cricket bat obo:BFO_0000169 one-sided s-dependence of one occurrent on multiple independent continuants: a relational process of paying cash to a merchant in exchange for a bag of figs obo:BFO_0000169 reciprocal s-dependence between occurrents: a process of buying and the associated process of selling obo:BFO_0000169 reciprocal s-dependence between occurrents: a process of increasing the volume of a portion of gas while temperature remains constant and the associated process of decreasing the pressure exerted by the gas obo:BFO_0000169 reciprocal s-dependence between occurrents: in a game of chess the process of playing with the white pieces is mutually dependent on the process of playing with the black pieces obo:BFO_0000169 the one-sided dependence of an occurrent on an independent continuant: football match on the players, the ground, the ball obo:BFO_0000169 the one-sided dependence of an occurrent on an independent continuant: handwave on a hand obo:BFO_0000169 the three-sided reciprocal s-dependence of the hue, saturation and brightness of a color [45 obo:BFO_0000169 the three-sided reciprocal s-dependence of the pitch, timbre and volume of a tone [45 obo:BFO_0000169 the two-sided reciprocal s-dependence of the roles of husband and wife [20 obo:BFO_0000169 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance level, relation. The BFO reading of the binary relation 'specifically depends on at some time@en' is: exists t, exists_at(x,t) & exists_at(y,t) & 'specifically depends on@en'(x,y,t) obo:BFO_0000169 BFO 2 Reference: An entity – for example an act of communication or a game of football – can s-depends_on more than one entity. Complex phenomena for example in the psychological and social realms (such as inferring, commanding and requesting) or in the realm of multi-organismal biological processes (such as infection and resistance), will involve multiple families of dependence relations, involving both continuants and occurrents [1, 4, 28 obo:BFO_0000169 BFO 2 Reference: S-dependence is just one type of dependence among many; it is what, in the literature, is referred to as ‘existential dependence’ [87, 46, 65, 20 obo:BFO_0000169 BFO 2 Reference: the relation of s-depends_on does not in every case require simultaneous existence of its relata. Note the difference between such cases and the cases of continuant universals defined historically: the act of answering depends existentially on the prior act of questioning; the human being who was baptized or who answered a question does not himself depend existentially on the prior act of baptism or answering. He would still exist even if these acts had never taken place. obo:BFO_0000169 BFO2 Reference: specifically dependent continuant\; process; process boundary obo:BFO_0000169 obo:ogg.owl obo:BFO_0000169 To say that b s-depends_on a at t is to say that b and c do not share common parts & b is of its nature such that it cannot exist unless c exists & b is not a boundary of c and b is not a site of which c is the host [64 obo:bfo/axiom/052-001 obo:BFO_0000169 If b is s-depends_on something at some time, then b is not a material entity. (axiom label in BFO2 Reference: [052-001]) obo:bfo/axiom/136-001 obo:BFO_0000169 If b s-depends_on something at t, then there is some c, which is an independent continuant and not a spatial region, such that b s-depends_on c at t. (axiom label in BFO2 Reference: [136-001]) obo:bfo/axiom/015-002 obo:BFO_0000169 If occurrent b s-depends_on some independent continuant c at t, then b s-depends_on c at every time at which b exists. (axiom label in BFO2 Reference: [015-002]) obo:bfo/axiom/013-002 obo:BFO_0000169 an entity does not s-depend_on any of its (continuant or occurrent) parts or on anything it is part of. (axiom label in BFO2 Reference: [013-002]) obo:bfo/axiom/054-002 obo:BFO_0000169 if b s-depends_on c at t & c s-depends_on d at t then b s-depends_on d at t. (axiom label in BFO2 Reference: [054-002]) obo:bfo/axiom/013-002 obo:BFO_0000169 (forall (x y t) (if (and (Entity x) (or (continuantPartOfAt y x t) (continuantPartOfAt x y t) (occurrentPartOf x y) (occurrentPartOf y x))) (not (specificallyDependsOnAt x y t)))) // axiom label in BFO2 CLIF: [013-002] obo:bfo/axiom/015-002 obo:BFO_0000169 (forall (x y t) (if (and (Occurrent x) (IndependentContinuant y) (specificallyDependsOnAt x y t)) (forall (t_1) (if (existsAt x t_1) (specificallyDependsOnAt x y t_1))))) // axiom label in BFO2 CLIF: [015-002] obo:bfo/axiom/136-001 obo:BFO_0000169 (forall (x y t) (if (specificallyDependsOnAt x y t) (exists (z) (and (IndependentContinuant z) (not (SpatialRegion z)) (specificallyDependsOnAt x z t))))) // axiom label in BFO2 CLIF: [136-001] obo:bfo/axiom/054-002 obo:BFO_0000169 (forall (x y z t) (if (and (specificallyDependsOnAt x y t) (specificallyDependsOnAt y z t)) (specificallyDependsOnAt x z t))) // axiom label in BFO2 CLIF: [054-002] obo:bfo/axiom/052-001 obo:BFO_0000169 (forall (x) (if (exists (y t) (specificallyDependsOnAt x y t)) (not (MaterialEntity x)))) // axiom label in BFO2 CLIF: [052-001] obo:BFO_0000169 obo:bfo.owl obo:BFO_0000169 specifically depends on at some time obo:BFO_0000170 has-location_at obo:BFO_0000170 obo:bfo.owl obo:BFO_0000170 has location at all times obo:BFO_0000171 located-in_st obo:BFO_0000171 locatedInAt obo:BFO_0000171 Mary located_in Salzburg obo:BFO_0000171 the Empire State Building located_in New York. obo:BFO_0000171 this portion of cocaine located_in this portion of blood obo:BFO_0000171 this stem cell located_in this portion of bone marrow obo:BFO_0000171 your arm located_in your body obo:bfo/axiom/045-001 obo:BFO_0000171 b located_in c at t = Def. b and c are independent continuants, and the region at which b is located at t is a (proper or improper) continuant_part_of the region at which c is located at t. (axiom label in BFO2 Reference: [045-001]) obo:BFO_0000171 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance level, relation. The BFO reading of the binary relation 'located in at some time@en' is: exists t, exists_at(x,t) & exists_at(y,t) & 'located in@en'(x,y,t) obo:BFO_0000171 BFO2 Reference: independent continuant obo:bfo/axiom/046-001 obo:BFO_0000171 Located_in is transitive. (axiom label in BFO2 Reference: [046-001]) obo:bfo/axiom/048-001 obo:BFO_0000171 for all independent continuants b, c, and d: if b continuant_part_of c at t & c located_in d at t, then b located_in d at t. (axiom label in BFO2 Reference: [048-001]) obo:bfo/axiom/049-001 obo:BFO_0000171 for all independent continuants b, c, and d: if b located_in c at t & c continuant_part_of d at t, then b located_in d at t. (axiom label in BFO2 Reference: [049-001]) obo:bfo/axiom/048-001 obo:BFO_0000171 (forall (x y z t) (if (and (IndependentContinuant x) (IndependentContinuant y) (IndependentContinuant z) (continuantPartOfAt x y t) (locatedInAt y z t)) (locatedInAt x z t))) // axiom label in BFO2 CLIF: [048-001] obo:bfo/axiom/049-001 obo:BFO_0000171 (forall (x y z t) (if (and (IndependentContinuant x) (IndependentContinuant y) (IndependentContinuant z) (locatedInAt x y t) (continuantPartOfAt y z t)) (locatedInAt x z t))) // axiom label in BFO2 CLIF: [049-001] obo:bfo/axiom/046-001 obo:BFO_0000171 (forall (x y z t) (if (and (locatedInAt x y t) (locatedInAt y z t)) (locatedInAt x z t))) // axiom label in BFO2 CLIF: [046-001] obo:bfo/axiom/045-001 obo:BFO_0000171 (iff (locatedInAt a b t) (and (IndependentContinuant a) (IndependentContinuant b) (exists (r_1 r_2) (and (occupiesSpatialRegionAt a r_1 t) (occupiesSpatialRegionAt b r_2 t) (continuantPartOfAt r_1 r_2 t))))) // axiom label in BFO2 CLIF: [045-001] obo:BFO_0000171 obo:bfo.owl obo:BFO_0000171 located in at some time obo:BFO_0000172 has-member-part_at obo:BFO_0000172 obo:bfo.owl obo:BFO_0000172 has member part at all times obo:BFO_0000173 member-part-of_at obo:BFO_0000173 memberPartOfAt obo:BFO_0000173 each piece in a chess set is a member part of the chess set; each Beatle in the collection called The Beatles is a member part of The Beatles. obo:BFO_0000173 each tree in a forest is a member_part of the forest obo:bfo/axiom/026-004 obo:BFO_0000173 b member_part_of c at t =Def. b is an object & there is at t a mutually exhaustive and pairwise disjoint partition of c into objects x1, …, xn (for some n &gt; 1) with b = xi for some 1 ? i ? n. (axiom label in BFO2 Reference: [026-004]) obo:BFO_0000173 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance-level, relation. The BFO reading of the binary relation 'member part of at all times@en' is: forall(t) exists_at(x,t) -> exists_at(y,t) and 'member part of@en(x,y,t)'. obo:BFO_0000173 BFO2 Reference: object obo:BFO_0000173 BFO2 Reference: object aggregate obo:bfo/axiom/104-001 obo:BFO_0000173 if b member_part_of c at t then b continuant_part_of c at t. (axiom label in BFO2 Reference: [104-001]) obo:bfo/axiom/104-001 obo:BFO_0000173 (forall (x y t) (if (memberPartOfAt x y t) (continuantPartOfAt x y t))) // axiom label in BFO2 CLIF: [104-001] obo:BFO_0000173 obo:bfo.owl obo:BFO_0000173 member part of at all times obo:BFO_0000174 c-has-ppart_st obo:BFO_0000174 hasProperContinuantPartAt obo:BFO_0000174 [copied from inverse property 'proper part of continuant at some time'] b proper_continuant_part_of c at t =Def. b continuant_part_of c at t & b and c are not identical. (axiom label in BFO2 Reference: [004-001]) obo:BFO_0000174 b has_proper_continuant_part c at t = Def. c proper_continuant_part_of b at t. [XXX-001 obo:BFO_0000174 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance level, relation. The BFO reading of the binary relation 'has proper continuant part at some time@en' is: exists t, exists_at(x,t) & exists_at(y,t) & 'has proper continuant part@en'(x,y,t) obo:BFO_0000174 [copied from inverse property 'proper part of continuant at some time'] Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance level, relation. The BFO reading of the binary relation 'proper part of continuant at some time@en' is: exists t, exists_at(x,t) & exists_at(y,t) & 'proper part of continuant@en'(x,y,t) obo:BFO_0000174 obo:bfo.owl obo:BFO_0000174 has proper continuant part at some time obo:BFO_0000175 c-ppart-of_st obo:BFO_0000175 properContinuantPartOfAt obo:BFO_0000175 [copied from inverse property 'has proper continuant part at some time'] b has_proper_continuant_part c at t = Def. c proper_continuant_part_of b at t. [XXX-001 obo:bfo/axiom/004-001 obo:BFO_0000175 b proper_continuant_part_of c at t =Def. b continuant_part_of c at t & b and c are not identical. (axiom label in BFO2 Reference: [004-001]) obo:BFO_0000175 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance level, relation. The BFO reading of the binary relation 'proper part of continuant at some time@en' is: exists t, exists_at(x,t) & exists_at(y,t) & 'proper part of continuant@en'(x,y,t) obo:BFO_0000175 [copied from inverse property 'has proper continuant part at some time'] Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance level, relation. The BFO reading of the binary relation 'has proper continuant part at some time@en' is: exists t, exists_at(x,t) & exists_at(y,t) & 'has proper continuant part@en'(x,y,t) obo:bfo/axiom/004-001 obo:BFO_0000175 (iff (properContinuantPartOfAt a b t) (and (continuantPartOfAt a b t) (not (= a b)))) // axiom label in BFO2 CLIF: [004-001] obo:BFO_0000175 obo:bfo.owl obo:BFO_0000175 proper part of continuant at some time obo:BFO_0000176 c-part-of_st obo:BFO_0000176 continuantPartOfAt obo:BFO_0000176 Mary’s arm continuant_part_of Mary in the time of her life prior to her operation obo:BFO_0000176 the Northern hemisphere of the planet Earth is a part of the planet Earth at all times at which the planet Earth exists. obo:BFO_0000176 [copied from inverse property 'has continuant part at some time'] b has_continuant_part c at t = Def. c continuant_part_of b at t. (axiom label in BFO2 Reference: [006-001]) obo:BFO_0000176 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance level, relation. The BFO reading of the binary relation 'part of continuant at some time@en' is: exists t, exists_at(x,t) & exists_at(y,t) & 'part of continuant@en'(x,y,t) obo:bfo/axiom/028-001 obo:BFO_0000176 BFO 2 Reference: Immaterial entities are in some cases continuant parts of their material hosts. Thus the hold of a ship, for example, is a part of the ship; it may itself have parts, which may have names (used for example by ship stow planners, customs inspectors, and the like). Immaterial entities under both 1. and 2. can be of zero, one, two or three dimensions. We define:a(immaterial entity)[Definition: a is an immaterial entity = Def. a is an independent continuant that has no material entities as parts. (axiom label in BFO2 Reference: [028-001]) obo:BFO_0000176 BFO 2 Reference: a (continuant or occurrent) part of itself. We appreciate that this is counterintuitive for some users, since it implies for example that President Obama is a part of himself. However it brings benefits in simplifying the logical formalism, and it captures an important feature of identity, namely that it is the limit case of mereological inclusion. obo:BFO_0000176 BFO2 Reference: continuant obo:BFO_0000176 BFO2 Reference: continuantThe range for ‘t’ (as in all cases throughout this document unless otherwise specified) is: temporal region. obo:BFO_0000176 [copied from inverse property 'has continuant part at some time'] Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance level, relation. The BFO reading of the binary relation 'has continuant part at some time@en' is: exists t, exists_at(x,t) & exists_at(y,t) & 'has continuant part@en'(x,y,t) obo:BFO_0000176 obo:ogg.owl obo:bfo/axiom/002-001 obo:BFO_0000176 b continuant_part_of c at t =Def. b is a part of c at t & t is a time & b and c are continuants. (axiom label in BFO2 Reference: [002-001]) obo:bfo/axiom/120-001 obo:BFO_0000176 continuant_part_of is antisymmetric. (axiom label in BFO2 Reference: [120-001]) obo:bfo/axiom/111-002 obo:BFO_0000176 continuant_part_of is reflexive (every continuant entity is a continuant_part_of itself). (axiom label in BFO2 Reference: [111-002]) obo:bfo/axiom/110-001 obo:BFO_0000176 continuant_part_of is transitive. (axiom label in BFO2 Reference: [110-001]) obo:bfo/axiom/122-001 obo:BFO_0000176 continuant_part_of satisfies unique product. (axiom label in BFO2 Reference: [122-001]) obo:bfo/axiom/121-001 obo:BFO_0000176 continuant_part_of satisfies weak supplementation. (axiom label in BFO2 Reference: [121-001]) obo:bfo/axiom/047-002 obo:BFO_0000176 if b continuant_part_of c at t and b is an independent continuant, then b is located_in c at t. (axiom label in BFO2 Reference: [047-002]) obo:bfo/axiom/111-002 obo:BFO_0000176 (forall (x t) (if (Continuant x) (continuantPartOfAt x x t))) // axiom label in BFO2 CLIF: [111-002] obo:bfo/axiom/047-002 obo:BFO_0000176 (forall (x y t) (if (and (continuantPartOfAt x y t) (IndependentContinuant x)) (locatedInAt x y t))) // axiom label in BFO2 CLIF: [047-002] obo:bfo/axiom/120-001 obo:BFO_0000176 (forall (x y t) (if (and (continuantPartOfAt x y t) (continuantPartOfAt y x t)) (= x y))) // axiom label in BFO2 CLIF: [120-001] obo:bfo/axiom/121-001 obo:BFO_0000176 (forall (x y t) (if (and (continuantPartOfAt x y t) (not (= x y))) (exists (z) (and (continuantPartOfAt z y t) (not (exists (w) (and (continuantPartOfAt w x t) (continuantPartOfAt w z t)))))))) // axiom label in BFO2 CLIF: [121-001] obo:bfo/axiom/122-001 obo:BFO_0000176 (forall (x y t) (if (exists (v) (and (continuantPartOfAt v x t) (continuantPartOfAt v y t))) (exists (z) (forall (u w) (iff (iff (continuantPartOfAt w u t) (and (continuantPartOfAt w x t) (continuantPartOfAt w y t))) (= z u)))))) // axiom label in BFO2 CLIF: [122-001] obo:bfo/axiom/110-001 obo:BFO_0000176 (forall (x y z t) (if (and (continuantPartOfAt x y t) (continuantPartOfAt y z t)) (continuantPartOfAt x z t))) // axiom label in BFO2 CLIF: [110-001] obo:bfo/axiom/028-001 obo:BFO_0000176 (iff (ImmaterialEntity a) (and (IndependentContinuant a) (not (exists (b t) (and (MaterialEntity b) (continuantPartOfAt b a t)))))) // axiom label in BFO2 CLIF: [028-001] obo:BFO_0000176 obo:bfo.owl obo:BFO_0000176 part of continuant at some time obo:BFO_0000177 c-part-of_at obo:BFO_0000177 continuantPartOfAt obo:BFO_0000177 Mary’s arm continuant_part_of Mary in the time of her life prior to her operation obo:BFO_0000177 the Northern hemisphere of the planet Earth is a part of the planet Earth at all times at which the planet Earth exists. obo:BFO_0000177 [copied from inverse property 'has continuant part at all times that part exists'] forall(t) exists_at(y,t) -> exists_at(x,t) and 'has continuant part'(x,y,t) obo:BFO_0000177 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance-level, relation. The BFO reading of the binary relation 'part of continuant at all times@en' is: forall(t) exists_at(x,t) -> exists_at(y,t) and 'part of continuant@en(x,y,t)'. obo:bfo/axiom/028-001 obo:BFO_0000177 BFO 2 Reference: Immaterial entities are in some cases continuant parts of their material hosts. Thus the hold of a ship, for example, is a part of the ship; it may itself have parts, which may have names (used for example by ship stow planners, customs inspectors, and the like). Immaterial entities under both 1. and 2. can be of zero, one, two or three dimensions. We define:a(immaterial entity)[Definition: a is an immaterial entity = Def. a is an independent continuant that has no material entities as parts. (axiom label in BFO2 Reference: [028-001]) obo:BFO_0000177 BFO 2 Reference: a (continuant or occurrent) part of itself. We appreciate that this is counterintuitive for some users, since it implies for example that President Obama is a part of himself. However it brings benefits in simplifying the logical formalism, and it captures an important feature of identity, namely that it is the limit case of mereological inclusion. obo:BFO_0000177 BFO2 Reference: continuant obo:BFO_0000177 BFO2 Reference: continuantThe range for ‘t’ (as in all cases throughout this document unless otherwise specified) is: temporal region. obo:BFO_0000177 [copied from inverse property 'has continuant part at all times that part exists'] This is a binary version of a ternary time-indexed, instance level, relation. Unlike the rest of the temporalized relations which temporally quantify over existence of the subject of the relation, this relation temporally quantifies over the existence of the object of the relation. The relation is provided tentatively, to assess whether the GO needs such a relation. It is inverse of 'part of continuant at all times' obo:bfo/axiom/002-001 obo:BFO_0000177 b continuant_part_of c at t =Def. b is a part of c at t & t is a time & b and c are continuants. (axiom label in BFO2 Reference: [002-001]) obo:bfo/axiom/120-001 obo:BFO_0000177 continuant_part_of is antisymmetric. (axiom label in BFO2 Reference: [120-001]) obo:bfo/axiom/111-002 obo:BFO_0000177 continuant_part_of is reflexive (every continuant entity is a continuant_part_of itself). (axiom label in BFO2 Reference: [111-002]) obo:bfo/axiom/110-001 obo:BFO_0000177 continuant_part_of is transitive. (axiom label in BFO2 Reference: [110-001]) obo:bfo/axiom/122-001 obo:BFO_0000177 continuant_part_of satisfies unique product. (axiom label in BFO2 Reference: [122-001]) obo:bfo/axiom/121-001 obo:BFO_0000177 continuant_part_of satisfies weak supplementation. (axiom label in BFO2 Reference: [121-001]) obo:bfo/axiom/047-002 obo:BFO_0000177 if b continuant_part_of c at t and b is an independent continuant, then b is located_in c at t. (axiom label in BFO2 Reference: [047-002]) obo:bfo/axiom/111-002 obo:BFO_0000177 (forall (x t) (if (Continuant x) (continuantPartOfAt x x t))) // axiom label in BFO2 CLIF: [111-002] obo:bfo/axiom/047-002 obo:BFO_0000177 (forall (x y t) (if (and (continuantPartOfAt x y t) (IndependentContinuant x)) (locatedInAt x y t))) // axiom label in BFO2 CLIF: [047-002] obo:bfo/axiom/120-001 obo:BFO_0000177 (forall (x y t) (if (and (continuantPartOfAt x y t) (continuantPartOfAt y x t)) (= x y))) // axiom label in BFO2 CLIF: [120-001] obo:bfo/axiom/121-001 obo:BFO_0000177 (forall (x y t) (if (and (continuantPartOfAt x y t) (not (= x y))) (exists (z) (and (continuantPartOfAt z y t) (not (exists (w) (and (continuantPartOfAt w x t) (continuantPartOfAt w z t)))))))) // axiom label in BFO2 CLIF: [121-001] obo:bfo/axiom/122-001 obo:BFO_0000177 (forall (x y t) (if (exists (v) (and (continuantPartOfAt v x t) (continuantPartOfAt v y t))) (exists (z) (forall (u w) (iff (iff (continuantPartOfAt w u t) (and (continuantPartOfAt w x t) (continuantPartOfAt w y t))) (= z u)))))) // axiom label in BFO2 CLIF: [122-001] obo:bfo/axiom/110-001 obo:BFO_0000177 (forall (x y z t) (if (and (continuantPartOfAt x y t) (continuantPartOfAt y z t)) (continuantPartOfAt x z t))) // axiom label in BFO2 CLIF: [110-001] obo:bfo/axiom/028-001 obo:BFO_0000177 (iff (ImmaterialEntity a) (and (IndependentContinuant a) (not (exists (b t) (and (MaterialEntity b) (continuantPartOfAt b a t)))))) // axiom label in BFO2 CLIF: [028-001] obo:BFO_0000177 obo:bfo.owl obo:BFO_0000177 part of continuant at all times obo:BFO_0000178 c-has-part_st obo:BFO_0000178 hasContinuantPartAt obo:BFO_0000178 [copied from inverse property 'part of continuant at some time'] Mary’s arm continuant_part_of Mary in the time of her life prior to her operation obo:BFO_0000178 [copied from inverse property 'part of continuant at some time'] the Northern hemisphere of the planet Earth is a part of the planet Earth at all times at which the planet Earth exists. obo:bfo/axiom/006-001 obo:BFO_0000178 b has_continuant_part c at t = Def. c continuant_part_of b at t. (axiom label in BFO2 Reference: [006-001]) obo:BFO_0000178 Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance level, relation. The BFO reading of the binary relation 'has continuant part at some time@en' is: exists t, exists_at(x,t) & exists_at(y,t) & 'has continuant part@en'(x,y,t) obo:BFO_0000178 [copied from inverse property 'part of continuant at some time'] Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance level, relation. The BFO reading of the binary relation 'part of continuant at some time@en' is: exists t, exists_at(x,t) & exists_at(y,t) & 'part of continuant@en'(x,y,t) obo:BFO_0000178 [copied from inverse property 'part of continuant at some time'] BFO 2 Reference: Immaterial entities are in some cases continuant parts of their material hosts. Thus the hold of a ship, for example, is a part of the ship; it may itself have parts, which may have names (used for example by ship stow planners, customs inspectors, and the like). Immaterial entities under both 1. and 2. can be of zero, one, two or three dimensions. We define:a(immaterial entity)[Definition: a is an immaterial entity = Def. a is an independent continuant that has no material entities as parts. (axiom label in BFO2 Reference: [028-001]) obo:BFO_0000178 [copied from inverse property 'part of continuant at some time'] BFO 2 Reference: a (continuant or occurrent) part of itself. We appreciate that this is counterintuitive for some users, since it implies for example that President Obama is a part of himself. However it brings benefits in simplifying the logical formalism, and it captures an important feature of identity, namely that it is the limit case of mereological inclusion. obo:BFO_0000178 [copied from inverse property 'part of continuant at some time'] BFO2 Reference: continuant obo:BFO_0000178 [copied from inverse property 'part of continuant at some time'] BFO2 Reference: continuantThe range for ‘t’ (as in all cases throughout this document unless otherwise specified) is: temporal region. obo:BFO_0000178 obo:ogg.owl obo:BFO_0000178 [copied from inverse property 'part of continuant at some time'] b continuant_part_of c at t =Def. b is a part of c at t & t is a time & b and c are continuants. (axiom label in BFO2 Reference: [002-001]) obo:bfo/axiom/006-001 obo:BFO_0000178 (iff (hasContinuantPartAt a b t) (continuantPartOfAt b a t)) // axiom label in BFO2 CLIF: [006-001] obo:BFO_0000178 obo:bfo.owl obo:BFO_0000178 has continuant part at some time obo:BFO_0000179 Relates an entity in the ontology to the name of the variable that is used to represent it in the code that generates the BFO OWL file from the lispy specification. obo:BFO_0000179 Really of interest to developers only obo:BFO_0000179 BFO OWL specification label obo:BFO_0000180 Relates an entity in the ontology to the term that is used to represent it in the the CLIF specification of BFO2 obo:BFO_0000180 Person:Alan Ruttenberg obo:BFO_0000180 Really of interest to developers only obo:BFO_0000180 BFO CLIF specification label obo:BFO_0000181 has-t-ppart obo:BFO_0000181 obo:bfo.owl obo:BFO_0000181 has proper temporal part obo:BFO_0000184 history-of obo:BFO_0000184 historyOf obo:BFO_0000184 [copied from inverse property 'has history'] b has_history c iff c history_of b [XXX-001 obo:BFO_0000184 b history_of c if c is a material entity or site and b is a history that is the unique history of cAxiom: if b history_of c and b history_of d then c=d [XXX-001 obo:BFO_0000184 obo:bfo.owl obo:BFO_0000184 history of obo:BFO_0000185 has-history obo:BFO_0000185 hasHistory obo:BFO_0000185 b has_history c iff c history_of b [XXX-001 obo:BFO_0000185 [copied from inverse property 'history of'] b history_of c if c is a material entity or site and b is a history that is the unique history of cAxiom: if b history_of c and b history_of d then c=d [XXX-001 obo:BFO_0000185 obo:bfo.owl obo:BFO_0000185 has history obo:BFO_0000186 c-part-of-object_at obo:BFO_0000186 [copied from inverse property 'has continuant part at all times'] b has_continuant_part c at t = Def. c continuant_part_of b at t. (axiom label in BFO2 Reference: [006-001]) obo:bfo/axiom/0000598 obo:BFO_0000186 forall(t) exists_at(y,t) -> exists_at(x,t) and 'part of continuant'(x,y,t) obo:bfo/axiom/0000599 obo:BFO_0000186 This is a binary version of a ternary time-indexed, instance level, relation. Unlike the rest of the temporalized relations which temporally quantify over existence of the subject of the relation, this relation temporally quantifies over the existence of the object of the relation. The relation is provided tentatively, to assess whether the GO needs such a relation. It is inverse of 'has continuant part at all times' obo:BFO_0000186 [copied from inverse property 'has continuant part at all times'] Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance-level, relation. The BFO reading of the binary relation 'has continuant part at all times@en' is: forall(t) exists_at(x,t) -> exists_at(y,t) and 'has continuant part@en(x,y,t)'. obo:BFO_0000186 obo:ogg.owl obo:BFO_0000186 obo:bfo.owl obo:BFO_0000186 part of continuant at all times that whole exists obo:BFO_0000187 c-has-part-object_at obo:BFO_0000187 [copied from inverse property 'part of continuant at all times'] Mary’s arm continuant_part_of Mary in the time of her life prior to her operation obo:BFO_0000187 [copied from inverse property 'part of continuant at all times'] the Northern hemisphere of the planet Earth is a part of the planet Earth at all times at which the planet Earth exists. obo:bfo/axiom/0000599 obo:BFO_0000187 forall(t) exists_at(y,t) -> exists_at(x,t) and 'has continuant part'(x,y,t) obo:bfo/axiom/0000600 obo:BFO_0000187 This is a binary version of a ternary time-indexed, instance level, relation. Unlike the rest of the temporalized relations which temporally quantify over existence of the subject of the relation, this relation temporally quantifies over the existence of the object of the relation. The relation is provided tentatively, to assess whether the GO needs such a relation. It is inverse of 'part of continuant at all times' obo:BFO_0000187 [copied from inverse property 'part of continuant at all times'] Alan Ruttenberg: This is a binary version of a ternary time-indexed, instance-level, relation. The BFO reading of the binary relation 'part of continuant at all times@en' is: forall(t) exists_at(x,t) -> exists_at(y,t) and 'part of continuant@en(x,y,t)'. obo:BFO_0000187 [copied from inverse property 'part of continuant at all times'] BFO 2 Reference: Immaterial entities are in some cases continuant parts of their material hosts. Thus the hold of a ship, for example, is a part of the ship; it may itself have parts, which may have names (used for example by ship stow planners, customs inspectors, and the like). Immaterial entities under both 1. and 2. can be of zero, one, two or three dimensions. We define:a(immaterial entity)[Definition: a is an immaterial entity = Def. a is an independent continuant that has no material entities as parts. (axiom label in BFO2 Reference: [028-001]) obo:BFO_0000187 [copied from inverse property 'part of continuant at all times'] BFO 2 Reference: a (continuant or occurrent) part of itself. We appreciate that this is counterintuitive for some users, since it implies for example that President Obama is a part of himself. However it brings benefits in simplifying the logical formalism, and it captures an important feature of identity, namely that it is the limit case of mereological inclusion. obo:BFO_0000187 [copied from inverse property 'part of continuant at all times'] BFO2 Reference: continuant obo:BFO_0000187 [copied from inverse property 'part of continuant at all times'] BFO2 Reference: continuantThe range for ‘t’ (as in all cases throughout this document unless otherwise specified) is: temporal region. obo:BFO_0000187 obo:ogg.owl obo:BFO_0000187 [copied from inverse property 'part of continuant at all times'] b continuant_part_of c at t =Def. b is a part of c at t & t is a time & b and c are continuants. (axiom label in BFO2 Reference: [002-001]) obo:BFO_0000187 obo:bfo.owl obo:BFO_0000187 has continuant part at all times that part exists obo:GO_0000012 The repair of single strand breaks in DNA. Repair of such breaks is mediated by the same enzyme systems as are used in base excision repair. obo:GO_0000012 obo:go.owl obo:GO_0000012 biological_process obo:GO_0000012 GO:0000012 obo:GO_0000012 single strand break repair obo:GO_0000041 The directed movement of transition metal ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. A transition metal is an element whose atom has an incomplete d-subshell of extranuclear electrons, or which gives rise to a cation or cations with an incomplete d-subshell. Transition metals often have more than one valency state. Biologically relevant transition metals include vanadium, manganese, iron, copper, cobalt, nickel, molybdenum and silver. obo:GO_0000041 obo:go.owl obo:GO_0000041 transition metal transport obo:GO_0000041 biological_process obo:GO_0000041 GO:0000041 obo:GO_0000041 transition metal ion transport obo:GO_0000049 Interacting selectively and non-covalently with transfer RNA. obo:GO_0000049 obo:go.owl obo:GO_0000049 GO:0000946 obo:GO_0000049 base pairing with tRNA obo:GO_0000049 molecular_function obo:GO_0000049 GO:0000049 obo:GO_0000049 tRNA binding obo:GO_0000062 Interacting selectively and non-covalently with acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in thiolester linkage with a fatty acyl group. obo:GO_0000062 obo:go.owl obo:GO_0000062 acyl-CoA or acyl binding obo:GO_0000062 molecular_function obo:GO_0000062 GO:0000062 obo:GO_0000062 fatty-acyl-CoA binding obo:GO_0000149 Interacting selectively and non-covalently with a SNARE (soluble N-ethylmaleimide-sensitive factor attached protein receptor) protein. obo:GO_0000149 obo:go.owl obo:GO_0000149 Reactome:R-HSA-210426 obo:GO_0000149 Reactome:R-HSA-210430 obo:GO_0000149 Reactome:R-HSA-265166 obo:GO_0000149 Reactome:R-HSA-372505 obo:GO_0000149 Reactome:R-HSA-372529 obo:GO_0000149 Reactome:R-HSA-374899 obo:GO_0000149 Reactome:R-HSA-374922 obo:GO_0000149 Reactome:R-HSA-376357 obo:GO_0000149 Reactome:R-HSA-376364 obo:GO_0000149 Reactome:R-HSA-376369 obo:GO_0000149 Reactome:R-HSA-380574 obo:GO_0000149 Reactome:R-HSA-380869 obo:GO_0000149 Reactome:R-HSA-380901 obo:GO_0000149 Reactome:R-HSA-380905 obo:GO_0000149 Reactome:R-HSA-888589 obo:GO_0000149 Reactome:R-HSA-9023173 obo:GO_0000149 Reactome:R-HSA-917744 obo:GO_0000149 SNAP receptor binding obo:GO_0000149 molecular_function obo:GO_0000149 GO:0000149 obo:GO_0000149 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0000149 SNARE binding obo:GO_0000155 Catalysis of the phosphorylation of a histidine residue in response to detection of an extracellular signal such as a chemical ligand or change in environment, to initiate a change in cell state or activity. The two-component sensor is a histidine kinase that autophosphorylates a histidine residue in its active site. The phosphate is then transferred to an aspartate residue in a downstream response regulator, to trigger a response. obo:GO_0000155 obo:go.owl obo:GO_0000155 EC:2.7.3 obo:GO_0000155 two-component sensor activity obo:GO_0000155 two-component sensor molecule obo:GO_0000155 two-component system sensor activity obo:GO_0000155 molecular_function obo:GO_0000155 GO:0000155 obo:GO_0000155 phosphorelay sensor kinase activity obo:GO_0000166 Interacting selectively and non-covalently with a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose. obo:GO_0000166 obo:go.owl obo:GO_0000166 MIPS_funcat:16.19 obo:GO_0000166 molecular_function obo:GO_0000166 GO:0000166 obo:GO_0000166 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0000166 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0000166 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0000166 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0000166 nucleotide binding obo:GO_0000182 Interacting selectively and non-covalently with DNA sequences encoding ribosomal RNA. obo:GO_0000182 obo:go.owl obo:GO_0000182 ribosomal DNA binding obo:GO_0000182 molecular_function obo:GO_0000182 GO:0000182 obo:GO_0000182 rDNA binding obo:GO_0000217 Interacting selectively and non-covalently with DNA containing secondary structure elements such as four-way junctions, bubbles, loops, Y-form DNA, or double-strand/single-strand junctions. obo:GO_0000217 obo:go.owl obo:GO_0000217 molecular_function obo:GO_0000217 GO:0000217 obo:GO_0000217 DNA secondary structure binding obo:GO_0000268 Interacting selectively and non-covalently with a peroxisomal targeting sequence, any of several sequences of amino acids within a protein that can act as a signal for the localization of the protein into the peroxisome. obo:GO_0000268 obo:go.owl obo:GO_0000268 GO:0005051 obo:GO_0000268 PTS binding obo:GO_0000268 PTS receptor obo:GO_0000268 peroxisome targeting signal receptor obo:GO_0000268 molecular_function obo:GO_0000268 GO:0000268 obo:GO_0000268 peroxisome targeting sequence binding obo:GO_0000287 Interacting selectively and non-covalently with magnesium (Mg) ions. obo:GO_0000287 obo:go.owl obo:GO_0000287 MIPS_funcat:16.17.07 obo:GO_0000287 magnesium binding obo:GO_0000287 molecular_function obo:GO_0000287 GO:0000287 obo:GO_0000287 magnesium ion binding obo:GO_0000302 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a reactive oxygen species stimulus. Reactive oxygen species include singlet oxygen, superoxide, and oxygen free radicals. obo:GO_0000302 obo:go.owl obo:GO_0000302 response to AOS obo:GO_0000302 response to ROI obo:GO_0000302 response to ROS obo:GO_0000302 response to active oxygen species obo:GO_0000302 response to reactive oxidative species obo:GO_0000302 response to reactive oxygen intermediate obo:GO_0000302 biological_process obo:GO_0000302 GO:0000302 obo:GO_0000302 response to reactive oxygen species obo:GO_0000332 Provision of the template used by reverse transcriptase to synthesize the G-rich strand of telomeric DNA. obo:GO_0000332 obo:go.owl obo:GO_0000332 telomerase RNA obo:GO_0000332 telomerase, template obo:GO_0000332 molecular_function obo:GO_0000332 GO:0000332 obo:GO_0000332 Note that this term describes the activity of an RNA gene product that interacts with other nucleic acid molecules via base pairing; it should not be used to annotate proteins. obo:GO_0000332 template for synthesis of G-rich strand of telomere DNA activity obo:GO_0000339 Interacting selectively and non-covalently with a 7-methylguanosine (m7G) group or derivative located at the 5' end of an RNA molecule. obo:GO_0000339 obo:go.owl obo:GO_0000339 binding to mRNA cap obo:GO_0000339 mRNA cap binding obo:GO_0000339 snRNA cap binding obo:GO_0000339 molecular_function obo:GO_0000339 GO:0000339 obo:GO_0000339 RNA cap binding obo:GO_0000340 Interacting selectively and non-covalently with the 7-methylguanosine group added cotranscriptionally to the 5' end of RNA molecules transcribed by polymerase II. obo:GO_0000340 obo:go.owl obo:GO_0000340 RNA m7G cap binding obo:GO_0000340 molecular_function obo:GO_0000340 GO:0000340 obo:GO_0000340 RNA 7-methylguanosine cap binding obo:GO_0000341 Interacting selectively and non-covalently with the trimethylguanosine (m(3)(2,2,7)-GTP) group located at the 5' end of some RNA molecules. Such trimethylated cap structures, generally produced by posttranscriptional modification of a 7-methylguanosine cap, are often found on snRNAs and snoRNAs transcribed by RNA polymerase II, but have also be found on snRNAs transcribed by RNA polymerase III. They have also been found on a subset of the mRNA population in some species, e.g. C. elegans. obo:GO_0000341 obo:go.owl obo:GO_0000341 RNA m2,2,7G cap binding obo:GO_0000341 molecular_function obo:GO_0000341 GO:0000341 obo:GO_0000341 RNA trimethylguanosine cap binding obo:GO_0000342 Interacting selectively and non-covalently with a hypermethylated cap structure consisting of 7-methylguanosine (m(7)G) followed by four methylated nucleotides (cap 4): 7-methylguanosine-ppp-N6, N6, 2'-O-trimethyladenosine-p-2'-O-methyladenosine-p-2'-O-methylcytosine-p-N3, 2'-O-dimethyluridine Such caps are known to be found at the 5' ends of SL RNAs of trypanosomatid protozoa. obo:GO_0000342 obo:go.owl obo:GO_0000342 molecular_function obo:GO_0000342 GO:0000342 obo:GO_0000342 RNA cap 4 binding obo:GO_0000400 Interacting selectively and non-covalently with DNA containing four-way junctions, also known as Holliday junctions, a structure where two DNA double strands are held together by reciprocal exchange of two of the four strands, one strand each from the two original helices. obo:GO_0000400 obo:go.owl obo:GO_0000400 forked DNA binding obo:GO_0000400 Holliday junction binding obo:GO_0000400 molecular_function obo:GO_0000400 GO:0000400 obo:GO_0000400 four-way junction DNA binding obo:GO_0000401 Interacting selectively and non-covalently with DNA containing the open form of a four-way junction, also known as a Holliday junction, a structure where two DNA double strands are held together by reciprocal exchange of two of the four strands, one strand each from the two original helices. The open form of a four-way junction can be diagrammed without any of the strands crossing over. obo:GO_0000401 obo:go.owl obo:GO_0000401 open form Holliday junction binding obo:GO_0000401 molecular_function obo:GO_0000401 GO:0000401 obo:GO_0000401 open form four-way junction DNA binding obo:GO_0000402 Interacting selectively and non-covalently with DNA containing the crossed form of a four-way junction, also known as a Holliday junction, a structure where two DNA double strands are held together by reciprocal exchange of two of the four strands, one strand each from the two original helices. The crossed form of a four-way junction cannot be diagrammed without any of the strands crossing over, and instead contains a single crossover between two of the strands. obo:GO_0000402 obo:go.owl obo:GO_0000402 crossed form Holliday junction binding obo:GO_0000402 molecular_function obo:GO_0000402 GO:0000402 obo:GO_0000402 crossed form four-way junction DNA binding obo:GO_0000403 Interacting selectively and non-covalently with segment of DNA shaped like a Y. This shape occurs when DNA contains a region of paired double-stranded DNA on one end and a region of unpaired DNA strands on the opposite end. obo:GO_0000403 obo:go.owl obo:GO_0000403 forked DNA binding obo:GO_0000403 splayed Y-form DNA binding obo:GO_0000403 molecular_function obo:GO_0000403 GO:0000403 obo:GO_0000403 Y-form DNA binding obo:GO_0000404 Interacting selectively and non-covalently with DNA containing a loop. A loop occurs when DNA contains a large insertion or deletion that causes a region of unpaired single-stranded DNA to loop out, while the rest of the DNA is in a paired double-stranded configuration. obo:GO_0000404 obo:go.owl obo:GO_0000404 molecular_function obo:GO_0000404 loop DNA binding obo:GO_0000404 GO:0000404 obo:GO_0000404 heteroduplex DNA loop binding obo:GO_0000405 Interacting selectively and non-covalently with DNA that contains a bubble. A bubble occurs when DNA contains a region of unpaired, single-stranded DNA flanked on both sides by regions of paired, double-stranded DNA. obo:GO_0000405 obo:go.owl obo:GO_0000405 molecular_function obo:GO_0000405 GO:0000405 obo:GO_0000405 bubble DNA binding obo:GO_0000406 Interacting selectively and non-covalently with a region of DNA that contains double-stranded DNA flanked by a region of single-stranded DNA. obo:GO_0000406 obo:go.owl obo:GO_0000406 molecular_function obo:GO_0000406 GO:0000406 obo:GO_0000406 double-strand/single-strand DNA junction binding obo:GO_0000497 Interacting selectively and non-covalently with nucleic acid via hydrogen bonds between the bases of a gene product molecule and the bases of a target DNA molecule. obo:GO_0000497 obo:go.owl obo:GO_0000497 molecular_function obo:GO_0000497 base pairing with DNA obo:GO_0000497 GO:0000497 obo:GO_0000497 Note that with respect to annotation, "base pairing" and its child terms are intended to be used to annotate the activity of gene products composed of nucleic acid, presumably RNA, to interact with DNA molecules via base pairing. Internal base pairing with itself is considered part of the secondary structure of the molecule and is not within the scope of GO function. obo:GO_0000497 DNA template activity obo:GO_0000719 The repair of UV-induced T-T, C-T and C-C dimers by directly reversing the damage to restore the original pyrimidines. obo:GO_0000719 obo:go.owl obo:GO_0000719 pyrimidine-dimer repair by photolyase obo:GO_0000719 biological_process obo:GO_0000719 GO:0000719 obo:GO_0000719 photoreactive repair obo:GO_0000720 The repair of UV-induced T-T, C-T, and C-C dimers by the recognition and removal of the damaged DNA strand from the DNA helix as an oligonucleotide. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase. obo:GO_0000720 obo:go.owl obo:GO_0000720 biological_process obo:GO_0000720 GO:0000720 obo:GO_0000720 Note that the repair of pyrimidine dimers by nucleotide excision repair involves the same gene products that are involved in general nucleotide excision repair. Consider also annotating to other children of the biological process term 'nucleotide-excision repair ; GO:0006289'. obo:GO_0000720 pyrimidine dimer repair by nucleotide-excision repair obo:GO_0000724 The error-free repair of a double-strand break in DNA in which the broken DNA molecule is repaired using homologous sequences. A strand in the broken DNA searches for a homologous region in an intact chromosome to serve as the template for DNA synthesis. The restoration of two intact DNA molecules results in the exchange, reciprocal or nonreciprocal, of genetic material between the intact DNA molecule and the broken DNA molecule. obo:GO_0000724 obo:go.owl obo:GO_0000724 GO:0016924 obo:GO_0000724 HDR obo:GO_0000724 HRR obo:GO_0000724 Rad51-dependent recombinational repair obo:GO_0000724 Rhp51-dependent recombinational repair obo:GO_0000724 homologous recombinational repair obo:GO_0000724 homology-directed repair obo:GO_0000724 biological_process obo:GO_0000724 GO:0000724 obo:GO_0000724 double-strand break repair via homologous recombination obo:GO_0000725 A DNA repair process that involves the exchange, reciprocal or nonreciprocal, of genetic material between the broken DNA molecule and a homologous region of DNA. obo:GO_0000725 obo:go.owl obo:GO_0000725 Wikipedia:Recombinational_repair obo:GO_0000725 biological_process obo:GO_0000725 GO:0000725 obo:GO_0000725 recombinational repair obo:GO_0000726 A DNA repair process in which that does not require the exchange of genetic material between the broken DNA molecule and a homologous region of DNA. obo:GO_0000726 obo:go.owl obo:GO_0000726 biological_process obo:GO_0000726 GO:0000726 obo:GO_0000726 non-recombinational repair obo:GO_0000727 The error-free repair of a double-strand break in DNA in which the centromere-proximal end of a broken chromosome searches for a homologous region in an intact chromosome. DNA synthesis initiates from the 3' end of the invading DNA strand, using the intact chromosome as the template, and progresses to the end of the chromosome. obo:GO_0000727 obo:go.owl obo:GO_0000727 biological_process obo:GO_0000727 GO:0000727 obo:GO_0000727 double-strand break repair via break-induced replication obo:GO_0000731 Synthesis of DNA that proceeds from the broken 3' single-strand DNA end and uses the homologous intact duplex as the template. obo:GO_0000731 obo:go.owl obo:GO_0000731 DNA repair synthesis obo:GO_0000731 mitotic DNA repair synthesis obo:GO_0000731 biological_process obo:GO_0000731 DNA synthesis during DNA repair obo:GO_0000731 GO:0000731 obo:GO_0000731 DNA synthesis involved in DNA repair obo:GO_0000772 The activity of binding to and activating specific cell surface receptors, thereby inducing a behavioral or physiological response(s) from a responding organism or cell that leads to the transfer or union of genetic material between organisms or cells. The mating pheromone can either be retained on the cell surface or secreted. obo:GO_0000772 obo:go.owl obo:GO_0000772 molecular_function obo:GO_0000772 GO:0000772 obo:GO_0000772 mating pheromone activity obo:GO_0000774 Stimulates the hydrolysis and exchange of adenyl nucleotides by other proteins. obo:GO_0000774 obo:go.owl obo:GO_0000774 Reactome:R-HSA-5252079 obo:GO_0000774 molecular_function obo:GO_0000774 GO:0000774 obo:GO_0000774 adenyl-nucleotide exchange factor activity obo:GO_0000822 Interacting selectively and non-covalently with inositol hexakisphosphate. obo:GO_0000822 obo:go.owl obo:GO_0000822 IP6 binding obo:GO_0000822 InsP6 binding obo:GO_0000822 molecular_function obo:GO_0000822 GO:0000822 obo:GO_0000822 inositol hexakisphosphate binding obo:GO_0000976 Interacting selectively and non-covalently with a specific sequence of DNA that is part of a regulatory region that controls transcription of that section of the DNA. The transcribed region might be described as a gene, cistron, or operon. obo:GO_0000976 obo:go.owl obo:GO_0000976 kchris obo:GO_0000976 2010-08-10T11:00:02Z obo:GO_0000976 molecular_function obo:GO_0000976 GO:0000976 obo:GO_0000976 The word "promoter" is used variously in the literature to describe the core promoter specifically or the entire proximal regulatory region (excluding any distal enhancers) including both the core promoter and the upstream region where activating transcription factors such as Gal4 in S. cerevisiae or catabolite activator protein (CAP) in E. coli bind. To minimize ambiguity in the use of the word "promoter" in GO, we have chosen the phrase "transcription regulatory region" in order to refer to all of the regulatory regions. Regulatory regions in the DNA which control initiation may include the "core promoter" where the basal transcription machinery binds, the "core promoter proximal region" where regulatory factors other than the basal machinery bind, and "enhancer" regions which are typically more distal from the core promoter. There are also additional regulatory regions, in both the DNA and the RNA transcript, which regulate elongation or termination of transcription. ANNOTATION NOTE: Regarding annotation to "transcription regulatory region DNA binding" (GO:0044212) and any of its is_a children, note that annotation to these terms specifies DNA binding only without any statement about transcription factor activity. To make an annotation about a function of transcription factor activity, consider "sequence-specific DNA-binding transcription factor activity" (GO:0003700) or its is_a children which have has_part relationships to the appropriate kind of "transcription regulatory region DNA binding". obo:GO_0000976 transcription regulatory region sequence-specific DNA binding obo:GO_0000977 Interacting selectively and non-covalently with a specific sequence of DNA that is part of a regulatory region that controls the transcription of a gene or cistron by RNA polymerase II. obo:GO_0000977 obo:go.owl obo:GO_0000977 kchris obo:GO_0000977 2010-08-10T11:05:36Z obo:GO_0000977 molecular_function obo:GO_0000977 GO:0000977 obo:GO_0000977 The word "promoter" is used variously in the literature to describe the core promoter specifically or the entire proximal regulatory region (excluding any distal enhancers) including both the core promoter and the upstream region where activating transcription factors such as Gal4 in S. cerevisiae or catabolite activator protein (CAP) in E. coli bind. To minimize ambiguity in the use of the word "promoter" in GO, we have chosen the phrase "transcription regulatory region" in order to refer to all of the regulatory regions. Regulatory regions in the DNA which control initiation may include the "core promoter" where the basal transcription machinery binds, the "core promoter proximal region" where regulatory factors other than the basal machinery bind, and "enhancer" regions which are typically more distal from the core promoter. There are also additional regulatory regions, in both the DNA and the RNA transcript, which regulate elongation or termination of transcription. ANNOTATION NOTE: Regarding annotation to "transcription regulatory region DNA binding" (GO:0044212) and any of its is_a children, note that annotation to these terms specifies DNA binding only without any statement about transcription factor activity. To make an annotation about a function of transcription factor activity, consider "sequence-specific DNA-binding transcription factor activity" (GO:0003700) or its is_a children which have has_part relationships to the appropriate kind of "transcription regulatory region DNA binding". obo:GO_0000977 RNA polymerase II regulatory region sequence-specific DNA binding obo:GO_0000978 Interacting selectively and non-covalently with a specific upstream regulatory DNA sequence (transcription factor recognition sequence or binding site) located in the proximal promoter of a gene transcribed by RNA polymerase II. The proximal promoter is in cis with and relatively close to the core promoter. obo:GO_0000978 obo:go.owl obo:GO_0000978 kchris obo:GO_0000978 2010-08-10T02:17:19Z obo:GO_0000978 RNA polymerase II core promoter proximal region sequence-specific DNA binding obo:GO_0000978 RNA polymerase II promoter proximal region sequence-specific DNA binding obo:GO_0000978 molecular_function obo:GO_0000978 RNA polymerase II upstream activating sequence (UAS) sequence-specific DNA binding obo:GO_0000978 GO:0000978 obo:GO_0000978 Note that the phrase "upstream activating sequence", or UAS is often used in S. cerevisiae literature to refer to regulatory sequences that occur in the region upstream and proximal to the core promoter. In contrast, in bacteria such as E. coli, the phrase "upstream activating sequence", or UAS is a synonym for "enhancer". obo:GO_0000978 RNA polymerase II proximal promoter sequence-specific DNA binding obo:GO_0000979 Interacting selectively and non-covalently with a DNA sequence that is part of the core promoter of a RNA polymerase II-transcribed gene. obo:GO_0000979 obo:go.owl obo:GO_0000979 kchris obo:GO_0000979 2010-08-10T02:17:28Z obo:GO_0000979 molecular_function obo:GO_0000979 GO:0000979 obo:GO_0000979 RNA polymerase II core promoter sequence-specific DNA binding obo:GO_0000980 Interacting selectively and non-covalently with a RNA polymerase II (Pol II) distal enhancer. In mammalian cells, enhancers are distal sequences that increase the utilization of some promoters, and can function in either orientation and in any location (upstream or downstream) relative to the core promoter. obo:GO_0000980 obo:go.owl obo:GO_0000980 kchris obo:GO_0000980 2010-08-10T02:29:25Z obo:GO_0000980 molecular_function obo:GO_0000980 GO:0000980 obo:GO_0000980 Note that distal enhancers of the type found in mammalian cells are not known to occur in either Saccharomyces cerevisiae or Schizosaccharomyces pombe. While some S. cerevisiae literature does refer to sequences distal to the initiation site, these distal sites do not seem to function independently of position or orientation as mammalian distal enhancers do and are not considered to be enhancers. obo:GO_0000980 RNA polymerase II distal enhancer sequence-specific DNA binding obo:GO_0000984 Interacting selectively and non-covalently with a sequence of DNA that is part of a regulatory region that controls the transcription of a gene or operon by a bacterial-type RNA polymerase. obo:GO_0000984 obo:go.owl obo:GO_0000984 kchris obo:GO_0000984 2010-08-10T02:58:18Z obo:GO_0000984 molecular_function obo:GO_0000984 eubacterial-type RNA polymerase regulatory region sequence-specific DNA binding obo:GO_0000984 GO:0000984 obo:GO_0000984 The word "promoter" is used variously in the literature to describe the core promoter specifically or the entire proximal regulatory region (excluding any distal enhancers) including both the core promoter and the upstream region where activating transcription factors such as Gal4 in S. cerevisiae or catabolite activator protein (CAP) in E. coli bind. To minimize ambiguity in the use of the word "promoter" in GO, we have chosen the phrase "transcription regulatory region" in order to refer to all of the regulatory regions. Regulatory regions in the DNA which control initiation may include the "core promoter" where the basal transcription machinery binds, the "core promoter proximal region" where regulatory factors other than the basal machinery bind, and "enhancer" regions which are typically more distal from the core promoter. There are also additional regulatory regions, in both the DNA and the RNA transcript, which regulate elongation or termination of transcription. ANNOTATION NOTE: Regarding annotation to "transcription regulatory region DNA binding" (GO:0044212) and any of its is_a children, note that annotation to these terms specifies DNA binding only without any statement about transcription factor activity. To make an annotation about a function of transcription factor activity, consider "sequence-specific DNA-binding transcription factor activity" (GO:0003700) or its is_a children which have has_part relationships to the appropriate kind of "transcription regulatory region DNA binding". obo:GO_0000984 bacterial-type RNA polymerase regulatory region sequence-specific DNA binding obo:GO_0000985 Interacting selectively and non-covalently with a DNA sequence that is part of the core promoter of a bacterial gene. obo:GO_0000985 obo:go.owl obo:GO_0000985 kchris obo:GO_0000985 2010-08-10T03:01:38Z obo:GO_0000985 eubacterial-type RNA polymerase core promoter sequence-specific DNA binding obo:GO_0000985 molecular_function obo:GO_0000985 GO:0000985 obo:GO_0000985 bacterial-type RNA polymerase core promoter sequence-specific DNA binding obo:GO_0000986 Interacting selectively and non-covalently with a specific upstream regulatory DNA sequence (transcription factor recognition sequence or binding site) located in the proximal promoter of a bacterial gene (or cistron, or operon). The proximal promoter is in cis with and relatively close to the core promoter. obo:GO_0000986 obo:go.owl obo:GO_0000986 kchris obo:GO_0000986 2010-08-10T03:02:31Z obo:GO_0000986 bacterial-type RNA polymerase core promoter proximal region sequence-specific DNA binding obo:GO_0000986 eubacterial-type RNA polymerase regulatory transcription factor sequence-specific DNA binding obo:GO_0000986 molecular_function obo:GO_0000986 GO:0000986 obo:GO_0000986 bacterial-type proximal promoter sequence-specific DNA binding obo:GO_0000987 Interacting selectively and non-covalently with a specific upstream regulatory DNA sequence (transcription factor recognition sequence or binding site) located in the proximal promoter. The proximal promoter is in cis with and relatively close to the core promoter. obo:GO_0000987 obo:go.owl obo:GO_0000987 kchris obo:GO_0000987 2010-08-10T03:40:16Z obo:GO_0000987 GO:0001159 obo:GO_0000987 core promoter proximal region sequence-specific DNA binding obo:GO_0000987 promoter proximal region sequence-specific DNA binding obo:GO_0000987 molecular_function obo:GO_0000987 core promoter proximal region DNA binding obo:GO_0000987 GO:0000987 obo:GO_0000987 The word "promoter" is used variously in the literature to describe the core promoter specifically or the entire proximal regulatory region (excluding any distal enhancers) including both the core promoter and the upstream region where activating transcription factors such as Gal4 in S. cerevisiae or catabolite activator protein (CAP) in E. coli bind. To minimize ambiguity in the use of the word "promoter" in GO, we have chosen the phrase "transcription regulatory region" in order to refer to all of the regulatory regions. Regulatory regions in the DNA which control initiation may include the "core promoter" where the basal transcription machinery binds, the "core promoter proximal region" where regulatory factors other than the basal machinery bind, and "enhancer" regions which are typically more distal from the core promoter. There are also additional regulatory regions, in both the DNA and the RNA transcript, which regulate elongation or termination of transcription. ANNOTATION NOTE: Regarding annotation to "transcription regulatory region DNA binding" (GO:0044212) and any of its is_a children, note that annotation to these terms specifies DNA binding only without any statement about transcription factor activity. To make an annotation about a function of transcription factor activity, consider "sequence-specific DNA-binding transcription factor activity" (GO:0003700) or its is_a children which have has_part relationships to the appropriate kind of "transcription regulatory region DNA binding". obo:GO_0000987 proximal promoter sequence-specific DNA binding obo:GO_0000992 Interacting selectively and non-covalently with a sequence of DNA that is part of a regulatory region that controls transcription by RNA polymerase III. The transcribed region might be contain a single gene or a cistron containing multiple genes. obo:GO_0000992 obo:go.owl obo:GO_0000992 kchris obo:GO_0000992 2010-08-11T03:49:28Z obo:GO_0000992 molecular_function obo:GO_0000992 GO:0000992 obo:GO_0000992 The word "promoter" is used variously in the literature to describe the core promoter specifically or the entire proximal regulatory region (excluding any distal enhancers) including both the core promoter and the upstream region where activating transcription factors such as Gal4 in S. cerevisiae or catabolite activator protein (CAP) in E. coli bind. To minimize ambiguity in the use of the word "promoter" in GO, we have chosen the phrase "transcription regulatory region" in order to refer to all of the regulatory regions. Regulatory regions in the DNA which control initiation may include the "core promoter" where the basal transcription machinery binds, the "core promoter proximal region" where regulatory factors other than the basal machinery bind, and "enhancer" regions which are typically more distal from the core promoter. There are also additional regulatory regions, in both the DNA and the RNA transcript, which regulate elongation or termination of transcription. ANNOTATION NOTE: Regarding annotation to "transcription regulatory region DNA binding" (GO:0044212) and any of its is_a children, note that annotation to these terms specifies DNA binding only without any statement about transcription factor activity. To make an annotation about a function of transcription factor activity, consider "sequence-specific DNA-binding transcription factor activity" (GO:0003700) or its is_a children which have has_part relationships to the appropriate kind of "transcription regulatory region DNA binding". obo:GO_0000992 polymerase III regulatory region sequence-specific DNA binding obo:GO_0000993 Interacting selectively and non-covalently with RNA polymerase II core enzyme, a multisubunit eukaryotic nuclear RNA polymerase typically composed of twelve subunits. obo:GO_0000993 obo:go.owl obo:GO_0000993 kchris obo:GO_0000993 2010-08-11T03:57:27Z obo:GO_0000993 RNA polymerase II core binding obo:GO_0000993 RNAP II core binding obo:GO_0000993 molecular_function obo:GO_0000993 GO:0000993 obo:GO_0000993 RNA polymerase II complex binding obo:GO_0000994 Interacting selectively and non-covalently with RNA polymerase III core enzyme, a multisubunit eukaryotic nuclear RNA polymerase typically composed of seventeen subunits. obo:GO_0000994 obo:go.owl obo:GO_0000994 kchris obo:GO_0000994 2010-08-11T03:58:58Z obo:GO_0000994 molecular_function obo:GO_0000994 GO:0000994 obo:GO_0000994 RNA polymerase III core binding obo:GO_0001000 Interacting selectively and non-covalently with the bacterial-type RNA polymerase core enzyme, typically consisting of two alpha, one beta, one beta prime, and one omega subunit. obo:GO_0001000 obo:go.owl obo:GO_0001000 kchris obo:GO_0001000 2010-08-17T04:59:00Z obo:GO_0001000 eubacterial-type RNA polymerase core enzyme binding obo:GO_0001000 molecular_function obo:GO_0001000 GO:0001000 obo:GO_0001000 Should omega be included here? obo:GO_0001000 bacterial-type RNA polymerase core enzyme binding obo:GO_0001001 Interacting selectively and non-covalently with a single subunit mitochondrial RNA polymerase enzyme, which is composed of a single catalytic subunit similar to the RNA polymerase enzymes from phages T3, T7, and SP6. obo:GO_0001001 obo:go.owl obo:GO_0001001 kchris obo:GO_0001001 2010-08-17T05:01:28Z obo:GO_0001001 molecular_function obo:GO_0001001 GO:0001001 obo:GO_0001001 mitochondrial single-subunit type RNA polymerase binding obo:GO_0001002 Interacting selectively and non-covalently with a sequence of DNA that is a part of a type 1 promoter that controls transcription by RNA polymerase III. Type 1 promoters are found in 5S rRNA genes, downstream of the transcription start site within the sequence of the mature RNA, and require TFIIIA for recognition. obo:GO_0001002 obo:go.owl obo:GO_0001002 kchris obo:GO_0001002 2010-08-18T05:38:20Z obo:GO_0001002 molecular_function obo:GO_0001002 GO:0001002 obo:GO_0001002 RNA polymerase III type 1 promoter sequence-specific DNA binding obo:GO_0001003 Interacting selectively and non-covalently with a sequence of DNA that is a part of a type 2 promoter that controls transcription by RNA polymerase III. Type 2 promoters consist of an A box and a B box downstream of the transcription start site within the sequence within the sequence of the mature RNA. Type 2 promoters are found in many tRNA genes as well as in other small RNAs. obo:GO_0001003 obo:go.owl obo:GO_0001003 kchris obo:GO_0001003 2010-08-18T05:51:18Z obo:GO_0001003 molecular_function obo:GO_0001003 GO:0001003 obo:GO_0001003 RNA polymerase III type 2 promoter sequence-specific DNA binding obo:GO_0001004 Initiating the assembly of the RNA polymerase III pre-initiation complex by binding to a control sequence in the intragenic region. This allows to recruit TFIIIB to the DNA at a site centered approximately 26 base pairs upstream of the start site of transcription. For tRNA genes, TFIIIC first associates with DNA, and then recruits TFIIIB. For 5S rRNA genes, TFIIIA binds to DNA first, followed by TFIIIC, which then recruits TFIIIB. obo:GO_0001004 obo:go.owl obo:GO_0001004 kchris obo:GO_0001004 2010-08-18T05:53:32Z obo:GO_0001004 GO:0001005 obo:GO_0001004 GO:0001008 obo:GO_0001004 GO:0001033 obo:GO_0001004 GO:0001038 obo:GO_0001004 GO:0001157 obo:GO_0001004 RNA polymerase III transcription factor recruiting activity obo:GO_0001004 transcription factor activity, RNA polymerase III promoter sequence-specific binding, TFIIIB recruiting obo:GO_0001004 RNA polymerase III hybrid type promoter TFIIIB recruiting transcription factor activity obo:GO_0001004 RNA polymerase III promoter sequence-specific DNA binding TFIIIB recruiting transcription factor activity obo:GO_0001004 RNA polymerase III type 1 promoter sequence-specific DNA binding TFIIIB recruiting transcription factor activity obo:GO_0001004 RNA polymerase III type 2 promoter sequence-specific DNA binding TFIIIB recruiting transcription factor activity obo:GO_0001004 RNA polymerase III type 3 promoter TFIIIB recruiting transcription factor activity obo:GO_0001004 transcription factor activity, RNA polymerase III type 1 promoter sequence-specific binding, TFIIIB recruiting obo:GO_0001004 transcription factor activity, RNA polymerase III type 2 promoter sequence-specific binding, TFIIIB recruiting obo:GO_0001004 transcription factor activity, RNA polymerase III type 3 promoter TFIIIB recruiting obo:GO_0001004 type 2 RNA polymerase III promoter recognition obo:GO_0001004 type 3 RNA polymerase III promoter recognition obo:GO_0001004 molecular_function obo:GO_0001004 RNA polymerase III assembly factor activity obo:GO_0001004 RNA polymerase III assembly factor activity, TFIIIB recruiting obo:GO_0001004 SNAPc-type activity obo:GO_0001004 TFIIIA activity obo:GO_0001004 TFIIIC-type activity obo:GO_0001004 transcription factor activity, RNA polymerase III type 1 promoter TFIIIB obo:GO_0001004 GO:0001004 obo:GO_0001004 Merged terms as in https://github.com/geneontology/go-ontology/issues/14852 obo:GO_0001004 RNA polymerase III transcription regulator recruiting activity obo:GO_0001006 Interacting selectively and non-covalently with a sequence of DNA that is a part of a type 3 promoter that controls transcription by RNA polymerase III (Pol III). A type 3 Pol III promoter is composed of elements upstream of the transcription start site, including a TATA box. The human U6 snRNA gene has a type 3 promoter. Type 3 Pol III promoters have not been observed in S. cerevisiae. obo:GO_0001006 obo:go.owl obo:GO_0001006 kchris obo:GO_0001006 2010-08-18T06:02:26Z obo:GO_0001006 molecular_function obo:GO_0001006 GO:0001006 obo:GO_0001006 RNA polymerase III type 3 promoter sequence-specific DNA binding obo:GO_0001010 The function of binding to a specific DNA sequence and recruiting another transcription factor to the DNA in order to modulate transcription. The recruited factor may bind DNA directly, or may be colocalized via protein-protein interactions. obo:GO_0001010 obo:go.owl obo:GO_0001010 kchris obo:GO_0001010 2010-08-18T06:46:33Z obo:GO_0001010 sequence-specific DNA binding transcription factor recruiting transcription factor activity obo:GO_0001010 transcription factor activity, sequence-specific DNA binding transcription factor recruiting obo:GO_0001010 molecular_function obo:GO_0001010 transcription factor activity, sequence-specific DNA-binding transcription factor recruiting obo:GO_0001010 GO:0001010 obo:GO_0001010 RNA polymerase II sequence-specific DNA-binding transcription factor recruiting activity obo:GO_0001012 Interacting selectively and non-covalently with a DNA region that controls the transcription of a region of DNA by RNA polymerase II. Binding may occur as a sequence specific interaction or as an interaction observed only once a factor has been recruited to the DNA by other factors. obo:GO_0001012 obo:go.owl obo:GO_0001012 kchris obo:GO_0001012 2010-08-19T09:43:58Z obo:GO_0001012 molecular_function obo:GO_0001012 GO:0001012 obo:GO_0001012 RNA polymerase II regulatory region DNA binding obo:GO_0001013 Interacting selectively and non-covalently with a DNA region that controls the transcription of a region of DNA by RNA polymerase I. Binding may occur as a sequence specific interaction or as an interaction observed only once a factor has been recruited to the DNA by other factors. obo:GO_0001013 obo:go.owl obo:GO_0001013 kchris obo:GO_0001013 2010-08-19T09:44:02Z obo:GO_0001013 molecular_function obo:GO_0001013 GO:0001013 obo:GO_0001013 RNA polymerase I regulatory region DNA binding obo:GO_0001016 Interacting selectively and non-covalently with a DNA region that controls the transcription of a gene by RNA polymerase III. Binding may occur as a sequence specific interaction or as an interaction observed only once a factor has been recruited to the DNA by other factors. obo:GO_0001016 obo:go.owl obo:GO_0001016 kchris obo:GO_0001016 2010-08-19T09:36:17Z obo:GO_0001016 molecular_function obo:GO_0001016 GO:0001016 obo:GO_0001016 RNA polymerase III regulatory region DNA binding obo:GO_0001017 Interacting selectively and non-covalently with a DNA region that controls the transcription of a gene or operon by a bacterial-type RNA polymerase. Binding may occur as a sequence specific interaction or as an interaction observed only once a factor has been recruited to the DNA by other factors. obo:GO_0001017 obo:go.owl obo:GO_0001017 kchris obo:GO_0001017 2010-08-19T09:45:42Z obo:GO_0001017 eubacterial-type RNA polymerase regulatory region DNA binding obo:GO_0001017 molecular_function obo:GO_0001017 GO:0001017 obo:GO_0001017 bacterial-type RNA polymerase regulatory region DNA binding obo:GO_0001018 Interacting selectively and non-covalently with a DNA region that controls the transcription of the mitochondrial DNA. obo:GO_0001018 obo:go.owl obo:GO_0001018 kchris obo:GO_0001018 2010-08-25T04:11:49Z obo:GO_0001018 GO:0000997 obo:GO_0001018 GO:0001044 obo:GO_0001018 GO:0001045 obo:GO_0001018 GO:0070361 obo:GO_0001018 GO:0070362 obo:GO_0001018 GO:0070363 obo:GO_0001018 GO:0070364 obo:GO_0001018 HSP coding strand binding obo:GO_0001018 HSP non-coding strand binding obo:GO_0001018 HSPas binding obo:GO_0001018 HSPs binding obo:GO_0001018 LSP coding strand binding obo:GO_0001018 LSP non-coding strand binding obo:GO_0001018 LSPas binding obo:GO_0001018 LSPs binding obo:GO_0001018 mitochondrial heavy strand promoter anti-sense binding obo:GO_0001018 mitochondrial heavy strand promoter sense binding obo:GO_0001018 mitochondrial light strand promoter anti-sense binding obo:GO_0001018 mitochondrial light strand promoter sense binding obo:GO_0001018 molecular_function obo:GO_0001018 mitochondrial RNA polymerase core promoter proximal region sequence-specific DNA binding obo:GO_0001018 mitochondrial RNA polymerase core promoter sequence-specific DNA binding obo:GO_0001018 mitochondrial RNA polymerase regulatory region DNA binding obo:GO_0001018 mitochondrial RNA polymerase regulatory region sequence-specific DNA binding obo:GO_0001018 mitochondrial proximal promoter sequence-specific DNA binding obo:GO_0001018 GO:0001018 obo:GO_0001018 mitochondrial promoter sequence-specific DNA binding obo:GO_0001019 Interacting selectively and non-covalently with a DNA region that controls the transcription of a region of DNA by a plastid RNA polymerase. Binding may occur as a sequence specific interaction or as an interaction observed only once a factor has been recruited to the DNA by other factors. obo:GO_0001019 obo:go.owl obo:GO_0001019 kchris obo:GO_0001019 2010-08-19T09:46:27Z obo:GO_0001019 molecular_function obo:GO_0001019 GO:0001019 obo:GO_0001019 plastid RNA polymerase regulatory region DNA binding obo:GO_0001025 Interacting selectively and non-covalently with an RNA polymerase III transcription factor, any protein required to initiate or regulate transcription by RNA polymerase III. obo:GO_0001025 obo:go.owl obo:GO_0001025 kchris obo:GO_0001025 2010-08-20T03:26:50Z obo:GO_0001025 RNA polymerase III transcription factor binding obo:GO_0001025 molecular_function obo:GO_0001025 GO:0001025 obo:GO_0001025 RNA polymerase III general transcription initiation factor binding obo:GO_0001030 Interacting selectively and non-covalently with a region of DNA that is a part of a type 1 promoter that controls transcription by RNA polymerase III. Type 1 promoters are found in 5S rRNA genes, downstream of the transcription start site within the sequence of the mature RNA, and require TFIIIA for recognition. obo:GO_0001030 obo:go.owl obo:GO_0001030 kchris obo:GO_0001030 2010-08-23T12:58:54Z obo:GO_0001030 molecular_function obo:GO_0001030 GO:0001030 obo:GO_0001030 RNA polymerase III type 1 promoter DNA binding obo:GO_0001031 Interacting selectively and non-covalently with a region of DNA that is a part of a type 2 promoter that controls transcription by RNA polymerase III. Type 2 promoters consist of an A box and a B box downstream of the transcription start site within the sequence within the sequence of the mature RNA. Type 2 promoters are found in many tRNA genes as well as in other small RNAs. obo:GO_0001031 obo:go.owl obo:GO_0001031 kchris obo:GO_0001031 2010-08-23T01:14:56Z obo:GO_0001031 molecular_function obo:GO_0001031 GO:0001031 obo:GO_0001031 RNA polymerase III type 2 promoter DNA binding obo:GO_0001032 Interacting selectively and non-covalently with a region of DNA that is a part of a type 3 promoter that controls transcription by RNA polymerase III. A type 3 Pol III promoter is composed of elements upstream of the transcription start site, including a TATA box. The human U6 snRNA gene has a type 3 promoter. Type 3 Pol III promoters have not been observed in S. cerevisiae. obo:GO_0001032 obo:go.owl obo:GO_0001032 kchris obo:GO_0001032 2010-08-23T01:15:14Z obo:GO_0001032 molecular_function obo:GO_0001032 GO:0001032 obo:GO_0001032 RNA polymerase III type 3 promoter DNA binding obo:GO_0001037 Interacting selectively and non-covalently with a region of DNA that is a part of a hybrid promoter that controls transcription by RNA polymerase III (Pol III). A hybrid Pol III promoter contains both regulatory elements both upstream and downstream of the transcription initiation site. An example gene with such a promoter is the S. cerevisiae U6 gene. obo:GO_0001037 obo:go.owl obo:GO_0001037 kchris obo:GO_0001037 2010-08-24T02:51:34Z obo:GO_0001037 molecular_function obo:GO_0001037 GO:0001037 obo:GO_0001037 RNA polymerase III hybrid type promoter DNA binding obo:GO_0001039 Interacting selectively and non-covalently with a sequence of DNA that is a part of a hybrid type promoter that controls transcription by RNA polymerase III (Pol III). A hybrid Pol III promoter contains both regulatory elements both upstream and downstream of the transcription initiation site. An example gene with such a promoter is the S. cerevisiae U6 gene. obo:GO_0001039 obo:go.owl obo:GO_0001039 kchris obo:GO_0001039 2010-08-23T06:21:24Z obo:GO_0001039 molecular_function obo:GO_0001039 GO:0001039 obo:GO_0001039 RNA polymerase III hybrid type promoter sequence-specific DNA binding obo:GO_0001042 Interacting selectively and non-covalently with RNA polymerase I core enzyme, a multisubunit eukaryotic nuclear RNA polymerase typically composed of seventeen subunits. obo:GO_0001042 obo:go.owl obo:GO_0001042 kchris obo:GO_0001042 2010-09-23T01:39:23Z obo:GO_0001042 molecular_function obo:GO_0001042 GO:0001042 obo:GO_0001042 RNA polymerase I core binding obo:GO_0001046 Interacting selectively and non-covalently with a sequence of DNA that is part of a core promoter region. The core promoter is composed of the transcription start site and binding sites for the RNA polymerase and the basal transcription machinery. The transcribed region might be described as a gene, cistron, or operon. obo:GO_0001046 obo:go.owl obo:GO_0001046 kchris obo:GO_0001046 2010-08-25T04:17:44Z obo:GO_0001046 molecular_function obo:GO_0001046 GO:0001046 obo:GO_0001046 The word "promoter" is used variously in the literature to describe the core promoter specifically or the entire proximal regulatory region (excluding any distal enhancers) including both the core promoter and the upstream region where activating transcription factors such as Gal4 in S. cerevisiae or catabolite activator protein (CAP) in E. coli bind. To minimize ambiguity in the use of the word "promoter" in GO, we have chosen the phrase "transcription regulatory region" in order to refer to all of the regulatory regions. Regulatory regions in the DNA which control initiation may include the "core promoter" where the basal transcription machinery binds, the "core promoter proximal region" where regulatory factors other than the basal machinery bind, and "enhancer" regions which are typically more distal from the core promoter. There are also additional regulatory regions, in both the DNA and the RNA transcript, which regulate elongation or termination of transcription. ANNOTATION NOTE: Regarding annotation to "transcription regulatory region DNA binding" (GO:0044212) and any of its is_a children, note that annotation to these terms specifies DNA binding only without any statement about transcription factor activity. To make an annotation about a function of transcription factor activity, consider "sequence-specific DNA-binding transcription factor activity" (GO:0003700) or its is_a children which have has_part relationships to the appropriate kind of "transcription regulatory region DNA binding". obo:GO_0001046 core promoter sequence-specific DNA binding obo:GO_0001047 Interacting selectively and non-covalently with the regulatory region composed of the transcription start site and binding sites for the basal transcription machinery. Binding may occur as a sequence specific interaction or as an interaction observed only once a factor has been recruited to the DNA by other factors. obo:GO_0001047 obo:go.owl obo:GO_0001047 kchris obo:GO_0001047 2010-08-27T03:00:52Z obo:GO_0001047 molecular_function obo:GO_0001047 GO:0001047 obo:GO_0001047 core promoter binding obo:GO_0001048 Interacting selectively and non-covalently with RNA polymerase IV core enzyme, a multisubunit eukaryotic nuclear RNA polymerase found in plants and involved in siRNA production. obo:GO_0001048 obo:go.owl obo:GO_0001048 kchris obo:GO_0001048 2010-09-23T01:41:03Z obo:GO_0001048 molecular_function obo:GO_0001048 GO:0001048 obo:GO_0001048 RNA polymerase IV core binding obo:GO_0001049 Interacting selectively and non-covalently with RNA polymerase V core enzyme, a multisubunit eukaryotic nuclear RNA polymerase found in plants and involved in production of noncoding transcripts at target loci for silencing. obo:GO_0001049 obo:go.owl obo:GO_0001049 kchris obo:GO_0001049 2010-09-23T01:41:08Z obo:GO_0001049 molecular_function obo:GO_0001049 GO:0001049 obo:GO_0001049 RNA polymerase V core binding obo:GO_0001050 Interacting selectively and non-covalently with a single subunit RNA polymerase enzyme, which is composed of a single catalytic subunit similar to the RNA polymerase enzymes from phages T3, T7, and SP6. obo:GO_0001050 obo:go.owl obo:GO_0001050 kchris obo:GO_0001050 2010-09-23T02:33:45Z obo:GO_0001050 SP6-type RNA polymerase binding obo:GO_0001050 T3-type RNA polymerase binding obo:GO_0001050 T3/T7 type RNA polymerase binding obo:GO_0001050 T7-type RNA polymerase binding obo:GO_0001050 molecular_function obo:GO_0001050 GO:0001050 obo:GO_0001050 single-subunit type RNA polymerase binding obo:GO_0001051 Interacting selectively and non-covalently with a single subunit plastid RNA polymerase enzyme, which is composed of a single catalytic subunit similar to the RNA polymerase enzymes from phages T3, T7, and SP6. obo:GO_0001051 obo:go.owl obo:GO_0001051 kchris obo:GO_0001051 2010-09-23T02:42:57Z obo:GO_0001051 molecular_function obo:GO_0001051 GO:0001051 obo:GO_0001051 plastid single-subunit type RNA polymerase binding obo:GO_0001052 Interacting selectively and non-covalently with the bacterial-type plastid PEP RNA polymerase core enzyme, typically consisting of two alpha, one beta, one beta prime, and one double prime subunit. obo:GO_0001052 obo:go.owl obo:GO_0001052 kchris obo:GO_0001052 2010-09-23T02:49:31Z obo:GO_0001052 molecular_function obo:GO_0001052 GO:0001052 obo:GO_0001052 plastid PEP RNA polymerase core enzyme binding obo:GO_0001067 Interacting selectively and non-covalently with a nucleic acid region that regulates a nucleic acid-based process. Such processes include transcription, DNA replication, and DNA repair. obo:GO_0001067 obo:go.owl obo:GO_0001067 kchris obo:GO_0001067 2010-10-21T04:08:56Z obo:GO_0001067 molecular_function obo:GO_0001067 GO:0001067 obo:GO_0001067 regulatory region nucleic acid binding obo:GO_0001068 Interacting selectively and non-covalently with a RNA region within the transcript that regulates the transcription of a region of DNA, which may be a gene, cistron, or operon. obo:GO_0001068 obo:go.owl obo:GO_0001068 kchris obo:GO_0001068 2010-10-21T04:15:32Z obo:GO_0001068 molecular_function obo:GO_0001068 GO:0001068 obo:GO_0001068 transcription regulatory region RNA binding obo:GO_0001069 Interacting selectively and non-covalently with a RNA region that regulates a nucleic acid-based process. Such processes include transcription, DNA replication, and DNA repair. obo:GO_0001069 obo:go.owl obo:GO_0001069 kchris obo:GO_0001069 2010-10-21T04:17:01Z obo:GO_0001069 molecular_function obo:GO_0001069 GO:0001069 obo:GO_0001069 regulatory region RNA binding obo:GO_0001085 Interacting selectively and non-covalently with an RNA polymerase II transcription factor, any protein required to initiate or regulate transcription by RNA polymerase II. obo:GO_0001085 obo:go.owl obo:GO_0001085 kchris obo:GO_0001085 2010-10-28T02:08:59Z obo:GO_0001085 molecular_function obo:GO_0001085 GO:0001085 obo:GO_0001085 RNA polymerase II transcription factor binding obo:GO_0001091 Interacting selectively and non-covalently with a basal RNA polymerase II transcription factor, any of the factors involved in formation of the preinitiation complex (PIC) by RNA polymerase II and defined as a basal or general transcription factor. obo:GO_0001091 obo:go.owl obo:GO_0001091 kchris obo:GO_0001091 2010-10-28T02:30:02Z obo:GO_0001091 RNA polymerase II basal transcription factor binding obo:GO_0001091 molecular_function obo:GO_0001091 GO:0001091 obo:GO_0001091 RNA polymerase II general transcription initiation factor binding obo:GO_0001092 Interacting selectively and non-covalently with a general RNA polymerase II transcription factor belonging to the TFIIA complex, one of the complexes involved in formation of the preinitiation complex (PIC) by RNA polymerase II and defined as a basal or general transcription factor. obo:GO_0001092 obo:go.owl obo:GO_0001092 kchris obo:GO_0001092 2010-10-28T02:37:19Z obo:GO_0001092 TFIIA-class transcription factor binding obo:GO_0001092 molecular_function obo:GO_0001092 GO:0001092 obo:GO_0001092 TFIIA-class transcription factor complex binding obo:GO_0001093 Interacting selectively and non-covalently with a general RNA polymerase II transcription factor of the TFIIB class, one of the factors involved in formation of the preinitiation complex (PIC) by RNA polymerase II. obo:GO_0001093 obo:go.owl obo:GO_0001093 kchris obo:GO_0001093 2010-10-28T02:46:15Z obo:GO_0001093 molecular_function obo:GO_0001093 GO:0001093 obo:GO_0001093 TFIIB-class transcription factor binding obo:GO_0001094 Interacting selectively and non-covalently with a general RNA polymerase II transcription factor belonging to the TFIID complex, one of the factors involved in formation of the preinitiation complex (PIC) by RNA polymerase II. obo:GO_0001094 obo:go.owl obo:GO_0001094 kchris obo:GO_0001094 2010-10-28T02:48:33Z obo:GO_0001094 TFIID-class transcription factor binding obo:GO_0001094 molecular_function obo:GO_0001094 GO:0001094 obo:GO_0001094 TFIID-class transcription factor complex binding obo:GO_0001095 Interacting selectively and non-covalently with a general RNA polymerase II transcription factor belonging to the TFIIE complex, one of the factors involved in formation of the preinitiation complex (PIC) by RNA polymerase II. obo:GO_0001095 obo:go.owl obo:GO_0001095 kchris obo:GO_0001095 2010-10-28T02:49:20Z obo:GO_0001095 TFIIE-class transcription factor binding obo:GO_0001095 molecular_function obo:GO_0001095 GO:0001095 obo:GO_0001095 TFIIE-class transcription factor complex binding obo:GO_0001096 Interacting selectively and non-covalently with a general RNA polymerase II transcription factor belonging to the TFIIF complex, one of the factors involved in formation of the preinitiation complex (PIC) by RNA polymerase II. obo:GO_0001096 obo:go.owl obo:GO_0001096 kchris obo:GO_0001096 2010-10-28T02:51:20Z obo:GO_0001096 TFIIF-class transcription factor binding obo:GO_0001096 molecular_function obo:GO_0001096 GO:0001096 obo:GO_0001096 TFIIF-class transcription factor complex binding obo:GO_0001097 Interacting selectively and non-covalently with a general RNA polymerase II transcription factor belonging to the TFIIH complex, one of the factors involved in formation of the preinitiation complex (PIC) by RNA polymerase II. obo:GO_0001097 obo:go.owl obo:GO_0001097 kchris obo:GO_0001097 2010-10-28T02:51:41Z obo:GO_0001097 TFIIH-class transcription factor binding obo:GO_0001097 molecular_function obo:GO_0001097 GO:0001097 obo:GO_0001097 TFIIH-class transcription factor complex binding obo:GO_0001098 Interacting selectively and non-covalently with the basal transcription machinery which is composed of the RNA polymerase core enzyme and the basal transcription factor(s), the minimal set of factors required for formation of the preinitiation complex (PIC) by the RNA polymerase. obo:GO_0001098 obo:go.owl obo:GO_0001098 kchris obo:GO_0001098 2010-11-24T12:50:49Z obo:GO_0001098 molecular_function obo:GO_0001098 GO:0001098 obo:GO_0001098 Note that the definition of basal, or general, transcription factors has typically been done at a small number of well characterized activator-independent promoters. At an activator-dependent promoter, one or more additional factors are generally required in addition to the basal factors. obo:GO_0001098 basal transcription machinery binding obo:GO_0001099 Interacting selectively and non-covalently with the basal transcription machinery for RNA polymerase II which is composed of the RNA polymerase II core enzyme, a multisubunit eukaryotic nuclear RNA polymerase typically composed of twelve subunits, and the basal RNA polymerase II transcription factors, the minimal set of factors required for formation of the preinitiation complex (PIC) by the RNA polymerase. obo:GO_0001099 obo:go.owl obo:GO_0001099 kchris obo:GO_0001099 2010-11-24T12:54:33Z obo:GO_0001099 basal RNAP II transcription machinery binding obo:GO_0001099 molecular_function obo:GO_0001099 GO:0001099 obo:GO_0001099 Note that the definition of basal, or general, transcription factors has typically been done at a small number of well characterized activator-independent promoters. At an activator-dependent promoter, one or more additional factors are generally required in addition to the basal factors. obo:GO_0001099 basal RNA polymerase II transcription machinery binding obo:GO_0001102 Interacting selectively and non-covalently with an RNA polymerase II transcription activating factor, a protein involved in positive regulation of transcription. obo:GO_0001102 obo:go.owl obo:GO_0001102 kchris obo:GO_0001102 2010-11-24T02:17:08Z obo:GO_0001102 molecular_function obo:GO_0001102 GO:0001102 obo:GO_0001102 RNA polymerase II activating transcription factor binding obo:GO_0001103 Interacting selectively and non-covalently with an RNA polymerase II transcription repressing factor, a protein involved in negative regulation of transcription. obo:GO_0001103 obo:go.owl obo:GO_0001103 kchris obo:GO_0001103 2010-11-24T02:34:55Z obo:GO_0001103 molecular_function obo:GO_0001103 GO:0001103 obo:GO_0001103 RNA polymerase II repressing transcription factor binding obo:GO_0001108 Interacting selectively and non-covalently with the basal transcription machinery which is composed of a bacterial-type RNA polymerase core enzyme and a sigma factor, the minimal set of factors required for formation of the preinitiation complex (PIC) by a bacterial-type RNA polymerase. obo:GO_0001108 obo:go.owl obo:GO_0001108 kchris obo:GO_0001108 2010-11-30T04:26:04Z obo:GO_0001108 basal bacterial-type RNA polymerase transcription machinery binding obo:GO_0001108 molecular_function obo:GO_0001108 GO:0001108 obo:GO_0001108 bacterial-type RNA polymerase holo enzyme binding obo:GO_0001134 The function of binding to an RNA polymerase (RNAP) transcription regulator and recruiting it to the general transcription machinery complex in order to modulate transcription initiation. obo:GO_0001134 obo:go.owl obo:GO_0001134 kchris obo:GO_0001134 2011-01-20T04:57:59Z obo:GO_0001134 transcription factor recruiting activity obo:GO_0001134 transcription factor recruiting transcription factor activity obo:GO_0001134 molecular_function obo:GO_0001134 transcription factor activity, transcription factor recruiting obo:GO_0001134 GO:0001134 obo:GO_0001134 Changed subclasses https://github.com/geneontology/go-ontology/issues/15577 obo:GO_0001134 transcription regulator recruiting activity obo:GO_0001135 The function of binding to an RNA polymerase II (RNAP II) transcription regulator and recruiting it to the general transcription machinery complex in order to modulate transcription initiation. obo:GO_0001135 obo:go.owl obo:GO_0001135 kchris obo:GO_0001135 2011-01-20T05:13:12Z obo:GO_0001135 GO:0001136 obo:GO_0001135 GO:0001137 obo:GO_0001135 GO:0001138 obo:GO_0001135 RNA polymerase II transcription factor recruiting activity obo:GO_0001135 RNA polymerase II transcription factor recruiting transcription factor activity obo:GO_0001135 TFIIE-class transcription factor recruiting transcription factor activity obo:GO_0001135 TFIIF-class transcription factor recruiting transcription factor activity obo:GO_0001135 TFIIH-class transcription factor recruiting transcription factor activity obo:GO_0001135 transcription factor activity, TFIIE-class transcription factor recruiting obo:GO_0001135 transcription factor activity, TFIIF-class transcription factor recruiting obo:GO_0001135 transcription factor activity, TFIIH-class transcription factor recruiting obo:GO_0001135 molecular_function obo:GO_0001135 transcription factor activity, RNA polymerase II transcription factor recruiting obo:GO_0001135 GO:0001135 obo:GO_0001135 Merged terms see https://github.com/geneontology/go-ontology/issues/15795 obo:GO_0001135 RNA polymerase II transcription regulator recruiting activity obo:GO_0001139 Interacting selectively and non-covalently with an RNA polymerase II (Pol II) complex, typically composed of twelve subunits, and with another protein, macromolecule, or complex, permitting those molecules to function in a coordinated way in order to facilitate the aggregation, arrangement and bonding together of proteins on an RNA polymerase II promoter DNA to form the transcriptional preinitiation complex (PIC), the formation of which is a prerequisite for transcription by RNA polymerase. obo:GO_0001139 obo:go.owl obo:GO_0001139 kchris obo:GO_0001139 2011-01-20T05:55:01Z obo:GO_0001139 core RNA polymerase II recruiting transcription factor activity obo:GO_0001139 molecular_function obo:GO_0001139 transcription factor activity, core RNA polymerase II recruiting obo:GO_0001139 GO:0001139 obo:GO_0001139 RNA polymerase II complex recruiting activity obo:GO_0001145 Interacting selectively and non-covalently with a DNA sequence that controls mitochondrial transcription termination. obo:GO_0001145 obo:go.owl obo:GO_0001145 kchris obo:GO_0001145 2011-01-27T02:42:23Z obo:GO_0001145 GO:0001146 obo:GO_0001145 mitochondrial RNA polymerase terminator site sequence-specific DNA binding transcription factor activity obo:GO_0001145 transcription factor activity, mitochondrial RNA polymerase terminator site sequence-specific binding obo:GO_0001145 molecular_function obo:GO_0001145 GO:0001145 obo:GO_0001145 mitochondrial RNA polymerase termination site sequence-specific DNA binding obo:GO_0001147 Interacting selectively and non-covalently with a sequence of DNA that promotes termination by RNA polymerase. The transcribed region might be described as a gene, cistron, or operon. obo:GO_0001147 obo:go.owl obo:GO_0001147 kchris obo:GO_0001147 2011-01-27T02:48:26Z obo:GO_0001147 molecular_function obo:GO_0001147 GO:0001147 obo:GO_0001147 Transcription termination sites can be recognized by the RNA polymerase (RNAP) itself or by another protein which interacts with the RNAP to promote transcription termination. Note that not all genes have a specific sequence that functions as a termination site; for most mRNAs transcribed by RNAP II termination is not mediated by a specific termination sequence, but is coupled to polyadenylation. obo:GO_0001147 transcription termination site sequence-specific DNA binding obo:GO_0001148 Interacting selectively and non-covalently with a sequence of DNA that is a terminator for bacterial-type RNA polymerase. obo:GO_0001148 obo:go.owl obo:GO_0001148 kchris obo:GO_0001148 2011-01-27T03:04:07Z obo:GO_0001148 molecular_function obo:GO_0001148 GO:0001148 obo:GO_0001148 bacterial-type RNA polymerase termination site sequence-specific DNA binding obo:GO_0001150 Interacting selectively and non-covalently with a sequence of DNA that is an enhancer region that helps activate transcription of a gene or operon by a bacterial-type RNA polymerase. Enhancers for sigma-54 holoenzymes are typically located 80 to 150 base pairs upstream from the transcription start site, although they can be further away or may be downstream of the promoter. Some transcription units dependent on sigma-70 holoenzymes may also include enhancer sequences. obo:GO_0001150 obo:go.owl obo:GO_0001150 kchris obo:GO_0001150 2011-01-27T03:42:53Z obo:GO_0001150 bacterial-type RNA polymerase upstream activating sequence (UAS) sequence-specific DNA binding obo:GO_0001150 molecular_function obo:GO_0001150 GO:0001150 obo:GO_0001150 Note that the phrase "upstream activating sequence", or UAS is often used in S. cerevisiae literature to refer to regulatory sequences that occur in the region upstream and proximal to the core promoter. In contrast, in bacteria such as E. coli, the phrase "upstream activating sequence", or UAS is a synonym for "enhancer". obo:GO_0001150 bacterial-type RNA polymerase enhancer sequence-specific DNA binding obo:GO_0001154 Interacting selectively and non-covalently with a general RNA polymerase III transcription factor belonging to the TFIIB complex, one of the factors involved in formation of the preinitiation complex (PIC) by RNA polymerase III. obo:GO_0001154 obo:go.owl obo:GO_0001154 kchris obo:GO_0001154 2011-01-27T04:53:50Z obo:GO_0001154 TFIIIB-class transcription factor binding obo:GO_0001154 molecular_function obo:GO_0001154 GO:0001154 obo:GO_0001154 TFIIIB-class transcription factor complex binding obo:GO_0001155 Interacting selectively and non-covalently with an RNA polymerase III transcription factor of the TFIIIA class, one of the factors involved in formation of the preinitiation complex (PIC) at RNA polymerase III promoters. obo:GO_0001155 obo:go.owl obo:GO_0001155 kchris obo:GO_0001155 2011-01-27T04:57:49Z obo:GO_0001155 molecular_function obo:GO_0001155 GO:0001155 obo:GO_0001155 TFIIIA-class transcription factor binding obo:GO_0001156 Interacting selectively and non-covalently with a general RNA polymerase III transcription factor belonging to the TFIIC complex, one of the factors involved in formation of the preinitiation complex (PIC) by RNA polymerase III. obo:GO_0001156 obo:go.owl obo:GO_0001156 kchris obo:GO_0001156 2011-01-27T05:02:22Z obo:GO_0001156 TFIIIC-class transcription factor binding obo:GO_0001156 molecular_function obo:GO_0001156 GO:0001156 obo:GO_0001156 TFIIIC-class transcription factor complex binding obo:GO_0001158 Interacting selectively and non-covalently with a specific sequence of DNA that is part of an enhancer, a transcription regulatory region that is somewhat distal from the core promoter and which enhances transcription from that promoter. obo:GO_0001158 obo:go.owl obo:GO_0001158 kchris obo:GO_0001158 2011-01-28T03:29:40Z obo:GO_0001158 molecular_function obo:GO_0001158 GO:0001158 obo:GO_0001158 enhancer sequence-specific DNA binding obo:GO_0001160 Interacting selectively and non-covalently with a region of DNA that promotes termination by RNA polymerase. The transcribed region might be described as a gene, cistron, or operon. obo:GO_0001160 obo:go.owl obo:GO_0001160 kchris obo:GO_0001160 2011-01-28T03:39:44Z obo:GO_0001160 molecular_function obo:GO_0001160 GO:0001160 obo:GO_0001160 transcription termination site DNA binding obo:GO_0001161 Interacting selectively and non-covalently with an intronic DNA sequence that regulates the transcription of the transcript it is contained within. obo:GO_0001161 obo:go.owl obo:GO_0001161 kchris obo:GO_0001161 2011-01-28T03:44:02Z obo:GO_0001161 molecular_function obo:GO_0001161 GO:0001161 obo:GO_0001161 intronic transcription regulatory region sequence-specific DNA binding obo:GO_0001162 Interacting selectively and non-covalently with an RNA polymerase II intronic DNA sequence that regulates the transcription of the transcript it is contained within. obo:GO_0001162 obo:go.owl obo:GO_0001162 kchris obo:GO_0001162 2011-01-28T03:46:19Z obo:GO_0001162 molecular_function obo:GO_0001162 GO:0001162 obo:GO_0001162 RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding obo:GO_0001163 Interacting selectively and non-covalently with a specific sequence of DNA that is part of a regulatory region that controls the transcription of a gene or cistron by RNA polymerase I. obo:GO_0001163 obo:go.owl obo:GO_0001163 kchris obo:GO_0001163 2011-01-31T04:12:06Z obo:GO_0001163 molecular_function obo:GO_0001163 GO:0001163 obo:GO_0001163 RNA polymerase I regulatory region sequence-specific DNA binding obo:GO_0001164 Interacting selectively and non-covalently with the regulatory region composed of the transcription start site and binding sites for transcription factors of the RNA polymerase I transcription machinery. This site is often referred to as the CORE element. In mammalian cells, the CORE element functions in conjunction with the Upstream Control Element (UCE), while in fungi, protozoa, and plants, the CORE element functions without a UCE. obo:GO_0001164 obo:go.owl obo:GO_0001164 kchris obo:GO_0001164 2011-01-31T04:47:48Z obo:GO_0001164 GO:0001187 obo:GO_0001164 RNA polymerase I core element sequence-specific DNA binding obo:GO_0001164 RNA polymerase I core promoter sequence-specific DNA binding obo:GO_0001164 molecular_function obo:GO_0001164 RNA polymerase I CORE element sequence-specific DNA binding transcription factor recruiting transcription factor activity obo:GO_0001164 transcription factor activity, RNA polymerase I CORE element binding transcription factor recruiting obo:GO_0001164 GO:0001164 obo:GO_0001164 RNA polymerase I CORE element sequence-specific DNA binding obo:GO_0001165 Interacting selectively and non-covalently with the upstream control element (UCE, or alternately referred to as the upstream element), a sequence of DNA that is in cis with and relatively close to a core promoter for RNA polymerase I. obo:GO_0001165 obo:go.owl obo:GO_0001165 kchris obo:GO_0001165 2011-01-31T05:09:10Z obo:GO_0001165 molecular_function obo:GO_0001165 RNA polymerase I upstream element sequence-specific DNA binding obo:GO_0001165 GO:0001165 obo:GO_0001165 RNA polymerase I upstream control element sequence-specific DNA binding obo:GO_0001166 Interacting selectively and non-covalently with a RNA polymerase I (Pol I) enhancer. In mammalian cells, enhancers are distal sequences that increase the utilization of promoters, and can function in either orientation and in any location (upstream or downstream) relative to the core promoter. obo:GO_0001166 obo:go.owl obo:GO_0001166 kchris obo:GO_0001166 2011-01-31T05:29:59Z obo:GO_0001166 molecular_function obo:GO_0001166 GO:0001166 obo:GO_0001166 RNA polymerase I enhancer sequence-specific DNA binding obo:GO_0001179 Interacting selectively and non-covalently with an RNA polymerase I transcription factor, any protein required to initiate or regulate transcription by RNA polymerase I. obo:GO_0001179 obo:go.owl obo:GO_0001179 kchris obo:GO_0001179 2011-08-12T03:03:03Z obo:GO_0001179 RNA polymerase I transcription factor binding obo:GO_0001179 molecular_function obo:GO_0001179 GO:0001179 obo:GO_0001179 RNA polymerase I general transcription initiation factor binding obo:GO_0001186 The function of binding to an RNA polymerase I (RNAP I) transcription regulator and recruiting it to the general transcription machinery complex in order to modulate transcription initiation. obo:GO_0001186 obo:go.owl obo:GO_0001186 kchris obo:GO_0001186 2011-08-24T04:00:18Z obo:GO_0001186 RNA polymerase I transcription factor recruiting activity obo:GO_0001186 RNA polymerase I transcription factor recruiting transcription factor activity obo:GO_0001186 molecular_function obo:GO_0001186 transcription factor activity, RNA polymerase I transcription factor recruiting obo:GO_0001186 GO:0001186 obo:GO_0001186 RNA polymerase I transcription regulator recruiting activity obo:GO_0001221 Interacting selectively and non-covalently with a transcription cofactor, any protein involved in regulation of transcription via protein-protein interactions with transcription factors and other transcription regulatory proteins. Cofactors do not bind DNA directly, but rather mediate protein-protein interactions between regulatory transcription factors and the basal transcription machinery. obo:GO_0001221 obo:go.owl obo:GO_0001221 kchris obo:GO_0001221 2012-04-16T03:19:05Z obo:GO_0001221 molecular_function obo:GO_0001221 GO:0001221 obo:GO_0001221 transcription cofactor binding obo:GO_0001222 Interacting selectively and non-covalently with a transcription corepressor, any protein involved in negative regulation of transcription via protein-protein interactions with transcription factors and other proteins that negatively regulate transcription. Transcription corepressors do not bind DNA directly, but rather mediate protein-protein interactions between repressing transcription factors and the basal transcription machinery. obo:GO_0001222 obo:go.owl obo:GO_0001222 kchris obo:GO_0001222 2012-04-16T03:27:26Z obo:GO_0001222 molecular_function obo:GO_0001222 GO:0001222 obo:GO_0001222 transcription corepressor binding obo:GO_0001223 Interacting selectively and non-covalently with a transcription coactivator, any protein involved in positive regulation of transcription via protein-protein interactions with transcription factors and other proteins that positively regulate transcription. Transcription coactivators do not bind DNA directly, but rather mediate protein-protein interactions between activating transcription factors and the basal transcription machinery. obo:GO_0001223 obo:go.owl obo:GO_0001223 kchris obo:GO_0001223 2012-04-16T03:30:16Z obo:GO_0001223 molecular_function obo:GO_0001223 GO:0001223 obo:GO_0001223 transcription coactivator binding obo:GO_0001224 Interacting selectively and non-covalently with a transcription cofactor for RNA polymerase II, any protein involved in regulation of transcription via protein-protein interactions with RNA polymerase II transcription factors and other transcription regulatory proteins. Cofactors do not bind DNA directly, but rather mediate protein-protein interactions between regulatory transcription factors and the basal transcription machinery of RNA polymerase II. obo:GO_0001224 obo:go.owl obo:GO_0001224 kchris obo:GO_0001224 2012-04-16T03:37:06Z obo:GO_0001224 molecular_function obo:GO_0001224 GO:0001224 obo:GO_0001224 RNA polymerase II transcription cofactor binding obo:GO_0001225 Interacting selectively and non-covalently with an RNA polymerase II transcription coactivator, any protein involved in positive regulation of transcription of RNA polymerase II via protein-protein interactions with transcription factors and other proteins that positively regulate transcription. Transcription coactivators do not bind DNA directly, but rather mediate protein-protein interactions between activating transcription factors and the basal transcription machinery of RNA polymerase II. obo:GO_0001225 obo:go.owl obo:GO_0001225 kchris obo:GO_0001225 2012-04-16T03:39:41Z obo:GO_0001225 molecular_function obo:GO_0001225 GO:0001225 obo:GO_0001225 RNA polymerase II transcription coactivator binding obo:GO_0001226 Interacting selectively and non-covalently with an RNA polymerase II transcription corepressor, any protein involved in negative regulation of transcription by RNA polymerase II via protein-protein interactions with transcription factors and other proteins that negatively regulate transcription. Transcription corepressors do not bind DNA directly, but rather mediate protein-protein interactions between repressing transcription factors and the basal transcription machinery of RNA polymerase II. obo:GO_0001226 obo:go.owl obo:GO_0001226 kchris obo:GO_0001226 2012-04-16T03:39:47Z obo:GO_0001226 molecular_function obo:GO_0001226 GO:0001226 obo:GO_0001226 RNA polymerase II transcription corepressor binding obo:GO_0001515 Naturally occurring peptide that is an opioid (any non-alkaloid having an opiate-like effect that can be reversed by naloxone or other recognized morphine antagonist). These include Leu- and Met-enkephalin, dynorphin and neoendorphin, alpha, beta, gamma and delta endorphins formed from beta-lipotropin, various pronase-resistant peptides such as beta casamorphin, and other peptides whose opiate-like action seems to be indirect. obo:GO_0001515 obo:go.owl obo:GO_0001515 molecular_function obo:GO_0001515 GO:0001515 obo:GO_0001515 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0001515 opioid peptide activity obo:GO_0001530 Interacting selectively and non-covalently with lipopolysaccharide. obo:GO_0001530 obo:go.owl obo:GO_0001530 endotoxin binding obo:GO_0001530 LPS binding obo:GO_0001530 molecular_function obo:GO_0001530 GO:0001530 obo:GO_0001530 lipopolysaccharide binding obo:GO_0001531 Interacting selectively and non-covalently with the interleukin-21 receptor. obo:GO_0001531 obo:go.owl obo:GO_0001531 IL-21 obo:GO_0001531 interleukin-21 receptor ligand obo:GO_0001531 molecular_function obo:GO_0001531 GO:0001531 obo:GO_0001531 interleukin-21 receptor binding obo:GO_0001540 Interacting selectively and non-covalently with amyloid-beta peptide/protein and/or its precursor. obo:GO_0001540 obo:go.owl obo:GO_0001540 beta-amyloid binding obo:GO_0001540 molecular_function obo:GO_0001540 GO:0001540 obo:GO_0001540 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0001540 amyloid-beta binding obo:GO_0001580 The series of events required for a bitter taste stimulus to be received and converted to a molecular signal. obo:GO_0001580 obo:go.owl obo:GO_0001580 bitter taste detection obo:GO_0001580 perception of bitter taste, detection of chemical stimulus obo:GO_0001580 perception of bitter taste, sensory transduction of chemical stimulus obo:GO_0001580 sensory detection of bitter taste obo:GO_0001580 sensory detection of chemical stimulus during perception of bitter taste obo:GO_0001580 sensory transduction of bitter taste obo:GO_0001580 sensory transduction of chemical stimulus during perception of bitter taste obo:GO_0001580 biological_process obo:GO_0001580 GO:0001580 obo:GO_0001580 detection of chemical stimulus involved in sensory perception of bitter taste obo:GO_0001581 The series of events required for a sour taste stimulus to be received and converted to a molecular signal. obo:GO_0001581 obo:go.owl obo:GO_0001581 perception of sour taste, detection of chemical stimulus obo:GO_0001581 perception of sour taste, sensory transduction of chemical stimulus obo:GO_0001581 sensory detection of chemical stimulus during perception of sour taste obo:GO_0001581 sensory detection of sour taste obo:GO_0001581 sensory transduction of chemical stimulus during perception of sour taste obo:GO_0001581 sensory transduction of sour taste obo:GO_0001581 sour taste detection obo:GO_0001581 biological_process obo:GO_0001581 GO:0001581 obo:GO_0001581 detection of chemical stimulus involved in sensory perception of sour taste obo:GO_0001582 The series of events required for a sweet taste stimulus to be received and converted to a molecular signal. obo:GO_0001582 obo:go.owl obo:GO_0001582 perception of sweet taste, detection of chemical stimulus obo:GO_0001582 perception of sweet taste, sensory transduction of chemical stimulus obo:GO_0001582 sensory detection of chemical stimulus during perception of sweet taste obo:GO_0001582 sensory detection of sweet taste obo:GO_0001582 sensory transduction of chemical stimulus during perception of sweet taste obo:GO_0001582 sensory transduction of sweet taste obo:GO_0001582 sweet taste detection obo:GO_0001582 biological_process obo:GO_0001582 GO:0001582 obo:GO_0001582 detection of chemical stimulus involved in sensory perception of sweet taste obo:GO_0001583 The series of events required for a salty taste stimulus to be received and converted to a molecular signal. obo:GO_0001583 obo:go.owl obo:GO_0001583 perception of salty taste, detection of chemical stimulus obo:GO_0001583 perception of salty taste, sensory transduction of chemical stimulus obo:GO_0001583 salty taste detection obo:GO_0001583 sensory detection of chemical stimulus during perception of salty taste obo:GO_0001583 sensory detection of salty taste obo:GO_0001583 sensory transduction of chemical stimulus during perception of salty taste obo:GO_0001583 sensory transduction of salty taste obo:GO_0001583 biological_process obo:GO_0001583 GO:0001583 obo:GO_0001583 detection of chemical stimulus involved in sensory perception of salty taste obo:GO_0001664 Interacting selectively and non-covalently with a G protein-coupled receptor. obo:GO_0001664 obo:go.owl obo:GO_0001664 Reactome:R-HSA-500717 obo:GO_0001664 G protein coupled receptor binding obo:GO_0001664 G-protein coupled receptor binding obo:GO_0001664 G protein coupled receptor ligand obo:GO_0001664 G-protein-coupled receptor ligand obo:GO_0001664 molecular_function obo:GO_0001664 GO:0001664 obo:GO_0001664 G protein-coupled receptor binding obo:GO_0001666 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level. obo:GO_0001666 obo:go.owl obo:GO_0001666 response to hypoxic stress obo:GO_0001666 response to lowered oxygen tension obo:GO_0001666 response to intermittent hypoxia obo:GO_0001666 response to sustained hypoxia obo:GO_0001666 biological_process obo:GO_0001666 GO:0001666 obo:GO_0001666 Note that this term should not be confused with 'response to anoxia ; GO:0034059'. Note that in laboratory studies, hypoxia is typically studied at O2 concentrations ranging from 0.1 - 5%. obo:GO_0001666 response to hypoxia obo:GO_0001678 A cellular homeostatic process involved in the maintenance of an internal steady state of glucose within a cell or between a cell and its external environment. obo:GO_0001678 obo:go.owl obo:GO_0001678 cell glucose homeostasis obo:GO_0001678 biological_process obo:GO_0001678 GO:0001678 obo:GO_0001678 cellular glucose homeostasis obo:GO_0001784 Interacting selectively and non-covalently with a phosphorylated tyrosine residue within a protein. obo:GO_0001784 obo:go.owl obo:GO_0001784 molecular_function obo:GO_0001784 phosphotyrosine binding obo:GO_0001784 GO:0001784 obo:GO_0001784 phosphotyrosine residue binding obo:GO_0001786 Interacting selectively and non-covalently with phosphatidylserine, a class of glycophospholipids in which a phosphatidyl group is esterified to the hydroxyl group of L-serine. obo:GO_0001786 obo:go.owl obo:GO_0001786 molecular_function obo:GO_0001786 GO:0001786 obo:GO_0001786 phosphatidylserine binding obo:GO_0001790 Interacting selectively and non-covalently with a J-chain-containing polymeric immunoglobulin of the IgA or IgM isotypes. obo:GO_0001790 obo:go.owl obo:GO_0001790 molecular_function obo:GO_0001790 GO:0001790 obo:GO_0001790 polymeric immunoglobulin binding obo:GO_0001791 Interacting selectively and non-covalently with an immunoglobulin of the IgM isotype. obo:GO_0001791 obo:go.owl obo:GO_0001791 molecular_function obo:GO_0001791 GO:0001791 obo:GO_0001791 IgM binding obo:GO_0001846 Interacting selectively and non-covalently with an opsonin, such as a complement component or antibody, deposited on the surface of a bacteria, virus, immune complex, or other particulate material. obo:GO_0001846 obo:go.owl obo:GO_0001846 molecular_function obo:GO_0001846 GO:0001846 obo:GO_0001846 Note that an opsonin is a blood serum protein or fragment which when deposited on the surface of a bacteria, virus, immune complex, or other particulate material acts a signal for phagocytosis to cells bearing the appropriate receptors. Not all complement components or fragments and not all antibodies have opsonic properties. obo:GO_0001846 opsonin binding obo:GO_0001848 Interacting selectively and non-covalently with any component or product of the complement cascade. obo:GO_0001848 obo:go.owl obo:GO_0001848 molecular_function obo:GO_0001848 GO:0001848 obo:GO_0001848 Note that the complement cascade includes all of the components involved in the classical complement pathway, the alternative complement pathway, and the lectin complement pathway, as well as the common components of all three pathways. obo:GO_0001848 complement binding obo:GO_0001849 Interacting selectively and non-covalently with the C1q component of the classical complement cascade. obo:GO_0001849 obo:go.owl obo:GO_0001849 molecular_function obo:GO_0001849 GO:0001849 obo:GO_0001849 complement component C1q binding obo:GO_0001850 Interacting selectively and non-covalently with the C3a product of the complement cascade. obo:GO_0001850 obo:go.owl obo:GO_0001850 molecular_function obo:GO_0001850 GO:0001850 obo:GO_0001850 complement component C3a binding obo:GO_0001851 Interacting selectively and non-covalently with the C3b product of the complement cascade. obo:GO_0001851 obo:go.owl obo:GO_0001851 molecular_function obo:GO_0001851 GO:0001851 obo:GO_0001851 complement component C3b binding obo:GO_0001852 Interacting selectively and non-covalently with the iC3b product of the complement cascade. obo:GO_0001852 obo:go.owl obo:GO_0001852 molecular_function obo:GO_0001852 GO:0001852 obo:GO_0001852 complement component iC3b binding obo:GO_0001853 Interacting selectively and non-covalently with the C3dg product of the complement cascade. obo:GO_0001853 obo:go.owl obo:GO_0001853 molecular_function obo:GO_0001853 GO:0001853 obo:GO_0001853 complement component C3dg binding obo:GO_0001854 Interacting selectively and non-covalently with the C3d product of the complement cascade. obo:GO_0001854 obo:go.owl obo:GO_0001854 molecular_function obo:GO_0001854 GO:0001854 obo:GO_0001854 complement component C3d binding obo:GO_0001855 Interacting selectively and non-covalently with the C4b product of the classical complement cascade. obo:GO_0001855 obo:go.owl obo:GO_0001855 molecular_function obo:GO_0001855 GO:0001855 obo:GO_0001855 complement component C4b binding obo:GO_0001856 Interacting selectively and non-covalently with the C5a product of the complement cascade. obo:GO_0001856 obo:go.owl obo:GO_0001856 molecular_function obo:GO_0001856 GO:0001856 obo:GO_0001856 complement component C5a binding obo:GO_0001862 Interacting selectively and non-covalently with a collectin, a member of a group of structurally related pattern recognition molecules characterized by having a carbohydrate recognition domain of the C-type lectin family at the C-terminus and a collagenous domain at the N-terminus. obo:GO_0001862 obo:go.owl obo:GO_0001862 molecular_function obo:GO_0001862 GO:0001862 obo:GO_0001862 Note that collectins include such proteins as mannose-binding lectins (MBL) and surfactant proteins A and D (SP-A and SP-D). obo:GO_0001862 collectin binding obo:GO_0001864 Interacting selectively and non-covalently with a pentraxin, a member of a family of inflammatory proteins with a radially symmetric arrangement of five identical, noncovalently linked chains in a pentagonal array. obo:GO_0001864 obo:go.owl obo:GO_0001864 molecular_function obo:GO_0001864 GO:0001864 obo:GO_0001864 Note that pentraxins include such proteins as serum amyloid P component (SAP) and C-reactive protein (CRP). obo:GO_0001864 pentraxin binding obo:GO_0001872 Interacting selectively and non-covalently with (1->3)-beta-D-glucans. obo:GO_0001872 obo:go.owl obo:GO_0001872 GO:0080087 obo:GO_0001872 1,3-beta-D-glucan binding obo:GO_0001872 callose binding obo:GO_0001872 zymosan binding obo:GO_0001872 molecular_function obo:GO_0001872 GO:0001872 obo:GO_0001872 (1->3)-beta-D-glucan binding obo:GO_0001876 Interacting selectively and non-covalently with lipoarabinomannan. obo:GO_0001876 obo:go.owl obo:GO_0001876 LAM binding obo:GO_0001876 molecular_function obo:GO_0001876 GO:0001876 obo:GO_0001876 lipoarabinomannan binding obo:GO_0001882 Interacting selectively and non-covalently with a nucleoside, a compound consisting of a purine or pyrimidine nitrogenous base linked either to ribose or deoxyribose. obo:GO_0001882 obo:go.owl obo:GO_0001882 molecular_function obo:GO_0001882 GO:0001882 obo:GO_0001882 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0001882 nucleoside binding obo:GO_0001883 Interacting selectively and non-covalently with a purine nucleoside, a compound consisting of a purine base linked either to ribose or deoxyribose. obo:GO_0001883 obo:go.owl obo:GO_0001883 molecular_function obo:GO_0001883 GO:0001883 obo:GO_0001883 purine nucleoside binding obo:GO_0001884 Interacting selectively and non-covalently with a pyrimidine nucleoside, a compound consisting of a pyrimidine base linked either to ribose or deoxyribose. obo:GO_0001884 obo:go.owl obo:GO_0001884 molecular_function obo:GO_0001884 GO:0001884 obo:GO_0001884 pyrimidine nucleoside binding obo:GO_0001918 Interacting selectively and non-covalently with a farnesylated protein. obo:GO_0001918 obo:go.owl obo:GO_0001918 molecular_function obo:GO_0001918 GO:0001918 obo:GO_0001918 farnesylated protein binding obo:GO_0001936 Any process that modulates the frequency, rate, or extent of endothelial cell proliferation. obo:GO_0001936 obo:go.owl obo:GO_0001936 biological_process obo:GO_0001936 GO:0001936 obo:GO_0001936 regulation of endothelial cell proliferation obo:GO_0001937 Any process that stops, prevents, or reduces the rate or extent of endothelial cell proliferation. obo:GO_0001937 obo:go.owl obo:GO_0001937 down regulation of endothelial cell proliferation obo:GO_0001937 down-regulation of endothelial cell proliferation obo:GO_0001937 downregulation of endothelial cell proliferation obo:GO_0001937 inhibition of endothelial cell proliferation obo:GO_0001937 biological_process obo:GO_0001937 GO:0001937 obo:GO_0001937 negative regulation of endothelial cell proliferation obo:GO_0001938 Any process that activates or increases the rate or extent of endothelial cell proliferation. obo:GO_0001938 obo:go.owl obo:GO_0001938 up regulation of endothelial cell proliferation obo:GO_0001938 up-regulation of endothelial cell proliferation obo:GO_0001938 upregulation of endothelial cell proliferation obo:GO_0001938 activation of endothelial cell proliferation obo:GO_0001938 stimulation of endothelial cell proliferation obo:GO_0001938 biological_process obo:GO_0001938 GO:0001938 obo:GO_0001938 positive regulation of endothelial cell proliferation obo:GO_0001965 Interacting selectively and non-covalently with a G-protein alpha subunit. The alpha subunit binds a guanine nucleotide. obo:GO_0001965 obo:go.owl obo:GO_0001965 G-alpha protein subunit binding obo:GO_0001965 molecular_function obo:GO_0001965 GO:0001965 obo:GO_0001965 G-protein alpha-subunit binding obo:GO_0001968 Interacting selectively and non-covalently with a fibronectin, a group of related adhesive glycoproteins of high molecular weight found on the surface of animal cells, connective tissue matrices, and in extracellular fluids. obo:GO_0001968 obo:go.owl obo:GO_0001968 molecular_function obo:GO_0001968 GO:0001968 obo:GO_0001968 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0001968 fibronectin binding obo:GO_0001972 Interacting selectively and non-covalently with retinoic acid, 3,7-dimethyl-9-(2,6,-trimethyl-1-cyclohexen-1-yl)-2,4,6,8-nonatetraenoic acid. obo:GO_0001972 obo:go.owl obo:GO_0001972 molecular_function obo:GO_0001972 GO:0001972 obo:GO_0001972 retinoic acid binding obo:GO_0002007 The process in which information about a lack of oxygen are received and are converted to a molecular signal by chemoreceptors in the carotid bodies and the aortic bodies. obo:GO_0002007 obo:go.owl obo:GO_0002007 detection of hypoxic conditions in blood by chemoreceptor signalling obo:GO_0002007 biological_process obo:GO_0002007 GO:0002007 obo:GO_0002007 detection of hypoxic conditions in blood by chemoreceptor signaling obo:GO_0002013 The process by a carbon dioxide stimulus is received and converted to a molecular signal by the vasomotor center of the central nervous system. obo:GO_0002013 obo:go.owl obo:GO_0002013 biological_process obo:GO_0002013 GO:0002013 obo:GO_0002013 detection of carbon dioxide by vasomotor center obo:GO_0002020 Interacting selectively and non-covalently with any protease or peptidase. obo:GO_0002020 obo:go.owl obo:GO_0002020 Reactome:R-HSA-1297354 obo:GO_0002020 molecular_function obo:GO_0002020 GO:0002020 obo:GO_0002020 protease binding obo:GO_0002028 Any process that modulates the frequency, rate or extent of the directed movement of sodium ions (Na+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0002028 obo:go.owl obo:GO_0002028 regulation of Na+ transport obo:GO_0002028 regulation of sodium transport obo:GO_0002028 biological_process obo:GO_0002028 GO:0002028 obo:GO_0002028 regulation of sodium ion transport obo:GO_0002039 Interacting selectively and non-covalently with one of the p53 family of proteins. obo:GO_0002039 obo:go.owl obo:GO_0002039 molecular_function obo:GO_0002039 GO:0002039 obo:GO_0002039 p53 binding obo:GO_0002046 Interacting selectively and non-covalently with an opsin, any of a group of hydrophobic, integral membrane glycoproteins located primarily in the disc membrane of rods or cones, involved in photoreception. obo:GO_0002046 obo:go.owl obo:GO_0002046 GO:0016030 obo:GO_0002046 metarhodopsin binding obo:GO_0002046 molecular_function obo:GO_0002046 GO:0002046 obo:GO_0002046 opsin binding obo:GO_0002053 The process of activating or increasing the rate or extent of mesenchymal cell proliferation. Mesenchymal cells are loosely organized embryonic cells. obo:GO_0002053 obo:go.owl obo:GO_0002053 up regulation of mesenchymal cell proliferation obo:GO_0002053 up-regulation of mesenchymal cell proliferation obo:GO_0002053 upregulation of mesenchymal cell proliferation obo:GO_0002053 activation of mesenchymal cell proliferation obo:GO_0002053 stimulation of mesenchymal cell proliferation obo:GO_0002053 biological_process obo:GO_0002053 GO:0002053 obo:GO_0002053 positive regulation of mesenchymal cell proliferation obo:GO_0002054 Interacting selectively and non-covalently with a nucleobase, any of a class of pyrmidines or purines, organic nitrogenous bases. obo:GO_0002054 obo:go.owl obo:GO_0002054 molecular_function obo:GO_0002054 GO:0002054 obo:GO_0002054 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0002054 nucleobase binding obo:GO_0002055 Interacting selectively and non-covalently with adenine, a purine base. obo:GO_0002055 obo:go.owl obo:GO_0002055 6-aminopurine binding obo:GO_0002055 molecular_function obo:GO_0002055 GO:0002055 obo:GO_0002055 adenine binding obo:GO_0002056 Interacting selectively and non-covalently with cytosine. obo:GO_0002056 obo:go.owl obo:GO_0002056 molecular_function obo:GO_0002056 GO:0002056 obo:GO_0002056 cytosine binding obo:GO_0002057 Interacting selectively and non-covalently with guanine. obo:GO_0002057 obo:go.owl obo:GO_0002057 molecular_function obo:GO_0002057 GO:0002057 obo:GO_0002057 guanine binding obo:GO_0002058 Interacting selectively and non-covalently with uracil. obo:GO_0002058 obo:go.owl obo:GO_0002058 molecular_function obo:GO_0002058 GO:0002058 obo:GO_0002058 uracil binding obo:GO_0002059 Interacting selectively and non-covalently with thymine. obo:GO_0002059 obo:go.owl obo:GO_0002059 molecular_function obo:GO_0002059 GO:0002059 obo:GO_0002059 thymine binding obo:GO_0002060 Interacting selectively and non-covalently with a purine nucleobase, an organic nitrogenous base with a purine skeleton. obo:GO_0002060 obo:go.owl obo:GO_0002060 purine base binding obo:GO_0002060 molecular_function obo:GO_0002060 purine binding obo:GO_0002060 GO:0002060 obo:GO_0002060 purine nucleobase binding obo:GO_0002061 Interacting selectively and non-covalently with a pyrimidine nucleobase, an organic nitrogenous base with a pyrimidine skeleton. obo:GO_0002061 obo:go.owl obo:GO_0002061 pyrimidine base binding obo:GO_0002061 1,3-diazine binding obo:GO_0002061 molecular_function obo:GO_0002061 pyrimidine binding obo:GO_0002061 GO:0002061 obo:GO_0002061 pyrimidine nucleobase binding obo:GO_0002112 Interacting selectively and non-covalently with the interleukin-33 receptor. obo:GO_0002112 obo:go.owl obo:GO_0002112 IL-33 obo:GO_0002112 interleukin-33 receptor ligand obo:GO_0002112 molecular_function obo:GO_0002112 GO:0002112 obo:GO_0002112 interleukin-33 receptor binding obo:GO_0002113 Interacting selectively and non-covalently with interleukin-33. obo:GO_0002113 obo:go.owl obo:GO_0002113 IL-33 binding obo:GO_0002113 molecular_function obo:GO_0002113 GO:0002113 obo:GO_0002113 interleukin-33 binding obo:GO_0002115 A calcium ion entry mechanism in the plasma membrane activated by the depletion of calcium ion from the internal calcium ion store in the endoplasmic reticulum. obo:GO_0002115 obo:go.owl obo:GO_0002115 calcium ion import obo:GO_0002115 SOCE obo:GO_0002115 capacitative calcium entry obo:GO_0002115 store-operated calcium import obo:GO_0002115 biological_process obo:GO_0002115 GO:0002115 obo:GO_0002115 SOCE is initiated by response to stiumlation of membrane receptors leading to the hydrolysis ofphosphatidylinositol bisphosphate (PIP2), inositol 1,4,5-trisphosphate (IP3) generation, and IP3-mediated calcium ion release from the endoplasmic reticulum. obo:GO_0002115 store-operated calcium entry obo:GO_0002134 Interacting selectively and non-covalently with UTP, uridine 5'-triphosphate. obo:GO_0002134 obo:go.owl obo:GO_0002134 molecular_function obo:GO_0002134 GO:0002134 obo:GO_0002134 UTP binding obo:GO_0002135 Interacting selectively and non-covalently with CTP, cytidine 5'-triphosphate. obo:GO_0002135 obo:go.owl obo:GO_0002135 molecular_function obo:GO_0002135 GO:0002135 obo:GO_0002135 CTP binding obo:GO_0002151 Interacting selectively and non-covalently with G-quadruplex RNA structures, in which groups of four guanines adopt a flat, cyclic hydrogen-bonding arrangement known as a guanine tetrad. obo:GO_0002151 obo:go.owl obo:GO_0002151 hjd obo:GO_0002151 2009-10-22T01:38:02Z obo:GO_0002151 G quartet binding obo:GO_0002151 G-quartet binding obo:GO_0002151 G quadruplex binding obo:GO_0002151 G quartet RNA binding obo:GO_0002151 molecular_function obo:GO_0002151 GO:0002151 obo:GO_0002151 The structures of RNA and DNA G quartets differ regarding sugar conformation so that a protein binding to the RNA structure might not bind to the DNA structure. obo:GO_0002151 G-quadruplex RNA binding obo:GO_0002153 Interacting selectively and non-covalently with the steroid receptor RNA activator RNA (SRA). SRA enhances steroid hormone receptor transcriptional activity as an RNA transcript by an indirect mechanism that does not involve SRA-steroid receptor binding. obo:GO_0002153 obo:go.owl obo:GO_0002153 hjd obo:GO_0002153 2009-11-16T02:18:55Z obo:GO_0002153 SRA binding obo:GO_0002153 molecular_function obo:GO_0002153 GO:0002153 obo:GO_0002153 Note: there is also evidence that the RNA itself may code a protein (solution structure of mouse steroid receptor RNA activator 1 (SRA1) protein submitted to PDB by Riken). obo:GO_0002153 steroid receptor RNA activator RNA binding obo:GO_0002162 Interacting selectively and non-covalently with dystroglycan. Dystroglycan is glycoprotein found in non-muscle tissues as well as in muscle tissues, often in association with dystrophin. The native dystroglycan cleaved into two non-covalently associated subunits, alpha (N-terminal) and beta (C-terminal). obo:GO_0002162 obo:go.owl obo:GO_0002162 hjd obo:GO_0002162 2010-02-22T02:17:58Z obo:GO_0002162 GO:0002163 obo:GO_0002162 GO:0002166 obo:GO_0002162 alpha-dystroglycan binding obo:GO_0002162 beta-dystroglycan binding obo:GO_0002162 molecular_function obo:GO_0002162 GO:0002162 obo:GO_0002162 dystroglycan binding obo:GO_0002237 Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus by molecules of bacterial origin such as peptides derived from bacterial flagellin. obo:GO_0002237 obo:go.owl obo:GO_0002237 response to bacteria associated molecule obo:GO_0002237 response to bacterial associated molecule obo:GO_0002237 response to bacterium associated molecule obo:GO_0002237 biological_process obo:GO_0002237 GO:0002237 obo:GO_0002237 response to molecule of bacterial origin obo:GO_0002238 Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus by molecules of fungal origin such as chito-octamer oligosaccharide. obo:GO_0002238 obo:go.owl obo:GO_0002238 response to fungus associated molecule obo:GO_0002238 biological_process obo:GO_0002238 GO:0002238 obo:GO_0002238 response to molecule of fungal origin obo:GO_0002831 Any process that modulates the frequency, rate, or extent of a response to biotic stimulus. obo:GO_0002831 obo:go.owl obo:GO_0002831 biological_process obo:GO_0002831 GO:0002831 obo:GO_0002831 http://purl.oboInOwllibrary.org/oboInOwl/go#gocheck_do_not_manually_annotate obo:GO_0002831 Note that this term is in the subset of terms that should not be used for direct gene product annotation. Instead, select a child term or, if no appropriate child term exists, please request a new term. Direct annotations to this term may be amended during annotation QC. obo:GO_0002831 regulation of response to biotic stimulus obo:GO_0002832 Any process that stops, prevents, or reduces the frequency, rate, or extent of a response to biotic stimulus. obo:GO_0002832 obo:go.owl obo:GO_0002832 down regulation of response to biotic stimulus obo:GO_0002832 down-regulation of response to biotic stimulus obo:GO_0002832 downregulation of response to biotic stimulus obo:GO_0002832 inhibition of response to biotic stimulus obo:GO_0002832 biological_process obo:GO_0002832 GO:0002832 obo:GO_0002832 http://purl.oboInOwllibrary.org/oboInOwl/go#gocheck_do_not_manually_annotate obo:GO_0002832 Note that this term is in the subset of terms that should not be used for direct gene product annotation. Instead, select a child term or, if no appropriate child term exists, please request a new term. Direct annotations to this term may be amended during annotation QC. obo:GO_0002832 negative regulation of response to biotic stimulus obo:GO_0002833 Any process that activates or increases the frequency, rate, or extent of a response to biotic stimulus. obo:GO_0002833 obo:go.owl obo:GO_0002833 up regulation of response to biotic stimulus obo:GO_0002833 up-regulation of response to biotic stimulus obo:GO_0002833 upregulation of response to biotic stimulus obo:GO_0002833 activation of response to biotic stimulus obo:GO_0002833 stimulation of response to biotic stimulus obo:GO_0002833 biological_process obo:GO_0002833 GO:0002833 obo:GO_0002833 http://purl.oboInOwllibrary.org/oboInOwl/go#gocheck_do_not_manually_annotate obo:GO_0002833 Note that this term is in the subset of terms that should not be used for direct gene product annotation. Instead, select a child term or, if no appropriate child term exists, please request a new term. Direct annotations to this term may be amended during annotation QC. obo:GO_0002833 positive regulation of response to biotic stimulus obo:GO_0003020 The process in which information about the levels of oxygen are received and are converted to a molecular signal by chemoreceptors in the carotid bodies and the aortic bodies. obo:GO_0003020 obo:go.owl obo:GO_0003020 detection of reduced oxygen by chemoreceptor signalling obo:GO_0003020 biological_process obo:GO_0003020 GO:0003020 obo:GO_0003020 detection of reduced oxygen by chemoreceptor signaling obo:GO_0003021 The process in which information about the levels of carbon dioxide are received and are converted to a molecular signal by chemoreceptors in the carotid bodies and the aortic bodies. obo:GO_0003021 obo:go.owl obo:GO_0003021 detection of increased carbon dioxide by chemoreceptor signalling obo:GO_0003021 biological_process obo:GO_0003021 GO:0003021 obo:GO_0003021 detection of increased carbon dioxide by chemoreceptor signaling obo:GO_0003022 The process in which information about the levels of hydrogen ions are received and are converted to a molecular signal by chemoreceptors. obo:GO_0003022 obo:go.owl obo:GO_0003022 detection of pH by chemoreceptor signalling obo:GO_0003022 biological_process obo:GO_0003022 GO:0003022 obo:GO_0003022 detection of pH by chemoreceptor signaling obo:GO_0003029 The process in which information about a lack of oxygen are received and are converted to a molecular signal by chemoreceptors in the carotid bodies. obo:GO_0003029 obo:go.owl obo:GO_0003029 detection of hypoxic conditions in blood by carotid body chemoreceptor signalling obo:GO_0003029 biological_process obo:GO_0003029 GO:0003029 obo:GO_0003029 detection of hypoxic conditions in blood by carotid body chemoreceptor signaling obo:GO_0003030 The series of events in which a hydrogen ion stimulus is received by a cell and converted into a molecular signal. obo:GO_0003030 obo:go.owl obo:GO_0003030 biological_process obo:GO_0003030 GO:0003030 obo:GO_0003030 detection of hydrogen ion obo:GO_0003031 The series of events in which a carbon dioxide stimulus is received by a cell and converted into a molecular signal. obo:GO_0003031 obo:go.owl obo:GO_0003031 biological_process obo:GO_0003031 GO:0003031 obo:GO_0003031 detection of carbon dioxide obo:GO_0003032 The series of events in which an oxygen stimulus is received by a cell and converted into a molecular signal. obo:GO_0003032 obo:go.owl obo:GO_0003032 biological_process obo:GO_0003032 GO:0003032 obo:GO_0003032 detection of oxygen obo:GO_0003033 The process in which information about a lack of oxygen are received and are converted to a molecular signal by chemoreceptors in the aortic bodies. obo:GO_0003033 obo:go.owl obo:GO_0003033 detection of hypoxic conditions in blood by aortic body chemoreceptor signalling obo:GO_0003033 biological_process obo:GO_0003033 GO:0003033 obo:GO_0003033 detection of hypoxic conditions in blood by aortic body chemoreceptor signaling obo:GO_0003034 The process in which information about the levels of carbon dioxide are received and are converted to a molecular signal by chemoreceptors in an aortic body. obo:GO_0003034 obo:go.owl obo:GO_0003034 detection of increased carbon dioxide by aortic body chemoreceptor signalling obo:GO_0003034 biological_process obo:GO_0003034 GO:0003034 obo:GO_0003034 detection of increased carbon dioxide by aortic body chemoreceptor signaling obo:GO_0003035 The process in which information about the levels of carbon dioxide are received and are converted to a molecular signal by chemoreceptors in a carotid body. obo:GO_0003035 obo:go.owl obo:GO_0003035 detection of increased carbon dioxide by carotid body chemoreceptor signalling obo:GO_0003035 biological_process obo:GO_0003035 GO:0003035 obo:GO_0003035 detection of increased carbon dioxide by carotid body chemoreceptor signaling obo:GO_0003036 The process in which information about the levels of hydrogen ions are received and are converted to a molecular signal by chemoreceptors in an aortic body. obo:GO_0003036 obo:go.owl obo:GO_0003036 detection of pH by aortic body chemoreceptor signalling obo:GO_0003036 biological_process obo:GO_0003036 GO:0003036 obo:GO_0003036 detection of pH by aortic body chemoreceptor signaling obo:GO_0003037 The process in which information about the levels of hydrogen ions are received and are converted to a molecular signal by chemoreceptors in a carotid body. obo:GO_0003037 obo:go.owl obo:GO_0003037 detection of pH by carotid body chemoreceptor signalling obo:GO_0003037 biological_process obo:GO_0003037 GO:0003037 obo:GO_0003037 detection of pH by carotid body chemoreceptor signaling obo:GO_0003038 The process in which information about the levels of oxygen are received and are converted to a molecular signal by chemoreceptors in an aortic body. obo:GO_0003038 obo:go.owl obo:GO_0003038 detection of reduced oxygen by aortic body chemoreceptor signalling obo:GO_0003038 biological_process obo:GO_0003038 GO:0003038 obo:GO_0003038 detection of reduced oxygen by aortic body chemoreceptor signaling obo:GO_0003039 The process in which information about the levels of oxygen are received and are converted to a molecular signal by chemoreceptors in a carotid body. obo:GO_0003039 obo:go.owl obo:GO_0003039 detection of reduced oxygen by carotid body chemoreceptor signalling obo:GO_0003039 biological_process obo:GO_0003039 GO:0003039 obo:GO_0003039 detection of reduced oxygen by carotid body chemoreceptor signaling obo:GO_0003096 The directed movement of sodium ions (Na+) by the kidney. obo:GO_0003096 obo:go.owl obo:GO_0003096 biological_process obo:GO_0003096 GO:0003096 obo:GO_0003096 renal sodium ion transport obo:GO_0003336 The delamination process that results in the shedding of a corneocyte from the surface of the epidermis. obo:GO_0003336 obo:go.owl obo:GO_0003336 dph obo:GO_0003336 2009-11-24T09:11:53Z obo:GO_0003336 epidermal desquamation obo:GO_0003336 biological_process obo:GO_0003336 GO:0003336 obo:GO_0003336 corneocyte desquamation obo:GO_0003674 A molecular process that can be carried out by the action of a single macromolecular machine, usually via direct physical interactions with other molecular entities. Function in this sense denotes an action, or activity, that a gene product (or a complex) performs. These actions are described from two distinct but related perspectives: (1) biochemical activity, and (2) role as a component in a larger system/process. obo:GO_0003674 obo:go.owl obo:GO_0003674 GO:0005554 obo:GO_0003674 molecular function obo:GO_0003674 molecular_function obo:GO_0003674 GO:0003674 obo:GO_0003674 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_aspergillus obo:GO_0003674 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_candida obo:GO_0003674 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0003674 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0003674 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0003674 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0003674 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0003674 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0003674 Note that, in addition to forming the root of the molecular function ontology, this term is recommended for use for the annotation of gene products whose molecular function is unknown. When this term is used for annotation, it indicates that no information was available about the molecular function of the gene product annotated as of the date the annotation was made; the evidence code "no data" (ND), is used to indicate this. Despite its name, this is not a type of 'function' in the sense typically defined by upper ontologies such as Basic Formal Ontology (BFO). It is instead a BFO:process carried out by a single gene product or complex. obo:GO_0003674 molecular function obo:GO_0003674 molecular_function obo:GO_0003676 Interacting selectively and non-covalently with any nucleic acid. obo:GO_0003676 obo:go.owl obo:GO_0003676 GO:0000496 obo:GO_0003676 MIPS_funcat:16.03 obo:GO_0003676 base pairing obo:GO_0003676 molecular_function obo:GO_0003676 GO:0003676 obo:GO_0003676 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0003676 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0003676 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0003676 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0003676 nucleic acid binding obo:GO_0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). obo:GO_0003677 obo:go.owl obo:GO_0003677 GO:0043566 obo:GO_0003677 MIPS_funcat:16.03.01 obo:GO_0003677 plasmid binding obo:GO_0003677 molecular_function obo:GO_0003677 microtubule/chromatin interaction obo:GO_0003677 structure specific DNA binding obo:GO_0003677 structure-specific DNA binding obo:GO_0003677 GO:0003677 obo:GO_0003677 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_agr obo:GO_0003677 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_aspergillus obo:GO_0003677 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_candida obo:GO_0003677 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0003677 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_flybase_ribbon obo:GO_0003677 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0003677 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_mouse obo:GO_0003677 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0003677 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0003677 DNA binding obo:GO_0003680 Interacting selectively and non-covalently with oligo(A) and oligo(T) tracts of DNA (AT DNA). obo:GO_0003680 obo:go.owl obo:GO_0003680 AT binding obo:GO_0003680 molecular_function obo:GO_0003680 GO:0003680 obo:GO_0003680 AT DNA binding obo:GO_0003681 Interacting selectively and non-covalently with DNA in a bent conformation. obo:GO_0003681 obo:go.owl obo:GO_0003681 molecular_function obo:GO_0003681 GO:0003681 obo:GO_0003681 bent DNA binding obo:GO_0003684 Interacting selectively and non-covalently with damaged DNA. obo:GO_0003684 obo:go.owl obo:GO_0003684 molecular_function obo:GO_0003684 DNA repair enzyme obo:GO_0003684 DNA repair protein obo:GO_0003684 GO:0003684 obo:GO_0003684 damaged DNA binding obo:GO_0003688 Interacting selectively and non-covalently with the DNA replication origin, a unique DNA sequence of a replicon at which DNA replication is initiated and proceeds bidirectionally or unidirectionally. obo:GO_0003688 obo:go.owl obo:GO_0003688 MIPS_funcat:10.01.03.03 obo:GO_0003688 ARS binding obo:GO_0003688 molecular_function obo:GO_0003688 GO:0003688 obo:GO_0003688 DNA replication origin binding obo:GO_0003689 Catalysis of the reaction: ATP + H2O = ADP + phosphate, to drive the opening of the ring structure of the PCNA complex, or any of the related sliding clamp complexes, and their closing around the DNA duplex. obo:GO_0003689 obo:go.owl obo:GO_0003689 Reactome:R-HSA-176264 obo:GO_0003689 DNA clamp loading ATPase activity obo:GO_0003689 PCNA loading activity obo:GO_0003689 PCNA loading complex activity obo:GO_0003689 molecular_function obo:GO_0003689 GO:0003689 obo:GO_0003689 DNA clamp loader activity obo:GO_0003690 Interacting selectively and non-covalently with double-stranded DNA. obo:GO_0003690 obo:go.owl obo:GO_0003690 dsDNA binding obo:GO_0003690 molecular_function obo:GO_0003690 GO:0003690 obo:GO_0003690 double-stranded DNA binding obo:GO_0003691 Interacting selectively and non-covalently with double-stranded telomere-associated DNA. obo:GO_0003691 obo:go.owl obo:GO_0003691 molecular_function obo:GO_0003691 GO:0003691 obo:GO_0003691 double-stranded telomeric DNA binding obo:GO_0003692 Interacting selectively and non-covalently with DNA in the Z form, i.e. a left-handed helix in which the phosphate backbone zigzags. obo:GO_0003692 obo:go.owl obo:GO_0003692 molecular_function obo:GO_0003692 GO:0003692 obo:GO_0003692 left-handed Z-DNA binding obo:GO_0003693 Interacting selectively and non-covalently with any P-element, a class of Drosophila transposon responsible for hybrid dysgenesis. obo:GO_0003693 obo:go.owl obo:GO_0003693 molecular_function obo:GO_0003693 GO:0003693 obo:GO_0003693 P-element binding obo:GO_0003695 Interacting selectively and non-covalently with DNA in a random coil configuration. obo:GO_0003695 obo:go.owl obo:GO_0003695 GO:0016017 obo:GO_0003695 random coil binding obo:GO_0003695 molecular_function obo:GO_0003695 GO:0003695 obo:GO_0003695 random coil DNA binding obo:GO_0003696 Interacting selectively and non-covalently with satellite DNA, the many tandem repeats (identical or related) of a short basic repeating unit; many have a base composition or other property different from the genome average that allows them to be separated from the bulk (main band) genomic DNA. obo:GO_0003696 obo:go.owl obo:GO_0003696 molecular_function obo:GO_0003696 GO:0003696 obo:GO_0003696 satellite DNA binding obo:GO_0003697 Interacting selectively and non-covalently with single-stranded DNA. obo:GO_0003697 obo:go.owl obo:GO_0003697 GO:0003698 obo:GO_0003697 GO:0003699 obo:GO_0003697 ssDNA binding obo:GO_0003697 molecular_function obo:GO_0003697 GO:0003697 obo:GO_0003697 Note that this term is restricted to those cases where the binding is to a single-stranded DNA molecule, not to one of the stands of double-stranded DNA. obo:GO_0003697 single-stranded DNA binding obo:GO_0003723 Interacting selectively and non-covalently with an RNA molecule or a portion thereof. obo:GO_0003723 obo:go.owl obo:GO_0003723 GO:0000498 obo:GO_0003723 GO:0044822 obo:GO_0003723 MIPS_funcat:16.03.03 obo:GO_0003723 Reactome:R-HSA-203922 obo:GO_0003723 base pairing with RNA obo:GO_0003723 molecular_function obo:GO_0003723 poly(A) RNA binding obo:GO_0003723 poly(A)-RNA binding obo:GO_0003723 poly-A RNA binding obo:GO_0003723 GO:0003723 obo:GO_0003723 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_agr obo:GO_0003723 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_aspergillus obo:GO_0003723 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_candida obo:GO_0003723 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0003723 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_flybase_ribbon obo:GO_0003723 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0003723 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_mouse obo:GO_0003723 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0003723 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0003723 RNA binding obo:GO_0003725 Interacting selectively and non-covalently with double-stranded RNA. obo:GO_0003725 obo:go.owl obo:GO_0003725 dsRNA binding obo:GO_0003725 molecular_function obo:GO_0003725 GO:0003725 obo:GO_0003725 double-stranded RNA binding obo:GO_0003727 Interacting selectively and non-covalently with single-stranded RNA. obo:GO_0003727 obo:go.owl obo:GO_0003727 GO:0003728 obo:GO_0003727 ssRNA binding obo:GO_0003727 molecular_function obo:GO_0003727 GO:0003727 obo:GO_0003727 single-stranded RNA binding obo:GO_0003729 Interacting selectively and non-covalently with messenger RNA (mRNA), an intermediate molecule between DNA and protein. mRNA includes UTR and coding sequences, but does not contain introns. obo:GO_0003729 obo:go.owl obo:GO_0003729 GO:0000499 obo:GO_0003729 base pairing with mRNA obo:GO_0003729 molecular_function obo:GO_0003729 GO:0003729 obo:GO_0003729 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0003729 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0003729 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0003729 mRNA binding obo:GO_0003730 Interacting selectively and non-covalently with the 3' untranslated region of an mRNA molecule. obo:GO_0003730 obo:go.owl obo:GO_0003730 mRNA 3' UTR binding obo:GO_0003730 molecular_function obo:GO_0003730 GO:0003730 obo:GO_0003730 mRNA 3'-UTR binding obo:GO_0003779 Interacting selectively and non-covalently with monomeric or multimeric forms of actin, including actin filaments. obo:GO_0003779 obo:go.owl obo:GO_0003779 membrane associated actin binding obo:GO_0003779 molecular_function obo:GO_0003779 GO:0003779 obo:GO_0003779 actin binding obo:GO_0003785 Interacting selectively and non-covalently with monomeric actin, also known as G-actin. obo:GO_0003785 obo:go.owl obo:GO_0003785 G actin binding obo:GO_0003785 molecular_function obo:GO_0003785 GO:0003785 obo:GO_0003785 actin monomer binding obo:GO_0003786 Interacting selectively and non-covalently with an actin filament along its length. obo:GO_0003786 obo:go.owl obo:GO_0003786 molecular_function obo:GO_0003786 GO:0003786 obo:GO_0003786 actin lateral binding obo:GO_0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic. obo:GO_0003824 obo:go.owl obo:GO_0003824 Wikipedia:Enzyme obo:GO_0003824 enzyme activity obo:GO_0003824 molecular_function obo:GO_0003824 GO:0003824 obo:GO_0003824 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0003824 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_flybase_ribbon obo:GO_0003824 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0003824 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0003824 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0003824 catalytic activity obo:GO_0004054 Catalysis of the reaction: L-arginine + ATP = N(omega)-phospho-L-arginine + ADP + 2 H(+). obo:GO_0004054 obo:go.owl obo:GO_0004054 EC:2.7.3.3 obo:GO_0004054 KEGG:R00554 obo:GO_0004054 MetaCyc:ARGININE-KINASE-RXN obo:GO_0004054 RHEA:22940 obo:GO_0004054 ATP:L-arginine N-phosphotransferase activity obo:GO_0004054 adenosine 5'-triphosphate-arginine phosphotransferase activity obo:GO_0004054 arginine phosphokinase activity obo:GO_0004054 molecular_function obo:GO_0004054 adenosine 5'-triphosphate:L-arginine obo:GO_0004054 GO:0004054 obo:GO_0004054 arginine kinase activity obo:GO_0004553 Catalysis of the hydrolysis of any O-glycosyl bond. obo:GO_0004553 obo:go.owl obo:GO_0004553 GO:0016800 obo:GO_0004553 EC:3.2.1 obo:GO_0004553 Reactome:R-HSA-5694563 obo:GO_0004553 Reactome:R-HSA-6786652 obo:GO_0004553 O-glucosyl hydrolase activity obo:GO_0004553 molecular_function obo:GO_0004553 GO:0004553 obo:GO_0004553 hydrolase activity, hydrolyzing O-glycosyl compounds obo:GO_0004659 Catalysis of the transfer of a prenyl group from one compound (donor) to another (acceptor). obo:GO_0004659 obo:go.owl obo:GO_0004659 MetaCyc:GPPSYN-RXN obo:GO_0004659 Reactome:R-HSA-6806674 obo:GO_0004659 molecular_function obo:GO_0004659 GO:0004659 obo:GO_0004659 prenyltransferase activity obo:GO_0004672 Catalysis of the phosphorylation of an amino acid residue in a protein, usually according to the reaction: a protein + ATP = a phosphoprotein + ADP. obo:GO_0004672 obo:go.owl obo:GO_0004672 GO:0050222 obo:GO_0004672 MetaCyc:PROTEIN-KINASE-RXN obo:GO_0004672 Reactome:R-HSA-156832 obo:GO_0004672 Reactome:R-HSA-937034 obo:GO_0004672 Reactome:R-HSA-9604606 obo:GO_0004672 Reactome:R-HSA-975139 obo:GO_0004672 protamine kinase activity obo:GO_0004672 molecular_function obo:GO_0004672 GO:0004672 obo:GO_0004672 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_aspergillus obo:GO_0004672 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_candida obo:GO_0004672 Note that triphosphate is used as a phosphate donor by at least one kinase. obo:GO_0004672 protein kinase activity obo:GO_0004673 Catalysis of the reaction: ATP + protein L-histidine = ADP + protein phospho-L-histidine. obo:GO_0004673 obo:go.owl obo:GO_0004673 GO:0008896 obo:GO_0004673 EC:2.7.13.3 obo:GO_0004673 MetaCyc:2.7.13.3-RXN obo:GO_0004673 ATP:protein-L-histidine N-phosphotransferase activity obo:GO_0004673 histidine kinase (ambiguous) obo:GO_0004673 histidine kinase activity obo:GO_0004673 histidine protein kinase (ambiguous) obo:GO_0004673 histidine protein kinase activity obo:GO_0004673 protein histidine kinase (ambiguous) obo:GO_0004673 protein kinase (histidine) obo:GO_0004673 protein kinase (histidine) (ambiguous) obo:GO_0004673 protein-histidine kinase activity obo:GO_0004673 EnvZ obo:GO_0004673 Sln1p obo:GO_0004673 molecular_function obo:GO_0004673 HK1 obo:GO_0004673 HP165 obo:GO_0004673 GO:0004673 obo:GO_0004673 protein histidine kinase activity obo:GO_0004674 Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate. obo:GO_0004674 obo:go.owl obo:GO_0004674 GO:0004695 obo:GO_0004674 GO:0004696 obo:GO_0004674 GO:0004700 obo:GO_0004674 EC:2.7.11 obo:GO_0004674 Reactome:R-HSA-109702 obo:GO_0004674 Reactome:R-HSA-109822 obo:GO_0004674 Reactome:R-HSA-109823 obo:GO_0004674 Reactome:R-HSA-109860 obo:GO_0004674 Reactome:R-HSA-109862 obo:GO_0004674 Reactome:R-HSA-111919 obo:GO_0004674 Reactome:R-HSA-111970 obo:GO_0004674 Reactome:R-HSA-112342 obo:GO_0004674 Reactome:R-HSA-112381 obo:GO_0004674 Reactome:R-HSA-1168635 obo:GO_0004674 Reactome:R-HSA-1168638 obo:GO_0004674 Reactome:R-HSA-1168641 obo:GO_0004674 Reactome:R-HSA-1181149 obo:GO_0004674 Reactome:R-HSA-1181156 obo:GO_0004674 Reactome:R-HSA-1181355 obo:GO_0004674 Reactome:R-HSA-1225894 obo:GO_0004674 Reactome:R-HSA-1358791 obo:GO_0004674 Reactome:R-HSA-1362270 obo:GO_0004674 Reactome:R-HSA-139908 obo:GO_0004674 Reactome:R-HSA-139918 obo:GO_0004674 Reactome:R-HSA-1445144 obo:GO_0004674 Reactome:R-HSA-1449597 obo:GO_0004674 Reactome:R-HSA-1454699 obo:GO_0004674 Reactome:R-HSA-1458463 obo:GO_0004674 Reactome:R-HSA-1549526 obo:GO_0004674 Reactome:R-HSA-156673 obo:GO_0004674 Reactome:R-HSA-156678 obo:GO_0004674 Reactome:R-HSA-156682 obo:GO_0004674 Reactome:R-HSA-156699 obo:GO_0004674 Reactome:R-HSA-156723 obo:GO_0004674 Reactome:R-HSA-1592233 obo:GO_0004674 Reactome:R-HSA-162363 obo:GO_0004674 Reactome:R-HSA-162657 obo:GO_0004674 Reactome:R-HSA-163010 obo:GO_0004674 Reactome:R-HSA-1632857 obo:GO_0004674 Reactome:R-HSA-163416 obo:GO_0004674 Reactome:R-HSA-163418 obo:GO_0004674 Reactome:R-HSA-1638803 obo:GO_0004674 Reactome:R-HSA-164151 obo:GO_0004674 Reactome:R-HSA-165162 obo:GO_0004674 Reactome:R-HSA-165182 obo:GO_0004674 Reactome:R-HSA-165692 obo:GO_0004674 Reactome:R-HSA-165718 obo:GO_0004674 Reactome:R-HSA-165726 obo:GO_0004674 Reactome:R-HSA-165758 obo:GO_0004674 Reactome:R-HSA-165766 obo:GO_0004674 Reactome:R-HSA-165777 obo:GO_0004674 Reactome:R-HSA-166119 obo:GO_0004674 Reactome:R-HSA-166245 obo:GO_0004674 Reactome:R-HSA-166284 obo:GO_0004674 Reactome:R-HSA-166286 obo:GO_0004674 Reactome:R-HSA-167084 obo:GO_0004674 Reactome:R-HSA-167098 obo:GO_0004674 Reactome:R-HSA-168053 obo:GO_0004674 Reactome:R-HSA-168140 obo:GO_0004674 Reactome:R-HSA-170055 obo:GO_0004674 Reactome:R-HSA-170076 obo:GO_0004674 Reactome:R-HSA-170087 obo:GO_0004674 Reactome:R-HSA-170116 obo:GO_0004674 Reactome:R-HSA-170126 obo:GO_0004674 Reactome:R-HSA-170977 obo:GO_0004674 Reactome:R-HSA-174119 obo:GO_0004674 Reactome:R-HSA-174174 obo:GO_0004674 Reactome:R-HSA-176116 obo:GO_0004674 Reactome:R-HSA-176298 obo:GO_0004674 Reactome:R-HSA-187688 obo:GO_0004674 Reactome:R-HSA-187949 obo:GO_0004674 Reactome:R-HSA-188350 obo:GO_0004674 Reactome:R-HSA-193647 obo:GO_0004674 Reactome:R-HSA-193705 obo:GO_0004674 Reactome:R-HSA-195275 obo:GO_0004674 Reactome:R-HSA-195283 obo:GO_0004674 Reactome:R-HSA-195287 obo:GO_0004674 Reactome:R-HSA-195300 obo:GO_0004674 Reactome:R-HSA-195318 obo:GO_0004674 Reactome:R-HSA-198270 obo:GO_0004674 Reactome:R-HSA-198347 obo:GO_0004674 Reactome:R-HSA-198371 obo:GO_0004674 Reactome:R-HSA-198599 obo:GO_0004674 Reactome:R-HSA-198609 obo:GO_0004674 Reactome:R-HSA-198611 obo:GO_0004674 Reactome:R-HSA-198613 obo:GO_0004674 Reactome:R-HSA-198621 obo:GO_0004674 Reactome:R-HSA-198640 obo:GO_0004674 Reactome:R-HSA-198669 obo:GO_0004674 Reactome:R-HSA-198731 obo:GO_0004674 Reactome:R-HSA-198746 obo:GO_0004674 Reactome:R-HSA-198756 obo:GO_0004674 Reactome:R-HSA-199298 obo:GO_0004674 Reactome:R-HSA-199299 obo:GO_0004674 Reactome:R-HSA-199839 obo:GO_0004674 Reactome:R-HSA-199863 obo:GO_0004674 Reactome:R-HSA-199895 obo:GO_0004674 Reactome:R-HSA-199910 obo:GO_0004674 Reactome:R-HSA-199917 obo:GO_0004674 Reactome:R-HSA-199929 obo:GO_0004674 Reactome:R-HSA-199935 obo:GO_0004674 Reactome:R-HSA-200143 obo:GO_0004674 Reactome:R-HSA-200421 obo:GO_0004674 Reactome:R-HSA-201677 obo:GO_0004674 Reactome:R-HSA-201691 obo:GO_0004674 Reactome:R-HSA-201717 obo:GO_0004674 Reactome:R-HSA-202222 obo:GO_0004674 Reactome:R-HSA-202437 obo:GO_0004674 Reactome:R-HSA-202459 obo:GO_0004674 Reactome:R-HSA-202500 obo:GO_0004674 Reactome:R-HSA-202510 obo:GO_0004674 Reactome:R-HSA-202541 obo:GO_0004674 Reactome:R-HSA-2028284 obo:GO_0004674 Reactome:R-HSA-2028555 obo:GO_0004674 Reactome:R-HSA-2028583 obo:GO_0004674 Reactome:R-HSA-2028589 obo:GO_0004674 Reactome:R-HSA-2028591 obo:GO_0004674 Reactome:R-HSA-2028598 obo:GO_0004674 Reactome:R-HSA-2028629 obo:GO_0004674 Reactome:R-HSA-2028635 obo:GO_0004674 Reactome:R-HSA-2028661 obo:GO_0004674 Reactome:R-HSA-2028670 obo:GO_0004674 Reactome:R-HSA-2028673 obo:GO_0004674 Reactome:R-HSA-2028675 obo:GO_0004674 Reactome:R-HSA-2028679 obo:GO_0004674 Reactome:R-HSA-2029454 obo:GO_0004674 Reactome:R-HSA-2029460 obo:GO_0004674 Reactome:R-HSA-2029469 obo:GO_0004674 Reactome:R-HSA-2060328 obo:GO_0004674 Reactome:R-HSA-209087 obo:GO_0004674 Reactome:R-HSA-211164 obo:GO_0004674 Reactome:R-HSA-211583 obo:GO_0004674 Reactome:R-HSA-211650 obo:GO_0004674 Reactome:R-HSA-2168079 obo:GO_0004674 Reactome:R-HSA-2176475 obo:GO_0004674 Reactome:R-HSA-2214351 obo:GO_0004674 Reactome:R-HSA-2243938 obo:GO_0004674 Reactome:R-HSA-2243942 obo:GO_0004674 Reactome:R-HSA-2294580 obo:GO_0004674 Reactome:R-HSA-2396007 obo:GO_0004674 Reactome:R-HSA-2399941 obo:GO_0004674 Reactome:R-HSA-2399966 obo:GO_0004674 Reactome:R-HSA-2399969 obo:GO_0004674 Reactome:R-HSA-2399977 obo:GO_0004674 Reactome:R-HSA-2399981 obo:GO_0004674 Reactome:R-HSA-2399982 obo:GO_0004674 Reactome:R-HSA-2399985 obo:GO_0004674 Reactome:R-HSA-2399988 obo:GO_0004674 Reactome:R-HSA-2399992 obo:GO_0004674 Reactome:R-HSA-2399996 obo:GO_0004674 Reactome:R-HSA-2399999 obo:GO_0004674 Reactome:R-HSA-2400001 obo:GO_0004674 Reactome:R-HSA-2422927 obo:GO_0004674 Reactome:R-HSA-2430535 obo:GO_0004674 Reactome:R-HSA-2466068 obo:GO_0004674 Reactome:R-HSA-2470508 obo:GO_0004674 Reactome:R-HSA-2529020 obo:GO_0004674 Reactome:R-HSA-2562526 obo:GO_0004674 Reactome:R-HSA-2574840 obo:GO_0004674 Reactome:R-HSA-2730856 obo:GO_0004674 Reactome:R-HSA-2730868 obo:GO_0004674 Reactome:R-HSA-2730876 obo:GO_0004674 Reactome:R-HSA-2730896 obo:GO_0004674 Reactome:R-HSA-2730900 obo:GO_0004674 Reactome:R-HSA-2984226 obo:GO_0004674 Reactome:R-HSA-2984258 obo:GO_0004674 Reactome:R-HSA-2990880 obo:GO_0004674 Reactome:R-HSA-2993898 obo:GO_0004674 Reactome:R-HSA-3000310 obo:GO_0004674 Reactome:R-HSA-3000327 obo:GO_0004674 Reactome:R-HSA-3132737 obo:GO_0004674 Reactome:R-HSA-3209160 obo:GO_0004674 Reactome:R-HSA-3222006 obo:GO_0004674 Reactome:R-HSA-3222020 obo:GO_0004674 Reactome:R-HSA-3228469 obo:GO_0004674 Reactome:R-HSA-3229102 obo:GO_0004674 Reactome:R-HSA-3229152 obo:GO_0004674 Reactome:R-HSA-3239014 obo:GO_0004674 Reactome:R-HSA-3239019 obo:GO_0004674 Reactome:R-HSA-3249371 obo:GO_0004674 Reactome:R-HSA-3371435 obo:GO_0004674 Reactome:R-HSA-3371531 obo:GO_0004674 Reactome:R-HSA-3371567 obo:GO_0004674 Reactome:R-HSA-349426 obo:GO_0004674 Reactome:R-HSA-349444 obo:GO_0004674 Reactome:R-HSA-349455 obo:GO_0004674 Reactome:R-HSA-374696 obo:GO_0004674 Reactome:R-HSA-3769394 obo:GO_0004674 Reactome:R-HSA-377186 obo:GO_0004674 Reactome:R-HSA-3772435 obo:GO_0004674 Reactome:R-HSA-380272 obo:GO_0004674 Reactome:R-HSA-381091 obo:GO_0004674 Reactome:R-HSA-381111 obo:GO_0004674 Reactome:R-HSA-3857328 obo:GO_0004674 Reactome:R-HSA-3857329 obo:GO_0004674 Reactome:R-HSA-3858480 obo:GO_0004674 Reactome:R-HSA-389756 obo:GO_0004674 Reactome:R-HSA-392752 obo:GO_0004674 Reactome:R-HSA-3928577 obo:GO_0004674 Reactome:R-HSA-3928608 obo:GO_0004674 Reactome:R-HSA-3928616 obo:GO_0004674 Reactome:R-HSA-3928620 obo:GO_0004674 Reactome:R-HSA-3928625 obo:GO_0004674 Reactome:R-HSA-3928640 obo:GO_0004674 Reactome:R-HSA-399939 obo:GO_0004674 Reactome:R-HSA-399944 obo:GO_0004674 Reactome:R-HSA-399950 obo:GO_0004674 Reactome:R-HSA-399951 obo:GO_0004674 Reactome:R-HSA-399952 obo:GO_0004674 Reactome:R-HSA-399978 obo:GO_0004674 Reactome:R-HSA-400382 obo:GO_0004674 Reactome:R-HSA-4088134 obo:GO_0004674 Reactome:R-HSA-419083 obo:GO_0004674 Reactome:R-HSA-419087 obo:GO_0004674 Reactome:R-HSA-419197 obo:GO_0004674 Reactome:R-HSA-419644 obo:GO_0004674 Reactome:R-HSA-428961 obo:GO_0004674 Reactome:R-HSA-429016 obo:GO_0004674 Reactome:R-HSA-429714 obo:GO_0004674 Reactome:R-HSA-432110 obo:GO_0004674 Reactome:R-HSA-4332358 obo:GO_0004674 Reactome:R-HSA-4332363 obo:GO_0004674 Reactome:R-HSA-4332388 obo:GO_0004674 Reactome:R-HSA-4411383 obo:GO_0004674 Reactome:R-HSA-4411402 obo:GO_0004674 Reactome:R-HSA-442724 obo:GO_0004674 Reactome:R-HSA-442739 obo:GO_0004674 Reactome:R-HSA-442832 obo:GO_0004674 Reactome:R-HSA-445072 obo:GO_0004674 Reactome:R-HSA-446694 obo:GO_0004674 Reactome:R-HSA-446701 obo:GO_0004674 Reactome:R-HSA-448948 obo:GO_0004674 Reactome:R-HSA-448955 obo:GO_0004674 Reactome:R-HSA-450222 obo:GO_0004674 Reactome:R-HSA-450325 obo:GO_0004674 Reactome:R-HSA-450463 obo:GO_0004674 Reactome:R-HSA-450474 obo:GO_0004674 Reactome:R-HSA-450490 obo:GO_0004674 Reactome:R-HSA-450499 obo:GO_0004674 Reactome:R-HSA-450827 obo:GO_0004674 Reactome:R-HSA-451152 obo:GO_0004674 Reactome:R-HSA-451347 obo:GO_0004674 Reactome:R-HSA-4551570 obo:GO_0004674 Reactome:R-HSA-4608825 obo:GO_0004674 Reactome:R-HSA-4793911 obo:GO_0004674 Reactome:R-HSA-5082387 obo:GO_0004674 Reactome:R-HSA-5082405 obo:GO_0004674 Reactome:R-HSA-5213464 obo:GO_0004674 Reactome:R-HSA-5213466 obo:GO_0004674 Reactome:R-HSA-5218814 obo:GO_0004674 Reactome:R-HSA-5218821 obo:GO_0004674 Reactome:R-HSA-5218826 obo:GO_0004674 Reactome:R-HSA-5218854 obo:GO_0004674 Reactome:R-HSA-5218906 obo:GO_0004674 Reactome:R-HSA-5218916 obo:GO_0004674 Reactome:R-HSA-5228811 obo:GO_0004674 Reactome:R-HSA-5229343 obo:GO_0004674 Reactome:R-HSA-5260201 obo:GO_0004674 Reactome:R-HSA-5357472 obo:GO_0004674 Reactome:R-HSA-5357477 obo:GO_0004674 Reactome:R-HSA-5357831 obo:GO_0004674 Reactome:R-HSA-5578777 obo:GO_0004674 Reactome:R-HSA-5607722 obo:GO_0004674 Reactome:R-HSA-5607726 obo:GO_0004674 Reactome:R-HSA-5607732 obo:GO_0004674 Reactome:R-HSA-5607742 obo:GO_0004674 Reactome:R-HSA-5610718 obo:GO_0004674 Reactome:R-HSA-5610722 obo:GO_0004674 Reactome:R-HSA-5610730 obo:GO_0004674 Reactome:R-HSA-5610732 obo:GO_0004674 Reactome:R-HSA-5624473 obo:GO_0004674 Reactome:R-HSA-5624492 obo:GO_0004674 Reactome:R-HSA-5627775 obo:GO_0004674 Reactome:R-HSA-5632670 obo:GO_0004674 Reactome:R-HSA-5632672 obo:GO_0004674 Reactome:R-HSA-5635841 obo:GO_0004674 Reactome:R-HSA-5635842 obo:GO_0004674 Reactome:R-HSA-5665868 obo:GO_0004674 Reactome:R-HSA-5666160 obo:GO_0004674 Reactome:R-HSA-5668545 obo:GO_0004674 Reactome:R-HSA-5668932 obo:GO_0004674 Reactome:R-HSA-5668947 obo:GO_0004674 Reactome:R-HSA-5668984 obo:GO_0004674 Reactome:R-HSA-5669250 obo:GO_0004674 Reactome:R-HSA-5671763 obo:GO_0004674 Reactome:R-HSA-5671919 obo:GO_0004674 Reactome:R-HSA-5672008 obo:GO_0004674 Reactome:R-HSA-5672010 obo:GO_0004674 Reactome:R-HSA-5672828 obo:GO_0004674 Reactome:R-HSA-5672948 obo:GO_0004674 Reactome:R-HSA-5672973 obo:GO_0004674 Reactome:R-HSA-5672978 obo:GO_0004674 Reactome:R-HSA-5674496 obo:GO_0004674 Reactome:R-HSA-5675194 obo:GO_0004674 Reactome:R-HSA-5675198 obo:GO_0004674 Reactome:R-HSA-5675868 obo:GO_0004674 Reactome:R-HSA-5679205 obo:GO_0004674 Reactome:R-HSA-5682026 obo:GO_0004674 Reactome:R-HSA-5682101 obo:GO_0004674 Reactome:R-HSA-5682598 obo:GO_0004674 Reactome:R-HSA-5682983 obo:GO_0004674 Reactome:R-HSA-5683425 obo:GO_0004674 Reactome:R-HSA-5683792 obo:GO_0004674 Reactome:R-HSA-5683801 obo:GO_0004674 Reactome:R-HSA-5683964 obo:GO_0004674 Reactome:R-HSA-5684096 obo:GO_0004674 Reactome:R-HSA-5684140 obo:GO_0004674 Reactome:R-HSA-5684887 obo:GO_0004674 Reactome:R-HSA-5685156 obo:GO_0004674 Reactome:R-HSA-5685230 obo:GO_0004674 Reactome:R-HSA-5685242 obo:GO_0004674 Reactome:R-HSA-5686578 obo:GO_0004674 Reactome:R-HSA-5686704 obo:GO_0004674 Reactome:R-HSA-5687086 obo:GO_0004674 Reactome:R-HSA-5687090 obo:GO_0004674 Reactome:R-HSA-5687094 obo:GO_0004674 Reactome:R-HSA-5687101 obo:GO_0004674 Reactome:R-HSA-5687121 obo:GO_0004674 Reactome:R-HSA-5687183 obo:GO_0004674 Reactome:R-HSA-5690250 obo:GO_0004674 Reactome:R-HSA-5692768 obo:GO_0004674 Reactome:R-HSA-5692775 obo:GO_0004674 Reactome:R-HSA-5692779 obo:GO_0004674 Reactome:R-HSA-5693536 obo:GO_0004674 Reactome:R-HSA-5693540 obo:GO_0004674 Reactome:R-HSA-5693549 obo:GO_0004674 Reactome:R-HSA-5693551 obo:GO_0004674 Reactome:R-HSA-5693575 obo:GO_0004674 Reactome:R-HSA-5693598 obo:GO_0004674 Reactome:R-HSA-5693609 obo:GO_0004674 Reactome:R-HSA-5694441 obo:GO_0004674 Reactome:R-HSA-6788392 obo:GO_0004674 Reactome:R-HSA-6795290 obo:GO_0004674 Reactome:R-HSA-6795460 obo:GO_0004674 Reactome:R-HSA-6795473 obo:GO_0004674 Reactome:R-HSA-6798372 obo:GO_0004674 Reactome:R-HSA-6798374 obo:GO_0004674 Reactome:R-HSA-6799097 obo:GO_0004674 Reactome:R-HSA-6799246 obo:GO_0004674 Reactome:R-HSA-6799332 obo:GO_0004674 Reactome:R-HSA-6799409 obo:GO_0004674 Reactome:R-HSA-6800490 obo:GO_0004674 Reactome:R-HSA-6801666 obo:GO_0004674 Reactome:R-HSA-6801675 obo:GO_0004674 Reactome:R-HSA-6802911 obo:GO_0004674 Reactome:R-HSA-6802919 obo:GO_0004674 Reactome:R-HSA-6802926 obo:GO_0004674 Reactome:R-HSA-6802933 obo:GO_0004674 Reactome:R-HSA-6802935 obo:GO_0004674 Reactome:R-HSA-6802943 obo:GO_0004674 Reactome:R-HSA-6802973 obo:GO_0004674 Reactome:R-HSA-6804266 obo:GO_0004674 Reactome:R-HSA-6804276 obo:GO_0004674 Reactome:R-HSA-6804955 obo:GO_0004674 Reactome:R-HSA-6805059 obo:GO_0004674 Reactome:R-HSA-6805103 obo:GO_0004674 Reactome:R-HSA-6805126 obo:GO_0004674 Reactome:R-HSA-6805276 obo:GO_0004674 Reactome:R-HSA-6805285 obo:GO_0004674 Reactome:R-HSA-6805399 obo:GO_0004674 Reactome:R-HSA-6805479 obo:GO_0004674 Reactome:R-HSA-6805640 obo:GO_0004674 Reactome:R-HSA-6805785 obo:GO_0004674 Reactome:R-HSA-6810233 obo:GO_0004674 Reactome:R-HSA-6811454 obo:GO_0004674 Reactome:R-HSA-6814409 obo:GO_0004674 Reactome:R-HSA-6814559 obo:GO_0004674 Reactome:R-HSA-69604 obo:GO_0004674 Reactome:R-HSA-69608 obo:GO_0004674 Reactome:R-HSA-69685 obo:GO_0004674 Reactome:R-HSA-69891 obo:GO_0004674 Reactome:R-HSA-75010 obo:GO_0004674 Reactome:R-HSA-75028 obo:GO_0004674 Reactome:R-HSA-75809 obo:GO_0004674 Reactome:R-HSA-75820 obo:GO_0004674 Reactome:R-HSA-77071 obo:GO_0004674 Reactome:R-HSA-8850945 obo:GO_0004674 Reactome:R-HSA-8852306 obo:GO_0004674 Reactome:R-HSA-8852317 obo:GO_0004674 Reactome:R-HSA-8853419 obo:GO_0004674 Reactome:R-HSA-8853444 obo:GO_0004674 Reactome:R-HSA-8854908 obo:GO_0004674 Reactome:R-HSA-8856813 obo:GO_0004674 Reactome:R-HSA-8863007 obo:GO_0004674 Reactome:R-HSA-8863011 obo:GO_0004674 Reactome:R-HSA-8863014 obo:GO_0004674 Reactome:R-HSA-8863895 obo:GO_0004674 Reactome:R-HSA-8868260 obo:GO_0004674 Reactome:R-HSA-8868340 obo:GO_0004674 Reactome:R-HSA-8868344 obo:GO_0004674 Reactome:R-HSA-8868567 obo:GO_0004674 Reactome:R-HSA-8868573 obo:GO_0004674 Reactome:R-HSA-8868666 obo:GO_0004674 Reactome:R-HSA-8870558 obo:GO_0004674 Reactome:R-HSA-8873929 obo:GO_0004674 Reactome:R-HSA-8876446 obo:GO_0004674 Reactome:R-HSA-8877691 obo:GO_0004674 Reactome:R-HSA-8878050 obo:GO_0004674 Reactome:R-HSA-8878054 obo:GO_0004674 Reactome:R-HSA-8933446 obo:GO_0004674 Reactome:R-HSA-8939963 obo:GO_0004674 Reactome:R-HSA-8940100 obo:GO_0004674 Reactome:R-HSA-8942836 obo:GO_0004674 Reactome:R-HSA-8944454 obo:GO_0004674 Reactome:R-HSA-8948039 obo:GO_0004674 Reactome:R-HSA-8948146 obo:GO_0004674 Reactome:R-HSA-8948757 obo:GO_0004674 Reactome:R-HSA-8952289 obo:GO_0004674 Reactome:R-HSA-9007539 obo:GO_0004674 Reactome:R-HSA-9008480 obo:GO_0004674 Reactome:R-HSA-9008822 obo:GO_0004674 Reactome:R-HSA-9009208 obo:GO_0004674 Reactome:R-HSA-9012319 obo:GO_0004674 Reactome:R-HSA-9013978 obo:GO_0004674 Reactome:R-HSA-9022314 obo:GO_0004674 Reactome:R-HSA-9023132 obo:GO_0004674 Reactome:R-HSA-9032751 obo:GO_0004674 Reactome:R-HSA-9032863 obo:GO_0004674 Reactome:R-HSA-912470 obo:GO_0004674 Reactome:R-HSA-913996 obo:GO_0004674 Reactome:R-HSA-918229 obo:GO_0004674 Reactome:R-HSA-933525 obo:GO_0004674 Reactome:R-HSA-934559 obo:GO_0004674 Reactome:R-HSA-936951 obo:GO_0004674 Reactome:R-HSA-937022 obo:GO_0004674 Reactome:R-HSA-937059 obo:GO_0004674 Reactome:R-HSA-9604328 obo:GO_0004674 Reactome:R-HSA-9612980 obo:GO_0004674 Reactome:R-HSA-9619515 obo:GO_0004674 Reactome:R-HSA-9619843 obo:GO_0004674 Reactome:R-HSA-9620004 obo:GO_0004674 Reactome:R-HSA-9624526 obo:GO_0004674 Reactome:R-HSA-9626880 obo:GO_0004674 Reactome:R-HSA-9627089 obo:GO_0004674 Reactome:R-HSA-9632868 obo:GO_0004674 Reactome:R-HSA-9634702 obo:GO_0004674 Reactome:R-HSA-975125 obo:GO_0004674 Reactome:R-HSA-975134 obo:GO_0004674 Reactome:R-HSA-975160 obo:GO_0004674 Reactome:R-HSA-975170 obo:GO_0004674 Reactome:R-HSA-975180 obo:GO_0004674 Reactome:R-HSA-975853 obo:GO_0004674 Reactome:R-HSA-975861 obo:GO_0004674 Reactome:R-HSA-975865 obo:GO_0004674 Reactome:R-HSA-975874 obo:GO_0004674 Reactome:R-HSA-975878 obo:GO_0004674 protein serine-threonine kinase activity obo:GO_0004674 serine(threonine) protein kinase activity obo:GO_0004674 serine/threonine protein kinase activity obo:GO_0004674 protein kinase (phosphorylating) activity obo:GO_0004674 protein phosphokinase activity obo:GO_0004674 protein serine kinase activity obo:GO_0004674 protein-serine kinase activity obo:GO_0004674 serine kinase activity obo:GO_0004674 serine protein kinase activity obo:GO_0004674 serine-specific protein kinase activity obo:GO_0004674 threonine-specific protein kinase activity obo:GO_0004674 molecular_function obo:GO_0004674 GO:0004674 obo:GO_0004674 protein serine/threonine kinase activity obo:GO_0004676 Catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein. This reaction requires the presence of a phosphatidylinositol-3-phosphate. obo:GO_0004676 obo:go.owl obo:GO_0004676 EC:2.7.11 obo:GO_0004676 Reactome:R-HSA-437195 obo:GO_0004676 phosphatidylinositol-3-phosphate protein kinase activity obo:GO_0004676 molecular_function obo:GO_0004676 PDK activity obo:GO_0004676 GO:0004676 obo:GO_0004676 3-phosphoinositide-dependent protein kinase activity obo:GO_0004677 Catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein. This reaction requires the presence of DNA. obo:GO_0004677 obo:go.owl obo:GO_0004677 EC:2.7.11 obo:GO_0004677 molecular_function obo:GO_0004677 GO:0004677 obo:GO_0004677 DNA-dependent protein kinase activity obo:GO_0004683 Catalysis of the reactions: ATP + a protein serine = ADP + protein serine phosphate; and ATP + a protein threonine = ADP + protein threonine phosphate. These reactions require the presence of calcium-bound calmodulin. obo:GO_0004683 obo:go.owl obo:GO_0004683 GO:0004684 obo:GO_0004683 GO:0004685 obo:GO_0004683 GO:0004688 obo:GO_0004683 EC:2.7.11.17 obo:GO_0004683 MetaCyc:2.7.11.17-RXN obo:GO_0004683 Reactome:R-HSA-111912 obo:GO_0004683 Reactome:R-HSA-111915 obo:GO_0004683 Reactome:R-HSA-416320 obo:GO_0004683 Reactome:R-HSA-442749 obo:GO_0004683 Reactome:R-HSA-9006992 obo:GO_0004683 Reactome:R-HSA-9617583 obo:GO_0004683 Reactome:R-HSA-9618750 obo:GO_0004683 Reactome:R-HSA-9619125 obo:GO_0004683 Reactome:R-HSA-9619355 obo:GO_0004683 Reactome:R-HSA-9619367 obo:GO_0004683 Reactome:R-HSA-9619478 obo:GO_0004683 Reactome:R-HSA-9619783 obo:GO_0004683 ATP:protein phosphotransferase (Ca2+/calmodulin-dependent) activity obo:GO_0004683 Ca2+/CaM-dependent kinase activity obo:GO_0004683 Ca2+/calmodulin-dependent protein kinase activity obo:GO_0004683 CaM kinase activity obo:GO_0004683 CaM-regulated serine/threonine kinase activity obo:GO_0004683 calcium- and calmodulin-dependent protein kinase activity obo:GO_0004683 calcium/calmodulin-dependent protein kinase activity obo:GO_0004683 calmodulin regulated protein kinase activity obo:GO_0004683 ATP:caldesmon O-phosphotransferase activity obo:GO_0004683 Ca2+/calmodulin-dependent microtubule-associated protein 2 kinase activity obo:GO_0004683 Ca2+/calmodulin-dependent protein kinase 1 activity obo:GO_0004683 Ca2+/calmodulin-dependent protein kinase II activity obo:GO_0004683 Ca2+/calmodulin-dependent protein kinase IV activity obo:GO_0004683 Ca2+/calmodulin-dependent protein kinase kinase activity obo:GO_0004683 Ca2+/calmodulin-dependent protein kinase kinase beta activity obo:GO_0004683 CaM kinase II activity obo:GO_0004683 calcium/calmodulin-dependent protein kinase type II activity obo:GO_0004683 caldesmon kinase (phosphorylating) activity obo:GO_0004683 calmodulin-dependent kinase II activity obo:GO_0004683 calmodulin-dependent protein kinase I activity obo:GO_0004683 molecular_function obo:GO_0004683 CAM PKII obo:GO_0004683 CaMKI obo:GO_0004683 CaMKII obo:GO_0004683 CaMKIV obo:GO_0004683 CaMKKalpha obo:GO_0004683 CaMKKbeta obo:GO_0004683 STK20 obo:GO_0004683 microtubule-associated protein 2 kinase activity obo:GO_0004683 multifunctional calcium- and calmodulin-regulated protein kinase activity obo:GO_0004683 multifunctional calcium/calmodulin regulated protein kinase activity obo:GO_0004683 GO:0004683 obo:GO_0004683 calmodulin-dependent protein kinase activity obo:GO_0004686 Catalysis of the reaction: ATP + [elongation factor 2] = ADP + [elongation factor 2] phosphate. obo:GO_0004686 obo:go.owl obo:GO_0004686 EC:2.7.11.20 obo:GO_0004686 MetaCyc:2.7.11.20-RXN obo:GO_0004686 ATP:elongation factor 2 phosphotransferase activity obo:GO_0004686 Ca/CaM-kinase III activity obo:GO_0004686 CaM kinase III activity obo:GO_0004686 calmodulin-dependent protein kinase III activity obo:GO_0004686 eEF-2 kinase activity obo:GO_0004686 eEF2 kinase activity obo:GO_0004686 elongation factor 2 kinase activity obo:GO_0004686 eukaryotic elongation factor 2 kinase activity obo:GO_0004686 molecular_function obo:GO_0004686 EF2K obo:GO_0004686 STK19 obo:GO_0004686 eEF2K obo:GO_0004686 GO:0004686 obo:GO_0004686 elongation factor-2 kinase activity obo:GO_0004687 Catalysis of the reaction: ATP + myosin-light-chain = ADP + myosin-light-chain phosphate. obo:GO_0004687 obo:go.owl obo:GO_0004687 ATP:myosin-light-chain O-phosphotransferase obo:GO_0004687 myosin light-chain kinase obo:GO_0004687 EC:2.7.11.18 obo:GO_0004687 MetaCyc:2.7.11.18-RXN obo:GO_0004687 Reactome:R-HSA-445813 obo:GO_0004687 Reactome:R-HSA-5668978 obo:GO_0004687 ATP:myosin-light-chain O-phosphotransferase activity obo:GO_0004687 MLCkase activity obo:GO_0004687 calcium/calmodulin-dependent myosin light chain kinase activity obo:GO_0004687 myosin kinase activity obo:GO_0004687 myosin light chain protein kinase activity obo:GO_0004687 myosin light-chain kinase (phosphorylating) obo:GO_0004687 myosin light-chain kinase (phosphorylating) activity obo:GO_0004687 myosin light-chain kinase activity obo:GO_0004687 myosin-light-chain kinase activity obo:GO_0004687 smooth-muscle-myosin-light-chain kinase activity obo:GO_0004687 molecular_function obo:GO_0004687 MLCK obo:GO_0004687 STK18 obo:GO_0004687 GO:0004687 obo:GO_0004687 myosin light chain kinase activity obo:GO_0004689 Catalysis of the reaction: 4 ATP + 2 phosphorylase b = 4 ADP + phosphorylase a. obo:GO_0004689 obo:go.owl obo:GO_0004689 GO:0008606 obo:GO_0004689 EC:2.7.11.19 obo:GO_0004689 MetaCyc:2.7.11.19-RXN obo:GO_0004689 Reactome:R-HSA-453337 obo:GO_0004689 Reactome:R-HSA-71541 obo:GO_0004689 Reactome:R-HSA-71588 obo:GO_0004689 ATP:phosphorylase-b phosphotransferase activity obo:GO_0004689 dephosphophosphorylase kinase activity obo:GO_0004689 glycogen phosphorylase kinase activity obo:GO_0004689 phosphorylase B kinase activity obo:GO_0004689 phosphorylase kinase (phosphorylating) activity obo:GO_0004689 phosphorylase kinase, intrinsic catalyst activity obo:GO_0004689 molecular_function obo:GO_0004689 PHK obo:GO_0004689 STK17 obo:GO_0004689 GO:0004689 obo:GO_0004689 phosphorylase kinase activity obo:GO_0004697 Catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein. This reaction requires diacylglycerol. obo:GO_0004697 obo:go.owl obo:GO_0004697 GO:0004701 obo:GO_0004697 EC:2.7.11.13 obo:GO_0004697 MetaCyc:2.7.11.13-RXN obo:GO_0004697 Reactome:R-HSA-1433508 obo:GO_0004697 Reactome:R-HSA-193703 obo:GO_0004697 Reactome:R-HSA-198314 obo:GO_0004697 Reactome:R-HSA-2179413 obo:GO_0004697 Reactome:R-HSA-2730863 obo:GO_0004697 Reactome:R-HSA-374664 obo:GO_0004697 Reactome:R-HSA-429698 obo:GO_0004697 Reactome:R-HSA-450533 obo:GO_0004697 Reactome:R-HSA-450550 obo:GO_0004697 Reactome:R-HSA-5138432 obo:GO_0004697 Reactome:R-HSA-5218805 obo:GO_0004697 Reactome:R-HSA-5218823 obo:GO_0004697 Reactome:R-HSA-5229194 obo:GO_0004697 Reactome:R-HSA-5623667 obo:GO_0004697 Reactome:R-HSA-5625784 obo:GO_0004697 Reactome:R-HSA-5671749 obo:GO_0004697 Reactome:R-HSA-74615 obo:GO_0004697 Reactome:R-HSA-751040 obo:GO_0004697 Reactome:R-HSA-8934446 obo:GO_0004697 Reactome:R-HSA-9010681 obo:GO_0004697 Reactome:R-HSA-9021357 obo:GO_0004697 Reactome:R-HSA-909552 obo:GO_0004697 Reactome:R-HSA-927889 obo:GO_0004697 Reactome:R-HSA-9626817 obo:GO_0004697 Reactome:R-HSA-9632858 obo:GO_0004697 ATP:protein phosphotransferase (diacylglycerol-dependent) activity obo:GO_0004697 PKC activity obo:GO_0004697 diacylglycerol-activated phospholipid-dependent PKC activity obo:GO_0004697 diacylglycerol-activated phospholipid-dependent protein kinase C activity obo:GO_0004697 protein kinase Cepsilon activity obo:GO_0004697 molecular_function obo:GO_0004697 PKC obo:GO_0004697 PKCalpha obo:GO_0004697 PKCbeta obo:GO_0004697 PKCdelta obo:GO_0004697 PKCepsilon obo:GO_0004697 PKCgamma obo:GO_0004697 PKCzeta obo:GO_0004697 Pkc1p obo:GO_0004697 STK24 obo:GO_0004697 cPKC obo:GO_0004697 cPKCalpha obo:GO_0004697 cPKCbeta obo:GO_0004697 cPKCgamma obo:GO_0004697 nPKC obo:GO_0004697 nPKCdelta obo:GO_0004697 nPKCepsilon obo:GO_0004697 nPKCeta obo:GO_0004697 nPKCtheta obo:GO_0004697 GO:0004697 obo:GO_0004697 protein kinase C activity obo:GO_0004698 Catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein. This reaction requires diacylglycerol and calcium. obo:GO_0004698 obo:go.owl obo:GO_0004698 EC:2.7.11 obo:GO_0004698 Reactome:R-HSA-114683 obo:GO_0004698 Reactome:R-HSA-114684 obo:GO_0004698 Reactome:R-HSA-416639 obo:GO_0004698 Reactome:R-HSA-421007 obo:GO_0004698 calcium-dependent PKC activity obo:GO_0004698 conventional protein kinase C activity obo:GO_0004698 molecular_function obo:GO_0004698 GO:0004698 obo:GO_0004698 calcium-dependent protein kinase C activity obo:GO_0004699 Catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein. This reaction requires diacylglycerol but not calcium. obo:GO_0004699 obo:go.owl obo:GO_0004699 Reactome:R-HSA-5607740 obo:GO_0004699 calcium-independent PKC activity obo:GO_0004699 novel protein kinase C activity obo:GO_0004699 molecular_function obo:GO_0004699 GO:0004699 obo:GO_0004699 calcium-independent protein kinase C activity obo:GO_0004703 Catalysis of the reaction: ATP + G protein-coupled receptor = ADP + G protein-coupled receptor phosphate. obo:GO_0004703 obo:go.owl obo:GO_0004703 GO:0004678 obo:GO_0004703 EC:2.7.11.16 obo:GO_0004703 ATP:G-protein-coupled receptor phosphotransferase activity obo:GO_0004703 G protein coupled receptor phosphorylating protein kinase activity obo:GO_0004703 G protein-coupled receptor kinase activity obo:GO_0004703 G-protein coupled receptor kinase activity obo:GO_0004703 G-protein-coupled receptor phosphorylating protein kinase activity obo:GO_0004703 GPCR kinase activity obo:GO_0004703 GPCR phosphorylating protein kinase activity obo:GO_0004703 molecular_function obo:GO_0004703 GPCRK obo:GO_0004703 GRK4 obo:GO_0004703 GRK5 obo:GO_0004703 GRK6 obo:GO_0004703 STK16 obo:GO_0004703 GO:0004703 obo:GO_0004703 G protein-coupled receptor kinase activity obo:GO_0004705 Catalysis of the reaction: JUN + ATP = JUN phosphate + ADP. This reaction is the phosphorylation and activation of members of the JUN family, a gene family that encodes nuclear transcription factors. obo:GO_0004705 obo:go.owl obo:GO_0004705 EC:2.7.11 obo:GO_0004705 Reactome:R-HSA-168136 obo:GO_0004705 Reactome:R-HSA-204949 obo:GO_0004705 Reactome:R-HSA-205075 obo:GO_0004705 Reactome:R-HSA-205132 obo:GO_0004705 JNK obo:GO_0004705 SAPK1 obo:GO_0004705 c-Jun N-terminal kinase activity obo:GO_0004705 molecular_function obo:GO_0004705 JNK3alpha1 obo:GO_0004705 GO:0004705 obo:GO_0004705 JUN kinase activity obo:GO_0004706 Catalysis of the reaction: JNKK + ATP = JNKK phosphate + ADP. This reaction is the phosphorylation and activation of JUN kinase kinases (JNKKs). obo:GO_0004706 obo:go.owl obo:GO_0004706 EC:2.7.11 obo:GO_0004706 JNKKK obo:GO_0004706 molecular_function obo:GO_0004706 JNK kinase kinase activity obo:GO_0004706 GO:0004706 obo:GO_0004706 JUN kinase kinase kinase activity obo:GO_0004707 Catalysis of the reaction: protein + ATP = protein phosphate + ADP. This reaction is the phosphorylation of proteins. Mitogen-activated protein kinase; a family of protein kinases that perform a crucial step in relaying signals from the plasma membrane to the nucleus. They are activated by a wide range of proliferation- or differentiation-inducing signals; activation is strong with agonists such as polypeptide growth factors and tumor-promoting phorbol esters, but weak (in most cell backgrounds) by stress stimuli. obo:GO_0004707 obo:go.owl obo:GO_0004707 GO:0008338 obo:GO_0004707 GO:0008339 obo:GO_0004707 GO:0016908 obo:GO_0004707 EC:2.7.11.24 obo:GO_0004707 KEGG:R00162 obo:GO_0004707 MetaCyc:2.7.11.24-RXN obo:GO_0004707 Reactome:R-HSA-111898 obo:GO_0004707 Reactome:R-HSA-198733 obo:GO_0004707 Reactome:R-HSA-445079 obo:GO_0004707 Reactome:R-HSA-451366 obo:GO_0004707 Reactome:R-HSA-5654560 obo:GO_0004707 Reactome:R-HSA-5654562 obo:GO_0004707 Reactome:R-HSA-5654565 obo:GO_0004707 Reactome:R-HSA-5654566 obo:GO_0004707 Reactome:R-HSA-73722 obo:GO_0004707 Reactome:R-HSA-9626832 obo:GO_0004707 ATP:protein phosphotransferase (MAPKK-activated) activity obo:GO_0004707 ERK1 obo:GO_0004707 mitogen activated kinase activity obo:GO_0004707 mitogen-activated protein kinase activity obo:GO_0004707 MAP kinase 1 activity obo:GO_0004707 MAP kinase 2 activity obo:GO_0004707 MAP-2 kinase activity obo:GO_0004707 MBP kinase I activity obo:GO_0004707 MBP kinase II activity obo:GO_0004707 MP kinase activity obo:GO_0004707 Mpk2 obo:GO_0004707 SAPK2 obo:GO_0004707 extracellular signal-regulated kinase activity obo:GO_0004707 myelin basic protein kinase activity obo:GO_0004707 p38 obo:GO_0004707 p42 mitogen-activated protein kinase activity obo:GO_0004707 molecular_function obo:GO_0004707 Dp38 obo:GO_0004707 ERK obo:GO_0004707 ERK2 obo:GO_0004707 LeMPK3 obo:GO_0004707 MAPK obo:GO_0004707 PMK-1 obo:GO_0004707 PMK-2 obo:GO_0004707 PMK-3 obo:GO_0004707 STK26 obo:GO_0004707 p38-2 obo:GO_0004707 p38delta obo:GO_0004707 p42mapk obo:GO_0004707 p44mpk obo:GO_0004707 pp42 obo:GO_0004707 pp44mapk obo:GO_0004707 GO:0004707 obo:GO_0004707 MAP kinase activity obo:GO_0004708 Catalysis of the concomitant phosphorylation of threonine (T) and tyrosine (Y) residues in a Thr-Glu-Tyr (TEY) thiolester sequence in a MAP kinase (MAPK) substrate. obo:GO_0004708 obo:go.owl obo:GO_0004708 MEK activity obo:GO_0004708 EC:2.7.11 obo:GO_0004708 MetaCyc:2.7.12.2-RXN obo:GO_0004708 Reactome:R-HSA-1247960 obo:GO_0004708 Reactome:R-HSA-3238999 obo:GO_0004708 Reactome:R-HSA-448951 obo:GO_0004708 Reactome:R-HSA-450333 obo:GO_0004708 Reactome:R-HSA-5218804 obo:GO_0004708 ATP:protein phosphotransferase (MAPKKK-activated) activity obo:GO_0004708 ERK activator kinase activity obo:GO_0004708 MAPK activator activity obo:GO_0004708 MAPKK activity obo:GO_0004708 mitogen-activated protein kinase kinase activity obo:GO_0004708 MAP kinase kinase 4 activity obo:GO_0004708 MAP kinase kinase 7 activity obo:GO_0004708 molecular_function obo:GO_0004708 MAP kinase or ERK kinase activity obo:GO_0004708 MAP2K obo:GO_0004708 MAPKK obo:GO_0004708 MAPKK1 obo:GO_0004708 MEK1 obo:GO_0004708 MEK2 obo:GO_0004708 MKK obo:GO_0004708 MKK2 obo:GO_0004708 MKK4 obo:GO_0004708 MKK6 obo:GO_0004708 MKK7 obo:GO_0004708 STK27 obo:GO_0004708 GO:0004708 obo:GO_0004708 MAP kinase kinase activity obo:GO_0004709 Catalysis of the phosphorylation and activation of a MAP kinase kinase; each MAP kinase kinase can be phosphorylated by any of several MAP kinase kinase kinases. obo:GO_0004709 obo:go.owl obo:GO_0004709 GO:0004710 obo:GO_0004709 EC:2.7.11.25 obo:GO_0004709 MetaCyc:2.7.11.25-RXN obo:GO_0004709 Reactome:R-HSA-168184 obo:GO_0004709 Reactome:R-HSA-2730887 obo:GO_0004709 Reactome:R-HSA-392530 obo:GO_0004709 Reactome:R-HSA-450337 obo:GO_0004709 Reactome:R-HSA-450346 obo:GO_0004709 Reactome:R-HSA-451649 obo:GO_0004709 Reactome:R-HSA-727819 obo:GO_0004709 Reactome:R-HSA-933530 obo:GO_0004709 ATP:protein phosphotransferase (MAPKKKK-activated) activity obo:GO_0004709 MAPK/ERK kinase kinase activity obo:GO_0004709 MAPKKK activity obo:GO_0004709 MEK kinase activity obo:GO_0004709 MEKK activity obo:GO_0004709 mitogen-activated protein kinase kinase kinase activity obo:GO_0004709 MLK-like mitogen-activated protein triple kinase activity obo:GO_0004709 molecular_function obo:GO_0004709 MAP3K obo:GO_0004709 MEKK obo:GO_0004709 MEKK1 obo:GO_0004709 MEKK2 obo:GO_0004709 MEKK3 obo:GO_0004709 MLTK obo:GO_0004709 MLTKa obo:GO_0004709 MLTKb obo:GO_0004709 Mil/Raf obo:GO_0004709 REKS obo:GO_0004709 STK28 obo:GO_0004709 cMos obo:GO_0004709 cRaf obo:GO_0004709 GO:0004709 obo:GO_0004709 MAP kinase kinase kinase activity obo:GO_0004711 Catalysis of the reaction: ribosomal protein S6 + ATP = ribosomal protein S6 phosphate + ATP. obo:GO_0004711 obo:go.owl obo:GO_0004711 EC:2.7.11 obo:GO_0004711 molecular_function obo:GO_0004711 GO:0004711 obo:GO_0004711 ribosomal protein S6 kinase activity obo:GO_0004712 Catalysis of the reactions: ATP + a protein serine = ADP + protein serine phosphate; ATP + a protein threonine = ADP + protein threonine phosphate; and ATP + a protein tyrosine = ADP + protein tyrosine phosphate. obo:GO_0004712 obo:go.owl obo:GO_0004712 dual-specificity kinase activity obo:GO_0004712 dual-specificity protein kinase obo:GO_0004712 EC:2.7.12.1 obo:GO_0004712 Reactome:R-HSA-5672969 obo:GO_0004712 Reactome:R-HSA-5674373 obo:GO_0004712 Reactome:R-HSA-6802910 obo:GO_0004712 Reactome:R-HSA-6802916 obo:GO_0004712 Reactome:R-HSA-6802918 obo:GO_0004712 Reactome:R-HSA-6802921 obo:GO_0004712 Reactome:R-HSA-6802922 obo:GO_0004712 Reactome:R-HSA-6802924 obo:GO_0004712 Reactome:R-HSA-6802927 obo:GO_0004712 Reactome:R-HSA-6802941 obo:GO_0004712 ATP:protein phosphotransferase (Ser/Thr- and Tyr-phosphorylating) activity obo:GO_0004712 Arabidopsis dual specificity kinase 1 activity obo:GO_0004712 protein threonine/tyrosine kinase activity obo:GO_0004712 molecular_function obo:GO_0004712 ADK1 obo:GO_0004712 CLK1 obo:GO_0004712 Mps1p obo:GO_0004712 dDYRK2 obo:GO_0004712 GO:0004712 obo:GO_0004712 protein serine/threonine/tyrosine kinase activity obo:GO_0004713 Catalysis of the reaction: ATP + a protein tyrosine = ADP + protein tyrosine phosphate. obo:GO_0004713 obo:go.owl obo:GO_0004713 GO:0004718 obo:GO_0004713 EC:2.7.10 obo:GO_0004713 Reactome:R-HSA-112333 obo:GO_0004713 Reactome:R-HSA-114600 obo:GO_0004713 Reactome:R-HSA-1168394 obo:GO_0004713 Reactome:R-HSA-1169421 obo:GO_0004713 Reactome:R-HSA-1225952 obo:GO_0004713 Reactome:R-HSA-1225960 obo:GO_0004713 Reactome:R-HSA-1247844 obo:GO_0004713 Reactome:R-HSA-1248655 obo:GO_0004713 Reactome:R-HSA-1250195 obo:GO_0004713 Reactome:R-HSA-1250315 obo:GO_0004713 Reactome:R-HSA-1250348 obo:GO_0004713 Reactome:R-HSA-1251922 obo:GO_0004713 Reactome:R-HSA-1295540 obo:GO_0004713 Reactome:R-HSA-1295609 obo:GO_0004713 Reactome:R-HSA-1307963 obo:GO_0004713 Reactome:R-HSA-1433418 obo:GO_0004713 Reactome:R-HSA-1433454 obo:GO_0004713 Reactome:R-HSA-1433488 obo:GO_0004713 Reactome:R-HSA-1433506 obo:GO_0004713 Reactome:R-HSA-1433542 obo:GO_0004713 Reactome:R-HSA-1470009 obo:GO_0004713 Reactome:R-HSA-1524186 obo:GO_0004713 Reactome:R-HSA-1671691 obo:GO_0004713 Reactome:R-HSA-170070 obo:GO_0004713 Reactome:R-HSA-170156 obo:GO_0004713 Reactome:R-HSA-170991 obo:GO_0004713 Reactome:R-HSA-171011 obo:GO_0004713 Reactome:R-HSA-174164 obo:GO_0004713 Reactome:R-HSA-177930 obo:GO_0004713 Reactome:R-HSA-177934 obo:GO_0004713 Reactome:R-HSA-177937 obo:GO_0004713 Reactome:R-HSA-182969 obo:GO_0004713 Reactome:R-HSA-183058 obo:GO_0004713 Reactome:R-HSA-1839065 obo:GO_0004713 Reactome:R-HSA-1839067 obo:GO_0004713 Reactome:R-HSA-1839098 obo:GO_0004713 Reactome:R-HSA-1839110 obo:GO_0004713 Reactome:R-HSA-1839112 obo:GO_0004713 Reactome:R-HSA-186786 obo:GO_0004713 Reactome:R-HSA-1888198 obo:GO_0004713 Reactome:R-HSA-190326 obo:GO_0004713 Reactome:R-HSA-190385 obo:GO_0004713 Reactome:R-HSA-190388 obo:GO_0004713 Reactome:R-HSA-190408 obo:GO_0004713 Reactome:R-HSA-190413 obo:GO_0004713 Reactome:R-HSA-190427 obo:GO_0004713 Reactome:R-HSA-190429 obo:GO_0004713 Reactome:R-HSA-191062 obo:GO_0004713 Reactome:R-HSA-191636 obo:GO_0004713 Reactome:R-HSA-1963581 obo:GO_0004713 Reactome:R-HSA-1963582 obo:GO_0004713 Reactome:R-HSA-1963586 obo:GO_0004713 Reactome:R-HSA-1982066 obo:GO_0004713 Reactome:R-HSA-2012073 obo:GO_0004713 Reactome:R-HSA-2012082 obo:GO_0004713 Reactome:R-HSA-2012087 obo:GO_0004713 Reactome:R-HSA-202165 obo:GO_0004713 Reactome:R-HSA-202168 obo:GO_0004713 Reactome:R-HSA-202174 obo:GO_0004713 Reactome:R-HSA-202216 obo:GO_0004713 Reactome:R-HSA-202233 obo:GO_0004713 Reactome:R-HSA-202245 obo:GO_0004713 Reactome:R-HSA-202248 obo:GO_0004713 Reactome:R-HSA-202291 obo:GO_0004713 Reactome:R-HSA-202307 obo:GO_0004713 Reactome:R-HSA-2023455 obo:GO_0004713 Reactome:R-HSA-2023460 obo:GO_0004713 Reactome:R-HSA-2029268 obo:GO_0004713 Reactome:R-HSA-2029449 obo:GO_0004713 Reactome:R-HSA-2029453 obo:GO_0004713 Reactome:R-HSA-2029459 obo:GO_0004713 Reactome:R-HSA-2029984 obo:GO_0004713 Reactome:R-HSA-2029989 obo:GO_0004713 Reactome:R-HSA-2033485 obo:GO_0004713 Reactome:R-HSA-2033486 obo:GO_0004713 Reactome:R-HSA-2033488 obo:GO_0004713 Reactome:R-HSA-2033490 obo:GO_0004713 Reactome:R-HSA-2038387 obo:GO_0004713 Reactome:R-HSA-2038944 obo:GO_0004713 Reactome:R-HSA-205289 obo:GO_0004713 Reactome:R-HSA-210291 obo:GO_0004713 Reactome:R-HSA-210872 obo:GO_0004713 Reactome:R-HSA-212710 obo:GO_0004713 Reactome:R-HSA-2130194 obo:GO_0004713 Reactome:R-HSA-2197698 obo:GO_0004713 Reactome:R-HSA-2201322 obo:GO_0004713 Reactome:R-HSA-2395412 obo:GO_0004713 Reactome:R-HSA-2395439 obo:GO_0004713 Reactome:R-HSA-2395801 obo:GO_0004713 Reactome:R-HSA-2396594 obo:GO_0004713 Reactome:R-HSA-2404193 obo:GO_0004713 Reactome:R-HSA-2404199 obo:GO_0004713 Reactome:R-HSA-2424484 obo:GO_0004713 Reactome:R-HSA-2424486 obo:GO_0004713 Reactome:R-HSA-2424487 obo:GO_0004713 Reactome:R-HSA-2428926 obo:GO_0004713 Reactome:R-HSA-2454208 obo:GO_0004713 Reactome:R-HSA-2454239 obo:GO_0004713 Reactome:R-HSA-2586553 obo:GO_0004713 Reactome:R-HSA-2586555 obo:GO_0004713 Reactome:R-HSA-2671742 obo:GO_0004713 Reactome:R-HSA-2671829 obo:GO_0004713 Reactome:R-HSA-2671850 obo:GO_0004713 Reactome:R-HSA-2730833 obo:GO_0004713 Reactome:R-HSA-2730843 obo:GO_0004713 Reactome:R-HSA-2730851 obo:GO_0004713 Reactome:R-HSA-2730858 obo:GO_0004713 Reactome:R-HSA-2730860 obo:GO_0004713 Reactome:R-HSA-2730862 obo:GO_0004713 Reactome:R-HSA-2730882 obo:GO_0004713 Reactome:R-HSA-2730884 obo:GO_0004713 Reactome:R-HSA-2730886 obo:GO_0004713 Reactome:R-HSA-2730888 obo:GO_0004713 Reactome:R-HSA-3215391 obo:GO_0004713 Reactome:R-HSA-354073 obo:GO_0004713 Reactome:R-HSA-354124 obo:GO_0004713 Reactome:R-HSA-372693 obo:GO_0004713 Reactome:R-HSA-373747 obo:GO_0004713 Reactome:R-HSA-373750 obo:GO_0004713 Reactome:R-HSA-374701 obo:GO_0004713 Reactome:R-HSA-377640 obo:GO_0004713 Reactome:R-HSA-380780 obo:GO_0004713 Reactome:R-HSA-388831 obo:GO_0004713 Reactome:R-HSA-388833 obo:GO_0004713 Reactome:R-HSA-389083 obo:GO_0004713 Reactome:R-HSA-389086 obo:GO_0004713 Reactome:R-HSA-389354 obo:GO_0004713 Reactome:R-HSA-389762 obo:GO_0004713 Reactome:R-HSA-391156 obo:GO_0004713 Reactome:R-HSA-391865 obo:GO_0004713 Reactome:R-HSA-391866 obo:GO_0004713 Reactome:R-HSA-391871 obo:GO_0004713 Reactome:R-HSA-3928578 obo:GO_0004713 Reactome:R-HSA-3928580 obo:GO_0004713 Reactome:R-HSA-3928583 obo:GO_0004713 Reactome:R-HSA-3928594 obo:GO_0004713 Reactome:R-HSA-3928604 obo:GO_0004713 Reactome:R-HSA-3928610 obo:GO_0004713 Reactome:R-HSA-3928627 obo:GO_0004713 Reactome:R-HSA-3928648 obo:GO_0004713 Reactome:R-HSA-399934 obo:GO_0004713 Reactome:R-HSA-399946 obo:GO_0004713 Reactome:R-HSA-399947 obo:GO_0004713 Reactome:R-HSA-4093332 obo:GO_0004713 Reactome:R-HSA-418163 obo:GO_0004713 Reactome:R-HSA-418859 obo:GO_0004713 Reactome:R-HSA-418872 obo:GO_0004713 Reactome:R-HSA-419646 obo:GO_0004713 Reactome:R-HSA-428888 obo:GO_0004713 Reactome:R-HSA-429441 obo:GO_0004713 Reactome:R-HSA-429449 obo:GO_0004713 Reactome:R-HSA-432129 obo:GO_0004713 Reactome:R-HSA-434836 obo:GO_0004713 Reactome:R-HSA-4420117 obo:GO_0004713 Reactome:R-HSA-4420121 obo:GO_0004713 Reactome:R-HSA-4420128 obo:GO_0004713 Reactome:R-HSA-4420206 obo:GO_0004713 Reactome:R-HSA-443817 obo:GO_0004713 Reactome:R-HSA-445076 obo:GO_0004713 Reactome:R-HSA-445084 obo:GO_0004713 Reactome:R-HSA-445085 obo:GO_0004713 Reactome:R-HSA-445091 obo:GO_0004713 Reactome:R-HSA-451942 obo:GO_0004713 Reactome:R-HSA-452097 obo:GO_0004713 Reactome:R-HSA-452100 obo:GO_0004713 Reactome:R-HSA-452122 obo:GO_0004713 Reactome:R-HSA-508282 obo:GO_0004713 Reactome:R-HSA-5218640 obo:GO_0004713 Reactome:R-HSA-5218642 obo:GO_0004713 Reactome:R-HSA-5218806 obo:GO_0004713 Reactome:R-HSA-5218809 obo:GO_0004713 Reactome:R-HSA-5218812 obo:GO_0004713 Reactome:R-HSA-5218820 obo:GO_0004713 Reactome:R-HSA-5218828 obo:GO_0004713 Reactome:R-HSA-5218830 obo:GO_0004713 Reactome:R-HSA-5218851 obo:GO_0004713 Reactome:R-HSA-5357429 obo:GO_0004713 Reactome:R-HSA-5607745 obo:GO_0004713 Reactome:R-HSA-5607750 obo:GO_0004713 Reactome:R-HSA-5621355 obo:GO_0004713 Reactome:R-HSA-5621363 obo:GO_0004713 Reactome:R-HSA-5621370 obo:GO_0004713 Reactome:R-HSA-5624486 obo:GO_0004713 Reactome:R-HSA-5637795 obo:GO_0004713 Reactome:R-HSA-5637796 obo:GO_0004713 Reactome:R-HSA-5654147 obo:GO_0004713 Reactome:R-HSA-5654149 obo:GO_0004713 Reactome:R-HSA-5654151 obo:GO_0004713 Reactome:R-HSA-5654222 obo:GO_0004713 Reactome:R-HSA-5654397 obo:GO_0004713 Reactome:R-HSA-5654407 obo:GO_0004713 Reactome:R-HSA-5654408 obo:GO_0004713 Reactome:R-HSA-5654418 obo:GO_0004713 Reactome:R-HSA-5654428 obo:GO_0004713 Reactome:R-HSA-5654545 obo:GO_0004713 Reactome:R-HSA-5654575 obo:GO_0004713 Reactome:R-HSA-5654578 obo:GO_0004713 Reactome:R-HSA-5654582 obo:GO_0004713 Reactome:R-HSA-5654587 obo:GO_0004713 Reactome:R-HSA-5654605 obo:GO_0004713 Reactome:R-HSA-5654607 obo:GO_0004713 Reactome:R-HSA-5654628 obo:GO_0004713 Reactome:R-HSA-5654631 obo:GO_0004713 Reactome:R-HSA-5654634 obo:GO_0004713 Reactome:R-HSA-5654653 obo:GO_0004713 Reactome:R-HSA-5654655 obo:GO_0004713 Reactome:R-HSA-5655243 obo:GO_0004713 Reactome:R-HSA-5655268 obo:GO_0004713 Reactome:R-HSA-5655270 obo:GO_0004713 Reactome:R-HSA-5655278 obo:GO_0004713 Reactome:R-HSA-5655284 obo:GO_0004713 Reactome:R-HSA-5655301 obo:GO_0004713 Reactome:R-HSA-5655341 obo:GO_0004713 Reactome:R-HSA-5683930 obo:GO_0004713 Reactome:R-HSA-5686587 obo:GO_0004713 Reactome:R-HSA-5690702 obo:GO_0004713 Reactome:R-HSA-6784006 obo:GO_0004713 Reactome:R-HSA-6784319 obo:GO_0004713 Reactome:R-HSA-6790087 obo:GO_0004713 Reactome:R-HSA-6806974 obo:GO_0004713 Reactome:R-HSA-68954 obo:GO_0004713 Reactome:R-HSA-69195 obo:GO_0004713 Reactome:R-HSA-873918 obo:GO_0004713 Reactome:R-HSA-873919 obo:GO_0004713 Reactome:R-HSA-873922 obo:GO_0004713 Reactome:R-HSA-873924 obo:GO_0004713 Reactome:R-HSA-879907 obo:GO_0004713 Reactome:R-HSA-879909 obo:GO_0004713 Reactome:R-HSA-879925 obo:GO_0004713 Reactome:R-HSA-8847977 obo:GO_0004713 Reactome:R-HSA-8848005 obo:GO_0004713 Reactome:R-HSA-8848077 obo:GO_0004713 Reactome:R-HSA-8848124 obo:GO_0004713 Reactome:R-HSA-8848436 obo:GO_0004713 Reactome:R-HSA-8848606 obo:GO_0004713 Reactome:R-HSA-8848726 obo:GO_0004713 Reactome:R-HSA-8848758 obo:GO_0004713 Reactome:R-HSA-8848776 obo:GO_0004713 Reactome:R-HSA-8848818 obo:GO_0004713 Reactome:R-HSA-8848873 obo:GO_0004713 Reactome:R-HSA-8848975 obo:GO_0004713 Reactome:R-HSA-8849032 obo:GO_0004713 Reactome:R-HSA-8849042 obo:GO_0004713 Reactome:R-HSA-8849068 obo:GO_0004713 Reactome:R-HSA-8849102 obo:GO_0004713 Reactome:R-HSA-8849463 obo:GO_0004713 Reactome:R-HSA-8851890 obo:GO_0004713 Reactome:R-HSA-8851933 obo:GO_0004713 Reactome:R-HSA-8853309 obo:GO_0004713 Reactome:R-HSA-8853313 obo:GO_0004713 Reactome:R-HSA-8853315 obo:GO_0004713 Reactome:R-HSA-8853325 obo:GO_0004713 Reactome:R-HSA-8855237 obo:GO_0004713 Reactome:R-HSA-8857555 obo:GO_0004713 Reactome:R-HSA-8857577 obo:GO_0004713 Reactome:R-HSA-8857583 obo:GO_0004713 Reactome:R-HSA-8857925 obo:GO_0004713 Reactome:R-HSA-8867041 obo:GO_0004713 Reactome:R-HSA-8874078 obo:GO_0004713 Reactome:R-HSA-8874080 obo:GO_0004713 Reactome:R-HSA-8874082 obo:GO_0004713 Reactome:R-HSA-8875451 obo:GO_0004713 Reactome:R-HSA-8875817 obo:GO_0004713 Reactome:R-HSA-8876230 obo:GO_0004713 Reactome:R-HSA-8876246 obo:GO_0004713 Reactome:R-HSA-8876948 obo:GO_0004713 Reactome:R-HSA-8937728 obo:GO_0004713 Reactome:R-HSA-8937807 obo:GO_0004713 Reactome:R-HSA-8937844 obo:GO_0004713 Reactome:R-HSA-8942607 obo:GO_0004713 Reactome:R-HSA-8948143 obo:GO_0004713 Reactome:R-HSA-8956659 obo:GO_0004713 Reactome:R-HSA-8964242 obo:GO_0004713 Reactome:R-HSA-8964252 obo:GO_0004713 Reactome:R-HSA-8983872 obo:GO_0004713 Reactome:R-HSA-9006323 obo:GO_0004713 Reactome:R-HSA-9006332 obo:GO_0004713 Reactome:R-HSA-9011241 obo:GO_0004713 Reactome:R-HSA-9012650 obo:GO_0004713 Reactome:R-HSA-9018572 obo:GO_0004713 Reactome:R-HSA-9021609 obo:GO_0004713 Reactome:R-HSA-9024726 obo:GO_0004713 Reactome:R-HSA-9026464 obo:GO_0004713 Reactome:R-HSA-9026502 obo:GO_0004713 Reactome:R-HSA-9026510 obo:GO_0004713 Reactome:R-HSA-9026579 obo:GO_0004713 Reactome:R-HSA-9026890 obo:GO_0004713 Reactome:R-HSA-9027272 obo:GO_0004713 Reactome:R-HSA-9027273 obo:GO_0004713 Reactome:R-HSA-9027425 obo:GO_0004713 Reactome:R-HSA-9028728 obo:GO_0004713 Reactome:R-HSA-9029151 obo:GO_0004713 Reactome:R-HSA-9029155 obo:GO_0004713 Reactome:R-HSA-9032426 obo:GO_0004713 Reactome:R-HSA-9032532 obo:GO_0004713 Reactome:R-HSA-9032601 obo:GO_0004713 Reactome:R-HSA-9032854 obo:GO_0004713 Reactome:R-HSA-9033284 obo:GO_0004713 Reactome:R-HSA-9034714 obo:GO_0004713 Reactome:R-HSA-9034814 obo:GO_0004713 Reactome:R-HSA-9034875 obo:GO_0004713 Reactome:R-HSA-9037040 obo:GO_0004713 Reactome:R-HSA-909718 obo:GO_0004713 Reactome:R-HSA-909726 obo:GO_0004713 Reactome:R-HSA-909729 obo:GO_0004713 Reactome:R-HSA-909730 obo:GO_0004713 Reactome:R-HSA-909732 obo:GO_0004713 Reactome:R-HSA-912629 obo:GO_0004713 Reactome:R-HSA-9603420 obo:GO_0004713 Reactome:R-HSA-9606159 obo:GO_0004713 Reactome:R-HSA-9606162 obo:GO_0004713 Reactome:R-HSA-9606163 obo:GO_0004713 Reactome:R-HSA-9612085 obo:GO_0004713 Reactome:R-HSA-9612996 obo:GO_0004713 Reactome:R-HSA-9613023 obo:GO_0004713 Reactome:R-HSA-9625487 obo:GO_0004713 Reactome:R-HSA-982807 obo:GO_0004713 Reactome:R-HSA-983703 obo:GO_0004713 Reactome:R-HSA-983707 obo:GO_0004713 Reactome:R-HSA-983709 obo:GO_0004713 protein-tyrosine kinase activity obo:GO_0004713 JAK obo:GO_0004713 Janus kinase activity obo:GO_0004713 molecular_function obo:GO_0004713 GO:0004713 obo:GO_0004713 protein tyrosine kinase activity obo:GO_0004715 Catalysis of the reaction: ATP + protein L-tyrosine = ADP + protein L-tyrosine phosphate by a non-membrane spanning protein. obo:GO_0004715 obo:go.owl obo:GO_0004715 ATP:protein-tyrosine O-phosphotransferase activity obo:GO_0004715 EC:2.7.10.2 obo:GO_0004715 MetaCyc:2.7.10.2-RXN obo:GO_0004715 Reactome:R-HSA-1112602 obo:GO_0004715 Reactome:R-HSA-1112703 obo:GO_0004715 Reactome:R-HSA-1168423 obo:GO_0004715 Reactome:R-HSA-1168459 obo:GO_0004715 Reactome:R-HSA-1168767 obo:GO_0004715 Reactome:R-HSA-1295519 obo:GO_0004715 Reactome:R-HSA-1369115 obo:GO_0004715 Reactome:R-HSA-432148 obo:GO_0004715 Reactome:R-HSA-437936 obo:GO_0004715 Reactome:R-HSA-453200 obo:GO_0004715 Reactome:R-HSA-6786095 obo:GO_0004715 Reactome:R-HSA-6786096 obo:GO_0004715 Reactome:R-HSA-6788582 obo:GO_0004715 Reactome:R-HSA-879910 obo:GO_0004715 Reactome:R-HSA-8871373 obo:GO_0004715 ATP:protein-L-tyrosine O-phosphotransferase (non-specific) activity obo:GO_0004715 non-specific protein-tyrosine kinase activity obo:GO_0004715 Bruton's tyrosine kinase activity obo:GO_0004715 cytoplasmic protein tyrosine kinase activity obo:GO_0004715 focal adhesion kinase activity obo:GO_0004715 janus kinase 1 activity obo:GO_0004715 janus kinase 2 activity obo:GO_0004715 janus kinase 3 activity obo:GO_0004715 p60c-src protein tyrosine kinase activity obo:GO_0004715 molecular_function obo:GO_0004715 GO:0004715 obo:GO_0004715 non-membrane spanning protein tyrosine kinase activity obo:GO_0004721 Catalysis of the reaction: a phosphoprotein + H2O = a protein + phosphate. Together with protein kinases, these enzymes control the state of phosphorylation of cell proteins and thereby provide an important mechanism for regulating cellular activity. obo:GO_0004721 obo:go.owl obo:GO_0004721 EC:3.1.3.16 obo:GO_0004721 MetaCyc:3.1.3.16-RXN obo:GO_0004721 Reactome:R-HSA-112383 obo:GO_0004721 Reactome:R-HSA-113503 obo:GO_0004721 Reactome:R-HSA-1363274 obo:GO_0004721 Reactome:R-HSA-1363276 obo:GO_0004721 Reactome:R-HSA-167072 obo:GO_0004721 Reactome:R-HSA-170153 obo:GO_0004721 Reactome:R-HSA-170158 obo:GO_0004721 Reactome:R-HSA-170161 obo:GO_0004721 Reactome:R-HSA-174110 obo:GO_0004721 Reactome:R-HSA-174124 obo:GO_0004721 Reactome:R-HSA-178178 obo:GO_0004721 Reactome:R-HSA-2529015 obo:GO_0004721 Reactome:R-HSA-69199 obo:GO_0004721 phosphoprotein phosphohydrolase activity obo:GO_0004721 protein phosphatase activity obo:GO_0004721 protein phosphatase-1 activity obo:GO_0004721 protein phosphatase-2A activity obo:GO_0004721 protein phosphatase-2B activity obo:GO_0004721 protein phosphatase-2C activity obo:GO_0004721 molecular_function obo:GO_0004721 GO:0004721 obo:GO_0004721 phosphoprotein phosphatase activity obo:GO_0004722 Catalysis of the reaction: protein serine phosphate + H2O = protein serine + phosphate, and protein threonine phosphate + H2O = protein threonine + phosphate. obo:GO_0004722 obo:go.owl obo:GO_0004722 GO:0000158 obo:GO_0004722 GO:0000163 obo:GO_0004722 GO:0008598 obo:GO_0004722 GO:0008600 obo:GO_0004722 GO:0015071 obo:GO_0004722 GO:0030357 obo:GO_0004722 GO:0030358 obo:GO_0004722 GO:0030360 obo:GO_0004722 GO:0030361 obo:GO_0004722 Reactome:R-HSA-1295632 obo:GO_0004722 Reactome:R-HSA-163568 obo:GO_0004722 Reactome:R-HSA-1638821 obo:GO_0004722 Reactome:R-HSA-199425 obo:GO_0004722 Reactome:R-HSA-199959 obo:GO_0004722 Reactome:R-HSA-201787 obo:GO_0004722 Reactome:R-HSA-201790 obo:GO_0004722 Reactome:R-HSA-209055 obo:GO_0004722 Reactome:R-HSA-2187401 obo:GO_0004722 Reactome:R-HSA-2995388 obo:GO_0004722 Reactome:R-HSA-3002811 obo:GO_0004722 Reactome:R-HSA-3601585 obo:GO_0004722 Reactome:R-HSA-380949 obo:GO_0004722 Reactome:R-HSA-4088141 obo:GO_0004722 Reactome:R-HSA-429730 obo:GO_0004722 Reactome:R-HSA-4419948 obo:GO_0004722 Reactome:R-HSA-5672957 obo:GO_0004722 Reactome:R-HSA-5672961 obo:GO_0004722 Reactome:R-HSA-5675431 obo:GO_0004722 Reactome:R-HSA-5675433 obo:GO_0004722 Reactome:R-HSA-5679206 obo:GO_0004722 Reactome:R-HSA-5683405 obo:GO_0004722 Reactome:R-HSA-5687758 obo:GO_0004722 Reactome:R-HSA-5692754 obo:GO_0004722 Reactome:R-HSA-5693153 obo:GO_0004722 Reactome:R-HSA-5694421 obo:GO_0004722 Reactome:R-HSA-6792863 obo:GO_0004722 Reactome:R-HSA-6811504 obo:GO_0004722 Reactome:R-HSA-6814559 obo:GO_0004722 Reactome:R-HSA-74948 obo:GO_0004722 Reactome:R-HSA-8948139 obo:GO_0004722 Reactome:R-HSA-9619430 obo:GO_0004722 Reactome:R-HSA-9619449 obo:GO_0004722 Reactome:R-HSA-9619467 obo:GO_0004722 serine/threonine specific protein phosphatase activity obo:GO_0004722 3-hydroxy 3-methylglutaryl coenzymeA reductase phosphatase obo:GO_0004722 Aspergillus awamori acid protein phosphatase obo:GO_0004722 BCKDH phosphatase obo:GO_0004722 HMG-CoA reductase phosphatase obo:GO_0004722 branched-chain alpha-keto acid dehydrogenase phosphatase obo:GO_0004722 calcineurin obo:GO_0004722 casein phosphatase obo:GO_0004722 phosphatase 2A obo:GO_0004722 phosphatase 2B obo:GO_0004722 phosphatase C-II obo:GO_0004722 phosphatase H-II obo:GO_0004722 phosphatase I obo:GO_0004722 phosphatase IB obo:GO_0004722 phosphatase II obo:GO_0004722 phosphatase III obo:GO_0004722 phosphatase IV obo:GO_0004722 phosphatase SP obo:GO_0004722 phosphopyruvate dehydrogenase phosphatase obo:GO_0004722 phosphospectrin phosphatase obo:GO_0004722 polycation modulated (PCM-) phosphatase obo:GO_0004722 protein D phosphatase obo:GO_0004722 protein phosphatase X obo:GO_0004722 protein phosphatase type 1 activity obo:GO_0004722 protein phosphatase type 1, intrinsic catalyst activity obo:GO_0004722 protein phosphatase type 2A activity obo:GO_0004722 protein phosphatase type 2A, intrinsic catalyst activity obo:GO_0004722 protein phosphatase type 2B activity obo:GO_0004722 protein phosphatase type 2B, intrinsic catalyst activity obo:GO_0004722 protein phosphatase type 2C activity obo:GO_0004722 protein phosphatase type 4 activity obo:GO_0004722 protein phosphatase type 4, intrinsic catalyst activity obo:GO_0004722 molecular_function obo:GO_0004722 GO:0004722 obo:GO_0004722 protein serine/threonine phosphatase activity obo:GO_0004723 Catalysis of the reactions: protein serine phosphate + H2O = protein serine + phosphate; and protein threonine phosphate + H2O = protein threonine + phosphate. These reactions require the presence of calcium ions. obo:GO_0004723 obo:go.owl obo:GO_0004723 GO:0008596 obo:GO_0004723 Reactome:R-HSA-2025882 obo:GO_0004723 calcium-dependent protein serine/threonine phosphatase, intrinsic catalyst activity obo:GO_0004723 calcineurin obo:GO_0004723 molecular_function obo:GO_0004723 GO:0004723 obo:GO_0004723 calcium-dependent protein serine/threonine phosphatase activity obo:GO_0004724 Catalysis of the reactions: protein serine phosphate + H2O = protein serine + phosphate; and protein threonine phosphate + H2O = protein threonine + phosphate. These reactions require the presence of magnesium. obo:GO_0004724 obo:go.owl obo:GO_0004724 molecular_function obo:GO_0004724 GO:0004724 obo:GO_0004724 magnesium-dependent protein serine/threonine phosphatase activity obo:GO_0004725 Catalysis of the reaction: protein tyrosine phosphate + H2O = protein tyrosine + phosphate. obo:GO_0004725 obo:go.owl obo:GO_0004725 EC:3.1.3.48 obo:GO_0004725 MetaCyc:PROTEIN-TYROSINE-PHOSPHATASE-RXN obo:GO_0004725 Reactome:R-HSA-1169188 obo:GO_0004725 Reactome:R-HSA-1169192 obo:GO_0004725 Reactome:R-HSA-1169210 obo:GO_0004725 Reactome:R-HSA-1549564 obo:GO_0004725 Reactome:R-HSA-202214 obo:GO_0004725 Reactome:R-HSA-203797 obo:GO_0004725 Reactome:R-HSA-377643 obo:GO_0004725 Reactome:R-HSA-389758 obo:GO_0004725 Reactome:R-HSA-391868 obo:GO_0004725 Reactome:R-HSA-445089 obo:GO_0004725 Reactome:R-HSA-5683967 obo:GO_0004725 Reactome:R-HSA-6807008 obo:GO_0004725 Reactome:R-HSA-6807027 obo:GO_0004725 Reactome:R-HSA-74733 obo:GO_0004725 Reactome:R-HSA-74747 obo:GO_0004725 Reactome:R-HSA-74748 obo:GO_0004725 Reactome:R-HSA-877308 obo:GO_0004725 Reactome:R-HSA-8849435 obo:GO_0004725 Reactome:R-HSA-8852200 obo:GO_0004725 Reactome:R-HSA-8855381 obo:GO_0004725 Reactome:R-HSA-8863804 obo:GO_0004725 Reactome:R-HSA-8864029 obo:GO_0004725 Reactome:R-HSA-8864036 obo:GO_0004725 Reactome:R-HSA-8864125 obo:GO_0004725 Reactome:R-HSA-8867047 obo:GO_0004725 Reactome:R-HSA-8937767 obo:GO_0004725 Reactome:R-HSA-914036 obo:GO_0004725 Reactome:R-HSA-9603719 obo:GO_0004725 Reactome:R-HSA-997309 obo:GO_0004725 Reactome:R-HSA-997311 obo:GO_0004725 Reactome:R-HSA-997314 obo:GO_0004725 Reactome:R-HSA-997326 obo:GO_0004725 PPT-phosphatase activity obo:GO_0004725 PTP-phosphatase activity obo:GO_0004725 PTPase activity obo:GO_0004725 [phosphotyrosine]protein phosphatase activity obo:GO_0004725 phosphoprotein phosphatase (phosphotyrosine) activity obo:GO_0004725 phosphotyrosine histone phosphatase activity obo:GO_0004725 phosphotyrosine phosphatase activity obo:GO_0004725 phosphotyrosine protein phosphatase activity obo:GO_0004725 phosphotyrosylprotein phosphatase activity obo:GO_0004725 protein phosphotyrosine phosphatase activity obo:GO_0004725 protein-tyrosine-phosphatase activity obo:GO_0004725 protein-tyrosine-phosphate phosphohydrolase activity obo:GO_0004725 tyrosine O-phosphate phosphatase activity obo:GO_0004725 tyrosylprotein phosphatase activity obo:GO_0004725 molecular_function obo:GO_0004725 GO:0004725 obo:GO_0004725 protein tyrosine phosphatase activity obo:GO_0004726 Catalysis of the reaction: non-membrane spanning protein tyrosine phosphate + H2O = non-membrane spanning protein tyrosine + phosphate. obo:GO_0004726 obo:go.owl obo:GO_0004726 Reactome:R-HSA-177923 obo:GO_0004726 Reactome:R-HSA-177924 obo:GO_0004726 Reactome:R-HSA-177926 obo:GO_0004726 Reactome:R-HSA-177935 obo:GO_0004726 molecular_function obo:GO_0004726 GO:0004726 obo:GO_0004726 non-membrane spanning protein tyrosine phosphatase activity obo:GO_0004727 Catalysis of the reaction: prenylated-protein tyrosine phosphate + H2O = prenylated-protein tyrosine + phosphate. obo:GO_0004727 obo:go.owl obo:GO_0004727 molecular_function obo:GO_0004727 GO:0004727 obo:GO_0004727 prenylated protein tyrosine phosphatase activity obo:GO_0004740 Catalysis of the reaction: ATP + pyruvate dehydrogenase (acetyl-transferring) = ADP + pyruvate dehydrogenase (acetyl-transferring) phosphate. obo:GO_0004740 obo:go.owl obo:GO_0004740 EC:2.7.11.2 obo:GO_0004740 MetaCyc:2.7.11.2-RXN obo:GO_0004740 Reactome:R-HSA-203946 obo:GO_0004740 ATP:pyruvate dehydrogenase (acetyl-transferring) phosphotransferase activity obo:GO_0004740 PDH kinase activity obo:GO_0004740 [pyruvate dehydrogenase (lipoamide)] kinase activity obo:GO_0004740 pyruvate dehydrogenase (lipoamide) kinase activity obo:GO_0004740 pyruvate dehydrogenase kinase (phosphorylating) activity obo:GO_0004740 pyruvate dehydrogenase kinase activity obo:GO_0004740 pyruvate dehydrogenase kinase activator protein activity obo:GO_0004740 molecular_function obo:GO_0004740 PDHK obo:GO_0004740 PDK obo:GO_0004740 PDK1 obo:GO_0004740 PDK2 obo:GO_0004740 PDK3 obo:GO_0004740 PDK4 obo:GO_0004740 STK1 obo:GO_0004740 GO:0004740 obo:GO_0004740 pyruvate dehydrogenase (acetyl-transferring) kinase activity obo:GO_0004741 Catalysis of the reaction: [pyruvate dehydrogenase (lipoamide)] phosphate + H2O = [pyruvate dehydrogenase (lipoamide)] + phosphate. obo:GO_0004741 obo:go.owl obo:GO_0004741 GO:0019906 obo:GO_0004741 EC:3.1.3.43 obo:GO_0004741 MetaCyc:3.1.3.43-RXN obo:GO_0004741 Reactome:R-HSA-204169 obo:GO_0004741 [pyruvate dehydrogenase (lipoamide)] phosphatase, intrinsic catalyst activity obo:GO_0004741 phosphopyruvate dehydrogenase phosphatase activity obo:GO_0004741 pyruvate dehydrogenase (lipoamide) phosphatase activity obo:GO_0004741 pyruvate dehydrogenase (lipoamide)-phosphatase activity obo:GO_0004741 pyruvate dehydrogenase (lipoamide)-phosphate phosphohydrolase activity obo:GO_0004741 pyruvate dehydrogenase phosphatase activity obo:GO_0004741 molecular_function obo:GO_0004741 GO:0004741 obo:GO_0004741 [pyruvate dehydrogenase (lipoamide)] phosphatase activity obo:GO_0005046 Interacting selectively and non-covalently with a KDEL sequence, the C terminus tetrapeptide sequence Lys-Asp-Glu-Leu found in proteins that are to be retained in the endoplasmic reticulum. obo:GO_0005046 obo:go.owl obo:GO_0005046 KDEL receptor activity obo:GO_0005046 molecular_function obo:GO_0005046 GO:0005046 obo:GO_0005046 KDEL sequence binding obo:GO_0005047 Interacting selectively and non-covalently with the signal recognition particle. obo:GO_0005047 obo:go.owl obo:GO_0005047 docking protein obo:GO_0005047 signal recognition particle receptor obo:GO_0005047 molecular_function obo:GO_0005047 GO:0005047 obo:GO_0005047 See also the cellular component term 'signal recognition particle, endoplasmic reticulum targeting ; GO:0005786'. obo:GO_0005047 signal recognition particle binding obo:GO_0005048 Interacting selectively and non-covalently with a signal sequence, a specific peptide sequence found on protein precursors or mature proteins that dictates where the mature protein is localized. obo:GO_0005048 obo:go.owl obo:GO_0005048 GO:0008249 obo:GO_0005048 leader sequence binding obo:GO_0005048 protein signal sequence binding obo:GO_0005048 signal sequence receptor obo:GO_0005048 molecular_function obo:GO_0005048 GO:0005048 obo:GO_0005048 signal sequence binding obo:GO_0005052 Interacting selectively and non-covalently with a type 1 peroxisome targeting signal, a tripeptide with the consensus sequence (S/A/C)-(K/R/H)-L. obo:GO_0005052 obo:go.owl obo:GO_0005052 PTS1 binding obo:GO_0005052 peroxisomal targeting signal 1 (PTS1) binding obo:GO_0005052 peroxisome targeting signal-1 binding obo:GO_0005052 PEX5 obo:GO_0005052 PTS1 receptor obo:GO_0005052 peroxisome targeting signal-1 receptor obo:GO_0005052 molecular_function obo:GO_0005052 GO:0005052 obo:GO_0005052 peroxisome matrix targeting signal-1 binding obo:GO_0005053 Interacting selectively and non-covalently with a type 2 peroxisome targeting signal, a nonapeptide with a broad consensus sequence of (R/K)-(L/V/I)-(XXXXX)-(H/Q)-(L/A/F). obo:GO_0005053 obo:go.owl obo:GO_0005053 PTS2 binding obo:GO_0005053 PTS2 receptor obo:GO_0005053 peroxisomal targeting signal 2 (PTS2) binding obo:GO_0005053 peroxisome targeting signal-2 binding obo:GO_0005053 PEX7 obo:GO_0005053 peroxisome targeting signal-2 receptor obo:GO_0005053 molecular_function obo:GO_0005053 GO:0005053 obo:GO_0005053 peroxisome matrix targeting signal-2 binding obo:GO_0005055 Combining with a laminin, a glycoprotein that constitutes the majority of proteins in the basement membrane, to initiate a change in cell activity. obo:GO_0005055 obo:go.owl obo:GO_0005055 molecular_function obo:GO_0005055 GO:0005055 obo:GO_0005055 Note that this term represents an activity and not a gene product. Consider also annotating to the molecular function terms 'cell adhesion molecule binding ; GO:0050839' and 'receptor binding ; GO:0005102' and the biological process term 'cell adhesion ; GO:0007155'. obo:GO_0005055 laminin receptor activity obo:GO_0005080 Interacting selectively and non-covalently with protein kinase C. obo:GO_0005080 obo:go.owl obo:GO_0005080 GO:0072568 obo:GO_0005080 GO:0072569 obo:GO_0005080 GO:0097024 obo:GO_0005080 PKC alpha binding obo:GO_0005080 PKC binding obo:GO_0005080 PKC delta binding obo:GO_0005080 PKC eta binding obo:GO_0005080 protein kinase C alpha binding obo:GO_0005080 protein kinase C delta binding obo:GO_0005080 protein kinase C eta binding obo:GO_0005080 molecular_function obo:GO_0005080 GO:0005080 obo:GO_0005080 protein kinase C binding obo:GO_0005085 Stimulates the exchange of guanyl nucleotides associated with a GTPase. Under normal cellular physiological conditions, the concentration of GTP is higher than that of GDP, favoring the replacement of GDP by GTP in association with the GTPase. obo:GO_0005085 obo:go.owl obo:GO_0005085 GO:0008433 obo:GO_0005085 GO:0016219 obo:GO_0005085 GO:0019839 obo:GO_0005085 MIPS_funcat:18.02.03 obo:GO_0005085 Reactome:R-HSA-114544 obo:GO_0005085 Reactome:R-HSA-1168636 obo:GO_0005085 Reactome:R-HSA-1433415 obo:GO_0005085 Reactome:R-HSA-156913 obo:GO_0005085 Reactome:R-HSA-169904 obo:GO_0005085 Reactome:R-HSA-170979 obo:GO_0005085 Reactome:R-HSA-187746 obo:GO_0005085 Reactome:R-HSA-2029445 obo:GO_0005085 Reactome:R-HSA-2029451 obo:GO_0005085 Reactome:R-HSA-2029467 obo:GO_0005085 Reactome:R-HSA-203977 obo:GO_0005085 Reactome:R-HSA-205039 obo:GO_0005085 Reactome:R-HSA-2424476 obo:GO_0005085 Reactome:R-HSA-2485180 obo:GO_0005085 Reactome:R-HSA-2730840 obo:GO_0005085 Reactome:R-HSA-354173 obo:GO_0005085 Reactome:R-HSA-379044 obo:GO_0005085 Reactome:R-HSA-379048 obo:GO_0005085 Reactome:R-HSA-380073 obo:GO_0005085 Reactome:R-HSA-389348 obo:GO_0005085 Reactome:R-HSA-389350 obo:GO_0005085 Reactome:R-HSA-392195 obo:GO_0005085 Reactome:R-HSA-3928592 obo:GO_0005085 Reactome:R-HSA-3928612 obo:GO_0005085 Reactome:R-HSA-3928628 obo:GO_0005085 Reactome:R-HSA-3928632 obo:GO_0005085 Reactome:R-HSA-3928633 obo:GO_0005085 Reactome:R-HSA-3928642 obo:GO_0005085 Reactome:R-HSA-3928651 obo:GO_0005085 Reactome:R-HSA-392870 obo:GO_0005085 Reactome:R-HSA-3965444 obo:GO_0005085 Reactome:R-HSA-399995 obo:GO_0005085 Reactome:R-HSA-4093336 obo:GO_0005085 Reactome:R-HSA-416530 obo:GO_0005085 Reactome:R-HSA-418579 obo:GO_0005085 Reactome:R-HSA-420883 obo:GO_0005085 Reactome:R-HSA-428750 obo:GO_0005085 Reactome:R-HSA-428917 obo:GO_0005085 Reactome:R-HSA-442273 obo:GO_0005085 Reactome:R-HSA-442291 obo:GO_0005085 Reactome:R-HSA-442314 obo:GO_0005085 Reactome:R-HSA-445064 obo:GO_0005085 Reactome:R-HSA-5218829 obo:GO_0005085 Reactome:R-HSA-5218839 obo:GO_0005085 Reactome:R-HSA-5218850 obo:GO_0005085 Reactome:R-HSA-5694409 obo:GO_0005085 Reactome:R-HSA-6807868 obo:GO_0005085 Reactome:R-HSA-6811429 obo:GO_0005085 Reactome:R-HSA-749453 obo:GO_0005085 Reactome:R-HSA-751029 obo:GO_0005085 Reactome:R-HSA-825631 obo:GO_0005085 Reactome:R-HSA-8848618 obo:GO_0005085 Reactome:R-HSA-8850041 obo:GO_0005085 Reactome:R-HSA-8851827 obo:GO_0005085 Reactome:R-HSA-8851877 obo:GO_0005085 Reactome:R-HSA-8851899 obo:GO_0005085 Reactome:R-HSA-8875568 obo:GO_0005085 Reactome:R-HSA-8875591 obo:GO_0005085 Reactome:R-HSA-8964604 obo:GO_0005085 Reactome:R-HSA-8982637 obo:GO_0005085 Reactome:R-HSA-8982640 obo:GO_0005085 Reactome:R-HSA-939265 obo:GO_0005085 GDP-dissociation stimulator activity obo:GO_0005085 GDS obo:GO_0005085 GEF obo:GO_0005085 guanyl-nucleotide release factor activity obo:GO_0005085 guanyl-nucleotide releasing factor obo:GO_0005085 GNRP obo:GO_0005085 molecular_function obo:GO_0005085 GO:0005085 obo:GO_0005085 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0005085 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0005085 Note that guanyl-nucleotide exchange factor (GEF) activity alters binding affinity, but not GTPase catalytic activity directly. Therefore GO:0005085 is under 'regulation of GTPase activity' but is not a 'GTPase regulator', which is reserved for cases where the action of one gene product directly alters the rate of catalysis by another gene product. obo:GO_0005085 guanyl-nucleotide exchange factor activity obo:GO_0005086 Stimulates the exchange of guanyl nucleotides associated with the GTPase ARF. Under normal cellular physiological conditions, the concentration of GTP is higher than that of GDP, favoring the replacement of GDP by GTP in association with the GTPase. obo:GO_0005086 obo:go.owl obo:GO_0005086 Reactome:R-HSA-350769 obo:GO_0005086 Reactome:R-HSA-5623508 obo:GO_0005086 Reactome:R-HSA-6811414 obo:GO_0005086 Reactome:R-HSA-6811418 obo:GO_0005086 molecular_function obo:GO_0005086 GO:0005086 obo:GO_0005086 ARF guanyl-nucleotide exchange factor activity obo:GO_0005087 Stimulates the exchange of guanyl nucleotides associated with a GTPase of the Ran family. Under normal cellular physiological conditions, the concentration of GTP is higher than that of GDP, favoring the replacement of GDP by GTP in association with the GTPase. obo:GO_0005087 obo:go.owl obo:GO_0005087 Reactome:R-HSA-180687 obo:GO_0005087 Wikipedia:RCC1 obo:GO_0005087 RCC1 obo:GO_0005087 molecular_function obo:GO_0005087 GO:0005087 obo:GO_0005087 Ran guanyl-nucleotide exchange factor activity obo:GO_0005088 Stimulates the exchange of guanyl nucleotides associated with a GTPase of the Ras superfamily. Under normal cellular physiological conditions, the concentration of GTP is higher than that of GDP, favoring the replacement of GDP by GTP in association with the GTPase. obo:GO_0005088 obo:go.owl obo:GO_0005088 Reactome:R-HSA-109807 obo:GO_0005088 Reactome:R-HSA-109817 obo:GO_0005088 Reactome:R-HSA-1225951 obo:GO_0005088 Reactome:R-HSA-1225957 obo:GO_0005088 Reactome:R-HSA-1250383 obo:GO_0005088 Reactome:R-HSA-1250463 obo:GO_0005088 Reactome:R-HSA-1250498 obo:GO_0005088 Reactome:R-HSA-1306972 obo:GO_0005088 Reactome:R-HSA-1433471 obo:GO_0005088 Reactome:R-HSA-177938 obo:GO_0005088 Reactome:R-HSA-177945 obo:GO_0005088 Reactome:R-HSA-186834 obo:GO_0005088 Reactome:R-HSA-210977 obo:GO_0005088 Reactome:R-HSA-2179407 obo:GO_0005088 Reactome:R-HSA-2424477 obo:GO_0005088 Reactome:R-HSA-392054 obo:GO_0005088 Reactome:R-HSA-442732 obo:GO_0005088 Reactome:R-HSA-5637806 obo:GO_0005088 Reactome:R-HSA-5637808 obo:GO_0005088 Reactome:R-HSA-5654392 obo:GO_0005088 Reactome:R-HSA-5654402 obo:GO_0005088 Reactome:R-HSA-5654413 obo:GO_0005088 Reactome:R-HSA-5654426 obo:GO_0005088 Reactome:R-HSA-5654600 obo:GO_0005088 Reactome:R-HSA-5654618 obo:GO_0005088 Reactome:R-HSA-5654647 obo:GO_0005088 Reactome:R-HSA-5654663 obo:GO_0005088 Reactome:R-HSA-5655241 obo:GO_0005088 Reactome:R-HSA-5655277 obo:GO_0005088 Reactome:R-HSA-5655326 obo:GO_0005088 Reactome:R-HSA-5655347 obo:GO_0005088 Reactome:R-HSA-5672965 obo:GO_0005088 Reactome:R-HSA-5686071 obo:GO_0005088 Reactome:R-HSA-5686318 obo:GO_0005088 Reactome:R-HSA-8853307 obo:GO_0005088 Reactome:R-HSA-9026891 obo:GO_0005088 Reactome:R-HSA-9029158 obo:GO_0005088 Reactome:R-HSA-9032067 obo:GO_0005088 molecular_function obo:GO_0005088 GO:0005088 obo:GO_0005088 Ras guanyl-nucleotide exchange factor activity obo:GO_0005089 Stimulates the exchange of guanyl nucleotides associated with a GTPase of the Rho family. Under normal cellular physiological conditions, the concentration of GTP is higher than that of GDP, favoring the replacement of GDP by GTP in association with the GTPase. obo:GO_0005089 obo:go.owl obo:GO_0005089 Reactome:R-HSA-194518 obo:GO_0005089 Reactome:R-HSA-194913 obo:GO_0005089 Reactome:R-HSA-416588 obo:GO_0005089 Reactome:R-HSA-418850 obo:GO_0005089 Reactome:R-HSA-418856 obo:GO_0005089 Reactome:R-HSA-419166 obo:GO_0005089 Rho guanine nucleotide exchange factor obo:GO_0005089 RhoGEF obo:GO_0005089 molecular_function obo:GO_0005089 GO:0005089 obo:GO_0005089 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0005089 Rho guanyl-nucleotide exchange factor activity obo:GO_0005090 Stimulates the exchange of guanyl nucleotides associated with a GTPase of the Sar family. Under normal cellular physiological conditions, the concentration of GTP is higher than that of GDP, favoring the replacement of GDP by GTP in association with the GTPase. obo:GO_0005090 obo:go.owl obo:GO_0005090 molecular_function obo:GO_0005090 GO:0005090 obo:GO_0005090 Note that the name Sar derives from 'secretion-associated, Ras-related'. obo:GO_0005090 Sar guanyl-nucleotide exchange factor activity obo:GO_0005102 Interacting selectively and non-covalently with one or more specific sites on a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function. obo:GO_0005102 obo:go.owl obo:GO_0005102 receptor binding obo:GO_0005102 Wikipedia:Ligand_(biochemistry) obo:GO_0005102 receptor ligand obo:GO_0005102 molecular_function obo:GO_0005102 receptor-associated protein activity obo:GO_0005102 GO:0005102 obo:GO_0005102 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_agr obo:GO_0005102 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0005102 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_flybase_ribbon obo:GO_0005102 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_mouse obo:GO_0005102 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0005102 Where appropriate, also consider annotating to 'receptor agonist activity ; GO:0048018'. obo:GO_0005102 signaling receptor binding obo:GO_0005104 Interacting selectively and non-covalently with the fibroblast growth factor receptor (FGFR). obo:GO_0005104 obo:go.owl obo:GO_0005104 GO:0001521 obo:GO_0005104 GO:0005162 obo:GO_0005104 fibroblast growth factor obo:GO_0005104 FGF receptor binding obo:GO_0005104 FGFR binding obo:GO_0005104 FGFR ligand obo:GO_0005104 fibroblast growth factor receptor ligand obo:GO_0005104 molecular_function obo:GO_0005104 GO:0005104 obo:GO_0005104 Note that branchless is the Drosophila gene encoding fibroblast growth factor. obo:GO_0005104 fibroblast growth factor receptor binding obo:GO_0005105 Interacting selectively and non-covalently with the type 1 fibroblast growth factor receptor (FGFR1). obo:GO_0005105 obo:go.owl obo:GO_0005105 FGFR1 binding obo:GO_0005105 FGFR1 ligand obo:GO_0005105 breathless binding obo:GO_0005105 breathless ligand obo:GO_0005105 type 1 fibroblast growth factor receptor ligand obo:GO_0005105 molecular_function obo:GO_0005105 GO:0005105 obo:GO_0005105 Note that breathless is the Drosophila gene encoding the type 1 fibroblast growth factor receptor (FGFR1). obo:GO_0005105 type 1 fibroblast growth factor receptor binding obo:GO_0005109 Interacting selectively and non-covalently with a frizzled (fz) receptor. obo:GO_0005109 obo:go.owl obo:GO_0005109 GO:0005110 obo:GO_0005109 fz binding obo:GO_0005109 frizzled ligand obo:GO_0005109 frizzled-2 binding obo:GO_0005109 frizzled-2 ligand obo:GO_0005109 fz ligand obo:GO_0005109 fz2 binding obo:GO_0005109 fz2 ligand obo:GO_0005109 molecular_function obo:GO_0005109 GO:0005109 obo:GO_0005109 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0005109 frizzled binding obo:GO_0005111 Interacting selectively and non-covalently with the type 2 fibroblast growth factor receptor (FGFR2). obo:GO_0005111 obo:go.owl obo:GO_0005111 FGFR2 binding obo:GO_0005111 heartless binding obo:GO_0005111 FGFR2 ligand obo:GO_0005111 heartless ligand obo:GO_0005111 type 2 fibroblast growth factor receptor ligand obo:GO_0005111 molecular_function obo:GO_0005111 GO:0005111 obo:GO_0005111 Note that heartless is the Drosophila gene encoding the type 2 fibroblast growth factor receptor (FGFR2). obo:GO_0005111 type 2 fibroblast growth factor receptor binding obo:GO_0005112 Interacting selectively and non-covalently with the Notch (N) protein, a surface receptor. obo:GO_0005112 obo:go.owl obo:GO_0005112 N binding obo:GO_0005112 Notch receptor binding obo:GO_0005112 N ligand obo:GO_0005112 Notch ligand obo:GO_0005112 molecular_function obo:GO_0005112 GO:0005112 obo:GO_0005112 Notch binding obo:GO_0005113 Interacting selectively and non-covalently with the patched (ptc) protein, a receptor for hedgehog proteins. obo:GO_0005113 obo:go.owl obo:GO_0005113 ptc binding obo:GO_0005113 patched ligand obo:GO_0005113 ptc ligand obo:GO_0005113 molecular_function obo:GO_0005113 GO:0005113 obo:GO_0005113 patched binding obo:GO_0005114 Interacting selectively and non-covalently with a type II transforming growth factor beta receptor. obo:GO_0005114 obo:go.owl obo:GO_0005114 TGF-beta type II binding obo:GO_0005114 transforming growth factor beta receptor type II binding obo:GO_0005114 type II TGF-beta binding obo:GO_0005114 punt binding obo:GO_0005114 punt ligand obo:GO_0005114 molecular_function obo:GO_0005114 transforming growth factor beta ligand binding to type II receptor obo:GO_0005114 GO:0005114 obo:GO_0005114 type II transforming growth factor beta receptor binding obo:GO_0005115 Interacting selectively and non-covalently with the receptor tyrosine kinase-like orphan receptor (Ror). obo:GO_0005115 obo:go.owl obo:GO_0005115 Ror binding obo:GO_0005115 receptor tyrosine kinase-like orphan receptor ligand obo:GO_0005115 molecular_function obo:GO_0005115 Ror ligand obo:GO_0005115 GO:0005115 obo:GO_0005115 receptor tyrosine kinase-like orphan receptor binding obo:GO_0005117 Interacting selectively and non-covalently with wishful thinking (Wit), a type II bone morphogenic protein receptor. obo:GO_0005117 obo:go.owl obo:GO_0005117 Wit binding obo:GO_0005117 SE20 receptor binding obo:GO_0005117 Wit ligand obo:GO_0005117 wishful thinking ligand obo:GO_0005117 molecular_function obo:GO_0005117 GO:0005117 obo:GO_0005117 wishful thinking binding obo:GO_0005118 Interacting selectively and non-covalently with the sevenless (sev) protein, a receptor tyrosine kinase. obo:GO_0005118 obo:go.owl obo:GO_0005118 sev binding obo:GO_0005118 sev ligand obo:GO_0005118 sevenless ligand obo:GO_0005118 molecular_function obo:GO_0005118 GO:0005118 obo:GO_0005118 sevenless binding obo:GO_0005119 Interacting selectively and non-covalently with the smoothened (smo) protein, which interacts with patched to transmit hedgehog signals. obo:GO_0005119 obo:go.owl obo:GO_0005119 smo binding obo:GO_0005119 smo ligand obo:GO_0005119 smoothened ligand obo:GO_0005119 molecular_function obo:GO_0005119 GO:0005119 obo:GO_0005119 smoothened binding obo:GO_0005121 Interacting selectively and non-covalently with the Toll protein, a transmembrane receptor. obo:GO_0005121 obo:go.owl obo:GO_0005121 Tl binding obo:GO_0005121 Toll receptor binding obo:GO_0005121 Toll ligand obo:GO_0005121 molecular_function obo:GO_0005121 GO:0005121 obo:GO_0005121 Toll binding obo:GO_0005122 Interacting selectively and non-covalently with the torso (tor) protein, a receptor tyrosine kinase. obo:GO_0005122 obo:go.owl obo:GO_0005122 tor binding obo:GO_0005122 tor ligand obo:GO_0005122 torso ligand obo:GO_0005122 molecular_function obo:GO_0005122 GO:0005122 obo:GO_0005122 torso binding obo:GO_0005123 Interacting selectively and non-covalently with any member of the death receptor (DR) family. The DR family falls within the tumor necrosis factor receptor superfamily and is characterized by a cytoplasmic region of ~80 residues termed the death domain (DD). obo:GO_0005123 obo:go.owl obo:GO_0005123 APO binding obo:GO_0005123 DR binding obo:GO_0005123 EDAR binding obo:GO_0005123 FAS binding obo:GO_0005123 KILLER binding obo:GO_0005123 NGFR binding obo:GO_0005123 TNFR1 binding obo:GO_0005123 TRAIL binding obo:GO_0005123 death receptor ligand obo:GO_0005123 molecular_function obo:GO_0005123 death receptor adaptor protein activity obo:GO_0005123 death receptor interacting protein activity obo:GO_0005123 death receptor-associated factor activity obo:GO_0005123 GO:0005123 obo:GO_0005123 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0005123 death receptor binding obo:GO_0005124 Interacting selectively and non-covalently with scavenger receptors, a family of proteins that are expressed on myeloid cells and are involved in the uptake of effete cellular components and foreign particles. obo:GO_0005124 obo:go.owl obo:GO_0005124 scavenger receptor ligand obo:GO_0005124 molecular_function obo:GO_0005124 GO:0005124 obo:GO_0005124 scavenger receptor binding obo:GO_0005125 Functions to control the survival, growth, differentiation and effector function of tissues and cells. obo:GO_0005125 obo:go.owl obo:GO_0005125 MIPS_funcat:40.02.03.01 obo:GO_0005125 molecular_function obo:GO_0005125 autocrine activity obo:GO_0005125 paracrine activity obo:GO_0005125 GO:0005125 obo:GO_0005125 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0005125 Also consider annotating to 'receptor agonist activity ; GO:0048018'. obo:GO_0005125 cytokine activity obo:GO_0005126 Interacting selectively and non-covalently with a cytokine receptor. obo:GO_0005126 obo:go.owl obo:GO_0005126 hematopoietin/interferon-class (D200-domain) cytokine receptor binding obo:GO_0005126 hematopoietin/interferon-class (D200-domain) cytokine receptor ligand obo:GO_0005126 molecular_function obo:GO_0005126 GO:0005126 obo:GO_0005126 cytokine receptor binding obo:GO_0005127 Interacting selectively and non-covalently with the ciliary neurotrophic factor receptor. obo:GO_0005127 obo:go.owl obo:GO_0005127 ciliary neurotrophic factor obo:GO_0005127 ciliary neurotrophic factor receptor ligand obo:GO_0005127 molecular_function obo:GO_0005127 GO:0005127 obo:GO_0005127 ciliary neurotrophic factor receptor binding obo:GO_0005128 Interacting selectively and non-covalently with the erythropoietin receptor. obo:GO_0005128 obo:go.owl obo:GO_0005128 erythropoietin obo:GO_0005128 erythropoietin receptor ligand obo:GO_0005128 molecular_function obo:GO_0005128 GO:0005128 obo:GO_0005128 erythropoietin receptor binding obo:GO_0005129 Interacting selectively and non-covalently with the granulocyte macrophage colony-stimulating factor receptor. obo:GO_0005129 obo:go.owl obo:GO_0005129 GM-CSF receptor binding obo:GO_0005129 granulocyte macrophage colony stimulating factor receptor binding obo:GO_0005129 GM-CSF receptor ligand obo:GO_0005129 GMC-SF receptor ligand obo:GO_0005129 granulocyte macrophage colony-stimulating factor obo:GO_0005129 granulocyte macrophage colony-stimulating factor receptor ligand obo:GO_0005129 molecular_function obo:GO_0005129 GO:0005129 obo:GO_0005129 granulocyte macrophage colony-stimulating factor receptor binding obo:GO_0005130 Interacting selectively and non-covalently with the granulocyte colony-stimulating factor receptor. obo:GO_0005130 obo:go.owl obo:GO_0005130 G-CSF receptor ligand obo:GO_0005130 GC-SF receptor ligand obo:GO_0005130 granulocyte colony stimulating factor receptor binding obo:GO_0005130 granulocyte colony-stimulating factor obo:GO_0005130 granulocyte colony-stimulating factor receptor ligand obo:GO_0005130 molecular_function obo:GO_0005130 GO:0005130 obo:GO_0005130 granulocyte colony-stimulating factor receptor binding obo:GO_0005131 Interacting selectively and non-covalently with the growth hormone receptor. obo:GO_0005131 obo:go.owl obo:GO_0005131 growth hormone obo:GO_0005131 growth hormone receptor ligand obo:GO_0005131 molecular_function obo:GO_0005131 GO:0005131 obo:GO_0005131 growth hormone receptor binding obo:GO_0005132 Interacting selectively and non-covalently with an interferon-type I receptor, a heterodimeric complex composed of an alpha subunit (IFNAR1) and a beta subunit (IFNAR2). obo:GO_0005132 obo:go.owl obo:GO_0005132 interferon-alpha/beta receptor binding obo:GO_0005132 IFNAR1 binding obo:GO_0005132 IFNAR2 binding obo:GO_0005132 interferon-alpha/beta obo:GO_0005132 interferon-alpha/beta receptor ligand obo:GO_0005132 molecular_function obo:GO_0005132 IFNAR binding obo:GO_0005132 GO:0005132 obo:GO_0005132 type I interferon receptor binding obo:GO_0005133 Interacting selectively and non-covalently with the interferon-gamma receptor. obo:GO_0005133 obo:go.owl obo:GO_0005133 interferon-gamma obo:GO_0005133 interferon-gamma receptor ligand obo:GO_0005133 molecular_function obo:GO_0005133 GO:0005133 obo:GO_0005133 interferon-gamma receptor binding obo:GO_0005134 Interacting selectively and non-covalently with the interleukin-2 receptor. obo:GO_0005134 obo:go.owl obo:GO_0005134 IL-2 obo:GO_0005134 interleukin-2 receptor ligand obo:GO_0005134 molecular_function obo:GO_0005134 GO:0005134 obo:GO_0005134 interleukin-2 receptor binding obo:GO_0005135 Interacting selectively and non-covalently with the interleukin-3 receptor. obo:GO_0005135 obo:go.owl obo:GO_0005135 IL-3 obo:GO_0005135 interleukin-3 receptor ligand obo:GO_0005135 molecular_function obo:GO_0005135 GO:0005135 obo:GO_0005135 interleukin-3 receptor binding obo:GO_0005136 Interacting selectively and non-covalently with the interleukin-4 receptor. obo:GO_0005136 obo:go.owl obo:GO_0005136 IL-4 obo:GO_0005136 interleukin-4 receptor ligand obo:GO_0005136 molecular_function obo:GO_0005136 GO:0005136 obo:GO_0005136 interleukin-4 receptor binding obo:GO_0005137 Interacting selectively and non-covalently with the interleukin-5 receptor. obo:GO_0005137 obo:go.owl obo:GO_0005137 IL-5 obo:GO_0005137 interleukin-5 receptor ligand obo:GO_0005137 molecular_function obo:GO_0005137 GO:0005137 obo:GO_0005137 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0005137 interleukin-5 receptor binding obo:GO_0005138 Interacting selectively and non-covalently with the interleukin-6 receptor. obo:GO_0005138 obo:go.owl obo:GO_0005138 IL-6 obo:GO_0005138 interleukin-6 receptor ligand obo:GO_0005138 molecular_function obo:GO_0005138 GO:0005138 obo:GO_0005138 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0005138 interleukin-6 receptor binding obo:GO_0005139 Interacting selectively and non-covalently with the interleukin-7 receptor. obo:GO_0005139 obo:go.owl obo:GO_0005139 IL-7 obo:GO_0005139 interleukin-7 receptor ligand obo:GO_0005139 molecular_function obo:GO_0005139 GO:0005139 obo:GO_0005139 interleukin-7 receptor binding obo:GO_0005140 Interacting selectively and non-covalently with the interleukin-9 receptor. obo:GO_0005140 obo:go.owl obo:GO_0005140 IL-9 obo:GO_0005140 interleukin-9 receptor ligand obo:GO_0005140 molecular_function obo:GO_0005140 GO:0005140 obo:GO_0005140 interleukin-9 receptor binding obo:GO_0005141 Interacting selectively and non-covalently with the interleukin-10 receptor. obo:GO_0005141 obo:go.owl obo:GO_0005141 IL-10 obo:GO_0005141 interleukin-10 receptor ligand obo:GO_0005141 molecular_function obo:GO_0005141 GO:0005141 obo:GO_0005141 interleukin-10 receptor binding obo:GO_0005142 Interacting selectively and non-covalently with the interleukin-11 receptor. obo:GO_0005142 obo:go.owl obo:GO_0005142 IL-11 obo:GO_0005142 interleukin-11 receptor ligand obo:GO_0005142 molecular_function obo:GO_0005142 GO:0005142 obo:GO_0005142 interleukin-11 receptor binding obo:GO_0005143 Interacting selectively and non-covalently with the interleukin-12 receptor. obo:GO_0005143 obo:go.owl obo:GO_0005143 IL-12 obo:GO_0005143 interleukin-12 receptor ligand obo:GO_0005143 molecular_function obo:GO_0005143 GO:0005143 obo:GO_0005143 interleukin-12 receptor binding obo:GO_0005144 Interacting selectively and non-covalently with the interleukin-13 receptor. obo:GO_0005144 obo:go.owl obo:GO_0005144 IL-13 obo:GO_0005144 interleukin-13 receptor ligand obo:GO_0005144 molecular_function obo:GO_0005144 GO:0005144 obo:GO_0005144 interleukin-13 receptor binding obo:GO_0005145 Interacting selectively and non-covalently with the interleukin-14 receptor. obo:GO_0005145 obo:go.owl obo:GO_0005145 IL-14 obo:GO_0005145 interleukin-14 receptor ligand obo:GO_0005145 molecular_function obo:GO_0005145 GO:0005145 obo:GO_0005145 interleukin-14 receptor binding obo:GO_0005146 Interacting selectively and non-covalently with the leukemia inhibitory factor receptor. obo:GO_0005146 obo:go.owl obo:GO_0005146 leukemia inhibitory factor obo:GO_0005146 leukemia inhibitory factor receptor ligand obo:GO_0005146 molecular_function obo:GO_0005146 GO:0005146 obo:GO_0005146 leukemia inhibitory factor receptor binding obo:GO_0005147 Interacting selectively and non-covalently with the oncostatin-M receptor. obo:GO_0005147 obo:go.owl obo:GO_0005147 oncostatin-M obo:GO_0005147 oncostatin-M receptor ligand obo:GO_0005147 molecular_function obo:GO_0005147 GO:0005147 obo:GO_0005147 oncostatin-M receptor binding obo:GO_0005148 Interacting selectively and non-covalently with the prolactin receptor. obo:GO_0005148 obo:go.owl obo:GO_0005148 prolactin obo:GO_0005148 prolactin receptor ligand obo:GO_0005148 molecular_function obo:GO_0005148 GO:0005148 obo:GO_0005148 prolactin receptor binding obo:GO_0005149 Interacting selectively and non-covalently with the interleukin-1 receptor. obo:GO_0005149 obo:go.owl obo:GO_0005149 IL-1 obo:GO_0005149 interleukin-1 receptor ligand obo:GO_0005149 molecular_function obo:GO_0005149 GO:0005149 obo:GO_0005149 interleukin-1 receptor binding obo:GO_0005150 Interacting selectively and non-covalently with a Type I interleukin-1 receptor. obo:GO_0005150 obo:go.owl obo:GO_0005150 IL-1 type I obo:GO_0005150 interleukin-1, type I receptor ligand obo:GO_0005150 molecular_function obo:GO_0005150 GO:0005150 obo:GO_0005150 interleukin-1, type I receptor binding obo:GO_0005151 Interacting selectively and non-covalently with a Type II interleukin-1 receptor. obo:GO_0005151 obo:go.owl obo:GO_0005151 IL-1 type II obo:GO_0005151 interleukin-1, type II receptor ligand obo:GO_0005151 molecular_function obo:GO_0005151 GO:0005151 obo:GO_0005151 interleukin-1, type II receptor binding obo:GO_0005152 Blocks the binding of interleukin-1 to the interleukin-1 receptor complex. obo:GO_0005152 obo:go.owl obo:GO_0005152 IL-1ra obo:GO_0005152 molecular_function obo:GO_0005152 GO:0005152 obo:GO_0005152 interleukin-1 receptor antagonist activity obo:GO_0005153 Interacting selectively and non-covalently with the interleukin-8 receptor. obo:GO_0005153 obo:go.owl obo:GO_0005153 IL-8 obo:GO_0005153 interleukin-8 receptor ligand obo:GO_0005153 molecular_function obo:GO_0005153 GO:0005153 obo:GO_0005153 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0005153 interleukin-8 receptor binding obo:GO_0005154 Interacting selectively and non-covalently with the epidermal growth factor receptor. obo:GO_0005154 obo:go.owl obo:GO_0005154 GO:0008185 obo:GO_0005154 EGF receptor binding obo:GO_0005154 EGFR binding obo:GO_0005154 TGF-alpha receptor binding obo:GO_0005154 TGFalpha receptor binding obo:GO_0005154 transforming growth factor alpha receptor binding obo:GO_0005154 EGF obo:GO_0005154 EGF receptor ligand obo:GO_0005154 epidermal growth factor obo:GO_0005154 epidermal growth factor receptor ligand obo:GO_0005154 transforming growth factor alpha obo:GO_0005154 transforming growth factor alpha receptor ligand obo:GO_0005154 molecular_function obo:GO_0005154 GO:0005154 obo:GO_0005154 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0005154 epidermal growth factor receptor binding obo:GO_0005157 Interacting selectively and non-covalently with the macrophage colony-stimulating factor receptor. obo:GO_0005157 obo:go.owl obo:GO_0005157 M-CSF receptor binding obo:GO_0005157 macrophage colony stimulating factor receptor binding obo:GO_0005157 macrophage colony-stimulating factor receptor ligand obo:GO_0005157 molecular_function obo:GO_0005157 GO:0005157 obo:GO_0005157 macrophage colony-stimulating factor receptor binding obo:GO_0005158 Interacting selectively and non-covalently with the insulin receptor. obo:GO_0005158 obo:go.owl obo:GO_0005158 insulin receptor ligand obo:GO_0005158 molecular_function obo:GO_0005158 GO:0005158 obo:GO_0005158 insulin receptor binding obo:GO_0005159 Interacting selectively and non-covalently with the insulin-like growth factor receptor. obo:GO_0005159 obo:go.owl obo:GO_0005159 GO:0005067 obo:GO_0005159 IGF receptor binding obo:GO_0005159 insulin-like growth factor obo:GO_0005159 insulin-like growth factor receptor ligand obo:GO_0005159 molecular_function obo:GO_0005159 GO:0005159 obo:GO_0005159 insulin-like growth factor receptor binding obo:GO_0005160 Interacting selectively and non-covalently with the transforming growth factor beta receptor. obo:GO_0005160 obo:go.owl obo:GO_0005160 Reactome:R-HSA-170861 obo:GO_0005160 TGF-beta receptor binding obo:GO_0005160 TGFbeta receptor binding obo:GO_0005160 transforming growth factor beta obo:GO_0005160 transforming growth factor beta receptor ligand obo:GO_0005160 molecular_function obo:GO_0005160 activin obo:GO_0005160 inhibin obo:GO_0005160 transforming growth factor beta ligand binding to type I receptor obo:GO_0005160 transforming growth factor beta ligand binding to type II receptor obo:GO_0005160 transforming growth factor beta receptor anchoring activity obo:GO_0005160 GO:0005160 obo:GO_0005160 transforming growth factor beta receptor binding obo:GO_0005161 Interacting selectively and non-covalently with the platelet-derived growth factor receptor. obo:GO_0005161 obo:go.owl obo:GO_0005161 PDGF receptor binding obo:GO_0005161 PDGFR binding obo:GO_0005161 PDGF obo:GO_0005161 platelet-derived growth factor obo:GO_0005161 platelet-derived growth factor receptor ligand obo:GO_0005161 molecular_function obo:GO_0005161 GO:0005161 obo:GO_0005161 platelet-derived growth factor receptor binding obo:GO_0005163 Interacting selectively and non-covalently with the nerve growth factor receptor. obo:GO_0005163 obo:go.owl obo:GO_0005163 NGF receptor binding obo:GO_0005163 nerve growth factor receptor ligand obo:GO_0005163 neurotrophin obo:GO_0005163 molecular_function obo:GO_0005163 GO:0005163 obo:GO_0005163 nerve growth factor receptor binding obo:GO_0005164 Interacting selectively and non-covalently with the tumor necrosis factor receptor. obo:GO_0005164 obo:go.owl obo:GO_0005164 TNF receptor binding obo:GO_0005164 tumor necrosis factor obo:GO_0005164 tumor necrosis factor receptor ligand obo:GO_0005164 molecular_function obo:GO_0005164 GO:0005164 obo:GO_0005164 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0005164 tumor necrosis factor receptor binding obo:GO_0005165 Interacting selectively and non-covalently with a neurotrophin receptor. obo:GO_0005165 obo:go.owl obo:GO_0005165 neurotrophin obo:GO_0005165 neurotrophin receptor ligand obo:GO_0005165 molecular_function obo:GO_0005165 GO:0005165 obo:GO_0005165 neurotrophin receptor binding obo:GO_0005166 Interacting selectively and non-covalently with the neurotrophin p75 receptor. obo:GO_0005166 obo:go.owl obo:GO_0005166 neurotrophin p75 receptor ligand obo:GO_0005166 molecular_function obo:GO_0005166 GO:0005166 obo:GO_0005166 neurotrophin p75 receptor binding obo:GO_0005167 Interacting selectively and non-covalently with a neurotrophin TRK receptor. obo:GO_0005167 obo:go.owl obo:GO_0005167 neurotrophin TRK receptor ligand obo:GO_0005167 molecular_function obo:GO_0005167 GO:0005167 obo:GO_0005167 neurotrophin TRK receptor binding obo:GO_0005168 Interacting selectively and non-covalently with the neurotrophin TRKA receptor. obo:GO_0005168 obo:go.owl obo:GO_0005168 neurotrophin TRKA receptor ligand obo:GO_0005168 molecular_function obo:GO_0005168 GO:0005168 obo:GO_0005168 neurotrophin TRKA receptor binding obo:GO_0005169 Interacting selectively and non-covalently with the neurotrophin TRKB receptor. obo:GO_0005169 obo:go.owl obo:GO_0005169 neurotrophin TRKB receptor ligand obo:GO_0005169 molecular_function obo:GO_0005169 GO:0005169 obo:GO_0005169 neurotrophin TRKB receptor binding obo:GO_0005170 Interacting selectively and non-covalently with the neurotrophin TRKC receptor. obo:GO_0005170 obo:go.owl obo:GO_0005170 neurotrophin TRKC receptor ligand obo:GO_0005170 molecular_function obo:GO_0005170 GO:0005170 obo:GO_0005170 neurotrophin TRKC receptor binding obo:GO_0005171 Interacting selectively and non-covalently with the hepatocyte growth factor receptor. obo:GO_0005171 obo:go.owl obo:GO_0005171 HGF receptor binding obo:GO_0005171 hepatocyte growth factor obo:GO_0005171 hepatocyte growth factor receptor ligand obo:GO_0005171 molecular_function obo:GO_0005171 GO:0005171 obo:GO_0005171 hepatocyte growth factor receptor binding obo:GO_0005172 Interacting selectively and non-covalently with any vascular endothelial growth factor receptor. obo:GO_0005172 obo:go.owl obo:GO_0005172 VEGF receptor binding obo:GO_0005172 VEGFR binding obo:GO_0005172 vascular endothelial growth factor obo:GO_0005172 vascular endothelial growth factor receptor ligand obo:GO_0005172 molecular_function obo:GO_0005172 GO:0005172 obo:GO_0005172 vascular endothelial growth factor receptor binding obo:GO_0005173 Interacting selectively and non-covalently with the stem cell factor receptor (SCFR), a type III transmembrane kinase receptor. obo:GO_0005173 obo:go.owl obo:GO_0005173 SCFR binding obo:GO_0005173 KIT binding obo:GO_0005173 SCF obo:GO_0005173 stem cell factor obo:GO_0005173 stem cell factor receptor ligand obo:GO_0005173 molecular_function obo:GO_0005173 GO:0005173 obo:GO_0005173 stem cell factor receptor binding obo:GO_0005174 Interacting selectively and non-covalently with CD40, a receptor found on the surface of all B-lymphocytes. obo:GO_0005174 obo:go.owl obo:GO_0005174 molecular_function obo:GO_0005174 GO:0005174 obo:GO_0005174 CD40 receptor binding obo:GO_0005175 Interacting selectively and non-covalently with a CD27, a receptor found on the surface of T cells and some B cells and NK cells. obo:GO_0005175 obo:go.owl obo:GO_0005175 molecular_function obo:GO_0005175 GO:0005175 obo:GO_0005175 CD27 receptor binding obo:GO_0005176 Interacting selectively and non-covalently with the protein-tyrosine kinase receptor Neu/ErbB-2/HER2. obo:GO_0005176 obo:go.owl obo:GO_0005176 HER2 receptor binding obo:GO_0005176 Neu receptor binding obo:GO_0005176 ErbB-2 class receptor ligand obo:GO_0005176 HER2 receptor ligand obo:GO_0005176 Neu receptor ligand obo:GO_0005176 molecular_function obo:GO_0005176 GO:0005176 obo:GO_0005176 ErbB-2 class receptor binding obo:GO_0005178 Interacting selectively and non-covalently with an integrin. obo:GO_0005178 obo:go.owl obo:GO_0005178 integrin ligand obo:GO_0005178 molecular_function obo:GO_0005178 GO:0005178 obo:GO_0005178 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0005178 integrin binding obo:GO_0005179 The action characteristic of a hormone, any substance formed in very small amounts in one specialized organ or group of cells and carried (sometimes in the bloodstream) to another organ or group of cells in the same organism, upon which it has a specific regulatory action. The term was originally applied to agents with a stimulatory physiological action in vertebrate animals (as opposed to a chalone, which has a depressant action). Usage is now extended to regulatory compounds in lower animals and plants, and to synthetic substances having comparable effects; all bind receptors and trigger some biological process. obo:GO_0005179 obo:go.owl obo:GO_0005179 cAMP generating peptide activity obo:GO_0005179 glycopeptide hormone obo:GO_0005179 lipopeptide hormone obo:GO_0005179 peptide hormone obo:GO_0005179 molecular_function obo:GO_0005179 GO:0005179 obo:GO_0005179 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0005179 Also consider annotating to 'receptor agonist activity ; GO:0048018'. obo:GO_0005179 hormone activity obo:GO_0005183 The action characteristic of gonadotropin hormone-releasing hormone (GnRH), any of a family of decapeptide amide hormones that are released by the hypothalamus in response to neural and/or chemical stimuli. In at least mammals, upon receptor binding, GnRH causes the release of follicle-stimulating hormone (FSH) and luteinizing hormone (LH) by the anterior pituitary. obo:GO_0005183 obo:go.owl obo:GO_0005183 GnRH activity obo:GO_0005183 LH/FSH-RF obo:GO_0005183 LHRH activity obo:GO_0005183 gonadotrophin hormone-releasing hormone activity obo:GO_0005183 luteinizing hormone-releasing factor activity obo:GO_0005183 luteinizing hormone-releasing hormone activity obo:GO_0005183 luteinizing hormone/follicle-stimulating hormone releasing factor activity obo:GO_0005183 molecular_function obo:GO_0005183 GO:0005183 obo:GO_0005183 gonadotropin hormone-releasing hormone activity obo:GO_0005184 The action characteristic of a neuropeptide hormone, any peptide hormone that acts in the central nervous system. A neuropeptide is any of several types of molecules found in brain tissue, composed of short chains of amino acids; they include endorphins, enkephalins, vasopressin, and others. They are often localized in axon terminals at synapses and are classified as putative neurotransmitters, although some are also hormones. obo:GO_0005184 obo:go.owl obo:GO_0005184 Wikipedia:Neurohormone obo:GO_0005184 neurohormone obo:GO_0005184 molecular_function obo:GO_0005184 GO:0005184 obo:GO_0005184 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0005184 neuropeptide hormone activity obo:GO_0005185 The action characteristic of a neurohypophyseal hormone, any of a family of structurally and functionally related nonapeptides that are synthesized as part of a larger precursor molecule comprising a signal peptide, the nonapeptide hormone, and a neurophysin. obo:GO_0005185 obo:go.owl obo:GO_0005185 neurohypophysial hormone activity obo:GO_0005185 molecular_function obo:GO_0005185 GO:0005185 obo:GO_0005185 neurohypophyseal hormone activity obo:GO_0005186 The activity of binding to and activating specific cell surface receptors, thereby inducing behavioral, developmental, or physiological response(s) from a responding organism or cell. The substance may be released or retained on the cell surface. Pheromones may serve as a specific attractant, social communicator, or sexual stimulant. obo:GO_0005186 obo:go.owl obo:GO_0005186 molecular_function obo:GO_0005186 GO:0005186 obo:GO_0005186 Also consider annotating to 'receptor agonist activity ; GO:0048018'. obo:GO_0005186 pheromone activity obo:GO_0005484 Acting as a marker to identify a membrane and interacting selectively with one or more SNAREs on another membrane to mediate membrane fusion. obo:GO_0005484 obo:go.owl obo:GO_0005484 GO:0005485 obo:GO_0005484 GO:0005486 obo:GO_0005484 SNARE obo:GO_0005484 Q-SNARE activity obo:GO_0005484 R-SNARE activity obo:GO_0005484 SNAP-25 obo:GO_0005484 t-SNARE activity obo:GO_0005484 v-SNARE activity obo:GO_0005484 molecular_function obo:GO_0005484 GO:0005484 obo:GO_0005484 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0005484 SNAP receptor activity obo:GO_0005488 The selective, non-covalent, often stoichiometric, interaction of a molecule with one or more specific sites on another molecule. obo:GO_0005488 obo:go.owl obo:GO_0005488 Wikipedia:Binding_(molecular) obo:GO_0005488 ligand obo:GO_0005488 molecular_function obo:GO_0005488 GO:0005488 obo:GO_0005488 http://purl.oboInOwllibrary.org/oboInOwl/go#gocheck_do_not_manually_annotate obo:GO_0005488 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0005488 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0005488 Note that this term is in the subset of terms that should not be used for direct, manual gene product annotation. Please choose a more specific child term, or request a new one if no suitable term is available. For ligands that bind to signal transducing receptors, consider the molecular function term 'receptor binding ; GO:0005102' and its children. obo:GO_0005488 binding obo:GO_0005496 Interacting selectively and non-covalently with a steroid, any of a large group of substances that have in common a ring system based on 1,2-cyclopentanoperhydrophenanthrene. obo:GO_0005496 obo:go.owl obo:GO_0005496 molecular_function obo:GO_0005496 GO:0005496 obo:GO_0005496 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0005496 steroid binding obo:GO_0005497 Interacting selectively and non-covalently with any androgen, male sex hormones. obo:GO_0005497 obo:go.owl obo:GO_0005497 molecular_function obo:GO_0005497 GO:0005497 obo:GO_0005497 androgen binding obo:GO_0005499 Interacting selectively and non-covalently with vitamin D, any of a group of related, fat-soluble compounds that are derived from delta-5,7 steroids and play a central role in calcium metabolism. Specific forms of vitamin D include calciferol (ergocalciferol; vitamin D2) and cholecalciferol (calciol; vitamin D3). obo:GO_0005499 obo:go.owl obo:GO_0005499 calciferol binding obo:GO_0005499 cholecalciferol binding obo:GO_0005499 ergocalciferol binding obo:GO_0005499 molecular_function obo:GO_0005499 GO:0005499 obo:GO_0005499 vitamin D binding obo:GO_0005500 Interacting selectively and non-covalently with juvenile hormone, the three sesquiterpenoid derivatives that function to maintain the larval state of insects at molting and that may be required for other processes, e.g. oogenesis. obo:GO_0005500 obo:go.owl obo:GO_0005500 molecular_function obo:GO_0005500 GO:0005500 obo:GO_0005500 juvenile hormone binding obo:GO_0005501 Interacting selectively and non-covalently with retinoids, any member of a class of isoprenoids that contain or are derived from four prenyl groups linked head-to-tail. Retinoids include retinol and retinal and structurally similar natural derivatives or synthetic compounds, but need not have vitamin A activity. obo:GO_0005501 obo:go.owl obo:GO_0005501 Reactome:R-HSA-2454113 obo:GO_0005501 Reactome:R-HSA-2464809 obo:GO_0005501 Reactome:R-HSA-2465934 obo:GO_0005501 Reactome:R-HSA-2465938 obo:GO_0005501 molecular_function obo:GO_0005501 GO:0005501 obo:GO_0005501 retinoid binding obo:GO_0005502 Interacting selectively and non-covalently with 11-cis retinal, an isomer of retinal that plays an important role in the visual process in most vertebrates. 11-cis retinal combines with opsin in the rods (scotopsin) to form rhodopsin or visual purple. Retinal is one of the three compounds that makes up vitamin A. obo:GO_0005502 obo:go.owl obo:GO_0005502 vitamin A binding obo:GO_0005502 11-cis retinaldehyde binding obo:GO_0005502 11-cis-retinal binding obo:GO_0005502 molecular_function obo:GO_0005502 GO:0005502 obo:GO_0005502 11-cis retinal binding obo:GO_0005503 Interacting selectively and non-covalently with all-trans retinal, a compound that plays an important role in the visual process in most vertebrates. All-trans retinal (trans r., visual yellow) results from the bleaching of rhodopsin by light, in which the 11-cis form is converted to the all-trans form. Retinal is one of the forms of vitamin A. obo:GO_0005503 obo:go.owl obo:GO_0005503 vitamin A binding obo:GO_0005503 all-trans retinaldehyde binding obo:GO_0005503 trans retinal binding obo:GO_0005503 visual yellow binding obo:GO_0005503 molecular_function obo:GO_0005503 xanthopsin obo:GO_0005503 GO:0005503 obo:GO_0005503 all-trans retinal binding obo:GO_0005504 Interacting selectively and non-covalently with fatty acids, aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis. obo:GO_0005504 obo:go.owl obo:GO_0005504 MIPS_funcat:16.13.03 obo:GO_0005504 molecular_function obo:GO_0005504 GO:0005504 obo:GO_0005504 fatty acid binding obo:GO_0005506 Interacting selectively and non-covalently with iron (Fe) ions. obo:GO_0005506 obo:go.owl obo:GO_0005506 iron binding obo:GO_0005506 molecular_function obo:GO_0005506 GO:0005506 obo:GO_0005506 iron ion binding obo:GO_0005507 Interacting selectively and non-covalently with copper (Cu) ions. obo:GO_0005507 obo:go.owl obo:GO_0005507 copper/cadmium binding obo:GO_0005507 copper binding obo:GO_0005507 molecular_function obo:GO_0005507 GO:0005507 obo:GO_0005507 copper ion binding obo:GO_0005509 Interacting selectively and non-covalently with calcium ions (Ca2+). obo:GO_0005509 obo:go.owl obo:GO_0005509 MIPS_funcat:16.17.01 obo:GO_0005509 molecular_function obo:GO_0005509 calcium ion storage activity obo:GO_0005509 GO:0005509 obo:GO_0005509 calcium ion binding obo:GO_0005515 Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules). obo:GO_0005515 obo:go.owl obo:GO_0005515 GO:0001948 obo:GO_0005515 GO:0045308 obo:GO_0005515 MIPS_funcat:16.01 obo:GO_0005515 MIPS_funcat:18.01.07 obo:GO_0005515 Reactome:R-HSA-170835 obo:GO_0005515 Reactome:R-HSA-170846 obo:GO_0005515 protein amino acid binding obo:GO_0005515 glycoprotein binding obo:GO_0005515 molecular_function obo:GO_0005515 GO:0005515 obo:GO_0005515 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_aspergillus obo:GO_0005515 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_candida obo:GO_0005515 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0005515 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0005515 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0005515 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0005515 protein binding obo:GO_0005516 Interacting selectively and non-covalently with calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states. obo:GO_0005516 obo:go.owl obo:GO_0005516 molecular_function obo:GO_0005516 GO:0005516 obo:GO_0005516 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0005516 calmodulin binding obo:GO_0005518 Interacting selectively and non-covalently with collagen, a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals. Collagen is highly enriched in glycine (some regions are 33% glycine) and proline, occurring predominantly as 3-hydroxyproline (about 20%). obo:GO_0005518 obo:go.owl obo:GO_0005518 molecular_function obo:GO_0005518 GO:0005518 obo:GO_0005518 collagen binding obo:GO_0005519 Interacting selectively and non-covalently with any protein involved in modulating the reorganization of the cytoskeleton. obo:GO_0005519 obo:go.owl obo:GO_0005519 molecular_function obo:GO_0005519 GO:0005519 obo:GO_0005519 cytoskeletal regulatory protein binding obo:GO_0005520 Interacting selectively and non-covalently with an insulin-like growth factor, any member of a group of polypeptides that are structurally homologous to insulin and share many of its biological activities, but are immunologically distinct from it. obo:GO_0005520 obo:go.owl obo:GO_0005520 IGF binding obo:GO_0005520 molecular_function obo:GO_0005520 GO:0005520 obo:GO_0005520 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0005520 insulin-like growth factor binding obo:GO_0005521 Interacting selectively and non-covalently with lamin; any of a group of intermediate-filament proteins that form the fibrous matrix on the inner surface of the nuclear envelope. obo:GO_0005521 obo:go.owl obo:GO_0005521 lamin/chromatin binding obo:GO_0005521 molecular_function obo:GO_0005521 GO:0005521 obo:GO_0005521 lamin binding obo:GO_0005522 Interacting selectively and non-covalently with profilin, an actin-binding protein that forms a complex with G-actin and prevents it from polymerizing to form F-actin. obo:GO_0005522 obo:go.owl obo:GO_0005522 molecular_function obo:GO_0005522 GO:0005522 obo:GO_0005522 profilin binding obo:GO_0005523 Interacting selectively and non-covalently with tropomyosin, a protein associated with actin filaments both in cytoplasm and, in association with troponin, in the thin filament of striated muscle. obo:GO_0005523 obo:go.owl obo:GO_0005523 molecular_function obo:GO_0005523 GO:0005523 obo:GO_0005523 tropomyosin binding obo:GO_0005524 Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. obo:GO_0005524 obo:go.owl obo:GO_0005524 MIPS_funcat:16.19.03 obo:GO_0005524 Reactome:R-HSA-265682 obo:GO_0005524 molecular_function obo:GO_0005524 GO:0005524 obo:GO_0005524 ATP binding obo:GO_0005525 Interacting selectively and non-covalently with GTP, guanosine triphosphate. obo:GO_0005525 obo:go.owl obo:GO_0005525 MIPS_funcat:16.19.05 obo:GO_0005525 Reactome:R-HSA-167429 obo:GO_0005525 molecular_function obo:GO_0005525 GO:0005525 obo:GO_0005525 GTP binding obo:GO_0005527 Interacting selectively and non-covalently with a macrolide, any of a large group of structurally related antibiotics produced by Streptomyces species. obo:GO_0005527 obo:go.owl obo:GO_0005527 molecular_function obo:GO_0005527 GO:0005527 obo:GO_0005527 macrolide binding obo:GO_0005528 Interacting selectively and non-covalently with the 23-membered macrolide lactone FK506. obo:GO_0005528 obo:go.owl obo:GO_0005528 molecular_function obo:GO_0005528 FK506-sensitive peptidyl-prolyl cis-trans isomerase obo:GO_0005528 GO:0005528 obo:GO_0005528 FK506 binding obo:GO_0005534 Interacting selectively and non-covalently with the aldohexose galactose (galacto-hexose), a common constituent of many oligo- and polysaccharides. obo:GO_0005534 obo:go.owl obo:GO_0005534 molecular_function obo:GO_0005534 galactose binding lectin obo:GO_0005534 GO:0005534 obo:GO_0005534 galactose binding obo:GO_0005536 Interacting selectively and non-covalently with the D- or L-enantiomer of glucose. obo:GO_0005536 obo:go.owl obo:GO_0005536 molecular_function obo:GO_0005536 GO:0005536 obo:GO_0005536 glucose binding obo:GO_0005537 Interacting selectively and non-covalently with mannose, a monosaccharide hexose, stereoisomeric with glucose, that occurs naturally only in polymerized forms called mannans. obo:GO_0005537 obo:go.owl obo:GO_0005537 Reactome:R-HSA-947991 obo:GO_0005537 molecular_function obo:GO_0005537 mannose binding lectin obo:GO_0005537 GO:0005537 obo:GO_0005537 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0005537 mannose binding obo:GO_0005539 Interacting selectively and non-covalently with any glycan (polysaccharide) containing a substantial proportion of aminomonosaccharide residues. obo:GO_0005539 obo:go.owl obo:GO_0005539 molecular_function obo:GO_0005539 GO:0005539 obo:GO_0005539 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0005539 glycosaminoglycan binding obo:GO_0005540 Interacting selectively and non-covalently with hyaluronic acid, a polymer composed of repeating dimeric units of glucuronic acid and N-acetyl glucosamine. obo:GO_0005540 obo:go.owl obo:GO_0005540 hyaluronan binding obo:GO_0005540 molecular_function obo:GO_0005540 GO:0005540 obo:GO_0005540 hyaluronic acid binding obo:GO_0005542 Interacting selectively and non-covalently with folic acid, pteroylglutamic acid. Folic acid is widely distributed as a member of the vitamin B complex and is essential for the synthesis of purine and pyrimidines. obo:GO_0005542 obo:go.owl obo:GO_0005542 folate binding obo:GO_0005542 vitamin B9 binding obo:GO_0005542 vitamin M binding obo:GO_0005542 molecular_function obo:GO_0005542 GO:0005542 obo:GO_0005542 folic acid binding obo:GO_0005543 Interacting selectively and non-covalently with phospholipids, a class of lipids containing phosphoric acid as a mono- or diester. obo:GO_0005543 obo:go.owl obo:GO_0005543 molecular_function obo:GO_0005543 GO:0005543 obo:GO_0005543 phospholipid binding obo:GO_0005544 Interacting selectively and non-covalently with phospholipids, a class of lipids containing phosphoric acid as a mono- or diester, in the presence of calcium. obo:GO_0005544 obo:go.owl obo:GO_0005544 molecular_function obo:GO_0005544 GO:0005544 obo:GO_0005544 calcium-dependent phospholipid binding obo:GO_0005545 Interacting selectively and non-covalently with phosphatidylinositol, any glycophospholipid with its sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol. obo:GO_0005545 obo:go.owl obo:GO_0005545 molecular_function obo:GO_0005545 GO:0005545 obo:GO_0005545 1-phosphatidylinositol binding obo:GO_0005546 Interacting selectively and non-covalently with phosphatidylinositol-4,5-bisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 4' and 5' positions. obo:GO_0005546 obo:go.owl obo:GO_0005546 PIP2 binding obo:GO_0005546 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate binding obo:GO_0005546 PtdIns(4,5)P2 binding obo:GO_0005546 phosphatidylinositol 4,5-bisphosphate binding obo:GO_0005546 molecular_function obo:GO_0005546 GO:0005546 obo:GO_0005546 phosphatidylinositol-4,5-bisphosphate binding obo:GO_0005547 Interacting selectively and non-covalently with phosphatidylinositol-3,4,5-trisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3', 4' and 5' positions. obo:GO_0005547 obo:go.owl obo:GO_0005547 PIP3 binding obo:GO_0005547 molecular_function obo:GO_0005547 GO:0005547 obo:GO_0005547 phosphatidylinositol-3,4,5-trisphosphate binding obo:GO_0005975 The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. Includes the formation of carbohydrate derivatives by the addition of a carbohydrate residue to another molecule. obo:GO_0005975 obo:go.owl obo:GO_0005975 janelomax obo:GO_0005975 2012-10-23T15:40:34Z obo:GO_0005975 GO:0044261 obo:GO_0005975 GO:0044723 obo:GO_0005975 MIPS_funcat:01.05 obo:GO_0005975 Wikipedia:Carbohydrate_metabolism obo:GO_0005975 carbohydrate metabolism obo:GO_0005975 multicellular organismal carbohydrate metabolic process obo:GO_0005975 biological_process obo:GO_0005975 single-organism carbohydrate metabolic process obo:GO_0005975 GO:0005975 obo:GO_0005975 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_agr obo:GO_0005975 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_aspergillus obo:GO_0005975 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_candida obo:GO_0005975 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0005975 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0005975 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0005975 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0005975 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0005975 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pombe obo:GO_0005975 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0005975 carbohydrate metabolic process obo:GO_0005984 The chemical reactions and pathways involving any disaccharide, sugars composed of two monosaccharide units. obo:GO_0005984 obo:go.owl obo:GO_0005984 disaccharide metabolism obo:GO_0005984 biological_process obo:GO_0005984 GO:0005984 obo:GO_0005984 disaccharide metabolic process obo:GO_0006139 Any cellular metabolic process involving nucleobases, nucleosides, nucleotides and nucleic acids. obo:GO_0006139 obo:go.owl obo:GO_0006139 GO:0055134 obo:GO_0006139 cellular nucleobase, nucleoside, nucleotide and nucleic acid metabolic process obo:GO_0006139 cellular nucleobase, nucleoside, nucleotide and nucleic acid metabolism obo:GO_0006139 nucleobase, nucleoside, nucleotide and nucleic acid metabolism obo:GO_0006139 biological_process obo:GO_0006139 nucleobase, nucleoside and nucleotide metabolic process obo:GO_0006139 nucleobase, nucleoside, nucleotide and nucleic acid metabolic process obo:GO_0006139 GO:0006139 obo:GO_0006139 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0006139 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0006139 nucleobase-containing compound metabolic process obo:GO_0006259 Any cellular metabolic process involving deoxyribonucleic acid. This is one of the two main types of nucleic acid, consisting of a long, unbranched macromolecule formed from one, or more commonly, two, strands of linked deoxyribonucleotides. obo:GO_0006259 obo:go.owl obo:GO_0006259 GO:0055132 obo:GO_0006259 MIPS_funcat:10 obo:GO_0006259 MIPS_funcat:10.01 obo:GO_0006259 DNA metabolism obo:GO_0006259 cellular DNA metabolism obo:GO_0006259 biological_process obo:GO_0006259 GO:0006259 obo:GO_0006259 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_agr obo:GO_0006259 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_aspergillus obo:GO_0006259 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_candida obo:GO_0006259 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0006259 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_flybase_ribbon obo:GO_0006259 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0006259 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0006259 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0006259 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0006259 DNA metabolic process obo:GO_0006281 The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway. obo:GO_0006281 obo:go.owl obo:GO_0006281 MIPS_funcat:10.01.05 obo:GO_0006281 MIPS_funcat:10.01.05.01 obo:GO_0006281 Wikipedia:DNA_repair obo:GO_0006281 biological_process obo:GO_0006281 GO:0006281 obo:GO_0006281 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0006281 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pombe obo:GO_0006281 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0006281 DNA repair obo:GO_0006283 The nucleotide-excision repair process that carries out preferential repair of DNA lesions on the actively transcribed strand of the DNA duplex. In addition, the transcription-coupled nucleotide-excision repair pathway is required for the recognition and repair of a small subset of lesions that are not recognized by the global genome nucleotide excision repair pathway. obo:GO_0006283 obo:go.owl obo:GO_0006283 TC-NER obo:GO_0006283 transcription-coupled NER obo:GO_0006283 transcription-coupled repair obo:GO_0006283 biological_process obo:GO_0006283 TCR obo:GO_0006283 GO:0006283 obo:GO_0006283 transcription-coupled nucleotide-excision repair obo:GO_0006284 In base excision repair, an altered base is removed by a DNA glycosylase enzyme, followed by excision of the resulting sugar phosphate. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase. obo:GO_0006284 obo:go.owl obo:GO_0006284 Wikipedia:Base_excision_repair obo:GO_0006284 BER obo:GO_0006284 biological_process obo:GO_0006284 GO:0006284 obo:GO_0006284 base-excision repair obo:GO_0006289 A DNA repair process in which a small region of the strand surrounding the damage is removed from the DNA helix as an oligonucleotide. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase. Nucleotide excision repair recognizes a wide range of substrates, including damage caused by UV irradiation (pyrimidine dimers and 6-4 photoproducts) and chemicals (intrastrand cross-links and bulky adducts). obo:GO_0006289 obo:go.owl obo:GO_0006289 GO:0045001 obo:GO_0006289 NER obo:GO_0006289 pyrimidine-dimer repair, DNA damage excision obo:GO_0006289 biological_process obo:GO_0006289 intrastrand cross-link repair obo:GO_0006289 GO:0006289 obo:GO_0006289 Note that although intrastrand cross-link repair is not exactly synonymous with nucleotide excision repair, nucleotide excision repair includes the repair of intrastrand cross-links. The synonym field is being used to reflect the broad substrate specificity of nucleotide excision repair. obo:GO_0006289 nucleotide-excision repair obo:GO_0006290 The repair of UV-induced T-T, C-T and C-C dimers. obo:GO_0006290 obo:go.owl obo:GO_0006290 biological_process obo:GO_0006290 GO:0006290 obo:GO_0006290 pyrimidine dimer repair obo:GO_0006298 A system for the correction of errors in which an incorrect base, which cannot form hydrogen bonds with the corresponding base in the parent strand, is incorporated into the daughter strand. The mismatch repair system promotes genomic fidelity by repairing base-base mismatches, insertion-deletion loops and heterologies generated during DNA replication and recombination. obo:GO_0006298 obo:go.owl obo:GO_0006298 GO:0006300 obo:GO_0006298 Wikipedia:DNA_mismatch_repair obo:GO_0006298 MMR obo:GO_0006298 long patch mismatch repair system obo:GO_0006298 biological_process obo:GO_0006298 MutS/MutL/MutH pathway obo:GO_0006298 mismatch repair, MutL-like pathway obo:GO_0006298 GO:0006298 obo:GO_0006298 mismatch repair obo:GO_0006301 The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA after replication. Includes pathways that remove replication-blocking lesions in conjunction with DNA replication. obo:GO_0006301 obo:go.owl obo:GO_0006301 Wikipedia:Postreplication_repair obo:GO_0006301 postreplication DNA repair obo:GO_0006301 biological_process obo:GO_0006301 GO:0006301 obo:GO_0006301 postreplication repair obo:GO_0006302 The repair of double-strand breaks in DNA via homologous and nonhomologous mechanisms to reform a continuous DNA helix. obo:GO_0006302 obo:go.owl obo:GO_0006302 biological_process obo:GO_0006302 GO:0006302 obo:GO_0006302 Note that the processes of nuclear double-strand break repair and mitochondrial double-strand break repair are genetically separable (PMID:22214610). To annotate gene products involved in mitochondrial double-strand break repair, please use GO:0097551 'mitochondrial double-strand break repair'. obo:GO_0006302 double-strand break repair obo:GO_0006303 The repair of a double-strand break in DNA in which the two broken ends are rejoined with little or no sequence complementarity. Information at the DNA ends may be lost due to the modification of broken DNA ends. This term covers instances of separate pathways, called classical (or canonical) and alternative nonhomologous end joining (C-NHEJ and A-NHEJ). These in turn may further branch into sub-pathways, but evidence is still unclear. obo:GO_0006303 obo:go.owl obo:GO_0006303 NHEJ obo:GO_0006303 biological_process obo:GO_0006303 GO:0006303 obo:GO_0006303 double-strand break repair via nonhomologous end joining obo:GO_0006304 The covalent alteration of one or more nucleotide sites in DNA, resulting in a change in its properties. obo:GO_0006304 obo:go.owl obo:GO_0006304 MIPS_funcat:10.01.09 obo:GO_0006304 biological_process obo:GO_0006304 GO:0006304 obo:GO_0006304 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0006304 DNA modification obo:GO_0006355 Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription. obo:GO_0006355 obo:go.owl obo:GO_0006355 GO:0032583 obo:GO_0006355 GO:0045449 obo:GO_0006355 GO:0061019 obo:GO_0006355 transcriptional control obo:GO_0006355 regulation of cellular transcription, DNA-dependent obo:GO_0006355 regulation of transcription, DNA-dependent obo:GO_0006355 biological_process obo:GO_0006355 regulation of gene-specific transcription obo:GO_0006355 GO:0006355 obo:GO_0006355 regulation of transcription, DNA-templated obo:GO_0006464 The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications) occurring at the level of an individual cell. Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification). obo:GO_0006464 obo:go.owl obo:GO_0006464 protein modification process obo:GO_0006464 MIPS_funcat:14 obo:GO_0006464 MIPS_funcat:14.07 obo:GO_0006464 MIPS_funcat:18.01.01 obo:GO_0006464 biological_process obo:GO_0006464 process resulting in protein modification obo:GO_0006464 protein tagging activity obo:GO_0006464 GO:0006464 obo:GO_0006464 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_aspergillus obo:GO_0006464 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_candida obo:GO_0006464 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0006464 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0006464 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0006464 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0006464 cellular protein modification process obo:GO_0006468 The process of introducing a phosphate group on to a protein. obo:GO_0006468 obo:go.owl obo:GO_0006468 MIPS_funcat:14.07.03 obo:GO_0006468 protein amino acid phosphorylation obo:GO_0006468 biological_process obo:GO_0006468 GO:0006468 obo:GO_0006468 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0006468 protein phosphorylation obo:GO_0006470 The process of removing one or more phosphoric residues from a protein. obo:GO_0006470 obo:go.owl obo:GO_0006470 MIPS_funcat:14.07.03 obo:GO_0006470 protein amino acid dephosphorylation obo:GO_0006470 biological_process obo:GO_0006470 GO:0006470 obo:GO_0006470 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0006470 protein dephosphorylation obo:GO_0006516 The chemical reactions and pathways resulting in the breakdown of glycoproteins, any protein that contains covalently bound glycose (i.e. monosaccharide) residues; the glycose occurs most commonly as oligosaccharide or fairly small polysaccharide but occasionally as monosaccharide. obo:GO_0006516 obo:go.owl obo:GO_0006516 glycoprotein breakdown obo:GO_0006516 glycoprotein catabolism obo:GO_0006516 glycoprotein degradation obo:GO_0006516 biological_process obo:GO_0006516 GO:0006516 obo:GO_0006516 glycoprotein catabolic process obo:GO_0006582 The chemical reactions and pathways involving melanins, pigments largely of animal origin. High molecular weight polymers of indole quinone, they are irregular polymeric structures and are divided into three groups: allomelanins in the plant kingdom and eumelanins and phaeomelanins in the animal kingdom. obo:GO_0006582 obo:go.owl obo:GO_0006582 melanin metabolism obo:GO_0006582 biological_process obo:GO_0006582 GO:0006582 obo:GO_0006582 melanin metabolic process obo:GO_0006725 The chemical reactions and pathways involving aromatic compounds, any organic compound characterized by one or more planar rings, each of which contains conjugated double bonds and delocalized pi electrons, as carried out by individual cells. obo:GO_0006725 obo:go.owl obo:GO_0006725 aromatic compound metabolism obo:GO_0006725 aromatic hydrocarbon metabolic process obo:GO_0006725 aromatic hydrocarbon metabolism obo:GO_0006725 biological_process obo:GO_0006725 GO:0006725 obo:GO_0006725 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0006725 cellular aromatic compound metabolic process obo:GO_0006795 Any process that modulates the frequency, rate or extent of phosphorus utilization. obo:GO_0006795 obo:go.owl obo:GO_0006795 MIPS_funcat:01.04.04 obo:GO_0006795 biological_process obo:GO_0006795 GO:0006795 obo:GO_0006795 regulation of phosphorus utilization obo:GO_0006796 The chemical reactions and pathways involving the phosphate group, the anion or salt of any phosphoric acid. obo:GO_0006796 obo:go.owl obo:GO_0006796 MIPS_funcat:01.04 obo:GO_0006796 phosphate metabolism obo:GO_0006796 biological_process obo:GO_0006796 phosphate metabolic process obo:GO_0006796 GO:0006796 obo:GO_0006796 phosphate-containing compound metabolic process obo:GO_0006807 The chemical reactions and pathways involving organic or inorganic compounds that contain nitrogen. obo:GO_0006807 obo:go.owl obo:GO_0006807 MIPS_funcat:01.02 obo:GO_0006807 nitrogen compound metabolism obo:GO_0006807 biological_process obo:GO_0006807 GO:0006807 obo:GO_0006807 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0006807 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0006807 nitrogen compound metabolic process obo:GO_0006808 Any process that modulates the frequency, rate or extent of nitrogen utilization. obo:GO_0006808 obo:go.owl obo:GO_0006808 MIPS_funcat:01.02.04 obo:GO_0006808 MIPS_funcat:01.02.04.01 obo:GO_0006808 biological_process obo:GO_0006808 GO:0006808 obo:GO_0006808 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0006808 regulation of nitrogen utilization obo:GO_0006810 The directed movement of substances (such as macromolecules, small molecules, ions) or cellular components (such as complexes and organelles) into, out of or within a cell, or between cells, or within a multicellular organism by means of some agent such as a transporter, pore or motor protein. obo:GO_0006810 obo:go.owl obo:GO_0006810 janelomax obo:GO_0006810 2012-12-13T16:25:32Z obo:GO_0006810 GO:0015457 obo:GO_0006810 GO:0015460 obo:GO_0006810 GO:0044765 obo:GO_0006810 MIPS_funcat:20 obo:GO_0006810 small molecule transport obo:GO_0006810 solute:solute exchange obo:GO_0006810 biological_process obo:GO_0006810 single-organism transport obo:GO_0006810 GO:0006810 obo:GO_0006810 http://purl.oboInOwllibrary.org/oboInOwl/go#gocheck_do_not_annotate obo:GO_0006810 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_aspergillus obo:GO_0006810 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_candida obo:GO_0006810 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0006810 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0006810 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0006810 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0006810 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0006810 Note that this term should not be used for direct annotation. It should be possible to make a more specific annotation to one of the children of this term, for e.g. to transmembrane transport, to microtubule-based transport or to vesicle-mediated transport. obo:GO_0006810 transport obo:GO_0006811 The directed movement of charged atoms or small charged molecules into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0006811 obo:go.owl obo:GO_0006811 MIPS_funcat:20.01.01 obo:GO_0006811 biological_process obo:GO_0006811 GO:0006811 obo:GO_0006811 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0006811 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0006811 ion transport obo:GO_0006812 The directed movement of cations, atoms or small molecules with a net positive charge, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0006812 obo:go.owl obo:GO_0006812 GO:0006819 obo:GO_0006812 GO:0015674 obo:GO_0006812 MIPS_funcat:20.01.01.01 obo:GO_0006812 di-, tri-valent inorganic cation transport obo:GO_0006812 biological_process obo:GO_0006812 GO:0006812 obo:GO_0006812 cation transport obo:GO_0006813 The directed movement of potassium ions (K+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0006813 obo:go.owl obo:GO_0006813 midori obo:GO_0006813 2010-09-03T02:39:22Z obo:GO_0006813 GO:0015458 obo:GO_0006813 GO:0071804 obo:GO_0006813 sodium/potassium transport obo:GO_0006813 cellular potassium ion transport obo:GO_0006813 potassium conductance obo:GO_0006813 potassium ion conductance obo:GO_0006813 biological_process obo:GO_0006813 K+ conductance obo:GO_0006813 low voltage-dependent potassium channel auxiliary protein activity obo:GO_0006813 low voltage-gated potassium channel auxiliary protein activity obo:GO_0006813 potassium transport obo:GO_0006813 GO:0006813 obo:GO_0006813 potassium ion transport obo:GO_0006814 The directed movement of sodium ions (Na+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0006814 obo:go.owl obo:GO_0006814 GO:0006834 obo:GO_0006814 GO:0016974 obo:GO_0006814 sodium/potassium transport obo:GO_0006814 sodium transport obo:GO_0006814 mitochondrial sodium/calcium ion exchange obo:GO_0006814 sodium:calcium exchange obo:GO_0006814 sodium:solute transport obo:GO_0006814 biological_process obo:GO_0006814 sodium channel auxiliary protein activity obo:GO_0006814 GO:0006814 obo:GO_0006814 sodium ion transport obo:GO_0006816 The directed movement of calcium (Ca) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0006816 obo:go.owl obo:GO_0006816 calcium transport obo:GO_0006816 mitochondrial sodium/calcium ion exchange obo:GO_0006816 sodium:calcium exchange obo:GO_0006816 biological_process obo:GO_0006816 GO:0006816 obo:GO_0006816 calcium ion transport obo:GO_0006817 The directed movement of phosphate into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0006817 obo:go.owl obo:GO_0006817 MIPS_funcat:20.01.01.07.07 obo:GO_0006817 biological_process obo:GO_0006817 phosphate transport obo:GO_0006817 GO:0006817 obo:GO_0006817 phosphate ion transport obo:GO_0006820 The directed movement of anions, atoms or small molecules with a net negative charge, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0006820 obo:go.owl obo:GO_0006820 GO:0006822 obo:GO_0006820 MIPS_funcat:20.01.01.07 obo:GO_0006820 biological_process obo:GO_0006820 GO:0006820 obo:GO_0006820 anion transport obo:GO_0006821 The directed movement of chloride into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0006821 obo:go.owl obo:GO_0006821 MIPS_funcat:20.01.01.07.09 obo:GO_0006821 biological_process obo:GO_0006821 GO:0006821 obo:GO_0006821 chloride transport obo:GO_0006824 The directed movement of cobalt (Co) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0006824 obo:go.owl obo:GO_0006824 cobalt transport obo:GO_0006824 biological_process obo:GO_0006824 GO:0006824 obo:GO_0006824 cobalt ion transport obo:GO_0006825 The directed movement of copper (Cu) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0006825 obo:go.owl obo:GO_0006825 biological_process obo:GO_0006825 GO:0006825 obo:GO_0006825 copper ion transport obo:GO_0006826 The directed movement of iron (Fe) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0006826 obo:go.owl obo:GO_0006826 paola obo:GO_0006826 2012-04-18T03:33:45Z obo:GO_0006826 GO:0015681 obo:GO_0006826 GO:0015682 obo:GO_0006826 GO:0015684 obo:GO_0006826 GO:0033216 obo:GO_0006826 GO:0097286 obo:GO_0006826 iron transport obo:GO_0006826 ferric ion import obo:GO_0006826 ferric ion transport obo:GO_0006826 ferric iron import obo:GO_0006826 ferric iron transport obo:GO_0006826 ferric iron uptake obo:GO_0006826 ferrous ion transport obo:GO_0006826 ferrous iron transport obo:GO_0006826 biological_process obo:GO_0006826 iron ion import obo:GO_0006826 GO:0006826 obo:GO_0006826 iron ion transport obo:GO_0006828 The directed movement of manganese (Mn) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0006828 obo:go.owl obo:GO_0006828 biological_process obo:GO_0006828 GO:0006828 obo:GO_0006828 manganese ion transport obo:GO_0006829 The directed movement of zinc (Zn II) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0006829 obo:go.owl obo:GO_0006829 zinc II ion transport obo:GO_0006829 zinc transport obo:GO_0006829 biological_process obo:GO_0006829 GO:0006829 obo:GO_0006829 zinc ion transport obo:GO_0006851 The process in which a calcium ion (Ca2+) is transported across a mitochondrial membrane, into or out of the mitochondrion. obo:GO_0006851 obo:go.owl obo:GO_0006851 mitochondrial calcium transport obo:GO_0006851 biological_process obo:GO_0006851 GO:0006851 obo:GO_0006851 mitochondrial calcium ion transmembrane transport obo:GO_0006933 The disassembly of adhesions at the front and rear of a migrating cell. At the leading edge, adhesion disassembly accompanies the formation of new protrusions; at the cell rear, it promotes tail retraction. obo:GO_0006933 obo:go.owl obo:GO_0006933 substrate-bound cell migration, cell release from substrate obo:GO_0006933 biological_process obo:GO_0006933 GO:0006933 obo:GO_0006933 negative regulation of cell adhesion involved in substrate-bound cell migration obo:GO_0006935 The directed movement of a motile cell or organism, or the directed growth of a cell guided by a specific chemical concentration gradient. Movement may be towards a higher concentration (positive chemotaxis) or towards a lower concentration (negative chemotaxis). obo:GO_0006935 obo:go.owl obo:GO_0006935 MIPS_funcat:34.11.03.03 obo:GO_0006935 Wikipedia:Chemotaxis obo:GO_0006935 taxis in response to chemical stimulus obo:GO_0006935 biological_process obo:GO_0006935 GO:0006935 obo:GO_0006935 chemotaxis obo:GO_0006950 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a disturbance in organismal or cellular homeostasis, usually, but not necessarily, exogenous (e.g. temperature, humidity, ionizing radiation). obo:GO_0006950 obo:go.owl obo:GO_0006950 MIPS_funcat:32.01 obo:GO_0006950 biological_process obo:GO_0006950 response to abiotic stress obo:GO_0006950 response to biotic stress obo:GO_0006950 GO:0006950 obo:GO_0006950 http://purl.oboInOwllibrary.org/oboInOwl/go#gocheck_do_not_manually_annotate obo:GO_0006950 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_aspergillus obo:GO_0006950 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_candida obo:GO_0006950 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0006950 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0006950 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0006950 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0006950 Note that this term is in the subset of terms that should not be used for direct gene product annotation. Instead, select a child term or, if no appropriate child term exists, please request a new term. Direct annotations to this term may be amended during annotation QC. obo:GO_0006950 response to stress obo:GO_0006970 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating an increase or decrease in the concentration of solutes outside the organism or cell. obo:GO_0006970 obo:go.owl obo:GO_0006970 MIPS_funcat:32.01.03 obo:GO_0006970 MIPS_funcat:36.20.35.09.05 obo:GO_0006970 osmotic response obo:GO_0006970 osmotic stress response obo:GO_0006970 biological_process obo:GO_0006970 GO:0006970 obo:GO_0006970 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0006970 response to osmotic stress obo:GO_0006971 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, a hypotonic environment, i.e. an environment with a lower concentration of solutes than the organism or cell. obo:GO_0006971 obo:go.owl obo:GO_0006971 hypo-osmotic response obo:GO_0006971 biological_process obo:GO_0006971 GO:0006971 obo:GO_0006971 hypotonic response obo:GO_0006972 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, a hyperosmotic environment, i.e. an environment with a higher concentration of solutes than the organism or cell. obo:GO_0006972 obo:go.owl obo:GO_0006972 HOG response obo:GO_0006972 hypertonic response obo:GO_0006972 response to hypertonicity obo:GO_0006972 biological_process obo:GO_0006972 GO:0006972 obo:GO_0006972 hyperosmotic response obo:GO_0006974 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism. obo:GO_0006974 obo:go.owl obo:GO_0006974 GO:0034984 obo:GO_0006974 response to DNA damage stimulus obo:GO_0006974 MIPS_funcat:32.01.09 obo:GO_0006974 DNA damage response obo:GO_0006974 cellular DNA damage response obo:GO_0006974 response to genotoxic stress obo:GO_0006974 biological_process obo:GO_0006974 GO:0006974 obo:GO_0006974 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0006974 cellular response to DNA damage stimulus obo:GO_0006975 The widespread phosphorylation of various molecules, triggering many downstream processes, that occurs in response to the detection of DNA damage. obo:GO_0006975 obo:go.owl obo:GO_0006975 biological_process obo:GO_0006975 GO:0006975 obo:GO_0006975 DNA damage induced protein phosphorylation obo:GO_0006979 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals. obo:GO_0006979 obo:go.owl obo:GO_0006979 MIPS_funcat:32.01.01 obo:GO_0006979 biological_process obo:GO_0006979 GO:0006979 obo:GO_0006979 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0006979 response to oxidative stress obo:GO_0006982 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a lipid hydroperoxide stimulus. Lipid hydroperoxide is the highly reactive primary oxygenated products of polyunsaturated fatty acids. obo:GO_0006982 obo:go.owl obo:GO_0006982 response to LHPO obo:GO_0006982 biological_process obo:GO_0006982 GO:0006982 obo:GO_0006982 response to lipid hydroperoxide obo:GO_0006995 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of nitrogen. obo:GO_0006995 obo:go.owl obo:GO_0006995 biological_process obo:GO_0006995 GO:0006995 obo:GO_0006995 cellular response to nitrogen starvation obo:GO_0007154 Any process that mediates interactions between a cell and its surroundings. Encompasses interactions such as signaling or attachment between one cell and another cell, between a cell and an extracellular matrix, or between a cell and any other aspect of its environment. obo:GO_0007154 obo:go.owl obo:GO_0007154 Wikipedia:Cell_signaling obo:GO_0007154 biological_process obo:GO_0007154 GO:0007154 obo:GO_0007154 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0007154 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0007154 cell communication obo:GO_0007162 Any process that stops, prevents, or reduces the frequency, rate or extent of cell adhesion. obo:GO_0007162 obo:go.owl obo:GO_0007162 down regulation of cell adhesion obo:GO_0007162 down-regulation of cell adhesion obo:GO_0007162 downregulation of cell adhesion obo:GO_0007162 inhibition of cell adhesion obo:GO_0007162 biological_process obo:GO_0007162 cell adhesion receptor inhibitor activity obo:GO_0007162 GO:0007162 obo:GO_0007162 negative regulation of cell adhesion obo:GO_0007165 The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell. obo:GO_0007165 obo:go.owl obo:GO_0007165 GO:0023033 obo:GO_0007165 MIPS_funcat:30 obo:GO_0007165 Wikipedia:Signal_transduction obo:GO_0007165 signaling cascade obo:GO_0007165 signalling cascade obo:GO_0007165 biological_process obo:GO_0007165 signaling pathway obo:GO_0007165 signalling pathway obo:GO_0007165 GO:0007165 obo:GO_0007165 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_aspergillus obo:GO_0007165 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_candida obo:GO_0007165 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0007165 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0007165 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0007165 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0007165 Note that signal transduction is defined broadly to include a ligand interacting with a receptor, downstream signaling steps and a response being triggered. A change in form of the signal in every step is not necessary. Note that in many cases the end of this process is regulation of the initiation of transcription. Note that specific transcription factors may be annotated to this term, but core/general transcription machinery such as RNA polymerase should not. obo:GO_0007165 signal transduction obo:GO_0007231 The series of molecular signals initiated in response to osmotic change. obo:GO_0007231 obo:go.owl obo:GO_0007231 osmolarity sensing obo:GO_0007231 osmolarity sensing signaling pathway obo:GO_0007231 osmolarity sensing signalling pathway obo:GO_0007231 osmosensory signal transduction obo:GO_0007231 osmosensory signalling pathway obo:GO_0007231 signal transduction during osmotic stress obo:GO_0007231 biological_process obo:GO_0007231 GO:0007231 obo:GO_0007231 osmosensory signaling pathway obo:GO_0007584 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a nutrient stimulus. obo:GO_0007584 obo:go.owl obo:GO_0007584 response to nutrients obo:GO_0007584 nutritional response pathway obo:GO_0007584 biological_process obo:GO_0007584 GO:0007584 obo:GO_0007584 response to nutrient obo:GO_0008009 The function of a family of small chemotactic cytokines; their name is derived from their ability to induce directed chemotaxis in nearby responsive cells. All chemokines possess a number of conserved cysteine residues involved in intramolecular disulfide bond formation. Some chemokines are considered pro-inflammatory and can be induced during an immune response to recruit cells of the immune system to a site of infection, while others are considered homeostatic and are involved in controlling the migration of cells during normal processes of tissue maintenance or development. Chemokines are found in all vertebrates, some viruses and some bacteria. obo:GO_0008009 obo:go.owl obo:GO_0008009 MIPS_funcat:40.02.03.03 obo:GO_0008009 molecular_function obo:GO_0008009 GO:0008009 obo:GO_0008009 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0008009 See also the molecular function terms 'cytokine activity ; GO:0005125' and 'receptor agonist activity ; GO:0048018'. obo:GO_0008009 chemokine activity obo:GO_0008013 Interacting selectively and non-covalently with the beta subunit of the catenin complex. obo:GO_0008013 obo:go.owl obo:GO_0008013 molecular_function obo:GO_0008013 GO:0008013 obo:GO_0008013 beta-catenin binding obo:GO_0008017 Interacting selectively and non-covalently with microtubules, filaments composed of tubulin monomers. obo:GO_0008017 obo:go.owl obo:GO_0008017 molecular_function obo:GO_0008017 microtubule severing activity obo:GO_0008017 microtubule/chromatin interaction obo:GO_0008017 GO:0008017 obo:GO_0008017 microtubule binding obo:GO_0008022 Interacting selectively and non-covalently with a protein C-terminus, the end of any peptide chain at which the 1-carboxyl function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue. obo:GO_0008022 obo:go.owl obo:GO_0008022 C-terminal binding obo:GO_0008022 C-terminal end binding obo:GO_0008022 COOH-terminal binding obo:GO_0008022 COOH-terminus binding obo:GO_0008022 carboxylate-terminus binding obo:GO_0008022 molecular_function obo:GO_0008022 carboxy-terminal binding obo:GO_0008022 carboxy-terminus binding obo:GO_0008022 carboxyl-terminal binding obo:GO_0008022 carboxyl-terminus binding obo:GO_0008022 carboxylate-terminal binding obo:GO_0008022 GO:0008022 obo:GO_0008022 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0008022 protein C-terminus binding obo:GO_0008031 The action characteristic of eclosion hormone, a peptide hormone that, upon receptor binding, triggers the death of certain muscles and neurons during insect metamorphosis. obo:GO_0008031 obo:go.owl obo:GO_0008031 molecular_function obo:GO_0008031 GO:0008031 obo:GO_0008031 eclosion hormone activity obo:GO_0008035 Interacting selectively and non-covalently with high-density lipoprotein particle, a lipoprotein particle with a high density (typically 1.063-1.21 g/ml) and a diameter of 5-10 nm that contains APOAs and may contain APOCs and APOE. obo:GO_0008035 obo:go.owl obo:GO_0008035 HDL binding obo:GO_0008035 molecular_function obo:GO_0008035 GO:0008035 obo:GO_0008035 high-density lipoprotein particle binding obo:GO_0008047 Binds to and increases the activity of an enzyme. obo:GO_0008047 obo:go.owl obo:GO_0008047 GO:0010577 obo:GO_0008047 MIPS_funcat:18.02.01.01 obo:GO_0008047 metalloenzyme activator activity obo:GO_0008047 molecular_function obo:GO_0008047 GO:0008047 obo:GO_0008047 enzyme activator activity obo:GO_0008061 Interacting selectively and non-covalently with chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues. obo:GO_0008061 obo:go.owl obo:GO_0008061 molecular_function obo:GO_0008061 GO:0008061 obo:GO_0008061 chitin binding obo:GO_0008081 Catalysis of the hydrolysis of a phosphodiester to give a phosphomonoester and a free hydroxyl group. obo:GO_0008081 obo:go.owl obo:GO_0008081 GO:0004434 obo:GO_0008081 GO:0016792 obo:GO_0008081 EC:3.1.4 obo:GO_0008081 Reactome:R-HSA-5693578 obo:GO_0008081 phosphodiesterase obo:GO_0008081 molecular_function obo:GO_0008081 GO:0008081 obo:GO_0008081 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0008081 phosphoric diester hydrolase activity obo:GO_0008083 The function that stimulates a cell to grow or proliferate. Most growth factors have other actions besides the induction of cell growth or proliferation. obo:GO_0008083 obo:go.owl obo:GO_0008083 MIPS_funcat:40.02.03.05 obo:GO_0008083 molecular_function obo:GO_0008083 GO:0008083 obo:GO_0008083 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0008083 Also consider annotating to 'receptor agonist activity ; GO:0048018'. obo:GO_0008083 growth factor activity obo:GO_0008084 Interacting selectively and non-covalently with an imaginal disc growth factor receptor. obo:GO_0008084 obo:go.owl obo:GO_0008084 imaginal disc growth factor obo:GO_0008084 molecular_function obo:GO_0008084 GO:0008084 obo:GO_0008084 imaginal disc growth factor receptor binding obo:GO_0008092 Interacting selectively and non-covalently with any protein component of any cytoskeleton (actin, microtubule, or intermediate filament cytoskeleton). obo:GO_0008092 obo:go.owl obo:GO_0008092 molecular_function obo:GO_0008092 GO:0008092 obo:GO_0008092 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_agr obo:GO_0008092 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0008092 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_flybase_ribbon obo:GO_0008092 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0008092 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_mouse obo:GO_0008092 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0008092 cytoskeletal protein binding obo:GO_0008097 Interacting selectively and non-covalently with 5S ribosomal RNA, the smallest RNA constituent of a ribosome. obo:GO_0008097 obo:go.owl obo:GO_0008097 molecular_function obo:GO_0008097 GO:0008097 obo:GO_0008097 5S rRNA binding obo:GO_0008098 Interacting selectively and non-covalently with the unprocessed 5S ribosomal RNA transcript. obo:GO_0008098 obo:go.owl obo:GO_0008098 molecular_function obo:GO_0008098 GO:0008098 obo:GO_0008098 5S rRNA primary transcript binding obo:GO_0008134 Interacting selectively and non-covalently with a transcription factor, a protein required to initiate or regulate transcription. obo:GO_0008134 obo:go.owl obo:GO_0008134 TF binding obo:GO_0008134 molecular_function obo:GO_0008134 GO:0008134 obo:GO_0008134 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_agr obo:GO_0008134 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0008134 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0008134 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0008134 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0008134 transcription factor binding obo:GO_0008138 Catalysis of the reactions: protein serine + H2O = protein serine + phosphate; protein threonine phosphate + H2O = protein threonine + phosphate; and protein tyrosine phosphate + H2O = protein tyrosine + phosphate. obo:GO_0008138 obo:go.owl obo:GO_0008138 dual-specificity protein phosphatase obo:GO_0008138 Reactome:R-HSA-5675373 obo:GO_0008138 Reactome:R-HSA-5675376 obo:GO_0008138 molecular_function obo:GO_0008138 GO:0008138 obo:GO_0008138 Note that this term applies only to free amino acids. Consider 'protein serine/threonine phosphatase activity' or 'protein tyrosine/serine/threonine phosphatase activity' if you want to annotate a protein phosphatase. See discussion at https://github.com/geneontology/go-ontology/issues/12183 obo:GO_0008138 protein tyrosine/serine/threonine phosphatase activity obo:GO_0008139 Interacting selectively and non-covalently with a nuclear localization sequence, a specific peptide sequence that acts as a signal to localize the protein within the nucleus. obo:GO_0008139 obo:go.owl obo:GO_0008139 NLS binding obo:GO_0008139 nuclear localisation sequence binding obo:GO_0008139 nuclear localization signal binding obo:GO_0008139 molecular_function obo:GO_0008139 GO:0008139 obo:GO_0008139 nuclear localization sequence binding obo:GO_0008140 Interacting selectively and non-covalently with a cAMP response element binding protein (a CREB protein). obo:GO_0008140 obo:go.owl obo:GO_0008140 3',5' cAMP response element binding protein binding obo:GO_0008140 3',5'-cAMP response element binding protein binding obo:GO_0008140 CREB binding obo:GO_0008140 adenosine 3',5'-cyclophosphate response element binding protein binding obo:GO_0008140 cyclic AMP response element binding protein binding obo:GO_0008140 molecular_function obo:GO_0008140 CBP obo:GO_0008140 GO:0008140 obo:GO_0008140 cAMP response element binding protein binding obo:GO_0008142 Interacting selectively and non-covalently with oxysterol, an oxidized form of cholesterol. obo:GO_0008142 obo:go.owl obo:GO_0008142 molecular_function obo:GO_0008142 GO:0008142 obo:GO_0008142 oxysterol binding obo:GO_0008143 Interacting selectively and non-covalently with a sequence of adenylyl residues in an RNA molecule, such as the poly(A) tail, a sequence of adenylyl residues at the 3' end of eukaryotic mRNA. obo:GO_0008143 obo:go.owl obo:GO_0008143 poly(A) binding, within an RNA molecule obo:GO_0008143 poly(rA) binding obo:GO_0008143 poly-A binding obo:GO_0008143 polyadenylate binding obo:GO_0008143 molecular_function obo:GO_0008143 GO:0008143 obo:GO_0008143 poly(A) binding obo:GO_0008144 Interacting selectively and non-covalently with a drug, any naturally occurring or synthetic substance, other than a nutrient, that, when administered or applied to an organism, affects the structure or functioning of the organism; in particular, any such substance used in the diagnosis, prevention, or treatment of disease. obo:GO_0008144 obo:go.owl obo:GO_0008144 molecular_function obo:GO_0008144 GO:0008144 obo:GO_0008144 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0008144 drug binding obo:GO_0008146 Catalysis of the transfer of a sulfate group from 3'-phosphoadenosine 5'-phosphosulfate to the hydroxyl group of an acceptor, producing the sulfated derivative and 3'-phosphoadenosine 5'-phosphate. obo:GO_0008146 obo:go.owl obo:GO_0008146 EC:2.8.2 obo:GO_0008146 Reactome:R-HSA-176588 obo:GO_0008146 Reactome:R-HSA-176604 obo:GO_0008146 Reactome:R-HSA-176669 obo:GO_0008146 Reactome:R-HSA-2022061 obo:GO_0008146 sulphotransferase activity obo:GO_0008146 molecular_function obo:GO_0008146 GO:0008146 obo:GO_0008146 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0008146 sulfotransferase activity obo:GO_0008150 A biological process represents a specific objective that the organism is genetically programmed to achieve. Biological processes are often described by their outcome or ending state, e.g., the biological process of cell division results in the creation of two daughter cells (a divided cell) from a single parent cell. A biological process is accomplished by a particular set of molecular functions carried out by specific gene products (or macromolecular complexes), often in a highly regulated manner and in a particular temporal sequence. obo:GO_0008150 obo:go.owl obo:GO_0008150 janelomax obo:GO_0008150 2012-09-19T15:05:24Z obo:GO_0008150 GO:0000004 obo:GO_0008150 GO:0007582 obo:GO_0008150 GO:0044699 obo:GO_0008150 Wikipedia:Biological_process obo:GO_0008150 biological process obo:GO_0008150 physiological process obo:GO_0008150 biological_process obo:GO_0008150 single organism process obo:GO_0008150 single-organism process obo:GO_0008150 GO:0008150 obo:GO_0008150 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_aspergillus obo:GO_0008150 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_candida obo:GO_0008150 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0008150 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0008150 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0008150 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0008150 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0008150 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pombe obo:GO_0008150 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0008150 Note that, in addition to forming the root of the biological process ontology, this term is recommended for use for the annotation of gene products whose biological process is unknown. When this term is used for annotation, it indicates that no information was available about the biological process of the gene product annotated as of the date the annotation was made; the evidence code "no data" (ND), is used to indicate this. obo:GO_0008150 biological process obo:GO_0008152 The chemical reactions and pathways, including anabolism and catabolism, by which living organisms transform chemical substances. Metabolic processes typically transform small molecules, but also include macromolecular processes such as DNA repair and replication, and protein synthesis and degradation. obo:GO_0008152 obo:go.owl obo:GO_0008152 janelomax obo:GO_0008152 2012-10-17T15:46:40Z obo:GO_0008152 GO:0044236 obo:GO_0008152 GO:0044710 obo:GO_0008152 MIPS_funcat:01 obo:GO_0008152 Wikipedia:Metabolism obo:GO_0008152 metabolism obo:GO_0008152 metabolic process resulting in cell growth obo:GO_0008152 metabolism resulting in cell growth obo:GO_0008152 multicellular organism metabolic process obo:GO_0008152 biological_process obo:GO_0008152 single-organism metabolic process obo:GO_0008152 GO:0008152 obo:GO_0008152 http://purl.oboInOwllibrary.org/oboInOwl/go#gocheck_do_not_manually_annotate obo:GO_0008152 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0008152 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0008152 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0008152 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0008152 Note that metabolic processes do not include single functions or processes such as protein-protein interactions, protein-nucleic acids, nor receptor-ligand interactions. obo:GO_0008152 metabolic process obo:GO_0008157 Interacting selectively and non-covalently with the enzyme protein phosphatase 1. obo:GO_0008157 obo:go.owl obo:GO_0008157 molecular_function obo:GO_0008157 GO:0008157 obo:GO_0008157 protein phosphatase 1 binding obo:GO_0008168 Catalysis of the transfer of a methyl group to an acceptor molecule. obo:GO_0008168 obo:go.owl obo:GO_0008168 GO:0004480 obo:GO_0008168 methylase obo:GO_0008168 EC:2.1.1 obo:GO_0008168 Reactome:R-HSA-379387 obo:GO_0008168 Reactome:R-HSA-379464 obo:GO_0008168 Reactome:R-HSA-6800149 obo:GO_0008168 Reactome:R-HSA-71286 obo:GO_0008168 molecular_function obo:GO_0008168 GO:0008168 obo:GO_0008168 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0008168 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0008168 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0008168 methyltransferase activity obo:GO_0008169 Catalysis of the transfer of a methyl group to the carbon atom of an acceptor molecule. obo:GO_0008169 obo:go.owl obo:GO_0008169 EC:2.1.1 obo:GO_0008169 molecular_function obo:GO_0008169 GO:0008169 obo:GO_0008169 C-methyltransferase activity obo:GO_0008170 Catalysis of the transfer of a methyl group to the nitrogen atom of an acceptor molecule. obo:GO_0008170 obo:go.owl obo:GO_0008170 EC:2.1.1 obo:GO_0008170 molecular_function obo:GO_0008170 GO:0008170 obo:GO_0008170 N-methyltransferase activity obo:GO_0008171 Catalysis of the transfer of a methyl group to the oxygen atom of an acceptor molecule. obo:GO_0008171 obo:go.owl obo:GO_0008171 EC:2.1.1 obo:GO_0008171 Reactome:R-HSA-5578717 obo:GO_0008171 Reactome:R-HSA-5629203 obo:GO_0008171 Reactome:R-HSA-5629218 obo:GO_0008171 Reactome:R-HSA-5629237 obo:GO_0008171 Reactome:R-HSA-6790907 obo:GO_0008171 molecular_function obo:GO_0008171 GO:0008171 obo:GO_0008171 O-methyltransferase activity obo:GO_0008179 Interacting selectively and non-covalently with the enzyme adenylate cyclase. obo:GO_0008179 obo:go.owl obo:GO_0008179 Reactome:R-HSA-170672 obo:GO_0008179 adenylyl cyclase binding obo:GO_0008179 molecular_function obo:GO_0008179 GO:0008179 obo:GO_0008179 adenylate cyclase binding obo:GO_0008187 Interacting selectively and non-covalently with any stretch of pyrimidines (cytosine or uracil) in an RNA molecule. obo:GO_0008187 obo:go.owl obo:GO_0008187 molecular_function obo:GO_0008187 GO:0008187 obo:GO_0008187 poly-pyrimidine tract binding obo:GO_0008190 Interacting selectively and non-covalently with eukaryotic initiation factor 4E, a polypeptide factor involved in the initiation of ribosome-mediated translation. obo:GO_0008190 obo:go.owl obo:GO_0008190 eIF4E binding obo:GO_0008190 molecular_function obo:GO_0008190 GO:0008190 obo:GO_0008190 eukaryotic initiation factor 4E binding obo:GO_0008194 Catalysis of the transfer of a glycosyl group from a UDP-sugar to a small hydrophobic molecule. obo:GO_0008194 obo:go.owl obo:GO_0008194 Reactome:R-HSA-162730 obo:GO_0008194 molecular_function obo:GO_0008194 GO:0008194 obo:GO_0008194 UDP-glycosyltransferase activity obo:GO_0008198 Interacting selectively and non-covalently with ferrous iron, Fe(II). obo:GO_0008198 obo:go.owl obo:GO_0008198 molecular_function obo:GO_0008198 GO:0008198 obo:GO_0008198 ferrous iron binding obo:GO_0008199 Interacting selectively and non-covalently with ferric iron, Fe(III). obo:GO_0008199 obo:go.owl obo:GO_0008199 molecular_function obo:GO_0008199 GO:0008199 obo:GO_0008199 ferric iron binding obo:GO_0008201 Interacting selectively and non-covalently with heparin, any member of a group of glycosaminoglycans found mainly as an intracellular component of mast cells and which consist predominantly of alternating alpha-(1->4)-linked D-galactose and N-acetyl-D-glucosamine-6-sulfate residues. obo:GO_0008201 obo:go.owl obo:GO_0008201 molecular_function obo:GO_0008201 heparan sulfate binding obo:GO_0008201 GO:0008201 obo:GO_0008201 heparin binding obo:GO_0008219 Any biological process that results in permanent cessation of all vital functions of a cell. A cell should be considered dead when any one of the following molecular or morphological criteria is met: (1) the cell has lost the integrity of its plasma membrane; (2) the cell, including its nucleus, has undergone complete fragmentation into discrete bodies (frequently referred to as apoptotic bodies). The cell corpse (or its fragments) may be engulfed by an adjacent cell in vivo, but engulfment of whole cells should not be considered a strict criteria to define cell death as, under some circumstances, live engulfed cells can be released from phagosomes (see PMID:18045538). obo:GO_0008219 obo:go.owl obo:GO_0008219 MIPS_funcat:40.10 obo:GO_0008219 biological_process obo:GO_0008219 accidental cell death obo:GO_0008219 necrosis obo:GO_0008219 GO:0008219 obo:GO_0008219 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_agr obo:GO_0008219 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0008219 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0008219 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_mouse obo:GO_0008219 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0008219 This term should not be used for direct annotation. The only exception should be when experimental data (e.g., staining with trypan blue or propidium iodide) show that cell death has occurred, but fail to provide details on death modality (accidental versus programmed). When information is provided on the cell death mechanism, annotations should be made to the appropriate descendant of 'cell death' (such as, but not limited to, GO:0097300 'programmed necrotic cell death' or GO:0006915 'apoptotic process'). Also, if experimental data suggest that a gene product influences cell death indirectly, rather than being involved in the death process directly, consider annotating to a 'regulation' term. obo:GO_0008219 cell death obo:GO_0008255 The action characteristic of ecdysis-triggering hormone, a peptide hormone that, upon receptor binding, initiates pre-ecdysis and ecdysis (i.e. cuticle shedding) through direct action on the central nervous system. obo:GO_0008255 obo:go.owl obo:GO_0008255 molecular_function obo:GO_0008255 GO:0008255 obo:GO_0008255 ecdysis-triggering hormone activity obo:GO_0008256 Catalysis of the reaction: ATP + protein L-histidine = ADP + protein N(pi)-phospho-L-histidine. obo:GO_0008256 obo:go.owl obo:GO_0008256 EC:2.7.13.1 obo:GO_0008256 MetaCyc:2.7.13.1-RXN obo:GO_0008256 ATP:protein-L-histidine N-pros-phosphotransferase activity obo:GO_0008256 ATP:protein-L-histidine Npi-phosphotransferase activity obo:GO_0008256 protein-histidine pros-kinase activity obo:GO_0008256 molecular_function obo:GO_0008256 HK2 obo:GO_0008256 GO:0008256 obo:GO_0008256 protein histidine pros-kinase activity obo:GO_0008257 Catalysis of the reaction: ATP + protein L-histidine = ADP + protein N(tau)-phospho-L-histidine. obo:GO_0008257 obo:go.owl obo:GO_0008257 EC:2.7.13.2 obo:GO_0008257 MetaCyc:2.7.13.2-RXN obo:GO_0008257 ATP:protein-L-histidine N-tele-phosphotransferase activity obo:GO_0008257 ATP:protein-L-histidine Ntau-phosphotransferase activity obo:GO_0008257 protein-histidine tele-kinase activity obo:GO_0008257 molecular_function obo:GO_0008257 HK3 obo:GO_0008257 GO:0008257 obo:GO_0008257 protein histidine tele-kinase activity obo:GO_0008266 Interacting selectively and non-covalently with a sequence of uracil residues in an RNA molecule. obo:GO_0008266 obo:go.owl obo:GO_0008266 poly(U) binding obo:GO_0008266 molecular_function obo:GO_0008266 GO:0008266 obo:GO_0008266 poly(U) RNA binding obo:GO_0008267 Interacting selectively and non-covalently with a polyglutamine tract, i.e. a series of consecutive glutamine residues, in a protein. obo:GO_0008267 obo:go.owl obo:GO_0008267 molecular_function obo:GO_0008267 GO:0008267 obo:GO_0008267 poly-glutamine tract binding obo:GO_0008270 Interacting selectively and non-covalently with zinc (Zn) ions. obo:GO_0008270 obo:go.owl obo:GO_0008270 zinc binding obo:GO_0008270 molecular_function obo:GO_0008270 GO:0008270 obo:GO_0008270 zinc ion binding obo:GO_0008272 The directed movement of sulfate into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0008272 obo:go.owl obo:GO_0008272 GO:0006870 obo:GO_0008272 MIPS_funcat:20.01.01.07.05 obo:GO_0008272 sulphate transport obo:GO_0008272 biological_process obo:GO_0008272 GO:0008272 obo:GO_0008272 sulfate transport obo:GO_0008284 Any process that activates or increases the rate or extent of cell proliferation. obo:GO_0008284 obo:go.owl obo:GO_0008284 up regulation of cell proliferation obo:GO_0008284 up-regulation of cell proliferation obo:GO_0008284 upregulation of cell proliferation obo:GO_0008284 activation of cell proliferation obo:GO_0008284 stimulation of cell proliferation obo:GO_0008284 biological_process obo:GO_0008284 positive regulation of cell proliferation obo:GO_0008284 GO:0008284 obo:GO_0008284 positive regulation of cell population proliferation obo:GO_0008285 Any process that stops, prevents or reduces the rate or extent of cell proliferation. obo:GO_0008285 obo:go.owl obo:GO_0008285 down regulation of cell proliferation obo:GO_0008285 down-regulation of cell proliferation obo:GO_0008285 downregulation of cell proliferation obo:GO_0008285 inhibition of cell proliferation obo:GO_0008285 biological_process obo:GO_0008285 negative regulation of cell proliferation obo:GO_0008285 GO:0008285 obo:GO_0008285 negative regulation of cell population proliferation obo:GO_0008289 Interacting selectively and non-covalently with a lipid. obo:GO_0008289 obo:go.owl obo:GO_0008289 MIPS_funcat:16.09 obo:GO_0008289 molecular_function obo:GO_0008289 GO:0008289 obo:GO_0008289 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_agr obo:GO_0008289 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_candida obo:GO_0008289 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0008289 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_flybase_ribbon obo:GO_0008289 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0008289 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_mouse obo:GO_0008289 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0008289 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0008289 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0008289 lipid binding obo:GO_0008301 The activity of binding selectively and non-covalently to and distorting the original structure of DNA, typically a straight helix, into a bend, or increasing the bend if the original structure was intrinsically bent due to its sequence. obo:GO_0008301 obo:go.owl obo:GO_0008301 DNA bending activity obo:GO_0008301 DNA bending involving DNA binding obo:GO_0008301 molecular_function obo:GO_0008301 GO:0008301 obo:GO_0008301 DNA binding, bending obo:GO_0008312 Interacting selectively and non-covalently with 7S RNA, the RNA component of the signal recognition particle (SRP). obo:GO_0008312 obo:go.owl obo:GO_0008312 molecular_function obo:GO_0008312 GO:0008312 obo:GO_0008312 7S RNA binding obo:GO_0008317 Interacting selectively and non-covalently with the gurken growth factor receptor. obo:GO_0008317 obo:go.owl obo:GO_0008317 gurken receptor ligand obo:GO_0008317 molecular_function obo:GO_0008317 GO:0008317 obo:GO_0008317 gurken receptor binding obo:GO_0008321 Stimulates the exchange of guanyl nucleotides associated with a GTPase of the Ral family. Under normal cellular physiological conditions, the concentration of GTP is higher than that of GDP, favoring the replacement of GDP by GTP in association with the GTPase. obo:GO_0008321 obo:go.owl obo:GO_0008321 GO:0016220 obo:GO_0008321 Reactome:R-HSA-171026 obo:GO_0008321 Ral GDP-dissociation stimulator activity obo:GO_0008321 molecular_function obo:GO_0008321 GO:0008321 obo:GO_0008321 Ral guanyl-nucleotide exchange factor activity obo:GO_0008327 Interacting selectively and non-covalently with a methylated cytosine/guanine dinucleotide. obo:GO_0008327 obo:go.owl obo:GO_0008327 molecular_function obo:GO_0008327 GO:0008327 obo:GO_0008327 methyl-CpG binding obo:GO_0008330 Catalysis of the reactions: protein threonine phosphate + H2O = protein threonine + phosphate; and protein tyrosine phosphate + H2O = protein tyrosine + phosphate. obo:GO_0008330 obo:go.owl obo:GO_0008330 EC:3.1.3 obo:GO_0008330 molecular_function obo:GO_0008330 GO:0008330 obo:GO_0008330 protein tyrosine/threonine phosphatase activity obo:GO_0008349 Catalysis of the phosphorylation of serine and threonine residues in a mitogen-activated protein kinase kinase kinase (MAPKKK), resulting in activation of MAPKKK. MAPKKK signaling pathways relay, amplify and integrate signals from the plasma membrane to the nucleus in response to a diverse range of extracellular stimuli. obo:GO_0008349 obo:go.owl obo:GO_0008349 EC:2.7.11 obo:GO_0008349 Reactome:R-HSA-177692 obo:GO_0008349 Reactome:R-HSA-936991 obo:GO_0008349 MAP4K activity obo:GO_0008349 MAPKKKK obo:GO_0008349 molecular_function obo:GO_0008349 GO:0008349 obo:GO_0008349 MAP kinase kinase kinase kinase activity obo:GO_0008353 Catalysis of the reaction: ATP + (DNA-directed RNA polymerase II) = ADP + phospho-(DNA-directed RNA polymerase II); phosphorylation occurs on residues in the carboxy-terminal domain (CTD) repeats. obo:GO_0008353 obo:go.owl obo:GO_0008353 ATP:DNA-directed RNA polymerase phosphotransferase activity obo:GO_0008353 RNA polymerase subunit kinase activity obo:GO_0008353 RNA-polymerase-subunit kinase activity obo:GO_0008353 [RNA-polymerase]-subunit kinase activity obo:GO_0008353 EC:2.7.11.23 obo:GO_0008353 MetaCyc:RNA-POLYMERASE-SUBUNIT-KINASE-RXN obo:GO_0008353 Reactome:R-HSA-167191 obo:GO_0008353 Reactome:R-HSA-170704 obo:GO_0008353 Reactome:R-HSA-170706 obo:GO_0008353 CTD kinase activity obo:GO_0008353 RNA polymerase II carboxy-terminal domain kinase activity obo:GO_0008353 molecular_function obo:GO_0008353 STK9 obo:GO_0008353 GO:0008353 obo:GO_0008353 RNA polymerase II CTD heptapeptide repeat kinase activity obo:GO_0008374 Catalysis of the transfer of an acyl group to an oxygen atom on the acceptor molecule. obo:GO_0008374 obo:go.owl obo:GO_0008374 EC:2.3.1 obo:GO_0008374 Reactome:R-HSA-1482775 obo:GO_0008374 Reactome:R-HSA-1482781 obo:GO_0008374 Reactome:R-HSA-1482850 obo:GO_0008374 Reactome:R-HSA-1482861 obo:GO_0008374 Reactome:R-HSA-1482867 obo:GO_0008374 Reactome:R-HSA-162683 obo:GO_0008374 Reactome:R-HSA-3238694 obo:GO_0008374 Reactome:R-HSA-422017 obo:GO_0008374 Reactome:R-HSA-422104 obo:GO_0008374 Reactome:R-HSA-5358343 obo:GO_0008374 Reactome:R-HSA-5483229 obo:GO_0008374 molecular_function obo:GO_0008374 GO:0008374 obo:GO_0008374 O-acyltransferase activity obo:GO_0008375 Catalysis of the transfer of an N-acetylglucosaminyl residue from UDP-N-acetyl-glucosamine to a sugar. obo:GO_0008375 obo:go.owl obo:GO_0008375 MetaCyc:2.4.1.223-RXN obo:GO_0008375 Reactome:R-HSA-5694487 obo:GO_0008375 Reactome:R-HSA-8879117 obo:GO_0008375 GlcNAc transferase activity obo:GO_0008375 molecular_function obo:GO_0008375 GO:0008375 obo:GO_0008375 acetylglucosaminyltransferase activity obo:GO_0008376 Catalysis of the transfer of an N-acetylgalactosaminyl residue from UDP-N-acetyl-galactosamine to an oligosaccharide. obo:GO_0008376 obo:go.owl obo:GO_0008376 Reactome:R-HSA-8855954 obo:GO_0008376 Reactome:R-HSA-8931648 obo:GO_0008376 Reactome:R-HSA-9605700 obo:GO_0008376 GalNAc transferase activity obo:GO_0008376 molecular_function obo:GO_0008376 GO:0008376 obo:GO_0008376 acetylgalactosaminyltransferase activity obo:GO_0008378 Catalysis of the transfer of a galactosyl group to an acceptor molecule, typically another carbohydrate or a lipid. obo:GO_0008378 obo:go.owl obo:GO_0008378 MetaCyc:2.4.1.151-RXN obo:GO_0008378 Reactome:R-HSA-1964501 obo:GO_0008378 molecular_function obo:GO_0008378 GO:0008378 obo:GO_0008378 galactosyltransferase activity obo:GO_0008384 Catalysis of the reaction: ATP + IkappaB protein = ADP + IkappaB phosphoprotein. obo:GO_0008384 obo:go.owl obo:GO_0008384 EC:2.7.11.10 obo:GO_0008384 MetaCyc:2.7.11.10-RXN obo:GO_0008384 Reactome:R-HSA-5684267 obo:GO_0008384 Reactome:R-HSA-5684275 obo:GO_0008384 ATP:IkappaB protein phosphotransferase activity obo:GO_0008384 ikappaB kinase activity obo:GO_0008384 inhibitor of NF-kappaB kinase activity obo:GO_0008384 inhibitor of NFkappaB kinase activity obo:GO_0008384 TANK-binding kinase 1 activity obo:GO_0008384 molecular_function obo:GO_0008384 CHUK obo:GO_0008384 IKBKA obo:GO_0008384 IKBKB obo:GO_0008384 IKK obo:GO_0008384 IKK-1 obo:GO_0008384 IKK-2 obo:GO_0008384 STK12 obo:GO_0008384 TBK1 obo:GO_0008384 GO:0008384 obo:GO_0008384 Note that phosphorylation of IkappaB targets it for proteasomal degradation and allows the nuclear translocation of kB. obo:GO_0008384 IkappaB kinase activity obo:GO_0008417 Catalysis of the transfer of a fucosyl group to an acceptor molecule, typically another carbohydrate or a lipid. obo:GO_0008417 obo:go.owl obo:GO_0008417 Reactome:R-HSA-9033949 obo:GO_0008417 molecular_function obo:GO_0008417 GO:0008417 obo:GO_0008417 fucosyltransferase activity obo:GO_0008420 Catalysis of the reaction: phospho-(DNA-directed RNA polymerase II) + H2O = (DNA-directed RNA polymerase II) + phosphate. obo:GO_0008420 obo:go.owl obo:GO_0008420 CTD phosphatase activity obo:GO_0008420 RNA polymerase II carboxy-terminal domain phosphatase activity obo:GO_0008420 molecular_function obo:GO_0008420 GO:0008420 obo:GO_0008420 RNA polymerase II CTD heptapeptide repeat phosphatase activity obo:GO_0008429 Interacting selectively and non-covalently with phosphatidylethanolamine, any of a class of glycerophospholipids in which a phosphatidyl group is esterified to the hydroxyl group of ethanolamine. obo:GO_0008429 obo:go.owl obo:GO_0008429 molecular_function obo:GO_0008429 GO:0008429 obo:GO_0008429 phosphatidylethanolamine binding obo:GO_0008430 Interacting selectively and non-covalently with selenium (Se). obo:GO_0008430 obo:go.owl obo:GO_0008430 molecular_function obo:GO_0008430 GO:0008430 obo:GO_0008430 selenium binding obo:GO_0008431 Interacting selectively and non-covalently with vitamin E, tocopherol, which includes a series of eight structurally similar compounds. Alpha-tocopherol is the most active form in humans and is a powerful biological antioxidant. obo:GO_0008431 obo:go.owl obo:GO_0008431 tocopherol binding obo:GO_0008431 alpha-tocopherol binding obo:GO_0008431 molecular_function obo:GO_0008431 GO:0008431 obo:GO_0008431 vitamin E binding obo:GO_0008432 Interacting selectively and non-covalently with JUN kinase, an enzyme that catalyzes the phosphorylation and activation of members of the JUN family. obo:GO_0008432 obo:go.owl obo:GO_0008432 JNK binding obo:GO_0008432 molecular_function obo:GO_0008432 GO:0008432 obo:GO_0008432 JUN kinase binding obo:GO_0008437 The action characteristic of thyrotropin-releasing hormone (TRH), a hormone released by the mammalian hypothalamus into the hypophyseal-portal circulation in response to neural and/or chemical stimuli. Upon receptor binding, TRH increases the secretion of thyroid-stimulating hormone by the anterior pituitary. obo:GO_0008437 obo:go.owl obo:GO_0008437 TRH activity obo:GO_0008437 thyrotropin releasing hormone activity obo:GO_0008437 molecular_function obo:GO_0008437 GO:0008437 obo:GO_0008437 thyrotropin-releasing hormone activity obo:GO_0008536 Interacting selectively and non-covalently with Ran, a conserved Ras-like GTP-binding protein, implicated in nucleocytoplasmic transport, cell cycle progression, spindle assembly, nuclear organization and nuclear envelope (NE) assembly. obo:GO_0008536 obo:go.owl obo:GO_0008536 Ran protein binding obo:GO_0008536 molecular_function obo:GO_0008536 Ran-binding protein obo:GO_0008536 GO:0008536 obo:GO_0008536 Ran GTPase binding obo:GO_0008545 Catalysis of the phosphorylation of tyrosine and threonine residues in a c-Jun NH2-terminal kinase (JNK), a member of a subgroup of mitogen-activated protein kinases (MAPKs), which signal in response to cytokines and exposure to environmental stress. JUN kinase kinase (JNKK) is a dual-specificity protein kinase kinase and requires activation by a serine/threonine kinase JUN kinase kinase kinase. obo:GO_0008545 obo:go.owl obo:GO_0008545 EC:2.7.11 obo:GO_0008545 Reactome:R-HSA-168162 obo:GO_0008545 JNKK obo:GO_0008545 molecular_function obo:GO_0008545 GO:0008545 obo:GO_0008545 JUN kinase kinase activity obo:GO_0008579 Catalysis of the reaction: JUN kinase serine/threonine/tyrosine phosphate + H2O = JUN kinase serine/threonine/tyrosine + phosphate. obo:GO_0008579 obo:go.owl obo:GO_0008579 molecular_function obo:GO_0008579 GO:0008579 obo:GO_0008579 JUN kinase phosphatase activity obo:GO_0008613 The action characteristic of a diuretic hormone, any peptide hormone that, upon receptor binding, regulates water balance and fluid secretion. obo:GO_0008613 obo:go.owl obo:GO_0008613 molecular_function obo:GO_0008613 GO:0008613 obo:GO_0008613 diuretic hormone activity obo:GO_0008658 Interacting selectively and non-covalently with penicillin, any antibiotic that contains the condensed beta-lactamthiazolidine ring system. obo:GO_0008658 obo:go.owl obo:GO_0008658 molecular_function obo:GO_0008658 GO:0008658 obo:GO_0008658 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0008658 penicillin binding obo:GO_0008757 Catalysis of the transfer of a methyl group from S-adenosyl-L-methionine to a substrate. obo:GO_0008757 obo:go.owl obo:GO_0008757 S-adenosyl methionine-dependent methyltransferase activity obo:GO_0008757 SAM-dependent methyltransferase activity obo:GO_0008757 molecular_function obo:GO_0008757 GO:0008757 obo:GO_0008757 S-adenosylmethionine-dependent methyltransferase activity obo:GO_0008772 Catalysis of the reaction: ATP + (isocitrate dehydrogenase (NADP)) = ADP + (isocitrate dehydrogenase (NADP)) phosphate. obo:GO_0008772 obo:go.owl obo:GO_0008772 ICDH kinase/phosphatase activity obo:GO_0008772 IDH kinase/phosphatase activity obo:GO_0008772 IDHK/P obo:GO_0008772 isocitrate dehydrogenase kinase/phosphatase activity obo:GO_0008772 EC:2.7.11.5 obo:GO_0008772 MetaCyc:PHOSICITDEHASE-RXN obo:GO_0008772 ATP:isocitrate dehydrogenase (NADP+) phosphotransferase activity obo:GO_0008772 IDH kinase activity obo:GO_0008772 isocitrate dehydrogenase (NADP) kinase activity obo:GO_0008772 isocitrate dehydrogenase (NADP+) kinase activity obo:GO_0008772 isocitrate dehydrogenase kinase (phosphorylating) activity obo:GO_0008772 isocitrate dehydrogenase kinase activity obo:GO_0008772 molecular_function obo:GO_0008772 IDH-K/P obo:GO_0008772 GO:0008772 obo:GO_0008772 [isocitrate dehydrogenase (NADP+)] kinase activity obo:GO_0009056 The chemical reactions and pathways resulting in the breakdown of substances, including the breakdown of carbon compounds with the liberation of energy for use by the cell or organism. obo:GO_0009056 obo:go.owl obo:GO_0009056 janelomax obo:GO_0009056 2012-10-17T15:52:35Z obo:GO_0009056 GO:0044243 obo:GO_0009056 GO:0044712 obo:GO_0009056 Wikipedia:Catabolism obo:GO_0009056 breakdown obo:GO_0009056 catabolism obo:GO_0009056 degradation obo:GO_0009056 multicellular organismal catabolic process obo:GO_0009056 biological_process obo:GO_0009056 single-organism catabolic process obo:GO_0009056 GO:0009056 obo:GO_0009056 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_agr obo:GO_0009056 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0009056 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0009056 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0009056 catabolic process obo:GO_0009057 The chemical reactions and pathways resulting in the breakdown of a macromolecule, any molecule of high relative molecular mass, the structure of which essentially comprises the multiple repetition of units derived, actually or conceptually, from molecules of low relative molecular mass. obo:GO_0009057 obo:go.owl obo:GO_0009057 GO:0043285 obo:GO_0009057 GO:0044266 obo:GO_0009057 biopolymer catabolic process obo:GO_0009057 macromolecule breakdown obo:GO_0009057 macromolecule catabolism obo:GO_0009057 macromolecule degradation obo:GO_0009057 multicellular organismal macromolecule catabolic process obo:GO_0009057 biological_process obo:GO_0009057 GO:0009057 obo:GO_0009057 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0009057 macromolecule catabolic process obo:GO_0009058 The chemical reactions and pathways resulting in the formation of substances; typically the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones. obo:GO_0009058 obo:go.owl obo:GO_0009058 janelomax obo:GO_0009058 2012-10-17T15:52:18Z obo:GO_0009058 GO:0044274 obo:GO_0009058 GO:0044711 obo:GO_0009058 formation obo:GO_0009058 Wikipedia:Anabolism obo:GO_0009058 anabolism obo:GO_0009058 biosynthesis obo:GO_0009058 synthesis obo:GO_0009058 multicellular organismal biosynthetic process obo:GO_0009058 biological_process obo:GO_0009058 single-organism biosynthetic process obo:GO_0009058 GO:0009058 obo:GO_0009058 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0009058 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0009058 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0009058 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0009058 biosynthetic process obo:GO_0009059 The chemical reactions and pathways resulting in the formation of a macromolecule, any molecule of high relative molecular mass, the structure of which essentially comprises the multiple repetition of units derived, actually or conceptually, from molecules of low relative molecular mass. obo:GO_0009059 obo:go.owl obo:GO_0009059 GO:0043284 obo:GO_0009059 biopolymer biosynthetic process obo:GO_0009059 macromolecule anabolism obo:GO_0009059 macromolecule biosynthesis obo:GO_0009059 macromolecule formation obo:GO_0009059 macromolecule synthesis obo:GO_0009059 biological_process obo:GO_0009059 GO:0009059 obo:GO_0009059 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0009059 macromolecule biosynthetic process obo:GO_0009100 The chemical reactions and pathways involving glycoproteins, any protein that contains covalently bound glycose (i.e. monosaccharide) residues; the glycose occurs most commonly as oligosaccharide or fairly small polysaccharide but occasionally as monosaccharide. obo:GO_0009100 obo:go.owl obo:GO_0009100 glycoprotein metabolism obo:GO_0009100 biological_process obo:GO_0009100 GO:0009100 obo:GO_0009100 glycoprotein metabolic process obo:GO_0009266 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a temperature stimulus. obo:GO_0009266 obo:go.owl obo:GO_0009266 MIPS_funcat:34.11.09 obo:GO_0009266 response to thermal stimulus obo:GO_0009266 biological_process obo:GO_0009266 GO:0009266 obo:GO_0009266 response to temperature stimulus obo:GO_0009267 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of nourishment. obo:GO_0009267 obo:go.owl obo:GO_0009267 biological_process obo:GO_0009267 GO:0009267 obo:GO_0009267 cellular response to starvation obo:GO_0009268 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a pH stimulus. pH is a measure of the acidity or basicity of an aqueous solution. obo:GO_0009268 obo:go.owl obo:GO_0009268 MIPS_funcat:32.01.04 obo:GO_0009268 MIPS_funcat:34.11.03.11 obo:GO_0009268 MIPS_funcat:36.20.35.09.03 obo:GO_0009268 biological_process obo:GO_0009268 GO:0009268 obo:GO_0009268 response to pH obo:GO_0009314 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an electromagnetic radiation stimulus. Electromagnetic radiation is a propagating wave in space with electric and magnetic components. These components oscillate at right angles to each other and to the direction of propagation. obo:GO_0009314 obo:go.owl obo:GO_0009314 MIPS_funcat:32.01.13 obo:GO_0009314 response to electromagnetic radiation stimulus obo:GO_0009314 response to radiation stimulus obo:GO_0009314 biological_process obo:GO_0009314 GO:0009314 obo:GO_0009314 Note that 'radiation' refers to electromagnetic radiation of any wavelength. obo:GO_0009314 response to radiation obo:GO_0009374 Interacting selectively and non-covalently with biotin (cis-tetrahydro-2-oxothieno(3,4-d)imidazoline-4-valeric acid), the (+) enantiomer of which is very widely distributed in cells and serves as a carrier in a number of enzymatic beta-carboxylation reactions. obo:GO_0009374 obo:go.owl obo:GO_0009374 MIPS_funcat:16.21.15 obo:GO_0009374 vitamin B7 binding obo:GO_0009374 vitamin H binding obo:GO_0009374 molecular_function obo:GO_0009374 GO:0009374 obo:GO_0009374 biotin binding obo:GO_0009408 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism. obo:GO_0009408 obo:go.owl obo:GO_0009408 GO:0006951 obo:GO_0009408 MIPS_funcat:32.01.05 obo:GO_0009408 response to heat shock obo:GO_0009408 biological_process obo:GO_0009408 GO:0009408 obo:GO_0009408 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0009408 response to heat obo:GO_0009409 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cold stimulus, a temperature stimulus below the optimal temperature for that organism. obo:GO_0009409 obo:go.owl obo:GO_0009409 MIPS_funcat:32.01.06 obo:GO_0009409 biological_process obo:GO_0009409 freezing tolerance obo:GO_0009409 GO:0009409 obo:GO_0009409 response to cold obo:GO_0009411 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an ultraviolet radiation (UV light) stimulus. Ultraviolet radiation is electromagnetic radiation with a wavelength in the range of 10 to 380 nanometers. obo:GO_0009411 obo:go.owl obo:GO_0009411 response to UV light stimulus obo:GO_0009411 response to UV radiation stimulus obo:GO_0009411 response to ultraviolet light stimulus obo:GO_0009411 response to ultraviolet radiation stimulus obo:GO_0009411 biological_process obo:GO_0009411 GO:0009411 obo:GO_0009411 response to UV obo:GO_0009416 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a light stimulus, electromagnetic radiation of wavelengths classified as infrared, visible or ultraviolet light. obo:GO_0009416 obo:go.owl obo:GO_0009416 MIPS_funcat:34.11.01 obo:GO_0009416 MIPS_funcat:34.11.01.01 obo:GO_0009416 MIPS_funcat:36.20.35.11 obo:GO_0009416 biological_process obo:GO_0009416 GO:0009416 obo:GO_0009416 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0009416 response to light stimulus obo:GO_0009432 An error-prone process for repairing damaged microbial DNA. obo:GO_0009432 obo:go.owl obo:GO_0009432 Wikipedia:SOS_response obo:GO_0009432 biological_process obo:GO_0009432 GO:0009432 obo:GO_0009432 SOS response obo:GO_0009581 The series of events in which an external stimulus is received by a cell and converted into a molecular signal. obo:GO_0009581 obo:go.owl obo:GO_0009581 biological_process obo:GO_0009581 perception of external stimulus obo:GO_0009581 GO:0009581 obo:GO_0009581 detection of external stimulus obo:GO_0009582 The series of events in which an (non-living) abiotic stimulus is received by a cell and converted into a molecular signal. obo:GO_0009582 obo:go.owl obo:GO_0009582 biological_process obo:GO_0009582 perception of abiotic stimulus obo:GO_0009582 GO:0009582 obo:GO_0009582 detection of abiotic stimulus obo:GO_0009583 The series of events in which a light stimulus (in the form of photons) is received and converted into a molecular signal. obo:GO_0009583 obo:go.owl obo:GO_0009583 MIPS_funcat:34.11.01 obo:GO_0009583 MIPS_funcat:36.20.35.11 obo:GO_0009583 detection of light obo:GO_0009583 biological_process obo:GO_0009583 perception of light obo:GO_0009583 GO:0009583 obo:GO_0009583 detection of light stimulus obo:GO_0009584 The series of events in which a visible light stimulus is received by a cell and converted into a molecular signal. A visible light stimulus is electromagnetic radiation that can be perceived visually by an organism; for organisms lacking a visual system, this can be defined as light with a wavelength within the range 380 to 780 nm. obo:GO_0009584 obo:go.owl obo:GO_0009584 biological_process obo:GO_0009584 perception of visible light obo:GO_0009584 GO:0009584 obo:GO_0009584 detection of visible light obo:GO_0009589 The series of events in which an ultraviolet radiation (UV light) stimulus is received and converted into a molecular signal. Ultraviolet radiation is electromagnetic radiation with a wavelength in the range of 10 to 380 nanometers. obo:GO_0009589 obo:go.owl obo:GO_0009589 detection of UV light stimulus obo:GO_0009589 detection of UV radiation stimulus obo:GO_0009589 detection of ultraviolet light stimulus obo:GO_0009589 detection of ultraviolet radiation stimulus obo:GO_0009589 biological_process obo:GO_0009589 perception of UV obo:GO_0009589 GO:0009589 obo:GO_0009589 detection of UV obo:GO_0009593 The series of events in which a chemical stimulus is received by a cell and converted into a molecular signal. obo:GO_0009593 obo:go.owl obo:GO_0009593 MIPS_funcat:34.11.03 obo:GO_0009593 chemoperception obo:GO_0009593 detection of chemical substance obo:GO_0009593 biological_process obo:GO_0009593 chemoreception obo:GO_0009593 perception of chemical stimulus obo:GO_0009593 perception of chemical substance obo:GO_0009593 GO:0009593 obo:GO_0009593 detection of chemical stimulus obo:GO_0009595 The series of events in which a biotic stimulus, one caused or produced by a living organism, is received and converted into a molecular signal. obo:GO_0009595 obo:go.owl obo:GO_0009595 GO:0009596 obo:GO_0009595 biological_process obo:GO_0009595 perception of biotic stimulus obo:GO_0009595 GO:0009595 obo:GO_0009595 detection of biotic stimulus obo:GO_0009605 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an external stimulus. obo:GO_0009605 obo:go.owl obo:GO_0009605 MIPS_funcat:36.20.35 obo:GO_0009605 response to environmental stimulus obo:GO_0009605 biological_process obo:GO_0009605 GO:0009605 obo:GO_0009605 http://purl.oboInOwllibrary.org/oboInOwl/go#gocheck_do_not_manually_annotate obo:GO_0009605 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0009605 Note that this term is in the subset of terms that should not be used for direct gene product annotation. Instead, select a child term or, if no appropriate child term exists, please request a new term. Direct annotations to this term may be amended during annotation QC. obo:GO_0009605 response to external stimulus obo:GO_0009607 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a biotic stimulus, a stimulus caused or produced by a living organism. obo:GO_0009607 obo:go.owl obo:GO_0009607 response to biotic stress obo:GO_0009607 biological_process obo:GO_0009607 GO:0009607 obo:GO_0009607 http://purl.oboInOwllibrary.org/oboInOwl/go#gocheck_do_not_manually_annotate obo:GO_0009607 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0009607 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0009607 Note that this term is in the subset of terms that should not be used for direct gene product annotation. Instead, select a child term or, if no appropriate child term exists, please request a new term. Direct annotations to this term may be amended during annotation QC. obo:GO_0009607 response to biotic stimulus obo:GO_0009628 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an abiotic (not derived from living organisms) stimulus. obo:GO_0009628 obo:go.owl obo:GO_0009628 response to abiotic stress obo:GO_0009628 biological_process obo:GO_0009628 GO:0009628 obo:GO_0009628 http://purl.oboInOwllibrary.org/oboInOwl/go#gocheck_do_not_manually_annotate obo:GO_0009628 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0009628 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0009628 Note that this term is in the subset of terms that should not be used for direct gene product annotation. Instead, select a child term or, if no appropriate child term exists, please request a new term. Direct annotations to this term may be amended during annotation QC. Changed definition as requested in https://github.com/geneontology/go-ontology/issues/16572. obo:GO_0009628 response to abiotic stimulus obo:GO_0009629 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a gravitational stimulus. obo:GO_0009629 obo:go.owl obo:GO_0009629 MIPS_funcat:34.11.07 obo:GO_0009629 MIPS_funcat:36.20.35.13 obo:GO_0009629 response to gravitational stimulus obo:GO_0009629 biological_process obo:GO_0009629 GO:0009629 obo:GO_0009629 response to gravity obo:GO_0009637 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a blue light stimulus. Blue light is electromagnetic radiation with a wavelength of between 440 and 500nm. obo:GO_0009637 obo:go.owl obo:GO_0009637 response to blue light stimulus obo:GO_0009637 biological_process obo:GO_0009637 GO:0009637 obo:GO_0009637 response to blue light obo:GO_0009639 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a red or far red light stimulus. Red light is electromagnetic radiation of wavelength of 580-700nm. Far red light is electromagnetic radiation of wavelength 700-800nm. An example of this response is seen at the beginning of many plant species developmental stages. These include germination, and the point when cotyledon expansion is triggered. In certain species these processes take place in response to absorption of red light by the pigment molecule phytochrome, but the signal can be reversed by exposure to far red light. During the initial phase the phytochrome molecule is only present in the red light absorbing form, but on absorption of red light it changes to a far red light absorbing form, triggering progress through development. An immediate short period of exposure to far red light entirely returns the pigment to its initial state and prevents triggering of the developmental process. A thirty minute break between red and subsequent far red light exposure renders the red light effect irreversible, and development then occurs regardless of whether far red light exposure subsequently occurs. obo:GO_0009639 obo:go.owl obo:GO_0009639 biological_process obo:GO_0009639 GO:0009639 obo:GO_0009639 response to red or far red light obo:GO_0009641 Shade avoidance is a set of responses that plants display when they are subjected to the shade of another plant. It often includes elongation, altered flowering time, increased apical dominance and altered partitioning of resources. Plants are able to distinguish between the shade of an inanimate object (e.g. a rock) and the shade of another plant due to the altered balance between red and far-red light in the shade of a plant; this balance between red and far-red light is perceived by phytochrome. obo:GO_0009641 obo:go.owl obo:GO_0009641 Wikipedia:Shade_avoidance obo:GO_0009641 biological_process obo:GO_0009641 GO:0009641 obo:GO_0009641 shade avoidance obo:GO_0009642 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a light intensity stimulus. obo:GO_0009642 obo:go.owl obo:GO_0009642 biological_process obo:GO_0009642 GO:0009642 obo:GO_0009642 response to light intensity obo:GO_0009643 A response to light intensity in which exposure to medium-intensity light results in increased tolerance to high-intensity light. obo:GO_0009643 obo:go.owl obo:GO_0009643 light acclimatization obo:GO_0009643 photoacclimation obo:GO_0009643 biological_process obo:GO_0009643 GO:0009643 obo:GO_0009643 photosynthetic acclimation obo:GO_0009644 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a high light intensity stimulus. obo:GO_0009644 obo:go.owl obo:GO_0009644 biological_process obo:GO_0009644 GO:0009644 obo:GO_0009644 response to high light intensity obo:GO_0009645 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a low light intensity stimulus. Low light intensity is defined as a level of electromagnetic radiation at or below 0.1 micromols/m2. obo:GO_0009645 obo:go.owl obo:GO_0009645 biological_process obo:GO_0009645 GO:0009645 obo:GO_0009645 response to low light intensity stimulus obo:GO_0009646 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an absence of light stimuli. obo:GO_0009646 obo:go.owl obo:GO_0009646 biological_process obo:GO_0009646 response to darkness obo:GO_0009646 GO:0009646 obo:GO_0009646 response to absence of light obo:GO_0009648 Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, a period of light or dark of a given length, measured relative to a particular duration known as the 'critical day length'. The critical day length varies between species. obo:GO_0009648 obo:go.owl obo:GO_0009648 Wikipedia:Photoperiodism obo:GO_0009648 response to day length obo:GO_0009648 response to night length obo:GO_0009648 response to photoperiod obo:GO_0009648 biological_process obo:GO_0009648 GO:0009648 obo:GO_0009648 photoperiodism obo:GO_0009650 Any process in which an organism or cell protects itself from ultraviolet radiation (UV), which may also result in resistance to repeated exposure to UV. obo:GO_0009650 obo:go.owl obo:GO_0009650 ultraviolet protection obo:GO_0009650 biological_process obo:GO_0009650 UV resistance obo:GO_0009650 UV tolerance obo:GO_0009650 ultraviolet resistance obo:GO_0009650 ultraviolet tolerance obo:GO_0009650 GO:0009650 obo:GO_0009650 UV protection obo:GO_0009651 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating an increase or decrease in the concentration of salt (particularly but not exclusively sodium and chloride ions) in the environment. obo:GO_0009651 obo:go.owl obo:GO_0009651 response to ionic osmotic stress obo:GO_0009651 salinity response obo:GO_0009651 biological_process obo:GO_0009651 GO:0009651 obo:GO_0009651 response to salt stress obo:GO_0009704 The greening response of plants grown in the dark (etiolated) as a result of chloroplast biogenesis and the accumulation of chlorophyll. obo:GO_0009704 obo:go.owl obo:GO_0009704 biological_process obo:GO_0009704 GO:0009704 obo:GO_0009704 de-etiolation obo:GO_0009730 The series of events in which a carbohydrate stimulus is received by a cell and converted into a molecular signal. obo:GO_0009730 obo:go.owl obo:GO_0009730 biological_process obo:GO_0009730 perception of carbohydrate stimulus obo:GO_0009730 GO:0009730 obo:GO_0009730 detection of carbohydrate stimulus obo:GO_0009731 The series of events in which a sucrose stimulus is received by a cell and converted into a molecular signal. obo:GO_0009731 obo:go.owl obo:GO_0009731 biological_process obo:GO_0009731 perception of sucrose stimulus obo:GO_0009731 GO:0009731 obo:GO_0009731 detection of sucrose stimulus obo:GO_0009732 The series of events in which a stimulus from a hexose is received and converted into a molecular signal. obo:GO_0009732 obo:go.owl obo:GO_0009732 biological_process obo:GO_0009732 perception of hexose stimulus obo:GO_0009732 GO:0009732 obo:GO_0009732 detection of hexose stimulus obo:GO_0009745 A series of molecular signals mediated by the detection of sucrose. obo:GO_0009745 obo:go.owl obo:GO_0009745 sucrose mediated signalling obo:GO_0009745 biological_process obo:GO_0009745 GO:0009745 obo:GO_0009745 sucrose mediated signaling obo:GO_0009747 A series of molecular signals mediated by hexose and dependent on the detection of hexokinase. obo:GO_0009747 obo:go.owl obo:GO_0009747 hexokinase-dependent signalling obo:GO_0009747 biological_process obo:GO_0009747 GO:0009747 obo:GO_0009747 hexokinase-dependent signaling obo:GO_0009748 A series of molecular signals mediated by hexose and independent of hexokinase. obo:GO_0009748 obo:go.owl obo:GO_0009748 hexokinase-independent signalling obo:GO_0009748 biological_process obo:GO_0009748 GO:0009748 obo:GO_0009748 hexokinase-independent signaling obo:GO_0009756 A series of molecular signals mediated by the detection of carbohydrate. obo:GO_0009756 obo:go.owl obo:GO_0009756 carbohydrate mediated signalling obo:GO_0009756 biological_process obo:GO_0009756 GO:0009756 obo:GO_0009756 carbohydrate mediated signaling obo:GO_0009757 A series of molecular signals mediated by the detection of hexose. obo:GO_0009757 obo:go.owl obo:GO_0009757 hexose mediated signalling obo:GO_0009757 biological_process obo:GO_0009757 GO:0009757 obo:GO_0009757 hexose mediated signaling obo:GO_0009892 Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways within a cell or an organism. obo:GO_0009892 obo:go.owl obo:GO_0009892 GO:0044252 obo:GO_0009892 down regulation of metabolic process obo:GO_0009892 down-regulation of metabolic process obo:GO_0009892 downregulation of metabolic process obo:GO_0009892 negative regulation of metabolism obo:GO_0009892 negative regulation of organismal metabolism obo:GO_0009892 inhibition of metabolic process obo:GO_0009892 inhibition of organismal metabolic process obo:GO_0009892 negative regulation of multicellular organismal metabolic process obo:GO_0009892 biological_process obo:GO_0009892 GO:0009892 obo:GO_0009892 negative regulation of metabolic process obo:GO_0009893 Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways within a cell or an organism. obo:GO_0009893 obo:go.owl obo:GO_0009893 GO:0044253 obo:GO_0009893 positive regulation of metabolism obo:GO_0009893 up regulation of metabolic process obo:GO_0009893 up-regulation of metabolic process obo:GO_0009893 upregulation of metabolic process obo:GO_0009893 activation of metabolic process obo:GO_0009893 positive regulation of multicellular organismal metabolic process obo:GO_0009893 positive regulation of organismal metabolism obo:GO_0009893 stimulation of metabolic process obo:GO_0009893 stimulation of organismal metabolic process obo:GO_0009893 up-regulation of organismal metabolic process obo:GO_0009893 biological_process obo:GO_0009893 GO:0009893 obo:GO_0009893 positive regulation of metabolic process obo:GO_0009906 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of the detection of a blue light photoperiod stimulus. Blue light is electromagnetic radiation with a wavelength of between 440 and 500nm. obo:GO_0009906 obo:go.owl obo:GO_0009906 biological_process obo:GO_0009906 GO:0009906 obo:GO_0009906 response to photoperiod, blue light obo:GO_0009907 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a red light photoperiod stimulus. Red light is electromagnetic radiation of wavelength of 580-700nm. obo:GO_0009907 obo:go.owl obo:GO_0009907 biological_process obo:GO_0009907 GO:0009907 obo:GO_0009907 response to photoperiod, red light obo:GO_0009931 Catalysis of the reactions: ATP + a protein serine = ADP + protein serine phosphate; and ATP + a protein threonine = ADP + protein threonine phosphate. These reactions are dependent on the presence of calcium ions. obo:GO_0009931 obo:go.owl obo:GO_0009931 molecular_function obo:GO_0009931 GO:0009931 obo:GO_0009931 calcium-dependent protein serine/threonine kinase activity obo:GO_0009940 Interacting selectively and non-covalently with an amino terminal propeptide, which functions as a sorting signal to sort away the soluble vacuolar protein from Golgi to lytic vacuole via clathrin-coated vesicles. obo:GO_0009940 obo:go.owl obo:GO_0009940 molecular_function obo:GO_0009940 GO:0009940 obo:GO_0009940 amino-terminal vacuolar sorting propeptide binding obo:GO_0009966 Any process that modulates the frequency, rate or extent of signal transduction. obo:GO_0009966 obo:go.owl obo:GO_0009966 GO:0035466 obo:GO_0009966 biological_process obo:GO_0009966 regulation of signaling pathway obo:GO_0009966 regulation of signalling pathway obo:GO_0009966 GO:0009966 obo:GO_0009966 regulation of signal transduction obo:GO_0009970 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of sulfate. obo:GO_0009970 obo:go.owl obo:GO_0009970 cellular response to sulphate starvation obo:GO_0009970 biological_process obo:GO_0009970 GO:0009970 obo:GO_0009970 cellular response to sulfate starvation obo:GO_0009987 Any process that is carried out at the cellular level, but not necessarily restricted to a single cell. For example, cell communication occurs among more than one cell, but occurs at the cellular level. obo:GO_0009987 obo:go.owl obo:GO_0009987 janelomax obo:GO_0009987 2012-12-11T16:56:55Z obo:GO_0009987 GO:0008151 obo:GO_0009987 GO:0044763 obo:GO_0009987 GO:0050875 obo:GO_0009987 cell physiology obo:GO_0009987 cellular physiological process obo:GO_0009987 cell growth and/or maintenance obo:GO_0009987 biological_process obo:GO_0009987 single-organism cellular process obo:GO_0009987 GO:0009987 obo:GO_0009987 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0009987 cellular process obo:GO_0009991 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an extracellular stimulus. obo:GO_0009991 obo:go.owl obo:GO_0009991 biological_process obo:GO_0009991 GO:0009991 obo:GO_0009991 response to extracellular stimulus obo:GO_0009995 The recognition of soluble molecules in the environment. obo:GO_0009995 obo:go.owl obo:GO_0009995 biological_process obo:GO_0009995 GO:0009995 obo:GO_0009995 soluble molecule recognition obo:GO_0010011 Interacting selectively and non-covalently with auxin, plant hormones that regulate aspects of plant growth. obo:GO_0010011 obo:go.owl obo:GO_0010011 auxin receptor obo:GO_0010011 molecular_function obo:GO_0010011 GO:0010011 obo:GO_0010011 auxin binding obo:GO_0010013 Interacting selectively and non-covalently with N-1-naphthylphthalamic acid, an auxin transport inhibitor. obo:GO_0010013 obo:go.owl obo:GO_0010013 molecular_function obo:GO_0010013 GO:0010013 obo:GO_0010013 N-1-naphthylphthalamic acid binding obo:GO_0010106 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of iron ions. obo:GO_0010106 obo:go.owl obo:GO_0010106 biological_process obo:GO_0010106 GO:0010106 obo:GO_0010106 cellular response to iron ion starvation obo:GO_0010108 The series of events in which a glutamine stimulus is received by a cell and converted into a molecular signal. obo:GO_0010108 obo:go.owl obo:GO_0010108 glutamine detection obo:GO_0010108 biological_process obo:GO_0010108 glutamine perception obo:GO_0010108 glutamine sensing obo:GO_0010108 GO:0010108 obo:GO_0010108 detection of glutamine obo:GO_0010114 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a red light stimulus. Red light is electromagnetic radiation of wavelength of 580-700nm. An example of this response is seen at the beginning of many plant species developmental stages. These include germination, and the point when cotyledon expansion is triggered. In certain species these processes take place in response to absorption of red light by the pigment molecule phytochrome, but the signal can be reversed by exposure to far red light. During the initial phase the phytochrome molecule is only present in the red light absorbing form, but on absorption of red light it changes to a far red light absorbing form, triggering progress through development. An immediate short period of exposure to far red light entirely returns the pigment to its initial state and prevents triggering of the developmental process. A thirty minute break between red and subsequent far red light exposure renders the red light effect irreversible, and development then occurs regardless of whether far red light exposure subsequently occurs. obo:GO_0010114 obo:go.owl obo:GO_0010114 response to red light stimulus obo:GO_0010114 biological_process obo:GO_0010114 GO:0010114 obo:GO_0010114 response to red light obo:GO_0010117 Protection mechanism used by plants under conditions of excess energy absorption as a consequence of the light reactions of photosynthesis. obo:GO_0010117 obo:go.owl obo:GO_0010117 biological_process obo:GO_0010117 GO:0010117 obo:GO_0010117 photoprotection obo:GO_0010155 Any process that modulates the frequency, rate or extent of proton transport into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0010155 obo:go.owl obo:GO_0010155 biological_process obo:GO_0010155 GO:0010155 obo:GO_0010155 regulation of proton transport obo:GO_0010165 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of X-ray radiation. An X-ray is a form of electromagnetic radiation with a wavelength in the range of 10 nanometers to 100 picometers (corresponding to frequencies in the range 30 PHz to 3 EHz). obo:GO_0010165 obo:go.owl obo:GO_0010165 response to X-ray radiation stimulus obo:GO_0010165 biological_process obo:GO_0010165 GO:0010165 obo:GO_0010165 response to X-ray obo:GO_0010180 Interacting selectively and non-covalently with the enzyme thioglucosidase. obo:GO_0010180 obo:go.owl obo:GO_0010180 myrosinase binding obo:GO_0010180 molecular_function obo:GO_0010180 GO:0010180 obo:GO_0010180 thioglucosidase binding obo:GO_0010181 Interacting selectively and non-covalently with flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. obo:GO_0010181 obo:go.owl obo:GO_0010181 MIPS_funcat:16.21.05 obo:GO_0010181 flavin mononucleotide binding obo:GO_0010181 molecular_function obo:GO_0010181 GO:0010181 obo:GO_0010181 FMN binding obo:GO_0010182 The process in which a change in the level of a mono- or disaccharide such as glucose, fructose or sucrose triggers the expression of genes controlling metabolic and developmental processes. obo:GO_0010182 obo:go.owl obo:GO_0010182 sugar mediated signalling obo:GO_0010182 biological_process obo:GO_0010182 GO:0010182 obo:GO_0010182 sugar mediated signaling pathway obo:GO_0010196 The process by which excess light energy absorbed by chlorophyll and not used to drive photosynthesis is emitted as heat. This process helps maintain the balance between dissipation and utilization of light energy to minimize generation of oxidizing molecules, thereby protecting the plant against photo-oxidative damage. obo:GO_0010196 obo:go.owl obo:GO_0010196 biological_process obo:GO_0010196 GO:0010196 obo:GO_0010196 nonphotochemical quenching obo:GO_0010201 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of the detection of a continuous far red light stimulus by the high-irradiance response system. Far red light is electromagnetic radiation of wavelength 700-800nm. The activity of the high-irradiance response system is characterized by stronger effects of continuous than pulsed light at equal total fluence. obo:GO_0010201 obo:go.owl obo:GO_0010201 biological_process obo:GO_0010201 GO:0010201 obo:GO_0010201 response to continuous far red light stimulus by the high-irradiance response system obo:GO_0010202 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a low fluence red light stimulus. Red light is electromagnetic radiation of wavelength of 580-700nm. Low fluence red light is defined in this case as short pulses of red light followed by darkness, providing a light level of 0.001-0.1 mmol/m2/sec. obo:GO_0010202 obo:go.owl obo:GO_0010202 biological_process obo:GO_0010202 GO:0010202 obo:GO_0010202 response to low fluence red light stimulus obo:GO_0010203 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a very low fluence red light stimulus. Red light is electromagnetic radiation of wavelength of 580-700nm. Very low fluence red light is defined in this case as short pulses of red light followed by darkness, providing light levels of less than 0.001 mmol/m2/sec. obo:GO_0010203 obo:go.owl obo:GO_0010203 biological_process obo:GO_0010203 GO:0010203 obo:GO_0010203 response to very low fluence red light stimulus obo:GO_0010209 Interacting selectively and non-covalently with a vacuolar sorting signal, a specific peptide sequence that acts as a signal to localize the protein within the vacuole. obo:GO_0010209 obo:go.owl obo:GO_0010209 molecular_function obo:GO_0010209 GO:0010209 obo:GO_0010209 vacuolar sorting signal binding obo:GO_0010212 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a ionizing radiation stimulus. Ionizing radiation is radiation with sufficient energy to remove electrons from atoms and may arise from spontaneous decay of unstable isotopes, resulting in alpha and beta particles and gamma rays. Ionizing radiation also includes X-rays. obo:GO_0010212 obo:go.owl obo:GO_0010212 response to ionising radiation obo:GO_0010212 response to ionizing radiation stimulus obo:GO_0010212 biological_process obo:GO_0010212 GO:0010212 obo:GO_0010212 response to ionizing radiation obo:GO_0010213 A DNA repair process that is involved in repairing UV-induced DNA damage under non-photoreactivating conditions. The mechanism by which this repair process operates has not yet been completely elucidated. obo:GO_0010213 obo:go.owl obo:GO_0010213 light-independent DNA repair obo:GO_0010213 biological_process obo:GO_0010213 GO:0010213 obo:GO_0010213 non-photoreactive DNA repair obo:GO_0010218 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of far red light stimulus. Far red light is electromagnetic radiation of wavelength 700-800nm. An example of this response is seen at the beginning of many plant species developmental stages. These include germination, and the point when cotyledon expansion is triggered. In certain species these processes take place in response to absorption of red light by the pigment molecule phytochrome, but the signal can be reversed by exposure to far red light. During the initial phase the phytochrome molecule is only present in the red light absorbing form, but on absorption of red light it changes to a far red light absorbing form, triggering progress through development. An immediate short period of exposure to far red light entirely returns the pigment to its initial state and prevents triggering of the developmental process. A thirty minute break between red and subsequent far red light exposure renders the red light effect irreversible, and development then occurs regardless of whether far red light exposure subsequently occurs. obo:GO_0010218 obo:go.owl obo:GO_0010218 response to far red light stimulus obo:GO_0010218 biological_process obo:GO_0010218 GO:0010218 obo:GO_0010218 response to far red light obo:GO_0010224 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a UV-B radiation stimulus. UV-B radiation (UV-B light) spans the wavelengths 280 to 315 nm. obo:GO_0010224 obo:go.owl obo:GO_0010224 response to UV-B light stimulus obo:GO_0010224 response to UV-B radiation stimulus obo:GO_0010224 response to UVB light stimulus obo:GO_0010224 response to UVB radiation stimulus obo:GO_0010224 response to medium wave ultraviolet light stimulus obo:GO_0010224 response to medium wave ultraviolet radiation stimulus obo:GO_0010224 biological_process obo:GO_0010224 GO:0010224 obo:GO_0010224 response to UV-B obo:GO_0010225 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a UV-C radiation stimulus. UV-C radiation (UV-C light) spans the wavelengths 100 to 280 nm. obo:GO_0010225 obo:go.owl obo:GO_0010225 response to UV-C light stimulus obo:GO_0010225 response to UV-C radiation stimulus obo:GO_0010225 response to UVC light stimulus obo:GO_0010225 response to UVC radiation stimulus obo:GO_0010225 response to germicidal ultraviolet light stimulus obo:GO_0010225 response to germicidal ultraviolet radiation stimulus obo:GO_0010225 response to shortwave ultraviolet light stimulus obo:GO_0010225 response to shortwave ultraviolet radiation stimulus obo:GO_0010225 biological_process obo:GO_0010225 GO:0010225 obo:GO_0010225 response to UV-C obo:GO_0010244 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of the detection of a low fluence blue light stimulus by the blue low-fluence system. Blue light is electromagnetic radiation with a wavelength of between 440 and 500nm. The blue low-fluence system responds to blue light at or below 0.1 micromols/m2. In certain species excitation of the blue low fluence system induces the transcription of a number of nuclear and plastid coded genes. obo:GO_0010244 obo:go.owl obo:GO_0010244 response to low fluence blue light obo:GO_0010244 response to low fluence blue light by blf system obo:GO_0010244 biological_process obo:GO_0010244 GO:0010244 obo:GO_0010244 response to low fluence blue light stimulus by blue low-fluence system obo:GO_0010247 The series of events in which a phosphate ion stimulus is received by a cell and converted into a molecular signal. obo:GO_0010247 obo:go.owl obo:GO_0010247 phosphate ion detection obo:GO_0010247 biological_process obo:GO_0010247 phosphate ion perception obo:GO_0010247 phosphate ion sensing obo:GO_0010247 GO:0010247 obo:GO_0010247 detection of phosphate ion obo:GO_0010255 The process in which a change in the level of mono- and disaccharide glucose trigger the expression of genes controlling metabolic and developmental processes. obo:GO_0010255 obo:go.owl obo:GO_0010255 glucose mediated signalling obo:GO_0010255 biological_process obo:GO_0010255 GO:0010255 obo:GO_0010255 glucose mediated signaling pathway obo:GO_0010297 Interacting selectively and non-covalently with heteropolysaccharides. A heteropolysaccharide is a glycan composed of more than one type of monosaccharide residue. obo:GO_0010297 obo:go.owl obo:GO_0010297 heteroglycan binding obo:GO_0010297 molecular_function obo:GO_0010297 GO:0010297 obo:GO_0010297 heteropolysaccharide binding obo:GO_0010313 Interacting selectively and non-covalently with phytochrome. obo:GO_0010313 obo:go.owl obo:GO_0010313 molecular_function obo:GO_0010313 GO:0010313 obo:GO_0010313 phytochrome binding obo:GO_0010314 Interacting selectively and non-covalently with phosphatidylinositol-5-phosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 5' position. obo:GO_0010314 obo:go.owl obo:GO_0010314 molecular_function obo:GO_0010314 GO:0010314 obo:GO_0010314 phosphatidylinositol-5-phosphate binding obo:GO_0010331 Interacting selectively and non-covalently with gibberellins, plant hormones that regulate aspects of plant growth. obo:GO_0010331 obo:go.owl obo:GO_0010331 molecular_function obo:GO_0010331 gibberellic acid receptor obo:GO_0010331 gibberellin receptor obo:GO_0010331 GO:0010331 obo:GO_0010331 gibberellin binding obo:GO_0010332 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a gamma radiation stimulus. Gamma radiation is a form of electromagnetic radiation (EMR) or light emission of a specific frequency produced from sub-atomic particle interaction, such as electron-positron annihilation and radioactive decay. Gamma rays are generally characterized as EMR having the highest frequency and energy, and also the shortest wavelength, within the electromagnetic radiation spectrum. obo:GO_0010332 obo:go.owl obo:GO_0010332 biological_process obo:GO_0010332 response to gamma ray obo:GO_0010332 response to gamma-ray photon obo:GO_0010332 GO:0010332 obo:GO_0010332 response to gamma radiation obo:GO_0010335 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating an increase or decrease in the concentration of non-ionic solutes (e.g. mannitol, sorbitol) in the environment. obo:GO_0010335 obo:go.owl obo:GO_0010335 biological_process obo:GO_0010335 GO:0010335 obo:GO_0010335 response to non-ionic osmotic stress obo:GO_0010340 Catalysis of the transfer of a methyl group to the carboxyl group of an acceptor molecule to form a methyl ester. obo:GO_0010340 obo:go.owl obo:GO_0010340 molecular_function obo:GO_0010340 GO:0010340 obo:GO_0010340 carboxyl-O-methyltransferase activity obo:GO_0010350 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of magnesium. obo:GO_0010350 obo:go.owl obo:GO_0010350 biological_process obo:GO_0010350 GO:0010350 obo:GO_0010350 cellular response to magnesium starvation obo:GO_0010351 The directed movement of lithium ion into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0010351 obo:go.owl obo:GO_0010351 lithium transport obo:GO_0010351 biological_process obo:GO_0010351 GO:0010351 obo:GO_0010351 lithium ion transport obo:GO_0010352 The directed movement of lithium ion out of a cell or organelle. obo:GO_0010352 obo:go.owl obo:GO_0010352 lithium export obo:GO_0010352 biological_process obo:GO_0010352 lithium ion efflux obo:GO_0010352 lithium ion export obo:GO_0010352 GO:0010352 obo:GO_0010352 lithium ion export across the plasma membrane obo:GO_0010359 Any process that modulates the frequency, rate or extent of anion channel activity. obo:GO_0010359 obo:go.owl obo:GO_0010359 biological_process obo:GO_0010359 GO:0010359 obo:GO_0010359 regulation of anion channel activity obo:GO_0010360 Any process that stops, prevents, or reduces the frequency, rate, or extent of the anion channel activity. obo:GO_0010360 obo:go.owl obo:GO_0010360 biological_process obo:GO_0010360 GO:0010360 obo:GO_0010360 negative regulation of anion channel activity obo:GO_0010361 Any process in which blue light modulates the frequency, rate or extent of anion channel activity. obo:GO_0010361 obo:go.owl obo:GO_0010361 regulation by blue light of anion channel activity obo:GO_0010361 biological_process obo:GO_0010361 GO:0010361 obo:GO_0010361 regulation of anion channel activity by blue light obo:GO_0010362 Any process in which blue light stops, prevents, or reduces the frequency, rate, or extent of the anion channel activity. obo:GO_0010362 obo:go.owl obo:GO_0010362 negative regulation by blue light of anion channel activity obo:GO_0010362 inhibition by blue light of anion channel activity obo:GO_0010362 biological_process obo:GO_0010362 GO:0010362 obo:GO_0010362 negative regulation of anion channel activity by blue light obo:GO_0010385 Interacting selectively and non-covalently with double-stranded methylated DNA. Methylation of cytosine or adenine in DNA is an important mechanism for establishing stable heritable epigenetic marks. obo:GO_0010385 obo:go.owl obo:GO_0010385 molecular_function obo:GO_0010385 GO:0010385 obo:GO_0010385 double-stranded methylated DNA binding obo:GO_0010427 Interacting selectively and non-covalently with abscisic acid, plant hormones that regulate aspects of plant growth. obo:GO_0010427 obo:go.owl obo:GO_0010427 molecular_function obo:GO_0010427 ABA binding obo:GO_0010427 abscisate binding obo:GO_0010427 GO:0010427 obo:GO_0010427 abscisic acid binding obo:GO_0010428 Interacting selectively and non-covalently with a methylated cytosine/unspecified/guanine trinucleotide. obo:GO_0010428 obo:go.owl obo:GO_0010428 molecular_function obo:GO_0010428 GO:0010428 obo:GO_0010428 methyl-CpNpG binding obo:GO_0010429 Interacting selectively and non-covalently with a methylated cytosine/unspecified/unspecified trinucleotide. obo:GO_0010429 obo:go.owl obo:GO_0010429 molecular_function obo:GO_0010429 GO:0010429 obo:GO_0010429 methyl-CpNpN binding obo:GO_0010438 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of sulfur. obo:GO_0010438 obo:go.owl obo:GO_0010438 biological_process obo:GO_0010438 GO:0010438 obo:GO_0010438 cellular response to sulfur starvation obo:GO_0010446 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a pH stimulus with pH > 7. pH is a measure of the acidity or basicity of an aqueous solution. obo:GO_0010446 obo:go.owl obo:GO_0010446 response to alkalinity obo:GO_0010446 response to basic pH obo:GO_0010446 biological_process obo:GO_0010446 GO:0010446 obo:GO_0010446 response to alkaline pH obo:GO_0010447 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a pH stimulus with pH < 7. pH is a measure of the acidity or basicity of an aqueous solution. obo:GO_0010447 obo:go.owl obo:GO_0010447 response to acidity obo:GO_0010447 biological_process obo:GO_0010447 GO:0010447 obo:GO_0010447 This term should be used to annotate instances where a cell or organism is responding to a chemical that is playing the role of an acid (e.g. proton donor) and therefore lowering the pH. If instead you wish to describe a response to a specific acid as a chemical, such as the anion portion of glutamate, please annotate to the appropriate child of GO:0001101 'response to acid chemical'. obo:GO_0010447 response to acidic pH obo:GO_0010464 Any process that modulates the frequency, rate or extent of mesenchymal cell proliferation. A mesenchymal cell is a cell that normally gives rise to other cells that are organized as three-dimensional masses, rather than sheets. obo:GO_0010464 obo:go.owl obo:GO_0010464 biological_process obo:GO_0010464 GO:0010464 obo:GO_0010464 regulation of mesenchymal cell proliferation obo:GO_0010468 Any process that modulates the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA or circRNA (for protein-coding genes) and the translation of that mRNA or circRNA into protein. Protein maturation is included when required to form an active form of a product from an inactive precursor form. obo:GO_0010468 obo:go.owl obo:GO_0010468 Wikipedia:Regulation_of_gene_expression obo:GO_0010468 regulation of protein expression obo:GO_0010468 biological_process obo:GO_0010468 regulation of gene product expression obo:GO_0010468 GO:0010468 obo:GO_0010468 This class covers any process that regulates the rate of production of a mature gene product, and so includes processes that regulate that rate by regulating the level, stability or availability of intermediates in the process of gene expression. For example, it covers any process that regulates the level, stability or availability of mRNA or circRNA for translation and thereby regulates the rate of production of the encoded protein via translation. obo:GO_0010468 regulation of gene expression obo:GO_0010498 The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds that is mediated by the proteasome. obo:GO_0010498 obo:go.owl obo:GO_0010498 proteasome-mediated protein catabolic process obo:GO_0010498 proteasome-mediated protein catabolism obo:GO_0010498 biological_process obo:GO_0010498 GO:0010498 obo:GO_0010498 proteasomal protein catabolic process obo:GO_0010522 Any process that modulates the rate of the directed movement of calcium ions into the cytosol of a cell. The cytosol is that part of the cytoplasm that does not contain membranous or particulate subcellular components. obo:GO_0010522 obo:go.owl obo:GO_0010522 biological_process obo:GO_0010522 GO:0010522 obo:GO_0010522 regulation of calcium ion transport into cytosol obo:GO_0010523 Any process that decreases the rate of the directed movement of calcium ions into the cytosol of a cell. The cytosol is that part of the cytoplasm that does not contain membranous or particulate subcellular components. obo:GO_0010523 obo:go.owl obo:GO_0010523 biological_process obo:GO_0010523 GO:0010523 obo:GO_0010523 negative regulation of calcium ion transport into cytosol obo:GO_0010524 Any process that increases the rate of the directed movement of calcium ions into the cytosol of a cell. The cytosol is that part of the cytoplasm that does not contain membranous or particulate subcellular components. obo:GO_0010524 obo:go.owl obo:GO_0010524 biological_process obo:GO_0010524 GO:0010524 obo:GO_0010524 positive regulation of calcium ion transport into cytosol obo:GO_0010736 Interacting selectively and non-covalently with the serum response element (SRE), a short sequence with dyad symmetry found in the promoters of some of the cellular immediate-early genes, regulated by serum. obo:GO_0010736 obo:go.owl obo:GO_0010736 molecular_function obo:GO_0010736 GO:0010736 obo:GO_0010736 Note that as agreed during the transcription overhaul, terms specifying binding to specific transcription regulatory motifs are no longer being created. The level of specificity GO has decided to go to is the "core promoter", "core promoter proximal region" and "enhancer". To capture more detail, please consider using column 16. obo:GO_0010736 serum response element binding obo:GO_0010765 Any process that increases the frequency, rate or extent of the directed movement of sodium ions (Na+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0010765 obo:go.owl obo:GO_0010765 biological_process obo:GO_0010765 GO:0010765 obo:GO_0010765 positive regulation of sodium ion transport obo:GO_0010766 Any process that decreases the frequency, rate or extent of the directed movement of sodium ions (Na+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0010766 obo:go.owl obo:GO_0010766 biological_process obo:GO_0010766 GO:0010766 obo:GO_0010766 negative regulation of sodium ion transport obo:GO_0010827 Any process that modulates the frequency, rate or extent of glucose transport across a membrane. Glucose transport is the directed movement of the hexose monosaccharide glucose into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0010827 obo:go.owl obo:GO_0010827 biological_process obo:GO_0010827 regulation of glucose transport obo:GO_0010827 GO:0010827 obo:GO_0010827 regulation of glucose transmembrane transport obo:GO_0010828 Any process that increases the frequency, rate or extent of glucose transport across a membrane. Glucose transport is the directed movement of the hexose monosaccharide glucose into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0010828 obo:go.owl obo:GO_0010828 biological_process obo:GO_0010828 positive regulation of glucose transport obo:GO_0010828 GO:0010828 obo:GO_0010828 positive regulation of glucose transmembrane transport obo:GO_0010829 Any process that decreases the frequency, rate or extent of glucose transport across a membrane. Glucose transport is the directed movement of the hexose monosaccharide glucose into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0010829 obo:go.owl obo:GO_0010829 biological_process obo:GO_0010829 negative regulation of glucose transport obo:GO_0010829 GO:0010829 obo:GO_0010829 negative regulation of glucose transmembrane transport obo:GO_0010837 Any process that modulates the rate, frequency or extent of keratinocyte proliferation. Keratinocyte proliferation is the multiplication or reproduction of keratinocytes, resulting in the expansion of a cell population. obo:GO_0010837 obo:go.owl obo:GO_0010837 biological_process obo:GO_0010837 GO:0010837 obo:GO_0010837 regulation of keratinocyte proliferation obo:GO_0010838 Any process that increases the rate, frequency or extent of keratinocyte proliferation. Keratinocyte proliferation is the multiplication or reproduction of keratinocytes, resulting in the expansion of a cell population. obo:GO_0010838 obo:go.owl obo:GO_0010838 biological_process obo:GO_0010838 GO:0010838 obo:GO_0010838 positive regulation of keratinocyte proliferation obo:GO_0010839 Any process that decreases the rate, frequency or extent of keratinocyte proliferation. Keratinocyte proliferation is the multiplication or reproduction of keratinocytes, resulting in the expansion of a cell population. obo:GO_0010839 obo:go.owl obo:GO_0010839 biological_process obo:GO_0010839 GO:0010839 obo:GO_0010839 negative regulation of keratinocyte proliferation obo:GO_0010844 Interacting selectively and non-covalently with a region in a genome which promotes recombination. obo:GO_0010844 obo:go.owl obo:GO_0010844 DNA binding, recombination hotspot obo:GO_0010844 molecular_function obo:GO_0010844 GO:0010844 obo:GO_0010844 recombination hotspot binding obo:GO_0010849 Any process that modulates the rate of ATP hydrolysis by an ATPase. Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + H+(in) = ADP + phosphate + H+(out), by a rotational mechanism. obo:GO_0010849 obo:go.owl obo:GO_0010849 regulation of V-type ATPase activity obo:GO_0010849 regulation of hydrogen ion transporting ATPase activity, rotational mechanism obo:GO_0010849 biological_process obo:GO_0010849 GO:0010849 obo:GO_0010849 regulation of proton-transporting ATPase activity, rotational mechanism obo:GO_0010857 Catalysis of the reaction: a protein + ATP = a phosphoprotein + ADP. This reaction requires the presence of calcium. obo:GO_0010857 obo:go.owl obo:GO_0010857 Reactome:R-HSA-8986937 obo:GO_0010857 Reactome:R-HSA-9005561 obo:GO_0010857 molecular_function obo:GO_0010857 GO:0010857 obo:GO_0010857 calcium-dependent protein kinase activity obo:GO_0010883 Any process that modulates the rate, frequency or extent of lipid storage. Lipid storage is the accumulation and maintenance in cells or tissues of lipids, compounds soluble in organic solvents but insoluble or sparingly soluble in aqueous solvents. Lipid reserves can be accumulated during early developmental stages for mobilization and utilization at later stages of development. obo:GO_0010883 obo:go.owl obo:GO_0010883 regulation of lipid sequestration obo:GO_0010883 biological_process obo:GO_0010883 GO:0010883 obo:GO_0010883 regulation of lipid storage obo:GO_0010884 Any process that increases the rate, frequency or extent of lipid storage. Lipid storage is the accumulation and maintenance in cells or tissues of lipids, compounds soluble in organic solvents but insoluble or sparingly soluble in aqueous solvents. Lipid reserves can be accumulated during early developmental stages for mobilization and utilization at later stages of development. obo:GO_0010884 obo:go.owl obo:GO_0010884 positive regulation of lipid sequestration obo:GO_0010884 biological_process obo:GO_0010884 GO:0010884 obo:GO_0010884 positive regulation of lipid storage obo:GO_0010885 Any process that modulates the rate or extent of cholesterol storage. Cholesterol storage is the accumulation and maintenance in cells or tissues of cholesterol, cholest-5-en-3 beta-ol, the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones. obo:GO_0010885 obo:go.owl obo:GO_0010885 biological_process obo:GO_0010885 GO:0010885 obo:GO_0010885 regulation of cholesterol storage obo:GO_0010886 Any process that increases the rate or extent of cholesterol storage. Cholesterol storage is the accumulation and maintenance in cells or tissues of cholesterol, cholest-5-en-3 beta-ol, the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones. obo:GO_0010886 obo:go.owl obo:GO_0010886 positive regulation of cholesterol sequestration obo:GO_0010886 biological_process obo:GO_0010886 GO:0010886 obo:GO_0010886 positive regulation of cholesterol storage obo:GO_0010887 Any process that decreases the rate or extent of cholesterol storage. Cholesterol storage is the accumulation and maintenance in cells or tissues of cholesterol, cholest-5-en-3 beta-ol, the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones. obo:GO_0010887 obo:go.owl obo:GO_0010887 negative regulation of cholesterol sequestration obo:GO_0010887 biological_process obo:GO_0010887 GO:0010887 obo:GO_0010887 negative regulation of cholesterol storage obo:GO_0010888 Any process that decreases the rate, frequency or extent of lipid storage. Lipid storage is the accumulation and maintenance in cells or tissues of lipids, compounds soluble in organic solvents but insoluble or sparingly soluble in aqueous solvents. Lipid reserves can be accumulated during early developmental stages for mobilization and utilization at later stages of development. obo:GO_0010888 obo:go.owl obo:GO_0010888 biological_process obo:GO_0010888 GO:0010888 obo:GO_0010888 negative regulation of lipid storage obo:GO_0010889 Any process that modulates the rate, frequency or extent of sequestering of triglyceride. Triglyceride sequestration is the process of binding or confining any triester of glycerol such that it is separated from other components of a biological system. obo:GO_0010889 obo:go.owl obo:GO_0010889 regulation of sequestering of triacylglycerol obo:GO_0010889 regulation of triacylglycerol sequestration obo:GO_0010889 biological_process obo:GO_0010889 GO:0010889 obo:GO_0010889 regulation of sequestering of triglyceride obo:GO_0010890 Any process that increases the rate, frequency or extent of sequestering of triglyceride. Triglyceride sequestration is the process of binding or confining any triester of glycerol such that it is separated from other components of a biological system. obo:GO_0010890 obo:go.owl obo:GO_0010890 positive regulation of sequestering of triacylglycerol obo:GO_0010890 positive regulation of triglyceride sequestration obo:GO_0010890 biological_process obo:GO_0010890 GO:0010890 obo:GO_0010890 positive regulation of sequestering of triglyceride obo:GO_0010891 Any process that decreases the rate, frequency or extent of sequestering of triglyceride. Triglyceride sequestration is the process of binding or confining any triester of glycerol such that it is separated from other components of a biological system. obo:GO_0010891 obo:go.owl obo:GO_0010891 negative regulation of sequestering of triacylglycerol obo:GO_0010891 negative regulation of triglyceride sequestration obo:GO_0010891 biological_process obo:GO_0010891 GO:0010891 obo:GO_0010891 negative regulation of sequestering of triglyceride obo:GO_0010959 Any process that modulates the frequency, rate, or extent of metal ion transport. Metal ion transport is the directed movement of metal ions, any metal ion with an electric charge, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0010959 obo:go.owl obo:GO_0010959 tanyaberardini obo:GO_0010959 2009-05-06T11:40:55Z obo:GO_0010959 biological_process obo:GO_0010959 GO:0010959 obo:GO_0010959 regulation of metal ion transport obo:GO_0010966 Any process that modulates the frequency, rate or extent of phosphate transport. Phosphate transport is the directed movement of phosphate into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0010966 obo:go.owl obo:GO_0010966 tanyaberardini obo:GO_0010966 2009-05-20T11:42:50Z obo:GO_0010966 biological_process obo:GO_0010966 GO:0010966 obo:GO_0010966 regulation of phosphate transport obo:GO_0010997 Interacting selectively and non-covalently with an anaphase-promoting complex. A ubiquitin ligase complex that degrades mitotic cyclins and anaphase inhibitory protein, thereby triggering sister chromatid separation and exit from mitosis. obo:GO_0010997 obo:go.owl obo:GO_0010997 tanyaberardini obo:GO_0010997 2009-06-10T11:18:22Z obo:GO_0010997 APC binding obo:GO_0010997 molecular_function obo:GO_0010997 GO:0010997 obo:GO_0010997 anaphase-promoting complex binding obo:GO_0014842 Any process that modulates the frequency, rate or extent of skeletal muscle satellite cell proliferation. obo:GO_0014842 obo:go.owl obo:GO_0014842 biological_process obo:GO_0014842 GO:0014842 obo:GO_0014842 regulation of skeletal muscle satellite cell proliferation obo:GO_0014843 Any process that modulates the frequency, rate or extent of satellite cell proliferation; dependent on specific growth factor activity such as fibroblast growth factors and transforming growth factor beta. obo:GO_0014843 obo:go.owl obo:GO_0014843 biological_process obo:GO_0014843 GO:0014843 obo:GO_0014843 growth factor dependent regulation of skeletal muscle satellite cell proliferation obo:GO_0014857 Any process that modulates the frequency, rate or extent of skeletal muscle cell proliferation. obo:GO_0014857 obo:go.owl obo:GO_0014857 biological_process obo:GO_0014857 GO:0014857 obo:GO_0014857 regulation of skeletal muscle cell proliferation obo:GO_0014858 Any process that activates or increases the frequency, rate or extent of skeletal muscle cell proliferation. obo:GO_0014858 obo:go.owl obo:GO_0014858 biological_process obo:GO_0014858 GO:0014858 obo:GO_0014858 positive regulation of skeletal muscle cell proliferation obo:GO_0014859 Any process that stops, prevents, or reduces the frequency, rate or extent of skeletal muscle cell proliferation. obo:GO_0014859 obo:go.owl obo:GO_0014859 biological_process obo:GO_0014859 GO:0014859 obo:GO_0014859 negative regulation of skeletal muscle cell proliferation obo:GO_0015485 Interacting selectively and non-covalently with cholesterol (cholest-5-en-3-beta-ol); the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones. obo:GO_0015485 obo:go.owl obo:GO_0015485 molecular_function obo:GO_0015485 GO:0015485 obo:GO_0015485 cholesterol binding obo:GO_0015631 Interacting selectively and non-covalently with monomeric or multimeric forms of tubulin, including microtubules. obo:GO_0015631 obo:go.owl obo:GO_0015631 molecular_function obo:GO_0015631 GO:0015631 obo:GO_0015631 tubulin binding obo:GO_0015643 Interacting selectively and non-covalently with a toxic substance, a poisonous substance that causes damage to biological systems. obo:GO_0015643 obo:go.owl obo:GO_0015643 molecular_function obo:GO_0015643 antitoxin activity obo:GO_0015643 lipoprotein antitoxin obo:GO_0015643 GO:0015643 obo:GO_0015643 toxic substance binding obo:GO_0015672 The directed movement of inorganic cations with a valency of one into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Inorganic cations are atoms or small molecules with a positive charge which do not contain carbon in covalent linkage. obo:GO_0015672 obo:go.owl obo:GO_0015672 biological_process obo:GO_0015672 GO:0015672 obo:GO_0015672 monovalent inorganic cation transport obo:GO_0015673 The directed movement of silver (Ag) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0015673 obo:go.owl obo:GO_0015673 silver transport obo:GO_0015673 biological_process obo:GO_0015673 GO:0015673 obo:GO_0015673 silver ion transport obo:GO_0015675 The directed movement of nickel (Ni) cations into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0015675 obo:go.owl obo:GO_0015675 biological_process obo:GO_0015675 GO:0015675 obo:GO_0015675 nickel cation transport obo:GO_0015676 The directed movement of vanadium (V) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0015676 obo:go.owl obo:GO_0015676 biological_process obo:GO_0015676 GO:0015676 obo:GO_0015676 vanadium ion transport obo:GO_0015677 The directed movement of copper ions into a cell or organelle. obo:GO_0015677 obo:go.owl obo:GO_0015677 copper ion uptake obo:GO_0015677 biological_process obo:GO_0015677 GO:0015677 obo:GO_0015677 copper ion import obo:GO_0015679 The directed movement of copper ions across the plasma membrane. obo:GO_0015679 obo:go.owl obo:GO_0015679 plasma membrane copper transport obo:GO_0015679 biological_process obo:GO_0015679 GO:0015679 obo:GO_0015679 plasma membrane copper ion transport obo:GO_0015685 A process in which ferric-enterobactin, the iron-bound form of the siderophore enterobactin, is transported into the cell by specific cell surface receptors. obo:GO_0015685 obo:go.owl obo:GO_0015685 ferric-enterobactin transport obo:GO_0015685 biological_process obo:GO_0015685 GO:0015685 obo:GO_0015685 ferric-enterobactin import into cell obo:GO_0015686 The directed movement of ferric triacetylfusarinine C into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0015686 obo:go.owl obo:GO_0015686 ferric triacetylfusarinine C transport obo:GO_0015686 biological_process obo:GO_0015686 GO:0015686 obo:GO_0015686 ferric triacetylfusarinine C import into cell obo:GO_0015691 The directed movement of cadmium (Cd) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0015691 obo:go.owl obo:GO_0015691 cadmium transport obo:GO_0015691 biological_process obo:GO_0015691 GO:0015691 obo:GO_0015691 cadmium ion transport obo:GO_0015692 The directed movement of lead (Pb) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0015692 obo:go.owl obo:GO_0015692 biological_process obo:GO_0015692 GO:0015692 obo:GO_0015692 lead ion transport obo:GO_0015693 The directed movement of magnesium (Mg) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0015693 obo:go.owl obo:GO_0015693 biological_process obo:GO_0015693 magnesium transport obo:GO_0015693 GO:0015693 obo:GO_0015693 magnesium ion transport obo:GO_0015694 The directed movement of mercury (Hg) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0015694 obo:go.owl obo:GO_0015694 mercury transport obo:GO_0015694 mercuric ion transport obo:GO_0015694 biological_process obo:GO_0015694 GO:0015694 obo:GO_0015694 mercury ion transport obo:GO_0015695 The directed movement of organic cations into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Organic cations are atoms or small molecules with a positive charge which contain carbon in covalent linkage. obo:GO_0015695 obo:go.owl obo:GO_0015695 biological_process obo:GO_0015695 GO:0015695 obo:GO_0015695 organic cation transport obo:GO_0015698 The directed movement of inorganic anions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Inorganic anions are atoms or small molecules with a negative charge which do not contain carbon in covalent linkage. obo:GO_0015698 obo:go.owl obo:GO_0015698 biological_process obo:GO_0015698 GO:0015698 obo:GO_0015698 inorganic anion transport obo:GO_0015702 The directed movement of chlorate into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0015702 obo:go.owl obo:GO_0015702 biological_process obo:GO_0015702 GO:0015702 obo:GO_0015702 chlorate transport obo:GO_0015706 The directed movement of nitrate into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0015706 obo:go.owl obo:GO_0015706 GO:0006872 obo:GO_0015706 GO:0080055 obo:GO_0015706 MIPS_funcat:20.01.01.07.01 obo:GO_0015706 low affinity nitrate transport obo:GO_0015706 low-affinity nitrate transport obo:GO_0015706 biological_process obo:GO_0015706 GO:0015706 obo:GO_0015706 nitrate transport obo:GO_0015707 The directed movement of nitrite into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0015707 obo:go.owl obo:GO_0015707 MIPS_funcat:20.01.01.07.03 obo:GO_0015707 biological_process obo:GO_0015707 GO:0015707 obo:GO_0015707 nitrite transport obo:GO_0015711 The directed movement of organic anions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Organic anions are atoms or small molecules with a negative charge which contain carbon in covalent linkage. obo:GO_0015711 obo:go.owl obo:GO_0015711 biological_process obo:GO_0015711 GO:0015711 obo:GO_0015711 organic anion transport obo:GO_0015760 The directed movement of glucose-6-phosphate into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Glucose-6-phosphate is a monophosphorylated derivative of glucose with the phosphate group attached to C-6. obo:GO_0015760 obo:go.owl obo:GO_0015760 biological_process obo:GO_0015760 GO:0015760 obo:GO_0015760 glucose-6-phosphate transport obo:GO_0015866 The directed movement of ADP, adenosine diphosphate, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0015866 obo:go.owl obo:GO_0015866 biological_process obo:GO_0015866 GO:0015866 obo:GO_0015866 ADP transport obo:GO_0015867 The directed movement of ATP, adenosine triphosphate, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0015867 obo:go.owl obo:GO_0015867 biological_process obo:GO_0015867 GO:0015867 obo:GO_0015867 ATP transport obo:GO_0015886 The directed movement of heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0015886 obo:go.owl obo:GO_0015886 haem transport obo:GO_0015886 biological_process obo:GO_0015886 GO:0015886 obo:GO_0015886 heme transport obo:GO_0015891 The directed movement of siderophores, low molecular weight Fe(III)-chelating substances, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0015891 obo:go.owl obo:GO_0015891 GO:0015892 obo:GO_0015891 iron-siderophore transport obo:GO_0015891 siderophore-iron transport obo:GO_0015891 iron-siderochrome transport obo:GO_0015891 siderochrome transport obo:GO_0015891 biological_process obo:GO_0015891 GO:0015891 obo:GO_0015891 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0015891 siderophore transport obo:GO_0015926 Catalysis of the hydrolysis of glucosyl compounds, substances containing a group derived from a cyclic form of glucose or a glucose derivative. obo:GO_0015926 obo:go.owl obo:GO_0015926 molecular_function obo:GO_0015926 GO:0015926 obo:GO_0015926 glucosidase activity obo:GO_0015968 A specific global change in the metabolism of a bacterial cell (the downregulation of nucleic acid and protein synthesis, and the simultaneous upregulation of protein degradation and amino acid synthesis) as a result of starvation. obo:GO_0015968 obo:go.owl obo:GO_0015968 Wikipedia:Stringent_response obo:GO_0015968 biological_process obo:GO_0015968 GO:0015968 obo:GO_0015968 stringent response obo:GO_0015985 The transport of protons across a membrane to generate an electrochemical gradient (proton-motive force) that provides energy for the synthesis of ATP or GTP. obo:GO_0015985 obo:go.owl obo:GO_0015985 biological_process obo:GO_0015985 GO:0015985 obo:GO_0015985 energy coupled proton transport, down electrochemical gradient obo:GO_0015986 The transport of protons across a membrane to generate an electrochemical gradient (proton-motive force) that powers ATP synthesis. obo:GO_0015986 obo:go.owl obo:GO_0015986 chemiosmosis obo:GO_0015986 biological_process obo:GO_0015986 GO:0015986 obo:GO_0015986 ATP synthesis coupled proton transport obo:GO_0015987 The transport of protons across a membrane to generate an electrochemical gradient (proton-motive force) that powers GTP synthesis. obo:GO_0015987 obo:go.owl obo:GO_0015987 biological_process obo:GO_0015987 GO:0015987 obo:GO_0015987 GTP synthesis coupled proton transport obo:GO_0015988 The transport of protons across a membrane and against an electrochemical gradient, using energy from a source such as ATP hydrolysis, light, or electron transport. obo:GO_0015988 obo:go.owl obo:GO_0015988 biological_process obo:GO_0015988 GO:0015988 obo:GO_0015988 energy coupled proton transmembrane transport, against electrochemical gradient obo:GO_0015989 The transport of protons against an electrochemical gradient, using energy from light. obo:GO_0015989 obo:go.owl obo:GO_0015989 biological_process obo:GO_0015989 GO:0015989 obo:GO_0015989 light-driven proton transport obo:GO_0015990 The transport of protons against an electrochemical gradient, using energy from electron transport. obo:GO_0015990 obo:go.owl obo:GO_0015990 biological_process obo:GO_0015990 GO:0015990 obo:GO_0015990 electron transport coupled proton transport obo:GO_0016015 Acts as a trigger for a pattern specification process when present at a specific concentration within a gradient. obo:GO_0016015 obo:go.owl obo:GO_0016015 molecular_function obo:GO_0016015 GO:0016015 obo:GO_0016015 morphogen activity obo:GO_0016018 Interacting selectively and non-covalently with cyclosporin A, a cyclic undecapeptide that contains several N-methylated and unusual amino acids. obo:GO_0016018 obo:go.owl obo:GO_0016018 molecular_function obo:GO_0016018 cyclophilin obo:GO_0016018 GO:0016018 obo:GO_0016018 cyclosporin A binding obo:GO_0016036 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of phosphate. obo:GO_0016036 obo:go.owl obo:GO_0016036 biological_process obo:GO_0016036 GO:0016036 obo:GO_0016036 cellular response to phosphate starvation obo:GO_0016043 A process that results in the assembly, arrangement of constituent parts, or disassembly of a cellular component. obo:GO_0016043 obo:go.owl obo:GO_0016043 GO:0044235 obo:GO_0016043 GO:0071842 obo:GO_0016043 MIPS_funcat:42 obo:GO_0016043 cell organisation obo:GO_0016043 cellular component organisation at cellular level obo:GO_0016043 cellular component organisation in other organism obo:GO_0016043 cellular component organization at cellular level obo:GO_0016043 cellular component organization in other organism obo:GO_0016043 biological_process obo:GO_0016043 cell organization and biogenesis obo:GO_0016043 GO:0016043 obo:GO_0016043 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_agr obo:GO_0016043 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_mouse obo:GO_0016043 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0016043 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0016043 cellular component organization obo:GO_0016048 The series of events in which a temperature stimulus (hot or cold) is received and converted into a molecular signal. obo:GO_0016048 obo:go.owl obo:GO_0016048 MIPS_funcat:34.11.09 obo:GO_0016048 detection of temperature obo:GO_0016048 detection of thermal stimulus obo:GO_0016048 biological_process obo:GO_0016048 perception of temperature obo:GO_0016048 GO:0016048 obo:GO_0016048 detection of temperature stimulus obo:GO_0016049 The process in which a cell irreversibly increases in size over time by accretion and biosynthetic production of matter similar to that already present. obo:GO_0016049 obo:go.owl obo:GO_0016049 GO:0048591 obo:GO_0016049 MIPS_funcat:40.01 obo:GO_0016049 cellular growth obo:GO_0016049 growth of cell obo:GO_0016049 biological_process obo:GO_0016049 cell expansion obo:GO_0016049 metabolic process resulting in cell growth obo:GO_0016049 metabolism resulting in cell growth obo:GO_0016049 non-developmental cell growth obo:GO_0016049 non-developmental growth of a unicellular organism obo:GO_0016049 GO:0016049 obo:GO_0016049 http://purl.oboInOwllibrary.org/oboInOwl/go#gocheck_do_not_annotate obo:GO_0016049 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0016049 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0016049 cell growth obo:GO_0016061 Any process that modulates the frequency, rate or extent of light-activated channel activity. obo:GO_0016061 obo:go.owl obo:GO_0016061 biological_process obo:GO_0016061 GO:0016061 obo:GO_0016061 regulation of light-activated channel activity obo:GO_0016084 The action characteristic of myostimulatory hormone, a peptide hormone that stimulates muscle contraction. obo:GO_0016084 obo:go.owl obo:GO_0016084 molecular_function obo:GO_0016084 GO:0016084 obo:GO_0016084 myostimulatory hormone activity obo:GO_0016085 The action characteristic of myostimulatory hormone, a peptide hormone that inhibits muscle contraction. obo:GO_0016085 obo:go.owl obo:GO_0016085 molecular_function obo:GO_0016085 GO:0016085 obo:GO_0016085 myoinhibitory hormone activity obo:GO_0016087 The action characteristic of ecdysiostatic hormone, a peptide hormone that inhibits ecdysone secretion. obo:GO_0016087 obo:go.owl obo:GO_0016087 molecular_function obo:GO_0016087 GO:0016087 obo:GO_0016087 ecdysiostatic hormone activity obo:GO_0016151 Interacting selectively and non-covalently with nickel (Ni) cations. obo:GO_0016151 obo:go.owl obo:GO_0016151 nickel binding obo:GO_0016151 molecular_function obo:GO_0016151 GO:0016151 obo:GO_0016151 nickel cation binding obo:GO_0016168 Interacting selectively and non-covalently with chlorophyll; any compound of magnesium complexed in a porphyrin (tetrapyrrole) ring and which functions as a photosynthetic pigment. obo:GO_0016168 obo:go.owl obo:GO_0016168 molecular_function obo:GO_0016168 GO:0016168 obo:GO_0016168 chlorophyll binding obo:GO_0016169 Interacting selectively and non-covalently with bacteriochlorophyll c, a chlorophyll of photosynthetic bacteria, for example green sulfur bacteria. obo:GO_0016169 obo:go.owl obo:GO_0016169 molecular_function obo:GO_0016169 GO:0016169 obo:GO_0016169 bacteriochlorophyll c binding obo:GO_0016170 Interacting selectively and non-covalently with the interleukin-15 receptor. obo:GO_0016170 obo:go.owl obo:GO_0016170 IL-15 obo:GO_0016170 interleukin-15 receptor ligand obo:GO_0016170 molecular_function obo:GO_0016170 GO:0016170 obo:GO_0016170 interleukin-15 receptor binding obo:GO_0016208 Interacting selectively and non-covalently with AMP, adenosine monophosphate. obo:GO_0016208 obo:go.owl obo:GO_0016208 molecular_function obo:GO_0016208 GO:0016208 obo:GO_0016208 AMP binding obo:GO_0016273 Enables the transfer of a methyl group from S-adenosyl-L-methionine to an amino group of an arginine residue. obo:GO_0016273 obo:go.owl obo:GO_0016273 EC:2.1.1.125 obo:GO_0016273 molecular_function obo:GO_0016273 GO:0016273 obo:GO_0016273 arginine N-methyltransferase activity obo:GO_0016278 Catalysis of the transfer of a methyl group from S-adenosyl-L-methionine to the epsilon-amino group of a lysine residue. obo:GO_0016278 obo:go.owl obo:GO_0016278 Reactome:R-HSA-3222237 obo:GO_0016278 Reactome:R-HSA-6805730 obo:GO_0016278 Reactome:R-HSA-6805740 obo:GO_0016278 Reactome:R-HSA-6805755 obo:GO_0016278 molecular_function obo:GO_0016278 GO:0016278 obo:GO_0016278 lysine N-methyltransferase activity obo:GO_0016301 Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule. obo:GO_0016301 obo:go.owl obo:GO_0016301 Reactome:R-HSA-6788855 obo:GO_0016301 Reactome:R-HSA-6788867 obo:GO_0016301 phosphokinase activity obo:GO_0016301 molecular_function obo:GO_0016301 GO:0016301 obo:GO_0016301 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0016301 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0016301 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0016301 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0016301 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0016301 Note that this term encompasses all activities that transfer a single phosphate group; although ATP is by far the most common phosphate donor, reactions using other phosphate donors are included in this term. obo:GO_0016301 kinase activity obo:GO_0016407 Catalysis of the transfer of an acetyl group to an acceptor molecule. obo:GO_0016407 obo:go.owl obo:GO_0016407 Reactome:R-HSA-5628871 obo:GO_0016407 Reactome:R-HSA-5660660 obo:GO_0016407 Reactome:R-HSA-5682044 obo:GO_0016407 Reactome:R-HSA-6792712 obo:GO_0016407 Reactome:R-HSA-6805638 obo:GO_0016407 Reactome:R-HSA-73736 obo:GO_0016407 acetylase activity obo:GO_0016407 molecular_function obo:GO_0016407 GO:0016407 obo:GO_0016407 acetyltransferase activity obo:GO_0016409 Catalysis of the transfer of a palmitoyl (CH3-[CH2]14-CO-) group to an acceptor molecule. obo:GO_0016409 obo:go.owl obo:GO_0016409 Reactome:R-HSA-203567 obo:GO_0016409 Reactome:R-HSA-5686304 obo:GO_0016409 molecular_function obo:GO_0016409 GO:0016409 obo:GO_0016409 palmitoyltransferase activity obo:GO_0016410 Catalysis of the transfer of an acyl group to a nitrogen atom on the acceptor molecule. obo:GO_0016410 obo:go.owl obo:GO_0016410 Reactome:R-HSA-177160 obo:GO_0016410 molecular_function obo:GO_0016410 GO:0016410 obo:GO_0016410 N-acyltransferase activity obo:GO_0016416 Catalysis of the transfer of a palmitoyl group to an oxygen atom on the acceptor molecule. obo:GO_0016416 obo:go.owl obo:GO_0016416 Reactome:R-HSA-2404137 obo:GO_0016416 Reactome:R-HSA-2453855 obo:GO_0016416 Reactome:R-HSA-2466710 obo:GO_0016416 molecular_function obo:GO_0016416 GO:0016416 obo:GO_0016416 O-palmitoyltransferase activity obo:GO_0016417 Catalysis of the transfer of an acyl group to a sulfur atom on the acceptor molecule. obo:GO_0016417 obo:go.owl obo:GO_0016417 molecular_function obo:GO_0016417 GO:0016417 obo:GO_0016417 S-acyltransferase activity obo:GO_0016418 Catalysis of the transfer of an acetyl group to a sulfur atom on the acceptor molecule. obo:GO_0016418 obo:go.owl obo:GO_0016418 EC:2.3.1.38 obo:GO_0016418 molecular_function obo:GO_0016418 GO:0016418 obo:GO_0016418 S-acetyltransferase activity obo:GO_0016462 Catalysis of the hydrolysis of a pyrophosphate bond between two phosphate groups, leaving one phosphate on each of the two fragments. obo:GO_0016462 obo:go.owl obo:GO_0016462 EC:3.6.1 obo:GO_0016462 Reactome:R-HSA-6810472 obo:GO_0016462 molecular_function obo:GO_0016462 GO:0016462 obo:GO_0016462 pyrophosphatase activity obo:GO_0016521 The action characteristic of pituitary adenylate cyclase activating polypeptide, a peptide produced in the hypothalamus that binds to receptors to exert pleiotropic effects including control of neurotransmitter release, vasodilation, bronchodilation, activation of intestinal motility, increase in insulin and histamine secretion, immune modulation, and stimulation of cell proliferation and differentiation. obo:GO_0016521 obo:go.owl obo:GO_0016521 pituitary adenylyl cyclase activating polypeptide activity obo:GO_0016521 molecular_function obo:GO_0016521 GO:0016521 obo:GO_0016521 pituitary adenylate cyclase activating polypeptide activity obo:GO_0016595 Interacting selectively and non-covalently with glutamate, the anion of 2-aminopentanedioic acid. obo:GO_0016595 obo:go.owl obo:GO_0016595 glutamic acid binding obo:GO_0016595 molecular_function obo:GO_0016595 GO:0016595 obo:GO_0016595 glutamate binding obo:GO_0016596 Interacting selectively and non-covalently with thienylcyclohexylpiperidine. obo:GO_0016596 obo:go.owl obo:GO_0016596 TCP binding obo:GO_0016596 molecular_function obo:GO_0016596 GO:0016596 obo:GO_0016596 thienylcyclohexylpiperidine binding obo:GO_0016597 Interacting selectively and non-covalently with an amino acid, organic acids containing one or more amino substituents. obo:GO_0016597 obo:go.owl obo:GO_0016597 MIPS_funcat:16.11 obo:GO_0016597 molecular_function obo:GO_0016597 GO:0016597 obo:GO_0016597 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0016597 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0016597 amino acid binding obo:GO_0016608 The action characteristic of growth hormone-releasing hormone, any of a family of peptide hormones that act on the anterior pituitary to stimulate the secretion of growth hormone and exert a trophic effect on the gland. obo:GO_0016608 obo:go.owl obo:GO_0016608 GHRF activity obo:GO_0016608 GHRH activity obo:GO_0016608 molecular_function obo:GO_0016608 GO:0016608 obo:GO_0016608 growth hormone-releasing hormone activity obo:GO_0016740 Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2. obo:GO_0016740 obo:go.owl obo:GO_0016740 EC:2 obo:GO_0016740 Reactome:R-HSA-1483089 obo:GO_0016740 Reactome:R-HSA-1483186 obo:GO_0016740 Reactome:R-HSA-5668414 obo:GO_0016740 Reactome:R-HSA-6787403 obo:GO_0016740 Reactome:R-HSA-8868783 obo:GO_0016740 molecular_function obo:GO_0016740 GO:0016740 obo:GO_0016740 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_agr obo:GO_0016740 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_aspergillus obo:GO_0016740 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_candida obo:GO_0016740 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0016740 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0016740 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_mouse obo:GO_0016740 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0016740 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0016740 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0016740 transferase activity obo:GO_0016741 Catalysis of the transfer of a one-carbon group from one compound (donor) to another (acceptor). obo:GO_0016741 obo:go.owl obo:GO_0016741 EC:2.1 obo:GO_0016741 molecular_function obo:GO_0016741 GO:0016741 obo:GO_0016741 transferase activity, transferring one-carbon groups obo:GO_0016746 Catalysis of the transfer of an acyl group from one compound (donor) to another (acceptor). obo:GO_0016746 obo:go.owl obo:GO_0016746 GO:0008415 obo:GO_0016746 EC:2.3 obo:GO_0016746 Reactome:R-HSA-159431 obo:GO_0016746 Reactome:R-HSA-192312 obo:GO_0016746 Reactome:R-HSA-193491 obo:GO_0016746 Reactome:R-HSA-6792572 obo:GO_0016746 Reactome:R-HSA-8858298 obo:GO_0016746 acyltransferase activity obo:GO_0016746 molecular_function obo:GO_0016746 GO:0016746 obo:GO_0016746 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0016746 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0016746 transferase activity, transferring acyl groups obo:GO_0016747 Catalysis of the transfer of an acyl group, other than amino-acyl, from one compound (donor) to another (acceptor). obo:GO_0016747 obo:go.owl obo:GO_0016747 EC:2.3.1 obo:GO_0016747 transferase activity, transferring groups other than amino-acyl groups obo:GO_0016747 molecular_function obo:GO_0016747 GO:0016747 obo:GO_0016747 transferase activity, transferring acyl groups other than amino-acyl groups obo:GO_0016748 Catalysis of the transfer of a succinyl (3-carboxypropanoyl) group to an acceptor molecule. obo:GO_0016748 obo:go.owl obo:GO_0016748 molecular_function obo:GO_0016748 GO:0016748 obo:GO_0016748 succinyltransferase activity obo:GO_0016751 Catalysis of the transfer of a succinyl group to a sulfur atom on the acceptor molecule. obo:GO_0016751 obo:go.owl obo:GO_0016751 molecular_function obo:GO_0016751 GO:0016751 obo:GO_0016751 S-succinyltransferase activity obo:GO_0016757 Catalysis of the transfer of a glycosyl group from one compound (donor) to another (acceptor). obo:GO_0016757 obo:go.owl obo:GO_0016757 GO:0016932 obo:GO_0016757 EC:2.4 obo:GO_0016757 Reactome:R-HSA-5173005 obo:GO_0016757 Reactome:R-HSA-6785565 obo:GO_0016757 glycosyltransferase activity obo:GO_0016757 transglycosidase activity obo:GO_0016757 transglycosylase activity obo:GO_0016757 transferase activity, transferring other glycosyl groups obo:GO_0016757 molecular_function obo:GO_0016757 GO:0016757 obo:GO_0016757 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0016757 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0016757 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0016757 Note that enzymes of class EC:2.4.99.- should also be annotated to this term. obo:GO_0016757 transferase activity, transferring glycosyl groups obo:GO_0016758 Catalysis of the transfer of a hexosyl group from one compound (donor) to another (acceptor). obo:GO_0016758 obo:go.owl obo:GO_0016758 EC:2.4.1 obo:GO_0016758 hexosyltransferase activity obo:GO_0016758 molecular_function obo:GO_0016758 GO:0016758 obo:GO_0016758 transferase activity, transferring hexosyl groups obo:GO_0016763 Catalysis of the transfer of a pentosyl group from one compound (donor) to another (acceptor). obo:GO_0016763 obo:go.owl obo:GO_0016763 EC:2.4.2 obo:GO_0016763 Reactome:R-HSA-112265 obo:GO_0016763 Reactome:R-HSA-112266 obo:GO_0016763 pentosyltransferase activity obo:GO_0016763 molecular_function obo:GO_0016763 GO:0016763 obo:GO_0016763 transferase activity, transferring pentosyl groups obo:GO_0016765 Catalysis of the transfer of an alkyl or aryl (but not methyl) group from one compound (donor) to another (acceptor). obo:GO_0016765 obo:go.owl obo:GO_0016765 GO:0016766 obo:GO_0016765 EC:2.5 obo:GO_0016765 EC:2.5.1 obo:GO_0016765 Reactome:R-HSA-4419978 obo:GO_0016765 Reactome:R-HSA-4755545 obo:GO_0016765 Reactome:R-HSA-6782893 obo:GO_0016765 transferase activity, transferring alkyl or aryl groups, other than methyl groups obo:GO_0016765 molecular_function obo:GO_0016765 GO:0016765 obo:GO_0016765 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0016765 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0016765 transferase activity, transferring alkyl or aryl (other than methyl) groups obo:GO_0016769 Catalysis of the transfer of a nitrogenous group from one compound (donor) to another (acceptor). obo:GO_0016769 obo:go.owl obo:GO_0016769 EC:2.6 obo:GO_0016769 transferase activity, transferring other nitrogenous groups obo:GO_0016769 molecular_function obo:GO_0016769 GO:0016769 obo:GO_0016769 Note that enzymes of class EC:2.6.99.- should also be annotated to this term. obo:GO_0016769 transferase activity, transferring nitrogenous groups obo:GO_0016772 Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to another (acceptor). obo:GO_0016772 obo:go.owl obo:GO_0016772 EC:2.7 obo:GO_0016772 molecular_function obo:GO_0016772 GO:0016772 obo:GO_0016772 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0016772 Note that this term encompasses all kinase activities, as well as activities that transfer other phosphorus-containing groups such as diphosphate or nucleotides. obo:GO_0016772 transferase activity, transferring phosphorus-containing groups obo:GO_0016773 Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to an alcohol group (acceptor). obo:GO_0016773 obo:go.owl obo:GO_0016773 EC:2.7.1 obo:GO_0016773 Reactome:R-HSA-2161193 obo:GO_0016773 molecular_function obo:GO_0016773 GO:0016773 obo:GO_0016773 phosphotransferase activity, alcohol group as acceptor obo:GO_0016775 Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to a nitrogenous group (acceptor). obo:GO_0016775 obo:go.owl obo:GO_0016775 EC:2.7.3 obo:GO_0016775 molecular_function obo:GO_0016775 GO:0016775 obo:GO_0016775 phosphotransferase activity, nitrogenous group as acceptor obo:GO_0016779 Catalysis of the transfer of a nucleotidyl group to a reactant. obo:GO_0016779 obo:go.owl obo:GO_0016779 EC:2.7.7 obo:GO_0016779 Reactome:R-HSA-6782434 obo:GO_0016779 molecular_function obo:GO_0016779 GO:0016779 obo:GO_0016779 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_aspergillus obo:GO_0016779 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_candida obo:GO_0016779 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0016779 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0016779 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0016779 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0016779 nucleotidyltransferase activity obo:GO_0016782 Catalysis of the transfer of a sulfur-containing group from one compound (donor) to another (acceptor). obo:GO_0016782 obo:go.owl obo:GO_0016782 EC:2.8 obo:GO_0016782 transferase activity, transferring sulphur-containing groups obo:GO_0016782 molecular_function obo:GO_0016782 GO:0016782 obo:GO_0016782 transferase activity, transferring sulfur-containing groups obo:GO_0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. Hydrolase is the systematic name for any enzyme of EC class 3. obo:GO_0016787 obo:go.owl obo:GO_0016787 EC:3 obo:GO_0016787 Reactome:R-HSA-1236938 obo:GO_0016787 Reactome:R-HSA-2029475 obo:GO_0016787 Reactome:R-HSA-5694583 obo:GO_0016787 Reactome:R-HSA-5695964 obo:GO_0016787 Reactome:R-HSA-6786190 obo:GO_0016787 Reactome:R-HSA-6788295 obo:GO_0016787 Reactome:R-HSA-8938314 obo:GO_0016787 Reactome:R-HSA-8952137 obo:GO_0016787 molecular_function obo:GO_0016787 GO:0016787 obo:GO_0016787 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_agr obo:GO_0016787 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_aspergillus obo:GO_0016787 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_candida obo:GO_0016787 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0016787 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0016787 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_mouse obo:GO_0016787 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0016787 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0016787 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0016787 hydrolase activity obo:GO_0016788 Catalysis of the hydrolysis of any ester bond. obo:GO_0016788 obo:go.owl obo:GO_0016788 EC:3.1 obo:GO_0016788 Reactome:R-HSA-162729 obo:GO_0016788 Reactome:R-HSA-9023617 obo:GO_0016788 Reactome:R-HSA-9023619 obo:GO_0016788 esterase activity obo:GO_0016788 molecular_function obo:GO_0016788 GO:0016788 obo:GO_0016788 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0016788 hydrolase activity, acting on ester bonds obo:GO_0016790 Catalysis of the reaction: RCO-SR' + H2O = RCOOH + HSR'. This reaction is the hydrolysis of a thiolester bond, an ester formed from a carboxylic acid and a thiol (i.e., RCO-SR'), such as that found in acetyl-coenzyme A. obo:GO_0016790 obo:go.owl obo:GO_0016790 EC:3.1.2 obo:GO_0016790 thiolesterase activity obo:GO_0016790 molecular_function obo:GO_0016790 GO:0016790 obo:GO_0016790 thiolester hydrolase activity obo:GO_0016791 Catalysis of the hydrolysis of phosphoric monoesters, releasing inorganic phosphate. obo:GO_0016791 obo:go.owl obo:GO_0016791 GO:0003869 obo:GO_0016791 GO:0016302 obo:GO_0016791 EC:3.1.3 obo:GO_0016791 MetaCyc:4-NITROPHENYLPHOSPHATASE-RXN obo:GO_0016791 RHEA:21664 obo:GO_0016791 Reactome:R-HSA-4419986 obo:GO_0016791 phosphoric monoester hydrolase activity obo:GO_0016791 4-nitrophenylphosphatase activity obo:GO_0016791 4-nitrophenylphosphate phosphohydrolase activity obo:GO_0016791 K-pNPPase activity obo:GO_0016791 NPPase activity obo:GO_0016791 PNPPase activity obo:GO_0016791 ecto-p-nitrophenyl phosphatase activity obo:GO_0016791 nitrophenyl phosphatase activity obo:GO_0016791 p-nitrophenylphosphatase activity obo:GO_0016791 p-nitrophenylphosphate phosphohydrolase activity obo:GO_0016791 para-nitrophenyl phosphatase activity obo:GO_0016791 molecular_function obo:GO_0016791 phosphatase obo:GO_0016791 GO:0016791 obo:GO_0016791 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_aspergillus obo:GO_0016791 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_candida obo:GO_0016791 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0016791 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0016791 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0016791 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0016791 phosphatase activity obo:GO_0016798 Catalysis of the hydrolysis of any glycosyl bond. obo:GO_0016798 obo:go.owl obo:GO_0016798 EC:3.2 obo:GO_0016798 Reactome:R-HSA-1793176 obo:GO_0016798 Reactome:R-HSA-2065233 obo:GO_0016798 glycosidase activity obo:GO_0016798 N-glycosylase obo:GO_0016798 glycosylase obo:GO_0016798 molecular_function obo:GO_0016798 GO:0016798 obo:GO_0016798 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0016798 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0016798 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0016798 hydrolase activity, acting on glycosyl bonds obo:GO_0016810 Catalysis of the hydrolysis of any carbon-nitrogen bond, C-N, with the exception of peptide bonds. obo:GO_0016810 obo:go.owl obo:GO_0016810 EC:3.5 obo:GO_0016810 Reactome:R-HSA-6803753 obo:GO_0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in other compounds obo:GO_0016810 molecular_function obo:GO_0016810 GO:0016810 obo:GO_0016810 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0016810 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0016810 Note that enzymes of class EC:3.5.99.- should also be annotated to this term. obo:GO_0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds obo:GO_0016811 Catalysis of the hydrolysis of any non-peptide carbon-nitrogen bond in a linear amide. obo:GO_0016811 obo:go.owl obo:GO_0016811 EC:3.5.1 obo:GO_0016811 molecular_function obo:GO_0016811 GO:0016811 obo:GO_0016811 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides obo:GO_0016817 Catalysis of the hydrolysis of any acid anhydride. obo:GO_0016817 obo:go.owl obo:GO_0016817 EC:3.6 obo:GO_0016817 hydrolase activity, acting on acid anhydrides, involved in cellular and subcellular movement obo:GO_0016817 molecular_function obo:GO_0016817 GO:0016817 obo:GO_0016817 hydrolase activity, acting on acid anhydrides obo:GO_0016818 Catalysis of the hydrolysis of any acid anhydride which contains phosphorus. obo:GO_0016818 obo:go.owl obo:GO_0016818 EC:3.6.1 obo:GO_0016818 molecular_function obo:GO_0016818 GO:0016818 obo:GO_0016818 hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides obo:GO_0016825 Catalysis of the hydrolysis of any acid phosphorus-nitrogen bond. obo:GO_0016825 obo:go.owl obo:GO_0016825 EC:3.9 obo:GO_0016825 molecular_function obo:GO_0016825 GO:0016825 obo:GO_0016825 hydrolase activity, acting on acid phosphorus-nitrogen bonds obo:GO_0016905 Catalysis of the reaction: ATP + myosin-heavy-chain = ADP + myosin-heavy-chain phosphate. obo:GO_0016905 obo:go.owl obo:GO_0016905 EC:2.7.11.7 obo:GO_0016905 ATP:myosin heavy-chain O-phosphotransferase activity obo:GO_0016905 ATP:myosin-heavy-chain O-phosphotransferase activity obo:GO_0016905 MIHC kinase activity obo:GO_0016905 calmodulin-dependent myosin heavy chain kinase activity obo:GO_0016905 myosin heavy chain kinase A activity obo:GO_0016905 myosin heavy-chain kinase activity obo:GO_0016905 myosin-heavy-chain kinase activity obo:GO_0016905 myosin I heavy chain kinase activity obo:GO_0016905 myosin I heavy-chain kinase activity obo:GO_0016905 myosin II heavy chain kinase activity obo:GO_0016905 myosin II heavy-chain kinase activity obo:GO_0016905 molecular_function obo:GO_0016905 MHCK obo:GO_0016905 STK6 obo:GO_0016905 GO:0016905 obo:GO_0016905 myosin heavy chain kinase activity obo:GO_0016909 Catalysis of the phosphorylation of proteins. A family of protein kinases that perform a crucial step in relaying signals from the plasma membrane to the nucleus. Strongly activated by stress signals such as heat or osmotic shock, DNA-damaging agents, inhibitors of protein synthesis and pro-inflammatory cytokines. obo:GO_0016909 obo:go.owl obo:GO_0016909 EC:2.7.11 obo:GO_0016909 SAPK obo:GO_0016909 stress-activated kinase activity obo:GO_0016909 stress-activated protein kinase activity obo:GO_0016909 molecular_function obo:GO_0016909 GO:0016909 obo:GO_0016909 SAP kinase activity obo:GO_0016913 The action characteristic of follicle-stimulating hormone (FSH), a gonadotrophic glycoprotein hormone secreted, in mammals, by the anterior pituitary gland. Upon receptor binding, FSH stimulates growth of Graafian follicles in the ovaries in females, and stimulates the epithelium of the seminiferous tubules to increase spermatogenesis. obo:GO_0016913 obo:go.owl obo:GO_0016913 FSH activity obo:GO_0016913 follicle stimulating hormone activity obo:GO_0016913 follitropin activity obo:GO_0016913 molecular_function obo:GO_0016913 GO:0016913 obo:GO_0016913 follicle-stimulating hormone activity obo:GO_0016918 Interacting selectively and non-covalently with retinal, one of the forms of vitamin A. Retinal plays an important role in the visual process in most vertebrates, combining with opsins to form visual pigments in the retina. obo:GO_0016918 obo:go.owl obo:GO_0016918 vitamin A binding obo:GO_0016918 retinaldehyde binding obo:GO_0016918 molecular_function obo:GO_0016918 UV-sensitive opsin obo:GO_0016918 blue-sensitive opsin obo:GO_0016918 green-sensitive opsin obo:GO_0016918 long-wave-sensitive opsin obo:GO_0016918 opsin obo:GO_0016918 red-sensitive opsin obo:GO_0016918 short-wave-sensitive opsin obo:GO_0016918 violet-sensitive opsin obo:GO_0016918 GO:0016918 obo:GO_0016918 retinal binding obo:GO_0016922 Interacting selectively and non-covalently, in a ligand dependent manner, with a nuclear receptor protein. obo:GO_0016922 obo:go.owl obo:GO_0016922 ligand-dependent nuclear receptor binding obo:GO_0016922 molecular_function obo:GO_0016922 ligand-dependent nuclear receptor interactor activity obo:GO_0016922 GO:0016922 obo:GO_0016922 nuclear receptor binding obo:GO_0016936 Interacting selectively and non-covalently with any glycoside in which the sugar group is galactose. obo:GO_0016936 obo:go.owl obo:GO_0016936 molecular_function obo:GO_0016936 GO:0016936 obo:GO_0016936 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0016936 galactoside binding obo:GO_0017016 Interacting selectively and non-covalently with any member of the Ras superfamily of monomeric GTPases. obo:GO_0017016 obo:go.owl obo:GO_0017016 molecular_function obo:GO_0017016 Ras interactor activity obo:GO_0017016 GO:0017016 obo:GO_0017016 Ras GTPase binding obo:GO_0017017 Catalysis of the reaction: MAP kinase serine/threonine/tyrosine phosphate + H2O = MAP kinase serine/threonine/tyrosine + phosphate. obo:GO_0017017 obo:go.owl obo:GO_0017017 dual-specificity MAP kinase phosphatase activity obo:GO_0017017 molecular_function obo:GO_0017017 GO:0017017 obo:GO_0017017 MAP kinase tyrosine/serine/threonine phosphatase activity obo:GO_0017018 Catalysis of the reaction: phosphomyosin + H2O = myosin + phosphate. obo:GO_0017018 obo:go.owl obo:GO_0017018 GO:0017019 obo:GO_0017018 Reactome:R-HSA-390593 obo:GO_0017018 Reactome:R-HSA-445699 obo:GO_0017018 myosin phosphatase, intrinsic catalyst activity obo:GO_0017018 molecular_function obo:GO_0017018 myosin phosphatase myosin binding obo:GO_0017018 GO:0017018 obo:GO_0017018 myosin phosphatase activity obo:GO_0017022 Interacting selectively and non-covalently with any part of a myosin complex; myosins are any of a superfamily of molecular motor proteins that bind to actin and use the energy of ATP hydrolysis to generate force and movement along actin filaments. obo:GO_0017022 obo:go.owl obo:GO_0017022 myosin phosphatase myosin binding obo:GO_0017022 molecular_function obo:GO_0017022 GO:0017022 obo:GO_0017022 myosin binding obo:GO_0017024 Interacting selectively and non-covalently with a class I myosin; myosin I heavy chains are single-headed, possess tails of various lengths, and do not self-associate into bipolar filaments. obo:GO_0017024 obo:go.owl obo:GO_0017024 molecular_function obo:GO_0017024 GO:0017024 obo:GO_0017024 myosin I binding obo:GO_0017025 Interacting selectively and non-covalently with a member of the class of TATA-binding proteins (TBP), including any of the TBP-related factors (TRFs). obo:GO_0017025 obo:go.owl obo:GO_0017025 TATA-binding protein binding obo:GO_0017025 TBP binding obo:GO_0017025 TBP-related factor (TRF) protein binding obo:GO_0017025 molecular_function obo:GO_0017025 GO:0017025 obo:GO_0017025 TBP-class protein binding obo:GO_0017034 Stimulates the exchange of guanyl nucleotides associated with a GTPase of the Rap family. Under normal cellular physiological conditions, the concentration of GTP is higher than that of GDP, favoring the replacement of GDP by GTP in association with the GTPase. obo:GO_0017034 obo:go.owl obo:GO_0017034 molecular_function obo:GO_0017034 GO:0017034 obo:GO_0017034 Rap guanyl-nucleotide exchange factor activity obo:GO_0017044 The action characteristic of melanocyte-stimulating hormone, any of three peptide hormones that are produced by the intermediate lobe of the pituitary gland and, upon receptor binding, cause dispersal of melanosomes in melanophores of poikilothermic vertebrates. obo:GO_0017044 obo:go.owl obo:GO_0017044 melanocyte stimulating hormone activity obo:GO_0017044 alpha-melanocyte stimulating hormone activity obo:GO_0017044 alpha-melanophore stimulating hormone activity obo:GO_0017044 molecular_function obo:GO_0017044 GO:0017044 obo:GO_0017044 melanocyte-stimulating hormone activity obo:GO_0017045 The action characteristic of corticotropin-releasing hormone (CRH), any of a number of peptides released by the mammalian hypothalamus into the hypophyseal-portal circulation in response to neural and/or chemical stimuli. Upon receptor binding, CRH increases the rate of corticotropin secretion by the anterior pituitary. obo:GO_0017045 obo:go.owl obo:GO_0017045 Wikipedia:Corticotropin-releasing_hormone obo:GO_0017045 adrenocorticotropin-releasing hormone obo:GO_0017045 molecular_function obo:GO_0017045 GO:0017045 obo:GO_0017045 corticotropin-releasing hormone activity obo:GO_0017046 Interacting selectively and non-covalently with any peptide with hormonal activity in animals. obo:GO_0017046 obo:go.owl obo:GO_0017046 polypeptide hormone binding obo:GO_0017046 molecular_function obo:GO_0017046 GO:0017046 obo:GO_0017046 peptide hormone binding obo:GO_0017048 Interacting selectively and non-covalently with Rho protein, any member of the Rho subfamily of the Ras superfamily of monomeric GTPases. Proteins in the Rho subfamily are involved in relaying signals from cell-surface receptors to the actin cytoskeleton. obo:GO_0017048 obo:go.owl obo:GO_0017048 GO:0017031 obo:GO_0017048 Rhophilin obo:GO_0017048 molecular_function obo:GO_0017048 Rho interactor activity obo:GO_0017048 GO:0017048 obo:GO_0017048 Rho GTPase binding obo:GO_0017049 Interacting selectively and non-covalently with the GTP-bound form of the Rho protein. obo:GO_0017049 obo:go.owl obo:GO_0017049 molecular_function obo:GO_0017049 GO:0017049 obo:GO_0017049 GTP-Rho binding obo:GO_0017058 Interacting selectively and non-covalently with a FH1 domain of a protein, a proline-rich domain, usually located in front of a FH2 domain. obo:GO_0017058 obo:go.owl obo:GO_0017058 molecular_function obo:GO_0017058 GO:0017058 obo:GO_0017058 FH1 domain binding obo:GO_0017069 Interacting selectively and non-covalently with a small nuclear RNA (snRNA). obo:GO_0017069 obo:go.owl obo:GO_0017069 GO:0000945 obo:GO_0017069 small nuclear RNA binding obo:GO_0017069 base pairing with snRNA obo:GO_0017069 molecular_function obo:GO_0017069 GO:0017069 obo:GO_0017069 snRNA binding obo:GO_0017070 Interacting selectively and non-covalently with the U6 small nuclear RNA (U6 snRNA). obo:GO_0017070 obo:go.owl obo:GO_0017070 molecular_function obo:GO_0017070 GO:0017070 obo:GO_0017070 Note that this term may be useful for annotating small nuclear RNAs (snRNAs). obo:GO_0017070 U6 snRNA binding obo:GO_0017075 Interacting selectively and non-covalently with the SNAP receptor syntaxin-1. obo:GO_0017075 obo:go.owl obo:GO_0017075 molecular_function obo:GO_0017075 GO:0017075 obo:GO_0017075 syntaxin-1 binding obo:GO_0017076 Interacting selectively and non-covalently with purine nucleotides, any compound consisting of a purine nucleoside esterified with (ortho)phosphate. obo:GO_0017076 obo:go.owl obo:GO_0017076 molecular_function obo:GO_0017076 GO:0017076 obo:GO_0017076 purine nucleotide binding obo:GO_0017091 Interacting selectively and non-covalently with a region of RNA containing frequent adenine and uridine bases. obo:GO_0017091 obo:go.owl obo:GO_0017091 ARE binding obo:GO_0017091 AU-specific RNA binding obo:GO_0017091 Adenylate/uridylate-rich element binding obo:GO_0017091 molecular_function obo:GO_0017091 GO:0017091 obo:GO_0017091 AU-rich element binding obo:GO_0017098 Interacting selectively and non-covalently with the sulfonylurea receptor, a regulatory subunit of the ATP-sensitive potassium ion channel. obo:GO_0017098 obo:go.owl obo:GO_0017098 sulphonylurea receptor binding obo:GO_0017098 sulfonylurea receptor ligand obo:GO_0017098 molecular_function obo:GO_0017098 GO:0017098 obo:GO_0017098 sulfonylurea receptor binding obo:GO_0017112 Stimulates the exchange of guanyl nucleotides associated with a GTPase of the Rab family. Under normal cellular physiological conditions, the concentration of GTP is higher than that of GDP, favoring the replacement of GDP by GTP in association with the GTPase. obo:GO_0017112 obo:go.owl obo:GO_0017112 Reactome:R-HSA-5617816 obo:GO_0017112 Reactome:R-HSA-5623521 obo:GO_0017112 Reactome:R-HSA-8875318 obo:GO_0017112 Reactome:R-HSA-8875320 obo:GO_0017112 Reactome:R-HSA-8876188 obo:GO_0017112 Reactome:R-HSA-8876190 obo:GO_0017112 Reactome:R-HSA-8876191 obo:GO_0017112 Reactome:R-HSA-8876193 obo:GO_0017112 Reactome:R-HSA-8876454 obo:GO_0017112 Reactome:R-HSA-8876615 obo:GO_0017112 Reactome:R-HSA-8876616 obo:GO_0017112 Reactome:R-HSA-8876837 obo:GO_0017112 Reactome:R-HSA-8877308 obo:GO_0017112 Reactome:R-HSA-8877311 obo:GO_0017112 Reactome:R-HSA-8877451 obo:GO_0017112 Reactome:R-HSA-8877475 obo:GO_0017112 Reactome:R-HSA-8877612 obo:GO_0017112 Reactome:R-HSA-8877760 obo:GO_0017112 Reactome:R-HSA-8877813 obo:GO_0017112 Reactome:R-HSA-8877998 obo:GO_0017112 molecular_function obo:GO_0017112 GO:0017112 obo:GO_0017112 Rab guanyl-nucleotide exchange factor activity obo:GO_0017124 Interacting selectively and non-covalently with a SH3 domain (Src homology 3) of a protein, small protein modules containing approximately 50 amino acid residues found in a great variety of intracellular or membrane-associated proteins. obo:GO_0017124 obo:go.owl obo:GO_0017124 molecular_function obo:GO_0017124 GO:0017124 obo:GO_0017124 SH3 domain binding obo:GO_0017129 Interacting selectively and non-covalently with any triester of glycerol. obo:GO_0017129 obo:go.owl obo:GO_0017129 triacylglycerol binding obo:GO_0017129 molecular_function obo:GO_0017129 GO:0017129 obo:GO_0017129 triglyceride binding obo:GO_0017130 Interacting selectively and non-covalently with a sequence of cytosine residues in an RNA molecule. obo:GO_0017130 obo:go.owl obo:GO_0017130 poly(C) binding obo:GO_0017130 poly(rC) binding obo:GO_0017130 molecular_function obo:GO_0017130 GO:0017130 obo:GO_0017130 poly(C) RNA binding obo:GO_0017131 Interacting selectively and non-covalently with U-rich sequence in the 3'-end of nuclear-transcribed mRNAs; required for cytoplasmic polyadenylylation. obo:GO_0017131 obo:go.owl obo:GO_0017131 U-rich CPE binding obo:GO_0017131 uridine-rich cytoplasmic polyadenylation element binding obo:GO_0017131 molecular_function obo:GO_0017131 GO:0017131 obo:GO_0017131 uridine-rich cytoplasmic polyadenylylation element binding obo:GO_0017134 Interacting selectively and non-covalently with a fibroblast growth factor. obo:GO_0017134 obo:go.owl obo:GO_0017134 GO:0048602 obo:GO_0017134 GO:0048603 obo:GO_0017134 GO:0048604 obo:GO_0017134 GO:0048605 obo:GO_0017134 GO:0048606 obo:GO_0017134 GO:0048607 obo:GO_0017134 FGF binding obo:GO_0017134 FGF 1 binding obo:GO_0017134 FGF 2 binding obo:GO_0017134 FGF 3 binding obo:GO_0017134 FGF 4 binding obo:GO_0017134 FGF 5 binding obo:GO_0017134 FGF 6 binding obo:GO_0017134 fibroblast growth factor 1 binding obo:GO_0017134 fibroblast growth factor 2 binding obo:GO_0017134 fibroblast growth factor 3 binding obo:GO_0017134 fibroblast growth factor 4 binding obo:GO_0017134 fibroblast growth factor 5 binding obo:GO_0017134 fibroblast growth factor 6 binding obo:GO_0017134 molecular_function obo:GO_0017134 GO:0017134 obo:GO_0017134 fibroblast growth factor binding obo:GO_0017137 Interacting selectively and non-covalently with Rab protein, any member of the Rab subfamily of the Ras superfamily of monomeric GTPases. obo:GO_0017137 obo:go.owl obo:GO_0017137 GO:0005084 obo:GO_0017137 REP obo:GO_0017137 Rab escort protein activity obo:GO_0017137 molecular_function obo:GO_0017137 Rab interactor activity obo:GO_0017137 GO:0017137 obo:GO_0017137 Rab GTPase binding obo:GO_0017147 Interacting selectively and non-covalently with Wnt-protein, a secreted growth factor involved in signaling. obo:GO_0017147 obo:go.owl obo:GO_0017147 molecular_function obo:GO_0017147 GO:0017147 obo:GO_0017147 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0017147 Wnt-protein binding obo:GO_0017151 Interacting selectively and non-covalently with the enzyme DEAD/H-box RNA helicase. obo:GO_0017151 obo:go.owl obo:GO_0017151 molecular_function obo:GO_0017151 GO:0017151 obo:GO_0017151 DEAD/H-box RNA helicase binding obo:GO_0017160 Interacting selectively and non-covalently with Ral protein, any member of the Ral subfamily of the Ras superfamily of monomeric GTPases. obo:GO_0017160 obo:go.owl obo:GO_0017160 GO:0034989 obo:GO_0017160 GTP-Ral binding obo:GO_0017160 molecular_function obo:GO_0017160 Ral interactor activity obo:GO_0017160 GO:0017160 obo:GO_0017160 Ral GTPase binding obo:GO_0017162 Interacting selectively and non-covalently with an aryl hydrocarbon receptor. obo:GO_0017162 obo:go.owl obo:GO_0017162 molecular_function obo:GO_0017162 GO:0017162 obo:GO_0017162 aryl hydrocarbon receptor binding obo:GO_0017166 Interacting selectively and non-covalently with vinculin, a protein found in muscle, fibroblasts, and epithelial cells that binds actin and appears to mediate attachment of actin filaments to integral proteins of the plasma membrane. obo:GO_0017166 obo:go.owl obo:GO_0017166 molecular_function obo:GO_0017166 GO:0017166 obo:GO_0017166 vinculin binding obo:GO_0017171 Catalysis of the hydrolysis of a substrate by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine). obo:GO_0017171 obo:go.owl obo:GO_0017171 molecular_function obo:GO_0017171 GO:0017171 obo:GO_0017171 serine hydrolase activity obo:GO_0018110 Catalysis of the reaction: histone L-arginine + ATP = histone N(omega)-phospho-L-arginine + ADP + 2 H(+). obo:GO_0018110 obo:go.owl obo:GO_0018110 EC:2.7.3 obo:GO_0018110 histone-arginine kinase activity obo:GO_0018110 molecular_function obo:GO_0018110 GO:0018110 obo:GO_0018110 histone arginine kinase activity obo:GO_0018130 The chemical reactions and pathways resulting in the formation of heterocyclic compounds, those with a cyclic molecular structure and at least two different atoms in the ring (or rings). obo:GO_0018130 obo:go.owl obo:GO_0018130 heterocycle anabolism obo:GO_0018130 heterocycle biosynthesis obo:GO_0018130 heterocycle formation obo:GO_0018130 heterocycle synthesis obo:GO_0018130 biological_process obo:GO_0018130 GO:0018130 obo:GO_0018130 heterocycle biosynthetic process obo:GO_0018445 The action characteristic of prothoracicotrophic hormone, a peptide hormone that is secreted by the brain and, upon receptor binding, acts on the prothoracic gland to stimulate the release of ecdysone in insects. obo:GO_0018445 obo:go.owl obo:GO_0018445 molecular_function obo:GO_0018445 GO:0018445 obo:GO_0018445 prothoracicotrophic hormone activity obo:GO_0018958 The chemical reactions and pathways involving a phenol, any compound containing one or more hydroxyl groups directly attached to an aromatic carbon ring. obo:GO_0018958 obo:go.owl obo:GO_0018958 UM-BBD_pathwayID:phe obo:GO_0018958 carbolic acid metabolic process obo:GO_0018958 carbolic acid metabolism obo:GO_0018958 hydroxybenzene metabolic process obo:GO_0018958 hydroxybenzene metabolism obo:GO_0018958 phenol-containing compound metabolism obo:GO_0018958 biological_process obo:GO_0018958 GO:0018958 obo:GO_0018958 Note that phenol metabolism is not included as a child of 'xenobiotic metabolism' because although it is synthesized industrially, phenol is also found naturally in animal wastes and other organic materials. It is often formed by the activity of microorganisms, which can chemically modify a variety of xenobiotic and naturally occurring phenolic compounds. obo:GO_0018958 phenol-containing compound metabolic process obo:GO_0019001 Interacting selectively and non-covalently with guanyl nucleotides, any compound consisting of guanosine esterified with (ortho)phosphate. obo:GO_0019001 obo:go.owl obo:GO_0019001 Reactome:R-HSA-156909 obo:GO_0019001 molecular_function obo:GO_0019001 GO:0019001 obo:GO_0019001 guanyl nucleotide binding obo:GO_0019002 Interacting selectively and non-covalently with GMP, guanosine monophosphate. obo:GO_0019002 obo:go.owl obo:GO_0019002 molecular_function obo:GO_0019002 GO:0019002 obo:GO_0019002 GMP binding obo:GO_0019003 Interacting selectively and non-covalently with GDP, guanosine 5'-diphosphate. obo:GO_0019003 obo:go.owl obo:GO_0019003 molecular_function obo:GO_0019003 GO:0019003 obo:GO_0019003 GDP binding obo:GO_0019103 Interacting selectively and non-covalently with pyrimidine nucleotide, any compound consisting of a pyrimidine nucleoside esterified with (ortho)phosphate. obo:GO_0019103 obo:go.owl obo:GO_0019103 molecular_function obo:GO_0019103 GO:0019103 obo:GO_0019103 pyrimidine nucleotide binding obo:GO_0019105 Catalysis of the transfer of a palmitoyl group to a nitrogen atom on the acceptor molecule. obo:GO_0019105 obo:go.owl obo:GO_0019105 molecular_function obo:GO_0019105 GO:0019105 obo:GO_0019105 N-palmitoyltransferase activity obo:GO_0019107 Catalysis of the transfer of a myristoyl (CH3-[CH2]12-CO-) group to an acceptor molecule. obo:GO_0019107 obo:go.owl obo:GO_0019107 Reactome:R-HSA-141367 obo:GO_0019107 Reactome:R-HSA-162914 obo:GO_0019107 molecular_function obo:GO_0019107 GO:0019107 obo:GO_0019107 myristoyltransferase activity obo:GO_0019202 Catalysis of the transfer of a phosphate group, usually from ATP, to an amino acid substrate. obo:GO_0019202 obo:go.owl obo:GO_0019202 molecular_function obo:GO_0019202 GO:0019202 obo:GO_0019202 amino acid kinase activity obo:GO_0019207 Modulates the activity of a kinase, an enzyme which catalyzes of the transfer of a phosphate group, usually from ATP, to a substrate molecule. obo:GO_0019207 obo:go.owl obo:GO_0019207 molecular_function obo:GO_0019207 GO:0019207 obo:GO_0019207 kinase regulator activity obo:GO_0019209 Binds to and increases the activity of a kinase, an enzyme which catalyzes of the transfer of a phosphate group, usually from ATP, to a substrate molecule. obo:GO_0019209 obo:go.owl obo:GO_0019209 MIPS_funcat:18.02.01.01.05 obo:GO_0019209 molecular_function obo:GO_0019209 GO:0019209 obo:GO_0019209 kinase activator activity obo:GO_0019213 Catalysis of the hydrolysis of an acetyl group or groups from a substrate molecule. obo:GO_0019213 obo:go.owl obo:GO_0019213 Reactome:R-HSA-5689000 obo:GO_0019213 molecular_function obo:GO_0019213 GO:0019213 obo:GO_0019213 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0019213 deacetylase activity obo:GO_0019215 Interacting selectively and non-covalently with an intermediate filament, a distinct elongated structure, characteristically 10 nm in diameter, that occurs in the cytoplasm of higher eukaryotic cells. Intermediate filaments form a fibrous system, composed of chemically heterogeneous subunits and involved in mechanically integrating the various components of the cytoplasmic space. obo:GO_0019215 obo:go.owl obo:GO_0019215 molecular_function obo:GO_0019215 GO:0019215 obo:GO_0019215 intermediate filament binding obo:GO_0019222 Any process that modulates the frequency, rate or extent of the chemical reactions and pathways within a cell or an organism. obo:GO_0019222 obo:go.owl obo:GO_0019222 GO:0044246 obo:GO_0019222 regulation of metabolism obo:GO_0019222 regulation of multicellular organismal metabolic process obo:GO_0019222 regulation of organismal metabolic process obo:GO_0019222 biological_process obo:GO_0019222 GO:0019222 obo:GO_0019222 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0019222 regulation of metabolic process obo:GO_0019237 Interacting selectively and non-covalently with a centromere, a region of chromosome where the spindle fibers attach during mitosis and meiosis. obo:GO_0019237 obo:go.owl obo:GO_0019237 centromere binding obo:GO_0019237 molecular_function obo:GO_0019237 GO:0019237 obo:GO_0019237 centromeric DNA binding obo:GO_0019438 The chemical reactions and pathways resulting in the formation of aromatic compounds, any substance containing an aromatic carbon ring. obo:GO_0019438 obo:go.owl obo:GO_0019438 MIPS_funcat:01.05.01.03.09 obo:GO_0019438 aromatic compound anabolism obo:GO_0019438 aromatic compound biosynthesis obo:GO_0019438 aromatic compound formation obo:GO_0019438 aromatic compound synthesis obo:GO_0019438 aromatic hydrocarbon biosynthesis obo:GO_0019438 aromatic hydrocarbon biosynthetic process obo:GO_0019438 biological_process obo:GO_0019438 GO:0019438 obo:GO_0019438 aromatic compound biosynthetic process obo:GO_0019538 The chemical reactions and pathways involving a protein. Includes protein modification. obo:GO_0019538 obo:go.owl obo:GO_0019538 GO:0006411 obo:GO_0019538 GO:0044268 obo:GO_0019538 Wikipedia:Protein_metabolism obo:GO_0019538 protein metabolic process and modification obo:GO_0019538 protein metabolism obo:GO_0019538 protein metabolism and modification obo:GO_0019538 multicellular organismal protein metabolic process obo:GO_0019538 biological_process obo:GO_0019538 GO:0019538 obo:GO_0019538 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_agr obo:GO_0019538 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_flybase_ribbon obo:GO_0019538 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_mouse obo:GO_0019538 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0019538 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0019538 protein metabolic process obo:GO_0019725 Any process involved in the maintenance of an internal steady state at the level of the cell. obo:GO_0019725 obo:go.owl obo:GO_0019725 biological_process obo:GO_0019725 GO:0019725 obo:GO_0019725 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_aspergillus obo:GO_0019725 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_candida obo:GO_0019725 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0019725 cellular homeostasis obo:GO_0019811 Interacting selectively and non-covalently with cocaine (2-beta-carbomethoxy-3-beta-benzoxytropane), an alkaloid obtained from dried leaves of the South American shrub Erythroxylon coca or by chemical synthesis. obo:GO_0019811 obo:go.owl obo:GO_0019811 molecular_function obo:GO_0019811 GO:0019811 obo:GO_0019811 cocaine binding obo:GO_0019825 Interacting selectively and non-covalently with oxygen (O2). obo:GO_0019825 obo:go.owl obo:GO_0019825 cytochrome P450 obo:GO_0019825 molecular_function obo:GO_0019825 cytochrome P450 activity obo:GO_0019825 GO:0019825 obo:GO_0019825 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0019825 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0019825 oxygen binding obo:GO_0019826 Interacting selectively and non-covalently with and responding, e.g. by conformational change, to changes in the cellular level of oxygen (O2). obo:GO_0019826 obo:go.owl obo:GO_0019826 molecular_function obo:GO_0019826 GO:0019826 obo:GO_0019826 oxygen sensor activity obo:GO_0019838 Interacting selectively and non-covalently with any growth factor, proteins or polypeptides that stimulate a cell or organism to grow or proliferate. obo:GO_0019838 obo:go.owl obo:GO_0019838 molecular_function obo:GO_0019838 neurotrophin TRK receptor activity obo:GO_0019838 GO:0019838 obo:GO_0019838 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0019838 growth factor binding obo:GO_0019840 Interacting selectively and non-covalently with any isoprenoid compound, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues. obo:GO_0019840 obo:go.owl obo:GO_0019840 molecular_function obo:GO_0019840 GO:0019840 obo:GO_0019840 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0019840 isoprenoid binding obo:GO_0019841 Interacting selectively and non-covalently with retinol, vitamin A1, 2,6,6-trimethyl-1-(9'-hydroxy-3',7'-dimethylnona-1',3',5',7'-tetraenyl)cyclohex-1-ene, one of the three components that makes up vitamin A. Retinol is an intermediate in the vision cycle and it also plays a role in growth and differentiation. obo:GO_0019841 obo:go.owl obo:GO_0019841 vitamin A1 alcohol binding obo:GO_0019841 vitamin A1 binding obo:GO_0019841 molecular_function obo:GO_0019841 GO:0019841 obo:GO_0019841 retinol binding obo:GO_0019842 Interacting selectively and non-covalently with a vitamin, one of a number of unrelated organic substances that occur in many foods in small amounts and that are necessary in trace amounts for the normal metabolic functioning of the body. obo:GO_0019842 obo:go.owl obo:GO_0019842 molecular_function obo:GO_0019842 GO:0019842 obo:GO_0019842 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0019842 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0019842 vitamin binding obo:GO_0019843 Interacting selectively and non-covalently with ribosomal RNA. obo:GO_0019843 obo:go.owl obo:GO_0019843 GO:0000944 obo:GO_0019843 base pairing with rRNA obo:GO_0019843 molecular_function obo:GO_0019843 GO:0019843 obo:GO_0019843 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0019843 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0019843 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0019843 rRNA binding obo:GO_0019862 Interacting selectively and non-covalently with an immunoglobulin of an IgA isotype. obo:GO_0019862 obo:go.owl obo:GO_0019862 molecular_function obo:GO_0019862 GO:0019862 obo:GO_0019862 IgA binding obo:GO_0019863 Interacting selectively and non-covalently with an immunoglobulin of the IgE isotype. obo:GO_0019863 obo:go.owl obo:GO_0019863 molecular_function obo:GO_0019863 GO:0019863 obo:GO_0019863 IgE binding obo:GO_0019864 Interacting selectively and non-covalently with an immunoglobulin of an IgG isotype. obo:GO_0019864 obo:go.owl obo:GO_0019864 molecular_function obo:GO_0019864 GO:0019864 obo:GO_0019864 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0019864 IgG binding obo:GO_0019865 Interacting selectively and non-covalently with an immunoglobulin. obo:GO_0019865 obo:go.owl obo:GO_0019865 molecular_function obo:GO_0019865 GO:0019865 obo:GO_0019865 immunoglobulin binding obo:GO_0019887 Modulates the activity of a protein kinase, an enzyme which phosphorylates a protein. obo:GO_0019887 obo:go.owl obo:GO_0019887 molecular_function obo:GO_0019887 GO:0019887 obo:GO_0019887 protein kinase regulator activity obo:GO_0019894 Interacting selectively and non-covalently and stoichiometrically with kinesin, a member of a superfamily of microtubule-based motor proteins that perform force-generating tasks such as organelle transport and chromosome segregation. obo:GO_0019894 obo:go.owl obo:GO_0019894 molecular_function obo:GO_0019894 GO:0019894 obo:GO_0019894 kinesin binding obo:GO_0019899 Interacting selectively and non-covalently with any enzyme. obo:GO_0019899 obo:go.owl obo:GO_0019899 molecular_function obo:GO_0019899 GO:0019899 obo:GO_0019899 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0019899 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0019899 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0019899 enzyme binding obo:GO_0019900 Interacting selectively and non-covalently with a kinase, any enzyme that catalyzes the transfer of a phosphate group. obo:GO_0019900 obo:go.owl obo:GO_0019900 molecular_function obo:GO_0019900 GO:0019900 obo:GO_0019900 kinase binding obo:GO_0019901 Interacting selectively and non-covalently with a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate. obo:GO_0019901 obo:go.owl obo:GO_0019901 molecular_function obo:GO_0019901 GO:0019901 obo:GO_0019901 protein kinase binding obo:GO_0019902 Interacting selectively and non-covalently with any phosphatase. obo:GO_0019902 obo:go.owl obo:GO_0019902 molecular_function obo:GO_0019902 GO:0019902 obo:GO_0019902 phosphatase binding obo:GO_0019903 Interacting selectively and non-covalently with any protein phosphatase. obo:GO_0019903 obo:go.owl obo:GO_0019903 molecular_function obo:GO_0019903 GO:0019903 obo:GO_0019903 protein phosphatase binding obo:GO_0019904 Interacting selectively and non-covalently with a specific domain of a protein. obo:GO_0019904 obo:go.owl obo:GO_0019904 protein domain-specific binding obo:GO_0019904 molecular_function obo:GO_0019904 GO:0019904 obo:GO_0019904 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0019904 protein domain specific binding obo:GO_0019905 Interacting selectively and non-covalently with a syntaxin, a SNAP receptor involved in the docking of synaptic vesicles at the presynaptic zone of a synapse. obo:GO_0019905 obo:go.owl obo:GO_0019905 GO:0030347 obo:GO_0019905 GO:0030349 obo:GO_0019905 GO:0050430 obo:GO_0019905 GO:0051535 obo:GO_0019905 syntaxin-13 binding obo:GO_0019905 syntaxin-2 binding obo:GO_0019905 syntaxin-5 binding obo:GO_0019905 syntaxin-6 binding obo:GO_0019905 molecular_function obo:GO_0019905 GO:0019905 obo:GO_0019905 syntaxin binding obo:GO_0019912 Catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein; increases the activity of a cyclin-dependent protein kinase (CDK). obo:GO_0019912 obo:go.owl obo:GO_0019912 GO:0019913 obo:GO_0019912 EC:2.7.11 obo:GO_0019912 CAK obo:GO_0019912 cdk-activating kinase activity obo:GO_0019912 cyclin-dependent protein kinase activating kinase, intrinsic catalyst activity obo:GO_0019912 molecular_function obo:GO_0019912 GO:0019912 obo:GO_0019912 cyclin-dependent protein kinase activating kinase activity obo:GO_0019941 The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent modification of the target protein. obo:GO_0019941 obo:go.owl obo:GO_0019941 modification-dependent protein breakdown obo:GO_0019941 modification-dependent protein catabolism obo:GO_0019941 modification-dependent protein degradation obo:GO_0019941 modification-dependent proteolysis obo:GO_0019941 modification-initiated protein catabolic process obo:GO_0019941 modification-initiated protein catabolism obo:GO_0019941 modification-initiated proteolysis obo:GO_0019941 protein-ligand-dependent protein catabolic process obo:GO_0019941 protein-ligand-dependent protein catabolism obo:GO_0019941 biological_process obo:GO_0019941 protein degradation tagging activity obo:GO_0019941 GO:0019941 obo:GO_0019941 modification-dependent protein catabolic process obo:GO_0019955 Interacting selectively and non-covalently with a cytokine, any of a group of proteins that function to control the survival, growth and differentiation of tissues and cells, and which have autocrine and paracrine activity. obo:GO_0019955 obo:go.owl obo:GO_0019955 GO:0019965 obo:GO_0019955 IL binding obo:GO_0019955 interleukin binding obo:GO_0019955 molecular_function obo:GO_0019955 GO:0019955 obo:GO_0019955 cytokine binding obo:GO_0019956 Interacting selectively and non-covalently with a chemokine. Chemokines are a family of small chemotactic cytokines; their name is derived from their ability to induce directed chemotaxis in nearby responsive cells. All chemokines possess a number of conserved cysteine residues involved in intramolecular disulfide bond formation. Some chemokines are considered pro-inflammatory and can be induced during an immune response to recruit cells of the immune system to a site of infection, while others are considered homeostatic and are involved in controlling the migration of cells during normal processes of tissue maintenance or development. Chemokines are found in all vertebrates, some viruses and some bacteria. obo:GO_0019956 obo:go.owl obo:GO_0019956 molecular_function obo:GO_0019956 GO:0019956 obo:GO_0019956 chemokine binding obo:GO_0019957 Interacting selectively and non-covalently with a C-C chemokine; C-C chemokines do not have an amino acid between the first two cysteines of the characteristic four-cysteine motif. obo:GO_0019957 obo:go.owl obo:GO_0019957 molecular_function obo:GO_0019957 GO:0019957 obo:GO_0019957 C-C chemokine binding obo:GO_0019958 Interacting selectively and non-covalently with a C-X-C chemokine; C-X-C chemokines have a single amino acid between the first two cysteines of the characteristic four cysteine motif. obo:GO_0019958 obo:go.owl obo:GO_0019958 molecular_function obo:GO_0019958 GO:0019958 obo:GO_0019958 C-X-C chemokine binding obo:GO_0019959 Interacting selectively and non-covalently with interleukin-8. obo:GO_0019959 obo:go.owl obo:GO_0019959 IL-8 binding obo:GO_0019959 molecular_function obo:GO_0019959 GO:0019959 obo:GO_0019959 interleukin-8 binding obo:GO_0019960 Interacting selectively and non-covalently with a C-X3-C chemokine; C-X3-C chemokines have three amino acids between the first two cysteines of the characteristic four-cysteine motif. obo:GO_0019960 obo:go.owl obo:GO_0019960 molecular_function obo:GO_0019960 GO:0019960 obo:GO_0019960 C-X3-C chemokine binding obo:GO_0019961 Interacting selectively and non-covalently with an interferon, a protein produced by the immune systems of many animals in response to a challenge by a foreign agent. obo:GO_0019961 obo:go.owl obo:GO_0019961 IFN binding obo:GO_0019961 molecular_function obo:GO_0019961 GO:0019961 obo:GO_0019961 interferon binding obo:GO_0019962 Interacting selectively and non-covalently with a type I interferon. Type I interferons include the interferon-alpha, beta, delta, epsilon, zeta, kappa, tau, and omega gene families. obo:GO_0019962 obo:go.owl obo:GO_0019962 type I IFN binding obo:GO_0019962 interferon-alpha binding obo:GO_0019962 interferon-alpha/beta binding obo:GO_0019962 interferon-beta binding obo:GO_0019962 interferon-delta binding obo:GO_0019962 interferon-epsilon binding obo:GO_0019962 interferon-kappa binding obo:GO_0019962 interferon-omega binding obo:GO_0019962 interferon-tau binding obo:GO_0019962 interferon-zeta binding obo:GO_0019962 molecular_function obo:GO_0019962 GO:0019962 obo:GO_0019962 type I interferon binding obo:GO_0019964 Interacting selectively and non-covalently with interferon-gamma. Interferon gamma is the only member of the type II interferon found so far. obo:GO_0019964 obo:go.owl obo:GO_0019964 type II interferon binding obo:GO_0019964 IFN-gamma binding obo:GO_0019964 IFNG binding obo:GO_0019964 molecular_function obo:GO_0019964 GO:0019964 obo:GO_0019964 interferon-gamma binding obo:GO_0019966 Interacting selectively and non-covalently with interleukin-1. obo:GO_0019966 obo:go.owl obo:GO_0019966 IL-1 binding obo:GO_0019966 molecular_function obo:GO_0019966 GO:0019966 obo:GO_0019966 interleukin-1 binding obo:GO_0019969 Interacting selectively and non-covalently with interleukin-10. obo:GO_0019969 obo:go.owl obo:GO_0019969 IL-10 binding obo:GO_0019969 molecular_function obo:GO_0019969 GO:0019969 obo:GO_0019969 interleukin-10 binding obo:GO_0019970 Interacting selectively and non-covalently with interleukin-11. obo:GO_0019970 obo:go.owl obo:GO_0019970 IL-11 binding obo:GO_0019970 molecular_function obo:GO_0019970 GO:0019970 obo:GO_0019970 interleukin-11 binding obo:GO_0019972 Interacting selectively and non-covalently with interleukin-12. obo:GO_0019972 obo:go.owl obo:GO_0019972 IL-12 binding obo:GO_0019972 molecular_function obo:GO_0019972 GO:0019972 obo:GO_0019972 interleukin-12 binding obo:GO_0019973 Interacting selectively and non-covalently with interleukin-13. obo:GO_0019973 obo:go.owl obo:GO_0019973 IL-13 binding obo:GO_0019973 molecular_function obo:GO_0019973 GO:0019973 obo:GO_0019973 interleukin-13 binding obo:GO_0019974 Interacting selectively and non-covalently with interleukin-14. obo:GO_0019974 obo:go.owl obo:GO_0019974 IL-14 binding obo:GO_0019974 molecular_function obo:GO_0019974 GO:0019974 obo:GO_0019974 interleukin-14 binding obo:GO_0019975 Interacting selectively and non-covalently with any member of the interleukin-17 family of cytokines. obo:GO_0019975 obo:go.owl obo:GO_0019975 IL-17 binding obo:GO_0019975 molecular_function obo:GO_0019975 GO:0019975 obo:GO_0019975 interleukin-17 binding obo:GO_0019976 Interacting selectively and non-covalently with interleukin-2. obo:GO_0019976 obo:go.owl obo:GO_0019976 IL-2 binding obo:GO_0019976 molecular_function obo:GO_0019976 GO:0019976 obo:GO_0019976 interleukin-2 binding obo:GO_0019977 Interacting selectively and non-covalently with interleukin-21. obo:GO_0019977 obo:go.owl obo:GO_0019977 IL-21 binding obo:GO_0019977 molecular_function obo:GO_0019977 GO:0019977 obo:GO_0019977 interleukin-21 binding obo:GO_0019978 Interacting selectively and non-covalently with interleukin-3. obo:GO_0019978 obo:go.owl obo:GO_0019978 IL-3 binding obo:GO_0019978 molecular_function obo:GO_0019978 GO:0019978 obo:GO_0019978 interleukin-3 binding obo:GO_0019979 Interacting selectively and non-covalently with interleukin-4. obo:GO_0019979 obo:go.owl obo:GO_0019979 IL-4 binding obo:GO_0019979 molecular_function obo:GO_0019979 GO:0019979 obo:GO_0019979 interleukin-4 binding obo:GO_0019980 Interacting selectively and non-covalently with interleukin-5. obo:GO_0019980 obo:go.owl obo:GO_0019980 IL-5 binding obo:GO_0019980 molecular_function obo:GO_0019980 GO:0019980 obo:GO_0019980 interleukin-5 binding obo:GO_0019981 Interacting selectively and non-covalently with interleukin-6. obo:GO_0019981 obo:go.owl obo:GO_0019981 IL-6 binding obo:GO_0019981 molecular_function obo:GO_0019981 GO:0019981 obo:GO_0019981 interleukin-6 binding obo:GO_0019982 Interacting selectively and non-covalently with interleukin-7. obo:GO_0019982 obo:go.owl obo:GO_0019982 IL-7 binding obo:GO_0019982 molecular_function obo:GO_0019982 GO:0019982 obo:GO_0019982 interleukin-7 binding obo:GO_0019983 Interacting selectively and non-covalently with interleukin-9. obo:GO_0019983 obo:go.owl obo:GO_0019983 IL-9 binding obo:GO_0019983 molecular_function obo:GO_0019983 GO:0019983 obo:GO_0019983 interleukin-9 binding obo:GO_0019985 The replication of damaged DNA by synthesis across a lesion in the template strand; a specialized DNA polymerase or replication complex inserts a defined nucleotide across from the lesion which allows DNA synthesis to continue beyond the lesion. This process can be mutagenic depending on the damaged nucleotide and the inserted nucleotide. obo:GO_0019985 obo:go.owl obo:GO_0019985 bypass DNA synthesis obo:GO_0019985 biological_process obo:GO_0019985 GO:0019985 obo:GO_0019985 translesion synthesis obo:GO_0019992 Interacting selectively and non-covalently with diacylglycerol, a diester of glycerol and two fatty acids. obo:GO_0019992 obo:go.owl obo:GO_0019992 molecular_function obo:GO_0019992 GO:0019992 obo:GO_0019992 diacylglycerol binding obo:GO_0020013 Any process in which a symbiont organism modulates the frequency, rate or extent of erythrocyte aggregation in its host organism, e.g. the binding of parasite-infected erythrocytes to uninfected erythrocytes. obo:GO_0020013 obo:go.owl obo:GO_0020013 Wikipedia:Rosetting obo:GO_0020013 rosetting obo:GO_0020013 biological_process obo:GO_0020013 GO:0020013 obo:GO_0020013 Please note that this term does not refer to the in vitro assay called erythrocyte rosetting. obo:GO_0020013 modulation by symbiont of host erythrocyte aggregation obo:GO_0020028 The directed movement into a tissue or a cell or organelle of externally available hemoglobin by receptor-mediated endocytosis. obo:GO_0020028 obo:go.owl obo:GO_0020028 haemoglobin uptake obo:GO_0020028 hemoglobin uptake obo:GO_0020028 biological_process obo:GO_0020028 GO:0020028 obo:GO_0020028 endocytic hemoglobin import obo:GO_0020037 Interacting selectively and non-covalently with heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring. obo:GO_0020037 obo:go.owl obo:GO_0020037 MIPS_funcat:16.21.01 obo:GO_0020037 haem binding obo:GO_0020037 molecular_function obo:GO_0020037 GO:0020037 obo:GO_0020037 heme binding obo:GO_0021804 The process that results in the loss of attachments of a cell in the ventricular zone. obo:GO_0021804 obo:go.owl obo:GO_0021804 down regulation of cell adhesion in ventricular zone obo:GO_0021804 down-regulation of cell adhesion in ventricular zone obo:GO_0021804 downregulation of cell adhesion in ventricular zone obo:GO_0021804 inhibition of cell adhesion in ventricular zone obo:GO_0021804 biological_process obo:GO_0021804 GO:0021804 obo:GO_0021804 This term was added by GO_REF:0000021. obo:GO_0021804 negative regulation of cell adhesion in ventricular zone obo:GO_0021821 The process that results in the release of migrating cells from their interaction with radial glial cells as a component of the process of cerebral cortex glial-mediated radial cell migration. obo:GO_0021821 obo:go.owl obo:GO_0021821 down regulation of cell-glial cell adhesion involved in cerebral cortex lamination obo:GO_0021821 down-regulation of cell-glial cell adhesion involved in cerebral cortex lamination obo:GO_0021821 downregulation of cell-glial cell adhesion involved in cerebral cortex lamination obo:GO_0021821 inhibition of cell-glial cell adhesion involved in cerebral cortex lamination obo:GO_0021821 biological_process obo:GO_0021821 GO:0021821 obo:GO_0021821 This term was added by GO_REF:0000021. obo:GO_0021821 negative regulation of cell-glial cell adhesion involved in cerebral cortex lamination obo:GO_0021921 The process that modulates the frequency, rate or extent of cell proliferation in the dorsal spinal cord. obo:GO_0021921 obo:go.owl obo:GO_0021921 biological_process obo:GO_0021921 GO:0021921 obo:GO_0021921 This term was added by GO_REF:0000021. obo:GO_0021921 regulation of cell proliferation in dorsal spinal cord obo:GO_0022407 Any process that modulates the frequency, rate or extent of attachment of a cell to another cell. obo:GO_0022407 obo:go.owl obo:GO_0022407 biological_process obo:GO_0022407 GO:0022407 obo:GO_0022407 regulation of cell-cell adhesion obo:GO_0022408 Any process that stops, prevents or reduces the rate or extent of cell adhesion to another cell. obo:GO_0022408 obo:go.owl obo:GO_0022408 down regulation of cell-cell adhesion obo:GO_0022408 down-regulation of cell-cell adhesion obo:GO_0022408 downregulation of cell-cell adhesion obo:GO_0022408 inhibition of cell-cell adhesion obo:GO_0022408 biological_process obo:GO_0022408 GO:0022408 obo:GO_0022408 negative regulation of cell-cell adhesion obo:GO_0022409 Any process that activates or increases the rate or extent of cell adhesion to another cell. obo:GO_0022409 obo:go.owl obo:GO_0022409 up regulation of cell-cell adhesion obo:GO_0022409 up-regulation of cell-cell adhesion obo:GO_0022409 upregulation of cell-cell adhesion obo:GO_0022409 activation of cell-cell adhesion obo:GO_0022409 stimulation of cell-cell adhesion obo:GO_0022409 biological_process obo:GO_0022409 GO:0022409 obo:GO_0022409 positive regulation of cell-cell adhesion obo:GO_0022898 Any process that modulates the frequency, rate or extent of transmembrane transporter activity. obo:GO_0022898 obo:go.owl obo:GO_0022898 biological_process obo:GO_0022898 GO:0022898 obo:GO_0022898 regulation of transmembrane transporter activity obo:GO_0023014 A process in which the transfer of one or more phosphate groups to a substrate transmits a signal to the phosphorylated substrate. obo:GO_0023014 obo:go.owl obo:GO_0023014 2010-02-16T09:30:50Z obo:GO_0023014 biological_process obo:GO_0023014 signal transduction via phosphorylation event obo:GO_0023014 signal transmission via phosphorylation event obo:GO_0023014 GO:0023014 obo:GO_0023014 signal transduction by protein phosphorylation obo:GO_0023015 A process in which the transfer of one or more phosphate groups by a kinase to a residue in the same kinase molecule transmits a signal. For example, ligand-binding can induce autophosphorylation of the activated receptor, creating binding sites for intracellular signaling molecules. obo:GO_0023015 obo:go.owl obo:GO_0023015 2010-02-16T09:30:50Z obo:GO_0023015 biological_process obo:GO_0023015 signal transduction via a cis-phosphorylation event obo:GO_0023015 signal transmission via a cis-phosphorylation event obo:GO_0023015 signal transmission via auto-phosphorylation obo:GO_0023015 GO:0023015 obo:GO_0023015 signal transduction by cis-phosphorylation obo:GO_0023016 A process in which the transfer of one or more phosphate groups by a kinase to a residue in a different protein molecule transmits a signal. obo:GO_0023016 obo:go.owl obo:GO_0023016 2010-02-16T09:30:50Z obo:GO_0023016 biological_process obo:GO_0023016 signal transduction via a trans-phosphorylation event obo:GO_0023016 signal transmission via a trans-phosphorylation event obo:GO_0023016 GO:0023016 obo:GO_0023016 signal transduction by trans-phosphorylation obo:GO_0023019 Any process that modulates the frequency, rate or extent of gene expression as a consequence of a process in which a signal is released and/or conveyed from one location to another. obo:GO_0023019 obo:go.owl obo:GO_0023019 2010-02-16T09:30:50Z obo:GO_0023019 biological_process obo:GO_0023019 regulation of gene expression as a consequence of signal transmission obo:GO_0023019 GO:0023019 obo:GO_0023019 signal transduction involved in regulation of gene expression obo:GO_0023023 Interacting selectively and non-covalently with the major histocompatibility complex. obo:GO_0023023 obo:go.owl obo:GO_0023023 2010-02-16T09:30:50Z obo:GO_0023023 molecular_function obo:GO_0023023 GO:0023023 obo:GO_0023023 MHC protein complex binding obo:GO_0023024 Interacting selectively and non-covalently with the class I major histocompatibility complex. obo:GO_0023024 obo:go.owl obo:GO_0023024 2010-02-16T09:30:50Z obo:GO_0023024 molecular_function obo:GO_0023024 GO:0023024 obo:GO_0023024 MHC class I protein complex binding obo:GO_0023025 Interacting selectively and non-covalently with the class Ib major histocompatibility complex. obo:GO_0023025 obo:go.owl obo:GO_0023025 2010-02-16T09:30:50Z obo:GO_0023025 molecular_function obo:GO_0023025 GO:0023025 obo:GO_0023025 MHC class Ib protein complex binding obo:GO_0023026 Interacting selectively and non-covalently with the class II major histocompatibility complex. obo:GO_0023026 obo:go.owl obo:GO_0023026 2010-02-16T09:30:50Z obo:GO_0023026 molecular_function obo:GO_0023026 GO:0023026 obo:GO_0023026 MHC class II protein complex binding obo:GO_0023027 Interacting selectively and non-covalently with major histocompatibility complex class I molecules via the antigen binding groove. obo:GO_0023027 obo:go.owl obo:GO_0023027 2010-02-16T09:30:50Z obo:GO_0023027 molecular_function obo:GO_0023027 GO:0023027 obo:GO_0023027 MHC class I protein binding, via antigen binding groove obo:GO_0023028 Interacting selectively and non-covalently with major histocompatibility complex class I molecules via the lateral surface. obo:GO_0023028 obo:go.owl obo:GO_0023028 2010-02-16T09:30:50Z obo:GO_0023028 molecular_function obo:GO_0023028 GO:0023028 obo:GO_0023028 MHC class I protein binding, via lateral surface obo:GO_0023029 Interacting selectively and non-covalently with major histocompatibility complex class Ib molecules. obo:GO_0023029 obo:go.owl obo:GO_0023029 2010-02-16T09:30:50Z obo:GO_0023029 molecular_function obo:GO_0023029 GO:0023029 obo:GO_0023029 MHC class Ib protein binding obo:GO_0023030 Interacting selectively and non-covalently with major histocompatibility complex class Ib molecules via the antigen binding groove. obo:GO_0023030 obo:go.owl obo:GO_0023030 2010-02-16T09:30:50Z obo:GO_0023030 molecular_function obo:GO_0023030 GO:0023030 obo:GO_0023030 MHC class Ib protein binding, via antigen binding groove obo:GO_0023031 Interacting selectively and non-covalently with major histocompatibility complex class Ib molecules via the lateral surface. obo:GO_0023031 obo:go.owl obo:GO_0023031 2010-02-16T09:30:50Z obo:GO_0023031 molecular_function obo:GO_0023031 GO:0023031 obo:GO_0023031 MHC class Ib protein binding, via lateral surface obo:GO_0023051 Any process that modulates the frequency, rate or extent of a signaling process. obo:GO_0023051 obo:go.owl obo:GO_0023051 2010-02-16T09:30:50Z obo:GO_0023051 biological_process obo:GO_0023051 regulation of signaling process obo:GO_0023051 regulation of signalling process obo:GO_0023051 GO:0023051 obo:GO_0023051 regulation of signaling obo:GO_0023056 Any process that activates, maintains or increases the frequency, rate or extent of a signaling process. obo:GO_0023056 obo:go.owl obo:GO_0023056 2010-02-16T09:30:50Z obo:GO_0023056 positive regulation of signalling process obo:GO_0023056 biological_process obo:GO_0023056 positive regulation of signaling process obo:GO_0023056 GO:0023056 obo:GO_0023056 positive regulation of signaling obo:GO_0023057 Any process that stops, prevents, or reduces the frequency, rate or extent of a signaling process. obo:GO_0023057 obo:go.owl obo:GO_0023057 2010-02-16T09:30:50Z obo:GO_0023057 biological_process obo:GO_0023057 negative regulation of signaling process obo:GO_0023057 negative regulation of signalling process obo:GO_0023057 GO:0023057 obo:GO_0023057 negative regulation of signaling obo:GO_0030001 The directed movement of metal ions, any metal ion with an electric charge, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0030001 obo:go.owl obo:GO_0030001 heavy metal ion transport obo:GO_0030001 biological_process obo:GO_0030001 GO:0030001 obo:GO_0030001 metal ion transport obo:GO_0030116 A growth factor that binds selectively and non-covalently to glial cell-derived neurotrophic factor receptors. obo:GO_0030116 obo:go.owl obo:GO_0030116 glial cell line-derived neurotrophic factor receptor ligand obo:GO_0030116 molecular_function obo:GO_0030116 glial cell line-derived neurotrophic factor receptor binding obo:GO_0030116 GO:0030116 obo:GO_0030116 glial cell-derived neurotrophic factor receptor binding obo:GO_0030145 Interacting selectively and non-covalently with manganese (Mn) ions. obo:GO_0030145 obo:go.owl obo:GO_0030145 manganese binding obo:GO_0030145 molecular_function obo:GO_0030145 GO:0030145 obo:GO_0030145 manganese ion binding obo:GO_0030151 Interacting selectively and non-covalently with molybdenum (Mo) ions. obo:GO_0030151 obo:go.owl obo:GO_0030151 molybdenum binding obo:GO_0030151 molecular_function obo:GO_0030151 GO:0030151 obo:GO_0030151 molybdenum ion binding obo:GO_0030155 Any process that modulates the frequency, rate or extent of attachment of a cell to another cell or to the extracellular matrix. obo:GO_0030155 obo:go.owl obo:GO_0030155 biological_process obo:GO_0030155 cell adhesion receptor regulator activity obo:GO_0030155 GO:0030155 obo:GO_0030155 regulation of cell adhesion obo:GO_0030156 Interacting selectively and non-covalently with the peripheral benzodiazepine receptor (PBR). obo:GO_0030156 obo:go.owl obo:GO_0030156 benzodiazepine receptor ligand obo:GO_0030156 molecular_function obo:GO_0030156 diazepam binding inhibitor activity obo:GO_0030156 GO:0030156 obo:GO_0030156 benzodiazepine receptor binding obo:GO_0030163 The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds. obo:GO_0030163 obo:go.owl obo:GO_0030163 GO:0044254 obo:GO_0030163 MIPS_funcat:14.13 obo:GO_0030163 Wikipedia:Protein_catabolism obo:GO_0030163 protein breakdown obo:GO_0030163 protein catabolism obo:GO_0030163 protein degradation obo:GO_0030163 multicellular organismal protein catabolic process obo:GO_0030163 biological_process obo:GO_0030163 pheromone catabolic process obo:GO_0030163 pheromone catabolism obo:GO_0030163 GO:0030163 obo:GO_0030163 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_aspergillus obo:GO_0030163 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_candida obo:GO_0030163 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pombe obo:GO_0030163 This term refers to the breakdown of mature proteins. For cleavage events involved in generating a mature protein from a precursor, consider instead the term 'protein maturation ; GO:0051604' and its children. obo:GO_0030163 protein catabolic process obo:GO_0030165 Interacting selectively and non-covalently with a PDZ domain of a protein, a domain found in diverse signaling proteins. obo:GO_0030165 obo:go.owl obo:GO_0030165 DHR-domain binding obo:GO_0030165 GLGF-domain binding obo:GO_0030165 molecular_function obo:GO_0030165 GO:0030165 obo:GO_0030165 PDZ domain binding obo:GO_0030169 Interacting selectively and non-covalently with a low-density lipoprotein particle, a lipoprotein particle that is rich in cholesterol esters and low in triglycerides, is typically composed of APOB100 and APOE, and has a density of 1.02-1.06 g/ml and a diameter of between 20-25 nm. obo:GO_0030169 obo:go.owl obo:GO_0030169 LDL binding obo:GO_0030169 molecular_function obo:GO_0030169 GO:0030169 obo:GO_0030169 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0030169 low-density lipoprotein particle binding obo:GO_0030170 Interacting selectively and non-covalently with pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6. obo:GO_0030170 obo:go.owl obo:GO_0030170 MIPS_funcat:16.21.17 obo:GO_0030170 molecular_function obo:GO_0030170 GO:0030170 obo:GO_0030170 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0030170 pyridoxal phosphate binding obo:GO_0030172 Interacting selectively and non-covalently with troponin C, the calcium-binding subunit of the troponin complex. obo:GO_0030172 obo:go.owl obo:GO_0030172 molecular_function obo:GO_0030172 GO:0030172 obo:GO_0030172 troponin C binding obo:GO_0030215 Interacting selectively and non-covalently with semaphorin receptors. obo:GO_0030215 obo:go.owl obo:GO_0030215 plexin binding obo:GO_0030215 plexin ligand obo:GO_0030215 semaphorin receptor ligand obo:GO_0030215 molecular_function obo:GO_0030215 GO:0030215 obo:GO_0030215 semaphorin receptor binding obo:GO_0030234 Binds to and modulates the activity of an enzyme. obo:GO_0030234 obo:go.owl obo:GO_0030234 GO:0010576 obo:GO_0030234 MIPS_funcat:18.02.01 obo:GO_0030234 catalytic regulator activity obo:GO_0030234 enzyme modulator obo:GO_0030234 metalloenzyme regulator activity obo:GO_0030234 molecular_function obo:GO_0030234 GO:0030234 obo:GO_0030234 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_agr obo:GO_0030234 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_aspergillus obo:GO_0030234 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_candida obo:GO_0030234 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0030234 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0030234 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_mouse obo:GO_0030234 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0030234 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0030234 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0030234 GO:0030234 is reserved for cases when the regulator directly interacts with the enzyme. When regulation of enzyme activity is achieved without enzyme binding, or when the mechanism of regulation is unknown, instead annotate to 'regulation of catalytic activity ; GO:0050790'. obo:GO_0030234 enzyme regulator activity obo:GO_0030246 Interacting selectively and non-covalently with any carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates. obo:GO_0030246 obo:go.owl obo:GO_0030246 GO:0005529 obo:GO_0030246 sugar binding obo:GO_0030246 molecular_function obo:GO_0030246 selectin obo:GO_0030246 GO:0030246 obo:GO_0030246 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_agr obo:GO_0030246 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0030246 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_flybase_ribbon obo:GO_0030246 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0030246 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0030246 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0030246 carbohydrate binding obo:GO_0030247 Interacting selectively and non-covalently with any polysaccharide, a polymer of many (typically more than 10) monosaccharide residues linked glycosidically. obo:GO_0030247 obo:go.owl obo:GO_0030247 MIPS_funcat:16.05 obo:GO_0030247 molecular_function obo:GO_0030247 GO:0030247 obo:GO_0030247 polysaccharide binding obo:GO_0030248 Interacting selectively and non-covalently with cellulose. obo:GO_0030248 obo:go.owl obo:GO_0030248 molecular_function obo:GO_0030248 GO:0030248 obo:GO_0030248 cellulose binding obo:GO_0030274 Interacting selectively and non-covalently with a LIM domain (for Lin-11 Isl-1 Mec-3) of a protein, a domain with seven conserved cysteine residues and a histidine, that binds two zinc ions and acts as an interface for protein-protein interactions. obo:GO_0030274 obo:go.owl obo:GO_0030274 molecular_function obo:GO_0030274 GO:0030274 obo:GO_0030274 LIM domain binding obo:GO_0030275 Interacting selectively and non-covalently with a LRR domain (leucine rich repeats) of a protein. obo:GO_0030275 obo:go.owl obo:GO_0030275 molecular_function obo:GO_0030275 GO:0030275 obo:GO_0030275 LRR domain binding obo:GO_0030276 Interacting selectively and non-covalently with a clathrin heavy or light chain, the main components of the coat of coated vesicles and coated pits, and which also occurs in synaptic vesicles. obo:GO_0030276 obo:go.owl obo:GO_0030276 molecular_function obo:GO_0030276 GO:0030276 obo:GO_0030276 clathrin binding obo:GO_0030295 Binds to and increases the activity of a protein kinase, an enzyme which phosphorylates a protein. obo:GO_0030295 obo:go.owl obo:GO_0030295 molecular_function obo:GO_0030295 GO:0030295 obo:GO_0030295 protein kinase activator activity obo:GO_0030306 Interacting selectively and non-covalently with ARF, ADP-ribosylation factor, a small monomeric cytosolic GTPase that, when bound to GTP, binds to the membranes of cells. obo:GO_0030306 obo:go.owl obo:GO_0030306 ARF binding obo:GO_0030306 molecular_function obo:GO_0030306 GO:0030306 obo:GO_0030306 ADP-ribosylation factor binding obo:GO_0030321 The directed movement of chloride ions from one side of an epithelium to the other. obo:GO_0030321 obo:go.owl obo:GO_0030321 biological_process obo:GO_0030321 GO:0030321 obo:GO_0030321 transepithelial chloride transport obo:GO_0030331 Interacting selectively and non-covalently with an estrogen receptor. obo:GO_0030331 obo:go.owl obo:GO_0030331 molecular_function obo:GO_0030331 GO:0030331 obo:GO_0030331 estrogen receptor binding obo:GO_0030332 Interacting selectively and non-covalently with cyclins, proteins whose levels in a cell varies markedly during the cell cycle, rising steadily until mitosis, then falling abruptly to zero. As cyclins reach a threshold level, they are thought to drive cells into G2 phase and thus to mitosis. obo:GO_0030332 obo:go.owl obo:GO_0030332 molecular_function obo:GO_0030332 GO:0030332 obo:GO_0030332 cyclin binding obo:GO_0030346 Interacting selectively and non-covalently with the enzyme protein phosphatase 2B. obo:GO_0030346 obo:go.owl obo:GO_0030346 calcineurin binding obo:GO_0030346 molecular_function obo:GO_0030346 protein phosphatase 3 binding obo:GO_0030346 GO:0030346 obo:GO_0030346 protein phosphatase 2B binding obo:GO_0030348 Interacting selectively and non-covalently with the SNAP receptor syntaxin-3. obo:GO_0030348 obo:go.owl obo:GO_0030348 molecular_function obo:GO_0030348 GO:0030348 obo:GO_0030348 syntaxin-3 binding obo:GO_0030350 Interacting selectively and non-covalently with the iron-responsive element, a regulatory sequence found in the 5'- and 3'-untranslated regions of mRNAs encoding many iron-binding proteins. obo:GO_0030350 obo:go.owl obo:GO_0030350 IRE binding obo:GO_0030350 molecular_function obo:GO_0030350 GO:0030350 obo:GO_0030350 iron-responsive element binding obo:GO_0030353 Interacts with the fibroblast growth factor receptor to reduce the action of another ligand, the agonist. obo:GO_0030353 obo:go.owl obo:GO_0030353 FGF receptor antagonist activity obo:GO_0030353 FGFR antagonist activity obo:GO_0030353 molecular_function obo:GO_0030353 GO:0030353 obo:GO_0030353 fibroblast growth factor receptor antagonist activity obo:GO_0030354 The action characteristic of melanin-concentrating hormone, a cyclic peptide hormone that, upon receptor binding, induces melanin aggregation in melanocytes, and is also involved in regulating food intake and energy balance in mammals. obo:GO_0030354 obo:go.owl obo:GO_0030354 molecular_function obo:GO_0030354 GO:0030354 obo:GO_0030354 melanin-concentrating hormone activity obo:GO_0030367 Interacting selectively and non-covalently with the interleukin-17 receptor. obo:GO_0030367 obo:go.owl obo:GO_0030367 IL-17 obo:GO_0030367 interleukin-17 receptor ligand obo:GO_0030367 molecular_function obo:GO_0030367 GO:0030367 obo:GO_0030367 interleukin-17 receptor binding obo:GO_0030370 Interacting selectively and non-covalently with receptors for intercellular adhesion molecule-3 (ICAM-3), such as DC-SIGN and LFA-1. obo:GO_0030370 obo:go.owl obo:GO_0030370 ICAM-3 receptor binding obo:GO_0030370 ICAM-3 receptor ligand obo:GO_0030370 intercellular adhesion molecule-3 receptor ligand obo:GO_0030370 molecular_function obo:GO_0030370 GO:0030370 obo:GO_0030370 intercellular adhesion molecule-3 receptor binding obo:GO_0030372 Interacting selectively and non-covalently with the high molecular weight B cell growth factor receptor. obo:GO_0030372 obo:go.owl obo:GO_0030372 high molecular weight B lymphocyte growth factor receptor binding obo:GO_0030372 high molecular weight B-cell growth factor receptor binding obo:GO_0030372 high molecular weight B-lymphocyte growth factor receptor binding obo:GO_0030372 high molecular weight B cell growth factor receptor ligand obo:GO_0030372 molecular_function obo:GO_0030372 GO:0030372 obo:GO_0030372 high molecular weight B cell growth factor receptor binding obo:GO_0030380 Interacting selectively and non-covalently with the interleukin-17E receptor. obo:GO_0030380 obo:go.owl obo:GO_0030380 IL-17E obo:GO_0030380 interleukin-17E receptor ligand obo:GO_0030380 molecular_function obo:GO_0030380 GO:0030380 obo:GO_0030380 interleukin-17E receptor binding obo:GO_0030395 Interacting selectively and non-covalently with lactose, a disaccharide of glucose and galactose, the carbohydrate of milk. obo:GO_0030395 obo:go.owl obo:GO_0030395 molecular_function obo:GO_0030395 GO:0030395 obo:GO_0030395 lactose binding obo:GO_0030413 A small peptide excreted by a naturally transformable bacterium (e.g. Bacillus subtilis) that transmits a signal required for the establishment of competence. obo:GO_0030413 obo:go.owl obo:GO_0030413 molecular_function obo:GO_0030413 GO:0030413 obo:GO_0030413 competence pheromone activity obo:GO_0030492 Interacting selectively and non-covalently with hemoglobin, an oxygen carrying, conjugated protein containing four heme groups and globin. obo:GO_0030492 obo:go.owl obo:GO_0030492 globin binding obo:GO_0030492 haemoglobin binding obo:GO_0030492 molecular_function obo:GO_0030492 GO:0030492 obo:GO_0030492 hemoglobin binding obo:GO_0030506 Interacting selectively and non-covalently with ankyrin, a 200 kDa cytoskeletal protein that attaches other cytoskeletal proteins to integral membrane proteins. obo:GO_0030506 obo:go.owl obo:GO_0030506 molecular_function obo:GO_0030506 GO:0030506 obo:GO_0030506 ankyrin binding obo:GO_0030507 Interacting selectively and non-covalently with spectrin, a protein that is the major constituent of the erythrocyte cytoskeletal network. It associates with band 4.1 (see band protein) and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. It is composed of nonhomologous chains, alpha and beta, which aggregate side-to-side in an antiparallel fashion to form dimers, tetramers, and higher polymers. obo:GO_0030507 obo:go.owl obo:GO_0030507 molecular_function obo:GO_0030507 GO:0030507 obo:GO_0030507 spectrin binding obo:GO_0030515 Interacting selectively and non-covalently with small nucleolar RNA. obo:GO_0030515 obo:go.owl obo:GO_0030515 molecular_function obo:GO_0030515 GO:0030515 obo:GO_0030515 snoRNA binding obo:GO_0030519 Interacting selectively and non-covalently with any part of a small nucleolar ribonucleoprotein particle. obo:GO_0030519 obo:go.owl obo:GO_0030519 molecular_function obo:GO_0030519 GO:0030519 obo:GO_0030519 snoRNP binding obo:GO_0030523 Catalysis of the reaction: acyl-CoA + dihydrolipoamide = CoA + S-acyldihydrolipoamide. obo:GO_0030523 obo:go.owl obo:GO_0030523 EC:2.3.1.12 obo:GO_0030523 molecular_function obo:GO_0030523 GO:0030523 obo:GO_0030523 dihydrolipoamide S-acyltransferase activity obo:GO_0030544 Interacting selectively and non-covalently with Hsp70 proteins, any of a group of heat shock proteins around 70kDa in size. obo:GO_0030544 obo:go.owl obo:GO_0030544 molecular_function obo:GO_0030544 GO:0030544 obo:GO_0030544 Hsp70 protein binding obo:GO_0030545 The function of interacting (directly or indirectly) with receptors such that the proportion of receptors in the active form is changed. obo:GO_0030545 obo:go.owl obo:GO_0030545 MIPS_funcat:18.02.07 obo:GO_0030545 molecular_function obo:GO_0030545 GO:0030545 obo:GO_0030545 receptor regulator activity obo:GO_0030547 The function of interacting (directly or indirectly) with receptors such that the proportion of receptors in the active form is decreased. obo:GO_0030547 obo:go.owl obo:GO_0030547 molecular_function obo:GO_0030547 GO:0030547 obo:GO_0030547 receptor inhibitor activity obo:GO_0030551 Interacting selectively and non-covalently with a cyclic nucleotide, a nucleotide in which the phosphate group is in diester linkage to two positions on the sugar residue. obo:GO_0030551 obo:go.owl obo:GO_0030551 MIPS_funcat:16.19.01 obo:GO_0030551 molecular_function obo:GO_0030551 GO:0030551 obo:GO_0030551 cyclic nucleotide binding obo:GO_0030552 Interacting selectively and non-covalently with cAMP, the nucleotide cyclic AMP (adenosine 3',5'-cyclophosphate). obo:GO_0030552 obo:go.owl obo:GO_0030552 3',5' cAMP binding obo:GO_0030552 3',5'-cAMP binding obo:GO_0030552 adenosine 3',5'-cyclophosphate binding obo:GO_0030552 cyclic AMP binding obo:GO_0030552 molecular_function obo:GO_0030552 GO:0030552 obo:GO_0030552 cAMP binding obo:GO_0030553 Interacting selectively and non-covalently with cGMP, the nucleotide cyclic GMP (guanosine 3',5'-cyclophosphate). obo:GO_0030553 obo:go.owl obo:GO_0030553 3',5' cGMP binding obo:GO_0030553 3',5'-cGMP binding obo:GO_0030553 cyclic GMP binding obo:GO_0030553 molecular_function obo:GO_0030553 GO:0030553 obo:GO_0030553 cGMP binding obo:GO_0030554 Interacting selectively and non-covalently with adenyl nucleotides, any compound consisting of adenosine esterified with (ortho)phosphate. obo:GO_0030554 obo:go.owl obo:GO_0030554 molecular_function obo:GO_0030554 GO:0030554 obo:GO_0030554 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0030554 adenyl nucleotide binding obo:GO_0030555 Specifies the site of a posttranscriptional modification in an RNA molecule by base pairing with a short sequence around the target residue. obo:GO_0030555 obo:go.owl obo:GO_0030555 molecular_function obo:GO_0030555 GO:0030555 obo:GO_0030555 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0030555 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0030555 Note that this term describes the activity of a nucleic acid, usually RNA, gene product that interacts with other RNA molecules via base pairing; it should not be used to annotate proteins. obo:GO_0030555 RNA modification guide activity obo:GO_0030556 Specifies the site of a posttranscriptional modification in an rRNA molecule by base pairing with a short sequence around the target residue. obo:GO_0030556 obo:go.owl obo:GO_0030556 molecular_function obo:GO_0030556 GO:0030556 obo:GO_0030556 Note that this term describes the activity of a nucleic acid, usually RNA, gene product that interacts with other RNA molecules via base pairing; it should not be used to annotate proteins. obo:GO_0030556 rRNA modification guide activity obo:GO_0030557 Specifies the site of a posttranscriptional modification in a tRNA molecule by base pairing with a short sequence around the target residue. obo:GO_0030557 obo:go.owl obo:GO_0030557 molecular_function obo:GO_0030557 GO:0030557 obo:GO_0030557 Note that this term describes the activity of a nucleic acid, usually RNA, gene product that interacts with other RNA molecules via base pairing; it should not be used to annotate proteins. obo:GO_0030557 tRNA modification guide activity obo:GO_0030558 Specifies the site of pseudouridylation in an RNA molecule by base pairing with a short sequence around the target residue. obo:GO_0030558 obo:go.owl obo:GO_0030558 molecular_function obo:GO_0030558 GO:0030558 obo:GO_0030558 Note that this term describes the activity of a nucleic acid, usually RNA, gene product that interacts with other RNA molecules via base pairing; it should not be used to annotate proteins. obo:GO_0030558 RNA pseudouridylation guide activity obo:GO_0030559 Specifies the site of pseudouridylation in an rRNA molecule by base pairing with a short sequence around the target residue. obo:GO_0030559 obo:go.owl obo:GO_0030559 molecular_function obo:GO_0030559 GO:0030559 obo:GO_0030559 Note that this term describes the activity of a nucleic acid, usually RNA, gene product that interacts with other RNA molecules via base pairing; it should not be used to annotate proteins. obo:GO_0030559 rRNA pseudouridylation guide activity obo:GO_0030560 Specifies the site of pseudouridylation in a tRNA molecule by base pairing with a short sequence around the target residue. obo:GO_0030560 obo:go.owl obo:GO_0030560 molecular_function obo:GO_0030560 GO:0030560 obo:GO_0030560 Note that this term describes the activity of a nucleic acid, usually RNA, gene product that interacts with other RNA molecules via base pairing; it should not be used to annotate proteins. obo:GO_0030560 tRNA pseudouridylation guide activity obo:GO_0030561 Specifies the site of 2'-O-ribose methylation in an RNA molecule by base pairing with a short sequence around the target residue. obo:GO_0030561 obo:go.owl obo:GO_0030561 molecular_function obo:GO_0030561 GO:0030561 obo:GO_0030561 Note that this term describes the activity of a nucleic acid, usually RNA, gene product that interacts with other RNA molecules via base pairing; it should not be used to annotate proteins. obo:GO_0030561 RNA 2'-O-ribose methylation guide activity obo:GO_0030562 Specifies the site of 2'-O-ribose methylation in an rRNA molecule by base pairing with a short sequence around the target residue. obo:GO_0030562 obo:go.owl obo:GO_0030562 molecular_function obo:GO_0030562 GO:0030562 obo:GO_0030562 Note that this term describes the activity of a nucleic acid, usually RNA, gene product that interacts with other RNA molecules via base pairing; it should not be used to annotate proteins. obo:GO_0030562 rRNA 2'-O-ribose methylation guide activity obo:GO_0030563 Activity that provides specificity to a methylase by using base complementarity to guide site-specific 2'-O-ribose methylations to a small nuclear RNA molecule. obo:GO_0030563 obo:go.owl obo:GO_0030563 molecular_function obo:GO_0030563 GO:0030563 obo:GO_0030563 Note that this term describes the activity of a nucleic acid, usually RNA, gene product that interacts with other RNA molecules via base pairing; it should not be used to annotate proteins. Note that this term may be useful for annotating snoRNAs. obo:GO_0030563 snRNA 2'-O-ribose methylation guide activity obo:GO_0030564 Specifies the site of 2'-O-ribose methylation in a tRNA molecule by base pairing with a short sequence around the target residue. obo:GO_0030564 obo:go.owl obo:GO_0030564 molecular_function obo:GO_0030564 GO:0030564 obo:GO_0030564 Note that this term describes the activity of a nucleic acid, usually RNA, gene product that interacts with other RNA molecules via base pairing; it should not be used to annotate proteins. obo:GO_0030564 tRNA 2'-O-ribose methylation guide activity obo:GO_0030565 Activity that provides specificity to a pseudouridine synthetase by using base complementarity to guide site-specific pseudouridylations to a small nuclear RNA molecule. obo:GO_0030565 obo:go.owl obo:GO_0030565 molecular_function obo:GO_0030565 GO:0030565 obo:GO_0030565 Note that this term describes the activity of a nucleic acid, usually RNA, gene product that interacts with other RNA molecules via base pairing; it should not be used to annotate proteins. Note that this term may be useful for annotating snoRNAs. obo:GO_0030565 snRNA pseudouridylation guide activity obo:GO_0030566 Specifies the site of a posttranscriptional modification in an snRNA molecule by base pairing with a short sequence around the target residue. obo:GO_0030566 obo:go.owl obo:GO_0030566 molecular_function obo:GO_0030566 GO:0030566 obo:GO_0030566 Note that this term describes the activity of a nucleic acid, usually RNA, gene product that interacts with other RNA molecules via base pairing; it should not be used to annotate proteins. obo:GO_0030566 snRNA modification guide activity obo:GO_0030619 Interacting selectively and non-covalently with the U1 small nuclear RNA (U1 snRNA). obo:GO_0030619 obo:go.owl obo:GO_0030619 molecular_function obo:GO_0030619 GO:0030619 obo:GO_0030619 Note that this term may be useful for annotating other small nuclear RNAs (snRNAs). obo:GO_0030619 U1 snRNA binding obo:GO_0030620 Interacting selectively and non-covalently with the U2 small nuclear RNA (U2 snRNA). obo:GO_0030620 obo:go.owl obo:GO_0030620 molecular_function obo:GO_0030620 GO:0030620 obo:GO_0030620 U2 snRNA binding obo:GO_0030621 Interacting selectively and non-covalently with the U4 small nuclear RNA (U4 snRNA). obo:GO_0030621 obo:go.owl obo:GO_0030621 molecular_function obo:GO_0030621 GO:0030621 obo:GO_0030621 U4 snRNA binding obo:GO_0030622 Interacting selectively and non-covalently with the U4atac small nuclear RNA (U4atac snRNA). obo:GO_0030622 obo:go.owl obo:GO_0030622 molecular_function obo:GO_0030622 GO:0030622 obo:GO_0030622 U4atac snRNA binding obo:GO_0030623 Interacting selectively and non-covalently with the U5 small nuclear RNA (U5 snRNA). obo:GO_0030623 obo:go.owl obo:GO_0030623 molecular_function obo:GO_0030623 GO:0030623 obo:GO_0030623 U5 snRNA binding obo:GO_0030624 Interacting selectively and non-covalently with the U6atac small nuclear RNA (U6atac snRNA). obo:GO_0030624 obo:go.owl obo:GO_0030624 molecular_function obo:GO_0030624 GO:0030624 obo:GO_0030624 U6atac snRNA binding obo:GO_0030625 Interacting selectively and non-covalently with the U11 small nuclear RNA (U11 snRNA). obo:GO_0030625 obo:go.owl obo:GO_0030625 molecular_function obo:GO_0030625 GO:0030625 obo:GO_0030625 U11 snRNA binding obo:GO_0030626 Interacting selectively and non-covalently with the U12 small nuclear RNA (U12 snRNA). obo:GO_0030626 obo:go.owl obo:GO_0030626 molecular_function obo:GO_0030626 GO:0030626 obo:GO_0030626 U12 snRNA binding obo:GO_0030627 Interacting selectively and non-covalently with the pre-mRNA 5' splice site sequence. obo:GO_0030627 obo:go.owl obo:GO_0030627 pre-mRNA 5' splice site binding obo:GO_0030627 molecular_function obo:GO_0030627 GO:0030627 obo:GO_0030627 pre-mRNA 5'-splice site binding obo:GO_0030628 Interacting selectively and non-covalently with the pre-mRNA 3' splice site sequence. obo:GO_0030628 obo:go.owl obo:GO_0030628 pre-mRNA 3' splice site binding obo:GO_0030628 molecular_function obo:GO_0030628 GO:0030628 obo:GO_0030628 pre-mRNA 3'-splice site binding obo:GO_0030629 Interacting selectively and non-covalently with the 3' end of the U6 small nuclear RNA (U6 snRNA). obo:GO_0030629 obo:go.owl obo:GO_0030629 U6 snRNA 3' end binding obo:GO_0030629 molecular_function obo:GO_0030629 GO:0030629 obo:GO_0030629 Note that this term may be useful for annotating small nuclear RNAs (snRNAs). obo:GO_0030629 U6 snRNA 3'-end binding obo:GO_0030676 Stimulates the exchange of guanyl nucleotides associated with a GTPase of the Rac family. Under normal cellular physiological conditions, the concentration of GTP is higher than that of GDP, favoring the replacement of GDP by GTP in association with the GTPase. obo:GO_0030676 obo:go.owl obo:GO_0030676 Reactome:R-HSA-399938 obo:GO_0030676 Reactome:R-HSA-428535 obo:GO_0030676 Reactome:R-HSA-9032798 obo:GO_0030676 Reactome:R-HSA-9033292 obo:GO_0030676 Reactome:R-HSA-9619803 obo:GO_0030676 molecular_function obo:GO_0030676 GO:0030676 obo:GO_0030676 Rac guanyl-nucleotide exchange factor activity obo:GO_0030695 Modulates the rate of GTP hydrolysis by a GTPase. obo:GO_0030695 obo:go.owl obo:GO_0030695 GO:0005083 obo:GO_0030695 molecular_function obo:GO_0030695 small GTPase regulator activity obo:GO_0030695 small GTPase regulatory/interacting protein activity obo:GO_0030695 GO:0030695 obo:GO_0030695 GTPase regulator activity obo:GO_0030709 The delamination process that results in the splitting off of border cells from the anterior epithelium, prior to border cell migration. obo:GO_0030709 obo:go.owl obo:GO_0030709 border cell delamination obo:GO_0030709 biological_process obo:GO_0030709 GO:0030709 obo:GO_0030709 border follicle cell delamination obo:GO_0030742 Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules) when at least one of the interacting partners is in the GTP-bound state. obo:GO_0030742 obo:go.owl obo:GO_0030742 molecular_function obo:GO_0030742 GO:0030742 obo:GO_0030742 This term may be used to annotate both partners in a GTP-dependent binding interaction, both the GTP-bound protein and the protein(s) which interact with it. obo:GO_0030742 GTP-dependent protein binding obo:GO_0030881 Interacting selectively and non-covalently with beta-2-microglobulin. obo:GO_0030881 obo:go.owl obo:GO_0030881 molecular_function obo:GO_0030881 GO:0030881 obo:GO_0030881 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0030881 beta-2-microglobulin binding obo:GO_0030911 Interacting selectively and non-covalently with a tetratricopeptide repeat (TPR) domain of a protein, the consensus sequence of which is defined by a pattern of small and large hydrophobic amino acids and a structure composed of helices. obo:GO_0030911 obo:go.owl obo:GO_0030911 tetratricopeptide repeat domain binding obo:GO_0030911 molecular_function obo:GO_0030911 GO:0030911 obo:GO_0030911 TPR domain binding obo:GO_0030941 Interacting selectively and non-covalently with a chloroplast targeting sequence, a specific peptide sequence that acts as a signal to localize the protein within the chloroplast. obo:GO_0030941 obo:go.owl obo:GO_0030941 molecular_function obo:GO_0030941 GO:0030941 obo:GO_0030941 chloroplast targeting sequence binding obo:GO_0030942 Interacting selectively and non-covalently with an endoplasmic reticulum signal peptide, a specific peptide sequence that acts as a signal to localize the protein within the endoplasmic reticulum. obo:GO_0030942 obo:go.owl obo:GO_0030942 ER signal peptide binding obo:GO_0030942 molecular_function obo:GO_0030942 GO:0030942 obo:GO_0030942 endoplasmic reticulum signal peptide binding obo:GO_0030943 Interacting selectively and non-covalently with a mitochondrion targeting sequence, a specific peptide sequence that acts as a signal to localize the protein within the mitochondrion. obo:GO_0030943 obo:go.owl obo:GO_0030943 mitochondrial targeting sequence binding obo:GO_0030943 molecular_function obo:GO_0030943 GO:0030943 obo:GO_0030943 mitochondrion targeting sequence binding obo:GO_0030944 Interacting selectively and non-covalently with a KDEL sequence, the C terminus tetrapeptide sequence Asp-Asp-Glu-Leu found in proteins that are to be retained in the endoplasmic reticulum. obo:GO_0030944 obo:go.owl obo:GO_0030944 molecular_function obo:GO_0030944 GO:0030944 obo:GO_0030944 DDEL sequence binding obo:GO_0030945 The catalysis of phosphate removal from a phosphotyrosine using cysteine as a nucleophile and proceed by means of a thiol-phosphate intermediate. obo:GO_0030945 obo:go.owl obo:GO_0030945 molecular_function obo:GO_0030945 GO:0030945 obo:GO_0030945 protein tyrosine phosphatase activity, via thiol-phosphate intermediate obo:GO_0030946 Catalysis of the reaction: protein tyrosine phosphate + H2O = protein tyrosine + phosphate. This reaction requires metal ions. obo:GO_0030946 obo:go.owl obo:GO_0030946 molecular_function obo:GO_0030946 GO:0030946 obo:GO_0030946 protein tyrosine phosphatase activity, metal-dependent obo:GO_0030955 Interacting selectively and non-covalently with potassium (K+) ions. obo:GO_0030955 obo:go.owl obo:GO_0030955 MIPS_funcat:16.17.03 obo:GO_0030955 molecular_function obo:GO_0030955 GO:0030955 obo:GO_0030955 potassium ion binding obo:GO_0030957 Interacting selectively and non-covalently with Tat, a viral transactivating regulatory protein from the human immunodeficiency virus, or the equivalent protein from another virus. obo:GO_0030957 obo:go.owl obo:GO_0030957 molecular_function obo:GO_0030957 GO:0030957 obo:GO_0030957 Tat protein binding obo:GO_0030971 Interacting selectively and non-covalently with a receptor that possesses protein tyrosine kinase activity. obo:GO_0030971 obo:go.owl obo:GO_0030971 molecular_function obo:GO_0030971 transmembrane receptor protein tyrosine kinase ligand binding obo:GO_0030971 GO:0030971 obo:GO_0030971 receptor tyrosine kinase binding obo:GO_0030973 Interacting selectively and non-covalently with molybdate (MoO4 2-) ions. obo:GO_0030973 obo:go.owl obo:GO_0030973 molecular_function obo:GO_0030973 GO:0030973 obo:GO_0030973 molybdate ion binding obo:GO_0030975 Interacting selectively and non-covalently with thiamine (vitamin B1), a water soluble vitamin present in fresh vegetables and meats, especially liver. obo:GO_0030975 obo:go.owl obo:GO_0030975 thiamin binding obo:GO_0030975 vitamin B1 binding obo:GO_0030975 molecular_function obo:GO_0030975 GO:0030975 obo:GO_0030975 thiamine binding obo:GO_0030976 Interacting selectively and non-covalently with thiamine pyrophosphate, the diphosphoric ester of thiamine. Acts as a coenzyme of several (de)carboxylases, transketolases, and alpha-oxoacid dehydrogenases. obo:GO_0030976 obo:go.owl obo:GO_0030976 MIPS_funcat:16.21.11 obo:GO_0030976 TPP binding obo:GO_0030976 aneurine pyrophosphate binding obo:GO_0030976 cocarboxylase binding obo:GO_0030976 diphosphothiamin binding obo:GO_0030976 thiamin pyrophosphate binding obo:GO_0030976 molecular_function obo:GO_0030976 GO:0030976 obo:GO_0030976 thiamine pyrophosphate binding obo:GO_0030977 Interacting selectively and non-covalently with taurine. obo:GO_0030977 obo:go.owl obo:GO_0030977 molecular_function obo:GO_0030977 GO:0030977 obo:GO_0030977 taurine binding obo:GO_0030983 Interacting selectively and non-covalently with double-stranded DNA containing one or more mismatches. obo:GO_0030983 obo:go.owl obo:GO_0030983 GO:0032134 obo:GO_0030983 mispair binding obo:GO_0030983 mispaired DNA binding obo:GO_0030983 molecular_function obo:GO_0030983 GO:0030983 obo:GO_0030983 mismatched DNA binding obo:GO_0030984 Interacting selectively and non-covalently with a kininogen, any of a group of plasma proteins that are kinin precursors. obo:GO_0030984 obo:go.owl obo:GO_0030984 molecular_function obo:GO_0030984 GO:0030984 obo:GO_0030984 kininogen binding obo:GO_0030985 Interacting selectively and non-covalently with a kininogen of high molecular mass. obo:GO_0030985 obo:go.owl obo:GO_0030985 HK binding obo:GO_0030985 HMW kininogen binding obo:GO_0030985 molecular_function obo:GO_0030985 GO:0030985 obo:GO_0030985 high molecular weight kininogen binding obo:GO_0030986 Interacting selectively and non-covalently with a kininogen of low molecular mass. obo:GO_0030986 obo:go.owl obo:GO_0030986 LK binding obo:GO_0030986 LMW kininogen binding obo:GO_0030986 molecular_function obo:GO_0030986 GO:0030986 obo:GO_0030986 low molecular weight kininogen binding obo:GO_0030987 Interacting selectively and non-covalently with a high molecular weight kininogen receptor. obo:GO_0030987 obo:go.owl obo:GO_0030987 molecular_function obo:GO_0030987 GO:0030987 obo:GO_0030987 high molecular weight kininogen receptor binding obo:GO_0031001 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a brefeldin A stimulus. obo:GO_0031001 obo:go.owl obo:GO_0031001 biological_process obo:GO_0031001 GO:0031001 obo:GO_0031001 response to brefeldin A obo:GO_0031005 Interacting selectively and non-covalently with a filamin, any member of a family of high molecular mass cytoskeletal proteins that crosslink actin filaments to form networks and stress fibers. Filamins contain an amino-terminal alpha-actinin-like actin binding domain, which is followed by a rod-domain composed of 4 to 24 100-residue repetitive segments including a carboxy-terminal dimerization domain. obo:GO_0031005 obo:go.owl obo:GO_0031005 GO:0031006 obo:GO_0031005 GO:0031007 obo:GO_0031005 GO:0031008 obo:GO_0031005 filamin C binding obo:GO_0031005 filamin-B binding obo:GO_0031005 ABP-278/276 binding obo:GO_0031005 ABP-280 binding obo:GO_0031005 ABPL binding obo:GO_0031005 alpha-filamin binding obo:GO_0031005 beta-filamin binding obo:GO_0031005 filamin A binding obo:GO_0031005 filamin B binding obo:GO_0031005 filamin-1 binding obo:GO_0031005 filamin-2 binding obo:GO_0031005 filamin-3 binding obo:GO_0031005 filamin-A binding obo:GO_0031005 filamin-C binding obo:GO_0031005 gamma-filamin binding obo:GO_0031005 molecular_function obo:GO_0031005 GO:0031005 obo:GO_0031005 filamin binding obo:GO_0031013 Interacting selectively and non-covalently with troponin I, the inhibitory subunit of the troponin complex. obo:GO_0031013 obo:go.owl obo:GO_0031013 molecular_function obo:GO_0031013 GO:0031013 obo:GO_0031013 troponin I binding obo:GO_0031014 Interacting selectively and non-covalently with troponin T, the tropomyosin-binding subunit of the troponin complex. obo:GO_0031014 obo:go.owl obo:GO_0031014 molecular_function obo:GO_0031014 GO:0031014 obo:GO_0031014 troponin T binding obo:GO_0031072 Interacting selectively and non-covalently with a heat shock protein, any protein synthesized or activated in response to heat shock. obo:GO_0031072 obo:go.owl obo:GO_0031072 molecular_function obo:GO_0031072 GO:0031072 obo:GO_0031072 heat shock protein binding obo:GO_0031177 Interacting selectively and non-covalently with phosphopantetheine, the vitamin pantetheine 4'-(dihydrogen phosphate). obo:GO_0031177 obo:go.owl obo:GO_0031177 molecular_function obo:GO_0031177 GO:0031177 obo:GO_0031177 phosphopantetheine binding obo:GO_0031208 Interacting selectively and non-covalently with a POZ (poxvirus and zinc finger) domain of a protein, a protein-protein interaction domain found in many transcription factors. obo:GO_0031208 obo:go.owl obo:GO_0031208 BTB domain obo:GO_0031208 broad-complex, tramtrack, and bric-a-brac domain binding obo:GO_0031208 molecular_function obo:GO_0031208 GO:0031208 obo:GO_0031208 POZ domain binding obo:GO_0031249 Interacting selectively and non-covalently with denatured proteins. obo:GO_0031249 obo:go.owl obo:GO_0031249 molecular_function obo:GO_0031249 GO:0031249 obo:GO_0031249 Note that this term should not be confused with 'unfolded protein binding ; GO:0051082', which usually refers to proteins that have not yet folded into their active states. Denatured proteins once were in their correct functional conformations, but have become incorrectly folded, and often form aggregates. obo:GO_0031249 denatured protein binding obo:GO_0031267 Interacting selectively and non-covalently with a small monomeric GTPase. obo:GO_0031267 obo:go.owl obo:GO_0031267 molecular_function obo:GO_0031267 GO:0031267 obo:GO_0031267 small GTPase binding obo:GO_0031341 Any process that modulates the frequency, rate or extent of cell killing, the process in which a cell brings about the death of another cell, either in the same or a different organism. obo:GO_0031341 obo:go.owl obo:GO_0031341 biological_process obo:GO_0031341 GO:0031341 obo:GO_0031341 regulation of cell killing obo:GO_0031342 Any process that stops, prevents, or reduces the frequency, rate or extent of cell killing. obo:GO_0031342 obo:go.owl obo:GO_0031342 down regulation of cell killing obo:GO_0031342 down-regulation of cell killing obo:GO_0031342 downregulation of cell killing obo:GO_0031342 inhibition of cell killing obo:GO_0031342 biological_process obo:GO_0031342 GO:0031342 obo:GO_0031342 negative regulation of cell killing obo:GO_0031343 Any process that activates or increases the frequency, rate or extent of cell killing. obo:GO_0031343 obo:go.owl obo:GO_0031343 up regulation of cell killing obo:GO_0031343 up-regulation of cell killing obo:GO_0031343 upregulation of cell killing obo:GO_0031343 activation of cell killing obo:GO_0031343 stimulation of cell killing obo:GO_0031343 biological_process obo:GO_0031343 GO:0031343 obo:GO_0031343 positive regulation of cell killing obo:GO_0031369 Interacting selectively and non-covalently with a translation initiation factor, any polypeptide factor involved in the initiation of ribosome-mediated translation. obo:GO_0031369 obo:go.owl obo:GO_0031369 molecular_function obo:GO_0031369 GO:0031369 obo:GO_0031369 translation initiation factor binding obo:GO_0031370 Interacting selectively and non-covalently with eukaryotic initiation factor 4G, a polypeptide factor involved in the initiation of ribosome-mediated translation. obo:GO_0031370 obo:go.owl obo:GO_0031370 eIF4G binding obo:GO_0031370 molecular_function obo:GO_0031370 GO:0031370 obo:GO_0031370 eukaryotic initiation factor 4G binding obo:GO_0031402 Interacting selectively and non-covalently with sodium ions (Na+). obo:GO_0031402 obo:go.owl obo:GO_0031402 MIPS_funcat:16.17.05 obo:GO_0031402 molecular_function obo:GO_0031402 GO:0031402 obo:GO_0031402 sodium ion binding obo:GO_0031403 Interacting selectively and non-covalently with lithium ions (Li+). obo:GO_0031403 obo:go.owl obo:GO_0031403 molecular_function obo:GO_0031403 GO:0031403 obo:GO_0031403 lithium ion binding obo:GO_0031404 Interacting selectively and non-covalently with chloride ions (Cl-). obo:GO_0031404 obo:go.owl obo:GO_0031404 chloride binding obo:GO_0031404 molecular_function obo:GO_0031404 GO:0031404 obo:GO_0031404 chloride ion binding obo:GO_0031405 Interacting selectively and non-covalently with lipoic acid, 1,2-dithiolane-3-pentanoic acid. obo:GO_0031405 obo:go.owl obo:GO_0031405 molecular_function obo:GO_0031405 GO:0031405 obo:GO_0031405 lipoic acid binding obo:GO_0031406 Interacting selectively and non-covalently with a carboxylic acid, any organic acid containing one or more carboxyl (COOH) groups or anions (COO-). obo:GO_0031406 obo:go.owl obo:GO_0031406 molecular_function obo:GO_0031406 GO:0031406 obo:GO_0031406 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0031406 carboxylic acid binding obo:GO_0031418 Interacting selectively and non-covalently with L-ascorbic acid, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate; L-ascorbic acid is vitamin C and has co-factor and anti-oxidant activities in many species. obo:GO_0031418 obo:go.owl obo:GO_0031418 L-ascorbate binding obo:GO_0031418 vitamin C binding obo:GO_0031418 molecular_function obo:GO_0031418 GO:0031418 obo:GO_0031418 L-ascorbic acid binding obo:GO_0031419 Interacting selectively and non-covalently with cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom. obo:GO_0031419 obo:go.owl obo:GO_0031419 MIPS_funcat:16.21.09 obo:GO_0031419 vitamin B12 binding obo:GO_0031419 molecular_function obo:GO_0031419 GO:0031419 obo:GO_0031419 cobalamin binding obo:GO_0031420 Interacting selectively and non-covalently with any alkali metal ion; alkali metals are those elements in group Ia of the periodic table, with the exception of hydrogen. obo:GO_0031420 obo:go.owl obo:GO_0031420 molecular_function obo:GO_0031420 GO:0031420 obo:GO_0031420 alkali metal ion binding obo:GO_0031423 Interacting selectively and non-covalently with a hexon, the major protein component of the icosahedral capsid of an adenovirus. obo:GO_0031423 obo:go.owl obo:GO_0031423 molecular_function obo:GO_0031423 GO:0031423 obo:GO_0031423 hexon binding obo:GO_0031432 Interacting selectively and non-covalently with titin, any of a family of giant proteins found in striated and smooth muscle. In striated muscle, single titin molecules span half the sarcomere, with their N- and C-termini in the Z-disc and M-line, respectively. obo:GO_0031432 obo:go.owl obo:GO_0031432 molecular_function obo:GO_0031432 GO:0031432 obo:GO_0031432 titin binding obo:GO_0031433 Interacting selectively and non-covalently with telethonin, a protein found in the Z disc of striated muscle and which is a substrate of the titin kinase. obo:GO_0031433 obo:go.owl obo:GO_0031433 molecular_function obo:GO_0031433 GO:0031433 obo:GO_0031433 telethonin binding obo:GO_0031434 Interacting selectively and non-covalently with a mitogen-activated protein kinase kinase, any protein that can phosphorylate a MAP kinase. obo:GO_0031434 obo:go.owl obo:GO_0031434 MAPKK binding obo:GO_0031434 molecular_function obo:GO_0031434 GO:0031434 obo:GO_0031434 mitogen-activated protein kinase kinase binding obo:GO_0031435 Interacting selectively and non-covalently with a mitogen-activated protein kinase kinase kinase, any protein that can phosphorylate a MAP kinase kinase. obo:GO_0031435 obo:go.owl obo:GO_0031435 MAPKKK binding obo:GO_0031435 molecular_function obo:GO_0031435 GO:0031435 obo:GO_0031435 mitogen-activated protein kinase kinase kinase binding obo:GO_0031473 Interacting selectively and non-covalently with a class III myosin; myosin III is monomeric and has an N terminal kinase domain. obo:GO_0031473 obo:go.owl obo:GO_0031473 molecular_function obo:GO_0031473 GO:0031473 obo:GO_0031473 myosin III binding obo:GO_0031489 Interacting selectively and non-covalently with a class V myosin; myosin V is a dimeric molecule involved in intracellular transport. obo:GO_0031489 obo:go.owl obo:GO_0031489 molecular_function obo:GO_0031489 GO:0031489 obo:GO_0031489 myosin V binding obo:GO_0031530 Interacting selectively and non-covalently with a receptor for gonadotropin-releasing hormone (GnRH), a peptide hormone that is synthesized and released by the hypothalamus and is responsible for the release of follicle-stimulating hormone (FSH) and luteinizing hormone (LH) from the anterior pituitary. obo:GO_0031530 obo:go.owl obo:GO_0031530 GnRH receptor binding obo:GO_0031530 gonadotrophin-releasing hormone receptor binding obo:GO_0031530 molecular_function obo:GO_0031530 GO:0031530 obo:GO_0031530 gonadotropin-releasing hormone receptor binding obo:GO_0031531 Interacting selectively and non-covalently with a receptor for thyrotropin-releasing hormone, a tripeptide hormone that is produced by the hypothalamus and stimulates the release of thyroid-stimulating hormone (TSH) and prolactin by the anterior pituitary. obo:GO_0031531 obo:go.owl obo:GO_0031531 GO:0031888 obo:GO_0031531 thyrotropin releasing hormone receptor binding obo:GO_0031531 thyrotropin-releasing hormone receptor ligand obo:GO_0031531 molecular_function obo:GO_0031531 GO:0031531 obo:GO_0031531 thyrotropin-releasing hormone receptor binding obo:GO_0031546 Interacting selectively and non-covalently with the brain-derived neurotrophic factor receptor. obo:GO_0031546 obo:go.owl obo:GO_0031546 BDNF receptor binding obo:GO_0031546 brain-derived neurotrophic factor ligand obo:GO_0031546 molecular_function obo:GO_0031546 GO:0031546 obo:GO_0031546 brain-derived neurotrophic factor receptor binding obo:GO_0031593 Interacting selectively and non-covalently with a protein upon poly-ubiquitination of the target protein. obo:GO_0031593 obo:go.owl obo:GO_0031593 molecular_function obo:GO_0031593 GO:0031593 obo:GO_0031593 polyubiquitin modification-dependent protein binding obo:GO_0031624 Interacting selectively and non-covalently with a ubiquitin conjugating enzyme, any of the E2 proteins. obo:GO_0031624 obo:go.owl obo:GO_0031624 molecular_function obo:GO_0031624 GO:0031624 obo:GO_0031624 ubiquitin conjugating enzyme binding obo:GO_0031625 Interacting selectively and non-covalently with a ubiquitin protein ligase enzyme, any of the E3 proteins. obo:GO_0031625 obo:go.owl obo:GO_0031625 ubiquitin ligase binding obo:GO_0031625 molecular_function obo:GO_0031625 GO:0031625 obo:GO_0031625 ubiquitin protein ligase binding obo:GO_0031628 Interacting selectively and non-covalently with an opioid receptor. obo:GO_0031628 obo:go.owl obo:GO_0031628 molecular_function obo:GO_0031628 GO:0031628 obo:GO_0031628 opioid receptor binding obo:GO_0031634 Interacting selectively and non-covalently with replication fork barriers, sites that inhibit the progress of replication forks. obo:GO_0031634 obo:go.owl obo:GO_0031634 molecular_function obo:GO_0031634 GO:0031634 obo:GO_0031634 replication fork barrier binding obo:GO_0031667 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus reflecting the presence, absence, or concentration of nutrients. obo:GO_0031667 obo:go.owl obo:GO_0031667 biological_process obo:GO_0031667 GO:0031667 obo:GO_0031667 response to nutrient levels obo:GO_0031668 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an extracellular stimulus. obo:GO_0031668 obo:go.owl obo:GO_0031668 biological_process obo:GO_0031668 GO:0031668 obo:GO_0031668 cellular response to extracellular stimulus obo:GO_0031669 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus reflecting the presence, absence, or concentration of nutrients. obo:GO_0031669 obo:go.owl obo:GO_0031669 biological_process obo:GO_0031669 GO:0031669 obo:GO_0031669 cellular response to nutrient levels obo:GO_0031670 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a nutrient stimulus. obo:GO_0031670 obo:go.owl obo:GO_0031670 biological_process obo:GO_0031670 GO:0031670 obo:GO_0031670 cellular response to nutrient obo:GO_0031681 Interacting selectively and non-covalently with a G-protein beta subunit. obo:GO_0031681 obo:go.owl obo:GO_0031681 G-beta protein subunit binding obo:GO_0031681 molecular_function obo:GO_0031681 GO:0031681 obo:GO_0031681 G-protein beta-subunit binding obo:GO_0031682 Interacting selectively and non-covalently with a G-protein gamma subunit. obo:GO_0031682 obo:go.owl obo:GO_0031682 G-gamma protein subunit binding obo:GO_0031682 molecular_function obo:GO_0031682 GO:0031682 obo:GO_0031682 G-protein gamma-subunit binding obo:GO_0031683 Interacting selectively and non-covalently with a complex of G-protein beta/gamma subunits. obo:GO_0031683 obo:go.owl obo:GO_0031683 molecular_function obo:GO_0031683 GO:0031683 obo:GO_0031683 G-protein beta/gamma-subunit complex binding obo:GO_0031685 Interacting selectively and non-covalently with an adenosine receptor. obo:GO_0031685 obo:go.owl obo:GO_0031685 adenosine receptor ligand obo:GO_0031685 molecular_function obo:GO_0031685 GO:0031685 obo:GO_0031685 adenosine receptor binding obo:GO_0031686 Interacting selectively and non-covalently with an A1 adenosine receptor. obo:GO_0031686 obo:go.owl obo:GO_0031686 A1 adenosine receptor ligand obo:GO_0031686 molecular_function obo:GO_0031686 GO:0031686 obo:GO_0031686 A1 adenosine receptor binding obo:GO_0031687 Interacting selectively and non-covalently with an A2A adenosine receptor. obo:GO_0031687 obo:go.owl obo:GO_0031687 A2A adenosine receptor ligand obo:GO_0031687 molecular_function obo:GO_0031687 GO:0031687 obo:GO_0031687 A2A adenosine receptor binding obo:GO_0031688 Interacting selectively and non-covalently with an A2B adenosine receptor. obo:GO_0031688 obo:go.owl obo:GO_0031688 A2B adenosine receptor ligand obo:GO_0031688 molecular_function obo:GO_0031688 GO:0031688 obo:GO_0031688 A2B adenosine receptor binding obo:GO_0031689 Interacting selectively and non-covalently with an A3 adenosine receptor. obo:GO_0031689 obo:go.owl obo:GO_0031689 A3 adenosine receptor ligand obo:GO_0031689 molecular_function obo:GO_0031689 GO:0031689 obo:GO_0031689 A3 adenosine receptor binding obo:GO_0031690 Interacting selectively and non-covalently with an adrenergic receptor. obo:GO_0031690 obo:go.owl obo:GO_0031690 adrenergic receptor ligand obo:GO_0031690 molecular_function obo:GO_0031690 GO:0031690 obo:GO_0031690 adrenergic receptor binding obo:GO_0031691 Interacting selectively and non-covalently with an alpha-1A adrenergic receptor. obo:GO_0031691 obo:go.owl obo:GO_0031691 alpha-1A adrenergic receptor ligand obo:GO_0031691 molecular_function obo:GO_0031691 GO:0031691 obo:GO_0031691 alpha-1A adrenergic receptor binding obo:GO_0031692 Interacting selectively and non-covalently with an alpha-1B adrenergic receptor. obo:GO_0031692 obo:go.owl obo:GO_0031692 alpha-1B adrenergic receptor ligand obo:GO_0031692 molecular_function obo:GO_0031692 GO:0031692 obo:GO_0031692 alpha-1B adrenergic receptor binding obo:GO_0031693 Interacting selectively and non-covalently with an alpha-1D adrenergic receptor. obo:GO_0031693 obo:go.owl obo:GO_0031693 alpha-1D adrenergic receptor ligand obo:GO_0031693 molecular_function obo:GO_0031693 GO:0031693 obo:GO_0031693 alpha-1D adrenergic receptor binding obo:GO_0031694 Interacting selectively and non-covalently with an alpha-2A adrenergic receptor. obo:GO_0031694 obo:go.owl obo:GO_0031694 alpha-2A adrenergic receptor ligand obo:GO_0031694 molecular_function obo:GO_0031694 GO:0031694 obo:GO_0031694 alpha-2A adrenergic receptor binding obo:GO_0031695 Interacting selectively and non-covalently with an alpha-2B adrenergic receptor. obo:GO_0031695 obo:go.owl obo:GO_0031695 alpha-2B adrenergic receptor ligand obo:GO_0031695 molecular_function obo:GO_0031695 GO:0031695 obo:GO_0031695 alpha-2B adrenergic receptor binding obo:GO_0031696 Interacting selectively and non-covalently with an alpha-2C adrenergic receptor. obo:GO_0031696 obo:go.owl obo:GO_0031696 alpha-2C adrenergic receptor ligand obo:GO_0031696 molecular_function obo:GO_0031696 GO:0031696 obo:GO_0031696 alpha-2C adrenergic receptor binding obo:GO_0031697 Interacting selectively and non-covalently with a beta-1 adrenergic receptor. obo:GO_0031697 obo:go.owl obo:GO_0031697 beta-1 adrenergic receptor ligand obo:GO_0031697 molecular_function obo:GO_0031697 GO:0031697 obo:GO_0031697 beta-1 adrenergic receptor binding obo:GO_0031698 Interacting selectively and non-covalently with a beta-2 adrenergic receptor. obo:GO_0031698 obo:go.owl obo:GO_0031698 beta-2 adrenergic receptor ligand obo:GO_0031698 molecular_function obo:GO_0031698 GO:0031698 obo:GO_0031698 beta-2 adrenergic receptor binding obo:GO_0031699 Interacting selectively and non-covalently with a beta-3 adrenergic receptor. obo:GO_0031699 obo:go.owl obo:GO_0031699 beta-3 adrenergic receptor ligand obo:GO_0031699 molecular_function obo:GO_0031699 GO:0031699 obo:GO_0031699 beta-3 adrenergic receptor binding obo:GO_0031700 Interacting selectively and non-covalently with an adrenomedullin receptor. obo:GO_0031700 obo:go.owl obo:GO_0031700 adrenomedullin receptor ligand obo:GO_0031700 molecular_function obo:GO_0031700 GO:0031700 obo:GO_0031700 adrenomedullin receptor binding obo:GO_0031701 Interacting selectively and non-covalently with an angiotensin receptor. obo:GO_0031701 obo:go.owl obo:GO_0031701 angiotensin receptor ligand obo:GO_0031701 molecular_function obo:GO_0031701 GO:0031701 obo:GO_0031701 angiotensin receptor binding obo:GO_0031702 Interacting selectively and non-covalently with a type 1 angiotensin receptor. obo:GO_0031702 obo:go.owl obo:GO_0031702 AT1 receptor binding obo:GO_0031702 type 1 angiotensin receptor ligand obo:GO_0031702 molecular_function obo:GO_0031702 GO:0031702 obo:GO_0031702 type 1 angiotensin receptor binding obo:GO_0031703 Interacting selectively and non-covalently with a type 2 angiotensin receptor. obo:GO_0031703 obo:go.owl obo:GO_0031703 AT2 receptor binding obo:GO_0031703 type 2 angiotensin receptor ligand obo:GO_0031703 molecular_function obo:GO_0031703 GO:0031703 obo:GO_0031703 type 2 angiotensin receptor binding obo:GO_0031704 Interacting selectively and non-covalently with an apelin receptor. obo:GO_0031704 obo:go.owl obo:GO_0031704 GO:0042569 obo:GO_0031704 APJ receptor binding obo:GO_0031704 apelin receptor ligand obo:GO_0031704 molecular_function obo:GO_0031704 GO:0031704 obo:GO_0031704 apelin receptor binding obo:GO_0031705 Interacting selectively and non-covalently with a bombesin receptor. obo:GO_0031705 obo:go.owl obo:GO_0031705 bombesin receptor ligand obo:GO_0031705 molecular_function obo:GO_0031705 GO:0031705 obo:GO_0031705 bombesin receptor binding obo:GO_0031706 Interacting selectively and non-covalently with a subtype 3 bombesin receptor. obo:GO_0031706 obo:go.owl obo:GO_0031706 subtype 3 bombesin receptor ligand obo:GO_0031706 molecular_function obo:GO_0031706 GO:0031706 obo:GO_0031706 subtype 3 bombesin receptor binding obo:GO_0031707 Interacting selectively and non-covalently with an endothelin A receptor. obo:GO_0031707 obo:go.owl obo:GO_0031707 endothelin-1 receptor binding obo:GO_0031707 endothelin A receptor ligand obo:GO_0031707 molecular_function obo:GO_0031707 GO:0031707 obo:GO_0031707 endothelin A receptor binding obo:GO_0031708 Interacting selectively and non-covalently with an endothelin B receptor. obo:GO_0031708 obo:go.owl obo:GO_0031708 endothelin B receptor ligand obo:GO_0031708 molecular_function obo:GO_0031708 GO:0031708 obo:GO_0031708 endothelin B receptor binding obo:GO_0031709 Interacting selectively and non-covalently with a gastrin-releasing peptide receptor. obo:GO_0031709 obo:go.owl obo:GO_0031709 GRP receptor binding obo:GO_0031709 gastrin-releasing peptide receptor ligand obo:GO_0031709 molecular_function obo:GO_0031709 GO:0031709 obo:GO_0031709 gastrin-releasing peptide receptor binding obo:GO_0031710 Interacting selectively and non-covalently with a neuromedin B receptor. obo:GO_0031710 obo:go.owl obo:GO_0031710 neuromedin B receptor ligand obo:GO_0031710 molecular_function obo:GO_0031710 GO:0031710 obo:GO_0031710 neuromedin B receptor binding obo:GO_0031711 Interacting selectively and non-covalently with a bradykinin receptor. obo:GO_0031711 obo:go.owl obo:GO_0031711 bradykinin receptor ligand obo:GO_0031711 molecular_function obo:GO_0031711 GO:0031711 obo:GO_0031711 bradykinin receptor binding obo:GO_0031712 Interacting selectively and non-covalently with a B1 bradykinin receptor. obo:GO_0031712 obo:go.owl obo:GO_0031712 B1 bradykinin receptor ligand obo:GO_0031712 molecular_function obo:GO_0031712 GO:0031712 obo:GO_0031712 B1 bradykinin receptor binding obo:GO_0031713 Interacting selectively and non-covalently with a B2 bradykinin receptor. obo:GO_0031713 obo:go.owl obo:GO_0031713 B2 bradykinin receptor ligand obo:GO_0031713 molecular_function obo:GO_0031713 GO:0031713 obo:GO_0031713 B2 bradykinin receptor binding obo:GO_0031714 Interacting selectively and non-covalently with a C5a anaphylatoxin chemotactic receptor. obo:GO_0031714 obo:go.owl obo:GO_0031714 C5a anaphylatoxin chemotactic receptor ligand obo:GO_0031714 molecular_function obo:GO_0031714 GO:0031714 obo:GO_0031714 C5a anaphylatoxin chemotactic receptor binding obo:GO_0031715 Interacting selectively and non-covalently with a C5L2 anaphylatoxin chemotactic receptor. obo:GO_0031715 obo:go.owl obo:GO_0031715 C5L2 anaphylatoxin chemotactic receptor ligand obo:GO_0031715 molecular_function obo:GO_0031715 GO:0031715 obo:GO_0031715 C5L2 anaphylatoxin chemotactic receptor binding obo:GO_0031716 Interacting selectively and non-covalently with a calcitonin receptor. obo:GO_0031716 obo:go.owl obo:GO_0031716 calcitonin receptor ligand obo:GO_0031716 molecular_function obo:GO_0031716 GO:0031716 obo:GO_0031716 calcitonin receptor binding obo:GO_0031717 Interacting selectively and non-covalently with a cannabinoid receptor. obo:GO_0031717 obo:go.owl obo:GO_0031717 cannabinoid receptor ligand obo:GO_0031717 molecular_function obo:GO_0031717 GO:0031717 obo:GO_0031717 cannabinoid receptor binding obo:GO_0031718 Interacting selectively and non-covalently with a type 1 cannabinoid receptor. obo:GO_0031718 obo:go.owl obo:GO_0031718 type 1 cannabinoid receptor ligand obo:GO_0031718 molecular_function obo:GO_0031718 GO:0031718 obo:GO_0031718 type 1 cannabinoid receptor binding obo:GO_0031719 Interacting selectively and non-covalently with a type 2 cannabinoid receptor. obo:GO_0031719 obo:go.owl obo:GO_0031719 type 2 cannabinoid receptor ligand obo:GO_0031719 molecular_function obo:GO_0031719 GO:0031719 obo:GO_0031719 type 2 cannabinoid receptor binding obo:GO_0031720 Interacting selectively and non-covalently with a haptoglobin, any alpha2 globulin of blood plasma that can combine with free oxyhemoglobin to form a stable complex. obo:GO_0031720 obo:go.owl obo:GO_0031720 molecular_function obo:GO_0031720 GO:0031720 obo:GO_0031720 haptoglobin binding obo:GO_0031721 Interacting selectively and non-covalently with a hemoglobin alpha chain. obo:GO_0031721 obo:go.owl obo:GO_0031721 molecular_function obo:GO_0031721 GO:0031721 obo:GO_0031721 hemoglobin alpha binding obo:GO_0031722 Interacting selectively and non-covalently with a hemoglobin beta chain. obo:GO_0031722 obo:go.owl obo:GO_0031722 molecular_function obo:GO_0031722 GO:0031722 obo:GO_0031722 hemoglobin beta binding obo:GO_0031723 Interacting selectively and non-covalently with a CXCR4 chemokine receptor. obo:GO_0031723 obo:go.owl obo:GO_0031723 stromal cell-derived factor 1 receptor binding obo:GO_0031723 CXCR4 chemokine receptor ligand obo:GO_0031723 molecular_function obo:GO_0031723 GO:0031723 obo:GO_0031723 CXCR4 chemokine receptor binding obo:GO_0031724 Interacting selectively and non-covalently with a CXCR5 chemokine receptor. obo:GO_0031724 obo:go.owl obo:GO_0031724 type 1 Burkitt's lymphoma receptor binding obo:GO_0031724 CXCR5 chemokine receptor ligand obo:GO_0031724 molecular_function obo:GO_0031724 GO:0031724 obo:GO_0031724 CXCR5 chemokine receptor binding obo:GO_0031725 Interacting selectively and non-covalently with a CXCR6 chemokine receptor. obo:GO_0031725 obo:go.owl obo:GO_0031725 STRL33 receptor binding obo:GO_0031725 bonzo receptor binding obo:GO_0031725 CXCR6 chemokine receptor ligand obo:GO_0031725 molecular_function obo:GO_0031725 GO:0031725 obo:GO_0031725 CXCR6 chemokine receptor binding obo:GO_0031726 Interacting selectively and non-covalently with a CCR1 chemokine receptor. obo:GO_0031726 obo:go.owl obo:GO_0031726 macrophage inflammatory protein-1 alpha receptor binding obo:GO_0031726 CCR1 chemokine receptor ligand obo:GO_0031726 molecular_function obo:GO_0031726 GO:0031726 obo:GO_0031726 CCR1 chemokine receptor binding obo:GO_0031727 Interacting selectively and non-covalently with a CCR2 chemokine receptor. obo:GO_0031727 obo:go.owl obo:GO_0031727 monocyte chemoattractant protein 1 receptor binding obo:GO_0031727 CCR2 chemokine receptor ligand obo:GO_0031727 molecular_function obo:GO_0031727 GO:0031727 obo:GO_0031727 CCR2 chemokine receptor binding obo:GO_0031728 Interacting selectively and non-covalently with a CCR3 chemokine receptor. obo:GO_0031728 obo:go.owl obo:GO_0031728 eosinophil eotaxin receptor binding obo:GO_0031728 CCR3 chemokine receptor ligand obo:GO_0031728 molecular_function obo:GO_0031728 GO:0031728 obo:GO_0031728 CCR3 chemokine receptor binding obo:GO_0031729 Interacting selectively and non-covalently with a CCR4 chemokine receptor. obo:GO_0031729 obo:go.owl obo:GO_0031729 CCR4 chemokine receptor ligand obo:GO_0031729 molecular_function obo:GO_0031729 GO:0031729 obo:GO_0031729 CCR4 chemokine receptor binding obo:GO_0031730 Interacting selectively and non-covalently with a CCR5 chemokine receptor. obo:GO_0031730 obo:go.owl obo:GO_0031730 CCR5 chemokine receptor ligand obo:GO_0031730 molecular_function obo:GO_0031730 GO:0031730 obo:GO_0031730 CCR5 chemokine receptor binding obo:GO_0031731 Interacting selectively and non-covalently with a CCR6 chemokine receptor. obo:GO_0031731 obo:go.owl obo:GO_0031731 LARC receptor binding obo:GO_0031731 CCR6 chemokine receptor ligand obo:GO_0031731 molecular_function obo:GO_0031731 GO:0031731 obo:GO_0031731 CCR6 chemokine receptor binding obo:GO_0031732 Interacting selectively and non-covalently with a CCR7 chemokine receptor. obo:GO_0031732 obo:go.owl obo:GO_0031732 MIP-3 beta receptor binding obo:GO_0031732 type 1 EBV-induced G-protein coupled receptor binding obo:GO_0031732 CCR7 chemokine receptor ligand obo:GO_0031732 molecular_function obo:GO_0031732 GO:0031732 obo:GO_0031732 CCR7 chemokine receptor binding obo:GO_0031733 Interacting selectively and non-covalently with a CCR8 chemokine receptor. obo:GO_0031733 obo:go.owl obo:GO_0031733 CCR8 chemokine receptor ligand obo:GO_0031733 molecular_function obo:GO_0031733 GO:0031733 obo:GO_0031733 CCR8 chemokine receptor binding obo:GO_0031734 Interacting selectively and non-covalently with a CCR9 chemokine receptor. obo:GO_0031734 obo:go.owl obo:GO_0031734 CCR9 chemokine receptor ligand obo:GO_0031734 molecular_function obo:GO_0031734 GO:0031734 obo:GO_0031734 CCR9 chemokine receptor binding obo:GO_0031735 Interacting selectively and non-covalently with a CCR10 chemokine receptor. obo:GO_0031735 obo:go.owl obo:GO_0031735 CCR10 chemokine receptor ligand obo:GO_0031735 molecular_function obo:GO_0031735 GO:0031735 obo:GO_0031735 CCR10 chemokine receptor binding obo:GO_0031736 Interacting selectively and non-covalently with a CCR11 chemokine receptor. obo:GO_0031736 obo:go.owl obo:GO_0031736 CCR11 chemokine receptor ligand obo:GO_0031736 molecular_function obo:GO_0031736 GO:0031736 obo:GO_0031736 CCR11 chemokine receptor binding obo:GO_0031737 Interacting selectively and non-covalently with a CX3C chemokine receptor. obo:GO_0031737 obo:go.owl obo:GO_0031737 fractalkine receptor binding obo:GO_0031737 CX3C chemokine receptor ligand obo:GO_0031737 molecular_function obo:GO_0031737 GO:0031737 obo:GO_0031737 CX3C chemokine receptor binding obo:GO_0031738 Interacting selectively and non-covalently with a XCR1 chemokine receptor. obo:GO_0031738 obo:go.owl obo:GO_0031738 lymphotactin receptor binding obo:GO_0031738 XCR1 chemokine receptor ligand obo:GO_0031738 molecular_function obo:GO_0031738 GO:0031738 obo:GO_0031738 XCR1 chemokine receptor binding obo:GO_0031739 Interacting selectively and non-covalently with a cholecystokinin receptor. obo:GO_0031739 obo:go.owl obo:GO_0031739 cholecystokinin receptor ligand obo:GO_0031739 molecular_function obo:GO_0031739 GO:0031739 obo:GO_0031739 cholecystokinin receptor binding obo:GO_0031740 Interacting selectively and non-covalently with a type A cholecystokinin receptor. obo:GO_0031740 obo:go.owl obo:GO_0031740 type A cholecystokinin receptor ligand obo:GO_0031740 molecular_function obo:GO_0031740 GO:0031740 obo:GO_0031740 type A cholecystokinin receptor binding obo:GO_0031741 Interacting selectively and non-covalently with a type B gastrin/cholecystokinin receptor. obo:GO_0031741 obo:go.owl obo:GO_0031741 type B gastrin/cholecystokinin receptor ligand obo:GO_0031741 molecular_function obo:GO_0031741 GO:0031741 obo:GO_0031741 type B gastrin/cholecystokinin receptor binding obo:GO_0031745 Interacting selectively and non-covalently with a cysteinyl leukotriene receptor. obo:GO_0031745 obo:go.owl obo:GO_0031745 cysteinyl leukotriene receptor ligand obo:GO_0031745 molecular_function obo:GO_0031745 GO:0031745 obo:GO_0031745 cysteinyl leukotriene receptor binding obo:GO_0031746 Interacting selectively and non-covalently with a type 1 cysteinyl leukotriene receptor. obo:GO_0031746 obo:go.owl obo:GO_0031746 type 1 cysteinyl leukotriene receptor ligand obo:GO_0031746 molecular_function obo:GO_0031746 GO:0031746 obo:GO_0031746 type 1 cysteinyl leukotriene receptor binding obo:GO_0031747 Interacting selectively and non-covalently with a type 2 cysteinyl leukotriene receptor. obo:GO_0031747 obo:go.owl obo:GO_0031747 type 2 cysteinyl leukotriene receptor ligand obo:GO_0031747 molecular_function obo:GO_0031747 GO:0031747 obo:GO_0031747 type 2 cysteinyl leukotriene receptor binding obo:GO_0031748 Interacting selectively and non-covalently with a D1 dopamine receptor. obo:GO_0031748 obo:go.owl obo:GO_0031748 D1A dopamine receptor binding obo:GO_0031748 D1 dopamine receptor ligand obo:GO_0031748 molecular_function obo:GO_0031748 GO:0031748 obo:GO_0031748 D1 dopamine receptor binding obo:GO_0031749 Interacting selectively and non-covalently with a D2 dopamine receptor. obo:GO_0031749 obo:go.owl obo:GO_0031749 D2 dopamine receptor ligand obo:GO_0031749 molecular_function obo:GO_0031749 GO:0031749 obo:GO_0031749 D2 dopamine receptor binding obo:GO_0031750 Interacting selectively and non-covalently with a D3 dopamine receptor. obo:GO_0031750 obo:go.owl obo:GO_0031750 D3 dopamine receptor ligand obo:GO_0031750 molecular_function obo:GO_0031750 GO:0031750 obo:GO_0031750 D3 dopamine receptor binding obo:GO_0031751 Interacting selectively and non-covalently with a D4 dopamine receptor. obo:GO_0031751 obo:go.owl obo:GO_0031751 D4 dopamine receptor ligand obo:GO_0031751 molecular_function obo:GO_0031751 GO:0031751 obo:GO_0031751 D4 dopamine receptor binding obo:GO_0031752 Interacting selectively and non-covalently with a D5 dopamine receptor. obo:GO_0031752 obo:go.owl obo:GO_0031752 D1B dopamine receptor binding obo:GO_0031752 D5 dopamine receptor ligand obo:GO_0031752 molecular_function obo:GO_0031752 GO:0031752 obo:GO_0031752 D5 dopamine receptor binding obo:GO_0031753 Interacting selectively and non-covalently with an endothelial differentiation G protein-coupled receptor. obo:GO_0031753 obo:go.owl obo:GO_0031753 endothelial differentiation G-protein coupled receptor binding obo:GO_0031753 endothelial differentiation G-protein coupled receptor ligand obo:GO_0031753 molecular_function obo:GO_0031753 GO:0031753 obo:GO_0031753 endothelial differentiation G protein-coupled receptor binding obo:GO_0031754 Interacting selectively and non-covalently with an Edg-1 sphingosine 1-phosphate receptor. obo:GO_0031754 obo:go.owl obo:GO_0031754 Edg-1 sphingosine 1-phosphate receptor ligand obo:GO_0031754 molecular_function obo:GO_0031754 GO:0031754 obo:GO_0031754 Edg-1 sphingosine 1-phosphate receptor binding obo:GO_0031755 Interacting selectively and non-covalently with an Edg-2 lysophosphatidic acid receptor. obo:GO_0031755 obo:go.owl obo:GO_0031755 LPA1 receptor binding obo:GO_0031755 Edg-2 lysophosphatidic acid receptor ligand obo:GO_0031755 molecular_function obo:GO_0031755 GO:0031755 obo:GO_0031755 Edg-2 lysophosphatidic acid receptor binding obo:GO_0031756 Interacting selectively and non-covalently with an Edg-3 sphingosine 1-phosphate receptor. obo:GO_0031756 obo:go.owl obo:GO_0031756 Edg-3 sphingosine 1-phosphate receptor ligand obo:GO_0031756 molecular_function obo:GO_0031756 GO:0031756 obo:GO_0031756 Edg-3 sphingosine 1-phosphate receptor binding obo:GO_0031757 Interacting selectively and non-covalently with an Edg-4 lysophosphatidic acid receptor. obo:GO_0031757 obo:go.owl obo:GO_0031757 LPA2 receptor binding obo:GO_0031757 Edg-4 lysophosphatidic acid receptor ligand obo:GO_0031757 molecular_function obo:GO_0031757 GO:0031757 obo:GO_0031757 Edg-4 lysophosphatidic acid receptor binding obo:GO_0031758 Interacting selectively and non-covalently with an Edg-5 sphingosine 1-phosphate receptor. obo:GO_0031758 obo:go.owl obo:GO_0031758 Edg-5 sphingosine 1-phosphate receptor ligand obo:GO_0031758 molecular_function obo:GO_0031758 GO:0031758 obo:GO_0031758 Edg-5 sphingosine 1-phosphate receptor binding obo:GO_0031759 Interacting selectively and non-covalently with an Edg-6 sphingosine 1-phosphate receptor. obo:GO_0031759 obo:go.owl obo:GO_0031759 Edg-6 sphingosine 1-phosphate receptor ligand obo:GO_0031759 molecular_function obo:GO_0031759 GO:0031759 obo:GO_0031759 Edg-6 sphingosine 1-phosphate receptor binding obo:GO_0031760 Interacting selectively and non-covalently with an Edg-7 lysophosphatidic acid receptor. obo:GO_0031760 obo:go.owl obo:GO_0031760 LPA3 receptor binding obo:GO_0031760 Edg-7 lysophosphatidic acid receptor ligand obo:GO_0031760 molecular_function obo:GO_0031760 GO:0031760 obo:GO_0031760 Edg-7 lysophosphatidic acid receptor binding obo:GO_0031761 Interacting selectively and non-covalently with a fMet-Leu-Phe receptor. obo:GO_0031761 obo:go.owl obo:GO_0031761 N-formyl peptide receptor binding obo:GO_0031761 fMet-Leu-Phe receptor ligand obo:GO_0031761 molecular_function obo:GO_0031761 GO:0031761 obo:GO_0031761 fMet-Leu-Phe receptor binding obo:GO_0031762 Interacting selectively and non-covalently with a follicle-stimulating hormone receptor. obo:GO_0031762 obo:go.owl obo:GO_0031762 FSH receptor binding obo:GO_0031762 follicle stimulating hormone receptor binding obo:GO_0031762 follicle stimulating hormone receptor ligand obo:GO_0031762 molecular_function obo:GO_0031762 GO:0031762 obo:GO_0031762 follicle-stimulating hormone receptor binding obo:GO_0031763 Interacting selectively and non-covalently with a galanin receptor. obo:GO_0031763 obo:go.owl obo:GO_0031763 galanin receptor ligand obo:GO_0031763 molecular_function obo:GO_0031763 GO:0031763 obo:GO_0031763 galanin receptor binding obo:GO_0031764 Interacting selectively and non-covalently with a type 1 galanin receptor. obo:GO_0031764 obo:go.owl obo:GO_0031764 type 1 galanin receptor ligand obo:GO_0031764 molecular_function obo:GO_0031764 GO:0031764 obo:GO_0031764 type 1 galanin receptor binding obo:GO_0031765 Interacting selectively and non-covalently with a type 2 galanin receptor. obo:GO_0031765 obo:go.owl obo:GO_0031765 type 2 galanin receptor ligand obo:GO_0031765 molecular_function obo:GO_0031765 GO:0031765 obo:GO_0031765 type 2 galanin receptor binding obo:GO_0031766 Interacting selectively and non-covalently with a type 3 galanin receptor. obo:GO_0031766 obo:go.owl obo:GO_0031766 type 3 galanin receptor ligand obo:GO_0031766 molecular_function obo:GO_0031766 GO:0031766 obo:GO_0031766 type 3 galanin receptor binding obo:GO_0031767 Interacting selectively and non-covalently with a gastric inhibitory polypeptide receptor. obo:GO_0031767 obo:go.owl obo:GO_0031767 gastric inhibitory polypeptide receptor ligand obo:GO_0031767 molecular_function obo:GO_0031767 GO:0031767 obo:GO_0031767 gastric inhibitory polypeptide receptor binding obo:GO_0031768 Interacting selectively and non-covalently with a ghrelin receptor. obo:GO_0031768 obo:go.owl obo:GO_0031768 type 1 growth hormone secretagogue GH-releasing peptide receptor binding obo:GO_0031768 ghrelin receptor ligand obo:GO_0031768 molecular_function obo:GO_0031768 GO:0031768 obo:GO_0031768 ghrelin receptor binding obo:GO_0031769 Interacting selectively and non-covalently with a glucagon receptor. obo:GO_0031769 obo:go.owl obo:GO_0031769 glucagon receptor ligand obo:GO_0031769 molecular_function obo:GO_0031769 GO:0031769 obo:GO_0031769 glucagon receptor binding obo:GO_0031770 Interacting selectively and non-covalently with a growth hormone-releasing hormone receptor. obo:GO_0031770 obo:go.owl obo:GO_0031770 growth hormone-releasing hormone receptor ligand obo:GO_0031770 molecular_function obo:GO_0031770 GO:0031770 obo:GO_0031770 growth hormone-releasing hormone receptor binding obo:GO_0031771 Interacting selectively and non-covalently with a type 1 hypocretin receptor. obo:GO_0031771 obo:go.owl obo:GO_0031771 type 1 orexin receptor binding obo:GO_0031771 type 1 hypocretin receptor ligand obo:GO_0031771 molecular_function obo:GO_0031771 GO:0031771 obo:GO_0031771 type 1 hypocretin receptor binding obo:GO_0031772 Interacting selectively and non-covalently with a type 2 hypocretin receptor. obo:GO_0031772 obo:go.owl obo:GO_0031772 type 2 orexin receptor binding obo:GO_0031772 type 2 hypocretin receptor ligand obo:GO_0031772 molecular_function obo:GO_0031772 GO:0031772 obo:GO_0031772 type 2 hypocretin receptor binding obo:GO_0031773 Interacting selectively and non-covalently with a kisspeptin receptor. obo:GO_0031773 obo:go.owl obo:GO_0031773 G-protein coupled receptor 54 binding obo:GO_0031773 KiSS-1 receptor binding obo:GO_0031773 hOT7T175 receptor binding obo:GO_0031773 hypogonadotropin-1 receptor binding obo:GO_0031773 metastin receptor binding obo:GO_0031773 kisspeptin receptor ligand obo:GO_0031773 molecular_function obo:GO_0031773 GO:0031773 obo:GO_0031773 kisspeptin receptor binding obo:GO_0031774 Interacting selectively and non-covalently with a leukotriene receptor. obo:GO_0031774 obo:go.owl obo:GO_0031774 leukotriene receptor ligand obo:GO_0031774 molecular_function obo:GO_0031774 GO:0031774 obo:GO_0031774 leukotriene receptor binding obo:GO_0031775 Interacting selectively and non-covalently with a lutropin-choriogonadotropic hormone receptor. obo:GO_0031775 obo:go.owl obo:GO_0031775 lutropin-choriogonadotropic hormone receptor ligand obo:GO_0031775 molecular_function obo:GO_0031775 GO:0031775 obo:GO_0031775 lutropin-choriogonadotropic hormone receptor binding obo:GO_0031776 Interacting selectively and non-covalently with a melanin-concentrating hormone receptor. obo:GO_0031776 obo:go.owl obo:GO_0031776 melanin-concentrating hormone receptor ligand obo:GO_0031776 molecular_function obo:GO_0031776 GO:0031776 obo:GO_0031776 melanin-concentrating hormone receptor binding obo:GO_0031777 Interacting selectively and non-covalently with a type 1 melanin-concentrating hormone receptor. obo:GO_0031777 obo:go.owl obo:GO_0031777 type 1 melanin-concentrating hormone receptor ligand obo:GO_0031777 molecular_function obo:GO_0031777 GO:0031777 obo:GO_0031777 type 1 melanin-concentrating hormone receptor binding obo:GO_0031778 Interacting selectively and non-covalently with a type 2 melanin-concentrating hormone receptor. obo:GO_0031778 obo:go.owl obo:GO_0031778 type 2 melanin-concentrating hormone receptor ligand obo:GO_0031778 molecular_function obo:GO_0031778 GO:0031778 obo:GO_0031778 type 2 melanin-concentrating hormone receptor binding obo:GO_0031779 Interacting selectively and non-covalently with a melanocortin receptor. obo:GO_0031779 obo:go.owl obo:GO_0031779 melanocortin receptor ligand obo:GO_0031779 molecular_function obo:GO_0031779 GO:0031779 obo:GO_0031779 melanocortin receptor binding obo:GO_0031780 Interacting selectively and non-covalently with a corticotropin hormone receptor. obo:GO_0031780 obo:go.owl obo:GO_0031780 GO:0071856 obo:GO_0031780 ACTH receptor binding obo:GO_0031780 adrenocorticotropin hormone receptor binding obo:GO_0031780 adrenocorticotropin receptor binding obo:GO_0031780 corticotropin receptor binding obo:GO_0031780 adrenocorticotropic hormone receptor ligand obo:GO_0031780 molecular_function obo:GO_0031780 GO:0031780 obo:GO_0031780 corticotropin hormone receptor binding obo:GO_0031781 Interacting selectively and non-covalently with a type 3 melanocortin receptor. obo:GO_0031781 obo:go.owl obo:GO_0031781 type 3 melanocortin receptor ligand obo:GO_0031781 molecular_function obo:GO_0031781 GO:0031781 obo:GO_0031781 type 3 melanocortin receptor binding obo:GO_0031782 Interacting selectively and non-covalently with a type 4 melanocortin receptor. obo:GO_0031782 obo:go.owl obo:GO_0031782 type 4 melanocortin receptor ligand obo:GO_0031782 molecular_function obo:GO_0031782 GO:0031782 obo:GO_0031782 type 4 melanocortin receptor binding obo:GO_0031783 Interacting selectively and non-covalently with a type 5 melanocortin receptor. obo:GO_0031783 obo:go.owl obo:GO_0031783 type 5 melanocortin receptor ligand obo:GO_0031783 molecular_function obo:GO_0031783 GO:0031783 obo:GO_0031783 type 5 melanocortin receptor binding obo:GO_0031784 Interacting selectively and non-covalently with a melatonin receptor. obo:GO_0031784 obo:go.owl obo:GO_0031784 melatonin receptor ligand obo:GO_0031784 molecular_function obo:GO_0031784 GO:0031784 obo:GO_0031784 melatonin receptor binding obo:GO_0031785 Interacting selectively and non-covalently with a type 1A melatonin receptor. obo:GO_0031785 obo:go.owl obo:GO_0031785 type 1A melatonin receptor ligand obo:GO_0031785 molecular_function obo:GO_0031785 GO:0031785 obo:GO_0031785 type 1A melatonin receptor binding obo:GO_0031786 Interacting selectively and non-covalently with a type 1B melatonin receptor. obo:GO_0031786 obo:go.owl obo:GO_0031786 type 1B melatonin receptor ligand obo:GO_0031786 molecular_function obo:GO_0031786 GO:0031786 obo:GO_0031786 type 1B melatonin receptor binding obo:GO_0031787 Interacting selectively and non-covalently with a H9 melatonin receptor. obo:GO_0031787 obo:go.owl obo:GO_0031787 H9 melatonin receptor ligand obo:GO_0031787 molecular_function obo:GO_0031787 GO:0031787 obo:GO_0031787 H9 melatonin receptor binding obo:GO_0031788 Interacting selectively and non-covalently with a motilin receptor. obo:GO_0031788 obo:go.owl obo:GO_0031788 motilin receptor ligand obo:GO_0031788 molecular_function obo:GO_0031788 GO:0031788 obo:GO_0031788 motilin receptor binding obo:GO_0031789 Interacting selectively and non-covalently with a G protein-coupled acetylcholine receptor. obo:GO_0031789 obo:go.owl obo:GO_0031789 GO:0031790 obo:GO_0031789 GO:0031791 obo:GO_0031789 GO:0031792 obo:GO_0031789 GO:0031793 obo:GO_0031789 GO:0031794 obo:GO_0031789 G-protein coupled acetylcholine receptor binding obo:GO_0031789 muscarinic acetylcholine receptor binding obo:GO_0031789 M1 muscarinic acetylcholine receptor binding obo:GO_0031789 M1 muscarinic acetylcholine receptor ligand obo:GO_0031789 M2 muscarinic acetylcholine receptor binding obo:GO_0031789 M2 muscarinic acetylcholine receptor ligand obo:GO_0031789 M3 muscarinic acetylcholine receptor binding obo:GO_0031789 M3 muscarinic acetylcholine receptor ligand obo:GO_0031789 M4 muscarinic acetylcholine receptor binding obo:GO_0031789 M4 muscarinic acetylcholine receptor ligand obo:GO_0031789 M5 muscarinic acetylcholine receptor binding obo:GO_0031789 M5 muscarinic acetylcholine receptor ligand obo:GO_0031789 muscarinic acetylcholine receptor ligand obo:GO_0031789 molecular_function obo:GO_0031789 GO:0031789 obo:GO_0031789 G protein-coupled acetylcholine receptor binding obo:GO_0031795 Interacting selectively and non-covalently with a G protein-coupled (metabotropic) GABA receptor. obo:GO_0031795 obo:go.owl obo:GO_0031795 G-protein coupled GABA receptor binding obo:GO_0031795 GABAB receptor binding obo:GO_0031795 metabotropic GABA receptor binding obo:GO_0031795 metabotropic GABA receptor ligand obo:GO_0031795 molecular_function obo:GO_0031795 GO:0031795 obo:GO_0031795 G protein-coupled GABA receptor binding obo:GO_0031796 Interacting selectively and non-covalently with a type 1 metabotropic GABA receptor. obo:GO_0031796 obo:go.owl obo:GO_0031796 type 1 metabotropic GABA receptor ligand obo:GO_0031796 molecular_function obo:GO_0031796 GO:0031796 obo:GO_0031796 type 1 metabotropic GABA receptor binding obo:GO_0031797 Interacting selectively and non-covalently with a type 2 metabotropic GABA receptor. obo:GO_0031797 obo:go.owl obo:GO_0031797 type 2 metabotropic GABA receptor ligand obo:GO_0031797 molecular_function obo:GO_0031797 GO:0031797 obo:GO_0031797 type 2 metabotropic GABA receptor binding obo:GO_0031798 Interacting selectively and non-covalently with a type 1 metabotropic glutamate receptor. obo:GO_0031798 obo:go.owl obo:GO_0031798 type 1 metabotropic glutamate receptor ligand obo:GO_0031798 molecular_function obo:GO_0031798 GO:0031798 obo:GO_0031798 type 1 metabotropic glutamate receptor binding obo:GO_0031799 Interacting selectively and non-covalently with a type 2 metabotropic glutamate receptor. obo:GO_0031799 obo:go.owl obo:GO_0031799 type 2 metabotropic glutamate receptor ligand obo:GO_0031799 molecular_function obo:GO_0031799 GO:0031799 obo:GO_0031799 type 2 metabotropic glutamate receptor binding obo:GO_0031800 Interacting selectively and non-covalently with a type 3 metabotropic glutamate receptor. obo:GO_0031800 obo:go.owl obo:GO_0031800 type 3 metabotropic glutamate receptor ligand obo:GO_0031800 molecular_function obo:GO_0031800 GO:0031800 obo:GO_0031800 type 3 metabotropic glutamate receptor binding obo:GO_0031801 Interacting selectively and non-covalently with a type 4 metabotropic glutamate receptor. obo:GO_0031801 obo:go.owl obo:GO_0031801 type 4 metabotropic glutamate receptor ligand obo:GO_0031801 molecular_function obo:GO_0031801 GO:0031801 obo:GO_0031801 type 4 metabotropic glutamate receptor binding obo:GO_0031802 Interacting selectively and non-covalently with a type 5 metabotropic glutamate receptor. obo:GO_0031802 obo:go.owl obo:GO_0031802 type 5 metabotropic glutamate receptor ligand obo:GO_0031802 molecular_function obo:GO_0031802 GO:0031802 obo:GO_0031802 type 5 metabotropic glutamate receptor binding obo:GO_0031803 Interacting selectively and non-covalently with a type 6 metabotropic glutamate receptor. obo:GO_0031803 obo:go.owl obo:GO_0031803 type 6 metabotropic glutamate receptor ligand obo:GO_0031803 molecular_function obo:GO_0031803 GO:0031803 obo:GO_0031803 type 6 metabotropic glutamate receptor binding obo:GO_0031804 Interacting selectively and non-covalently with a type 7 metabotropic glutamate receptor. obo:GO_0031804 obo:go.owl obo:GO_0031804 type 7 metabotropic glutamate receptor ligand obo:GO_0031804 molecular_function obo:GO_0031804 GO:0031804 obo:GO_0031804 type 7 metabotropic glutamate receptor binding obo:GO_0031805 Interacting selectively and non-covalently with a type 8 metabotropic glutamate receptor. obo:GO_0031805 obo:go.owl obo:GO_0031805 type 8 metabotropic glutamate receptor ligand obo:GO_0031805 molecular_function obo:GO_0031805 GO:0031805 obo:GO_0031805 type 8 metabotropic glutamate receptor binding obo:GO_0031806 Interacting selectively and non-covalently with a G protein-coupled (metabotropic) histamine receptor. obo:GO_0031806 obo:go.owl obo:GO_0031806 G-protein coupled histamine receptor binding obo:GO_0031806 metabotropic histamine receptor binding obo:GO_0031806 metabotropic histamine receptor ligand obo:GO_0031806 molecular_function obo:GO_0031806 GO:0031806 obo:GO_0031806 G protein-coupled histamine receptor binding obo:GO_0031807 Interacting selectively and non-covalently with a H1 histamine receptor. obo:GO_0031807 obo:go.owl obo:GO_0031807 H1 histamine receptor ligand obo:GO_0031807 molecular_function obo:GO_0031807 GO:0031807 obo:GO_0031807 H1 histamine receptor binding obo:GO_0031808 Interacting selectively and non-covalently with a H2 histamine receptor. obo:GO_0031808 obo:go.owl obo:GO_0031808 H2 histamine receptor ligand obo:GO_0031808 molecular_function obo:GO_0031808 GO:0031808 obo:GO_0031808 H2 histamine receptor binding obo:GO_0031809 Interacting selectively and non-covalently with a H3 histamine receptor. obo:GO_0031809 obo:go.owl obo:GO_0031809 H3 histamine receptor ligand obo:GO_0031809 molecular_function obo:GO_0031809 GO:0031809 obo:GO_0031809 H3 histamine receptor binding obo:GO_0031810 Interacting selectively and non-covalently with a H4 histamine receptor. obo:GO_0031810 obo:go.owl obo:GO_0031810 H4 histamine receptor ligand obo:GO_0031810 molecular_function obo:GO_0031810 GO:0031810 obo:GO_0031810 H4 histamine receptor binding obo:GO_0031811 Interacting selectively and non-covalently with a G protein-coupled (metabotropic) nucleotide receptor. obo:GO_0031811 obo:go.owl obo:GO_0031811 G-protein coupled nucleotide receptor binding obo:GO_0031811 P2Y receptor binding obo:GO_0031811 metabotropic nucleotide receptor binding obo:GO_0031811 metabotropic nucleotide receptor ligand obo:GO_0031811 molecular_function obo:GO_0031811 GO:0031811 obo:GO_0031811 G protein-coupled nucleotide receptor binding obo:GO_0031812 Interacting selectively and non-covalently with a P2Y1 nucleotide receptor. obo:GO_0031812 obo:go.owl obo:GO_0031812 P2Y1 nucleotide receptor ligand obo:GO_0031812 molecular_function obo:GO_0031812 GO:0031812 obo:GO_0031812 P2Y1 nucleotide receptor binding obo:GO_0031813 Interacting selectively and non-covalently with a P2Y2 nucleotide receptor. obo:GO_0031813 obo:go.owl obo:GO_0031813 P2Y2 nucleotide receptor ligand obo:GO_0031813 molecular_function obo:GO_0031813 GO:0031813 obo:GO_0031813 P2Y2 nucleotide receptor binding obo:GO_0031814 Interacting selectively and non-covalently with a P2Y4 nucleotide receptor. obo:GO_0031814 obo:go.owl obo:GO_0031814 P2Y4 nucleotide receptor ligand obo:GO_0031814 molecular_function obo:GO_0031814 GO:0031814 obo:GO_0031814 P2Y4 nucleotide receptor binding obo:GO_0031815 Interacting selectively and non-covalently with a P2Y5 nucleotide receptor. obo:GO_0031815 obo:go.owl obo:GO_0031815 P2Y5 nucleotide receptor ligand obo:GO_0031815 molecular_function obo:GO_0031815 GO:0031815 obo:GO_0031815 P2Y5 nucleotide receptor binding obo:GO_0031816 Interacting selectively and non-covalently with a P2Y6 nucleotide receptor. obo:GO_0031816 obo:go.owl obo:GO_0031816 P2Y6 nucleotide receptor ligand obo:GO_0031816 molecular_function obo:GO_0031816 GO:0031816 obo:GO_0031816 P2Y6 nucleotide receptor binding obo:GO_0031817 Interacting selectively and non-covalently with a P2Y8 nucleotide receptor. obo:GO_0031817 obo:go.owl obo:GO_0031817 P2Y8 nucleotide receptor ligand obo:GO_0031817 molecular_function obo:GO_0031817 GO:0031817 obo:GO_0031817 P2Y8 nucleotide receptor binding obo:GO_0031818 Interacting selectively and non-covalently with a P2Y9 nucleotide receptor. obo:GO_0031818 obo:go.owl obo:GO_0031818 P2Y9 nucleotide receptor ligand obo:GO_0031818 molecular_function obo:GO_0031818 GO:0031818 obo:GO_0031818 P2Y9 nucleotide receptor binding obo:GO_0031819 Interacting selectively and non-covalently with a P2Y10 nucleotide receptor. obo:GO_0031819 obo:go.owl obo:GO_0031819 P2Y10 nucleotide receptor ligand obo:GO_0031819 molecular_function obo:GO_0031819 GO:0031819 obo:GO_0031819 P2Y10 nucleotide receptor binding obo:GO_0031820 Interacting selectively and non-covalently with a P2Y11 nucleotide receptor. obo:GO_0031820 obo:go.owl obo:GO_0031820 P2Y11 nucleotide receptor ligand obo:GO_0031820 molecular_function obo:GO_0031820 GO:0031820 obo:GO_0031820 P2Y11 nucleotide receptor binding obo:GO_0031821 Interacting selectively and non-covalently with a metabotropic serotonin receptor. obo:GO_0031821 obo:go.owl obo:GO_0031821 G-protein coupled serotonin receptor binding obo:GO_0031821 metabotropic 5-hydroxytryptamine receptor binding obo:GO_0031821 metabotropic serotonin receptor binding obo:GO_0031821 metabotropic serotonin receptor ligand obo:GO_0031821 molecular_function obo:GO_0031821 GO:0031821 obo:GO_0031821 G protein-coupled serotonin receptor binding obo:GO_0031822 Interacting selectively and non-covalently with a type 1B serotonin receptor. obo:GO_0031822 obo:go.owl obo:GO_0031822 5-hydroxytryptamine 1B receptor binding obo:GO_0031822 type 1B serotonin receptor ligand obo:GO_0031822 molecular_function obo:GO_0031822 GO:0031822 obo:GO_0031822 type 1B serotonin receptor binding obo:GO_0031823 Interacting selectively and non-covalently with a type 1D serotonin receptor. obo:GO_0031823 obo:go.owl obo:GO_0031823 5-hydroxytryptamine 1D receptor binding obo:GO_0031823 type 1D serotonin receptor ligand obo:GO_0031823 molecular_function obo:GO_0031823 GO:0031823 obo:GO_0031823 type 1D serotonin receptor binding obo:GO_0031824 Interacting selectively and non-covalently with a type 1E serotonin receptor. obo:GO_0031824 obo:go.owl obo:GO_0031824 5-hydroxytryptamine 1E receptor binding obo:GO_0031824 type 1E serotonin receptor ligand obo:GO_0031824 molecular_function obo:GO_0031824 GO:0031824 obo:GO_0031824 type 1E serotonin receptor binding obo:GO_0031825 Interacting selectively and non-covalently with a type 1F serotonin receptor. obo:GO_0031825 obo:go.owl obo:GO_0031825 5-hydroxytryptamine 1F receptor binding obo:GO_0031825 type 1F serotonin receptor ligand obo:GO_0031825 molecular_function obo:GO_0031825 GO:0031825 obo:GO_0031825 type 1F serotonin receptor binding obo:GO_0031826 Interacting selectively and non-covalently with a type 2A serotonin receptor. obo:GO_0031826 obo:go.owl obo:GO_0031826 5-hydroxytryptamine 2A receptor binding obo:GO_0031826 type 2A serotonin receptor ligand obo:GO_0031826 molecular_function obo:GO_0031826 GO:0031826 obo:GO_0031826 type 2A serotonin receptor binding obo:GO_0031827 Interacting selectively and non-covalently with a type 2B serotonin receptor. obo:GO_0031827 obo:go.owl obo:GO_0031827 5-hydroxytryptamine 2B receptor binding obo:GO_0031827 type 2B serotonin receptor ligand obo:GO_0031827 molecular_function obo:GO_0031827 GO:0031827 obo:GO_0031827 type 2B serotonin receptor binding obo:GO_0031828 Interacting selectively and non-covalently with a type 2C serotonin receptor. obo:GO_0031828 obo:go.owl obo:GO_0031828 5-hydroxytryptamine 2C receptor binding obo:GO_0031828 type 2C serotonin receptor ligand obo:GO_0031828 molecular_function obo:GO_0031828 GO:0031828 obo:GO_0031828 type 2C serotonin receptor binding obo:GO_0031829 Interacting selectively and non-covalently with a type 4 serotonin receptor. obo:GO_0031829 obo:go.owl obo:GO_0031829 5-hydroxytryptamine 4 receptor binding obo:GO_0031829 type 4 serotonin receptor ligand obo:GO_0031829 molecular_function obo:GO_0031829 GO:0031829 obo:GO_0031829 type 4 serotonin receptor binding obo:GO_0031830 Interacting selectively and non-covalently with a type 5A serotonin receptor. obo:GO_0031830 obo:go.owl obo:GO_0031830 5-hydroxytryptamine 5A receptor binding obo:GO_0031830 type 5A serotonin receptor ligand obo:GO_0031830 molecular_function obo:GO_0031830 GO:0031830 obo:GO_0031830 type 5A serotonin receptor binding obo:GO_0031831 Interacting selectively and non-covalently with a type 5B serotonin receptor. obo:GO_0031831 obo:go.owl obo:GO_0031831 5-hydroxytryptamine 5B receptor binding obo:GO_0031831 type 5B serotonin receptor ligand obo:GO_0031831 molecular_function obo:GO_0031831 GO:0031831 obo:GO_0031831 type 5B serotonin receptor binding obo:GO_0031832 Interacting selectively and non-covalently with a type 6 serotonin receptor. obo:GO_0031832 obo:go.owl obo:GO_0031832 5-hydroxytryptamine 6 receptor binding obo:GO_0031832 type 6 serotonin receptor ligand obo:GO_0031832 molecular_function obo:GO_0031832 GO:0031832 obo:GO_0031832 type 6 serotonin receptor binding obo:GO_0031833 Interacting selectively and non-covalently with a type 7 serotonin receptor. obo:GO_0031833 obo:go.owl obo:GO_0031833 5-hydroxytryptamine 7 receptor binding obo:GO_0031833 type 7 serotonin receptor ligand obo:GO_0031833 molecular_function obo:GO_0031833 GO:0031833 obo:GO_0031833 type 7 serotonin receptor binding obo:GO_0031834 Interacting selectively and non-covalently with a neurokinin receptor. obo:GO_0031834 obo:go.owl obo:GO_0031834 neurokinin receptor ligand obo:GO_0031834 molecular_function obo:GO_0031834 GO:0031834 obo:GO_0031834 neurokinin receptor binding obo:GO_0031835 Interacting selectively and non-covalently with a substance P receptor. obo:GO_0031835 obo:go.owl obo:GO_0031835 neurokinin-1 receptor binding obo:GO_0031835 substance P receptor ligand obo:GO_0031835 molecular_function obo:GO_0031835 GO:0031835 obo:GO_0031835 substance P receptor binding obo:GO_0031836 Interacting selectively and non-covalently with a neuromedin K receptor. obo:GO_0031836 obo:go.owl obo:GO_0031836 neurokinin-B receptor binding obo:GO_0031836 neuromedin K receptor ligand obo:GO_0031836 molecular_function obo:GO_0031836 GO:0031836 obo:GO_0031836 neuromedin K receptor binding obo:GO_0031837 Interacting selectively and non-covalently with a substance K receptor. obo:GO_0031837 obo:go.owl obo:GO_0031837 neurokinin-A receptor binding obo:GO_0031837 substance K receptor ligand obo:GO_0031837 molecular_function obo:GO_0031837 GO:0031837 obo:GO_0031837 substance K receptor binding obo:GO_0031839 Interacting selectively and non-covalently with a type 1 neuromedin U receptor. obo:GO_0031839 obo:go.owl obo:GO_0031839 type 1 neuromedin U receptor ligand obo:GO_0031839 molecular_function obo:GO_0031839 GO:0031839 obo:GO_0031839 type 1 neuromedin U receptor binding obo:GO_0031840 Interacting selectively and non-covalently with a type 2 neuromedin U receptor. obo:GO_0031840 obo:go.owl obo:GO_0031840 type 2 neuromedin U receptor ligand obo:GO_0031840 molecular_function obo:GO_0031840 GO:0031840 obo:GO_0031840 type 2 neuromedin U receptor binding obo:GO_0031841 Interacting selectively and non-covalently with a neuropeptide Y receptor. obo:GO_0031841 obo:go.owl obo:GO_0031841 NPY receptor binding obo:GO_0031841 neuropeptide Y receptor ligand obo:GO_0031841 molecular_function obo:GO_0031841 GO:0031841 obo:GO_0031841 neuropeptide Y receptor binding obo:GO_0031842 Interacting selectively and non-covalently with a type 1 neuropeptide Y receptor. obo:GO_0031842 obo:go.owl obo:GO_0031842 type 1 neuropeptide Y receptor ligand obo:GO_0031842 molecular_function obo:GO_0031842 GO:0031842 obo:GO_0031842 type 1 neuropeptide Y receptor binding obo:GO_0031843 Interacting selectively and non-covalently with a type 2 neuropeptide Y receptor. obo:GO_0031843 obo:go.owl obo:GO_0031843 type 2 neuropeptide Y receptor ligand obo:GO_0031843 molecular_function obo:GO_0031843 GO:0031843 obo:GO_0031843 type 2 neuropeptide Y receptor binding obo:GO_0031844 Interacting selectively and non-covalently with a type 4 neuropeptide Y receptor. obo:GO_0031844 obo:go.owl obo:GO_0031844 pancreatic polypeptide receptor binding obo:GO_0031844 type 4 neuropeptide Y receptor ligand obo:GO_0031844 molecular_function obo:GO_0031844 GO:0031844 obo:GO_0031844 type 4 neuropeptide Y receptor binding obo:GO_0031845 Interacting selectively and non-covalently with a type 5 neuropeptide Y receptor. obo:GO_0031845 obo:go.owl obo:GO_0031845 type 5 neuropeptide Y receptor ligand obo:GO_0031845 molecular_function obo:GO_0031845 GO:0031845 obo:GO_0031845 type 5 neuropeptide Y receptor binding obo:GO_0031846 Interacting selectively and non-covalently with a neurotensin receptor. obo:GO_0031846 obo:go.owl obo:GO_0031846 neurotensin receptor ligand obo:GO_0031846 molecular_function obo:GO_0031846 GO:0031846 obo:GO_0031846 neurotensin receptor binding obo:GO_0031847 Interacting selectively and non-covalently with a type 1 neurotensin receptor. obo:GO_0031847 obo:go.owl obo:GO_0031847 type 1 neurotensin receptor ligand obo:GO_0031847 molecular_function obo:GO_0031847 GO:0031847 obo:GO_0031847 type 1 neurotensin receptor binding obo:GO_0031849 Interacting selectively and non-covalently with an olfactory receptor. obo:GO_0031849 obo:go.owl obo:GO_0031849 olfactory receptor ligand obo:GO_0031849 molecular_function obo:GO_0031849 GO:0031849 obo:GO_0031849 olfactory receptor binding obo:GO_0031850 Interacting selectively and non-covalently with a delta-type opioid receptor. obo:GO_0031850 obo:go.owl obo:GO_0031850 delta-type opioid receptor ligand obo:GO_0031850 molecular_function obo:GO_0031850 enkephalin receptor binding obo:GO_0031850 GO:0031850 obo:GO_0031850 delta-type opioid receptor binding obo:GO_0031851 Interacting selectively and non-covalently with a kappa-type opioid receptor. obo:GO_0031851 obo:go.owl obo:GO_0031851 kappa-type opioid receptor ligand obo:GO_0031851 molecular_function obo:GO_0031851 dynorphin receptor binding obo:GO_0031851 GO:0031851 obo:GO_0031851 kappa-type opioid receptor binding obo:GO_0031852 Interacting selectively and non-covalently with a mu-type opioid receptor. obo:GO_0031852 obo:go.owl obo:GO_0031852 mu-type opioid receptor ligand obo:GO_0031852 molecular_function obo:GO_0031852 morphine receptor binding obo:GO_0031852 GO:0031852 obo:GO_0031852 mu-type opioid receptor binding obo:GO_0031853 Interacting selectively and non-covalently with a nociceptin receptor. obo:GO_0031853 obo:go.owl obo:GO_0031853 nociceptin receptor ligand obo:GO_0031853 molecular_function obo:GO_0031853 GO:0031853 obo:GO_0031853 nociceptin receptor binding obo:GO_0031854 Interacting selectively and non-covalently with an orexigenic neuropeptide QRFP receptor. obo:GO_0031854 obo:go.owl obo:GO_0031854 orexigenic neuropeptide QRFP receptor ligand obo:GO_0031854 molecular_function obo:GO_0031854 GO:0031854 obo:GO_0031854 orexigenic neuropeptide QRFP receptor binding obo:GO_0031855 Interacting selectively and non-covalently with an oxytocin receptor. obo:GO_0031855 obo:go.owl obo:GO_0031855 oxytocin receptor ligand obo:GO_0031855 molecular_function obo:GO_0031855 GO:0031855 obo:GO_0031855 oxytocin receptor binding obo:GO_0031856 Interacting selectively and non-covalently with a parathyroid hormone receptor. obo:GO_0031856 obo:go.owl obo:GO_0031856 parathyroid hormone receptor ligand obo:GO_0031856 molecular_function obo:GO_0031856 GO:0031856 obo:GO_0031856 parathyroid hormone receptor binding obo:GO_0031857 Interacting selectively and non-covalently with a type 1 parathyroid hormone receptor. obo:GO_0031857 obo:go.owl obo:GO_0031857 type 1 parathyroid hormone receptor ligand obo:GO_0031857 molecular_function obo:GO_0031857 GO:0031857 obo:GO_0031857 type 1 parathyroid hormone receptor binding obo:GO_0031858 Interacting selectively and non-covalently with a pituitary adenylate cyclase-activating polypeptide receptor. obo:GO_0031858 obo:go.owl obo:GO_0031858 PACAP receptor binding obo:GO_0031858 pituitary adenylate cyclase activating peptide receptor binding obo:GO_0031858 pituitary adenylate cyclase-activating peptide receptor ligand obo:GO_0031858 molecular_function obo:GO_0031858 GO:0031858 obo:GO_0031858 pituitary adenylate cyclase-activating polypeptide receptor binding obo:GO_0031859 Interacting selectively and non-covalently with a platelet activating factor receptor. obo:GO_0031859 obo:go.owl obo:GO_0031859 platelet activating factor receptor ligand obo:GO_0031859 molecular_function obo:GO_0031859 GO:0031859 obo:GO_0031859 platelet activating factor receptor binding obo:GO_0031861 Interacting selectively and non-covalently with a prolactin-releasing peptide receptor. obo:GO_0031861 obo:go.owl obo:GO_0031861 prolactin-releasing peptide receptor ligand obo:GO_0031861 molecular_function obo:GO_0031861 GO:0031861 obo:GO_0031861 prolactin-releasing peptide receptor binding obo:GO_0031862 Interacting selectively and non-covalently with a prostanoid receptor. obo:GO_0031862 obo:go.owl obo:GO_0031862 prostanoid receptor ligand obo:GO_0031862 molecular_function obo:GO_0031862 GO:0031862 obo:GO_0031862 prostanoid receptor binding obo:GO_0031863 Interacting selectively and non-covalently with a prostaglandin D2 receptor. obo:GO_0031863 obo:go.owl obo:GO_0031863 prostanoid DP receptor binding obo:GO_0031863 prostaglandin D2 receptor ligand obo:GO_0031863 molecular_function obo:GO_0031863 GO:0031863 obo:GO_0031863 prostaglandin D2 receptor binding obo:GO_0031864 Interacting selectively and non-covalently with an EP1 subtype prostaglandin E2 receptor. obo:GO_0031864 obo:go.owl obo:GO_0031864 prostanoid EP1 receptor binding obo:GO_0031864 EP1 subtype prostaglandin E2 receptor ligand obo:GO_0031864 molecular_function obo:GO_0031864 GO:0031864 obo:GO_0031864 EP1 subtype prostaglandin E2 receptor binding obo:GO_0031865 Interacting selectively and non-covalently with an EP2 subtype prostaglandin E2 receptor. obo:GO_0031865 obo:go.owl obo:GO_0031865 prostanoid EP2 receptor binding obo:GO_0031865 EP2 subtype prostaglandin E2 receptor ligand obo:GO_0031865 molecular_function obo:GO_0031865 GO:0031865 obo:GO_0031865 EP2 subtype prostaglandin E2 receptor binding obo:GO_0031866 Interacting selectively and non-covalently with an EP3 subtype prostaglandin E2 receptor. obo:GO_0031866 obo:go.owl obo:GO_0031866 prostanoid EP3 receptor binding obo:GO_0031866 EP3 subtype prostaglandin E2 receptor ligand obo:GO_0031866 molecular_function obo:GO_0031866 GO:0031866 obo:GO_0031866 EP3 subtype prostaglandin E2 receptor binding obo:GO_0031867 Interacting selectively and non-covalently with an EP4 subtype prostaglandin E2 receptor. obo:GO_0031867 obo:go.owl obo:GO_0031867 prostanoid EP4 receptor binding obo:GO_0031867 EP4 subtype prostaglandin E2 receptor ligand obo:GO_0031867 molecular_function obo:GO_0031867 GO:0031867 obo:GO_0031867 EP4 subtype prostaglandin E2 receptor binding obo:GO_0031868 Interacting selectively and non-covalently with a prostaglandin F2-alpha receptor. obo:GO_0031868 obo:go.owl obo:GO_0031868 prostanoid FP receptor binding obo:GO_0031868 prostaglandin F2-alpha receptor ligand obo:GO_0031868 molecular_function obo:GO_0031868 GO:0031868 obo:GO_0031868 prostaglandin F2-alpha receptor binding obo:GO_0031869 Interacting selectively and non-covalently with a prostacyclin receptor. obo:GO_0031869 obo:go.owl obo:GO_0031869 prostanoid IP receptor binding obo:GO_0031869 prostacyclin receptor ligand obo:GO_0031869 molecular_function obo:GO_0031869 GO:0031869 obo:GO_0031869 prostacyclin receptor binding obo:GO_0031870 Interacting selectively and non-covalently with a thromboxane A2 receptor. obo:GO_0031870 obo:go.owl obo:GO_0031870 prostanoid TP receptor binding obo:GO_0031870 thromboxane A2 receptor ligand obo:GO_0031870 molecular_function obo:GO_0031870 GO:0031870 obo:GO_0031870 thromboxane A2 receptor binding obo:GO_0031871 Interacting selectively and non-covalently with a proteinase activated receptor. obo:GO_0031871 obo:go.owl obo:GO_0031871 proteinase activated receptor ligand obo:GO_0031871 molecular_function obo:GO_0031871 GO:0031871 obo:GO_0031871 proteinase activated receptor binding obo:GO_0031872 Interacting selectively and non-covalently with a type 1 proteinase activated receptor. obo:GO_0031872 obo:go.owl obo:GO_0031872 thrombin receptor binding obo:GO_0031872 type 1 proteinase activated receptor ligand obo:GO_0031872 molecular_function obo:GO_0031872 GO:0031872 obo:GO_0031872 type 1 proteinase activated receptor binding obo:GO_0031873 Interacting selectively and non-covalently with a type 2 proteinase activated receptor. obo:GO_0031873 obo:go.owl obo:GO_0031873 type 2 proteinase activated receptor ligand obo:GO_0031873 molecular_function obo:GO_0031873 GO:0031873 obo:GO_0031873 type 2 proteinase activated receptor binding obo:GO_0031874 Interacting selectively and non-covalently with a type 3 proteinase activated receptor. obo:GO_0031874 obo:go.owl obo:GO_0031874 type 3 proteinase activated receptor ligand obo:GO_0031874 molecular_function obo:GO_0031874 GO:0031874 obo:GO_0031874 type 3 proteinase activated receptor binding obo:GO_0031875 Interacting selectively and non-covalently with a type 4 proteinase activated receptor. obo:GO_0031875 obo:go.owl obo:GO_0031875 type 4 proteinase activated receptor ligand obo:GO_0031875 molecular_function obo:GO_0031875 GO:0031875 obo:GO_0031875 type 4 proteinase activated receptor binding obo:GO_0031876 Interacting selectively and non-covalently with a secretin receptor. obo:GO_0031876 obo:go.owl obo:GO_0031876 secretin receptor ligand obo:GO_0031876 molecular_function obo:GO_0031876 GO:0031876 obo:GO_0031876 secretin receptor binding obo:GO_0031877 Interacting selectively and non-covalently with a somatostatin receptor. obo:GO_0031877 obo:go.owl obo:GO_0031877 somatostatin receptor ligand obo:GO_0031877 molecular_function obo:GO_0031877 GO:0031877 obo:GO_0031877 somatostatin receptor binding obo:GO_0031878 Interacting selectively and non-covalently with a type 1 somatostatin receptor. obo:GO_0031878 obo:go.owl obo:GO_0031878 type 1 somatostatin receptor ligand obo:GO_0031878 molecular_function obo:GO_0031878 GO:0031878 obo:GO_0031878 type 1 somatostatin receptor binding obo:GO_0031879 Interacting selectively and non-covalently with a type 2 somatostatin receptor. obo:GO_0031879 obo:go.owl obo:GO_0031879 type 2 somatostatin receptor ligand obo:GO_0031879 molecular_function obo:GO_0031879 GO:0031879 obo:GO_0031879 type 2 somatostatin receptor binding obo:GO_0031880 Interacting selectively and non-covalently with a type 3 somatostatin receptor. obo:GO_0031880 obo:go.owl obo:GO_0031880 type 3 somatostatin receptor ligand obo:GO_0031880 molecular_function obo:GO_0031880 GO:0031880 obo:GO_0031880 type 3 somatostatin receptor binding obo:GO_0031881 Interacting selectively and non-covalently with a type 4 somatostatin receptor. obo:GO_0031881 obo:go.owl obo:GO_0031881 type 4 somatostatin receptor ligand obo:GO_0031881 molecular_function obo:GO_0031881 GO:0031881 obo:GO_0031881 type 4 somatostatin receptor binding obo:GO_0031882 Interacting selectively and non-covalently with a type 5 somatostatin receptor. obo:GO_0031882 obo:go.owl obo:GO_0031882 type 5 somatostatin receptor ligand obo:GO_0031882 molecular_function obo:GO_0031882 GO:0031882 obo:GO_0031882 type 5 somatostatin receptor binding obo:GO_0031883 Interacting selectively and non-covalently with a taste receptor. obo:GO_0031883 obo:go.owl obo:GO_0031883 taste receptor ligand obo:GO_0031883 molecular_function obo:GO_0031883 GO:0031883 obo:GO_0031883 taste receptor binding obo:GO_0031884 Interacting selectively and non-covalently with a type 1 member 1 taste receptor. obo:GO_0031884 obo:go.owl obo:GO_0031884 type 1 member 1 taste receptor ligand obo:GO_0031884 molecular_function obo:GO_0031884 GO:0031884 obo:GO_0031884 type 1 member 1 taste receptor binding obo:GO_0031885 Interacting selectively and non-covalently with a type 1 member 2 taste receptor. obo:GO_0031885 obo:go.owl obo:GO_0031885 type 1 member 2 taste receptor ligand obo:GO_0031885 molecular_function obo:GO_0031885 GO:0031885 obo:GO_0031885 type 1 member 2 taste receptor binding obo:GO_0031886 Interacting selectively and non-covalently with a type 1 member 3 taste receptor. obo:GO_0031886 obo:go.owl obo:GO_0031886 sweet taste receptor binding obo:GO_0031886 type 1 member 3 taste receptor ligand obo:GO_0031886 molecular_function obo:GO_0031886 GO:0031886 obo:GO_0031886 type 1 member 3 taste receptor binding obo:GO_0031889 Interacting selectively and non-covalently with a urotensin receptor. obo:GO_0031889 obo:go.owl obo:GO_0031889 urotensin receptor ligand obo:GO_0031889 molecular_function obo:GO_0031889 GO:0031889 obo:GO_0031889 urotensin receptor binding obo:GO_0031890 Interacting selectively and non-covalently with a vasoactive intestinal polypeptide receptor. obo:GO_0031890 obo:go.owl obo:GO_0031890 VIP receptor binding obo:GO_0031890 vasoactive intestinal polypeptide receptor ligand obo:GO_0031890 molecular_function obo:GO_0031890 GO:0031890 obo:GO_0031890 vasoactive intestinal polypeptide receptor binding obo:GO_0031891 Interacting selectively and non-covalently with a type 1 vasoactive intestinal polypeptide receptor. obo:GO_0031891 obo:go.owl obo:GO_0031891 type 2 PACAP receptor binding obo:GO_0031891 type 1 vasoactive intestinal polypeptide receptor ligand obo:GO_0031891 molecular_function obo:GO_0031891 GO:0031891 obo:GO_0031891 type 1 vasoactive intestinal polypeptide receptor binding obo:GO_0031892 Interacting selectively and non-covalently with a type 2 vasoactive intestinal polypeptide receptor. obo:GO_0031892 obo:go.owl obo:GO_0031892 type 3 PACAP receptor binding obo:GO_0031892 type 2 vasoactive intestinal polypeptide receptor ligand obo:GO_0031892 molecular_function obo:GO_0031892 GO:0031892 obo:GO_0031892 type 2 vasoactive intestinal polypeptide receptor binding obo:GO_0031893 Interacting selectively and non-covalently with a vasopressin receptor. obo:GO_0031893 obo:go.owl obo:GO_0031893 vasopressin receptor ligand obo:GO_0031893 molecular_function obo:GO_0031893 GO:0031893 obo:GO_0031893 vasopressin receptor binding obo:GO_0031894 Interacting selectively and non-covalently with a V1A vasopressin receptor. obo:GO_0031894 obo:go.owl obo:GO_0031894 V1A vasopressin receptor ligand obo:GO_0031894 molecular_function obo:GO_0031894 GO:0031894 obo:GO_0031894 V1A vasopressin receptor binding obo:GO_0031895 Interacting selectively and non-covalently with a V1B vasopressin receptor. obo:GO_0031895 obo:go.owl obo:GO_0031895 V1B vasopressin receptor ligand obo:GO_0031895 molecular_function obo:GO_0031895 GO:0031895 obo:GO_0031895 V1B vasopressin receptor binding obo:GO_0031896 Interacting selectively and non-covalently with a V2 vasopressin receptor. obo:GO_0031896 obo:go.owl obo:GO_0031896 V2 vasopressin receptor ligand obo:GO_0031896 molecular_function obo:GO_0031896 GO:0031896 obo:GO_0031896 V2 vasopressin receptor binding obo:GO_0031961 Interacting selectively and non-covalently with a cortisol receptor. obo:GO_0031961 obo:go.owl obo:GO_0031961 molecular_function obo:GO_0031961 GO:0031961 obo:GO_0031961 cortisol receptor binding obo:GO_0031962 Interacting selectively and non-covalently with a mineralocorticoid receptor. obo:GO_0031962 obo:go.owl obo:GO_0031962 molecular_function obo:GO_0031962 GO:0031962 obo:GO_0031962 mineralocorticoid receptor binding obo:GO_0031994 Interacting selectively and non-covalently with insulin-like growth factor I. obo:GO_0031994 obo:go.owl obo:GO_0031994 IGF-I binding obo:GO_0031994 molecular_function obo:GO_0031994 GO:0031994 obo:GO_0031994 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0031994 insulin-like growth factor I binding obo:GO_0031995 Interacting selectively and non-covalently with insulin-like growth factor II. obo:GO_0031995 obo:go.owl obo:GO_0031995 IGF-II binding obo:GO_0031995 molecular_function obo:GO_0031995 GO:0031995 obo:GO_0031995 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0031995 insulin-like growth factor II binding obo:GO_0031996 Interacting selectively and non-covalently with any thioesterase enzyme. obo:GO_0031996 obo:go.owl obo:GO_0031996 thiolesterase binding obo:GO_0031996 molecular_function obo:GO_0031996 GO:0031996 obo:GO_0031996 thioesterase binding obo:GO_0031997 Interacting selectively and non-covalently with the N-terminus of a protein that has the potential to be, or has been, modified by N-terminal myristoylation. Binding affinity is typically altered by myristoylation; for example, N-terminal myristoylation of HIV Nef increases its affinity for calmodulin. obo:GO_0031997 obo:go.owl obo:GO_0031997 molecular_function obo:GO_0031997 GO:0031997 obo:GO_0031997 N-terminal myristoylation domain binding obo:GO_0032003 Interacting selectively and non-covalently with the interleukin-28 receptor. obo:GO_0032003 obo:go.owl obo:GO_0032003 IL-28 obo:GO_0032003 interleukin-28 receptor ligand obo:GO_0032003 molecular_function obo:GO_0032003 GO:0032003 obo:GO_0032003 interleukin-28 receptor binding obo:GO_0032027 Interacting selectively and non-covalently with a light chain of a myosin complex. obo:GO_0032027 obo:go.owl obo:GO_0032027 molecular_function obo:GO_0032027 GO:0032027 obo:GO_0032027 myosin light chain binding obo:GO_0032028 Interacting selectively and non-covalently with the head/neck region of a myosin heavy chain. obo:GO_0032028 obo:go.owl obo:GO_0032028 molecular_function obo:GO_0032028 GO:0032028 obo:GO_0032028 myosin head/neck binding obo:GO_0032029 Interacting selectively and non-covalently with the tail region of a myosin heavy chain. obo:GO_0032029 obo:go.owl obo:GO_0032029 molecular_function obo:GO_0032029 GO:0032029 obo:GO_0032029 myosin tail binding obo:GO_0032030 Interacting selectively and non-covalently with a light chain of a myosin I complex. obo:GO_0032030 obo:go.owl obo:GO_0032030 molecular_function obo:GO_0032030 GO:0032030 obo:GO_0032030 myosin I light chain binding obo:GO_0032031 Interacting selectively and non-covalently with the head/neck region of a myosin I heavy chain. obo:GO_0032031 obo:go.owl obo:GO_0032031 molecular_function obo:GO_0032031 GO:0032031 obo:GO_0032031 myosin I head/neck binding obo:GO_0032032 Interacting selectively and non-covalently with the tail region of a myosin I heavy chain. obo:GO_0032032 obo:go.owl obo:GO_0032032 molecular_function obo:GO_0032032 GO:0032032 obo:GO_0032032 myosin I tail binding obo:GO_0032033 Interacting selectively and non-covalently with a light chain of a myosin II complex. obo:GO_0032033 obo:go.owl obo:GO_0032033 molecular_function obo:GO_0032033 GO:0032033 obo:GO_0032033 myosin II light chain binding obo:GO_0032034 Interacting selectively and non-covalently with the head/neck region of a myosin II heavy chain. obo:GO_0032034 obo:go.owl obo:GO_0032034 molecular_function obo:GO_0032034 GO:0032034 obo:GO_0032034 myosin II head/neck binding obo:GO_0032035 Interacting selectively and non-covalently with the tail region of a myosin II heavy chain. obo:GO_0032035 obo:go.owl obo:GO_0032035 molecular_function obo:GO_0032035 GO:0032035 obo:GO_0032035 myosin II tail binding obo:GO_0032036 Interacting selectively and non-covalently with a heavy chain of a myosin complex. obo:GO_0032036 obo:go.owl obo:GO_0032036 molecular_function obo:GO_0032036 GO:0032036 obo:GO_0032036 myosin heavy chain binding obo:GO_0032037 Interacting selectively and non-covalently with a heavy chain of a myosin I complex. obo:GO_0032037 obo:go.owl obo:GO_0032037 molecular_function obo:GO_0032037 GO:0032037 obo:GO_0032037 myosin I heavy chain binding obo:GO_0032038 Interacting selectively and non-covalently with a heavy chain of a myosin II complex. obo:GO_0032038 obo:go.owl obo:GO_0032038 molecular_function obo:GO_0032038 GO:0032038 obo:GO_0032038 myosin II heavy chain binding obo:GO_0032042 The chemical reactions and pathways involving mitochondrial DNA. obo:GO_0032042 obo:go.owl obo:GO_0032042 mitochondrial DNA metabolism obo:GO_0032042 mtDNA metabolic process obo:GO_0032042 mtDNA metabolism obo:GO_0032042 biological_process obo:GO_0032042 GO:0032042 obo:GO_0032042 mitochondrial DNA metabolic process obo:GO_0032050 Interacting selectively and non-covalently with a clathrin heavy chain. obo:GO_0032050 obo:go.owl obo:GO_0032050 molecular_function obo:GO_0032050 GO:0032050 obo:GO_0032050 clathrin heavy chain binding obo:GO_0032051 Interacting selectively and non-covalently with a clathrin light chain. obo:GO_0032051 obo:go.owl obo:GO_0032051 molecular_function obo:GO_0032051 GO:0032051 obo:GO_0032051 clathrin light chain binding obo:GO_0032052 Interacting selectively and non-covalently with bile acids, any of a group of steroid carboxylic acids occurring in bile. obo:GO_0032052 obo:go.owl obo:GO_0032052 molecular_function obo:GO_0032052 GO:0032052 obo:GO_0032052 bile acid binding obo:GO_0032089 Interacting selectively and non-covalently with a NACHT (NAIP, CIITA, HET-E and TP1) domain. The NACHT domain consists of seven distinct conserved motifs, including an ATP/GTPase specific P-loop, a Mg(2+)-binding site and five more specific motifs. obo:GO_0032089 obo:go.owl obo:GO_0032089 molecular_function obo:GO_0032089 GO:0032089 obo:GO_0032089 NACHT domain binding obo:GO_0032090 Interacting selectively and non-covalently with a Pyrin (PAAD/DAPIN) domain, a protein-protein interaction domain that has the same fold as the Death domain. obo:GO_0032090 obo:go.owl obo:GO_0032090 DAPIN domain binding obo:GO_0032090 PAAD domain binding obo:GO_0032090 molecular_function obo:GO_0032090 GO:0032090 obo:GO_0032090 Pyrin domain binding obo:GO_0032093 Interacting selectively and non-covalently with a SAM (Sterile Alpha Motif) domain, which is a 70-amino acid protein sequence that participates in protein-protein, protein-lipid, and protein-RNA interactions and is conserved from lower to higher eukaryotes. obo:GO_0032093 obo:go.owl obo:GO_0032093 Sterile Alpha Motif domain binding obo:GO_0032093 molecular_function obo:GO_0032093 GO:0032093 obo:GO_0032093 SAM domain binding obo:GO_0032101 Any process that modulates the frequency, rate or extent of a response to an external stimulus. obo:GO_0032101 obo:go.owl obo:GO_0032101 biological_process obo:GO_0032101 GO:0032101 obo:GO_0032101 http://purl.oboInOwllibrary.org/oboInOwl/go#gocheck_do_not_manually_annotate obo:GO_0032101 Note that this term is in the subset of terms that should not be used for direct gene product annotation. Instead, select a child term or, if no appropriate child term exists, please request a new term. Direct annotations to this term may be amended during annotation QC. obo:GO_0032101 regulation of response to external stimulus obo:GO_0032102 Any process that stops, prevents, or reduces the frequency, rate or extent of a response to an external stimulus. obo:GO_0032102 obo:go.owl obo:GO_0032102 down regulation of response to external stimulus obo:GO_0032102 down-regulation of response to external stimulus obo:GO_0032102 downregulation of response to external stimulus obo:GO_0032102 inhibition of response to external stimulus obo:GO_0032102 biological_process obo:GO_0032102 GO:0032102 obo:GO_0032102 http://purl.oboInOwllibrary.org/oboInOwl/go#gocheck_do_not_manually_annotate obo:GO_0032102 Note that this term is in the subset of terms that should not be used for direct gene product annotation. Instead, select a child term or, if no appropriate child term exists, please request a new term. Direct annotations to this term may be amended during annotation QC. obo:GO_0032102 negative regulation of response to external stimulus obo:GO_0032103 Any process that activates, maintains or increases the rate of a response to an external stimulus. obo:GO_0032103 obo:go.owl obo:GO_0032103 up regulation of response to external stimulus obo:GO_0032103 up-regulation of response to external stimulus obo:GO_0032103 upregulation of response to external stimulus obo:GO_0032103 activation of response to external stimulus obo:GO_0032103 stimulation of response to external stimulus obo:GO_0032103 biological_process obo:GO_0032103 GO:0032103 obo:GO_0032103 http://purl.oboInOwllibrary.org/oboInOwl/go#gocheck_do_not_manually_annotate obo:GO_0032103 Note that this term is in the subset of terms that should not be used for direct gene product annotation. Instead, select a child term or, if no appropriate child term exists, please request a new term. Direct annotations to this term may be amended during annotation QC. obo:GO_0032103 positive regulation of response to external stimulus obo:GO_0032131 Interacting selectively and non-covalently with alkylated residues in DNA. obo:GO_0032131 obo:go.owl obo:GO_0032131 molecular_function obo:GO_0032131 GO:0032131 obo:GO_0032131 alkylated DNA binding obo:GO_0032132 Interacting selectively and non-covalently with O6-alkylguanine adducts in DNA. obo:GO_0032132 obo:go.owl obo:GO_0032132 molecular_function obo:GO_0032132 GO:0032132 obo:GO_0032132 O6-alkylguanine-DNA binding obo:GO_0032135 Interacting selectively and non-covalently with double-stranded DNA containing insertions or deletions. obo:GO_0032135 obo:go.owl obo:GO_0032135 insertion binding obo:GO_0032135 DNA insertion binding obo:GO_0032135 molecular_function obo:GO_0032135 GO:0032135 obo:GO_0032135 DNA insertion or deletion binding obo:GO_0032136 Interacting selectively and non-covalently with double-stranded DNA containing an A/C mispair. obo:GO_0032136 obo:go.owl obo:GO_0032136 A/C mispair binding obo:GO_0032136 C/A mispair binding obo:GO_0032136 molecular_function obo:GO_0032136 cytosine/adenine mispair binding obo:GO_0032136 GO:0032136 obo:GO_0032136 adenine/cytosine mispair binding obo:GO_0032137 Interacting selectively and non-covalently with double-stranded DNA containing a G/T mispair. obo:GO_0032137 obo:go.owl obo:GO_0032137 G/T mispair binding obo:GO_0032137 T/G mispair binding obo:GO_0032137 thymine/guanine mispair binding obo:GO_0032137 molecular_function obo:GO_0032137 GO:0032137 obo:GO_0032137 guanine/thymine mispair binding obo:GO_0032138 Interacting selectively and non-covalently with double-stranded DNA containing a single base insertion or deletion. obo:GO_0032138 obo:go.owl obo:GO_0032138 single base insertion binding obo:GO_0032138 molecular_function obo:GO_0032138 GO:0032138 obo:GO_0032138 single base insertion or deletion binding obo:GO_0032139 Interacting selectively and non-covalently with double-stranded DNA containing a dinucleotide insertion or deletion. obo:GO_0032139 obo:go.owl obo:GO_0032139 dinucleotide insertion binding obo:GO_0032139 molecular_function obo:GO_0032139 GO:0032139 obo:GO_0032139 dinucleotide insertion or deletion binding obo:GO_0032140 Interacting selectively and non-covalently with double-stranded DNA containing a single adenine insertion or a deletion that results in an unpaired adenine. obo:GO_0032140 obo:go.owl obo:GO_0032140 molecular_function obo:GO_0032140 GO:0032140 obo:GO_0032140 single adenine insertion binding obo:GO_0032141 Interacting selectively and non-covalently with double-stranded DNA containing a single cytosine insertion or a deletion that results in an unpaired cytosine. obo:GO_0032141 obo:go.owl obo:GO_0032141 molecular_function obo:GO_0032141 GO:0032141 obo:GO_0032141 single cytosine insertion binding obo:GO_0032142 Interacting selectively and non-covalently with double-stranded DNA containing a single guanine insertion or a deletion that results in an unpaired guanine. obo:GO_0032142 obo:go.owl obo:GO_0032142 molecular_function obo:GO_0032142 GO:0032142 obo:GO_0032142 single guanine insertion binding obo:GO_0032143 Interacting selectively and non-covalently with double-stranded DNA containing a single thymine insertion or a deletion that results in an unpaired thymine. obo:GO_0032143 obo:go.owl obo:GO_0032143 molecular_function obo:GO_0032143 GO:0032143 obo:GO_0032143 single thymine insertion binding obo:GO_0032145 Interacting selectively and non-covalently with succinate-semialdehyde dehydrogenase. obo:GO_0032145 obo:go.owl obo:GO_0032145 succinic semialdehyde dehydrogenase binding obo:GO_0032145 molecular_function obo:GO_0032145 GO:0032145 obo:GO_0032145 succinate-semialdehyde dehydrogenase binding obo:GO_0032181 Interacting selectively and non-covalently with double-stranded DNA containing a dinucleotide repeat insertion or a deletion resulting in unpaired dinucleotide repeats. obo:GO_0032181 obo:go.owl obo:GO_0032181 molecular_function obo:GO_0032181 GO:0032181 obo:GO_0032181 dinucleotide repeat insertion binding obo:GO_0032182 Interacting selectively and non-covalently with a small conjugating protein such as ubiquitin or a ubiquitin-like protein. obo:GO_0032182 obo:go.owl obo:GO_0032182 small conjugating protein binding obo:GO_0032182 molecular_function obo:GO_0032182 GO:0032182 obo:GO_0032182 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0032182 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0032182 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0032182 ubiquitin-like protein binding obo:GO_0032183 Interacting selectively and non-covalently with the small ubiquitin-like protein SUMO. obo:GO_0032183 obo:go.owl obo:GO_0032183 Smt3 monomer binding obo:GO_0032183 molecular_function obo:GO_0032183 Smt3 binding obo:GO_0032183 GO:0032183 obo:GO_0032183 SUMO binding obo:GO_0032184 Interacting selectively and non-covalently with a polymer of the small ubiquitin-like protein SUMO. obo:GO_0032184 obo:go.owl obo:GO_0032184 Smt3 polymer binding obo:GO_0032184 molecular_function obo:GO_0032184 GO:0032184 obo:GO_0032184 SUMO polymer binding obo:GO_0032190 Interacting selectively and non-covalently with acrosin, a protein that is found in the acrosomes of sperm and possesses protease and carbohydrate binding activities. obo:GO_0032190 obo:go.owl obo:GO_0032190 GO:0032191 obo:GO_0032190 GO:0032192 obo:GO_0032190 acrosin heavy chain binding obo:GO_0032190 acrosin light chain binding obo:GO_0032190 molecular_function obo:GO_0032190 GO:0032190 obo:GO_0032190 acrosin binding obo:GO_0032237 A process that initiates the activity of an inactive store-operated calcium channel. obo:GO_0032237 obo:go.owl obo:GO_0032237 biological_process obo:GO_0032237 GO:0032237 obo:GO_0032237 activation of store-operated calcium channel activity obo:GO_0032266 Interacting selectively and non-covalently with phosphatidylinositol-3-phosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3' position. obo:GO_0032266 obo:go.owl obo:GO_0032266 PtdIns-3-P binding obo:GO_0032266 phosphatidylinositol 3-phosphate binding obo:GO_0032266 molecular_function obo:GO_0032266 GO:0032266 obo:GO_0032266 phosphatidylinositol-3-phosphate binding obo:GO_0032356 Interacting selectively and non-covalently with oxidized residues in DNA. obo:GO_0032356 obo:go.owl obo:GO_0032356 oxidised DNA binding obo:GO_0032356 molecular_function obo:GO_0032356 GO:0032356 obo:GO_0032356 oxidized DNA binding obo:GO_0032357 Interacting selectively and non-covalently with oxidized purine residues in DNA. obo:GO_0032357 obo:go.owl obo:GO_0032357 oxidised purine DNA binding obo:GO_0032357 oxidized purine base DNA binding obo:GO_0032357 oxidized purine nucleobase DNA binding obo:GO_0032357 molecular_function obo:GO_0032357 GO:0032357 obo:GO_0032357 oxidized purine DNA binding obo:GO_0032358 Interacting selectively and non-covalently with oxidized pyrimidine residues in DNA. obo:GO_0032358 obo:go.owl obo:GO_0032358 oxidised pyrimidine DNA binding obo:GO_0032358 oxidized pyrimidine base DNA binding obo:GO_0032358 oxidized pyrimidine nucleobase DNA binding obo:GO_0032358 molecular_function obo:GO_0032358 GO:0032358 obo:GO_0032358 oxidized pyrimidine DNA binding obo:GO_0032386 Any process that modulates the frequency, rate or extent of the directed movement of substances within cells. obo:GO_0032386 obo:go.owl obo:GO_0032386 biological_process obo:GO_0032386 GO:0032386 obo:GO_0032386 regulation of intracellular transport obo:GO_0032387 Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of substances within cells. obo:GO_0032387 obo:go.owl obo:GO_0032387 down regulation of intracellular transport obo:GO_0032387 down-regulation of intracellular transport obo:GO_0032387 downregulation of intracellular transport obo:GO_0032387 inhibition of intracellular transport obo:GO_0032387 biological_process obo:GO_0032387 GO:0032387 obo:GO_0032387 negative regulation of intracellular transport obo:GO_0032388 Any process that activates or increases the frequency, rate or extent of the directed movement of substances within cells. obo:GO_0032388 obo:go.owl obo:GO_0032388 up regulation of intracellular transport obo:GO_0032388 up-regulation of intracellular transport obo:GO_0032388 upregulation of intracellular transport obo:GO_0032388 activation of intracellular transport obo:GO_0032388 stimulation of intracellular transport obo:GO_0032388 biological_process obo:GO_0032388 GO:0032388 obo:GO_0032388 positive regulation of intracellular transport obo:GO_0032399 Interacting selectively and non-covalently with a HECT, 'Homologous to the E6-AP Carboxy-Terminus', domain of a protein. obo:GO_0032399 obo:go.owl obo:GO_0032399 molecular_function obo:GO_0032399 GO:0032399 obo:GO_0032399 HECT domain binding obo:GO_0032404 Interacting selectively and non-covalently with a mismatch repair complex. obo:GO_0032404 obo:go.owl obo:GO_0032404 molecular_function obo:GO_0032404 GO:0032404 obo:GO_0032404 mismatch repair complex binding obo:GO_0032405 Interacting selectively and non-covalently with the mismatch repair complex MutLalpha. obo:GO_0032405 obo:go.owl obo:GO_0032405 molecular_function obo:GO_0032405 GO:0032405 obo:GO_0032405 MutLalpha complex binding obo:GO_0032406 Interacting selectively and non-covalently with the mismatch repair complex MutLbeta. obo:GO_0032406 obo:go.owl obo:GO_0032406 molecular_function obo:GO_0032406 GO:0032406 obo:GO_0032406 MutLbeta complex binding obo:GO_0032407 Interacting selectively and non-covalently with the mismatch repair complex MutSalpha. obo:GO_0032407 obo:go.owl obo:GO_0032407 molecular_function obo:GO_0032407 GO:0032407 obo:GO_0032407 MutSalpha complex binding obo:GO_0032408 Interacting selectively and non-covalently with the mismatch repair complex MutSbeta. obo:GO_0032408 obo:go.owl obo:GO_0032408 molecular_function obo:GO_0032408 GO:0032408 obo:GO_0032408 MutSbeta complex binding obo:GO_0032410 Any process that stops or reduces the activity of a transporter. obo:GO_0032410 obo:go.owl obo:GO_0032410 down regulation of transporter activity obo:GO_0032410 down-regulation of transporter activity obo:GO_0032410 downregulation of transporter activity obo:GO_0032410 inhibition of transporter activity obo:GO_0032410 biological_process obo:GO_0032410 GO:0032410 obo:GO_0032410 negative regulation of transporter activity obo:GO_0032411 Any process that activates or increases the activity of a transporter. obo:GO_0032411 obo:go.owl obo:GO_0032411 up regulation of transporter activity obo:GO_0032411 up-regulation of transporter activity obo:GO_0032411 upregulation of transporter activity obo:GO_0032411 activation of transporter activity obo:GO_0032411 stimulation of transporter activity obo:GO_0032411 biological_process obo:GO_0032411 GO:0032411 obo:GO_0032411 positive regulation of transporter activity obo:GO_0032412 Any process that modulates the activity of an ion transporter. obo:GO_0032412 obo:go.owl obo:GO_0032412 regulation of ion transporter activity obo:GO_0032412 biological_process obo:GO_0032412 GO:0032412 obo:GO_0032412 regulation of ion transmembrane transporter activity obo:GO_0032413 Any process that stops or reduces the activity of an ion transporter. obo:GO_0032413 obo:go.owl obo:GO_0032413 down regulation of ion transporter activity obo:GO_0032413 down-regulation of ion transporter activity obo:GO_0032413 downregulation of ion transporter activity obo:GO_0032413 negative regulation of ion transporter activity obo:GO_0032413 inhibition of ion transporter activity obo:GO_0032413 biological_process obo:GO_0032413 GO:0032413 obo:GO_0032413 negative regulation of ion transmembrane transporter activity obo:GO_0032414 Any process that activates or increases the activity of an ion transporter. obo:GO_0032414 obo:go.owl obo:GO_0032414 positive regulation of ion transporter activity obo:GO_0032414 up regulation of ion transporter activity obo:GO_0032414 up-regulation of ion transporter activity obo:GO_0032414 upregulation of ion transporter activity obo:GO_0032414 activation of ion transporter activity obo:GO_0032414 stimulation of ion transporter activity obo:GO_0032414 biological_process obo:GO_0032414 GO:0032414 obo:GO_0032414 positive regulation of ion transmembrane transporter activity obo:GO_0032415 Any process that modulates the activity of a sodium:hydrogen antiporter, which catalyzes the reaction: Na+(out) + H+(in) = Na+(in) + H+(out). obo:GO_0032415 obo:go.owl obo:GO_0032415 regulation of sodium:hydrogen antiporter activity obo:GO_0032415 biological_process obo:GO_0032415 GO:0032415 obo:GO_0032415 regulation of sodium:proton antiporter activity obo:GO_0032416 Any process that stops or reduces the activity of a sodium:hydrogen antiporter, which catalyzes the reaction: Na+(out) + H+(in) = Na+(in) + H+(out). obo:GO_0032416 obo:go.owl obo:GO_0032416 down regulation of sodium:hydrogen antiporter activity obo:GO_0032416 down-regulation of sodium:hydrogen antiporter activity obo:GO_0032416 downregulation of sodium:hydrogen antiporter activity obo:GO_0032416 negative regulation of sodium:hydrogen antiporter activity obo:GO_0032416 inhibition of sodium:hydrogen antiporter activity obo:GO_0032416 biological_process obo:GO_0032416 GO:0032416 obo:GO_0032416 negative regulation of sodium:proton antiporter activity obo:GO_0032417 Any process that activates or increases the activity of a sodium:hydrogen antiporter, which catalyzes the reaction: Na+(out) + H+(in) = Na+(in) + H+(out). obo:GO_0032417 obo:go.owl obo:GO_0032417 positive regulation of sodium:hydrogen antiporter activity obo:GO_0032417 up regulation of sodium:hydrogen antiporter activity obo:GO_0032417 up-regulation of sodium:hydrogen antiporter activity obo:GO_0032417 upregulation of sodium:hydrogen antiporter activity obo:GO_0032417 activation of sodium:hydrogen antiporter activity obo:GO_0032417 stimulation of sodium:hydrogen antiporter activity obo:GO_0032417 biological_process obo:GO_0032417 GO:0032417 obo:GO_0032417 positive regulation of sodium:proton antiporter activity obo:GO_0032422 Interacting selectively and non-covalently with a 30-bp purine-rich negative regulatory element; the best characterized such element is found in the first intronic region of the rat cardiac alpha-myosin heavy chain gene, and contains two palindromic high-affinity Ets-binding sites (CTTCCCTGGAAG). The presence of this element restricts expression of the gene containing it to cardiac myocytes. obo:GO_0032422 obo:go.owl obo:GO_0032422 PNR element binding obo:GO_0032422 molecular_function obo:GO_0032422 GO:0032422 obo:GO_0032422 purine-rich negative regulatory element binding obo:GO_0032427 Interacting selectively and non-covalently with the GTPase protein binding domain (GDB) domain of a protein. The GBD is a short motif, including a minimum region of 16 amino acids, identified in proteins that bind to small GTPases such as Cdc42 and Rac. obo:GO_0032427 obo:go.owl obo:GO_0032427 CRIB motif binding obo:GO_0032427 Cdc42/Rac interactive binding motif binding obo:GO_0032427 P21-Rho-binding domain binding obo:GO_0032427 PMD binding obo:GO_0032427 molecular_function obo:GO_0032427 GO:0032427 obo:GO_0032427 GBD domain binding obo:GO_0032448 Interacting selectively and non-covalently with DNA containing a hairpin. A hairpin structure forms when a DNA strand folds back on itself and intrachain base pairing occurs between inverted repeat sequences. obo:GO_0032448 obo:go.owl obo:GO_0032448 molecular_function obo:GO_0032448 GO:0032448 obo:GO_0032448 DNA hairpin binding obo:GO_0032472 The directed movement of calcium ions (Ca2+) into, out of or within the Golgi apparatus. obo:GO_0032472 obo:go.owl obo:GO_0032472 Golgi calcium transport obo:GO_0032472 biological_process obo:GO_0032472 GO:0032472 obo:GO_0032472 Golgi calcium ion transport obo:GO_0032490 The series of events in which a stimulus from a molecule of bacterial origin is received and converted into a molecular signal. obo:GO_0032490 obo:go.owl obo:GO_0032490 detection of bacteria associated molecule obo:GO_0032490 detection of bacterial associated molecule obo:GO_0032490 detection of bacterium associated molecule obo:GO_0032490 biological_process obo:GO_0032490 GO:0032490 obo:GO_0032490 detection of molecule of bacterial origin obo:GO_0032491 The series of events in which a stimulus from a molecule of fungal origin is received and converted into a molecular signal. obo:GO_0032491 obo:go.owl obo:GO_0032491 detection of fungal associated molecule obo:GO_0032491 detection of fungus associated molecule obo:GO_0032491 biological_process obo:GO_0032491 GO:0032491 obo:GO_0032491 detection of molecule of fungal origin obo:GO_0032492 The series of events in which a stimulus from a molecule of oomycetes origin is received and converted into a molecular signal. obo:GO_0032492 obo:go.owl obo:GO_0032492 detection of oomycetes associated molecule obo:GO_0032492 biological_process obo:GO_0032492 GO:0032492 obo:GO_0032492 detection of molecule of oomycetes origin obo:GO_0032493 Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a bacterial lipoprotein stimulus. obo:GO_0032493 obo:go.owl obo:GO_0032493 biological_process obo:GO_0032493 GO:0032493 obo:GO_0032493 response to bacterial lipoprotein obo:GO_0032496 Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a lipopolysaccharide stimulus; lipopolysaccharide is a major component of the cell wall of gram-negative bacteria. obo:GO_0032496 obo:go.owl obo:GO_0032496 response to endotoxin obo:GO_0032496 response to LPS obo:GO_0032496 biological_process obo:GO_0032496 GO:0032496 obo:GO_0032496 response to lipopolysaccharide obo:GO_0032497 The series of events in which a lipopolysaccharide stimulus is received by a cell and converted into a molecular signal. Lipopolysaccharide is a major component of the cell wall of gram-negative bacteria. obo:GO_0032497 obo:go.owl obo:GO_0032497 detection of LPS obo:GO_0032497 biological_process obo:GO_0032497 GO:0032497 obo:GO_0032497 detection of lipopolysaccharide obo:GO_0032500 Interacting selectively and non-covalently, in a non-covalent manner, with muramyl dipeptide; muramyl dipeptide is derived from peptidoglycan. obo:GO_0032500 obo:go.owl obo:GO_0032500 molecular_function obo:GO_0032500 GO:0032500 obo:GO_0032500 muramyl dipeptide binding obo:GO_0032535 A process that modulates the size of a cellular component. obo:GO_0032535 obo:go.owl obo:GO_0032535 biological_process obo:GO_0032535 GO:0032535 obo:GO_0032535 regulation of cellular component size obo:GO_0032546 Interacting selectively and non-covalently with a deoxyribonucleoside, a compound consisting of a purine or pyrimidine nitrogenous base linked to deoxyribose. obo:GO_0032546 obo:go.owl obo:GO_0032546 molecular_function obo:GO_0032546 GO:0032546 obo:GO_0032546 deoxyribonucleoside binding obo:GO_0032547 Interacting selectively and non-covalently with a purine deoxyribonucleoside, a compound consisting of a purine base linked to deoxyribose. obo:GO_0032547 obo:go.owl obo:GO_0032547 molecular_function obo:GO_0032547 GO:0032547 obo:GO_0032547 purine deoxyribonucleoside binding obo:GO_0032548 Interacting selectively and non-covalently with a pyrimidine deoxyribonucleoside, a compound consisting of a pyrimidine base linked to deoxyribose. obo:GO_0032548 obo:go.owl obo:GO_0032548 molecular_function obo:GO_0032548 GO:0032548 obo:GO_0032548 pyrimidine deoxyribonucleoside binding obo:GO_0032549 Interacting selectively and non-covalently with a ribonucleoside, a compound consisting of a purine or pyrimidine nitrogenous base linked to ribose. obo:GO_0032549 obo:go.owl obo:GO_0032549 molecular_function obo:GO_0032549 GO:0032549 obo:GO_0032549 ribonucleoside binding obo:GO_0032550 Interacting selectively and non-covalently with a purine ribonucleoside, a compound consisting of a purine base linked to ribose. obo:GO_0032550 obo:go.owl obo:GO_0032550 molecular_function obo:GO_0032550 GO:0032550 obo:GO_0032550 purine ribonucleoside binding obo:GO_0032551 Interacting selectively and non-covalently with a pyrimidine ribonucleoside, a compound consisting of a pyrimidine base linked to ribose. obo:GO_0032551 obo:go.owl obo:GO_0032551 molecular_function obo:GO_0032551 GO:0032551 obo:GO_0032551 pyrimidine ribonucleoside binding obo:GO_0032552 Interacting selectively and non-covalently with a deoxyribonucleotide, any compound consisting of a deoxyribonucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the deoxyribose moiety. obo:GO_0032552 obo:go.owl obo:GO_0032552 molecular_function obo:GO_0032552 GO:0032552 obo:GO_0032552 deoxyribonucleotide binding obo:GO_0032553 Interacting selectively and non-covalently with a ribonucleotide, any compound consisting of a ribonucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose moiety. obo:GO_0032553 obo:go.owl obo:GO_0032553 molecular_function obo:GO_0032553 GO:0032553 obo:GO_0032553 ribonucleotide binding obo:GO_0032554 Interacting selectively and non-covalently with a purine deoxyribonucleotide, any compound consisting of a purine deoxyribonucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the deoxyribose moiety. obo:GO_0032554 obo:go.owl obo:GO_0032554 molecular_function obo:GO_0032554 GO:0032554 obo:GO_0032554 purine deoxyribonucleotide binding obo:GO_0032555 Interacting selectively and non-covalently with a purine ribonucleotide, any compound consisting of a purine ribonucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose moiety. obo:GO_0032555 obo:go.owl obo:GO_0032555 molecular_function obo:GO_0032555 GO:0032555 obo:GO_0032555 purine ribonucleotide binding obo:GO_0032556 Interacting selectively and non-covalently with a pyrimidine deoxyribonucleotide, any compound consisting of a pyrimidine deoxyribonucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the deoxyribose moiety. obo:GO_0032556 obo:go.owl obo:GO_0032556 molecular_function obo:GO_0032556 GO:0032556 obo:GO_0032556 pyrimidine deoxyribonucleotide binding obo:GO_0032557 Interacting selectively and non-covalently with a pyrimidine ribonucleotide, any compound consisting of a pyrimidine ribonucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose moiety. obo:GO_0032557 obo:go.owl obo:GO_0032557 molecular_function obo:GO_0032557 GO:0032557 obo:GO_0032557 pyrimidine ribonucleotide binding obo:GO_0032558 Interacting selectively and non-covalently with an adenyl deoxyribonucleotide, any compound consisting of adenosine esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the deoxyribose moiety. obo:GO_0032558 obo:go.owl obo:GO_0032558 molecular_function obo:GO_0032558 GO:0032558 obo:GO_0032558 adenyl deoxyribonucleotide binding obo:GO_0032559 Interacting selectively and non-covalently with an adenyl ribonucleotide, any compound consisting of adenosine esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose moiety. obo:GO_0032559 obo:go.owl obo:GO_0032559 molecular_function obo:GO_0032559 GO:0032559 obo:GO_0032559 adenyl ribonucleotide binding obo:GO_0032560 Interacting selectively and non-covalently with a guanyl deoxyribonucleotide, any compound consisting of guanosine esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the deoxyribose moiety. obo:GO_0032560 obo:go.owl obo:GO_0032560 molecular_function obo:GO_0032560 GO:0032560 obo:GO_0032560 guanyl deoxyribonucleotide binding obo:GO_0032561 Interacting selectively and non-covalently with a guanyl ribonucleotide, any compound consisting of guanosine esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose moiety. obo:GO_0032561 obo:go.owl obo:GO_0032561 molecular_function obo:GO_0032561 GO:0032561 obo:GO_0032561 guanyl ribonucleotide binding obo:GO_0032562 Interacting selectively and non-covalently with dAMP, deoxyadenosine monophosphate. obo:GO_0032562 obo:go.owl obo:GO_0032562 molecular_function obo:GO_0032562 GO:0032562 obo:GO_0032562 dAMP binding obo:GO_0032563 Interacting selectively and non-covalently with dADP, deoxyadenosine diphosphate. obo:GO_0032563 obo:go.owl obo:GO_0032563 molecular_function obo:GO_0032563 GO:0032563 obo:GO_0032563 dADP binding obo:GO_0032564 Interacting selectively and non-covalently with dATP, deoxyadenosine triphosphate. obo:GO_0032564 obo:go.owl obo:GO_0032564 molecular_function obo:GO_0032564 GO:0032564 obo:GO_0032564 dATP binding obo:GO_0032565 Interacting selectively and non-covalently with dGMP, deoxyguanosine monophosphate. obo:GO_0032565 obo:go.owl obo:GO_0032565 molecular_function obo:GO_0032565 GO:0032565 obo:GO_0032565 dGMP binding obo:GO_0032566 Interacting selectively and non-covalently with dGDP, deoxyguanosine diphosphate. obo:GO_0032566 obo:go.owl obo:GO_0032566 molecular_function obo:GO_0032566 GO:0032566 obo:GO_0032566 dGDP binding obo:GO_0032567 Interacting selectively and non-covalently with dGTP, deoxyguanosine triphosphate. obo:GO_0032567 obo:go.owl obo:GO_0032567 molecular_function obo:GO_0032567 GO:0032567 obo:GO_0032567 dGTP binding obo:GO_0032571 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a vitamin K stimulus. obo:GO_0032571 obo:go.owl obo:GO_0032571 biological_process obo:GO_0032571 GO:0032571 obo:GO_0032571 response to vitamin K obo:GO_0032767 Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules), in the presence of copper. obo:GO_0032767 obo:go.owl obo:GO_0032767 molecular_function obo:GO_0032767 GO:0032767 obo:GO_0032767 copper-dependent protein binding obo:GO_0032791 Interacting selectively and non-covalently with lead (Pb) ions. obo:GO_0032791 obo:go.owl obo:GO_0032791 molecular_function obo:GO_0032791 GO:0032791 obo:GO_0032791 lead ion binding obo:GO_0032794 Interacting selectively and non-covalently with a GTPase activating protein. obo:GO_0032794 obo:go.owl obo:GO_0032794 GAP binding obo:GO_0032794 molecular_function obo:GO_0032794 GO:0032794 obo:GO_0032794 GTPase activating protein binding obo:GO_0032795 Interacting selectively and non-covalently with a heterotrimeric G-protein. obo:GO_0032795 obo:go.owl obo:GO_0032795 molecular_function obo:GO_0032795 GO:0032795 obo:GO_0032795 heterotrimeric G-protein binding obo:GO_0032810 Interacting selectively and non-covalently with the sterol response element (SRE), a nonpalindromic sequence found in the promoters of genes involved in lipid metabolism. obo:GO_0032810 obo:go.owl obo:GO_0032810 SRE binding obo:GO_0032810 molecular_function obo:GO_0032810 GO:0032810 obo:GO_0032810 Note that as agreed during the transcription overhaul, terms specifying binding to specific transcription regulatory motifs are no longer being created. The level of specificity GO has decided to go to is the "core promoter", "core promoter proximal region" and "enhancer". To capture more detail, please consider using column 16. obo:GO_0032810 sterol response element binding obo:GO_0032813 Interacting selectively and non-covalently with any member of the tumor necrosis factor receptor superfamily. obo:GO_0032813 obo:go.owl obo:GO_0032813 TNF receptor superfamily binding obo:GO_0032813 molecular_function obo:GO_0032813 GO:0032813 obo:GO_0032813 tumor necrosis factor receptor superfamily binding obo:GO_0032840 Interacting selectively and non-covalently with a proline-rich region within the same polypeptide. obo:GO_0032840 obo:go.owl obo:GO_0032840 intramolecular proline-rich region binding obo:GO_0032840 molecular_function obo:GO_0032840 GO:0032840 obo:GO_0032840 intramolecular proline-rich ligand binding obo:GO_0032841 Interacting selectively and non-covalently with calcitonin, a peptide hormone responsible for reducing serum calcium levels by inhibiting osteoclastic bone reabsorption and promoting renal calcium excretion. It is synthesized and released by the C cells of the thyroid. obo:GO_0032841 obo:go.owl obo:GO_0032841 molecular_function obo:GO_0032841 GO:0032841 obo:GO_0032841 calcitonin binding obo:GO_0032879 Any process that modulates the frequency, rate or extent of any process in which a cell, a substance, or a cellular entity is transported to, or maintained in, a specific location. obo:GO_0032879 obo:go.owl obo:GO_0032879 regulation of localisation obo:GO_0032879 biological_process obo:GO_0032879 GO:0032879 obo:GO_0032879 regulation of localization obo:GO_0032880 Any process that modulates the frequency, rate or extent of any process in which a protein is transported to, or maintained in, a specific location. obo:GO_0032880 obo:go.owl obo:GO_0032880 regulation of protein localisation obo:GO_0032880 biological_process obo:GO_0032880 GO:0032880 obo:GO_0032880 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0032880 regulation of protein localization obo:GO_0032890 Any process that modulates the frequency, rate or extent of the directed movement of organic acids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0032890 obo:go.owl obo:GO_0032890 biological_process obo:GO_0032890 GO:0032890 obo:GO_0032890 regulation of organic acid transport obo:GO_0032891 Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of organic acids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0032891 obo:go.owl obo:GO_0032891 down regulation of organic acid transport obo:GO_0032891 down-regulation of organic acid transport obo:GO_0032891 downregulation of organic acid transport obo:GO_0032891 inhibition of organic acid transport obo:GO_0032891 biological_process obo:GO_0032891 GO:0032891 obo:GO_0032891 negative regulation of organic acid transport obo:GO_0032892 Any process that activates or increases the frequency, rate or extent of the directed movement of organic acids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0032892 obo:go.owl obo:GO_0032892 up regulation of organic acid transport obo:GO_0032892 up-regulation of organic acid transport obo:GO_0032892 upregulation of organic acid transport obo:GO_0032892 activation of organic acid transport obo:GO_0032892 stimulation of organic acid transport obo:GO_0032892 biological_process obo:GO_0032892 GO:0032892 obo:GO_0032892 positive regulation of organic acid transport obo:GO_0032934 Interacting selectively and non-covalently with a sterol, any steroid containing a hydroxy group in the 3 position, closely related to cholestan-3-ol. obo:GO_0032934 obo:go.owl obo:GO_0032934 GO:0005498 obo:GO_0032934 molecular_function obo:GO_0032934 sterol carrier activity obo:GO_0032934 GO:0032934 obo:GO_0032934 sterol binding obo:GO_0032935 Interacting selectively and non-covalently with and responding, e.g. by conformational change, to changes in the cellular level of a sterol. obo:GO_0032935 obo:go.owl obo:GO_0032935 sterol-sensing domain obo:GO_0032935 molecular_function obo:GO_0032935 GO:0032935 obo:GO_0032935 sterol sensor activity obo:GO_0032944 Any process that modulates the frequency, rate or extent of mononuclear cell proliferation. obo:GO_0032944 obo:go.owl obo:GO_0032944 regulation of PBMC proliferation obo:GO_0032944 regulation of peripheral blood mononuclear cell proliferation obo:GO_0032944 biological_process obo:GO_0032944 GO:0032944 obo:GO_0032944 regulation of mononuclear cell proliferation obo:GO_0032945 Any process that stops, prevents, or reduces the frequency, rate or extent of mononuclear cell proliferation. obo:GO_0032945 obo:go.owl obo:GO_0032945 negative regulation of PBMC proliferation obo:GO_0032945 negative regulation of peripheral blood mononuclear cell proliferation obo:GO_0032945 biological_process obo:GO_0032945 GO:0032945 obo:GO_0032945 negative regulation of mononuclear cell proliferation obo:GO_0032946 Any process that activates or increases the frequency, rate or extent of mononuclear cell proliferation. obo:GO_0032946 obo:go.owl obo:GO_0032946 up regulation of mononuclear cell proliferation obo:GO_0032946 up-regulation of mononuclear cell proliferation obo:GO_0032946 upregulation of mononuclear cell proliferation obo:GO_0032946 activation of mononuclear cell proliferation obo:GO_0032946 positive regulation of PBMC proliferation obo:GO_0032946 positive regulation of peripheral blood mononuclear cell proliferation obo:GO_0032946 stimulation of mononuclear cell proliferation obo:GO_0032946 biological_process obo:GO_0032946 GO:0032946 obo:GO_0032946 positive regulation of mononuclear cell proliferation obo:GO_0033130 Interacting selectively and non-covalently with an acetylcholine receptor. obo:GO_0033130 obo:go.owl obo:GO_0033130 molecular_function obo:GO_0033130 GO:0033130 obo:GO_0033130 acetylcholine receptor binding obo:GO_0033134 Interacting selectively and non-covalently with a ubiquitin activating enzyme, any of the E1 proteins. obo:GO_0033134 obo:go.owl obo:GO_0033134 molecular_function obo:GO_0033134 GO:0033134 obo:GO_0033134 ubiquitin activating enzyme binding obo:GO_0033142 Interacting selectively and non-covalently with a progesterone receptor. obo:GO_0033142 obo:go.owl obo:GO_0033142 molecular_function obo:GO_0033142 GO:0033142 obo:GO_0033142 progesterone receptor binding obo:GO_0033149 Interacting selectively and non-covalently with the FFAT motif, a short motif containing diphenylalanine in an acidic tract that targets proteins to the cytosolic surface of the ER and to the nuclear membrane by binding directly to members of the VAP (VAMP-associated protein) protein family. obo:GO_0033149 obo:go.owl obo:GO_0033149 molecular_function obo:GO_0033149 GO:0033149 obo:GO_0033149 FFAT motif binding obo:GO_0033161 Interacting selectively and non-covalently with a mitogen-activated protein kinase kinase kinase kinase, any protein that can phosphorylate a MAP kinase kinase kinase. obo:GO_0033161 obo:go.owl obo:GO_0033161 MAPKKKK binding obo:GO_0033161 molecular_function obo:GO_0033161 GO:0033161 obo:GO_0033161 mitogen-activated protein kinase kinase kinase kinase binding obo:GO_0033189 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a vitamin A stimulus. obo:GO_0033189 obo:go.owl obo:GO_0033189 response to retinol obo:GO_0033189 biological_process obo:GO_0033189 GO:0033189 obo:GO_0033189 response to vitamin A obo:GO_0033192 Catalysis of the reaction: protein serine/threonine phosphate + H2O = protein serine/threonine + phosphate, dependent on the presence of calcium-bound calmodulin. obo:GO_0033192 obo:go.owl obo:GO_0033192 Reactome:R-HSA-2730849 obo:GO_0033192 Reactome:R-HSA-4551451 obo:GO_0033192 calcium- and calmodulin-dependent protein phosphatase activity obo:GO_0033192 calcium/calmodulin-dependent protein phosphatase activity obo:GO_0033192 calcineurin activity obo:GO_0033192 molecular_function obo:GO_0033192 Ca2+/CaM-dependent protein phosphatase activity obo:GO_0033192 GO:0033192 obo:GO_0033192 calmodulin-dependent protein phosphatase activity obo:GO_0033194 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a hydroperoxide stimulus. Hydroperoxides are monosubstitution products of hydrogen peroxide, HOOH. obo:GO_0033194 obo:go.owl obo:GO_0033194 biological_process obo:GO_0033194 GO:0033194 obo:GO_0033194 response to hydroperoxide obo:GO_0033195 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an alkyl hydroperoxide stimulus. Alkyl hydroperoxides are monosubstitution products of hydrogen peroxide, HOOH, where the substituent is an alkyl group. obo:GO_0033195 obo:go.owl obo:GO_0033195 biological_process obo:GO_0033195 GO:0033195 obo:GO_0033195 response to alkyl hydroperoxide obo:GO_0033197 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a vitamin E stimulus. obo:GO_0033197 obo:go.owl obo:GO_0033197 response to DL-alpha-tocopherol acetate obo:GO_0033197 response to DL-alpha-tocopheryl acetate obo:GO_0033197 response to O-Acetyl-alpha-tocopherol obo:GO_0033197 biological_process obo:GO_0033197 GO:0033197 obo:GO_0033197 response to vitamin E obo:GO_0033204 Interacting selectively and non-covalently with the RNA subunit of ribonuclease P. obo:GO_0033204 obo:go.owl obo:GO_0033204 RNase P RNA binding obo:GO_0033204 molecular_function obo:GO_0033204 GO:0033204 obo:GO_0033204 ribonuclease P RNA binding obo:GO_0033212 The directed movement of iron ions from outside of a cell into the cytoplasmic compartment. This may occur via transport across the plasma membrane or via endocytosis. obo:GO_0033212 obo:go.owl obo:GO_0033212 midori obo:GO_0033212 2009-05-01T04:19:14Z obo:GO_0033212 GO:0070627 obo:GO_0033212 ferrous ion import obo:GO_0033212 ferrous iron import obo:GO_0033212 ferrous iron uptake obo:GO_0033212 biological_process obo:GO_0033212 iron assimilation obo:GO_0033212 GO:0033212 obo:GO_0033212 iron import into cell obo:GO_0033214 A process in which iron (Fe3+) is solubilized by ferric iron-specific chelators, known as siderophores, excreted by a cell; the iron-siderophore complex is then transported into the cell by specific cell surface receptors. obo:GO_0033214 obo:go.owl obo:GO_0033214 GO:0015688 obo:GO_0033214 GO:0033213 obo:GO_0033214 iron chelate transport obo:GO_0033214 iron assimilation by chelation and transport obo:GO_0033214 biological_process obo:GO_0033214 iron assimilation by capture and transport obo:GO_0033214 GO:0033214 obo:GO_0033214 siderophore-dependent iron import into cell obo:GO_0033215 A process in which iron is solubilized by reduction from Fe3+ to Fe2+ via a cell surface reductase and subsequent transport of the iron across the membrane by iron uptake proteins. obo:GO_0033215 obo:go.owl obo:GO_0033215 iron assimilation by reduction and transport obo:GO_0033215 biological_process obo:GO_0033215 GO:0033215 obo:GO_0033215 reductive iron assimilation obo:GO_0033218 Interacting selectively and non-covalently with an amide, any derivative of an oxoacid in which an acidic hydroxy group has been replaced by an amino or substituted amino group. obo:GO_0033218 obo:go.owl obo:GO_0033218 molecular_function obo:GO_0033218 GO:0033218 obo:GO_0033218 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0033218 amide binding obo:GO_0033219 Interacting selectively and non-covalently with urea, a water-soluble carboxamide with the structure H2N-CO-NH2. obo:GO_0033219 obo:go.owl obo:GO_0033219 molecular_function obo:GO_0033219 GO:0033219 obo:GO_0033219 urea binding obo:GO_0033222 Interacting selectively and non-covalently with the D- or L-enantiomer of xylose. obo:GO_0033222 obo:go.owl obo:GO_0033222 molecular_function obo:GO_0033222 GO:0033222 obo:GO_0033222 xylose binding obo:GO_0033273 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a vitamin stimulus. obo:GO_0033273 obo:go.owl obo:GO_0033273 biological_process obo:GO_0033273 GO:0033273 obo:GO_0033273 response to vitamin obo:GO_0033280 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a vitamin D stimulus. obo:GO_0033280 obo:go.owl obo:GO_0033280 response to calciferol obo:GO_0033280 response to cholecalciferol obo:GO_0033280 response to ergocalciferol obo:GO_0033280 biological_process obo:GO_0033280 GO:0033280 obo:GO_0033280 response to vitamin D obo:GO_0033293 Interacting selectively and non-covalently with a monocarboxylic acid, any organic acid containing one carboxyl (COOH) group or anion (COO-). obo:GO_0033293 obo:go.owl obo:GO_0033293 molecular_function obo:GO_0033293 GO:0033293 obo:GO_0033293 monocarboxylic acid binding obo:GO_0033294 Interacting selectively and non-covalently with ectoine, 1,4,5,6-tetrahydro-2-methyl-4-pyrimidinecarboxylic acid. obo:GO_0033294 obo:go.owl obo:GO_0033294 molecular_function obo:GO_0033294 GO:0033294 obo:GO_0033294 ectoine binding obo:GO_0033295 Interacting selectively and non-covalently with hydroxyectoine. obo:GO_0033295 obo:go.owl obo:GO_0033295 molecular_function obo:GO_0033295 GO:0033295 obo:GO_0033295 hydroxyectoine binding obo:GO_0033296 Interacting selectively and non-covalently with the D- or L-enantiomer of rhamnose. obo:GO_0033296 obo:go.owl obo:GO_0033296 molecular_function obo:GO_0033296 GO:0033296 obo:GO_0033296 rhamnose binding obo:GO_0033328 Interacting selectively and non-covalently with a peroxisomal membrane targeting sequence, any of several sequences of amino acids within a protein that can act as a signal for the localization of the protein into the peroxisome membrane. obo:GO_0033328 obo:go.owl obo:GO_0033328 PMP targeting signal (mPTS) binding obo:GO_0033328 PMP targeting signal binding obo:GO_0033328 mPTS binding obo:GO_0033328 peroxisomal membrane protein (PMP) targeting signal (mPTS) binding obo:GO_0033328 molecular_function obo:GO_0033328 GO:0033328 obo:GO_0033328 peroxisome membrane targeting sequence binding obo:GO_0033549 Catalysis of the reaction: a phosphorylated MAP kinase + H2O = a MAP kinase + phosphate. obo:GO_0033549 obo:go.owl obo:GO_0033549 MAPK phosphatase activity obo:GO_0033549 molecular_function obo:GO_0033549 GO:0033549 obo:GO_0033549 MAP kinase phosphatase activity obo:GO_0033550 Catalysis of the reaction: MAP kinase tyrosine phosphate + H2O = MAP kinase tyrosine + phosphate. obo:GO_0033550 obo:go.owl obo:GO_0033550 tyrosine-specific MAP kinase phosphatase activity obo:GO_0033550 molecular_function obo:GO_0033550 GO:0033550 obo:GO_0033550 MAP kinase tyrosine phosphatase activity obo:GO_0033552 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a vitamin B3 stimulus. obo:GO_0033552 obo:go.owl obo:GO_0033552 response to niacin obo:GO_0033552 response to nicotinamide obo:GO_0033552 biological_process obo:GO_0033552 GO:0033552 obo:GO_0033552 response to vitamin B3 obo:GO_0033554 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating the organism is under stress. The stress is usually, but not necessarily, exogenous (e.g. temperature, humidity, ionizing radiation). obo:GO_0033554 obo:go.owl obo:GO_0033554 biological_process obo:GO_0033554 GO:0033554 obo:GO_0033554 http://purl.oboInOwllibrary.org/oboInOwl/go#gocheck_do_not_manually_annotate obo:GO_0033554 Note that this term is in the subset of terms that should not be used for direct gene product annotation. Instead, select a child term or, if no appropriate child term exists, please request a new term. Direct annotations to this term may be amended during annotation QC. obo:GO_0033554 cellular response to stress obo:GO_0033571 The directed movement of lactoferrin into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0033571 obo:go.owl obo:GO_0033571 biological_process obo:GO_0033571 GO:0033571 obo:GO_0033571 lactoferrin transport obo:GO_0033572 The directed movement of transferrin into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0033572 obo:go.owl obo:GO_0033572 melanotransferrin transport obo:GO_0033572 biological_process obo:GO_0033572 GO:0033572 obo:GO_0033572 transferrin transport obo:GO_0033592 Facilitates the base-pairing of complementary single-stranded RNA. obo:GO_0033592 obo:go.owl obo:GO_0033592 molecular_function obo:GO_0033592 GO:0033592 obo:GO_0033592 RNA strand annealing activity obo:GO_0033612 Interacting selectively and non-covalently with a receptor that possesses protein serine/threonine kinase activity. obo:GO_0033612 obo:go.owl obo:GO_0033612 molecular_function obo:GO_0033612 transmembrane receptor protein serine/threonine kinase ligand binding obo:GO_0033612 GO:0033612 obo:GO_0033612 receptor serine/threonine kinase binding obo:GO_0033613 Interacting selectively and non-covalently with an activating transcription factor, any protein whose activity is required to initiate or upregulate transcription. obo:GO_0033613 obo:go.owl obo:GO_0033613 GO:0001107 obo:GO_0033613 transcription activator binding obo:GO_0033613 molecular_function obo:GO_0033613 GO:0033613 obo:GO_0033613 activating transcription factor binding obo:GO_0033688 Any process that modulates the frequency, rate or extent of osteoblast proliferation. obo:GO_0033688 obo:go.owl obo:GO_0033688 biological_process obo:GO_0033688 GO:0033688 obo:GO_0033688 regulation of osteoblast proliferation obo:GO_0033689 Any process that stops, prevents or reduces the rate or extent of osteoblast proliferation. obo:GO_0033689 obo:go.owl obo:GO_0033689 down regulation of osteoblast proliferation obo:GO_0033689 down-regulation of osteoblast proliferation obo:GO_0033689 downregulation of osteoblast proliferation obo:GO_0033689 inhibition of osteoblast proliferation obo:GO_0033689 biological_process obo:GO_0033689 GO:0033689 obo:GO_0033689 negative regulation of osteoblast proliferation obo:GO_0033690 Any process that activates or increases the rate or extent of osteoblast proliferation. obo:GO_0033690 obo:go.owl obo:GO_0033690 up regulation of osteoblast proliferation obo:GO_0033690 up-regulation of osteoblast proliferation obo:GO_0033690 upregulation of osteoblast proliferation obo:GO_0033690 activation of osteoblast proliferation obo:GO_0033690 stimulation of osteoblast proliferation obo:GO_0033690 biological_process obo:GO_0033690 GO:0033690 obo:GO_0033690 positive regulation of osteoblast proliferation obo:GO_0033691 Interacting selectively and non-covalently with sialic acid, any of a variety of N- or O- substituted derivatives of neuraminic acid, a nine carbon monosaccharide. Sialic acids often occur in polysaccharides, glycoproteins, and glycolipids in animals and bacteria. obo:GO_0033691 obo:go.owl obo:GO_0033691 N-acetylneuraminic acid binding obo:GO_0033691 molecular_function obo:GO_0033691 GO:0033691 obo:GO_0033691 sialic acid binding obo:GO_0033867 Catalysis of the reaction: ATP + Fas-activated serine/threonine protein = ADP + Fas-activated serine/threonine phosphoprotein. obo:GO_0033867 obo:go.owl obo:GO_0033867 EC:2.7.11.8 obo:GO_0033867 MetaCyc:2.7.11.8-RXN obo:GO_0033867 ATP:Fas-activated serine/threonine protein phosphotransferase activity obo:GO_0033867 molecular_function obo:GO_0033867 FAST obo:GO_0033867 FASTK obo:GO_0033867 STK10 obo:GO_0033867 GO:0033867 obo:GO_0033867 Fas-activated serine/threonine kinase activity obo:GO_0034046 Interacting selectively and non-covalently with a sequence of guanine residues in an RNA molecule. obo:GO_0034046 obo:go.owl obo:GO_0034046 poly(G) binding, within an RNA molecule obo:GO_0034046 poly(rG) binding obo:GO_0034046 molecular_function obo:GO_0034046 GO:0034046 obo:GO_0034046 poly(G) binding obo:GO_0034056 Interacting selectively and non-covalently with the estrogen response element (ERE), a conserved sequence found in the promoters of genes whose expression is regulated in response to estrogen. obo:GO_0034056 obo:go.owl obo:GO_0034056 ERE binding obo:GO_0034056 molecular_function obo:GO_0034056 GO:0034056 obo:GO_0034056 Note that as agreed during the transcription overhaul, terms specifying binding to specific transcription regulatory motifs are no longer being created. The level of specificity GO has decided to go to is the "core promoter", "core promoter proximal region" and "enhancer". To capture more detail, please consider using column 16. obo:GO_0034056 estrogen response element binding obo:GO_0034057 Facilitates the displacement of one strand of an RNA-RNA duplex and its replacement with a different strand of higher complementarity. obo:GO_0034057 obo:go.owl obo:GO_0034057 molecular_function obo:GO_0034057 GO:0034057 obo:GO_0034057 RNA strand-exchange activity obo:GO_0034110 Any process that modulates the frequency, rate, or extent of homotypic cell-cell adhesion. obo:GO_0034110 obo:go.owl obo:GO_0034110 biological_process obo:GO_0034110 GO:0034110 obo:GO_0034110 regulation of homotypic cell-cell adhesion obo:GO_0034111 Any process that stops, prevents, or reduces the frequency, rate, or extent of homotypic cell-cell adhesion. obo:GO_0034111 obo:go.owl obo:GO_0034111 biological_process obo:GO_0034111 GO:0034111 obo:GO_0034111 negative regulation of homotypic cell-cell adhesion obo:GO_0034112 Any process that activates or increases the frequency, rate, or extent of homotypic cell-cell adhesion. obo:GO_0034112 obo:go.owl obo:GO_0034112 biological_process obo:GO_0034112 GO:0034112 obo:GO_0034112 positive regulation of homotypic cell-cell adhesion obo:GO_0034114 Any process that modulates the frequency, rate, or extent of heterotypic cell-cell adhesion. obo:GO_0034114 obo:go.owl obo:GO_0034114 biological_process obo:GO_0034114 GO:0034114 obo:GO_0034114 regulation of heterotypic cell-cell adhesion obo:GO_0034116 Any process that activates or increases the frequency, rate, or extent of heterotypic cell-cell adhesion. obo:GO_0034116 obo:go.owl obo:GO_0034116 biological_process obo:GO_0034116 GO:0034116 obo:GO_0034116 positive regulation of heterotypic cell-cell adhesion obo:GO_0034118 Any process that modulates the frequency, rate, or extent of erythrocyte aggregation. obo:GO_0034118 obo:go.owl obo:GO_0034118 regulation of RBC aggregation obo:GO_0034118 regulation of red blood cell aggregation obo:GO_0034118 biological_process obo:GO_0034118 GO:0034118 obo:GO_0034118 regulation of erythrocyte aggregation obo:GO_0034119 Any process that stops, prevents, or reduces the frequency, rate, or extent of erythrocyte aggregation. obo:GO_0034119 obo:go.owl obo:GO_0034119 negative regulation of RBC aggregation obo:GO_0034119 negative regulation of red blood cell aggregation obo:GO_0034119 biological_process obo:GO_0034119 GO:0034119 obo:GO_0034119 negative regulation of erythrocyte aggregation obo:GO_0034120 Any process that activates or increases the frequency, rate, or extent of erythrocyte aggregation. obo:GO_0034120 obo:go.owl obo:GO_0034120 positive regulation of RBC aggregation obo:GO_0034120 positive regulation of red blood cell aggregation obo:GO_0034120 biological_process obo:GO_0034120 GO:0034120 obo:GO_0034120 positive regulation of erythrocyte aggregation obo:GO_0034185 Interacting selectively and non-covalently with an apolipoprotein, the protein component of a lipoprotein complex. obo:GO_0034185 obo:go.owl obo:GO_0034185 molecular_function obo:GO_0034185 GO:0034185 obo:GO_0034185 apolipoprotein binding obo:GO_0034186 Interacting selectively and non-covalently with apolipoprotein A-I. obo:GO_0034186 obo:go.owl obo:GO_0034186 molecular_function obo:GO_0034186 GO:0034186 obo:GO_0034186 apolipoprotein A-I binding obo:GO_0034189 Interacting selectively and non-covalently with a very-low-density lipoprotein particle, a triglyceride-rich lipoprotein particle that is typically composed of APOB100, APOE and APOCs and has a density of about 1.006 g/ml and a diameter of between 20-80 nm. obo:GO_0034189 obo:go.owl obo:GO_0034189 VLDL binding obo:GO_0034189 very-low-density lipoprotein binding obo:GO_0034189 molecular_function obo:GO_0034189 GO:0034189 obo:GO_0034189 very-low-density lipoprotein particle binding obo:GO_0034190 Interacting selectively and non-covalently with an apolipoprotein receptor. obo:GO_0034190 obo:go.owl obo:GO_0034190 molecular_function obo:GO_0034190 GO:0034190 obo:GO_0034190 apolipoprotein receptor binding obo:GO_0034191 Interacting selectively and non-covalently with an apolipoprotein A-I receptor. obo:GO_0034191 obo:go.owl obo:GO_0034191 molecular_function obo:GO_0034191 GO:0034191 obo:GO_0034191 Note that this term is to be used only to annotate gene products that bind to lipid-free APOA1. For receptors that bind lipid-associated apolipoproteins (plasma lipoprotein particles), consider annotating to 'lipoprotein receptor activity ; GO:0030228' or its child terms. obo:GO_0034191 apolipoprotein A-I receptor binding obo:GO_0034198 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of amino acids. obo:GO_0034198 obo:go.owl obo:GO_0034198 biological_process obo:GO_0034198 GO:0034198 obo:GO_0034198 cellular response to amino acid starvation obo:GO_0034211 Catalysis of the reaction: ATP + a protein serine/threonine = ADP + protein serine/threonine phosphate, dependent on the presence of GTP. obo:GO_0034211 obo:go.owl obo:GO_0034211 EC:2.7.11 obo:GO_0034211 molecular_function obo:GO_0034211 GO:0034211 obo:GO_0034211 GTP-dependent protein kinase activity obo:GO_0034220 A process in which an ion is transported across a membrane. obo:GO_0034220 obo:go.owl obo:GO_0034220 GO:0099131 obo:GO_0034220 ion membrane transport obo:GO_0034220 transmembrane ion transport obo:GO_0034220 ATP hydrolysis coupled ion transmembrane transport obo:GO_0034220 biological_process obo:GO_0034220 GO:0034220 obo:GO_0034220 Note that this term is not intended for use in annotating lateral movement within membranes. obo:GO_0034220 ion transmembrane transport obo:GO_0034224 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of zinc ions. obo:GO_0034224 obo:go.owl obo:GO_0034224 cellular response to zinc ion limitation obo:GO_0034224 cellular response to zinc starvation obo:GO_0034224 biological_process obo:GO_0034224 GO:0034224 obo:GO_0034224 cellular response to zinc ion starvation obo:GO_0034235 Interacting selectively and non-covalently with any glycosylphosphatidylinositol anchor. GPI anchors serve to attach membrane proteins to the lipid bilayer of cell membranes. obo:GO_0034235 obo:go.owl obo:GO_0034235 glycosylphosphatidylinositol binding obo:GO_0034235 molecular_function obo:GO_0034235 GO:0034235 obo:GO_0034235 Note that this term should be used to annotate gene products that interact non-covalently with GPI anchors, and not proteins that have GPI anchors covalently attached. obo:GO_0034235 GPI anchor binding obo:GO_0034236 Interacting selectively and non-covalently with one or both of the catalytic subunits of protein kinase A. obo:GO_0034236 obo:go.owl obo:GO_0034236 PKA catalytic subunit binding obo:GO_0034236 molecular_function obo:GO_0034236 GO:0034236 obo:GO_0034236 protein kinase A catalytic subunit binding obo:GO_0034237 Interacting selectively and non-covalently with one or both of the regulatory subunits of protein kinase A. obo:GO_0034237 obo:go.owl obo:GO_0034237 PKA regulatory subunit binding obo:GO_0034237 molecular_function obo:GO_0034237 protein kinase A anchoring activity obo:GO_0034237 GO:0034237 obo:GO_0034237 protein kinase A regulatory subunit binding obo:GO_0034260 Any process that stops or reduces the rate of GTP hydrolysis by a GTPase. obo:GO_0034260 obo:go.owl obo:GO_0034260 GO:0034259 obo:GO_0034260 GO:0034261 obo:GO_0034260 GO:1902264 obo:GO_0034260 GO:1902881 obo:GO_0034260 down regulation of GTPase activity obo:GO_0034260 down-regulation of GTPase activity obo:GO_0034260 downregulation of GTPase activity obo:GO_0034260 negative regulation of guanosinetriphosphatase activity obo:GO_0034260 down regulation of Rab GTPase activity obo:GO_0034260 down regulation of Ras GTPase activity obo:GO_0034260 down regulation of Rho GTPase activity obo:GO_0034260 down regulation of regulation of Ran GTPase activity obo:GO_0034260 down-regulation of Rab GTPase activity obo:GO_0034260 down-regulation of Ras GTPase activity obo:GO_0034260 down-regulation of Rho GTPase activity obo:GO_0034260 down-regulation of regulation of Ran GTPase activity obo:GO_0034260 downregulation of Rab GTPase activity obo:GO_0034260 downregulation of Ras GTPase activity obo:GO_0034260 downregulation of Rho GTPase activity obo:GO_0034260 downregulation of regulation of Ran GTPase activity obo:GO_0034260 inhibition of GTPase activity obo:GO_0034260 inhibition of Rab GTPase activity obo:GO_0034260 inhibition of Ras GTPase activity obo:GO_0034260 inhibition of Rho GTPase activity obo:GO_0034260 inhibition of regulation of Ran GTPase activity obo:GO_0034260 negative regulation of Rab GTPase activity obo:GO_0034260 negative regulation of Ran GTPase activity obo:GO_0034260 negative regulation of Ras GTPase activity obo:GO_0034260 negative regulation of Rho GTPase activity obo:GO_0034260 biological_process obo:GO_0034260 GO:0034260 obo:GO_0034260 An example of this is P2xA in Dictyostelium (UniProt symbol Q86JM7) in PMID:24335649. obo:GO_0034260 negative regulation of GTPase activity obo:GO_0034287 The series of events in which a stimulus from a monosaccharide is received and converted into a molecular signal. obo:GO_0034287 obo:go.owl obo:GO_0034287 biological_process obo:GO_0034287 perception of monosaccharide stimulus obo:GO_0034287 GO:0034287 obo:GO_0034287 detection of monosaccharide stimulus obo:GO_0034288 The series of events in which a stimulus from a disaccharide is received and converted into a molecular signal. obo:GO_0034288 obo:go.owl obo:GO_0034288 biological_process obo:GO_0034288 perception of disaccharide stimulus obo:GO_0034288 GO:0034288 obo:GO_0034288 detection of disaccharide stimulus obo:GO_0034289 The series of events in which a maltose stimulus is received by a cell and converted into a molecular signal. obo:GO_0034289 obo:go.owl obo:GO_0034289 biological_process obo:GO_0034289 perception of maltose stimulus obo:GO_0034289 GO:0034289 obo:GO_0034289 detection of maltose stimulus obo:GO_0034336 Interacting selectively and non-covalently with an RNA molecule that has assumed an incorrect conformation. obo:GO_0034336 obo:go.owl obo:GO_0034336 molecular_function obo:GO_0034336 RNA chaperone obo:GO_0034336 GO:0034336 obo:GO_0034336 misfolded RNA binding obo:GO_0034347 Interacting selectively and non-covalently with a type III interferon. Interferon lambda is the only member of the type III interferon found so far. obo:GO_0034347 obo:go.owl obo:GO_0034347 interferon-lambda binding obo:GO_0034347 molecular_function obo:GO_0034347 GO:0034347 obo:GO_0034347 Note that IL-28A, IL-28B, and IL-29 are types of interferon-lambda. obo:GO_0034347 type III interferon binding obo:GO_0034452 Interacting selectively and non-covalently with any part of a dynactin complex; dynactin is a large protein complex that activates dynein-based motor activity. obo:GO_0034452 obo:go.owl obo:GO_0034452 molecular_function obo:GO_0034452 GO:0034452 obo:GO_0034452 dynactin binding obo:GO_0034511 Interacting selectively and non-covalently with U3 small nucleolar RNA. obo:GO_0034511 obo:go.owl obo:GO_0034511 molecular_function obo:GO_0034511 GO:0034511 obo:GO_0034511 U3 snoRNA binding obo:GO_0034512 Interacting selectively and non-covalently with box C/D small nucleolar RNA. obo:GO_0034512 obo:go.owl obo:GO_0034512 molecular_function obo:GO_0034512 GO:0034512 obo:GO_0034512 box C/D snoRNA binding obo:GO_0034513 Interacting selectively and non-covalently with box H/ACA small nucleolar RNA. obo:GO_0034513 obo:go.owl obo:GO_0034513 molecular_function obo:GO_0034513 GO:0034513 obo:GO_0034513 box H/ACA snoRNA binding obo:GO_0034583 Interacting selectively and non-covalently with a 21U-RNA, a 21-nucleotide RNA characterized by a uridine 5'-monophosphate and a modified 3' end resistant to periodate degradation. 21U-RNAs are derived from distinct, autonomously expressed loci within the genome. obo:GO_0034583 obo:go.owl obo:GO_0034583 molecular_function obo:GO_0034583 GO:0034583 obo:GO_0034583 21U-RNA binding obo:GO_0034584 Interacting selectively and non-covalently with a piRNA, a Piwi-associated RNA, a 24- to 30-nucleotide RNA derived from repeat or complex DNA sequence elements and processed by a Dicer-independent mechanism. obo:GO_0034584 obo:go.owl obo:GO_0034584 Piwi-associated RNA binding obo:GO_0034584 molecular_function obo:GO_0034584 GO:0034584 obo:GO_0034584 piRNA binding obo:GO_0034599 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals. obo:GO_0034599 obo:go.owl obo:GO_0034599 adaptive response to oxidative stress obo:GO_0034599 biological_process obo:GO_0034599 GO:0034599 obo:GO_0034599 cellular response to oxidative stress obo:GO_0034605 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism. obo:GO_0034605 obo:go.owl obo:GO_0034605 cellular response to heat stress obo:GO_0034605 biological_process obo:GO_0034605 GO:0034605 obo:GO_0034605 cellular response to heat obo:GO_0034614 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a reactive oxygen species stimulus. Reactive oxygen species include singlet oxygen, superoxide, and oxygen free radicals. obo:GO_0034614 obo:go.owl obo:GO_0034614 cellular response to AOS obo:GO_0034614 cellular response to ROI obo:GO_0034614 cellular response to ROS obo:GO_0034614 cellular response to active oxygen species obo:GO_0034614 cellular response to reactive oxidative species obo:GO_0034614 cellular response to reactive oxygen intermediate obo:GO_0034614 biological_process obo:GO_0034614 GO:0034614 obo:GO_0034614 cellular response to reactive oxygen species obo:GO_0034617 Interacting selectively and non-covalently with a tetrahydrobiopterin, 5,6,7,8-tetrahydrobiopterin or a derivative thereof; tetrahydrobiopterins are enzyme cofactors that carry electrons in redox reactions. obo:GO_0034617 obo:go.owl obo:GO_0034617 BH4 binding obo:GO_0034617 H4biopterin binding obo:GO_0034617 sapropterin binding obo:GO_0034617 molecular_function obo:GO_0034617 GO:0034617 obo:GO_0034617 tetrahydrobiopterin binding obo:GO_0034618 Interacting selectively and non-covalently with 2-amino-5-(carbamimidamido)pentanoic acid. obo:GO_0034618 obo:go.owl obo:GO_0034618 Arg binding obo:GO_0034618 molecular_function obo:GO_0034618 aminopentanoic acid binding obo:GO_0034618 GO:0034618 obo:GO_0034618 arginine binding obo:GO_0034635 The directed movement of glutathione, the tripeptide glutamylcysteinylglycine, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0034635 obo:go.owl obo:GO_0034635 biological_process obo:GO_0034635 GO:0034635 obo:GO_0034635 glutathione transport obo:GO_0034641 The chemical reactions and pathways involving various organic and inorganic nitrogenous compounds, as carried out by individual cells. obo:GO_0034641 obo:go.owl obo:GO_0034641 cellular nitrogen compound metabolism obo:GO_0034641 biological_process obo:GO_0034641 GO:0034641 obo:GO_0034641 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0034641 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0034641 cellular nitrogen compound metabolic process obo:GO_0034644 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an ultraviolet radiation (UV light) stimulus. Ultraviolet radiation is electromagnetic radiation with a wavelength in the range of 10 to 380 nanometers. obo:GO_0034644 obo:go.owl obo:GO_0034644 cellular response to UV light stimulus obo:GO_0034644 cellular response to UV radiation stimulus obo:GO_0034644 cellular response to ultraviolet light stimulus obo:GO_0034644 cellular response to ultraviolet radiation stimulus obo:GO_0034644 biological_process obo:GO_0034644 GO:0034644 obo:GO_0034644 cellular response to UV obo:GO_0034645 The chemical reactions and pathways resulting in the formation of a macromolecule, any molecule of high relative molecular mass, the structure of which essentially comprises the multiple repetition of units derived, actually or conceptually, from molecules of low relative molecular mass, carried out by individual cells. obo:GO_0034645 obo:go.owl obo:GO_0034645 GO:0034961 obo:GO_0034645 cellular biopolymer biosynthetic process obo:GO_0034645 cellular macromolecule anabolism obo:GO_0034645 cellular macromolecule biosynthesis obo:GO_0034645 cellular macromolecule formation obo:GO_0034645 cellular macromolecule synthesis obo:GO_0034645 biological_process obo:GO_0034645 GO:0034645 obo:GO_0034645 cellular macromolecule biosynthetic process obo:GO_0034654 The chemical reactions and pathways resulting in the formation of nucleobases, nucleosides, nucleotides and nucleic acids. obo:GO_0034654 obo:go.owl obo:GO_0034654 nucleobase, nucleoside, nucleotide and nucleic acid anabolism obo:GO_0034654 nucleobase, nucleoside, nucleotide and nucleic acid biosynthesis obo:GO_0034654 nucleobase, nucleoside, nucleotide and nucleic acid formation obo:GO_0034654 nucleobase, nucleoside, nucleotide and nucleic acid synthesis obo:GO_0034654 biological_process obo:GO_0034654 GO:0034654 obo:GO_0034654 nucleobase-containing compound biosynthetic process obo:GO_0034710 Interacting selectively and non-covalently with an inhibin complex, a dimer of one inhibin-alpha subunit and one inhibin-beta subunit. obo:GO_0034710 obo:go.owl obo:GO_0034710 molecular_function obo:GO_0034710 GO:0034710 obo:GO_0034710 inhibin complex binding obo:GO_0034711 Interacting selectively and non-covalently with an inhibin monomer, any of the polypeptides that combine to form activin and inhibin dimers. obo:GO_0034711 obo:go.owl obo:GO_0034711 GO:0034712 obo:GO_0034711 GO:0048186 obo:GO_0034711 GO:0048187 obo:GO_0034711 inhibin monomer binding obo:GO_0034711 inhibin alpha binding obo:GO_0034711 inhibin beta-A binding obo:GO_0034711 inhibin beta-B binding obo:GO_0034711 molecular_function obo:GO_0034711 GO:0034711 obo:GO_0034711 inhibin binding obo:GO_0034713 Interacting selectively and non-covalently with a type I transforming growth factor beta receptor. obo:GO_0034713 obo:go.owl obo:GO_0034713 GO:0005103 obo:GO_0034713 GO:0005116 obo:GO_0034713 GO:0005120 obo:GO_0034713 TGF-beta type I binding obo:GO_0034713 transforming growth factor beta receptor type I binding obo:GO_0034713 type I TGF-beta binding obo:GO_0034713 babo binding obo:GO_0034713 babo ligand obo:GO_0034713 baboon binding obo:GO_0034713 baboon ligand obo:GO_0034713 baboon receptor ligand obo:GO_0034713 sax binding obo:GO_0034713 sax ligand obo:GO_0034713 saxophone binding obo:GO_0034713 saxophone ligand obo:GO_0034713 thickveins binding obo:GO_0034713 thickveins ligand obo:GO_0034713 tkv binding obo:GO_0034713 tkv ligand obo:GO_0034713 molecular_function obo:GO_0034713 transforming growth factor beta ligand binding to type I receptor obo:GO_0034713 GO:0034713 obo:GO_0034713 type I transforming growth factor beta receptor binding obo:GO_0034714 Interacting selectively and non-covalently with a type III transforming growth factor beta receptor. obo:GO_0034714 obo:go.owl obo:GO_0034714 TGF-beta type III binding obo:GO_0034714 transforming growth factor beta receptor type III binding obo:GO_0034714 type IIII TGF-beta binding obo:GO_0034714 molecular_function obo:GO_0034714 betaglycan binding obo:GO_0034714 transforming growth factor beta ligand binding to type III receptor obo:GO_0034714 GO:0034714 obo:GO_0034714 type III transforming growth factor beta receptor binding obo:GO_0034755 A process in which an iron ion is transported from one side of a membrane to the other by means of some agent such as a transporter or pore. obo:GO_0034755 obo:go.owl obo:GO_0034755 vw obo:GO_0034755 2015-02-06T11:29:22Z obo:GO_0034755 GO:0000040 obo:GO_0034755 GO:0006827 obo:GO_0034755 GO:0061839 obo:GO_0034755 GO:1903874 obo:GO_0034755 iron ion membrane transport obo:GO_0034755 transmembrane iron transport obo:GO_0034755 ferrous ion transmembrane transport obo:GO_0034755 ferrous iron transmembrane transport obo:GO_0034755 high affinity ferrous ion transmembrane transport obo:GO_0034755 high affinity iron ion transport obo:GO_0034755 high-affinity ferrous ion transmembrane transport obo:GO_0034755 high-affinity iron ion transmembrane transport obo:GO_0034755 high-affinity iron ion transport obo:GO_0034755 iron(2+) transmembrane transport obo:GO_0034755 low affinity iron ion transport obo:GO_0034755 low-affinity iron ion transmembrane transport obo:GO_0034755 low-affinity iron ion transport obo:GO_0034755 biological_process obo:GO_0034755 GO:0034755 obo:GO_0034755 Note that this term is not intended for use in annotating lateral movement within membranes. obo:GO_0034755 iron ion transmembrane transport obo:GO_0034756 Any process that modulates the frequency, rate or extent of the directed movement of iron ions (Fe) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0034756 obo:go.owl obo:GO_0034756 mah obo:GO_0034756 2012-04-18T04:00:14Z obo:GO_0034756 GO:1900390 obo:GO_0034756 regulation of Fe transport obo:GO_0034756 regulation of iron transport obo:GO_0034756 regulation of iron import obo:GO_0034756 regulation of iron ion import obo:GO_0034756 biological_process obo:GO_0034756 GO:0034756 obo:GO_0034756 regulation of iron ion transport obo:GO_0034757 Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of iron ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0034757 obo:go.owl obo:GO_0034757 down regulation of iron ion transport obo:GO_0034757 down-regulation of iron ion transport obo:GO_0034757 downregulation of iron ion transport obo:GO_0034757 negative regulation of iron transport obo:GO_0034757 inhibition of iron ion transport obo:GO_0034757 biological_process obo:GO_0034757 GO:0034757 obo:GO_0034757 negative regulation of iron ion transport obo:GO_0034758 Any process that activates or increases the frequency, rate or extent of the directed movement of iron ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0034758 obo:go.owl obo:GO_0034758 positive regulation of iron transport obo:GO_0034758 up regulation of iron ion transport obo:GO_0034758 up-regulation of iron ion transport obo:GO_0034758 upregulation of iron ion transport obo:GO_0034758 activation of iron ion transport obo:GO_0034758 stimulation of iron ion transport obo:GO_0034758 biological_process obo:GO_0034758 GO:0034758 obo:GO_0034758 positive regulation of iron ion transport obo:GO_0034759 Any process that modulates the frequency, rate or extent of the directed movement of iron ions (Fe) from one side of a membrane to the other by means of some agent such as a transporter or pore. obo:GO_0034759 obo:go.owl obo:GO_0034759 regulation of iron ion membrane transport obo:GO_0034759 regulation of transmembrane Fe transport obo:GO_0034759 regulation of transmembrane iron ion transport obo:GO_0034759 regulation of transmembrane iron transport obo:GO_0034759 biological_process obo:GO_0034759 GO:0034759 obo:GO_0034759 regulation of iron ion transmembrane transport obo:GO_0034760 Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of iron ions from one side of a membrane to the other by means of some agent such as a transporter or pore. obo:GO_0034760 obo:go.owl obo:GO_0034760 down regulation of transmembrane iron ion transport obo:GO_0034760 down-regulation of transmembrane iron ion transport obo:GO_0034760 downregulation of transmembrane iron ion transport obo:GO_0034760 negative regulation of iron ion membrane transport obo:GO_0034760 negative regulation of transmembrane iron ion transport obo:GO_0034760 negative regulation of transmembrane iron transport obo:GO_0034760 inhibition of transmembrane iron ion transport obo:GO_0034760 biological_process obo:GO_0034760 GO:0034760 obo:GO_0034760 negative regulation of iron ion transmembrane transport obo:GO_0034761 Any process that activates or increases the frequency, rate or extent of the directed movement of iron ions from one side of a membrane to the other by means of some agent such as a transporter or pore. obo:GO_0034761 obo:go.owl obo:GO_0034761 positive regulation of iron ion membrane transport obo:GO_0034761 positive regulation of transmembrane iron ion transport obo:GO_0034761 positive regulation of transmembrane iron transport obo:GO_0034761 up regulation of transmembrane iron ion transport obo:GO_0034761 up-regulation of transmembrane iron ion transport obo:GO_0034761 upregulation of transmembrane iron ion transport obo:GO_0034761 activation of transmembrane iron ion transport obo:GO_0034761 stimulation of transmembrane iron ion transport obo:GO_0034761 biological_process obo:GO_0034761 GO:0034761 obo:GO_0034761 positive regulation of iron ion transmembrane transport obo:GO_0034762 Any process that modulates the frequency, rate or extent of the directed movement of a solute from one side of a membrane to the other. obo:GO_0034762 obo:go.owl obo:GO_0034762 regulation of membrane transport obo:GO_0034762 biological_process obo:GO_0034762 GO:0034762 obo:GO_0034762 regulation of transmembrane transport obo:GO_0034763 Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of a solute from one side of a membrane to the other. obo:GO_0034763 obo:go.owl obo:GO_0034763 down regulation of transmembrane transport obo:GO_0034763 down-regulation of transmembrane transport obo:GO_0034763 downregulation of transmembrane transport obo:GO_0034763 negative regulation of membrane transport obo:GO_0034763 inhibition of transmembrane transport obo:GO_0034763 biological_process obo:GO_0034763 GO:0034763 obo:GO_0034763 negative regulation of transmembrane transport obo:GO_0034764 Any process that activates or increases the frequency, rate or extent of the directed movement of a solute from one side of a membrane to the other. obo:GO_0034764 obo:go.owl obo:GO_0034764 positive regulation of membrane transport obo:GO_0034764 up regulation of transmembrane transport obo:GO_0034764 up-regulation of transmembrane transport obo:GO_0034764 upregulation of transmembrane transport obo:GO_0034764 activation of transmembrane transport obo:GO_0034764 stimulation of transmembrane transport obo:GO_0034764 biological_process obo:GO_0034764 GO:0034764 obo:GO_0034764 positive regulation of transmembrane transport obo:GO_0034765 Any process that modulates the frequency, rate or extent of the directed movement of ions from one side of a membrane to the other. obo:GO_0034765 obo:go.owl obo:GO_0034765 regulation of ion membrane transport obo:GO_0034765 regulation of transmembrane ion transport obo:GO_0034765 biological_process obo:GO_0034765 GO:0034765 obo:GO_0034765 regulation of ion transmembrane transport obo:GO_0034766 Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of ions from one side of a membrane to the other. obo:GO_0034766 obo:go.owl obo:GO_0034766 down regulation of transmembrane ion transport obo:GO_0034766 down-regulation of transmembrane ion transport obo:GO_0034766 downregulation of transmembrane ion transport obo:GO_0034766 negative regulation of ion membrane transport obo:GO_0034766 negative regulation of transmembrane ion transport obo:GO_0034766 inhibition of transmembrane ion transport obo:GO_0034766 biological_process obo:GO_0034766 GO:0034766 obo:GO_0034766 negative regulation of ion transmembrane transport obo:GO_0034767 Any process that activates or increases the frequency, rate or extent of the directed movement of ions from one side of a membrane to the other. obo:GO_0034767 obo:go.owl obo:GO_0034767 positive regulation of ion membrane transport obo:GO_0034767 positive regulation of transmembrane ion transport obo:GO_0034767 up regulation of transmembrane ion transport obo:GO_0034767 up-regulation of transmembrane ion transport obo:GO_0034767 upregulation of transmembrane ion transport obo:GO_0034767 activation of transmembrane ion transport obo:GO_0034767 stimulation of transmembrane ion transport obo:GO_0034767 biological_process obo:GO_0034767 GO:0034767 obo:GO_0034767 positive regulation of ion transmembrane transport obo:GO_0034987 Interacting selectively and non-covalently with one or more specific sites on an immunoglobulin receptor molecule. obo:GO_0034987 obo:go.owl obo:GO_0034987 molecular_function obo:GO_0034987 Fc receptor binding obo:GO_0034987 GO:0034987 obo:GO_0034987 immunoglobulin receptor binding obo:GO_0034988 Interacting selectively and non-covalently with one or more specific sites on the Fc-gamma receptor I complex. The complex functions primarily as an activating receptor for IgG. obo:GO_0034988 obo:go.owl obo:GO_0034988 molecular_function obo:GO_0034988 GO:0034988 obo:GO_0034988 Fc-gamma receptor I complex binding obo:GO_0035035 Interacting selectively and non-covalently with the enzyme histone acetyltransferase. obo:GO_0035035 obo:go.owl obo:GO_0035035 histone acetylase binding obo:GO_0035035 molecular_function obo:GO_0035035 GO:0035035 obo:GO_0035035 histone acetyltransferase binding obo:GO_0035064 Interacting selectively and non-covalently with a histone in which a residue has been modified by methylation. Histones are any of a group of water-soluble proteins found in association with the DNA of eukaroytic chromosomes. obo:GO_0035064 obo:go.owl obo:GO_0035064 molecular_function obo:GO_0035064 GO:0035064 obo:GO_0035064 methylated histone binding obo:GO_0035091 Interacting selectively and non-covalently with any inositol-containing glycerophospholipid, i.e. phosphatidylinositol (PtdIns) and its phosphorylated derivatives. obo:GO_0035091 obo:go.owl obo:GO_0035091 phosphoinositide binding obo:GO_0035091 molecular_function obo:GO_0035091 GO:0035091 obo:GO_0035091 phosphatidylinositol binding obo:GO_0035100 Interacting selectively and non-covalently with 20-hydroxyecdysone (ecdysone). Ecdysone is an ecdysteroid produced by the prothoracic glands of immature insects and the ovaries of adult females, which stimulates growth and molting. obo:GO_0035100 obo:go.owl obo:GO_0035100 molecular_function obo:GO_0035100 GO:0035100 obo:GO_0035100 ecdysone binding obo:GO_0035173 Catalysis of the transfer of a phosphate group to a histone. Histones are any of a group of water-soluble proteins found in association with the DNA of eukaroytic chromosomes. obo:GO_0035173 obo:go.owl obo:GO_0035173 molecular_function obo:GO_0035173 GO:0035173 obo:GO_0035173 histone kinase activity obo:GO_0035174 Catalysis of the transfer of a phosphate group to a serine residue of a histone. Histones are any of a group of water-soluble proteins found in association with the DNA of eukaroytic chromosomes. obo:GO_0035174 obo:go.owl obo:GO_0035174 histone-serine kinase activity obo:GO_0035174 molecular_function obo:GO_0035174 GO:0035174 obo:GO_0035174 histone serine kinase activity obo:GO_0035175 Catalysis of the transfer of a phosphate group to the serine-10 residue of the N-terminal tail of histone H3. obo:GO_0035175 obo:go.owl obo:GO_0035175 GO:0044021 obo:GO_0035175 histone kinase activity (H3-S3 specific) obo:GO_0035175 histone serine kinase activity (H3-S10 specific) obo:GO_0035175 histone-serine kinase activity (H3-S10 specific) obo:GO_0035175 molecular_function obo:GO_0035175 GO:0035175 obo:GO_0035175 histone kinase activity (H3-S10 specific) obo:GO_0035184 Catalysis of the transfer of a phosphate group to a threonine residue of a histone. Histones are any of a group of water-soluble proteins found in association with the DNA of eukaroytic chromosomes. obo:GO_0035184 obo:go.owl obo:GO_0035184 histone-threonine kinase activity obo:GO_0035184 molecular_function obo:GO_0035184 GO:0035184 obo:GO_0035184 histone threonine kinase activity obo:GO_0035197 Interacting selectively and non-covalently with a small interfering RNA, a 21-23 nucleotide RNA that is processed from double stranded RNA (dsRNA) by an RNAse enzyme. obo:GO_0035197 obo:go.owl obo:GO_0035197 small interfering RNA binding obo:GO_0035197 molecular_function obo:GO_0035197 GO:0035197 obo:GO_0035197 siRNA binding obo:GO_0035198 Interacting selectively and non-covalently with a microRNA, a 21-23 nucleotide RNA that is processed from a stem-loop RNA precursor (pre-miRNA) that is encoded within plant and animal genomes. obo:GO_0035198 obo:go.owl obo:GO_0035198 microRNA binding obo:GO_0035198 molecular_function obo:GO_0035198 GO:0035198 obo:GO_0035198 miRNA binding obo:GO_0035226 Interacting selectively and non-covalently with the catalytic subunit of glutamate-cysteine ligase. obo:GO_0035226 obo:go.owl obo:GO_0035226 molecular_function obo:GO_0035226 GO:0035226 obo:GO_0035226 glutamate-cysteine ligase catalytic subunit binding obo:GO_0035240 Interacting selectively and non-covalently with dopamine, a catecholamine neurotransmitter formed by aromatic-L-amino-acid decarboxylase from 3,4-dihydroxy-L-phenylalanine. obo:GO_0035240 obo:go.owl obo:GO_0035240 molecular_function obo:GO_0035240 GO:0035240 obo:GO_0035240 dopamine binding obo:GO_0035250 Catalysis of the transfer of a galactose group from UDP-galactose to an acceptor molecule. obo:GO_0035250 obo:go.owl obo:GO_0035250 molecular_function obo:GO_0035250 GO:0035250 obo:GO_0035250 UDP-galactosyltransferase activity obo:GO_0035252 Catalysis of the transfer of a xylosyl group from UDP-xylose to an acceptor molecule. obo:GO_0035252 obo:go.owl obo:GO_0035252 Reactome:R-HSA-5617138 obo:GO_0035252 Reactome:R-HSA-6785668 obo:GO_0035252 Reactome:R-HSA-9638090 obo:GO_0035252 molecular_function obo:GO_0035252 GO:0035252 obo:GO_0035252 UDP-xylosyltransferase activity obo:GO_0035254 Interacting selectively and non-covalently with a glutamate receptor. obo:GO_0035254 obo:go.owl obo:GO_0035254 molecular_function obo:GO_0035254 GO:0035254 obo:GO_0035254 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0035254 glutamate receptor binding obo:GO_0035255 Interacting selectively and non-covalently with an ionotropic glutamate receptor. Ionotropic glutamate receptors bind glutamate and exert an effect through the regulation of ion channels. obo:GO_0035255 obo:go.owl obo:GO_0035255 molecular_function obo:GO_0035255 GO:0035255 obo:GO_0035255 ionotropic glutamate receptor binding obo:GO_0035256 Interacting selectively and non-covalently with a G protein-coupled glutamate receptor (a metabotropic glutamate receptor). obo:GO_0035256 obo:go.owl obo:GO_0035256 G-protein coupled glutamate receptor binding obo:GO_0035256 metabotropic glutamate receptor binding obo:GO_0035256 molecular_function obo:GO_0035256 GO:0035256 obo:GO_0035256 G protein-coupled glutamate receptor binding obo:GO_0035257 Interacting selectively and non-covalently with a nuclear hormone receptor, a ligand-dependent receptor found in the nucleus of the cell. obo:GO_0035257 obo:go.owl obo:GO_0035257 molecular_function obo:GO_0035257 GO:0035257 obo:GO_0035257 nuclear hormone receptor binding obo:GO_0035258 Interacting selectively and non-covalently with a steroid hormone receptor. obo:GO_0035258 obo:go.owl obo:GO_0035258 molecular_function obo:GO_0035258 GO:0035258 obo:GO_0035258 steroid hormone receptor binding obo:GO_0035259 Interacting selectively and non-covalently with a glucocorticoid receptor. obo:GO_0035259 obo:go.owl obo:GO_0035259 molecular_function obo:GO_0035259 GO:0035259 obo:GO_0035259 glucocorticoid receptor binding obo:GO_0035273 Interacting selectively and non-covalently with a phthalate, any ester or salt of phthalic acid. obo:GO_0035273 obo:go.owl obo:GO_0035273 molecular_function obo:GO_0035273 GO:0035273 obo:GO_0035273 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0035273 phthalate binding obo:GO_0035274 Interacting selectively and non-covalently with diphenyl phthalate, C(20)H(14)O(4). obo:GO_0035274 obo:go.owl obo:GO_0035274 DPP binding obo:GO_0035274 molecular_function obo:GO_0035274 GO:0035274 obo:GO_0035274 diphenyl phthalate binding obo:GO_0035275 Interacting selectively and non-covalently with dibutyl phthalate, C(16)H(22)O(4). obo:GO_0035275 obo:go.owl obo:GO_0035275 DBP binding obo:GO_0035275 phthalic acid dibutyl ester binding obo:GO_0035275 molecular_function obo:GO_0035275 GO:0035275 obo:GO_0035275 dibutyl phthalate binding obo:GO_0035276 Interacting selectively and non-covalently with ethanol, CH(3)-CH(2)-OH. obo:GO_0035276 obo:go.owl obo:GO_0035276 molecular_function obo:GO_0035276 GO:0035276 obo:GO_0035276 ethanol binding obo:GO_0035325 Interacting selectively and non-covalently with a Toll-like protein, a pattern recognition receptor that binds pattern motifs from a variety of microbial sources to initiate an innate immune response. obo:GO_0035325 obo:go.owl obo:GO_0035325 rfoulger obo:GO_0035325 2010-02-26T10:11:55Z obo:GO_0035325 TLR binding obo:GO_0035325 molecular_function obo:GO_0035325 GO:0035325 obo:GO_0035325 Toll-like receptor binding obo:GO_0035326 Interacting selectively and non-covalently with an enhancer, a transcription regulatory region that is somewhat distal from the core promoter and which enhances transcription from that promoter. obo:GO_0035326 obo:go.owl obo:GO_0035326 rfoulger obo:GO_0035326 2010-02-26T10:17:00Z obo:GO_0035326 molecular_function obo:GO_0035326 GO:0035326 obo:GO_0035326 enhancer binding obo:GO_0035351 The process in which heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring, is transported from one side of a membrane to the other by means of some agent such as a transporter or pore. obo:GO_0035351 obo:go.owl obo:GO_0035351 rfoulger obo:GO_0035351 2010-03-04T03:45:46Z obo:GO_0035351 heme membrane transport obo:GO_0035351 biological_process obo:GO_0035351 GO:0035351 obo:GO_0035351 Note that this term is not intended for use in annotating lateral movement within membranes. obo:GO_0035351 heme transmembrane transport obo:GO_0035368 Interacting selectively and non-covalently with the selenocysteine insertion sequence (SECIS), a regulatory sequence within mRNA which directs incorporation of a selenocysteine at a stop codon (UGA) during translation. obo:GO_0035368 obo:go.owl obo:GO_0035368 rfoulger obo:GO_0035368 2010-03-11T10:42:28Z obo:GO_0035368 SECIS binding obo:GO_0035368 molecular_function obo:GO_0035368 GO:0035368 obo:GO_0035368 selenocysteine insertion sequence binding obo:GO_0035373 Interacting selectively and non-covalently with a chondroitin sulfate proteoglycan, any proteoglycan containing chondroitin sulfate as the glycosaminoglycan carbohydrate unit. obo:GO_0035373 obo:go.owl obo:GO_0035373 rfoulger obo:GO_0035373 2010-03-12T10:23:55Z obo:GO_0035373 molecular_function obo:GO_0035373 GO:0035373 obo:GO_0035373 chondroitin sulfate proteoglycan binding obo:GO_0035374 Interacting selectively and non-covalently with chondroitin sulfate, a glycosaminoglycan made up of two alternating monosaccharides: D-glucuronic acid (GlcA) and N-acetyl-D-galactosamine (GalNAc). obo:GO_0035374 obo:go.owl obo:GO_0035374 rfoulger obo:GO_0035374 2010-03-12T10:25:34Z obo:GO_0035374 molecular_function obo:GO_0035374 GO:0035374 obo:GO_0035374 chondroitin sulfate binding obo:GO_0035375 Interacting selectively and non-covalently with a zymogen, an enzymatically inactive precursor of an enzyme that is often convertible to an active enzyme by proteolysis. obo:GO_0035375 obo:go.owl obo:GO_0035375 rfoulger obo:GO_0035375 2010-03-18T10:50:35Z obo:GO_0035375 proenzyme binding obo:GO_0035375 molecular_function obo:GO_0035375 GO:0035375 obo:GO_0035375 zymogen binding obo:GO_0035400 Catalysis of the transfer of a phosphate group to a tyrosine residue of a histone. Histones are any of a group of water-soluble proteins found in association with the DNA of eukaroytic chromosomes. obo:GO_0035400 obo:go.owl obo:GO_0035400 rfoulger obo:GO_0035400 2010-03-24T09:59:15Z obo:GO_0035400 histone-tyrosine kinase activity obo:GO_0035400 molecular_function obo:GO_0035400 GO:0035400 obo:GO_0035400 histone tyrosine kinase activity obo:GO_0035401 Catalysis of the transfer of a phosphate group to the tyrosine-41 residue of histone H3. obo:GO_0035401 obo:go.owl obo:GO_0035401 rfoulger obo:GO_0035401 2010-03-24T10:01:14Z obo:GO_0035401 histone tyrosine kinase activity (H3-Y41 specific) obo:GO_0035401 histone-tyrosine kinase activity (H3-Y41 specific) obo:GO_0035401 molecular_function obo:GO_0035401 GO:0035401 obo:GO_0035401 histone kinase activity (H3-Y41 specific) obo:GO_0035402 Catalysis of the transfer of a phosphate group to the threonine-11 residue of the N-terminal tail of histone H3. obo:GO_0035402 obo:go.owl obo:GO_0035402 rfoulger obo:GO_0035402 2010-03-24T10:04:40Z obo:GO_0035402 histone threonine kinase activity (H3-T11 specific) obo:GO_0035402 histone-threonine kinase activity (H3-T11 specific) obo:GO_0035402 molecular_function obo:GO_0035402 GO:0035402 obo:GO_0035402 histone kinase activity (H3-T11 specific) obo:GO_0035403 Catalysis of the transfer of a phosphate group to the threonine-6 residue of the N-terminal tail of histone H3. obo:GO_0035403 obo:go.owl obo:GO_0035403 rfoulger obo:GO_0035403 2010-03-24T10:05:39Z obo:GO_0035403 histone threonine kinase activity (H3-T6 specific) obo:GO_0035403 histone-threonine kinase activity (H3-T6 specific) obo:GO_0035403 molecular_function obo:GO_0035403 GO:0035403 obo:GO_0035403 histone kinase activity (H3-T6 specific) obo:GO_0035430 Any process that modulates the frequency, rate or extent of the directed movement of a gluconate across a membrane by means of some agent such as a transporter or pore. obo:GO_0035430 obo:go.owl obo:GO_0035430 rfoulger obo:GO_0035430 2010-04-08T10:37:18Z obo:GO_0035430 GO:0032893 obo:GO_0035430 regulation of gluconate membrane transport obo:GO_0035430 biological_process obo:GO_0035430 regulation of gluconate transport obo:GO_0035430 GO:0035430 obo:GO_0035430 regulation of gluconate transmembrane transport obo:GO_0035431 Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of gluconate across a membrane by means of some agent such as a transporter or pore. obo:GO_0035431 obo:go.owl obo:GO_0035431 rfoulger obo:GO_0035431 2010-04-08T10:39:08Z obo:GO_0035431 GO:0032894 obo:GO_0035431 down regulation of gluconate transport obo:GO_0035431 down-regulation of gluconate transport obo:GO_0035431 downregulation of gluconate transport obo:GO_0035431 negative regulation of gluconate membrane transport obo:GO_0035431 inhibition of gluconate transport obo:GO_0035431 biological_process obo:GO_0035431 negative regulation of gluconate transport obo:GO_0035431 GO:0035431 obo:GO_0035431 negative regulation of gluconate transmembrane transport obo:GO_0035432 Any process that activates or increases the frequency, rate or extent of the directed movement of gluconate across a membrane by means of some agent such as a transporter or pore. obo:GO_0035432 obo:go.owl obo:GO_0035432 rfoulger obo:GO_0035432 2010-04-08T10:39:58Z obo:GO_0035432 GO:0032895 obo:GO_0035432 positive regulation of gluconate membrane transport obo:GO_0035432 up regulation of gluconate transport obo:GO_0035432 up-regulation of gluconate transport obo:GO_0035432 upregulation of gluconate transport obo:GO_0035432 activation of gluconate transport obo:GO_0035432 induction of gluconate transport obo:GO_0035432 stimulation of gluconate transport obo:GO_0035432 biological_process obo:GO_0035432 positive regulation of gluconate transport obo:GO_0035432 GO:0035432 obo:GO_0035432 positive regulation of gluconate transmembrane transport obo:GO_0035434 The directed movement of copper cation across a membrane. obo:GO_0035434 obo:go.owl obo:GO_0035434 rfoulger obo:GO_0035434 2010-04-08T11:03:23Z obo:GO_0035434 GO:1901473 obo:GO_0035434 copper cation transmembrane transport obo:GO_0035434 copper ion membrane transport obo:GO_0035434 biological_process obo:GO_0035434 GO:0035434 obo:GO_0035434 Note that this term is not intended for use in annotating lateral movement within membranes. obo:GO_0035434 copper ion transmembrane transport obo:GO_0035438 Interacting selectively and non-covalently with cyclic-di-GMP, cyclic dimeric guanosine monophosphate. obo:GO_0035438 obo:go.owl obo:GO_0035438 rfoulger obo:GO_0035438 2010-04-09T02:40:17Z obo:GO_0035438 3',5'-cyclic di-GMP binding obo:GO_0035438 c-di-GMP binding obo:GO_0035438 cyclic dinucleotide di-GMP binding obo:GO_0035438 molecular_function obo:GO_0035438 GO:0035438 obo:GO_0035438 cyclic-di-GMP binding obo:GO_0035444 The directed movement of nickel (Ni) cations across a membrane by means of some agent such as a transporter or pore. obo:GO_0035444 obo:go.owl obo:GO_0035444 rfoulger obo:GO_0035444 2010-04-13T09:22:51Z obo:GO_0035444 nickel cation membrane transport obo:GO_0035444 biological_process obo:GO_0035444 GO:0035444 obo:GO_0035444 Note that this term is not intended for use in annotating lateral movement within membranes. obo:GO_0035444 nickel cation transmembrane transport obo:GO_0035473 Interacting selectively and non-covalently with any lipase. obo:GO_0035473 obo:go.owl obo:GO_0035473 rfoulger obo:GO_0035473 2010-04-22T05:28:52Z obo:GO_0035473 molecular_function obo:GO_0035473 GO:0035473 obo:GO_0035473 lipase binding obo:GO_0035478 Interacting selectively and non-covalently with a chylomicron, a large lipoprotein particle (diameter 75-1200 nm) composed of a central core of triglycerides and cholesterol surrounded by a protein-phospholipid coating. The proteins include one molecule of apolipoprotein B-48 and may include a variety of apolipoproteins, including APOAs, APOCs and APOE. obo:GO_0035478 obo:go.owl obo:GO_0035478 rfoulger obo:GO_0035478 2010-04-23T10:18:52Z obo:GO_0035478 molecular_function obo:GO_0035478 GO:0035478 obo:GO_0035478 chylomicron binding obo:GO_0035484 Interacting selectively and non-covalently with double-stranded DNA containing an A/A mispair. obo:GO_0035484 obo:go.owl obo:GO_0035484 rfoulger obo:GO_0035484 2010-04-23T10:54:52Z obo:GO_0035484 A/A mispair binding obo:GO_0035484 molecular_function obo:GO_0035484 GO:0035484 obo:GO_0035484 adenine/adenine mispair binding obo:GO_0035485 Interacting selectively and non-covalently with double-stranded DNA containing an A/G mispair. obo:GO_0035485 obo:go.owl obo:GO_0035485 rfoulger obo:GO_0035485 2010-04-23T10:55:43Z obo:GO_0035485 A/G mispair binding obo:GO_0035485 guanine-adenine mispair binding obo:GO_0035485 molecular_function obo:GO_0035485 G/A mispair binding obo:GO_0035485 GO:0035485 obo:GO_0035485 adenine/guanine mispair binding obo:GO_0035486 Interacting selectively and non-covalently with double-stranded DNA containing a C/C mispair. obo:GO_0035486 obo:go.owl obo:GO_0035486 rfoulger obo:GO_0035486 2010-04-23T10:56:10Z obo:GO_0035486 C/C mispair binding obo:GO_0035486 molecular_function obo:GO_0035486 GO:0035486 obo:GO_0035486 cytosine/cytosine mispair binding obo:GO_0035487 Interacting selectively and non-covalently with double-stranded DNA containing a T/T mispair. obo:GO_0035487 obo:go.owl obo:GO_0035487 rfoulger obo:GO_0035487 2010-04-23T10:56:37Z obo:GO_0035487 T/T mispair binding obo:GO_0035487 molecular_function obo:GO_0035487 GO:0035487 obo:GO_0035487 thymine/thymine mispair binding obo:GO_0035488 Interacting selectively and non-covalently with double-stranded DNA containing a C/T mispair. obo:GO_0035488 obo:go.owl obo:GO_0035488 rfoulger obo:GO_0035488 2010-04-23T10:57:13Z obo:GO_0035488 C/T mispair binding obo:GO_0035488 T/C mispair binding obo:GO_0035488 thymine/cytosine mispair binding obo:GO_0035488 molecular_function obo:GO_0035488 GO:0035488 obo:GO_0035488 cytosine/thymine mispair binding obo:GO_0035489 Interacting selectively and non-covalently with double-stranded DNA containing a G/G mispair. obo:GO_0035489 obo:go.owl obo:GO_0035489 rfoulger obo:GO_0035489 2010-04-23T11:16:55Z obo:GO_0035489 G/G mispair binding obo:GO_0035489 molecular_function obo:GO_0035489 GO:0035489 obo:GO_0035489 guanine/guanine mispair binding obo:GO_0035497 Interacting selectively and non-covalently with the cyclic AMP response element (CRE), a short palindrome-containing sequence found in the promoters of genes whose expression is regulated in response to cyclic AMP. obo:GO_0035497 obo:go.owl obo:GO_0035497 rfoulger obo:GO_0035497 2010-04-29T09:26:47Z obo:GO_0035497 CRE binding obo:GO_0035497 cAMP-responsive element binding obo:GO_0035497 cyclic AMP response element binding obo:GO_0035497 cyclic-AMP response element binding obo:GO_0035497 cyclic-AMP-responsive element binding obo:GO_0035497 molecular_function obo:GO_0035497 GO:0035497 obo:GO_0035497 Note that as agreed during the transcription overhaul, terms specifying binding to specific transcription regulatory motifs are no longer being created. The level of specificity GO has decided to go to is the "core promoter", "core promoter proximal region" and "enhancer". To capture more detail, please consider using column 16. obo:GO_0035497 cAMP response element binding obo:GO_0035500 Interacting selectively and non-covalently with the MH2 (MAD homology 2) domain of a protein. The MH2 domain is found at the carboxy-terminus of MAD related proteins such as Smads. The MH2 domain mediates interaction with a wide variety of proteins and provides specificity and selectivity to Smad function and also is critical for mediating interactions in Smad oligomers. obo:GO_0035500 obo:go.owl obo:GO_0035500 rfoulger obo:GO_0035500 2010-04-29T03:14:32Z obo:GO_0035500 MAD homology 2 domain binding obo:GO_0035500 molecular_function obo:GO_0035500 GO:0035500 obo:GO_0035500 MH2 domain binding obo:GO_0035501 Interacting selectively and non-covalently with the MH1 (MAD homology 1) domain of a protein. The MH1 domain is found at the amino terminus of MAD related proteins such as Smads and can mediate DNA binding in some proteins. Smads also use the MH1 domain to interact with some transcription factors. obo:GO_0035501 obo:go.owl obo:GO_0035501 rfoulger obo:GO_0035501 2010-04-29T03:17:27Z obo:GO_0035501 MAD homology 1 domain binding obo:GO_0035501 molecular_function obo:GO_0035501 GO:0035501 obo:GO_0035501 MH1 domain binding obo:GO_0035538 Interacting selectively and non-covalently with the carbohydrate response element (ChoRE) found in the promoters of genes whose expression is regulated in response to carbohydrates, such as the triglyceride synthesis genes. obo:GO_0035538 obo:go.owl obo:GO_0035538 rfoulger obo:GO_0035538 2010-05-07T10:48:30Z obo:GO_0035538 ChoRE binding obo:GO_0035538 molecular_function obo:GO_0035538 GO:0035538 obo:GO_0035538 Note that as agreed during the transcription overhaul, terms specifying binding to specific transcription regulatory motifs are no longer being created. The level of specificity GO has decided to go to is the "core promoter", "core promoter proximal region" and "enhancer". To capture more detail, please consider using column 16. obo:GO_0035538 carbohydrate response element binding obo:GO_0035594 Interacting selectively and non-covalently with a ganglioside, a ceramide oligosaccharide carrying in addition to other sugar residues, one or more sialic acid residues. obo:GO_0035594 obo:go.owl obo:GO_0035594 rfoulger obo:GO_0035594 2010-11-11T02:11:38Z obo:GO_0035594 molecular_function obo:GO_0035594 GO:0035594 obo:GO_0035594 ganglioside binding obo:GO_0035596 Catalysis of the addition of a methylthioether group (-SCH3) to a nucleic acid or protein acceptor. obo:GO_0035596 obo:go.owl obo:GO_0035596 rfoulger obo:GO_0035596 2010-11-12T01:24:38Z obo:GO_0035596 MTTase obo:GO_0035596 molecular_function obo:GO_0035596 GO:0035596 obo:GO_0035596 methylthiotransferase activity obo:GO_0035612 Interacting selectively and non-covalently with the AP-2 adaptor complex. The AP-2 adaptor complex is a heterotetrameric AP-type membrane coat adaptor complex that consists of alpha, beta2, mu2 and sigma2 subunits and links clathrin to the membrane surface of a vesicle. In at least humans, the AP-2 complex can be heterogeneric due to the existence of multiple subunit isoforms encoded by different alpha genes (alphaA and alphaC). obo:GO_0035612 obo:go.owl obo:GO_0035612 rfoulger obo:GO_0035612 2010-11-25T03:51:17Z obo:GO_0035612 molecular_function obo:GO_0035612 AP-2 clathrin adaptor complex binding obo:GO_0035612 GO:0035612 obo:GO_0035612 AP-2 adaptor complex binding obo:GO_0035613 Interacting selectively and non-covalently with a stem-loop in an RNA molecule. An RNA stem-loop is a secondary RNA structure consisting of a double-stranded RNA (dsRNA) stem and a terminal loop. obo:GO_0035613 obo:go.owl obo:GO_0035613 rfoulger obo:GO_0035613 2010-11-26T10:41:49Z obo:GO_0035613 RNA hairpin binding obo:GO_0035613 RNA hairpin loop binding obo:GO_0035613 molecular_function obo:GO_0035613 GO:0035613 obo:GO_0035613 RNA stem-loop binding obo:GO_0035614 Interacting selectively and non-covalently with a stem-loop in a small nuclear RNA (snRNA). An RNA stem-loop is a secondary RNA structure consisting of a double-stranded RNA (dsRNA) stem and a terminal loop. obo:GO_0035614 obo:go.owl obo:GO_0035614 rfoulger obo:GO_0035614 2010-11-26T10:43:17Z obo:GO_0035614 small nuclear RNA stem-loop binding obo:GO_0035614 snRNA hairpin binding obo:GO_0035614 snRNA hairpin loop binding obo:GO_0035614 molecular_function obo:GO_0035614 GO:0035614 obo:GO_0035614 snRNA stem-loop binding obo:GO_0035639 Interacting selectively and non-covalently with a purine ribonucleoside triphosphate, a compound consisting of a purine base linked to a ribose sugar esterified with triphosphate on the sugar. obo:GO_0035639 obo:go.owl obo:GO_0035639 rfoulger obo:GO_0035639 2011-01-14T02:46:42Z obo:GO_0035639 purine NTP binding obo:GO_0035639 molecular_function obo:GO_0035639 GO:0035639 obo:GO_0035639 purine ribonucleoside triphosphate binding obo:GO_0035650 Interacting selectively and non-covalently with the AP-1 adaptor complex. The AP-1 adaptor complex is a heterotetrameric AP-type membrane coat adaptor complex that consists of beta1, gamma, mu1 and sigma1 subunits and links clathrin to the membrane surface of a vesicle. In at least humans, the AP-1 complex can be heterogeneric due to the existence of multiple subunit isoforms encoded by different genes (gamma1 and gamma2, mu1A and mu1B, and sigma1A, sigma1B and sigma1C). obo:GO_0035650 obo:go.owl obo:GO_0035650 rfoulger obo:GO_0035650 2011-01-25T10:58:52Z obo:GO_0035650 molecular_function obo:GO_0035650 GO:0035650 obo:GO_0035650 AP-1 adaptor complex binding obo:GO_0035651 Interacting selectively and non-covalently with the AP-3 adaptor complex. The AP-3 adaptor complex is a heterotetrameric AP-type membrane coat adaptor complex that consists of beta3, delta, mu3 and sigma3 subunits and is found associated with endosomal membranes. In at least humans, the AP-3 complex can be heterogeneric due to the existence of multiple subunit isoforms encoded by different genes (beta3A and beta3B, mu3A and mu3B, and sigma3A and sigma3B). obo:GO_0035651 obo:go.owl obo:GO_0035651 rfoulger obo:GO_0035651 2011-01-25T10:59:36Z obo:GO_0035651 molecular_function obo:GO_0035651 GO:0035651 obo:GO_0035651 AP-3 adaptor complex binding obo:GO_0035662 Interacting selectively and non-covalently with a Toll-like 4 protein, a pattern recognition receptor that binds bacterial lipopolysaccharide (LPS) to initiate an innate immune response. obo:GO_0035662 obo:go.owl obo:GO_0035662 rfoulger obo:GO_0035662 2011-02-01T10:20:59Z obo:GO_0035662 TLR4 binding obo:GO_0035662 molecular_function obo:GO_0035662 GO:0035662 obo:GO_0035662 Toll-like receptor 4 binding obo:GO_0035663 Interacting selectively and non-covalently with a Toll-like 2 protein, a pattern recognition receptor that binds microbial pattern motifs to initiate an innate immune response. obo:GO_0035663 obo:go.owl obo:GO_0035663 rfoulger obo:GO_0035663 2011-02-01T10:21:51Z obo:GO_0035663 TLR2 binding obo:GO_0035663 molecular_function obo:GO_0035663 GO:0035663 obo:GO_0035663 Toll-like receptor 2 binding obo:GO_0035715 Interacting selectively and non-covalently with chemokine (C-C motif) ligand 2. obo:GO_0035715 obo:go.owl obo:GO_0035715 rfoulger obo:GO_0035715 2011-03-03T04:24:24Z obo:GO_0035715 CCL2 binding obo:GO_0035715 molecular_function obo:GO_0035715 GO:0035715 obo:GO_0035715 chemokine (C-C motif) ligand 2 binding obo:GO_0035716 Interacting selectively and non-covalently with chemokine (C-C motif) ligand 12. obo:GO_0035716 obo:go.owl obo:GO_0035716 rfoulger obo:GO_0035716 2011-03-03T04:25:01Z obo:GO_0035716 CCL12 binding obo:GO_0035716 molecular_function obo:GO_0035716 GO:0035716 obo:GO_0035716 chemokine (C-C motif) ligand 12 binding obo:GO_0035717 Interacting selectively and non-covalently with chemokine (C-C motif) ligand 7. obo:GO_0035717 obo:go.owl obo:GO_0035717 rfoulger obo:GO_0035717 2011-03-03T04:25:41Z obo:GO_0035717 CCL7 binding obo:GO_0035717 molecular_function obo:GO_0035717 GO:0035717 obo:GO_0035717 chemokine (C-C motif) ligand 7 binding obo:GO_0035718 Interacting selectively and non-covalently with the cytokine, macrophage migration inhibitory factor. obo:GO_0035718 obo:go.owl obo:GO_0035718 rfoulger obo:GO_0035718 2011-03-03T04:27:16Z obo:GO_0035718 MIF binding obo:GO_0035718 molecular_function obo:GO_0035718 GO:0035718 obo:GO_0035718 macrophage migration inhibitory factor binding obo:GO_0035725 A process in which a sodium ion is transported from one side of a membrane to the other by means of some agent such as a transporter or pore. obo:GO_0035725 obo:go.owl obo:GO_0035725 rfoulger obo:GO_0035725 2011-03-10T02:52:36Z obo:GO_0035725 sodium ion membrane transport obo:GO_0035725 biological_process obo:GO_0035725 GO:0035725 obo:GO_0035725 Note that this term is not intended for use in annotating lateral movement within membranes. obo:GO_0035725 sodium ion transmembrane transport obo:GO_0035727 Interacting selectively and non-covalently with lysophosphatidic acid (LPA), a phospholipid derivative that acts as a potent mitogen due to its activation of high-affinity G protein-coupled receptors. obo:GO_0035727 obo:go.owl obo:GO_0035727 rfoulger obo:GO_0035727 2011-03-10T03:00:05Z obo:GO_0035727 LPA binding obo:GO_0035727 molecular_function obo:GO_0035727 GO:0035727 obo:GO_0035727 lysophosphatidic acid binding obo:GO_0035730 Interacting selectively and non-covalently with S-nitrosoglutathione, a nitrosothiol considered to be a natural nitric oxide (NO) donor involved in S-nitrosylation, and in the storage and transport of nitric oxide in biological systems. obo:GO_0035730 obo:go.owl obo:GO_0035730 rfoulger obo:GO_0035730 2011-03-11T09:57:19Z obo:GO_0035730 GSNO binding obo:GO_0035730 molecular_function obo:GO_0035730 GO:0035730 obo:GO_0035730 S-nitrosoglutathione binding obo:GO_0035757 Interacting selectively and non-covalently with chemokine (C-C motif) ligand 19. obo:GO_0035757 obo:go.owl obo:GO_0035757 rfoulger obo:GO_0035757 2011-03-25T02:02:36Z obo:GO_0035757 CCL19 binding obo:GO_0035757 molecular_function obo:GO_0035757 GO:0035757 obo:GO_0035757 chemokine (C-C motif) ligand 19 binding obo:GO_0035758 Interacting selectively and non-covalently with chemokine (C-C motif) ligand 21. obo:GO_0035758 obo:go.owl obo:GO_0035758 rfoulger obo:GO_0035758 2011-03-25T02:03:53Z obo:GO_0035758 CCL21 binding obo:GO_0035758 molecular_function obo:GO_0035758 GO:0035758 obo:GO_0035758 chemokine (C-C motif) ligand 21 binding obo:GO_0035817 Any process where sodium ions are taken up from the collecting ducts and proximal and distal loops of the nephron, which contributes to decreasing the amount of sodium that is excreted in urine per unit time. obo:GO_0035817 obo:go.owl obo:GO_0035817 rfoulger obo:GO_0035817 2011-04-20T01:40:11Z obo:GO_0035817 biological_process obo:GO_0035817 GO:0035817 obo:GO_0035817 renal sodium ion absorption involved in negative regulation of renal sodium excretion obo:GO_0035851 Interacting selectively and non-covalently with a Krueppel-associated box (KRAB) domain of a protein. The approximately 75 amino acid KRAB domain is enriched in charged amino acids, and is found in the N-terminal regions of many zinc finger-containing transcription factors. obo:GO_0035851 obo:go.owl obo:GO_0035851 rfoulger obo:GO_0035851 2011-05-11T11:41:16Z obo:GO_0035851 KRAB domain binding obo:GO_0035851 Krueppel-associated box binding obo:GO_0035851 molecular_function obo:GO_0035851 GO:0035851 obo:GO_0035851 Krueppel-associated box domain binding obo:GO_0035874 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of copper ions. obo:GO_0035874 obo:go.owl obo:GO_0035874 rfoulger obo:GO_0035874 2011-05-31T09:28:47Z obo:GO_0035874 cellular response to copper starvation obo:GO_0035874 biological_process obo:GO_0035874 GO:0035874 obo:GO_0035874 cellular response to copper ion starvation obo:GO_0035877 Interacting selectively and non-covalently with a DED domain (death effector domain) of a protein, a homotypic protein interaction module composed of a bundle of six alpha-helices that is related in structure to the death domain (DD). obo:GO_0035877 obo:go.owl obo:GO_0035877 rfoulger obo:GO_0035877 2011-05-31T09:40:46Z obo:GO_0035877 DED binding obo:GO_0035877 molecular_function obo:GO_0035877 GO:0035877 obo:GO_0035877 For binding to the death domain, consider instead the term 'death domain binding ; GO:0070513'. obo:GO_0035877 death effector domain binding obo:GO_0035923 Interacting selectively and non-covalently with flurbiprofen. obo:GO_0035923 obo:go.owl obo:GO_0035923 rfoulger obo:GO_0035923 2011-07-15T03:53:53Z obo:GO_0035923 2-(2-fluoro-[1,1'-biphenyl-4-yl])propanoic acid binding obo:GO_0035923 molecular_function obo:GO_0035923 GO:0035923 obo:GO_0035923 flurbiprofen binding obo:GO_0035925 Interacting selectively and non-covalently with a region containing frequent adenine and uridine bases within the 3' untranslated region of a mRNA molecule. obo:GO_0035925 obo:go.owl obo:GO_0035925 rfoulger obo:GO_0035925 2011-07-19T09:30:18Z obo:GO_0035925 mRNA 3'-UTR adenylate/uridylate-rich element binding obo:GO_0035925 molecular_function obo:GO_0035925 GO:0035925 obo:GO_0035925 mRNA 3'-UTR AU-rich region binding obo:GO_0035939 Interacting selectively and non-covalently with a microsatellite, a repeat_region in DNA containing repeat units (2 to 4 base pairs) that is repeated multiple times in tandem. obo:GO_0035939 obo:go.owl obo:GO_0035939 rfoulger obo:GO_0035939 2011-07-20T01:26:26Z obo:GO_0035939 VNTR binding obo:GO_0035939 microsatellite DNA binding obo:GO_0035939 variable number tandem repeat binding obo:GO_0035939 molecular_function obo:GO_0035939 GO:0035939 obo:GO_0035939 microsatellite binding obo:GO_0035979 Catalysis of the transfer of a phosphate group to the serine-139 residue of the C-terminal tail of histone H2A. obo:GO_0035979 obo:go.owl obo:GO_0035979 rfoulger obo:GO_0035979 2011-08-22T01:13:34Z obo:GO_0035979 histone kinase activity (H2A.x-S139 specific) obo:GO_0035979 molecular_function obo:GO_0035979 GO:0035979 obo:GO_0035979 Residue 1 of histone H2A is taken as the first residue following removal of the initiating Methionine (Met). obo:GO_0035979 histone kinase activity (H2A-S139 specific) obo:GO_0036002 Interacting selectively and non-covalently with pre-messenger RNA (pre-mRNA), an intermediate molecule between DNA and protein that may contain introns and, at least in part, encodes one or more proteins. Introns are removed from pre-mRNA to form a mRNA molecule. obo:GO_0036002 obo:go.owl obo:GO_0036002 rfoulger obo:GO_0036002 2011-09-16T10:23:37Z obo:GO_0036002 molecular_function obo:GO_0036002 protein-coding primary transcript binding obo:GO_0036002 GO:0036002 obo:GO_0036002 pre-mRNA binding obo:GO_0036004 Interacting selectively and non-covalently with the GAF domain of a protein. obo:GO_0036004 obo:go.owl obo:GO_0036004 rfoulger obo:GO_0036004 2011-09-20T04:20:42Z obo:GO_0036004 molecular_function obo:GO_0036004 GO:0036004 obo:GO_0036004 GAF domain binding obo:GO_0036032 The negative regulation of cell adhesion process in which a neural crest cell physically separates from the rest of the neural tube. obo:GO_0036032 obo:go.owl obo:GO_0036032 rfoulger obo:GO_0036032 2011-10-31T03:50:30Z obo:GO_0036032 neural crest cell emigration obo:GO_0036032 neural crest cell individualization obo:GO_0036032 biological_process obo:GO_0036032 neural crest cell segregation obo:GO_0036032 GO:0036032 obo:GO_0036032 neural crest cell delamination obo:GO_0036033 Interacting selectively and non-covalently with a mediator complex. The mediator complex is a protein complex that interacts with the carboxy-terminal domain of the largest subunit of RNA polymerase II and plays an active role in transducing the signal from a transcription factor to the transcriptional machinery. The Saccharomyces complex contains several identifiable subcomplexes: a head domain comprising Srb2, -4, and -5, Med6, -8, and -11, and Rox3 proteins; a middle domain comprising Med1, -4, and -7, Nut1 and -2, Cse2, Rgr1, Soh1, and Srb7 proteins; a tail consisting of Gal11p, Med2p, Pgd1p, and Sin4p; and a regulatory subcomplex comprising Ssn2, -3, and -8, and Srb8 proteins. Metazoan mediator complexes have similar modular structures and include homologs of yeast Srb and Med proteins. obo:GO_0036033 obo:go.owl obo:GO_0036033 rfoulger obo:GO_0036033 2011-10-31T05:09:12Z obo:GO_0036033 molecular_function obo:GO_0036033 GO:0036033 obo:GO_0036033 mediator complex binding obo:GO_0036036 The negative regulation of cell adhesion process in which a cardiac neural crest cell physically separates from the rest of the neural tube. obo:GO_0036036 obo:go.owl obo:GO_0036036 rfoulger obo:GO_0036036 2011-11-02T05:23:29Z obo:GO_0036036 biological_process obo:GO_0036036 GO:0036036 obo:GO_0036036 cardiac neural crest cell delamination obo:GO_0036041 Interacting selectively and non-covalently with a long-chain fatty acid. A long-chain fatty acid is a fatty acid with a chain length between C13 and C22. obo:GO_0036041 obo:go.owl obo:GO_0036041 rfoulger obo:GO_0036041 2011-11-24T02:54:39Z obo:GO_0036041 long chain fatty acid binding obo:GO_0036041 molecular_function obo:GO_0036041 GO:0036041 obo:GO_0036041 long-chain fatty acid binding obo:GO_0036042 Interacting selectively and non-covalently with a long-chain fatty acyl-CoA. A long-chain fatty acyl-CoA is any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a long-chain fatty-acyl group. Long-chain fatty-acyl-CoAs have chain lengths of C13 or more. obo:GO_0036042 obo:go.owl obo:GO_0036042 rfoulger obo:GO_0036042 2011-11-24T04:31:09Z obo:GO_0036042 molecular_function obo:GO_0036042 GO:0036042 obo:GO_0036042 long-chain fatty acyl-CoA binding obo:GO_0036094 Interacting selectively and non-covalently with a small molecule, any low molecular weight, monomeric, non-encoded molecule. obo:GO_0036094 obo:go.owl obo:GO_0036094 rfoulger obo:GO_0036094 2012-01-17T04:20:34Z obo:GO_0036094 molecular_function obo:GO_0036094 GO:0036094 obo:GO_0036094 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_agr obo:GO_0036094 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_flybase_ribbon obo:GO_0036094 Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides. obo:GO_0036094 small molecule binding obo:GO_0036105 Interacting selectively and non-covalently with a class I peroxisomal membrane targeting sequence, any of several sequences of amino acids within a protein that can act as a signal for the localization of the protein into the peroxisome membrane in a PEX19-dependent manner. obo:GO_0036105 obo:go.owl obo:GO_0036105 rfoulger obo:GO_0036105 2012-01-27T02:02:22Z obo:GO_0036105 class 1 mPTS binding obo:GO_0036105 molecular_function obo:GO_0036105 PEX19-dependent mPTS binding obo:GO_0036105 GO:0036105 obo:GO_0036105 Currently identified mPTSs vary greatly in length, and cannot be distinguished by primary structure analysis, suggesting that the peroxisomal sorting information is not contained within a specific amino acid sequence. There do however appear to be two classes of mPTSs: class 1 mPTSs that are bound by PEX19 and imported in a PEX19-dependent manner, and class 2 mPTSs that are not bound by PEX19 and mediate protein import independently of PEX19. The two classes cannot be defined based on their amino acid sequence. obo:GO_0036105 peroxisome membrane class-1 targeting sequence binding obo:GO_0036106 Interacting selectively and non-covalently with a class II peroxisomal membrane targeting sequence, any of several sequences of amino acids within a protein that can act as a signal for the localization of the protein into the peroxisome membrane in a PEX19-independent manner. obo:GO_0036106 obo:go.owl obo:GO_0036106 rfoulger obo:GO_0036106 2012-01-27T02:02:22Z obo:GO_0036106 class 2 mPTS binding obo:GO_0036106 molecular_function obo:GO_0036106 PEX19-independent mPTS binding obo:GO_0036106 GO:0036106 obo:GO_0036106 Currently identified mPTSs vary greatly in length, and cannot be distinguished by primary structure analysis, suggesting that the peroxisomal sorting information is not contained within a specific amino acid sequence. There do however appear to be two classes of mPTSs: class 1 mPTSs that are bound by PEX19 and imported in a PEX19-dependent manner, and class 2 mPTSs that are not bound by PEX19 and mediate protein import independently of PEX19. The two classes cannot be defined based on their amino acid sequence. obo:GO_0036106 peroxisome membrane class-2 targeting sequence binding obo:GO_0036110 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of inositol. obo:GO_0036110 obo:go.owl obo:GO_0036110 rfoulger obo:GO_0036110 2012-02-15T10:46:07Z obo:GO_0036110 biological_process obo:GO_0036110 GO:0036110 obo:GO_0036110 cellular response to inositol starvation obo:GO_0036122 Interacting selectively and non-covalently with a member of the bone morphogenetic protein (BMP) family. obo:GO_0036122 obo:go.owl obo:GO_0036122 rfoulger obo:GO_0036122 2012-02-20T02:59:34Z obo:GO_0036122 bone morphogenetic protein binding obo:GO_0036122 molecular_function obo:GO_0036122 GO:0036122 obo:GO_0036122 BMP binding obo:GO_0036127 Interacting selectively and non-covalently with 3-sulfino-L-alanine (cysteine sulfinate). obo:GO_0036127 obo:go.owl obo:GO_0036127 rfoulger obo:GO_0036127 2012-02-28T03:15:40Z obo:GO_0036127 cysteine sulfinate binding obo:GO_0036127 molecular_function obo:GO_0036127 GO:0036127 obo:GO_0036127 3-sulfino-L-alanine binding obo:GO_0036143 Interacting selectively and non-covalently with a kringle domain. Kringle domains are protein domains that fold into large loops stabilized by 3 disulfide linkages, and are important in protein-protein interactions with blood coagulation factors. obo:GO_0036143 obo:go.owl obo:GO_0036143 rfoulger obo:GO_0036143 2012-03-09T09:49:43Z obo:GO_0036143 molecular_function obo:GO_0036143 GO:0036143 obo:GO_0036143 kringle domain binding obo:GO_0036173 Interacting selectively and non-covalently with the inorganic anion thiosulfate, a sulfur oxide that has formula O3S2. obo:GO_0036173 obo:go.owl obo:GO_0036173 rfoulger obo:GO_0036173 2012-03-29T10:38:15Z obo:GO_0036173 molecular_function obo:GO_0036173 GO:0036173 obo:GO_0036173 thiosulfate binding obo:GO_0036176 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a neutral pH (pH close to 7) stimulus. pH is a measure of the acidity or basicity of an aqueous solution. obo:GO_0036176 obo:go.owl obo:GO_0036176 rfoulger obo:GO_0036176 2012-03-29T01:38:00Z obo:GO_0036176 biological_process obo:GO_0036176 GO:0036176 obo:GO_0036176 response to neutral pH obo:GO_0036211 The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications). Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification). obo:GO_0036211 obo:go.owl obo:GO_0036211 rfoulger obo:GO_0036211 2012-04-26T01:47:12Z obo:GO_0036211 protein modification obo:GO_0036211 biological_process obo:GO_0036211 GO:0036211 obo:GO_0036211 protein modification process obo:GO_0036223 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of adenine. obo:GO_0036223 obo:go.owl obo:GO_0036223 rfoulger obo:GO_0036223 2012-05-09T02:26:52Z obo:GO_0036223 cellular response to adenine deprivation obo:GO_0036223 biological_process obo:GO_0036223 GO:0036223 obo:GO_0036223 cellular response to adenine starvation obo:GO_0036225 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of vitamin B1 (also called thiamin and thiamine). obo:GO_0036225 obo:go.owl obo:GO_0036225 rfoulger obo:GO_0036225 2012-05-09T02:35:55Z obo:GO_0036225 cellular response to thiamin starvation obo:GO_0036225 cellular response to vitamin B1 deprivation obo:GO_0036225 biological_process obo:GO_0036225 GO:0036225 obo:GO_0036225 cellular response to vitamin B1 starvation obo:GO_0036244 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a neutral pH (pH close to 7) stimulus. pH is a measure of the acidity or basicity of an aqueous solution. obo:GO_0036244 obo:go.owl obo:GO_0036244 rfoulger obo:GO_0036244 2012-05-28T10:21:03Z obo:GO_0036244 biological_process obo:GO_0036244 GO:0036244 obo:GO_0036244 cellular response to neutral pH obo:GO_0036249 The directed movement of cadmium ions into the vacuole. obo:GO_0036249 obo:go.owl obo:GO_0036249 rfoulger obo:GO_0036249 2012-05-31T11:13:44Z obo:GO_0036249 biological_process obo:GO_0036249 vacuolar cadmium import obo:GO_0036249 GO:0036249 obo:GO_0036249 cadmium ion import into vacuole obo:GO_0036289 The phosphorylation by a protein of one or more of its own serine amino acid residues, or a serine residue on an identical protein. obo:GO_0036289 obo:go.owl obo:GO_0036289 rfoulger obo:GO_0036289 2012-07-18T10:24:32Z obo:GO_0036289 serine autophosphorylation obo:GO_0036289 biological_process obo:GO_0036289 GO:0036289 obo:GO_0036289 peptidyl-serine autophosphorylation obo:GO_0036290 The phosphorylation by a protein of a residue on an identical protein. For example, phosphorylation by the other kinase within a homodimer. obo:GO_0036290 obo:go.owl obo:GO_0036290 rfoulger obo:GO_0036290 2012-07-18T10:27:06Z obo:GO_0036290 trans-autophosphorylation obo:GO_0036290 biological_process obo:GO_0036290 GO:0036290 obo:GO_0036290 protein trans-autophosphorylation obo:GO_0036291 The phosphorylation by a protein of one or more of its own amino acid residues. obo:GO_0036291 obo:go.owl obo:GO_0036291 rfoulger obo:GO_0036291 2012-07-18T10:27:06Z obo:GO_0036291 cis-autophosphorylation obo:GO_0036291 biological_process obo:GO_0036291 GO:0036291 obo:GO_0036291 protein cis-autophosphorylation obo:GO_0036293 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus reflecting a decline in the level of oxygen. obo:GO_0036293 obo:go.owl obo:GO_0036293 rfoulger obo:GO_0036293 2012-07-20T01:05:46Z obo:GO_0036293 response to lowered oxygen levels obo:GO_0036293 biological_process obo:GO_0036293 GO:0036293 obo:GO_0036293 This term should be used when a decrease in oxygen levels is not considered a stress response. For a hypoxic stress response, consider instead 'response to hypoxia ; GO:0001666'. obo:GO_0036293 response to decreased oxygen levels obo:GO_0036294 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus reflecting a decline in the level of oxygen. obo:GO_0036294 obo:go.owl obo:GO_0036294 rfoulger obo:GO_0036294 2012-07-20T01:08:40Z obo:GO_0036294 cellular response to lowered oxygen levels obo:GO_0036294 biological_process obo:GO_0036294 GO:0036294 obo:GO_0036294 This term should be used when a decrease in oxygen levels is not considered a stress response. For a hypoxic stress response, consider instead 'cellular response to hypoxia ; GO:0071456'. obo:GO_0036294 cellular response to decreased oxygen levels obo:GO_0036295 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus reflecting an increase in the level of oxygen. obo:GO_0036295 obo:go.owl obo:GO_0036295 rfoulger obo:GO_0036295 2012-07-20T01:09:39Z obo:GO_0036295 cellular response to raised oxygen levels obo:GO_0036295 biological_process obo:GO_0036295 GO:0036295 obo:GO_0036295 This term should be used when an increase in oxygen levels is not considered a stress response. For a hyperoxic stress response, consider instead 'cellular response to hyperoxia ; GO:0071455'. obo:GO_0036295 cellular response to increased oxygen levels obo:GO_0036296 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus reflecting an increase in the level of oxygen. obo:GO_0036296 obo:go.owl obo:GO_0036296 rfoulger obo:GO_0036296 2012-07-20T01:10:48Z obo:GO_0036296 response to raised oxygen levels obo:GO_0036296 biological_process obo:GO_0036296 GO:0036296 obo:GO_0036296 This term should be used when an increase in oxygen levels is not considered a stress response. For a hyperoxic stress response, consider instead 'response to hyperoxia ; GO:0055093. obo:GO_0036296 response to increased oxygen levels obo:GO_0036297 Removal of a DNA interstrand crosslink (a covalent attachment of DNA bases on opposite strands of the DNA) and restoration of the DNA. DNA interstrand crosslinks occur when both strands of duplex DNA are covalently tethered together (e.g. by an exogenous or endogenous agent), thus preventing the strand unwinding necessary for essential DNA functions such as transcription and replication. obo:GO_0036297 obo:go.owl obo:GO_0036297 rfoulger obo:GO_0036297 2012-08-07T11:05:19Z obo:GO_0036297 ICL repair obo:GO_0036297 biological_process obo:GO_0036297 GO:0036297 obo:GO_0036297 interstrand cross-link repair obo:GO_0036298 Removal of a DNA interstrand crosslink (a covalent attachment of DNA bases on opposite strands of the DNA) and restoration of the DNA by a mechanism that involves the exchange, reciprocal or nonreciprocal, of genetic material between the broken DNA molecule and a homologous region of DNA. obo:GO_0036298 obo:go.owl obo:GO_0036298 rfoulger obo:GO_0036298 2012-08-07T11:11:59Z obo:GO_0036298 recombination-dependent interstrand cross-link repair obo:GO_0036298 biological_process obo:GO_0036298 GO:0036298 obo:GO_0036298 recombinational interstrand cross-link repair obo:GO_0036299 Removal of a DNA interstrand crosslink (a covalent attachment of DNA bases on opposite strands of the DNA) and restoration of the DNA by a mechanism that does not involve homologous DNA recombination. obo:GO_0036299 obo:go.owl obo:GO_0036299 rfoulger obo:GO_0036299 2012-08-07T11:11:59Z obo:GO_0036299 recombination-independent ICL repair obo:GO_0036299 recombination-independent interstrand cross-link repair obo:GO_0036299 biological_process obo:GO_0036299 GO:0036299 obo:GO_0036299 non-recombinational interstrand cross-link repair obo:GO_0036312 Interacting selectively and non-covalently with a regulatory subunit of phosphatidylinositol 3-kinase. The regulatory subunit associates with the catalytic subunit to regulate both its activity and subcellular location. obo:GO_0036312 obo:go.owl obo:GO_0036312 rfoulger obo:GO_0036312 2012-08-16T10:58:45Z obo:GO_0036312 PI3K regulatory subunit binding obo:GO_0036312 molecular_function obo:GO_0036312 p85 binding obo:GO_0036312 GO:0036312 obo:GO_0036312 phosphatidylinositol 3-kinase regulatory subunit binding obo:GO_0036313 Interacting selectively and non-covalently with the catalytic subunit of a phosphatidylinositol 3-kinase. The catalytic subunit catalyzes the addition of a phosphate group to an inositol lipid at the 3' position of the inositol ring. obo:GO_0036313 obo:go.owl obo:GO_0036313 rfoulger obo:GO_0036313 2012-08-16T10:58:45Z obo:GO_0036313 PI3K catalytic subunit binding obo:GO_0036313 molecular_function obo:GO_0036313 p110 binding obo:GO_0036313 GO:0036313 obo:GO_0036313 phosphatidylinositol 3-kinase catalytic subunit binding obo:GO_0036367 The ability of a photoreceptor to adjust to varying levels of light. obo:GO_0036367 obo:go.owl obo:GO_0036367 rfoulger obo:GO_0036367 2012-09-26T13:28:14Z obo:GO_0036367 biological_process obo:GO_0036367 GO:0036367 obo:GO_0036367 Light adaptation is usually a combination of cell desensitization and response acceleration. obo:GO_0036367 light adaption obo:GO_0036368 The processes required for a cone photoreceptor to recover, following light activation, so that it can respond to a subsequent light stimulus. Cone recovery requires the shutoff of active participants in the phototransduction cascade, including the visual pigment and downstream signal transducers. obo:GO_0036368 obo:go.owl obo:GO_0036368 rfoulger obo:GO_0036368 2012-09-26T14:35:20Z obo:GO_0036368 cone response recovery obo:GO_0036368 biological_process obo:GO_0036368 cone phototransduction termination obo:GO_0036368 GO:0036368 obo:GO_0036368 cone photoresponse recovery obo:GO_0036376 The directed movement of sodium ions from inside of a cell, across the plasma membrane and into the extracellular region. obo:GO_0036376 obo:go.owl obo:GO_0036376 midori obo:GO_0036376 2009-12-16T11:13:55Z obo:GO_0036376 GO:0071436 obo:GO_0036376 GO:0098667 obo:GO_0036376 sodium ion export from cell obo:GO_0036376 biological_process obo:GO_0036376 sodium export obo:GO_0036376 sodium ion export obo:GO_0036376 GO:0036376 obo:GO_0036376 sodium ion export across plasma membrane obo:GO_0036435 Interacting selectively and non-covalently with a protein upon poly-ubiquitination formed by linkages between lysine residues at position 48 in the target protein. obo:GO_0036435 obo:go.owl obo:GO_0036435 rfoulger obo:GO_0036435 2013-09-18T14:51:06Z obo:GO_0036435 Reactome:R-HSA-5683077 obo:GO_0036435 molecular_function obo:GO_0036435 GO:0036435 obo:GO_0036435 K48-linked polyubiquitin modification-dependent protein binding obo:GO_0036444 A process in which a calcium ion (Ca2+) is transported from the cytosol, into the mitochondrial matrix. obo:GO_0036444 obo:go.owl obo:GO_0036444 rfoulger obo:GO_0036444 2013-10-28T09:32:39Z obo:GO_0036444 calcium ion import into mitochondrion obo:GO_0036444 mitochondrial calcium ion import obo:GO_0036444 calcium ion transmembrane import into mitochondrion obo:GO_0036444 mitochondrial calcium uptake obo:GO_0036444 biological_process obo:GO_0036444 GO:0036444 obo:GO_0036444 calcium import into the mitochondrion obo:GO_0036458 Interacting selectively and non-covalently with a hepatocyte growth factor. obo:GO_0036458 obo:go.owl obo:GO_0036458 rfoulger obo:GO_0036458 2013-12-09T14:07:20Z obo:GO_0036458 HGF binding obo:GO_0036458 molecular_function obo:GO_0036458 GO:0036458 obo:GO_0036458 hepatocyte growth factor binding obo:GO_0036460 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of stress acting at the cell envelope. obo:GO_0036460 obo:go.owl obo:GO_0036460 rfoulger obo:GO_0036460 2014-01-08T15:15:50Z obo:GO_0036460 envelope stress response obo:GO_0036460 biological_process obo:GO_0036460 GO:0036460 obo:GO_0036460 cellular response to cell envelope stress obo:GO_0036461 Interacting selectively and non-covalently with a BLOC-2 complex, a protein complex required for the biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules. obo:GO_0036461 obo:go.owl obo:GO_0036461 rebeccafoulger obo:GO_0036461 2014-06-11T09:14:55Z obo:GO_0036461 molecular_function obo:GO_0036461 GO:0036461 obo:GO_0036461 BLOC-2 complex binding obo:GO_0038034 A series of molecular signals initiated by the absence of a ligand or the withdrawal of a ligand from a receptor. obo:GO_0038034 obo:go.owl obo:GO_0038034 rfoulger obo:GO_0038034 2011-10-26T02:21:03Z obo:GO_0038034 addiction receptor signaling pathway obo:GO_0038034 dependence receptor signaling pathway obo:GO_0038034 non-classical signal transduction obo:GO_0038034 signal transduction in absence of agonist obo:GO_0038034 basal signaling obo:GO_0038034 biological_process obo:GO_0038034 negative signal transduction obo:GO_0038034 GO:0038034 obo:GO_0038034 signal transduction in absence of ligand obo:GO_0038057 Interacting selectively and non-covalently with tumor necrosis factor ligand superfamily member 11 (TNFSF11), a member of the tumor necrosis factor (TNF) cytokine family. obo:GO_0038057 obo:go.owl obo:GO_0038057 rfoulger obo:GO_0038057 2012-01-04T03:25:59Z obo:GO_0038057 CD254 binding obo:GO_0038057 ODF binding obo:GO_0038057 OPGL binding obo:GO_0038057 RANKL binding obo:GO_0038057 TNF-related activation-induced cytokine binding obo:GO_0038057 TRANCE binding obo:GO_0038057 osteoclast differentiation factor binding obo:GO_0038057 osteoprotegerin ligand binding obo:GO_0038057 receptor activator of nuclear factor kappa-B ligand binding obo:GO_0038057 tumor necrosis factor (ligand) superfamily member 11 binding obo:GO_0038057 tumor necrosis factor ligand superfamily member 11 binding obo:GO_0038057 tumor necrosis factor superfamily member 11 binding obo:GO_0038057 molecular_function obo:GO_0038057 GO:0038057 obo:GO_0038057 TNFSF11 binding obo:GO_0038075 Catalysis of the reaction: protein + ATP = protein phosphate + ADP by a mitogen-activated protein kinase, as part of a MAPK signaling cascade that contributes to an innate immune response. obo:GO_0038075 obo:go.owl obo:GO_0038075 rfoulger obo:GO_0038075 2012-01-26T02:35:52Z obo:GO_0038075 MAPK activity involved in innate immune response obo:GO_0038075 molecular_function obo:GO_0038075 GO:0038075 obo:GO_0038075 MAP kinase activity involved in innate immune response obo:GO_0038078 Catalysis of the reaction: a phosphorylated MAP kinase + H2O = a MAP kinase + phosphate, where the MAP kinase (MAPK) is part of a MAPK signaling cascade that contributes to an innate immune response. obo:GO_0038078 obo:go.owl obo:GO_0038078 rfoulger obo:GO_0038078 2012-01-26T02:35:52Z obo:GO_0038078 MAPK phosphatase activity involved in regulation of innate immune response obo:GO_0038078 molecular_function obo:GO_0038078 GO:0038078 obo:GO_0038078 MAP kinase phosphatase activity involved in regulation of innate immune response obo:GO_0038083 The phosphorylation by a protein of one or more of its own tyrosine amino acid residues, or a tyrosine residue on an identical protein. obo:GO_0038083 obo:go.owl obo:GO_0038083 rfoulger obo:GO_0038083 2012-02-01T02:14:18Z obo:GO_0038083 tyrosine autophosphorylation obo:GO_0038083 RTK autophosphorylation obo:GO_0038083 receptor tyrosine kinase autophosphorylation obo:GO_0038083 biological_process obo:GO_0038083 GO:0038083 obo:GO_0038083 peptidyl-tyrosine autophosphorylation obo:GO_0038085 Interacting selectively and non-covalently with a vascular endothelial growth factor. obo:GO_0038085 obo:go.owl obo:GO_0038085 rfoulger obo:GO_0038085 2012-02-01T02:36:36Z obo:GO_0038085 VEGF binding obo:GO_0038085 molecular_function obo:GO_0038085 GO:0038085 obo:GO_0038085 vascular endothelial growth factor binding obo:GO_0038100 Interacting selectively and non-covalently with a nodal protein, a member of the transforming growth factor-beta superfamily. obo:GO_0038100 obo:go.owl obo:GO_0038100 rfoulger obo:GO_0038100 2012-02-17T11:19:08Z obo:GO_0038100 molecular_function obo:GO_0038100 GO:0038100 obo:GO_0038100 nodal binding obo:GO_0038102 Interacting with an activin receptor complex to reduce the action of another ligand, the agonist. A receptor antagonist does not initiate signaling upon binding to a receptor, but instead blocks an agonist from binding to the receptor. obo:GO_0038102 obo:go.owl obo:GO_0038102 rfoulger obo:GO_0038102 2012-02-17T11:28:59Z obo:GO_0038102 molecular_function obo:GO_0038102 GO:0038102 obo:GO_0038102 This term refers to inhibition of a member of the activin receptor family; activin receptors bind to multiple ligands including activin and nodal. obo:GO_0038102 activin receptor antagonist activity obo:GO_0038103 Interacting with an activin receptor to reduce the action of the agonist nodal. A receptor antagonist does not initiate signaling upon binding to a receptor, but instead blocks an agonist from binding to the receptor. obo:GO_0038103 obo:go.owl obo:GO_0038103 rfoulger obo:GO_0038103 2012-02-17T11:30:21Z obo:GO_0038103 activin receptor antagonist activity involved in negative regulation of nodal signalling pathway obo:GO_0038103 nodal antagonist activity obo:GO_0038103 molecular_function obo:GO_0038103 GO:0038103 obo:GO_0038103 activin receptor antagonist activity involved in negative regulation of nodal signaling pathway obo:GO_0038106 Interacting selectively and non-covalently with choriogonadotropin hormone, a heterodimer, with an alpha subunit identical to that of luteinizing hormone (LH), follicle-stimulating hormone (FSH) and thyroid-stimulating hormone (TSH), and a unique beta subunit. obo:GO_0038106 obo:go.owl obo:GO_0038106 rfoulger obo:GO_0038106 2012-03-08T03:58:40Z obo:GO_0038106 chorionic gonadotrophin binding obo:GO_0038106 chorionic gonadotropin binding obo:GO_0038106 molecular_function obo:GO_0038106 GO:0038106 obo:GO_0038106 choriogonadotropin hormone binding obo:GO_0038132 Interacting selectively and non-covalently with a neuregulin, a member of the EGF family of growth factors. obo:GO_0038132 obo:go.owl obo:GO_0038132 rfoulger obo:GO_0038132 2012-03-30T10:59:56Z obo:GO_0038132 molecular_function obo:GO_0038132 GO:0038132 obo:GO_0038132 neuregulin binding obo:GO_0038177 Interacting with a death receptor such that the proportion of death receptors in an active form is increased. Ligand binding to a death receptor often induces a conformational change to activate the receptor. obo:GO_0038177 obo:go.owl obo:GO_0038177 rfoulger obo:GO_0038177 2012-09-20T12:52:00Z obo:GO_0038177 death receptor activator activity obo:GO_0038177 molecular_function obo:GO_0038177 GO:0038177 obo:GO_0038177 death receptor agonist activity obo:GO_0038191 Interacting selectively and non-covalently with a member of the neuropilin family. obo:GO_0038191 obo:go.owl obo:GO_0038191 rfoulger obo:GO_0038191 2013-08-01T16:11:33Z obo:GO_0038191 Nrp binding obo:GO_0038191 neuropilin-binding obo:GO_0038191 Nrp ligand obo:GO_0038191 molecular_function obo:GO_0038191 GO:0038191 obo:GO_0038191 neuropilin binding obo:GO_0039552 Interacting selectively and non-covalently with RIG-I, a cytosolic pattern recognition receptor that initiates an antiviral signaling pathway upon binding to viral RNA. obo:GO_0039552 obo:go.owl obo:GO_0039552 rfoulger obo:GO_0039552 2012-01-19T02:14:20Z obo:GO_0039552 DDX58 binding obo:GO_0039552 DDX58/RIG-I binding obo:GO_0039552 molecular_function obo:GO_0039552 GO:0039552 obo:GO_0039552 RIG-I binding obo:GO_0039556 Interacting selectively and non-covalently with MDA-5, a cytosolic pattern recognition receptor that initiates an antiviral signaling pathway upon binding to viral dsRNA. obo:GO_0039556 obo:go.owl obo:GO_0039556 rfoulger obo:GO_0039556 2012-03-09T04:12:33Z obo:GO_0039556 MDA5 binding obo:GO_0039556 molecular_function obo:GO_0039556 GO:0039556 obo:GO_0039556 MDA-5 binding obo:GO_0039706 Interacting selectively and non-covalently with a coreceptor. A coreceptor acts in cooperation with a primary receptor to transmit a signal within the cell. obo:GO_0039706 obo:go.owl obo:GO_0039706 rfoulger obo:GO_0039706 2013-11-25T14:41:42Z obo:GO_0039706 molecular_function obo:GO_0039706 GO:0039706 obo:GO_0039706 co-receptor binding obo:GO_0040007 The increase in size or mass of an entire organism, a part of an organism or a cell. obo:GO_0040007 obo:go.owl obo:GO_0040007 GO:0048590 obo:GO_0040007 biological_process obo:GO_0040007 growth pattern obo:GO_0040007 non-developmental growth obo:GO_0040007 GO:0040007 obo:GO_0040007 http://purl.oboInOwllibrary.org/oboInOwl/go#gocheck_do_not_annotate obo:GO_0040007 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0040007 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0040007 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0040007 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0040007 See also the biological process term 'cell growth ; GO:0016049'. obo:GO_0040007 growth obo:GO_0040008 Any process that modulates the frequency, rate or extent of the growth of all or part of an organism so that it occurs at its proper speed, either globally or in a specific part of the organism's development. obo:GO_0040008 obo:go.owl obo:GO_0040008 biological_process obo:GO_0040008 GO:0040008 obo:GO_0040008 regulation of growth obo:GO_0040009 Any process that modulates the rate of growth of all or part of an organism. obo:GO_0040009 obo:go.owl obo:GO_0040009 biological_process obo:GO_0040009 GO:0040009 obo:GO_0040009 Note that this term and its definition depart from the usual conventions for GO 'regulation' process terms; regulation of rate is not usually distinguished from regulation of extent or frequency, but it makes sense to do so for growth regulation. obo:GO_0040009 regulation of growth rate obo:GO_0040010 Any process that increases the rate of growth of all or part of an organism. obo:GO_0040010 obo:go.owl obo:GO_0040010 up regulation of growth rate obo:GO_0040010 up-regulation of growth rate obo:GO_0040010 upregulation of growth rate obo:GO_0040010 activation of growth rate obo:GO_0040010 stimulation of growth rate obo:GO_0040010 biological_process obo:GO_0040010 GO:0040010 obo:GO_0040010 Note that this term and its definition depart from the usual conventions for GO 'regulation' process terms; regulation of rate is not usually distinguished from regulation of extent or frequency, but it makes sense to do so for growth regulation. obo:GO_0040010 positive regulation of growth rate obo:GO_0040012 Any process that modulates the frequency, rate or extent of locomotion of a cell or organism. obo:GO_0040012 obo:go.owl obo:GO_0040012 biological_process obo:GO_0040012 GO:0040012 obo:GO_0040012 regulation of locomotion obo:GO_0040013 Any process that stops, prevents, or reduces the frequency, rate or extent of locomotion of a cell or organism. obo:GO_0040013 obo:go.owl obo:GO_0040013 down regulation of locomotion obo:GO_0040013 down-regulation of locomotion obo:GO_0040013 downregulation of locomotion obo:GO_0040013 inhibition of locomotion obo:GO_0040013 biological_process obo:GO_0040013 GO:0040013 obo:GO_0040013 negative regulation of locomotion obo:GO_0040017 Any process that activates or increases the frequency, rate or extent of locomotion of a cell or organism. obo:GO_0040017 obo:go.owl obo:GO_0040017 up regulation of locomotion obo:GO_0040017 up-regulation of locomotion obo:GO_0040017 upregulation of locomotion obo:GO_0040017 activation of locomotion obo:GO_0040017 stimulation of locomotion obo:GO_0040017 biological_process obo:GO_0040017 GO:0040017 obo:GO_0040017 positive regulation of locomotion obo:GO_0042007 Interacting selectively and non-covalently with interleukin-18. obo:GO_0042007 obo:go.owl obo:GO_0042007 IL-18 binding obo:GO_0042007 molecular_function obo:GO_0042007 GO:0042007 obo:GO_0042007 interleukin-18 binding obo:GO_0042009 Interacting selectively and non-covalently with interleukin-15. obo:GO_0042009 obo:go.owl obo:GO_0042009 IL-15 binding obo:GO_0042009 molecular_function obo:GO_0042009 GO:0042009 obo:GO_0042009 interleukin-15 binding obo:GO_0042011 Interacting selectively and non-covalently with interleukin-16. obo:GO_0042011 obo:go.owl obo:GO_0042011 IL-16 binding obo:GO_0042011 molecular_function obo:GO_0042011 GO:0042011 obo:GO_0042011 interleukin-16 binding obo:GO_0042013 Interacting selectively and non-covalently with interleukin-19. obo:GO_0042013 obo:go.owl obo:GO_0042013 IL-19 binding obo:GO_0042013 molecular_function obo:GO_0042013 GO:0042013 obo:GO_0042013 interleukin-19 binding obo:GO_0042015 Interacting selectively and non-covalently with interleukin-20. obo:GO_0042015 obo:go.owl obo:GO_0042015 IL-20 binding obo:GO_0042015 molecular_function obo:GO_0042015 GO:0042015 obo:GO_0042015 interleukin-20 binding obo:GO_0042017 Interacting selectively and non-covalently with interleukin-22. obo:GO_0042017 obo:go.owl obo:GO_0042017 IL-22 binding obo:GO_0042017 molecular_function obo:GO_0042017 GO:0042017 obo:GO_0042017 interleukin-22 binding obo:GO_0042019 Interacting selectively and non-covalently with interleukin-23. obo:GO_0042019 obo:go.owl obo:GO_0042019 IL-23 binding obo:GO_0042019 molecular_function obo:GO_0042019 GO:0042019 obo:GO_0042019 interleukin-23 binding obo:GO_0042021 Interacting selectively and non-covalently with the granulocyte macrophage colony-stimulating factor complex. obo:GO_0042021 obo:go.owl obo:GO_0042021 GM-CSF complex binding obo:GO_0042021 GMC-SF complex binding obo:GO_0042021 granulocyte macrophage colony stimulating factor complex binding obo:GO_0042021 molecular_function obo:GO_0042021 GO:0042021 obo:GO_0042021 granulocyte macrophage colony-stimulating factor complex binding obo:GO_0042043 Interacting selectively and non-covalently with neurexins, synaptic cell surface proteins related to latrotoxin receptor, laminin and agrin. Neurexins act as cell recognition molecules at nerve terminals. obo:GO_0042043 obo:go.owl obo:GO_0042043 GO:0019963 obo:GO_0042043 molecular_function obo:GO_0042043 neuroligin obo:GO_0042043 GO:0042043 obo:GO_0042043 neurexin family protein binding obo:GO_0042056 Providing the environmental signal that initiates the directed movement of a motile cell or organism towards a higher concentration of that signal. obo:GO_0042056 obo:go.owl obo:GO_0042056 attractant obo:GO_0042056 molecular_function obo:GO_0042056 GO:0042056 obo:GO_0042056 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0042056 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0042056 chemoattractant activity obo:GO_0042127 Any process that modulates the frequency, rate or extent of cell proliferation. obo:GO_0042127 obo:go.owl obo:GO_0042127 biological_process obo:GO_0042127 regulation of cell proliferation obo:GO_0042127 GO:0042127 obo:GO_0042127 regulation of cell population proliferation obo:GO_0042134 Interacting selectively and non-covalently with an unprocessed ribosomal RNA transcript. obo:GO_0042134 obo:go.owl obo:GO_0042134 molecular_function obo:GO_0042134 GO:0042134 obo:GO_0042134 rRNA primary transcript binding obo:GO_0042149 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of glucose. obo:GO_0042149 obo:go.owl obo:GO_0042149 biological_process obo:GO_0042149 GO:0042149 obo:GO_0042149 cellular response to glucose starvation obo:GO_0042162 Interacting selectively and non-covalently with a telomere, a specific structure at the end of a linear chromosome required for the integrity and maintenance of the end. obo:GO_0042162 obo:go.owl obo:GO_0042162 telomere binding obo:GO_0042162 telomeric repeat binding obo:GO_0042162 molecular_function obo:GO_0042162 GO:0042162 obo:GO_0042162 telomeric DNA binding obo:GO_0042163 Interacting selectively and non-covalently with the beta subunit of interleukin-12. obo:GO_0042163 obo:go.owl obo:GO_0042163 CLMFp40 binding obo:GO_0042163 IL-12B binding obo:GO_0042163 IL-12p40 binding obo:GO_0042163 NKSFp40 binding obo:GO_0042163 molecular_function obo:GO_0042163 GO:0042163 obo:GO_0042163 interleukin-12 beta subunit binding obo:GO_0042164 Interacting selectively and non-covalently with the alpha subunit of interleukin-12. obo:GO_0042164 obo:go.owl obo:GO_0042164 CLMFp35 binding obo:GO_0042164 IL-12A binding obo:GO_0042164 IL-12p35 binding obo:GO_0042164 NKSFp35 binding obo:GO_0042164 molecular_function obo:GO_0042164 GO:0042164 obo:GO_0042164 interleukin-12 alpha subunit binding obo:GO_0042169 Interacting selectively and non-covalently with a SH2 domain (Src homology 2) of a protein, a protein domain of about 100 amino-acid residues and belonging to the alpha + beta domain class. obo:GO_0042169 obo:go.owl obo:GO_0042169 molecular_function obo:GO_0042169 GO:0042169 obo:GO_0042169 SH2 domain binding obo:GO_0042221 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a chemical stimulus. obo:GO_0042221 obo:go.owl obo:GO_0042221 MIPS_funcat:34.11.03 obo:GO_0042221 MIPS_funcat:34.11.03.05 obo:GO_0042221 MIPS_funcat:36.20.35.09 obo:GO_0042221 response to chemical stimulus obo:GO_0042221 response to chemical substance obo:GO_0042221 biological_process obo:GO_0042221 GO:0042221 obo:GO_0042221 http://purl.oboInOwllibrary.org/oboInOwl/go#gocheck_do_not_manually_annotate obo:GO_0042221 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_aspergillus obo:GO_0042221 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_candida obo:GO_0042221 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0042221 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0042221 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0042221 Note that this term is in the subset of terms that should not be used for direct gene product annotation. Instead, select a child term or, if no appropriate child term exists, please request a new term. Direct annotations to this term may be amended during annotation QC. obo:GO_0042221 response to chemical obo:GO_0042262 Any process in which DNA is protected from damage by, for example, oxidative stress. obo:GO_0042262 obo:go.owl obo:GO_0042262 biological_process obo:GO_0042262 GO:0042262 obo:GO_0042262 DNA protection obo:GO_0042275 The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA via processes such as template switching, which does not remove the replication-blocking lesions but does not increase the endogenous mutation rate. obo:GO_0042275 obo:go.owl obo:GO_0042275 error-free PRR obo:GO_0042275 biological_process obo:GO_0042275 error-free replication restart obo:GO_0042275 GO:0042275 obo:GO_0042275 Note that 'error-free' does not mean that literally zero errors occur during DNA synthesis, but that the error rate is low, comparable to that of DNA synthesis during replication. obo:GO_0042275 error-free postreplication DNA repair obo:GO_0042276 The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA after replication by using a specialized DNA polymerase or replication complex to insert a defined nucleotide across the lesion. This process does not remove the replication-blocking lesions and causes an increase in the endogenous mutation level. For example, in E. coli, a low fidelity DNA polymerase, pol V, copies lesions that block replication fork progress. This produces mutations specifically targeted to DNA template damage sites, but it can also produce mutations at undamaged sites. obo:GO_0042276 obo:go.owl obo:GO_0042276 mutagenic PRR obo:GO_0042276 biological_process obo:GO_0042276 error-prone postreplication DNA repair obo:GO_0042276 mutagenic postreplication DNA repair obo:GO_0042276 GO:0042276 obo:GO_0042276 error-prone translesion synthesis obo:GO_0042277 Interacting selectively and non-covalently with peptides, any of a group of organic compounds comprising two or more amino acids linked by peptide bonds. obo:GO_0042277 obo:go.owl obo:GO_0042277 MIPS_funcat:16.02 obo:GO_0042277 molecular_function obo:GO_0042277 GO:0042277 obo:GO_0042277 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0042277 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0042277 peptide binding obo:GO_0042285 Catalysis of the transfer of a xylosyl group to an acceptor molecule, typically another carbohydrate or a lipid. obo:GO_0042285 obo:go.owl obo:GO_0042285 molecular_function obo:GO_0042285 GO:0042285 obo:GO_0042285 xylosyltransferase activity obo:GO_0042287 Interacting selectively and non-covalently with major histocompatibility complex molecules; a set of molecules displayed on cell surfaces that are responsible for lymphocyte recognition and antigen presentation. obo:GO_0042287 obo:go.owl obo:GO_0042287 major histocompatibility complex binding obo:GO_0042287 major histocompatibility complex ligand obo:GO_0042287 molecular_function obo:GO_0042287 GO:0042287 obo:GO_0042287 Note that this term does not include binding to the antigen peptide bound to the MHC protein, for this also annotate to 'peptide antigen binding ; GO:0042605' or one of its children. obo:GO_0042287 MHC protein binding obo:GO_0042288 Interacting selectively and non-covalently with major histocompatibility complex class I molecules; a set of molecules displayed on cell surfaces that are responsible for lymphocyte recognition and antigen presentation. obo:GO_0042288 obo:go.owl obo:GO_0042288 major histocompatibility complex class I binding obo:GO_0042288 major histocompatibility complex class I ligand obo:GO_0042288 molecular_function obo:GO_0042288 T cell receptor activity obo:GO_0042288 alpha-beta T cell receptor activity obo:GO_0042288 gamma-delta T cell receptor activity obo:GO_0042288 GO:0042288 obo:GO_0042288 Note that this term does not include binding to the antigen peptide bound to the MHC protein. Consider also annotating to the molecular function term 'peptide antigen binding ; GO:0042605' or one of its children. obo:GO_0042288 MHC class I protein binding obo:GO_0042289 Interacting selectively and non-covalently with major histocompatibility complex class II molecules; a set of molecules displayed on cell surfaces that are responsible for lymphocyte recognition and antigen presentation. obo:GO_0042289 obo:go.owl obo:GO_0042289 major histocompatibility complex class II binding obo:GO_0042289 major histocompatibility complex class II ligand obo:GO_0042289 molecular_function obo:GO_0042289 GO:0042289 obo:GO_0042289 Note that this term does not include binding to the antigen peptide bound to the MHC protein. Consider also annotating to the molecular function term 'peptide antigen binding ; GO:0042605' or one of its children. obo:GO_0042289 MHC class II protein binding obo:GO_0042301 Interacting selectively and non-covalently with phosphate. obo:GO_0042301 obo:go.owl obo:GO_0042301 molecular_function obo:GO_0042301 GO:0042301 obo:GO_0042301 phosphate ion binding obo:GO_0042314 Interacting selectively and non-covalently with bacteriochlorophyll, a form of chlorophyll found in photosynthetic bacteria, such as the purple and green bacteria. There are several types, designated a to g. Bacteriochlorophyll a and bacteriochlorophyll b are structurally similar to the chlorophyll a and chlorophyll b found in plants. obo:GO_0042314 obo:go.owl obo:GO_0042314 molecular_function obo:GO_0042314 GO:0042314 obo:GO_0042314 bacteriochlorophyll binding obo:GO_0042324 Interacting selectively and non-covalently with the hypocretin receptor. obo:GO_0042324 obo:go.owl obo:GO_0042324 orexin receptor binding obo:GO_0042324 hypocretin receptor ligand obo:GO_0042324 orexin receptor ligand obo:GO_0042324 molecular_function obo:GO_0042324 GO:0042324 obo:GO_0042324 hypocretin receptor binding obo:GO_0042330 The directed movement of a motile cell or organism in response to an external stimulus. obo:GO_0042330 obo:go.owl obo:GO_0042330 Wikipedia:Taxis obo:GO_0042330 directed movement in response to stimulus obo:GO_0042330 biological_process obo:GO_0042330 GO:0042330 obo:GO_0042330 taxis obo:GO_0042379 Interacting selectively and non-covalently with any chemokine receptor. obo:GO_0042379 obo:go.owl obo:GO_0042379 chemokine receptor ligand obo:GO_0042379 molecular_function obo:GO_0042379 GO:0042379 obo:GO_0042379 chemokine receptor binding obo:GO_0042393 Interacting selectively and non-covalently with a histone, any of a group of water-soluble proteins found in association with the DNA of eukaroytic chromosomes. They are involved in the condensation and coiling of chromosomes during cell division and have also been implicated in nonspecific suppression of gene activity. obo:GO_0042393 obo:go.owl obo:GO_0042393 molecular_function obo:GO_0042393 histone-specific chaperone activity obo:GO_0042393 GO:0042393 obo:GO_0042393 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0042393 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0042393 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0042393 histone binding obo:GO_0042494 The series of events in which a bacterial lipoprotein stimulus is received by a cell and converted into a molecular signal. Bacterial lipoproteins are lipoproteins characterized by the presence of conserved sequence motifs called pathogen-associated molecular patterns (PAMPs). obo:GO_0042494 obo:go.owl obo:GO_0042494 biological_process obo:GO_0042494 detection of BLP obo:GO_0042494 detection of Lpp obo:GO_0042494 perception of BLP obo:GO_0042494 perception of Lpp obo:GO_0042494 perception of bacterial lipoprotein obo:GO_0042494 GO:0042494 obo:GO_0042494 detection of bacterial lipoprotein obo:GO_0042495 The series of events in which a triacylated bacterial lipoprotein stimulus is received by a cell and converted into a molecular signal. Triacylated bacterial lipoproteins are lipopeptides of bacterial origin containing a nonprotein moiety consisting of three acyl groups. obo:GO_0042495 obo:go.owl obo:GO_0042495 detection of triacylated bacterial lipoprotein obo:GO_0042495 biological_process obo:GO_0042495 perception of triacylated bacterial lipopeptide obo:GO_0042495 perception of triacylated bacterial lipoprotein obo:GO_0042495 GO:0042495 obo:GO_0042495 Note that bacterial lipopeptides are derived from bacterial lipoproteins, but the two terms are sometimes used interchangeably in the literature. obo:GO_0042495 detection of triacyl bacterial lipopeptide obo:GO_0042496 The series of events in which a diacylated bacterial lipopeptide stimulus is received by a cell and converted into a molecular signal. Diacylated bacterial lipoproteins are lipopeptides of bacterial origin containing a nonprotein moiety consisting of two acyl groups. obo:GO_0042496 obo:go.owl obo:GO_0042496 detection of diacylated bacterial lipoprotein obo:GO_0042496 biological_process obo:GO_0042496 perception of diacylated bacterial lipopeptide obo:GO_0042496 perception of diacylated bacterial lipoprotein obo:GO_0042496 GO:0042496 obo:GO_0042496 Note that bacterial lipopeptides are derived from bacterial lipoproteins, but the two terms are sometimes used interchangeably in the literature. obo:GO_0042496 detection of diacyl bacterial lipopeptide obo:GO_0042497 Interacting selectively and non-covalently with a lipopeptide containing a nonprotein moiety consisting of three acyl groups. obo:GO_0042497 obo:go.owl obo:GO_0042497 triacylated lipopeptide binding obo:GO_0042497 bacterial triacyl lipopeptide binding obo:GO_0042497 molecular_function obo:GO_0042497 bacterial triacyl lipoprotein binding obo:GO_0042497 GO:0042497 obo:GO_0042497 Note that bacterial lipopeptides are derived from bacterial lipoproteins, but the two terms are sometimes used interchangeably in the literature. obo:GO_0042497 triacyl lipopeptide binding obo:GO_0042498 Interacting selectively and non-covalently with a lipopeptide containing a nonprotein moiety consisting of two acyl groups. obo:GO_0042498 obo:go.owl obo:GO_0042498 diacylated lipopeptide binding obo:GO_0042498 bacterial diacyl lipopeptide binding obo:GO_0042498 molecular_function obo:GO_0042498 bacterial diacyl lipoprotein binding obo:GO_0042498 GO:0042498 obo:GO_0042498 Note that bacterial lipopeptides are derived from bacterial lipoproteins, but the two terms are sometimes used interchangeably in the literature. obo:GO_0042498 diacyl lipopeptide binding obo:GO_0042538 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, an increase in the concentration of salt (particularly but not exclusively sodium and chloride ions) in the environment. obo:GO_0042538 obo:go.owl obo:GO_0042538 response to hyperosmotic salt stress obo:GO_0042538 biological_process obo:GO_0042538 salt tolerance obo:GO_0042538 GO:0042538 obo:GO_0042538 hyperosmotic salinity response obo:GO_0042539 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, a decrease in the concentration of salt (particularly but not exclusively sodium and chloride ions) in the environment. obo:GO_0042539 obo:go.owl obo:GO_0042539 response to hypotonic salt stress obo:GO_0042539 biological_process obo:GO_0042539 GO:0042539 obo:GO_0042539 hypotonic salinity response obo:GO_0042562 Interacting selectively and non-covalently with any hormone, naturally occurring substances secreted by specialized cells that affect the metabolism or behavior of other cells possessing functional receptors for the hormone. obo:GO_0042562 obo:go.owl obo:GO_0042562 molecular_function obo:GO_0042562 GO:0042562 obo:GO_0042562 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0042562 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0042562 hormone binding obo:GO_0042578 Catalysis of the reaction: RPO-R' + H2O = RPOOH + R'H. This reaction is the hydrolysis of any phosphoric ester bond, any ester formed from orthophosphoric acid, O=P(OH)3. obo:GO_0042578 obo:go.owl obo:GO_0042578 EC:3.1 obo:GO_0042578 molecular_function obo:GO_0042578 GO:0042578 obo:GO_0042578 phosphoric ester hydrolase activity obo:GO_0042592 Any biological process involved in the maintenance of an internal steady state. obo:GO_0042592 obo:go.owl obo:GO_0042592 GO:0032844 obo:GO_0042592 GO:0032845 obo:GO_0042592 GO:0032846 obo:GO_0042592 homeostasis obo:GO_0042592 activation of homeostatic process obo:GO_0042592 inhibition of homeostatic process obo:GO_0042592 biological_process obo:GO_0042592 negative regulation of homeostatic process obo:GO_0042592 positive regulation of homeostatic process obo:GO_0042592 regulation of homeostatic process obo:GO_0042592 GO:0042592 obo:GO_0042592 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_agr obo:GO_0042592 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0042592 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0042592 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_mouse obo:GO_0042592 homeostatic process obo:GO_0042594 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a starvation stimulus, deprivation of nourishment. obo:GO_0042594 obo:go.owl obo:GO_0042594 MIPS_funcat:32.01.11 obo:GO_0042594 biological_process obo:GO_0042594 GO:0042594 obo:GO_0042594 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0042594 response to starvation obo:GO_0042595 Any process that results in a change in the behavior of an organism as a result of deprivation of nourishment. obo:GO_0042595 obo:go.owl obo:GO_0042595 behavioural response to starvation obo:GO_0042595 biological_process obo:GO_0042595 GO:0042595 obo:GO_0042595 behavioral response to starvation obo:GO_0042608 Interacting selectively and non-covalently with a T cell receptor, the antigen-recognizing receptor on the surface of T cells. obo:GO_0042608 obo:go.owl obo:GO_0042608 T lymphocyte receptor binding obo:GO_0042608 T-cell receptor binding obo:GO_0042608 T-lymphocyte receptor binding obo:GO_0042608 TCR binding obo:GO_0042608 molecular_function obo:GO_0042608 GO:0042608 obo:GO_0042608 T cell receptor binding obo:GO_0042609 Interacting selectively and non-covalently with a CD4, a receptor found on the surface of T cells, monocytes and macrophages. obo:GO_0042609 obo:go.owl obo:GO_0042609 molecular_function obo:GO_0042609 GO:0042609 obo:GO_0042609 CD4 receptor binding obo:GO_0042610 Interacting selectively and non-covalently with a CD8, a receptor found on the surface of thymocytes and cytotoxic and suppressor T-lymphocytes. obo:GO_0042610 obo:go.owl obo:GO_0042610 molecular_function obo:GO_0042610 GO:0042610 obo:GO_0042610 CD8 receptor binding obo:GO_0042614 Interacting selectively and non-covalently with a CD70, a receptor found on the surface of most activated B cells and some activated T cells. obo:GO_0042614 obo:go.owl obo:GO_0042614 CD27L binding obo:GO_0042614 molecular_function obo:GO_0042614 CD27 receptor activity obo:GO_0042614 GO:0042614 obo:GO_0042614 CD70 receptor binding obo:GO_0042615 Interacting selectively and non-covalently with CD154, a receptor found on the surface of some activated lymphocytes. obo:GO_0042615 obo:go.owl obo:GO_0042615 CD40L binding obo:GO_0042615 molecular_function obo:GO_0042615 CD40 receptor activity obo:GO_0042615 GO:0042615 obo:GO_0042615 CD154 receptor binding obo:GO_0042656 Catalysis of the phosphorylation and activation of JUN kinase kinase kinases (JNKKKs). obo:GO_0042656 obo:go.owl obo:GO_0042656 JUNKKKK activity obo:GO_0042656 molecular_function obo:GO_0042656 GO:0042656 obo:GO_0042656 JUN kinase kinase kinase kinase activity obo:GO_0042657 Interacting selectively and non-covalently with the lateral surface of major histocompatibility complex class II molecules. obo:GO_0042657 obo:go.owl obo:GO_0042657 major histocompatibility complex class II protein binding, via lateral surface obo:GO_0042657 molecular_function obo:GO_0042657 GO:0042657 obo:GO_0042657 MHC class II protein binding, via lateral surface obo:GO_0042658 Interacting selectively and non-covalently with the antigen binding groove of major histocompatibility complex class II molecules. obo:GO_0042658 obo:go.owl obo:GO_0042658 major histocompatibility complex class II protein binding, via antigen binding groove obo:GO_0042658 molecular_function obo:GO_0042658 GO:0042658 obo:GO_0042658 MHC class II protein binding, via antigen binding groove obo:GO_0042731 Interacting selectively and non-covalently with a PH domain (pleckstrin homology) of a protein, a domain of about 100 residues that occurs in a wide range of proteins involved in intracellular signaling or as constituents of the cytoskeleton. obo:GO_0042731 obo:go.owl obo:GO_0042731 molecular_function obo:GO_0042731 GO:0042731 obo:GO_0042731 PH domain binding obo:GO_0042769 The series of events required to receive a stimulus indicating DNA damage has occurred and convert it to a molecular signal. obo:GO_0042769 obo:go.owl obo:GO_0042769 detection of DNA damage during DNA damage response obo:GO_0042769 biological_process obo:GO_0042769 DNA damage response, perception of DNA damage obo:GO_0042769 GO:0042769 obo:GO_0042769 DNA damage response, detection of DNA damage obo:GO_0042776 The transport of protons across a mitochondrial membrane to generate an electrochemical gradient (proton-motive force) that powers ATP synthesis. obo:GO_0042776 obo:go.owl obo:GO_0042776 mitochondrial proton transport obo:GO_0042776 biological_process obo:GO_0042776 GO:0042776 obo:GO_0042776 mitochondrial ATP synthesis coupled proton transport obo:GO_0042777 The transport of protons across the plasma membrane to generate an electrochemical gradient (proton-motive force) that powers ATP synthesis. obo:GO_0042777 obo:go.owl obo:GO_0042777 ATP synthesis coupled proton transport obo:GO_0042777 biological_process obo:GO_0042777 GO:0042777 obo:GO_0042777 plasma membrane ATP synthesis coupled proton transport obo:GO_0042802 Interacting selectively and non-covalently with an identical protein or proteins. obo:GO_0042802 obo:go.owl obo:GO_0042802 isoform-specific homophilic binding obo:GO_0042802 molecular_function obo:GO_0042802 protein homopolymerization obo:GO_0042802 GO:0042802 obo:GO_0042802 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0042802 identical protein binding obo:GO_0042803 Interacting selectively and non-covalently with an identical protein to form a homodimer. obo:GO_0042803 obo:go.owl obo:GO_0042803 dimerization activity obo:GO_0042803 molecular_function obo:GO_0042803 GO:0042803 obo:GO_0042803 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0042803 protein homodimerization activity obo:GO_0042805 Interacting selectively and non-covalently with actinin, any member of a family of proteins that crosslink F-actin. obo:GO_0042805 obo:go.owl obo:GO_0042805 GO:0051406 obo:GO_0042805 capZ binding obo:GO_0042805 beta-actinin binding obo:GO_0042805 molecular_function obo:GO_0042805 GO:0042805 obo:GO_0042805 actinin binding obo:GO_0042806 Interacting selectively and non-covalently with fucose, the pentose 6-deoxygalactose. obo:GO_0042806 obo:go.owl obo:GO_0042806 molecular_function obo:GO_0042806 GO:0042806 obo:GO_0042806 fucose binding obo:GO_0042809 Interacting selectively and non-covalently with the vitamin D receptor, a nuclear receptor that mediates the action of vitamin D by binding DNA and controlling the transcription of hormone-sensitive genes. obo:GO_0042809 obo:go.owl obo:GO_0042809 VDR binding obo:GO_0042809 calciferol receptor binding obo:GO_0042809 molecular_function obo:GO_0042809 GO:0042809 obo:GO_0042809 vitamin D receptor binding obo:GO_0042826 Interacting selectively and non-covalently with the enzyme histone deacetylase. obo:GO_0042826 obo:go.owl obo:GO_0042826 molecular_function obo:GO_0042826 GO:0042826 obo:GO_0042826 histone deacetylase binding obo:GO_0042834 Interacting selectively and non-covalently, in a non-covalent manner, with peptidoglycan, any of a class of glycoconjugates found in bacterial cell walls. obo:GO_0042834 obo:go.owl obo:GO_0042834 molecular_function obo:GO_0042834 GO:0042834 obo:GO_0042834 peptidoglycan binding obo:GO_0042835 Interacting selectively and non-covalently with the RNA element BRE (Bruno response element). obo:GO_0042835 obo:go.owl obo:GO_0042835 molecular_function obo:GO_0042835 GO:0042835 obo:GO_0042835 BRE binding obo:GO_0042922 Interacting selectively and non-covalently with one or more specific sites on a neuromedin U receptor. obo:GO_0042922 obo:go.owl obo:GO_0042922 molecular_function obo:GO_0042922 GO:0042922 obo:GO_0042922 neuromedin U receptor binding obo:GO_0042923 Interacting selectively and non-covalently and stoichiometrically with neuropeptides, peptides with direct synaptic effects (peptide neurotransmitters) or indirect modulatory effects on the nervous system (peptide neuromodulators). obo:GO_0042923 obo:go.owl obo:GO_0042923 molecular_function obo:GO_0042923 GO:0042923 obo:GO_0042923 neuropeptide binding obo:GO_0042924 Interacting selectively and non-covalently and stoichiometrically with neuromedin U, a hypothalamic peptide involved in energy homeostasis and stress responses. obo:GO_0042924 obo:go.owl obo:GO_0042924 NMU binding obo:GO_0042924 molecular_function obo:GO_0042924 GO:0042924 obo:GO_0042924 neuromedin U binding obo:GO_0042930 The directed movement of the siderochrome enterobactin, a cyclic trimer of 2, 3 dihydroxybenzoylserine into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0042930 obo:go.owl obo:GO_0042930 enterochelin transport obo:GO_0042930 biological_process obo:GO_0042930 GO:0042930 obo:GO_0042930 enterobactin transport obo:GO_0042974 Interacting selectively and non-covalently with the retinoic acid receptor, a ligand-regulated transcription factor belonging to the nuclear receptor superfamily. obo:GO_0042974 obo:go.owl obo:GO_0042974 RAR binding obo:GO_0042974 molecular_function obo:GO_0042974 GO:0042974 obo:GO_0042974 retinoic acid receptor binding obo:GO_0042975 Interacting selectively and non-covalently with any of the peroxisome proliferator activated receptors, alpha, beta or gamma. obo:GO_0042975 obo:go.owl obo:GO_0042975 PPAR binding obo:GO_0042975 molecular_function obo:GO_0042975 GO:0042975 obo:GO_0042975 peroxisome proliferator activated receptor binding obo:GO_0042988 Interacting selectively and non-covalently with X11-like protein, a neuron-specific adaptor protein. obo:GO_0042988 obo:go.owl obo:GO_0042988 X11L binding obo:GO_0042988 molecular_function obo:GO_0042988 GO:0042988 obo:GO_0042988 X11-like protein binding obo:GO_0043008 Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules) using energy from the hydrolysis of ATP. obo:GO_0043008 obo:go.owl obo:GO_0043008 molecular_function obo:GO_0043008 GO:0043008 obo:GO_0043008 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0043008 ATP-dependent protein binding obo:GO_0043014 Interacting selectively and non-covalently with the microtubule constituent protein alpha-tubulin. obo:GO_0043014 obo:go.owl obo:GO_0043014 alpha tubulin binding obo:GO_0043014 molecular_function obo:GO_0043014 GO:0043014 obo:GO_0043014 alpha-tubulin binding obo:GO_0043015 Interacting selectively and non-covalently with the microtubule constituent protein gamma-tubulin. obo:GO_0043015 obo:go.owl obo:GO_0043015 gamma tubulin binding obo:GO_0043015 molecular_function obo:GO_0043015 GO:0043015 obo:GO_0043015 gamma-tubulin binding obo:GO_0043021 Interacting selectively and non-covalently with any complex of RNA and protein. obo:GO_0043021 obo:go.owl obo:GO_0043021 RNP binding obo:GO_0043021 protein-RNA complex binding obo:GO_0043021 ribonucleoprotein binding obo:GO_0043021 molecular_function obo:GO_0043021 GO:0043021 obo:GO_0043021 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0043021 ribonucleoprotein complex binding obo:GO_0043022 Interacting selectively and non-covalently with any part of a ribosome. obo:GO_0043022 obo:go.owl obo:GO_0043022 GO:0030376 obo:GO_0043022 ribosome receptor activity obo:GO_0043022 molecular_function obo:GO_0043022 GO:0043022 obo:GO_0043022 ribosome binding obo:GO_0043023 Interacting selectively and non-covalently with any part of the larger ribosomal subunit. obo:GO_0043023 obo:go.owl obo:GO_0043023 molecular_function obo:GO_0043023 GO:0043023 obo:GO_0043023 ribosomal large subunit binding obo:GO_0043024 Interacting selectively and non-covalently with any part of the small ribosomal subunit. obo:GO_0043024 obo:go.owl obo:GO_0043024 molecular_function obo:GO_0043024 GO:0043024 obo:GO_0043024 ribosomal small subunit binding obo:GO_0043047 Interacting selectively and non-covalently with single-stranded telomere-associated DNA. obo:GO_0043047 obo:go.owl obo:GO_0043047 telomeric ssDNA binding obo:GO_0043047 molecular_function obo:GO_0043047 GO:0043047 obo:GO_0043047 single-stranded telomeric DNA binding obo:GO_0043110 Interacting selectively and non-covalently with replication fork barriers found in rDNA spacers, sites that inhibit replication forks in the direction opposite to rDNA transcription. obo:GO_0043110 obo:go.owl obo:GO_0043110 RFB binding obo:GO_0043110 molecular_function obo:GO_0043110 GO:0043110 obo:GO_0043110 rDNA spacer replication fork barrier binding obo:GO_0043120 Interacting selectively and non-covalently with tumor necrosis factor, a proinflammatory cytokine produced by monocytes and macrophages. obo:GO_0043120 obo:go.owl obo:GO_0043120 molecular_function obo:GO_0043120 GO:0043120 obo:GO_0043120 tumor necrosis factor binding obo:GO_0043121 Interacting selectively and non-covalently with a neurotrophin, any of a family of growth factors that prevent apoptosis in neurons and promote nerve growth. obo:GO_0043121 obo:go.owl obo:GO_0043121 GO:0048404 obo:GO_0043121 GO:0048405 obo:GO_0043121 neurotrophic factor binding obo:GO_0043121 NT 4/5 binding obo:GO_0043121 NT-3 binding obo:GO_0043121 NT-4 binding obo:GO_0043121 NT-4/5 binding obo:GO_0043121 NT-5 binding obo:GO_0043121 NT3 binding obo:GO_0043121 NT4 binding obo:GO_0043121 NT5 binding obo:GO_0043121 neurotrophin 3 binding obo:GO_0043121 neurotrophin 4/5 binding obo:GO_0043121 neurotrophin-3 binding obo:GO_0043121 neurotrophin-4/5 binding obo:GO_0043121 molecular_function obo:GO_0043121 neurotrophin TRK receptor activity obo:GO_0043121 neurotrophin TRKA receptor activity obo:GO_0043121 neurotrophin TRKB receptor activity obo:GO_0043121 neurotrophin TRKC receptor activity obo:GO_0043121 GO:0043121 obo:GO_0043121 Note that mammalian NT-5 was initially named differently from amphibian NT-4 because of sequence differences, but the two genes were later shown to be functionally equivalent [SF:919858]. obo:GO_0043121 neurotrophin binding obo:GO_0043125 Interacting selectively and non-covalently with the protein-tyrosine kinase receptor ErbB-3/HER3. obo:GO_0043125 obo:go.owl obo:GO_0043125 HER3 receptor binding obo:GO_0043125 molecular_function obo:GO_0043125 Neu/ErbB-2 receptor activity obo:GO_0043125 GO:0043125 obo:GO_0043125 ErbB-3 class receptor binding obo:GO_0043130 Interacting selectively and non-covalently with ubiquitin, a protein that when covalently bound to other cellular proteins marks them for proteolytic degradation. obo:GO_0043130 obo:go.owl obo:GO_0043130 Reactome:R-HSA-1169404 obo:GO_0043130 Reactome:R-HSA-205008 obo:GO_0043130 Reactome:R-HSA-983152 obo:GO_0043130 molecular_function obo:GO_0043130 GO:0043130 obo:GO_0043130 ubiquitin binding obo:GO_0043157 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of cation stress, an increase or decrease in the concentration of positively charged ions in the environment. obo:GO_0043157 obo:go.owl obo:GO_0043157 biological_process obo:GO_0043157 GO:0043157 obo:GO_0043157 response to cation stress obo:GO_0043161 The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome. obo:GO_0043161 obo:go.owl obo:GO_0043161 MIPS_funcat:14.13.01.01 obo:GO_0043161 proteasomal pathway obo:GO_0043161 proteasomal ubiquitin-dependent protein breakdown obo:GO_0043161 proteasomal ubiquitin-dependent protein catabolic process obo:GO_0043161 proteasomal ubiquitin-dependent protein catabolism obo:GO_0043161 proteasomal ubiquitin-dependent protein degradation obo:GO_0043161 biological_process obo:GO_0043161 proteasomal processing obo:GO_0043161 proteasome pathway obo:GO_0043161 GO:0043161 obo:GO_0043161 proteasome-mediated ubiquitin-dependent protein catabolic process obo:GO_0043167 Interacting selectively and non-covalently with ions, charged atoms or groups of atoms. obo:GO_0043167 obo:go.owl obo:GO_0043167 molecular_function obo:GO_0043167 atom binding obo:GO_0043167 GO:0043167 obo:GO_0043167 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0043167 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0043167 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0043167 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0043167 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0043167 ion binding obo:GO_0043168 Interacting selectively and non-covalently with anions, charged atoms or groups of atoms with a net negative charge. obo:GO_0043168 obo:go.owl obo:GO_0043168 molecular_function obo:GO_0043168 GO:0043168 obo:GO_0043168 anion binding obo:GO_0043169 Interacting selectively and non-covalently with cations, charged atoms or groups of atoms with a net positive charge. obo:GO_0043169 obo:go.owl obo:GO_0043169 molecular_function obo:GO_0043169 GO:0043169 obo:GO_0043169 cation binding obo:GO_0043170 The chemical reactions and pathways involving macromolecules, any molecule of high relative molecular mass, the structure of which essentially comprises the multiple repetition of units derived, actually or conceptually, from molecules of low relative molecular mass. obo:GO_0043170 obo:go.owl obo:GO_0043170 GO:0043283 obo:GO_0043170 GO:0044259 obo:GO_0043170 biopolymer metabolic process obo:GO_0043170 macromolecule metabolism obo:GO_0043170 organismal macromolecule metabolism obo:GO_0043170 multicellular organismal macromolecule metabolic process obo:GO_0043170 biological_process obo:GO_0043170 GO:0043170 obo:GO_0043170 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0043170 macromolecule metabolic process obo:GO_0043175 Interacting selectively and non-covalently with an RNA polymerase core enzyme, containing a specific subunit composition defined as the core enzyme. obo:GO_0043175 obo:go.owl obo:GO_0043175 molecular_function obo:GO_0043175 GO:0043175 obo:GO_0043175 RNA polymerase core enzyme binding obo:GO_0043177 Interacting selectively and non-covalently with an organic acid, any acidic compound containing carbon in covalent linkage. obo:GO_0043177 obo:go.owl obo:GO_0043177 molecular_function obo:GO_0043177 GO:0043177 obo:GO_0043177 organic acid binding obo:GO_0043178 Interacting selectively and non-covalently with an alcohol, any of a class of alkyl compounds containing a hydroxyl group. obo:GO_0043178 obo:go.owl obo:GO_0043178 molecular_function obo:GO_0043178 GO:0043178 obo:GO_0043178 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0043178 alcohol binding obo:GO_0043183 Interacting selectively and non-covalently with vascular endothelial growth factor receptor 1. obo:GO_0043183 obo:go.owl obo:GO_0043183 Flt-1 binding obo:GO_0043183 VEGF receptor 1 binding obo:GO_0043183 VEGFR 1 binding obo:GO_0043183 molecular_function obo:GO_0043183 GO:0043183 obo:GO_0043183 vascular endothelial growth factor receptor 1 binding obo:GO_0043184 Interacting selectively and non-covalently with vascular endothelial growth factor receptor 2. obo:GO_0043184 obo:go.owl obo:GO_0043184 KDR binding obo:GO_0043184 Flk-1 binding obo:GO_0043184 VEGF receptor 2 binding obo:GO_0043184 VEGFR 2 binding obo:GO_0043184 kinase domain region binding obo:GO_0043184 molecular_function obo:GO_0043184 GO:0043184 obo:GO_0043184 vascular endothelial growth factor receptor 2 binding obo:GO_0043185 Interacting selectively and non-covalently with vascular endothelial growth factor receptor 3. obo:GO_0043185 obo:go.owl obo:GO_0043185 VEGF receptor 3 binding obo:GO_0043185 VEGFR 3 binding obo:GO_0043185 fms-like-tyrosine kinase (Flt)-4 binding obo:GO_0043185 molecular_function obo:GO_0043185 GO:0043185 obo:GO_0043185 vascular endothelial growth factor receptor 3 binding obo:GO_0043199 Interacting selectively and non-covalently with sulfate, SO4(2-), a negatively charged small molecule. obo:GO_0043199 obo:go.owl obo:GO_0043199 MIPS_funcat:16.12 obo:GO_0043199 molecular_function obo:GO_0043199 GO:0043199 obo:GO_0043199 sulfate binding obo:GO_0043207 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an external biotic stimulus, an external stimulus caused by, or produced by living things. obo:GO_0043207 obo:go.owl obo:GO_0043207 biological_process obo:GO_0043207 GO:0043207 obo:GO_0043207 response to external biotic stimulus obo:GO_0043208 Interacting selectively and non-covalently with glycosphingolipid, a compound with residues of sphingoid and at least one monosaccharide. obo:GO_0043208 obo:go.owl obo:GO_0043208 molecular_function obo:GO_0043208 GO:0043208 obo:GO_0043208 glycosphingolipid binding obo:GO_0043210 Interacting selectively and non-covalently with alkanesulfonates, the anion of alkanesulfonic acids, sulfonic acid derivatives containing an aliphatic hydrocarbon group. obo:GO_0043210 obo:go.owl obo:GO_0043210 molecular_function obo:GO_0043210 GO:0043210 obo:GO_0043210 alkanesulfonate binding obo:GO_0043221 Interacting selectively and non-covalently with any protein from the structural maintenance of chromosomes (SMC) family, a group of chromosomal ATPases with a role in mitotic chromosome organization. obo:GO_0043221 obo:go.owl obo:GO_0043221 structural maintenance of chromosomes family protein binding obo:GO_0043221 molecular_function obo:GO_0043221 GO:0043221 obo:GO_0043221 SMC family protein binding obo:GO_0043266 Any process that modulates the frequency, rate or extent of the directed movement of potassium ions (K+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0043266 obo:go.owl obo:GO_0043266 regulation of K+ transport obo:GO_0043266 regulation of potassium transport obo:GO_0043266 regulation of K+ conductance obo:GO_0043266 regulation of potassium conductance obo:GO_0043266 regulation of potassium ion conductance obo:GO_0043266 biological_process obo:GO_0043266 GO:0043266 obo:GO_0043266 regulation of potassium ion transport obo:GO_0043267 Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of potassium ions (K+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0043267 obo:go.owl obo:GO_0043267 down regulation of potassium ion transport obo:GO_0043267 down-regulation of potassium ion transport obo:GO_0043267 downregulation of potassium ion transport obo:GO_0043267 negative regulation of K+ transport obo:GO_0043267 negative regulation of potassium transport obo:GO_0043267 inhibition of potassium ion transport obo:GO_0043267 negative regulation of potassium ion conductance obo:GO_0043267 regulation of K+ conductance obo:GO_0043267 regulation of potassium conductance obo:GO_0043267 biological_process obo:GO_0043267 transmembrane conductance regulator activity obo:GO_0043267 GO:0043267 obo:GO_0043267 negative regulation of potassium ion transport obo:GO_0043268 Any process that activates or increases the frequency, rate or extent of the directed movement of potassium ions (K+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0043268 obo:go.owl obo:GO_0043268 positive regulation of K+ transport obo:GO_0043268 positive regulation of potassium transport obo:GO_0043268 up regulation of potassium ion transport obo:GO_0043268 up-regulation of potassium ion transport obo:GO_0043268 upregulation of potassium ion transport obo:GO_0043268 activation of potassium ion transport obo:GO_0043268 positive regulation of K+ conductance obo:GO_0043268 positive regulation of potassium conductance obo:GO_0043268 positive regulation of potassium ion conductance obo:GO_0043268 stimulation of potassium ion transport obo:GO_0043268 biological_process obo:GO_0043268 GO:0043268 obo:GO_0043268 positive regulation of potassium ion transport obo:GO_0043269 Any process that modulates the frequency, rate or extent of the directed movement of charged atoms or small charged molecules into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0043269 obo:go.owl obo:GO_0043269 biological_process obo:GO_0043269 GO:0043269 obo:GO_0043269 regulation of ion transport obo:GO_0043270 Any process that activates or increases the frequency, rate or extent of the directed movement of charged atoms or small charged molecules into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0043270 obo:go.owl obo:GO_0043270 up regulation of ion transport obo:GO_0043270 up-regulation of ion transport obo:GO_0043270 upregulation of ion transport obo:GO_0043270 activation of ion transport obo:GO_0043270 stimulation of ion transport obo:GO_0043270 biological_process obo:GO_0043270 GO:0043270 obo:GO_0043270 positive regulation of ion transport obo:GO_0043271 Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of charged atoms or small charged molecules into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0043271 obo:go.owl obo:GO_0043271 down regulation of ion transport obo:GO_0043271 down-regulation of ion transport obo:GO_0043271 downregulation of ion transport obo:GO_0043271 inhibition of ion transport obo:GO_0043271 biological_process obo:GO_0043271 GO:0043271 obo:GO_0043271 negative regulation of ion transport obo:GO_0043274 Interacting selectively and non-covalently with any phospholipase, enzymes that catalyze of the hydrolysis of a glycerophospholipid. obo:GO_0043274 obo:go.owl obo:GO_0043274 molecular_function obo:GO_0043274 GO:0043274 obo:GO_0043274 phospholipase binding obo:GO_0043295 Interacting selectively and non-covalently with glutathione; a tripeptide composed of the three amino acids cysteine, glutamic acid and glycine. obo:GO_0043295 obo:go.owl obo:GO_0043295 molecular_function obo:GO_0043295 GO:0043295 obo:GO_0043295 glutathione binding obo:GO_0043325 Interacting selectively and non-covalently with phosphatidylinositol-3,4-bisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3' and 4' positions. obo:GO_0043325 obo:go.owl obo:GO_0043325 molecular_function obo:GO_0043325 GO:0043325 obo:GO_0043325 phosphatidylinositol-3,4-bisphosphate binding obo:GO_0043394 Interacting selectively and non-covalently with a proteoglycan, any glycoprotein in which the carbohydrate units are glycosaminoglycans. obo:GO_0043394 obo:go.owl obo:GO_0043394 molecular_function obo:GO_0043394 GO:0043394 obo:GO_0043394 proteoglycan binding obo:GO_0043395 Interacting selectively and non-covalently with a heparan sulfate proteoglycan, any proteoglycan containing heparan sulfate as the glycosaminoglycan carbohydrate unit. obo:GO_0043395 obo:go.owl obo:GO_0043395 molecular_function obo:GO_0043395 heparin proteoglycan binding obo:GO_0043395 GO:0043395 obo:GO_0043395 heparan sulfate proteoglycan binding obo:GO_0043398 Interacting selectively and non-covalently with Helix Loop Helix, a domain of 40-50 residues that occurs in specific DNA-binding proteins that act as transcription factors. The domain is formed of two amphipathic helices joined by a variable length linker region that can form a loop and it mediates protein dimerization. obo:GO_0043398 obo:go.owl obo:GO_0043398 molecular_function obo:GO_0043398 GO:0043398 obo:GO_0043398 HLH domain binding obo:GO_0043412 The covalent alteration of one or more monomeric units in a polypeptide, polynucleotide, polysaccharide, or other biological macromolecule, resulting in a change in its properties. obo:GO_0043412 obo:go.owl obo:GO_0043412 biological_process obo:GO_0043412 GO:0043412 obo:GO_0043412 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0043412 macromolecule modification obo:GO_0043422 Interacting selectively and non-covalently with protein kinase B, an intracellular kinase that is important in regulating glucose metabolism. obo:GO_0043422 obo:go.owl obo:GO_0043422 Akt binding obo:GO_0043422 PKB binding obo:GO_0043422 molecular_function obo:GO_0043422 GO:0043422 obo:GO_0043422 protein kinase B binding obo:GO_0043423 Interacting selectively and non-covalently with a 3-phosphoinositide-dependent protein kinase. obo:GO_0043423 obo:go.owl obo:GO_0043423 phosphatidylinositol-3-phosphate-dependent protein kinase binding obo:GO_0043423 molecular_function obo:GO_0043423 GO:0043423 obo:GO_0043423 3-phosphoinositide-dependent protein kinase binding obo:GO_0043424 Interacting selectively and non-covalently with protein histidine kinase. obo:GO_0043424 obo:go.owl obo:GO_0043424 histidine kinase binding obo:GO_0043424 histidine-protein kinase binding obo:GO_0043424 protein-histidine kinase binding obo:GO_0043424 molecular_function obo:GO_0043424 GO:0043424 obo:GO_0043424 protein histidine kinase binding obo:GO_0043425 Interacting selectively and non-covalently with any of the basic Helix-Loop-Helix (bHLH) superfamily of transcription factors, important regulatory components in transcriptional networks of many developmental pathways. obo:GO_0043425 obo:go.owl obo:GO_0043425 molecular_function obo:GO_0043425 GO:0043425 obo:GO_0043425 bHLH transcription factor binding obo:GO_0043426 Interacting selectively and non-covalently with Myogenic Regulatory Factor (MRF), a member of the basic Helix-Loop-Helix (bHLH) superfamily of transcription factors. obo:GO_0043426 obo:go.owl obo:GO_0043426 GO:0051576 obo:GO_0043426 GO:0051577 obo:GO_0043426 GO:0051578 obo:GO_0043426 GO:0051579 obo:GO_0043426 Mrf4 binding obo:GO_0043426 Myf5 binding obo:GO_0043426 MyoD binding obo:GO_0043426 myogenin binding obo:GO_0043426 molecular_function obo:GO_0043426 GO:0043426 obo:GO_0043426 MRF binding obo:GO_0043472 Interacting selectively and non-covalently with an immunoglobulin of a D isotype. obo:GO_0043472 obo:go.owl obo:GO_0043472 molecular_function obo:GO_0043472 GO:0043472 obo:GO_0043472 IgD binding obo:GO_0043504 The process of restoring mitochondrial DNA after damage. obo:GO_0043504 obo:go.owl obo:GO_0043504 biological_process obo:GO_0043504 GO:0043504 obo:GO_0043504 mitochondrial DNA repair obo:GO_0043515 Interacting selectively and non-covalently with a kinetochore, a proteinaceous structure on a condensed chromosome, beside the centromere, to which the spindle fibers are attached. obo:GO_0043515 obo:go.owl obo:GO_0043515 molecular_function obo:GO_0043515 GO:0043515 obo:GO_0043515 kinetochore binding obo:GO_0043522 Interacting selectively and non-covalently with a leucine zipper domain, a protein secondary structure exhibiting a periodic repetition of leucine residues at every seventh position over a distance covering eight helical turns. obo:GO_0043522 obo:go.owl obo:GO_0043522 leucine zipper binding obo:GO_0043522 molecular_function obo:GO_0043522 GO:0043522 obo:GO_0043522 leucine zipper domain binding obo:GO_0043531 Interacting selectively and non-covalently with ADP, adenosine 5'-diphosphate. obo:GO_0043531 obo:go.owl obo:GO_0043531 adenosine 5'-diphosphate binding obo:GO_0043531 adenosine diphosphate binding obo:GO_0043531 molecular_function obo:GO_0043531 GO:0043531 obo:GO_0043531 ADP binding obo:GO_0043532 Interacting selectively and non-covalently with angiostatin, a proteolytic product of plasminogen or plasmin containing at least one intact kringle domain, and which is an inhibitor of angiogenesis. obo:GO_0043532 obo:go.owl obo:GO_0043532 molecular_function obo:GO_0043532 GO:0043532 obo:GO_0043532 angiostatin binding obo:GO_0043533 Interacting selectively and non-covalently with inositol 1,3,4,5 tetrakisphosphate. obo:GO_0043533 obo:go.owl obo:GO_0043533 IP4 binding obo:GO_0043533 InsP4 binding obo:GO_0043533 molecular_function obo:GO_0043533 GO:0043533 obo:GO_0043533 inositol 1,3,4,5 tetrakisphosphate binding obo:GO_0043544 Interacting selectively and non-covalently with lipoamide, the functional form of lipoic acid in which the carboxyl group is attached to protein by an amide linkage to a lysine amino group. obo:GO_0043544 obo:go.owl obo:GO_0043544 MIPS_funcat:16.21.13 obo:GO_0043544 molecular_function obo:GO_0043544 GO:0043544 obo:GO_0043544 lipoamide binding obo:GO_0043546 Interacting selectively and non-covalently with the molybdopterin cofactor (Moco), essential for the catalytic activity of some enzymes, e.g. sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. The cofactor consists of a mononuclear molybdenum (Mo-molybdopterin) or tungsten ion (W-molybdopterin) coordinated by one or two molybdopterin ligands. obo:GO_0043546 obo:go.owl obo:GO_0043546 MIPS_funcat:16.21.03 obo:GO_0043546 Moco binding obo:GO_0043546 molecular_function obo:GO_0043546 GO:0043546 obo:GO_0043546 molybdopterin cofactor binding obo:GO_0043548 Interacting selectively and non-covalently with a phosphatidylinositol 3-kinase, any enzyme that catalyzes the addition of a phosphate group to an inositol lipid at the 3' position of the inositol ring. obo:GO_0043548 obo:go.owl obo:GO_0043548 PI3K binding obo:GO_0043548 phosphoinositide 3-kinase binding obo:GO_0043548 molecular_function obo:GO_0043548 GO:0043548 obo:GO_0043548 phosphatidylinositol 3-kinase binding obo:GO_0043559 Interacting selectively and non-covalently with insulin, a polypeptide hormone produced by the islets of Langerhans of the pancreas in mammals, and by the homologous organs of other organisms. obo:GO_0043559 obo:go.owl obo:GO_0043559 molecular_function obo:GO_0043559 GO:0043559 obo:GO_0043559 insulin binding obo:GO_0043560 Interacting selectively and non-covalently with any of the insulin receptor substrate (IRS) proteins, adaptor proteins that bind to the transphosphorylated insulin and insulin-like growth factor receptors, are themselves phosphorylated and in turn recruit SH2 domain-containing signaling molecules to form a productive signaling complex. obo:GO_0043560 obo:go.owl obo:GO_0043560 IRS [protein] binding obo:GO_0043560 IRS binding obo:GO_0043560 insulin receptor substrate [protein] binding obo:GO_0043560 molecular_function obo:GO_0043560 GO:0043560 obo:GO_0043560 insulin receptor substrate binding obo:GO_0043562 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus reflecting the presence, absence, or concentration of inorganic nitrogen. obo:GO_0043562 obo:go.owl obo:GO_0043562 biological_process obo:GO_0043562 GO:0043562 obo:GO_0043562 cellular response to nitrogen levels obo:GO_0043565 Interacting selectively and non-covalently with DNA of a specific nucleotide composition, e.g. GC-rich DNA binding, or with a specific sequence motif or type of DNA e.g. promotor binding or rDNA binding. obo:GO_0043565 obo:go.owl obo:GO_0043565 sequence specific DNA binding obo:GO_0043565 molecular_function obo:GO_0043565 GO:0043565 obo:GO_0043565 sequence-specific DNA binding obo:GO_0043575 The series of events in which a stimulus indicating an increase or decrease in the concentration of solutes outside the organism or cell is received and converted into a molecular signal. obo:GO_0043575 obo:go.owl obo:GO_0043575 MIPS_funcat:34.11.03.13 obo:GO_0043575 biological_process obo:GO_0043575 GO:0043575 obo:GO_0043575 detection of osmotic stimulus obo:GO_0043609 Any process that modulates the frequency, rate, or extent of carbon utilization. obo:GO_0043609 obo:go.owl obo:GO_0043609 MIPS_funcat:01.05.04 obo:GO_0043609 biological_process obo:GO_0043609 GO:0043609 obo:GO_0043609 regulation of carbon utilization obo:GO_0043610 Any process that modulates the frequency, rate or extent of carbohydrate utilization. obo:GO_0043610 obo:go.owl obo:GO_0043610 MIPS_funcat:01.05.04 obo:GO_0043610 regulation of sugar utilization obo:GO_0043610 biological_process obo:GO_0043610 GO:0043610 obo:GO_0043610 regulation of carbohydrate utilization obo:GO_0043617 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of sucrose. obo:GO_0043617 obo:go.owl obo:GO_0043617 biological_process obo:GO_0043617 GO:0043617 obo:GO_0043617 cellular response to sucrose starvation obo:GO_0043621 Interacting selectively and non-covalently with a domain within the same polypeptide. obo:GO_0043621 obo:go.owl obo:GO_0043621 intramolecular protein binding obo:GO_0043621 protein self association obo:GO_0043621 protein self binding obo:GO_0043621 molecular_function obo:GO_0043621 GO:0043621 obo:GO_0043621 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0043621 protein self-association obo:GO_0043695 The series of events in which a pheromone stimulus is received by a cell and converted into a molecular signal. obo:GO_0043695 obo:go.owl obo:GO_0043695 biological_process obo:GO_0043695 GO:0043695 obo:GO_0043695 detection of pheromone obo:GO_0043924 Interacting selectively and non-covalently with suramin, a naphthalenesulfonic acid compound which is used in the treatment of diseases caused by trypanosomes and worms. obo:GO_0043924 obo:go.owl obo:GO_0043924 Germanin binding obo:GO_0043924 molecular_function obo:GO_0043924 GO:0043924 obo:GO_0043924 suramin binding obo:GO_0044022 Catalysis of the transfer of a phosphate group to the serine-28 residue of the N-terminal tail of histone H3. obo:GO_0044022 obo:go.owl obo:GO_0044022 histone serine kinase activity (H3-S28 specific) obo:GO_0044022 histone-serine kinase activity (H3-S28 specific) obo:GO_0044022 molecular_function obo:GO_0044022 GO:0044022 obo:GO_0044022 histone kinase activity (H3-S28 specific) obo:GO_0044023 Catalysis of the transfer of a phosphate group to the serine-1 residue of the N-terminal tail of histone H4. obo:GO_0044023 obo:go.owl obo:GO_0044023 histone serine kinase activity (H4-S1 specific) obo:GO_0044023 histone-serine kinase activity (H4-S1 specific) obo:GO_0044023 molecular_function obo:GO_0044023 GO:0044023 obo:GO_0044023 histone kinase activity (H4-S1 specific) obo:GO_0044024 Catalysis of the transfer of a phosphate group to the serine-1 residue of the N-terminal tail of histone H2A. obo:GO_0044024 obo:go.owl obo:GO_0044024 histone serine kinase activity (H2A-S1 specific) obo:GO_0044024 histone-serine kinase activity (H2A-S1 specific) obo:GO_0044024 molecular_function obo:GO_0044024 GO:0044024 obo:GO_0044024 histone kinase activity (H2A-S1 specific) obo:GO_0044025 Catalysis of the transfer of a phosphate group to the serine-14 or an equivalent residue of the N-terminal tail of histone H2B. obo:GO_0044025 obo:go.owl obo:GO_0044025 histone serine kinase activity (H2B-S14 specific) obo:GO_0044025 histone-serine kinase activity (H2B-S14 specific) obo:GO_0044025 molecular_function obo:GO_0044025 GO:0044025 obo:GO_0044025 histone kinase activity (H2B-S14 specific) obo:GO_0044070 Any process that modulates the frequency, rate or extent of the directed movement of anions, atoms or small molecules with a net negative charge into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0044070 obo:go.owl obo:GO_0044070 biological_process obo:GO_0044070 GO:0044070 obo:GO_0044070 regulation of anion transport obo:GO_0044087 Any process that modulates the frequency, rate or extent of cellular component biogenesis, a process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of a cellular component. obo:GO_0044087 obo:go.owl obo:GO_0044087 biological_process obo:GO_0044087 GO:0044087 obo:GO_0044087 regulation of cellular component biogenesis obo:GO_0044089 Any process that activates or increases the frequency, rate or extent of cellular component biogenesis, a process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of a cellular component. obo:GO_0044089 obo:go.owl obo:GO_0044089 biological_process obo:GO_0044089 GO:0044089 obo:GO_0044089 positive regulation of cellular component biogenesis obo:GO_0044092 Any process that stops or reduces the rate or extent of a molecular function, an elemental biological activity occurring at the molecular level, such as catalysis or binding. obo:GO_0044092 obo:go.owl obo:GO_0044092 jane obo:GO_0044092 2009-04-21T04:07:27Z obo:GO_0044092 biological_process obo:GO_0044092 GO:0044092 obo:GO_0044092 negative regulation of molecular function obo:GO_0044093 Any process that activates or increases the rate or extent of a molecular function, an elemental biological activity occurring at the molecular level, such as catalysis or binding. obo:GO_0044093 obo:go.owl obo:GO_0044093 jane obo:GO_0044093 2009-04-21T04:11:06Z obo:GO_0044093 biological_process obo:GO_0044093 GO:0044093 obo:GO_0044093 positive regulation of molecular function obo:GO_0044197 Interacting selectively and non-covalently with a Rel Homology Domain (RHD) of a protein. The RHD is found in a family of eukaryotic transcription factors, which includes NF-kappaB, Dorsal, Relish and NFAT. obo:GO_0044197 obo:go.owl obo:GO_0044197 jane obo:GO_0044197 2009-10-20T03:57:48Z obo:GO_0044197 RHD binding obo:GO_0044197 molecular_function obo:GO_0044197 GO:0044197 obo:GO_0044197 Rel homology domain binding obo:GO_0044198 Interacting selectively and non-covalently with a TRAF-type zinc finger domain of a protein. obo:GO_0044198 obo:go.owl obo:GO_0044198 jane obo:GO_0044198 2009-10-20T04:09:08Z obo:GO_0044198 TRAF-type zinc finger domain binding obo:GO_0044198 zinc finger TRAF-type domain binding obo:GO_0044198 zinc-finger-TRAF domain binding obo:GO_0044198 molecular_function obo:GO_0044198 GO:0044198 obo:GO_0044198 zf-TRAF domain binding obo:GO_0044212 Interacting selectively and non-covalently with a DNA region that regulates the transcription of a region of DNA, which may be a gene, cistron, or operon. Binding may occur as a sequence specific interaction or as an interaction observed only once a factor has been recruited to the DNA by other factors. obo:GO_0044212 obo:go.owl obo:GO_0044212 kchris obo:GO_0044212 2009-11-04T12:58:25Z obo:GO_0044212 GO:0000975 obo:GO_0044212 regulatory region DNA binding obo:GO_0044212 molecular_function obo:GO_0044212 GO:0044212 obo:GO_0044212 The word "promoter" is used variously in the literature to describe the core promoter specifically or the entire proximal regulatory region (excluding any distal enhancers) including both the core promoter and the upstream region where activating transcription factors such as Gal4 in S. cerevisiae or catabolite activator protein (CAP) in E. coli bind. To minimize ambiguity in the use of the word "promoter" in GO, we have chosen the phrase "transcription regulatory region" in order to refer to all of the regulatory regions. Regulatory regions in the DNA which control initiation may include the "core promoter" where the basal transcription machinery binds, the "core promoter proximal region" where regulatory factors other than the basal machinery bind, and "enhancer" regions which are typically more distal from the core promoter. There are also additional regulatory regions, in both the DNA and the RNA transcript, which regulate elongation or termination of transcription. ANNOTATION NOTE: Regarding annotation to "transcription regulatory region DNA binding" (GO:0044212) and any of its is_a children, note that annotation to these terms specifies DNA binding only without any statement about transcription factor activity. To make an annotation about a function of transcription factor activity, consider "sequence-specific DNA-binding transcription factor activity" (GO:0003700) or its is_a children which have has_part relationships to the appropriate kind of "transcription regulatory region DNA binding". obo:GO_0044212 transcription regulatory region DNA binding obo:GO_0044213 Interacting selectively and non-covalently with an intronic DNA region that regulates the transcription of the transcript it is contained within. obo:GO_0044213 obo:go.owl obo:GO_0044213 jane obo:GO_0044213 2009-11-04T01:21:28Z obo:GO_0044213 molecular_function obo:GO_0044213 GO:0044213 obo:GO_0044213 intronic transcription regulatory region DNA binding obo:GO_0044237 The chemical reactions and pathways by which individual cells transform chemical substances. obo:GO_0044237 obo:go.owl obo:GO_0044237 cellular metabolism obo:GO_0044237 biological_process obo:GO_0044237 intermediary metabolism obo:GO_0044237 GO:0044237 obo:GO_0044237 cellular metabolic process obo:GO_0044238 The chemical reactions and pathways involving those compounds which are formed as a part of the normal anabolic and catabolic processes. These processes take place in most, if not all, cells of the organism. obo:GO_0044238 obo:go.owl obo:GO_0044238 primary metabolism obo:GO_0044238 biological_process obo:GO_0044238 GO:0044238 obo:GO_0044238 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0044238 primary metabolic process obo:GO_0044248 The chemical reactions and pathways resulting in the breakdown of substances, carried out by individual cells. obo:GO_0044248 obo:go.owl obo:GO_0044248 cellular breakdown obo:GO_0044248 cellular catabolism obo:GO_0044248 cellular degradation obo:GO_0044248 biological_process obo:GO_0044248 GO:0044248 obo:GO_0044248 cellular catabolic process obo:GO_0044249 The chemical reactions and pathways resulting in the formation of substances, carried out by individual cells. obo:GO_0044249 obo:go.owl obo:GO_0044249 cellular anabolism obo:GO_0044249 cellular biosynthesis obo:GO_0044249 cellular formation obo:GO_0044249 cellular synthesis obo:GO_0044249 biological_process obo:GO_0044249 GO:0044249 obo:GO_0044249 cellular biosynthetic process obo:GO_0044250 The slowing of metabolic processes to very low levels in order to conserve energy as a part of hibernation. obo:GO_0044250 obo:go.owl obo:GO_0044250 inhibition of metabolic activity during hibernation obo:GO_0044250 biological_process obo:GO_0044250 down regulation of metabolic activity during hibernation obo:GO_0044250 down-regulation of metabolic activity during hibernation obo:GO_0044250 downregulation of metabolic activity during hibernation obo:GO_0044250 negative regulation of metabolic activity during hibernation obo:GO_0044250 GO:0044250 obo:GO_0044250 negative regulation of metabolic activity involved in hibernation obo:GO_0044260 The chemical reactions and pathways involving macromolecules, any molecule of high relative molecular mass, the structure of which essentially comprises the multiple repetition of units derived, actually or conceptually, from molecules of low relative molecular mass, as carried out by individual cells. obo:GO_0044260 obo:go.owl obo:GO_0044260 GO:0034960 obo:GO_0044260 cellular biopolymer metabolic process obo:GO_0044260 cellular macromolecule metabolism obo:GO_0044260 biological_process obo:GO_0044260 GO:0044260 obo:GO_0044260 cellular macromolecule metabolic process obo:GO_0044262 The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y, as carried out by individual cells. obo:GO_0044262 obo:go.owl obo:GO_0044262 GO:0006092 obo:GO_0044262 cellular carbohydrate metabolism obo:GO_0044262 main pathways of carbohydrate metabolic process obo:GO_0044262 main pathways of carbohydrate metabolism obo:GO_0044262 biological_process obo:GO_0044262 GO:0044262 obo:GO_0044262 cellular carbohydrate metabolic process obo:GO_0044265 The chemical reactions and pathways resulting in the breakdown of a macromolecule, any large molecule including proteins, nucleic acids and carbohydrates, as carried out by individual cells. obo:GO_0044265 obo:go.owl obo:GO_0044265 GO:0034962 obo:GO_0044265 cellular biopolymer catabolic process obo:GO_0044265 cellular macromolecule breakdown obo:GO_0044265 cellular macromolecule catabolism obo:GO_0044265 cellular macromolecule degradation obo:GO_0044265 biological_process obo:GO_0044265 GO:0044265 obo:GO_0044265 cellular macromolecule catabolic process obo:GO_0044267 The chemical reactions and pathways involving a specific protein, rather than of proteins in general, occurring at the level of an individual cell. Includes cellular protein modification. obo:GO_0044267 obo:go.owl obo:GO_0044267 cellular protein metabolism obo:GO_0044267 biological_process obo:GO_0044267 GO:0044267 obo:GO_0044267 cellular protein metabolic process obo:GO_0044271 The chemical reactions and pathways resulting in the formation of organic and inorganic nitrogenous compounds. obo:GO_0044271 obo:go.owl obo:GO_0044271 nitrogen compound anabolism obo:GO_0044271 nitrogen compound biosynthesis obo:GO_0044271 nitrogen compound formation obo:GO_0044271 nitrogen compound synthesis obo:GO_0044271 biological_process obo:GO_0044271 GO:0044271 obo:GO_0044271 cellular nitrogen compound biosynthetic process obo:GO_0044323 Interacting selectively and non-covalently with a retinoic acid-responsive element, a variable direct repeat of the sequence PuGGTCA spaced by five nucleotides (DR5) found in the promoters of retinoic acid-responsive genes, to which retinoic acid receptors bind. obo:GO_0044323 obo:go.owl obo:GO_0044323 janelomax obo:GO_0044323 2010-08-03T03:19:05Z obo:GO_0044323 RARE binding obo:GO_0044323 molecular_function obo:GO_0044323 GO:0044323 obo:GO_0044323 Note that as agreed during the transcription overhaul, terms specifying binding to specific transcription regulatory motifs are no longer being created. The level of specificity GO has decided to go to is the "core promoter", "core promoter proximal region" and "enhancer". To capture more detail, please consider using column 16. obo:GO_0044323 retinoic acid-responsive element binding obo:GO_0044325 Interacting selectively and non-covalently with one or more specific sites on an ion channel, a protein complex that spans a membrane and forms a water-filled channel across the phospholipid bilayer allowing selective ion transport down its electrochemical gradient. obo:GO_0044325 obo:go.owl obo:GO_0044325 janelomax obo:GO_0044325 2010-08-04T12:52:59Z obo:GO_0044325 molecular_function obo:GO_0044325 GO:0044325 obo:GO_0044325 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0044325 ion channel binding obo:GO_0044341 The directed movement of phosphate into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore, by a mechanism dependent upon sodium ions. obo:GO_0044341 obo:go.owl obo:GO_0044341 janelomax obo:GO_0044341 2010-08-20T04:16:15Z obo:GO_0044341 biological_process obo:GO_0044341 GO:0044341 obo:GO_0044341 sodium-dependent phosphate transport obo:GO_0044373 Interacting selectively and non-covalently with a cytokinin, any of a class of adenine-derived compounds that can function in plants as growth regulators. obo:GO_0044373 obo:go.owl obo:GO_0044373 janelomax obo:GO_0044373 2011-12-01T03:42:10Z obo:GO_0044373 molecular_function obo:GO_0044373 GO:0044373 obo:GO_0044373 cytokinin binding obo:GO_0044374 The activity of binding selectively and non-covalently to DNA in a sequence-specific manner and distorting the original structure of DNA, typically a straight helix, into a bend, or increasing the bend if the original structure was intrinsically bent due to its sequence. obo:GO_0044374 obo:go.owl obo:GO_0044374 janelomax obo:GO_0044374 2011-12-01T04:05:59Z obo:GO_0044374 DNA bending involving sequence-specific DNA binding obo:GO_0044374 molecular_function obo:GO_0044374 GO:0044374 obo:GO_0044374 sequence-specific DNA binding, bending obo:GO_0044377 Interacting selectively and non-covalently with a proximal promoter DNA sequence of a gene transcribed by RNA polymerase II, and distorting the original structure of DNA, typically a straight helix, into a bend, or increasing the bend if the original structure was intrinsically bent due to its sequence. obo:GO_0044377 obo:go.owl obo:GO_0044377 janelomax obo:GO_0044377 2011-12-08T01:38:21Z obo:GO_0044377 RNA polymerase II core promoter proximal region sequence-specific DNA binding, bending obo:GO_0044377 RNA polymerase II promoter proximal region sequence-specific DNA binding, bending obo:GO_0044377 RNA polymerase II proximal promoter region sequence-specific DNA binding, bending obo:GO_0044377 molecular_function obo:GO_0044377 GO:0044377 obo:GO_0044377 RNA polymerase II proximal promoter sequence-specific DNA binding, bending obo:GO_0044378 The activity of binding selectively and non-covalently to DNA in a sequence-independent manner and distorting the original structure of DNA, typically a straight helix, into a bend, or increasing the bend if the original structure was intrinsically bent due to its sequence. obo:GO_0044378 obo:go.owl obo:GO_0044378 janelomax obo:GO_0044378 2011-12-08T02:02:13Z obo:GO_0044378 DNA bending involving non-sequence-specific DNA binding obo:GO_0044378 molecular_function obo:GO_0044378 GO:0044378 obo:GO_0044378 non-sequence-specific DNA binding, bending obo:GO_0044388 Interacting selectively and non-covalently with a small protein activating enzyme, such as ubiquitin-activating enzyme. obo:GO_0044388 obo:go.owl obo:GO_0044388 janelomax obo:GO_0044388 2011-12-15T04:28:17Z obo:GO_0044388 molecular_function obo:GO_0044388 GO:0044388 obo:GO_0044388 small protein activating enzyme binding obo:GO_0044389 Interacting selectively and non-covalently with a ubiquitin-like protein ligase, such as ubiquitin-ligase. obo:GO_0044389 obo:go.owl obo:GO_0044389 janelomax obo:GO_0044389 2011-12-15T04:33:20Z obo:GO_0044389 E3 protein ligase binding obo:GO_0044389 small conjugating protein ligase binding obo:GO_0044389 molecular_function obo:GO_0044389 GO:0044389 obo:GO_0044389 ubiquitin-like protein ligase binding obo:GO_0044390 Interacting selectively and non-covalently with a ubiquitin-like protein conjugating enzyme such as ubiquitin conjugating enzyme. obo:GO_0044390 obo:go.owl obo:GO_0044390 janelomax obo:GO_0044390 2011-12-15T04:38:44Z obo:GO_0044390 E2 protein ligase binding obo:GO_0044390 small protein conjugating enzyme binding obo:GO_0044390 molecular_function obo:GO_0044390 GO:0044390 obo:GO_0044390 ubiquitin-like protein conjugating enzyme binding obo:GO_0044547 Interacting selectively and non-covalently with a DNA topoisomerase. obo:GO_0044547 obo:go.owl obo:GO_0044547 janelomax obo:GO_0044547 2012-03-22T02:30:37Z obo:GO_0044547 GO:0017033 obo:GO_0044547 DNA topoisomerase I binding obo:GO_0044547 molecular_function obo:GO_0044547 GO:0044547 obo:GO_0044547 DNA topoisomerase binding obo:GO_0044548 Interacting selectively and non-covalently with a S100 protein. S100 is a small calcium and zinc binding protein produced in astrocytes that is implicated in Alzheimer's disease, Down Syndrome and ALS. obo:GO_0044548 obo:go.owl obo:GO_0044548 janelomax obo:GO_0044548 2012-03-22T03:23:51Z obo:GO_0044548 GO:0048154 obo:GO_0044548 GO:0048155 obo:GO_0044548 S100 binding obo:GO_0044548 S100 alpha binding obo:GO_0044548 S100 beta binding obo:GO_0044548 molecular_function obo:GO_0044548 GO:0044548 obo:GO_0044548 S100 protein binding obo:GO_0044549 Interacting selectively and non-covalently with a GTP cyclohydrolase. obo:GO_0044549 obo:go.owl obo:GO_0044549 janelomax obo:GO_0044549 2012-03-22T04:38:14Z obo:GO_0044549 GO:0043106 obo:GO_0044549 GTP cyclohydrolase I binding obo:GO_0044549 molecular_function obo:GO_0044549 GO:0044549 obo:GO_0044549 GTP cyclohydrolase binding obo:GO_0044583 Interacting selectively and non-covalently with cellotriose. obo:GO_0044583 obo:go.owl obo:GO_0044583 janelomax obo:GO_0044583 2012-04-24T04:48:01Z obo:GO_0044583 molecular_function obo:GO_0044583 GO:0044583 obo:GO_0044583 cellotriose binding obo:GO_0044584 Interacting selectively and non-covalently with cellodextrin, a glucose polymer of 2 or more glucose monomers. obo:GO_0044584 obo:go.owl obo:GO_0044584 janelomax obo:GO_0044584 2012-04-24T04:52:05Z obo:GO_0044584 molecular_function obo:GO_0044584 GO:0044584 obo:GO_0044584 cellodextrin binding obo:GO_0044585 Interacting selectively and non-covalently with cellobiose, a disaccharide that represents the basic repeating unit of cellulose. obo:GO_0044585 obo:go.owl obo:GO_0044585 janelomax obo:GO_0044585 2012-04-24T04:55:10Z obo:GO_0044585 molecular_function obo:GO_0044585 GO:0044585 obo:GO_0044585 cellobiose binding obo:GO_0044586 Interacting selectively and non-covalently with cellotetraose, an oligosaccharide consisting of four glucose residues resulting from hydrolysis of cellulose. obo:GO_0044586 obo:go.owl obo:GO_0044586 janelomax obo:GO_0044586 2012-04-24T04:56:10Z obo:GO_0044586 molecular_function obo:GO_0044586 GO:0044586 obo:GO_0044586 cellotetraose binding obo:GO_0044587 Interacting selectively and non-covalently with cellopentaose, an oligosaccharide consisting of four glucose residues resulting from hydrolysis of cellulose. obo:GO_0044587 obo:go.owl obo:GO_0044587 janelomax obo:GO_0044587 2012-04-24T04:57:01Z obo:GO_0044587 molecular_function obo:GO_0044587 GO:0044587 obo:GO_0044587 cellopentaose binding obo:GO_0044588 Interacting selectively and non-covalently with laminaribiose, a disaccharide. obo:GO_0044588 obo:go.owl obo:GO_0044588 janelomax obo:GO_0044588 2012-04-26T01:19:40Z obo:GO_0044588 molecular_function obo:GO_0044588 GO:0044588 obo:GO_0044588 laminaribiose binding obo:GO_0044589 Interacting selectively and non-covalently with pectin. obo:GO_0044589 obo:go.owl obo:GO_0044589 janelomax obo:GO_0044589 2012-04-26T01:26:56Z obo:GO_0044589 molecular_function obo:GO_0044589 GO:0044589 obo:GO_0044589 pectin binding obo:GO_0044590 Interacting selectively and non-covalently with iron molybdenum cofactor, the cofactor located at the active site of the molybdenum nitrogenase. obo:GO_0044590 obo:go.owl obo:GO_0044590 janelomax obo:GO_0044590 2012-04-26T02:27:39Z obo:GO_0044590 FeMo co binding obo:GO_0044590 FeMoco binding obo:GO_0044590 molecular_function obo:GO_0044590 GO:0044590 obo:GO_0044590 iron-sulfur-molybdenum cofactor binding obo:GO_0044620 Interacting selectively and non-covalently with the attachment site of the phosphopantetheine prosthetic group of an acyl carrier protein (ACP). obo:GO_0044620 obo:go.owl obo:GO_0044620 janelomax obo:GO_0044620 2012-07-04T03:25:04Z obo:GO_0044620 molecular_function obo:GO_0044620 GO:0044620 obo:GO_0044620 ACP phosphopantetheine attachment site binding obo:GO_0044718 The directed movement of siderophores, low molecular weight Fe(III)-chelating substances, from one side of a membrane to the other, by means of some agent such as a transporter or pore. obo:GO_0044718 obo:go.owl obo:GO_0044718 janelomax obo:GO_0044718 2012-10-18T13:43:56Z obo:GO_0044718 siderophore membrane transport obo:GO_0044718 biological_process obo:GO_0044718 GO:0044718 obo:GO_0044718 Note that this term is not intended for use in annotating lateral movement within membranes. obo:GO_0044718 siderophore transmembrane transport obo:GO_0044729 Interacting selectively and non-covalently with double-stranded hemi-methylated DNA at replication foci (one strand methylated, while the other strand is unmethylated). Methylation of cytosine or adenine in DNA is an important mechanism for establishing stable heritable epigenetic marks. obo:GO_0044729 obo:go.owl obo:GO_0044729 janelomax obo:GO_0044729 2012-10-24T14:58:14Z obo:GO_0044729 double-stranded hemi-methylated DNA binding obo:GO_0044729 molecular_function obo:GO_0044729 GO:0044729 obo:GO_0044729 hemi-methylated DNA-binding obo:GO_0044877 Interacting selectively and non-covalently with a macromolecular complex. obo:GO_0044877 obo:go.owl obo:GO_0044877 janelomax obo:GO_0044877 2014-12-16T11:38:58Z obo:GO_0044877 GO:0032403 obo:GO_0044877 protein complex binding obo:GO_0044877 molecular_function obo:GO_0044877 macromolecular complex binding obo:GO_0044877 GO:0044877 obo:GO_0044877 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0044877 protein-containing complex binding obo:GO_0045002 Repair of a DSB made between two repeated sequences oriented in the same direction occurs primarily by the single strand annealing pathway. The ends of the break are processed by a 5' to 3' exonuclease, exposing complementary single-strand regions of the direct repeats that can anneal, resulting in a deletion of the unique DNA between the direct repeats. obo:GO_0045002 obo:go.owl obo:GO_0045002 biological_process obo:GO_0045002 GO:0045002 obo:GO_0045002 double-strand break repair via single-strand annealing obo:GO_0045003 SDSA is a major mechanism of double-strand break repair in mitosis which allows for the error-free repair of a double-strand break without the exchange of adjacent sequences. The broken DNA searches for and base pairs with a homologous region in an intact chromosome. DNA synthesis initiates from the 3' end of the invading DNA strand, using the intact chromosome as the template. Newly synthesized DNA is then displaced from the template and anneal with its complement on the other side of the double-strand break. obo:GO_0045003 obo:go.owl obo:GO_0045003 SDSA obo:GO_0045003 biological_process obo:GO_0045003 mitotic gene conversion obo:GO_0045003 GO:0045003 obo:GO_0045003 double-strand break repair via synthesis-dependent strand annealing obo:GO_0045004 Correction of replication errors by DNA polymerase using a 3'-5' exonuclease activity. obo:GO_0045004 obo:go.owl obo:GO_0045004 biological_process obo:GO_0045004 GO:0045004 obo:GO_0045004 DNA replication proofreading obo:GO_0045005 A DNA metabolic process that prevents or corrects errors to ensure that DNA is replicated accurately. Errors can be corrected either by intrinsic DNA polymerase proofreading activity or via mismatch repair. obo:GO_0045005 obo:go.owl obo:GO_0045005 maintenance of fidelity involved in DNA-dependent DNA replication obo:GO_0045005 biological_process obo:GO_0045005 maintenance of fidelity during DNA-dependent DNA replication obo:GO_0045005 GO:0045005 obo:GO_0045005 DNA-dependent DNA replication maintenance of fidelity obo:GO_0045015 Interacting selectively and non-covalently with a HDEL sequence, the C terminus tetrapeptide sequence His-Asp-Glu-Leu found in proteins that are to be retained in the endoplasmic reticulum. obo:GO_0045015 obo:go.owl obo:GO_0045015 HDEL receptor activity obo:GO_0045015 molecular_function obo:GO_0045015 GO:0045015 obo:GO_0045015 HDEL sequence binding obo:GO_0045016 The process in which a magnesium ion (Mg2+) is transported across a mitochondrial membrane, into or out of the mitochondrion. obo:GO_0045016 obo:go.owl obo:GO_0045016 mcc obo:GO_0045016 2015-01-21T17:44:38Z obo:GO_0045016 GO:1990614 obo:GO_0045016 biological_process obo:GO_0045016 mitochondrial magnesium ion transport obo:GO_0045016 GO:0045016 obo:GO_0045016 mitochondrial magnesium ion transmembrane transport obo:GO_0045027 Interacting selectively and non-covalently with the ends of DNA that are exposed by the creation of double-strand breaks (DSBs). obo:GO_0045027 obo:go.owl obo:GO_0045027 molecular_function obo:GO_0045027 GO:0045027 obo:GO_0045027 DNA end binding obo:GO_0045131 Interacting selectively and non-covalently with a pre-mRNA branch point sequence, located upstream of the 3' splice site. obo:GO_0045131 obo:go.owl obo:GO_0045131 molecular_function obo:GO_0045131 GO:0045131 obo:GO_0045131 pre-mRNA branch point binding obo:GO_0045142 Interacting selectively and non-covalently with a DNA triple helix. The formation of triple helical DNA has been evoked in several cellular processes including transcription, replication, and recombination. obo:GO_0045142 obo:go.owl obo:GO_0045142 molecular_function obo:GO_0045142 GO:0045142 obo:GO_0045142 triplex DNA binding obo:GO_0045152 Interacting selectively and non-covalently with an antisigma factor, a factor which inhibits the ability of the sigma factor to function as a transcriptional initiator. obo:GO_0045152 obo:go.owl obo:GO_0045152 antisigma factor antagonist activity obo:GO_0045152 molecular_function obo:GO_0045152 GO:0045152 obo:GO_0045152 antisigma factor binding obo:GO_0045159 Interacting selectively and non-covalently with a class II myosin, any member of the class of 'conventional' double-headed myosins that includes muscle myosin. obo:GO_0045159 obo:go.owl obo:GO_0045159 molecular_function obo:GO_0045159 GO:0045159 obo:GO_0045159 myosin II binding obo:GO_0045236 Interacting selectively and non-covalently with a chemokine receptor in the CXCR family. obo:GO_0045236 obo:go.owl obo:GO_0045236 alpha chemokine receptor binding obo:GO_0045236 C-X-C chemokine receptor ligand obo:GO_0045236 CXC chemokine receptor ligand obo:GO_0045236 alpha chemokine receptor ligand obo:GO_0045236 molecular_function obo:GO_0045236 GO:0045236 obo:GO_0045236 CXCR chemokine receptor binding obo:GO_0045237 Interacting selectively and non-covalently with the CXCR1 chemokine receptor. obo:GO_0045237 obo:go.owl obo:GO_0045237 CXCR1 chemokine receptor ligand obo:GO_0045237 molecular_function obo:GO_0045237 GO:0045237 obo:GO_0045237 CXCR1 chemokine receptor binding obo:GO_0045238 Interacting selectively and non-covalently with the CXCR2 chemokine receptor. obo:GO_0045238 obo:go.owl obo:GO_0045238 CXCR2 chemokine receptor ligand obo:GO_0045238 molecular_function obo:GO_0045238 GO:0045238 obo:GO_0045238 CXCR2 chemokine receptor binding obo:GO_0045294 Interacting selectively and non-covalently with the alpha subunit of the catenin complex. obo:GO_0045294 obo:go.owl obo:GO_0045294 molecular_function obo:GO_0045294 GO:0045294 obo:GO_0045294 alpha-catenin binding obo:GO_0045295 Interacting selectively and non-covalently with the gamma subunit of the catenin complex. obo:GO_0045295 obo:go.owl obo:GO_0045295 plakoglobin binding obo:GO_0045295 molecular_function obo:GO_0045295 GO:0045295 obo:GO_0045295 gamma-catenin binding obo:GO_0045296 Interacting selectively and non-covalently with cadherin, a type I membrane protein involved in cell adhesion. obo:GO_0045296 obo:go.owl obo:GO_0045296 molecular_function obo:GO_0045296 GO:0045296 obo:GO_0045296 cadherin binding obo:GO_0045309 Interacting selectively and non-covalently with a phosphorylated amino acid residue within a protein. obo:GO_0045309 obo:go.owl obo:GO_0045309 molecular_function obo:GO_0045309 phosphoprotein amino acid binding obo:GO_0045309 GO:0045309 obo:GO_0045309 protein phosphorylated amino acid binding obo:GO_0045322 Interacting selectively and non-covalently with unmethylated CpG motifs. Unmethylated CpG dinucleotides are often associated with gene promoters. obo:GO_0045322 obo:go.owl obo:GO_0045322 molecular_function obo:GO_0045322 GO:0045322 obo:GO_0045322 unmethylated CpG binding obo:GO_0045340 Interacting selectively and non-covalently with mercury (Hg) ions. obo:GO_0045340 obo:go.owl obo:GO_0045340 mercury binding obo:GO_0045340 molecular_function obo:GO_0045340 GO:0045340 obo:GO_0045340 mercury ion binding obo:GO_0045352 Blocks the binding of interleukin-1 to interleukin-1 type I receptors. obo:GO_0045352 obo:go.owl obo:GO_0045352 IL-1ra type I obo:GO_0045352 molecular_function obo:GO_0045352 GO:0045352 obo:GO_0045352 interleukin-1 type I receptor antagonist activity obo:GO_0045353 Blocks the binding of interleukin-1 to interleukin-1 type II receptors. obo:GO_0045353 obo:go.owl obo:GO_0045353 IL-1ra type II obo:GO_0045353 molecular_function obo:GO_0045353 GO:0045353 obo:GO_0045353 interleukin-1 type II receptor antagonist activity obo:GO_0045471 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an ethanol stimulus. obo:GO_0045471 obo:go.owl obo:GO_0045471 GO:0017036 obo:GO_0045471 biological_process obo:GO_0045471 GO:0045471 obo:GO_0045471 response to ethanol obo:GO_0045499 Providing the environmental signal that initiates the directed movement of a motile cell or organism towards a lower concentration of that signal. obo:GO_0045499 obo:go.owl obo:GO_0045499 chemorepellant activity obo:GO_0045499 molecular_function obo:GO_0045499 GO:0045499 obo:GO_0045499 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0045499 chemorepellent activity obo:GO_0045503 Interacting selectively and non-covalently with a light chain of the dynein complex. obo:GO_0045503 obo:go.owl obo:GO_0045503 molecular_function obo:GO_0045503 GO:0045503 obo:GO_0045503 dynein light chain binding obo:GO_0045504 Interacting selectively and non-covalently with a heavy chain of the dynein complex. obo:GO_0045504 obo:go.owl obo:GO_0045504 molecular_function obo:GO_0045504 GO:0045504 obo:GO_0045504 dynein heavy chain binding obo:GO_0045505 Interacting selectively and non-covalently with an intermediate chain of the dynein complex. obo:GO_0045505 obo:go.owl obo:GO_0045505 molecular_function obo:GO_0045505 GO:0045505 obo:GO_0045505 dynein intermediate chain binding obo:GO_0045510 Interacting selectively and non-covalently with interleukin-24. obo:GO_0045510 obo:go.owl obo:GO_0045510 IL-24 binding obo:GO_0045510 molecular_function obo:GO_0045510 GO:0045510 obo:GO_0045510 interleukin-24 binding obo:GO_0045511 Interacting selectively and non-covalently with interleukin-25. obo:GO_0045511 obo:go.owl obo:GO_0045511 IL-25 binding obo:GO_0045511 molecular_function obo:GO_0045511 GO:0045511 obo:GO_0045511 interleukin-25 binding obo:GO_0045512 Interacting selectively and non-covalently with interleukin-26. obo:GO_0045512 obo:go.owl obo:GO_0045512 IL-26 binding obo:GO_0045512 molecular_function obo:GO_0045512 GO:0045512 obo:GO_0045512 interleukin-26 binding obo:GO_0045513 Interacting selectively and non-covalently with interleukin-27. obo:GO_0045513 obo:go.owl obo:GO_0045513 IL-27 binding obo:GO_0045513 molecular_function obo:GO_0045513 GO:0045513 obo:GO_0045513 interleukin-27 binding obo:GO_0045514 Interacting selectively and non-covalently with the interleukin-16 receptor. obo:GO_0045514 obo:go.owl obo:GO_0045514 IL-16 obo:GO_0045514 interleukin-16 receptor ligand obo:GO_0045514 molecular_function obo:GO_0045514 GO:0045514 obo:GO_0045514 interleukin-16 receptor binding obo:GO_0045515 Interacting selectively and non-covalently with the interleukin-18 receptor. obo:GO_0045515 obo:go.owl obo:GO_0045515 IL-18 obo:GO_0045515 interleukin-18 receptor ligand obo:GO_0045515 molecular_function obo:GO_0045515 GO:0045515 obo:GO_0045515 interleukin-18 receptor binding obo:GO_0045516 Interacting selectively and non-covalently with the interleukin-19 receptor. obo:GO_0045516 obo:go.owl obo:GO_0045516 IL-19 obo:GO_0045516 interleukin-19 receptor ligand obo:GO_0045516 molecular_function obo:GO_0045516 GO:0045516 obo:GO_0045516 interleukin-19 receptor binding obo:GO_0045517 Interacting selectively and non-covalently with the interleukin-20 receptor. obo:GO_0045517 obo:go.owl obo:GO_0045517 IL-20 obo:GO_0045517 interleukin-20 receptor ligand obo:GO_0045517 molecular_function obo:GO_0045517 GO:0045517 obo:GO_0045517 interleukin-20 receptor binding obo:GO_0045518 Interacting selectively and non-covalently with the interleukin-22 receptor. obo:GO_0045518 obo:go.owl obo:GO_0045518 IL-22 obo:GO_0045518 interleukin-22 receptor ligand obo:GO_0045518 molecular_function obo:GO_0045518 GO:0045518 obo:GO_0045518 interleukin-22 receptor binding obo:GO_0045519 Interacting selectively and non-covalently with the interleukin-23 receptor. obo:GO_0045519 obo:go.owl obo:GO_0045519 IL-23 obo:GO_0045519 interleukin-23 receptor ligand obo:GO_0045519 molecular_function obo:GO_0045519 GO:0045519 obo:GO_0045519 interleukin-23 receptor binding obo:GO_0045520 Interacting selectively and non-covalently with the interleukin-24 receptor. obo:GO_0045520 obo:go.owl obo:GO_0045520 IL-24 obo:GO_0045520 interleukin-24 receptor ligand obo:GO_0045520 molecular_function obo:GO_0045520 GO:0045520 obo:GO_0045520 interleukin-24 receptor binding obo:GO_0045521 Interacting selectively and non-covalently with the interleukin-25 receptor. obo:GO_0045521 obo:go.owl obo:GO_0045521 IL-25 obo:GO_0045521 interleukin-25 receptor ligand obo:GO_0045521 molecular_function obo:GO_0045521 GO:0045521 obo:GO_0045521 interleukin-25 receptor binding obo:GO_0045522 Interacting selectively and non-covalently with the interleukin-26 receptor. obo:GO_0045522 obo:go.owl obo:GO_0045522 IL-26 obo:GO_0045522 interleukin-26 receptor ligand obo:GO_0045522 molecular_function obo:GO_0045522 GO:0045522 obo:GO_0045522 interleukin-26 receptor binding obo:GO_0045523 Interacting selectively and non-covalently with the interleukin-27 receptor. obo:GO_0045523 obo:go.owl obo:GO_0045523 IL-27 obo:GO_0045523 interleukin-27 receptor ligand obo:GO_0045523 molecular_function obo:GO_0045523 GO:0045523 obo:GO_0045523 interleukin-27 receptor binding obo:GO_0045545 Interacting selectively and non-covalently with syndecan, an integral membrane proteoglycan (250-300 kDa) associated largely with epithelial cells. obo:GO_0045545 obo:go.owl obo:GO_0045545 molecular_function obo:GO_0045545 GO:0045545 obo:GO_0045545 syndecan binding obo:GO_0045569 Interacting selectively and non-covalently with TRAIL (TNF-related apoptosis inducing ligand), a member of the tumor necrosis factor ligand family that rapidly induces apoptosis in a variety of transformed cell lines. obo:GO_0045569 obo:go.owl obo:GO_0045569 Apo-2L binding obo:GO_0045569 molecular_function obo:GO_0045569 GO:0045569 obo:GO_0045569 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0045569 TRAIL binding obo:GO_0045785 Any process that activates or increases the frequency, rate or extent of cell adhesion. obo:GO_0045785 obo:go.owl obo:GO_0045785 up regulation of cell adhesion obo:GO_0045785 up-regulation of cell adhesion obo:GO_0045785 upregulation of cell adhesion obo:GO_0045785 activation of cell adhesion obo:GO_0045785 stimulation of cell adhesion obo:GO_0045785 biological_process obo:GO_0045785 GO:0045785 obo:GO_0045785 positive regulation of cell adhesion obo:GO_0045831 Any process that stops, prevents, or reduces the frequency, rate or extent of light-activated channel activity. obo:GO_0045831 obo:go.owl obo:GO_0045831 down regulation of light-activated channel activity obo:GO_0045831 down-regulation of light-activated channel activity obo:GO_0045831 downregulation of light-activated channel activity obo:GO_0045831 inhibition of light-activated channel activity obo:GO_0045831 biological_process obo:GO_0045831 GO:0045831 obo:GO_0045831 negative regulation of light-activated channel activity obo:GO_0045832 Any process that activates or increases the frequency, rate or extent of light-activated channel activity. obo:GO_0045832 obo:go.owl obo:GO_0045832 up regulation of light-activated channel activity obo:GO_0045832 up-regulation of light-activated channel activity obo:GO_0045832 upregulation of light-activated channel activity obo:GO_0045832 activation of light-activated channel activity obo:GO_0045832 stimulation of light-activated channel activity obo:GO_0045832 biological_process obo:GO_0045832 GO:0045832 obo:GO_0045832 positive regulation of light-activated channel activity obo:GO_0045847 Any process that stops, prevents, or reduces the frequency, rate or extent of nitrogen utilization. obo:GO_0045847 obo:go.owl obo:GO_0045847 down regulation of nitrogen utilization obo:GO_0045847 down-regulation of nitrogen utilization obo:GO_0045847 downregulation of nitrogen utilization obo:GO_0045847 inhibition of nitrogen utilization obo:GO_0045847 biological_process obo:GO_0045847 GO:0045847 obo:GO_0045847 negative regulation of nitrogen utilization obo:GO_0045848 Any process that activates or increases the frequency, rate or extent of nitrogen utilization. obo:GO_0045848 obo:go.owl obo:GO_0045848 up regulation of nitrogen utilization obo:GO_0045848 up-regulation of nitrogen utilization obo:GO_0045848 upregulation of nitrogen utilization obo:GO_0045848 activation of nitrogen utilization obo:GO_0045848 stimulation of nitrogen utilization obo:GO_0045848 biological_process obo:GO_0045848 GO:0045848 obo:GO_0045848 positive regulation of nitrogen utilization obo:GO_0045926 Any process that stops, prevents or reduces the rate or extent of growth, the increase in size or mass of all or part of an organism. obo:GO_0045926 obo:go.owl obo:GO_0045926 down regulation of growth obo:GO_0045926 down-regulation of growth obo:GO_0045926 downregulation of growth obo:GO_0045926 inhibition of growth obo:GO_0045926 biological_process obo:GO_0045926 GO:0045926 obo:GO_0045926 negative regulation of growth obo:GO_0045927 Any process that activates or increases the rate or extent of growth, the increase in size or mass of all or part of an organism. obo:GO_0045927 obo:go.owl obo:GO_0045927 up regulation of growth obo:GO_0045927 up-regulation of growth obo:GO_0045927 upregulation of growth obo:GO_0045927 activation of growth obo:GO_0045927 stimulation of growth obo:GO_0045927 biological_process obo:GO_0045927 GO:0045927 obo:GO_0045927 positive regulation of growth obo:GO_0045942 Any process that stops, prevents, or reduces the frequency, rate or extent of phosphorus utilization. obo:GO_0045942 obo:go.owl obo:GO_0045942 down regulation of phosphorus utilization obo:GO_0045942 down-regulation of phosphorus utilization obo:GO_0045942 downregulation of phosphorus utilization obo:GO_0045942 inhibition of phosphorus utilization obo:GO_0045942 biological_process obo:GO_0045942 GO:0045942 obo:GO_0045942 negative regulation of phosphorus utilization obo:GO_0045949 Any process that activates or increases the frequency, rate or extent of phosphorus utilization. obo:GO_0045949 obo:go.owl obo:GO_0045949 up regulation of phosphorus utilization obo:GO_0045949 up-regulation of phosphorus utilization obo:GO_0045949 upregulation of phosphorus utilization obo:GO_0045949 activation of phosphorus utilization obo:GO_0045949 stimulation of phosphorus utilization obo:GO_0045949 biological_process obo:GO_0045949 GO:0045949 obo:GO_0045949 positive regulation of phosphorus utilization obo:GO_0045967 Any process that reduces the rate of growth of all or part of an organism. obo:GO_0045967 obo:go.owl obo:GO_0045967 down regulation of growth rate obo:GO_0045967 down-regulation of growth rate obo:GO_0045967 downregulation of growth rate obo:GO_0045967 inhibition of growth rate obo:GO_0045967 biological_process obo:GO_0045967 GO:0045967 obo:GO_0045967 Note that this term and its definition depart from the usual conventions for GO 'regulation' process terms; regulation of rate is not usually distinguished from regulation of extent or frequency, but it makes sense to do so for growth regulation. obo:GO_0045967 negative regulation of growth rate obo:GO_0046324 Any process that modulates the frequency, rate or extent of the import of the hexose monosaccharide glucose into a cell or organelle. obo:GO_0046324 obo:go.owl obo:GO_0046324 regulation of glucose uptake obo:GO_0046324 biological_process obo:GO_0046324 GO:0046324 obo:GO_0046324 regulation of glucose import obo:GO_0046325 Any process that stops, prevents, or reduces the frequency, rate or extent of the import of the hexose monosaccharide glucose into a cell or organelle. obo:GO_0046325 obo:go.owl obo:GO_0046325 down regulation of glucose import obo:GO_0046325 down-regulation of glucose import obo:GO_0046325 downregulation of glucose import obo:GO_0046325 negative regulation of glucose uptake obo:GO_0046325 inhibition of glucose import obo:GO_0046325 biological_process obo:GO_0046325 GO:0046325 obo:GO_0046325 negative regulation of glucose import obo:GO_0046326 Any process that activates or increases the frequency, rate or extent of the import of the hexose monosaccharide glucose into a cell or organelle. obo:GO_0046326 obo:go.owl obo:GO_0046326 positive regulation of glucose uptake obo:GO_0046326 up regulation of glucose import obo:GO_0046326 up-regulation of glucose import obo:GO_0046326 upregulation of glucose import obo:GO_0046326 activation of glucose import obo:GO_0046326 stimulation of glucose import obo:GO_0046326 biological_process obo:GO_0046326 GO:0046326 obo:GO_0046326 positive regulation of glucose import obo:GO_0046332 Interacting selectively and non-covalently with a SMAD signaling protein. obo:GO_0046332 obo:go.owl obo:GO_0046332 molecular_function obo:GO_0046332 GO:0046332 obo:GO_0046332 SMAD binding obo:GO_0046483 The chemical reactions and pathways involving heterocyclic compounds, those with a cyclic molecular structure and at least two different atoms in the ring (or rings). obo:GO_0046483 obo:go.owl obo:GO_0046483 heterocycle metabolism obo:GO_0046483 biological_process obo:GO_0046483 GO:0046483 obo:GO_0046483 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0046483 heterocycle metabolic process obo:GO_0046527 Catalysis of the transfer of a glucosyl group to an acceptor molecule, typically another carbohydrate or a lipid. obo:GO_0046527 obo:go.owl obo:GO_0046527 EC:2.4.1 obo:GO_0046527 molecular_function obo:GO_0046527 GO:0046527 obo:GO_0046527 glucosyltransferase activity obo:GO_0046535 The series of events required for a umami taste stimulus to be received and converted to a molecular signal. Umami taste is the savory taste of meats and other foods that are rich in glutamates. obo:GO_0046535 obo:go.owl obo:GO_0046535 perception of umami taste, detection of chemical stimulus obo:GO_0046535 perception of umami taste, sensory transduction of chemical stimulus obo:GO_0046535 sensory detection of chemical stimulus during perception of umami taste obo:GO_0046535 sensory detection of umami taste obo:GO_0046535 sensory transduction of chemical stimulus during perception of umami taste obo:GO_0046535 sensory transduction of umami taste obo:GO_0046535 umami taste detection obo:GO_0046535 biological_process obo:GO_0046535 GO:0046535 obo:GO_0046535 detection of chemical stimulus involved in sensory perception of umami taste obo:GO_0046586 Any process that modulates the frequency, rate or extent of the attachment of one cell to another cell via adhesion molecules that require the presence of calcium for the interaction. obo:GO_0046586 obo:go.owl obo:GO_0046586 biological_process obo:GO_0046586 GO:0046586 obo:GO_0046586 regulation of calcium-dependent cell-cell adhesion obo:GO_0046587 Any process that activates or increases the frequency, rate or extent of calcium-dependent cell-cell adhesion. obo:GO_0046587 obo:go.owl obo:GO_0046587 up regulation of calcium-dependent cell-cell adhesion obo:GO_0046587 up-regulation of calcium-dependent cell-cell adhesion obo:GO_0046587 upregulation of calcium-dependent cell-cell adhesion obo:GO_0046587 activation of calcium-dependent cell-cell adhesion obo:GO_0046587 stimulation of calcium-dependent cell-cell adhesion obo:GO_0046587 biological_process obo:GO_0046587 GO:0046587 obo:GO_0046587 positive regulation of calcium-dependent cell-cell adhesion obo:GO_0046588 Any process that stops, prevents, or reduces the frequency, rate or extent of calcium-dependent cell-cell adhesion. obo:GO_0046588 obo:go.owl obo:GO_0046588 down regulation of calcium-dependent cell-cell adhesion obo:GO_0046588 down-regulation of calcium-dependent cell-cell adhesion obo:GO_0046588 downregulation of calcium-dependent cell-cell adhesion obo:GO_0046588 inhibition of calcium-dependent cell-cell adhesion obo:GO_0046588 biological_process obo:GO_0046588 GO:0046588 obo:GO_0046588 negative regulation of calcium-dependent cell-cell adhesion obo:GO_0046625 Interacting selectively and non-covalently with sphingolipids, a class of lipids containing the long-chain amine diol sphingosine or a closely related base (a sphingoid). obo:GO_0046625 obo:go.owl obo:GO_0046625 molecular_function obo:GO_0046625 GO:0046625 obo:GO_0046625 sphingolipid binding obo:GO_0046659 The action characteristic of a hormone that takes part in the digestion process. obo:GO_0046659 obo:go.owl obo:GO_0046659 secretin obo:GO_0046659 molecular_function obo:GO_0046659 GO:0046659 obo:GO_0046659 digestive hormone activity obo:GO_0046677 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an antibiotic stimulus. An antibiotic is a chemical substance produced by a microorganism which has the capacity to inhibit the growth of or to kill other microorganisms. obo:GO_0046677 obo:go.owl obo:GO_0046677 biological_process obo:GO_0046677 antibiotic susceptibility/resistance obo:GO_0046677 GO:0046677 obo:GO_0046677 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0046677 response to antibiotic obo:GO_0046679 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a streptomycin stimulus. Streptomycin is a commonly used antibiotic in cell culture media which acts only on prokaryotes and blocks transition from initiation complex to chain elongating ribosome. obo:GO_0046679 obo:go.owl obo:GO_0046679 biological_process obo:GO_0046679 streptomycin susceptibility/resistance obo:GO_0046679 GO:0046679 obo:GO_0046679 response to streptomycin obo:GO_0046703 Interacting selectively and non-covalently with a lectin-like natural killer cell receptor. obo:GO_0046703 obo:go.owl obo:GO_0046703 NK cell lectin-like receptor binding obo:GO_0046703 KLRC4 receptor binding obo:GO_0046703 NKG2D receptor binding obo:GO_0046703 molecular_function obo:GO_0046703 GO:0046703 obo:GO_0046703 natural killer cell lectin-like receptor binding obo:GO_0046714 Interacting selectively and non-covalently with borate, the anion (BO3)3-. obo:GO_0046714 obo:go.owl obo:GO_0046714 molecular_function obo:GO_0046714 boron binding obo:GO_0046714 GO:0046714 obo:GO_0046714 borate binding obo:GO_0046777 The phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation). obo:GO_0046777 obo:go.owl obo:GO_0046777 MIPS_funcat:14.07.03 obo:GO_0046777 Wikipedia:Autophosphorylation obo:GO_0046777 protein amino acid autophosphorylation obo:GO_0046777 biological_process obo:GO_0046777 GO:0046777 obo:GO_0046777 protein autophosphorylation obo:GO_0046787 The process of restoring viral DNA after damage or errors in replication. obo:GO_0046787 obo:go.owl obo:GO_0046787 biological_process obo:GO_0046787 GO:0046787 obo:GO_0046787 viral DNA repair obo:GO_0046817 Interacts with chemokine receptors to reduce the action of a chemokine. obo:GO_0046817 obo:go.owl obo:GO_0046817 molecular_function obo:GO_0046817 GO:0046817 obo:GO_0046817 chemokine receptor antagonist activity obo:GO_0046822 Any process that modulates the frequency, rate or extent of the directed movement of substances between the nucleus and the cytoplasm. obo:GO_0046822 obo:go.owl obo:GO_0046822 biological_process obo:GO_0046822 GO:0046822 obo:GO_0046822 regulation of nucleocytoplasmic transport obo:GO_0046823 Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of substances between the cytoplasm and the nucleus. obo:GO_0046823 obo:go.owl obo:GO_0046823 down regulation of nucleocytoplasmic transport obo:GO_0046823 down-regulation of nucleocytoplasmic transport obo:GO_0046823 downregulation of nucleocytoplasmic transport obo:GO_0046823 inhibition of nucleocytoplasmic transport obo:GO_0046823 biological_process obo:GO_0046823 GO:0046823 obo:GO_0046823 negative regulation of nucleocytoplasmic transport obo:GO_0046824 Any process that activates or increases the frequency, rate or extent of the directed movement of substances between the nucleus and the cytoplasm. obo:GO_0046824 obo:go.owl obo:GO_0046824 up regulation of nucleocytoplasmic transport obo:GO_0046824 up-regulation of nucleocytoplasmic transport obo:GO_0046824 upregulation of nucleocytoplasmic transport obo:GO_0046824 activation of nucleocytoplasmic transport obo:GO_0046824 stimulation of nucleocytoplasmic transport obo:GO_0046824 biological_process obo:GO_0046824 GO:0046824 obo:GO_0046824 positive regulation of nucleocytoplasmic transport obo:GO_0046870 Interacting selectively and non-covalently with cadmium (Cd) ions. obo:GO_0046870 obo:go.owl obo:GO_0046870 copper/cadmium binding obo:GO_0046870 cadmium binding obo:GO_0046870 molecular_function obo:GO_0046870 GO:0046870 obo:GO_0046870 cadmium ion binding obo:GO_0046871 Interacting selectively and non-covalently with N-acetylgalactosamine, 2-acetamido-2-deoxygalactopyranose, the n-acetyl derivative of galactosamine. obo:GO_0046871 obo:go.owl obo:GO_0046871 molecular_function obo:GO_0046871 N-acetylgalactosamine lectin obo:GO_0046871 GO:0046871 obo:GO_0046871 N-acetylgalactosamine binding obo:GO_0046872 Interacting selectively and non-covalently with any metal ion. obo:GO_0046872 obo:go.owl obo:GO_0046872 MIPS_funcat:16.17 obo:GO_0046872 metal binding obo:GO_0046872 heavy metal binding obo:GO_0046872 molecular_function obo:GO_0046872 GO:0046872 obo:GO_0046872 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_agr obo:GO_0046872 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_flybase_ribbon obo:GO_0046872 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0046872 metal ion binding obo:GO_0046875 Interacting selectively and non-covalently with an ephrin receptor. obo:GO_0046875 obo:go.owl obo:GO_0046875 Eph receptor binding obo:GO_0046875 GPI-linked ephrin obo:GO_0046875 ephrin obo:GO_0046875 transmembrane ephrin obo:GO_0046875 molecular_function obo:GO_0046875 GO:0046875 obo:GO_0046875 ephrin receptor binding obo:GO_0046876 Interacting selectively and non-covalently with 3,4-didehydroretinal, a form of retinal that plays a role in the visual process in freshwater fish and some amphibians analogous to that of all-trans retinal in other vertebrates. 3,4-didehydro-11-cis-retinal combines with an opsin to form cyanopsin (cone) or porphyropsin (rod). obo:GO_0046876 obo:go.owl obo:GO_0046876 UV-sensitive opsin obo:GO_0046876 blue-sensitive opsin obo:GO_0046876 green-sensitive opsin obo:GO_0046876 long-wave-sensitive opsin obo:GO_0046876 opsin obo:GO_0046876 red-sensitive opsin obo:GO_0046876 short-wave-sensitive opsin obo:GO_0046876 violet-sensitive opsin obo:GO_0046876 molecular_function obo:GO_0046876 GO:0046876 obo:GO_0046876 3,4-didehydroretinal binding obo:GO_0046903 The controlled release of a substance by a cell or a tissue. obo:GO_0046903 obo:go.owl obo:GO_0046903 MIPS_funcat:20.09.16 obo:GO_0046903 biological_process obo:GO_0046903 GO:0046903 obo:GO_0046903 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0046903 secretion obo:GO_0046906 Interacting selectively and non-covalently with a tetrapyrrole, a compound containing four pyrrole nuclei variously substituted and linked to each other through carbons at the alpha position. obo:GO_0046906 obo:go.owl obo:GO_0046906 porphyrin binding obo:GO_0046906 molecular_function obo:GO_0046906 GO:0046906 obo:GO_0046906 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0046906 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0046906 tetrapyrrole binding obo:GO_0046911 The formation of bonds from two or more atoms within the same ligand to a metal atom in complexes in which the metal is part of a ring. obo:GO_0046911 obo:go.owl obo:GO_0046911 metal chelation obo:GO_0046911 heavy metal chelation obo:GO_0046911 molecular_function obo:GO_0046911 GO:0046911 obo:GO_0046911 metal chelating activity obo:GO_0046914 Interacting selectively and non-covalently with a transition metal ions; a transition metal is an element whose atom has an incomplete d-subshell of extranuclear electrons, or which gives rise to a cation or cations with an incomplete d-subshell. Transition metals often have more than one valency state. Biologically relevant transition metals include vanadium, manganese, iron, copper, cobalt, nickel, molybdenum and silver. obo:GO_0046914 obo:go.owl obo:GO_0046914 molecular_function obo:GO_0046914 GO:0046914 obo:GO_0046914 transition metal ion binding obo:GO_0046920 Catalysis of the transfer of an L-fucosyl group from GDP-beta-L-fucose to an acceptor molecule to form an alpha-(1->3) linkage. obo:GO_0046920 obo:go.owl obo:GO_0046920 Reactome:R-HSA-9603984 obo:GO_0046920 Reactome:R-HSA-9605609 obo:GO_0046920 Reactome:R-HSA-9605644 obo:GO_0046920 Reactome:R-HSA-9605682 obo:GO_0046920 alpha(1,3)-fucosyltransferase activity obo:GO_0046920 alpha-(1,3)-fucosyltransferase activity obo:GO_0046920 alpha-1,3-fucosyltransferase activity obo:GO_0046920 molecular_function obo:GO_0046920 GO:0046920 obo:GO_0046920 alpha-(1->3)-fucosyltransferase activity obo:GO_0046921 Catalysis of the transfer of an L-fucosyl group from GDP-beta-L-fucose to an acceptor molecule to form an alpha-(1->6) linkage. obo:GO_0046921 obo:go.owl obo:GO_0046921 alpha(1,6)-fucosyltransferase activity obo:GO_0046921 alpha-(1,6)-fucosyltransferase activity obo:GO_0046921 alpha-1,6-fucosyltransferase activity obo:GO_0046921 molecular_function obo:GO_0046921 GO:0046921 obo:GO_0046921 alpha-(1->6)-fucosyltransferase activity obo:GO_0046923 Interacting selectively and non-covalently with an endoplasmic reticulum (ER) retention sequence, a specific peptide sequence that ensures a protein is retained within the ER. obo:GO_0046923 obo:go.owl obo:GO_0046923 endoplasmic reticulum retention sequence binding obo:GO_0046923 molecular_function obo:GO_0046923 GO:0046923 obo:GO_0046923 ER retention sequence binding obo:GO_0046965 Interacting selectively and non-covalently with a retinoid X receptor. obo:GO_0046965 obo:go.owl obo:GO_0046965 RXR binding obo:GO_0046965 molecular_function obo:GO_0046965 GO:0046965 obo:GO_0046965 retinoid X receptor binding obo:GO_0046966 Interacting selectively and non-covalently with a thyroid hormone receptor. obo:GO_0046966 obo:go.owl obo:GO_0046966 ligand-dependent thyroid hormone receptor interactor activity obo:GO_0046966 molecular_function obo:GO_0046966 GO:0046966 obo:GO_0046966 thyroid hormone receptor binding obo:GO_0046977 Interacting selectively and non-covalently with TAP protein, transporter associated with antigen processing protein. TAP protein is a heterodimeric peptide transporter consisting of the subunits TAP1 and TAP2. obo:GO_0046977 obo:go.owl obo:GO_0046977 molecular_function obo:GO_0046977 GO:0046977 obo:GO_0046977 TAP binding obo:GO_0046978 Interacting selectively and non-covalently with the TAP1 subunit of TAP (transporter associated with antigen processing) protein. obo:GO_0046978 obo:go.owl obo:GO_0046978 molecular_function obo:GO_0046978 GO:0046978 obo:GO_0046978 TAP1 binding obo:GO_0046979 Interacting selectively and non-covalently with the TAP2 subunit of TAP (transporter associated with antigen processing) protein. obo:GO_0046979 obo:go.owl obo:GO_0046979 molecular_function obo:GO_0046979 GO:0046979 obo:GO_0046979 TAP2 binding obo:GO_0046980 Interacting selectively and non-covalently with tapasin, a member of the MHC class I loading complex which bridges the TAP peptide transporter to class I molecules. obo:GO_0046980 obo:go.owl obo:GO_0046980 TAP binding protein binding obo:GO_0046980 molecular_function obo:GO_0046980 TAPBP binding obo:GO_0046980 GO:0046980 obo:GO_0046980 tapasin binding obo:GO_0046982 Interacting selectively and non-covalently with a nonidentical protein to form a heterodimer. obo:GO_0046982 obo:go.owl obo:GO_0046982 molecular_function obo:GO_0046982 GO:0046982 obo:GO_0046982 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0046982 protein heterodimerization activity obo:GO_0046983 The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits. obo:GO_0046983 obo:go.owl obo:GO_0046983 molecular_function obo:GO_0046983 GO:0046983 obo:GO_0046983 protein dimerization activity obo:GO_0047322 Catalysis of the reaction: [3-hydroxy-3-methylglutaryl-CoA reductase (NADPH)] + ATP = [3-hydroxy-3-methylglutaryl-CoA reductase (NADPH)] phosphate + ADP. obo:GO_0047322 obo:go.owl obo:GO_0047322 reductase kinase activity obo:GO_0047322 EC:2.7.11.31 obo:GO_0047322 MetaCyc:2.7.1.109-RXN obo:GO_0047322 3-hydroxy-3-methylglutaryl coenzyme A reductase kinase activity obo:GO_0047322 3-hydroxy-3-methylglutaryl-CoA reductase kinase activity obo:GO_0047322 ATP:hydroxymethylglutaryl-CoA reductase (NADPH) phosphotransferase activity obo:GO_0047322 HMG-CoA reductase kinase activity obo:GO_0047322 beta-hydroxy-beta-methylglutaryl-CoA reductase kinase activity obo:GO_0047322 hydroxymethylglutaryl coenzyme A reductase kinase (phosphorylating) activity obo:GO_0047322 hydroxymethylglutaryl coenzyme A reductase kinase activity obo:GO_0047322 hydroxymethylglutaryl-CoA reductase (NADPH) kinase activity obo:GO_0047322 hydroxymethylglutaryl-CoA reductase (NADPH2) kinase activity obo:GO_0047322 hydroxymethylglutaryl-CoA reductase kinase activity obo:GO_0047322 molecular_function obo:GO_0047322 AMPK obo:GO_0047322 STK29 obo:GO_0047322 GO:0047322 obo:GO_0047322 [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase activity obo:GO_0047323 Catalysis of the reaction: ATP + 3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) = ADP + 3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) phosphate. obo:GO_0047323 obo:go.owl obo:GO_0047323 EC:2.7.11.4 obo:GO_0047323 MetaCyc:2.7.11.4-RXN obo:GO_0047323 Reactome:R-HSA-5693148 obo:GO_0047323 3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase activity obo:GO_0047323 ATP:3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) phosphotransferase activity obo:GO_0047323 BCKD kinase activity obo:GO_0047323 BCODH kinase activity obo:GO_0047323 [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] kinase activity obo:GO_0047323 branched-chain 2-oxo acid dehydrogenase kinase activity obo:GO_0047323 branched-chain alpha-ketoacid dehydrogenase kinase activity obo:GO_0047323 branched-chain keto acid dehydrogenase kinase activity obo:GO_0047323 branched-chain oxo acid dehydrogenase kinase (phosphorylating) activity obo:GO_0047323 molecular_function obo:GO_0047323 BCK obo:GO_0047323 STK2 obo:GO_0047323 GO:0047323 obo:GO_0047323 [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase activity obo:GO_0047384 Catalysis of the reaction: H2O + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate = phosphate + [hydroxymethylglutaryl-CoA reductase (NADPH)]. obo:GO_0047384 obo:go.owl obo:GO_0047384 reductase phosphatase activity obo:GO_0047384 EC:3.1.3.47 obo:GO_0047384 MetaCyc:3.1.3.47-RXN obo:GO_0047384 hydroxymethylglutaryl-CoA reductase (NADPH)-phosphatase activity obo:GO_0047384 hydroxymethylglutaryl-CoA reductase (NADPH)-phosphate phosphohydrolase activity obo:GO_0047384 molecular_function obo:GO_0047384 GO:0047384 obo:GO_0047384 [hydroxymethylglutaryl-CoA reductase (NADPH)]-phosphatase activity obo:GO_0047385 Catalysis of the reaction: H2O + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate = phosphate + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]. obo:GO_0047385 obo:go.owl obo:GO_0047385 branched-chain alpha-keto acid dehydrogenase phosphatase obo:GO_0047385 EC:3.1.3.52 obo:GO_0047385 MetaCyc:3.1.3.52-RXN obo:GO_0047385 3-methyl-2-oxobutanoate dehydrogenase (lipoamide)-phosphatase activity obo:GO_0047385 3-methyl-2-oxobutanoate dehydrogenase (lipoamide)-phosphate phosphohydrolase activity obo:GO_0047385 branched-chain 2-keto acid dehydrogenase phosphatase activity obo:GO_0047385 molecular_function obo:GO_0047385 branched-chain oxo-acid dehydrogenase phosphatase activity obo:GO_0047385 GO:0047385 obo:GO_0047385 [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]-phosphatase activity obo:GO_0047485 Interacting selectively and non-covalently with a protein N-terminus, the end of any peptide chain at which the 2-amino (or 2-imino) function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue. obo:GO_0047485 obo:go.owl obo:GO_0047485 N-terminal binding obo:GO_0047485 N-terminal end binding obo:GO_0047485 NH2-terminal binding obo:GO_0047485 NH2-terminus binding obo:GO_0047485 molecular_function obo:GO_0047485 amino-terminal binding obo:GO_0047485 amino-terminus binding obo:GO_0047485 GO:0047485 obo:GO_0047485 protein N-terminus binding obo:GO_0047696 Catalysis of the reaction: ATP + beta-adrenergic receptor = ADP + phospho-beta-adrenergic receptor. obo:GO_0047696 obo:go.owl obo:GO_0047696 ATP:beta-adrenergic-receptor phosphotransferase activity obo:GO_0047696 adrenergic receptor kinase activity obo:GO_0047696 EC:2.7.11.15 obo:GO_0047696 Reactome:R-HSA-8851797 obo:GO_0047696 Reactome:R-HSA-8866268 obo:GO_0047696 [b-adrenergic-receptor] kinase activity obo:GO_0047696 beta-AR kinase activity obo:GO_0047696 beta-adrenergic receptor-specific kinase activity obo:GO_0047696 beta-adrenergic-receptor kinase (phosphorylating) activity obo:GO_0047696 beta-adrenergic-receptor kinase activity obo:GO_0047696 beta-adrenoceptor kinase activity obo:GO_0047696 beta-receptor kinase activity obo:GO_0047696 beta-adrenoceptor kinase 1 activity obo:GO_0047696 beta-adrenoceptor kinase 2 activity obo:GO_0047696 molecular_function obo:GO_0047696 ADRBK1 obo:GO_0047696 BARK1 obo:GO_0047696 GRK2 obo:GO_0047696 GRK3 obo:GO_0047696 STK15 obo:GO_0047696 beta-ARK obo:GO_0047696 beta-ARK 1 obo:GO_0047696 beta-ARK 2 obo:GO_0047696 beta2ARK obo:GO_0047696 betaARK1 obo:GO_0047696 GO:0047696 obo:GO_0047696 beta-adrenergic receptor kinase activity obo:GO_0047848 Catalysis of the reaction: ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase] = ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase]. obo:GO_0047848 obo:go.owl obo:GO_0047848 reductase kinase activity obo:GO_0047848 EC:2.7.11.3 obo:GO_0047848 MetaCyc:DEPHOSPHO-REDUCTASE-KINASE-KINASE-RXN obo:GO_0047848 AMP-activated kinase activity obo:GO_0047848 AMP-activated protein kinase kinase activity obo:GO_0047848 ATP:dephospho-{hydroxymethylglutaryl-CoA reductase (NADPH)kinase} phosphotransferase activity obo:GO_0047848 dephospho-reductase kinase kinase activity obo:GO_0047848 hydroxymethylglutaryl coenzyme A reductase kinase kinase (phosphorylating) activity obo:GO_0047848 hydroxymethylglutaryl coenzyme A reductase kinase kinase activity obo:GO_0047848 reductase kinase kinase activity obo:GO_0047848 molecular_function obo:GO_0047848 STK30 obo:GO_0047848 GO:0047848 obo:GO_0047848 dephospho-[reductase kinase] kinase activity obo:GO_0048018 The activity of a gene product that interacts with a receptor to effect a change in the activity of the receptor. Ligands may be produced by the same, or different, cell that expresses the receptor. Ligands may diffuse extracellularly from their point of origin to the receiving cell, or remain attached to an adjacent cell surface (e.g. Notch ligands). obo:GO_0048018 obo:go.owl obo:GO_0048018 midori obo:GO_0048018 2010-09-13T04:51:59Z obo:GO_0048018 GO:0071884 obo:GO_0048018 receptor agonist activity obo:GO_0048018 signaling molecule obo:GO_0048018 signaling receptor ligand activity obo:GO_0048018 vitamin D receptor activator activity obo:GO_0048018 molecular_function obo:GO_0048018 GO:0048018 obo:GO_0048018 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0048018 Definition discussed in https://github.com/geneontology/go-ontology/issues/14220 obo:GO_0048018 receptor ligand activity obo:GO_0048019 The activity of a gene product that interacts with a receptor to decrease the ability of the receptor agonist to bind and activate the receptor. obo:GO_0048019 obo:go.owl obo:GO_0048019 receptor ligand activity obo:GO_0048019 molecular_function obo:GO_0048019 GO:0048019 obo:GO_0048019 receptor antagonist activity obo:GO_0048020 Interacting selectively and non-covalently with a CCR chemokine receptor. obo:GO_0048020 obo:go.owl obo:GO_0048020 beta chemokine receptor binding obo:GO_0048020 CCR chemokine receptor ligand obo:GO_0048020 beta chemokine receptor ligand obo:GO_0048020 molecular_function obo:GO_0048020 GO:0048020 obo:GO_0048020 CCR chemokine receptor binding obo:GO_0048027 Interacting selectively and non-covalently with the 5' untranslated region of an mRNA molecule. obo:GO_0048027 obo:go.owl obo:GO_0048027 mRNA 5' UTR binding obo:GO_0048027 molecular_function obo:GO_0048027 GO:0048027 obo:GO_0048027 mRNA 5'-UTR binding obo:GO_0048028 Interacting selectively and non-covalently with any simple or complex galacturonan. Galacturonan is any glycan composed solely of galacturonic acid residues, a specific type of glycuronan, and a constituent of some pectins. obo:GO_0048028 obo:go.owl obo:GO_0048028 molecular_function obo:GO_0048028 polygalacturonide binding obo:GO_0048028 GO:0048028 obo:GO_0048028 galacturonan binding obo:GO_0048029 Interacting selectively and non-covalently with any monosaccharide. Monosaccharides are the simplest carbohydrates; they are polyhydroxy aldehydes H[CH(OH)]nC(=O)H or polyhydroxy ketones H[CHOH]nC(=O)[CHOH]mH with three or more carbon atoms. They form the constitutional repeating units of oligo- and polysaccharides. obo:GO_0048029 obo:go.owl obo:GO_0048029 molecular_function obo:GO_0048029 GO:0048029 obo:GO_0048029 monosaccharide binding obo:GO_0048030 Interacting selectively and non-covalently with any disaccharide. Disaccharides are sugars composed of two monosaccharide units. obo:GO_0048030 obo:go.owl obo:GO_0048030 molecular_function obo:GO_0048030 GO:0048030 obo:GO_0048030 disaccharide binding obo:GO_0048031 Interacting selectively and non-covalently with any trisaccharide. Trisaccharides are sugars composed of three monosaccharide units. obo:GO_0048031 obo:go.owl obo:GO_0048031 molecular_function obo:GO_0048031 GO:0048031 obo:GO_0048031 trisaccharide binding obo:GO_0048032 Interacting selectively and non-covalently with any galacturonate. Galacturonate is the anion of galacturonic acid, the uronic acid formally derived from galactose by oxidation of the hydroxymethylene group at C-6 to a carboxyl group. obo:GO_0048032 obo:go.owl obo:GO_0048032 galacturonic acid binding obo:GO_0048032 molecular_function obo:GO_0048032 GO:0048032 obo:GO_0048032 galacturonate binding obo:GO_0048037 Interacting selectively and non-covalently with a cofactor, a substance that is required for the activity of an enzyme or other protein. Cofactors may be inorganic, such as the metal atoms zinc, iron, and copper in certain forms, or organic, in which case they are referred to as coenzymes. Cofactors may either be bound tightly to active sites or bind loosely with the substrate. obo:GO_0048037 obo:go.owl obo:GO_0048037 MIPS_funcat:16.21 obo:GO_0048037 molecular_function obo:GO_0048037 GO:0048037 obo:GO_0048037 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0048037 cofactor binding obo:GO_0048038 Interacting selectively and non-covalently with a quinone, any member of a class of diketones derivable from aromatic compounds by conversion of two CH groups into CO groups with any necessary rearrangement of double bonds. obo:GO_0048038 obo:go.owl obo:GO_0048038 molecular_function obo:GO_0048038 GO:0048038 obo:GO_0048038 quinone binding obo:GO_0048039 Interacting selectively and non-covalently with ubiquinone, a quinone derivative with a tail of isoprene units. obo:GO_0048039 obo:go.owl obo:GO_0048039 coenzyme Q binding obo:GO_0048039 coenzyme Q6 binding obo:GO_0048039 molecular_function obo:GO_0048039 GO:0048039 obo:GO_0048039 ubiquinone binding obo:GO_0048145 Any process that modulates the frequency, rate or extent of multiplication or reproduction of fibroblast cells. obo:GO_0048145 obo:go.owl obo:GO_0048145 biological_process obo:GO_0048145 GO:0048145 obo:GO_0048145 regulation of fibroblast proliferation obo:GO_0048146 Any process that activates or increases the frequency, rate or extent of multiplication or reproduction of fibroblast cells. obo:GO_0048146 obo:go.owl obo:GO_0048146 up regulation of fibroblast proliferation obo:GO_0048146 up-regulation of fibroblast proliferation obo:GO_0048146 upregulation of fibroblast proliferation obo:GO_0048146 activation of fibroblast proliferation obo:GO_0048146 stimulation of fibroblast proliferation obo:GO_0048146 biological_process obo:GO_0048146 GO:0048146 obo:GO_0048146 positive regulation of fibroblast proliferation obo:GO_0048147 Any process that stops, prevents, or reduces the frequency, rate or extent of multiplication or reproduction of fibroblast cells. obo:GO_0048147 obo:go.owl obo:GO_0048147 down regulation of fibroblast proliferation obo:GO_0048147 down-regulation of fibroblast proliferation obo:GO_0048147 downregulation of fibroblast proliferation obo:GO_0048147 inhibition of fibroblast proliferation obo:GO_0048147 biological_process obo:GO_0048147 GO:0048147 obo:GO_0048147 negative regulation of fibroblast proliferation obo:GO_0048156 Interacting selectively and non-covalently with tau protein. tau is a microtubule-associated protein, implicated in Alzheimer's disease, Down Syndrome and ALS. obo:GO_0048156 obo:go.owl obo:GO_0048156 molecular_function obo:GO_0048156 GO:0048156 obo:GO_0048156 tau protein binding obo:GO_0048185 Interacting selectively and non-covalently with activin, a dimer of inhibin-beta subunits. obo:GO_0048185 obo:go.owl obo:GO_0048185 molecular_function obo:GO_0048185 GO:0048185 obo:GO_0048185 activin binding obo:GO_0048248 Interacting selectively and non-covalently with a the CXCR3 chemokine receptor. obo:GO_0048248 obo:go.owl obo:GO_0048248 molecular_function obo:GO_0048248 GO:0048248 obo:GO_0048248 CXCR3 chemokine receptor binding obo:GO_0048250 The process in which iron is transported from the cytosol, into the mitochondrial matrix. obo:GO_0048250 obo:go.owl obo:GO_0048250 al obo:GO_0048250 2016-02-10T11:24:22Z obo:GO_0048250 GO:1990925 obo:GO_0048250 mitochondrial iron cation transmembrane transport obo:GO_0048250 mitochondrial iron transport obo:GO_0048250 biological_process obo:GO_0048250 mitochondrial iron ion transmembrane transport obo:GO_0048250 mitochondrial iron ion transport obo:GO_0048250 GO:0048250 obo:GO_0048250 iron import into the mitochondrion obo:GO_0048273 Interacting selectively and non-covalently with mitogen-activated protein kinase p38, an enzyme that catalyzes the transfer of phosphate from ATP to hydroxyl side chains on proteins in response to mitogen activation. obo:GO_0048273 obo:go.owl obo:GO_0048273 MAPK p38 binding obo:GO_0048273 molecular_function obo:GO_0048273 GO:0048273 obo:GO_0048273 mitogen-activated protein kinase p38 binding obo:GO_0048306 Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules), in the presence of calcium. obo:GO_0048306 obo:go.owl obo:GO_0048306 molecular_function obo:GO_0048306 GO:0048306 obo:GO_0048306 calcium-dependent protein binding obo:GO_0048365 Interacting selectively and non-covalently with Rac protein, any member of the Rac subfamily of the Ras superfamily of monomeric GTPases. obo:GO_0048365 obo:go.owl obo:GO_0048365 molecular_function obo:GO_0048365 GO:0048365 obo:GO_0048365 Rac GTPase binding obo:GO_0048403 Interacting selectively and non-covalently with brain-derived neurotrophic factor. obo:GO_0048403 obo:go.owl obo:GO_0048403 BDNF binding obo:GO_0048403 molecular_function obo:GO_0048403 neurotrophin TRKB receptor activity obo:GO_0048403 GO:0048403 obo:GO_0048403 brain-derived neurotrophic factor binding obo:GO_0048406 Interacting selectively and non-covalently with nerve growth factor (NGF). obo:GO_0048406 obo:go.owl obo:GO_0048406 NGF binding obo:GO_0048406 beta-nerve growth factor binding obo:GO_0048406 molecular_function obo:GO_0048406 neurotrophin TRKA receptor activity obo:GO_0048406 GO:0048406 obo:GO_0048406 nerve growth factor binding obo:GO_0048407 Interacting selectively and non-covalently with platelet-derived growth factor. obo:GO_0048407 obo:go.owl obo:GO_0048407 PDGF binding obo:GO_0048407 molecular_function obo:GO_0048407 GO:0048407 obo:GO_0048407 platelet-derived growth factor binding obo:GO_0048408 Interacting selectively and non-covalently with epidermal growth factor. obo:GO_0048408 obo:go.owl obo:GO_0048408 EGF binding obo:GO_0048408 molecular_function obo:GO_0048408 GO:0048408 obo:GO_0048408 epidermal growth factor binding obo:GO_0048487 Interacting selectively and non-covalently with the microtubule constituent protein beta-tubulin. obo:GO_0048487 obo:go.owl obo:GO_0048487 beta tubulin binding obo:GO_0048487 molecular_function obo:GO_0048487 GO:0048487 obo:GO_0048487 beta-tubulin binding obo:GO_0048495 Interacting selectively and non-covalently with the Roundabout (ROBO) receptor, a transmembrane receptor. obo:GO_0048495 obo:go.owl obo:GO_0048495 molecular_function obo:GO_0048495 Roundabout receptor binding obo:GO_0048495 GO:0048495 obo:GO_0048495 Roundabout binding obo:GO_0048518 Any process that activates or increases the frequency, rate or extent of a biological process. Biological processes are regulated by many means; examples include the control of gene expression, protein modification or interaction with a protein or substrate molecule. obo:GO_0048518 obo:go.owl obo:GO_0048518 GO:0043119 obo:GO_0048518 positive regulation of physiological process obo:GO_0048518 up regulation of biological process obo:GO_0048518 up-regulation of biological process obo:GO_0048518 upregulation of biological process obo:GO_0048518 activation of biological process obo:GO_0048518 stimulation of biological process obo:GO_0048518 biological_process obo:GO_0048518 GO:0048518 obo:GO_0048518 http://purl.oboInOwllibrary.org/oboInOwl/go#gocheck_do_not_annotate obo:GO_0048518 positive regulation of biological process obo:GO_0048519 Any process that stops, prevents, or reduces the frequency, rate or extent of a biological process. Biological processes are regulated by many means; examples include the control of gene expression, protein modification or interaction with a protein or substrate molecule. obo:GO_0048519 obo:go.owl obo:GO_0048519 GO:0043118 obo:GO_0048519 down regulation of biological process obo:GO_0048519 down-regulation of biological process obo:GO_0048519 downregulation of biological process obo:GO_0048519 negative regulation of physiological process obo:GO_0048519 inhibition of biological process obo:GO_0048519 biological_process obo:GO_0048519 GO:0048519 obo:GO_0048519 http://purl.oboInOwllibrary.org/oboInOwl/go#gocheck_do_not_annotate obo:GO_0048519 negative regulation of biological process obo:GO_0048522 Any process that activates or increases the frequency, rate or extent of a cellular process, any of those that are carried out at the cellular level, but are not necessarily restricted to a single cell. For example, cell communication occurs among more than one cell, but occurs at the cellular level. obo:GO_0048522 obo:go.owl obo:GO_0048522 GO:0051242 obo:GO_0048522 positive regulation of cellular physiological process obo:GO_0048522 up regulation of cellular process obo:GO_0048522 up-regulation of cellular process obo:GO_0048522 upregulation of cellular process obo:GO_0048522 activation of cellular process obo:GO_0048522 stimulation of cellular process obo:GO_0048522 biological_process obo:GO_0048522 GO:0048522 obo:GO_0048522 positive regulation of cellular process obo:GO_0048523 Any process that stops, prevents, or reduces the frequency, rate or extent of a cellular process, any of those that are carried out at the cellular level, but are not necessarily restricted to a single cell. For example, cell communication occurs among more than one cell, but occurs at the cellular level. obo:GO_0048523 obo:go.owl obo:GO_0048523 GO:0051243 obo:GO_0048523 down regulation of cellular process obo:GO_0048523 down-regulation of cellular process obo:GO_0048523 downregulation of cellular process obo:GO_0048523 negative regulation of cellular physiological process obo:GO_0048523 inhibition of cellular process obo:GO_0048523 biological_process obo:GO_0048523 GO:0048523 obo:GO_0048523 negative regulation of cellular process obo:GO_0048531 Catalysis of the transfer of a galactose residue from a donor molecule to an oligosaccharide, forming a beta-1,3-linkage. obo:GO_0048531 obo:go.owl obo:GO_0048531 molecular_function obo:GO_0048531 GO:0048531 obo:GO_0048531 beta-1,3-galactosyltransferase activity obo:GO_0048571 Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, a day length that exceeds a particular duration known as the 'critical day length'. The critical day length varies between species. Although the term long-day is used, most species actually respond to the duration of the night, so that the response will occur when a period of darkness falls short of the number of hours defined by 24 hours minus the critical day length. obo:GO_0048571 obo:go.owl obo:GO_0048571 response to long-day obo:GO_0048571 response to short-night obo:GO_0048571 short-night photoperiodism obo:GO_0048571 biological_process obo:GO_0048571 response to long-day photoperiod obo:GO_0048571 GO:0048571 obo:GO_0048571 long-day photoperiodism obo:GO_0048572 Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, a day length that falls short of a particular duration known as the 'critical day length'. The critical day length varies between species. Although the term short-day is used, most species actually respond to the duration of the night, so that the response will occur when a period of darkness exceeds the number of hours defined by 24 hours minus the critical day length. obo:GO_0048572 obo:go.owl obo:GO_0048572 long-night photoperiodism obo:GO_0048572 response to long-night obo:GO_0048572 response to short-day obo:GO_0048572 biological_process obo:GO_0048572 response to short-day photoperiod obo:GO_0048572 GO:0048572 obo:GO_0048572 short-day photoperiodism obo:GO_0048573 A change from the vegetative to the reproductive phase as a result of detection of, or exposure to, a period of light or dark of a given length. The length of the period of light or dark required to initiate the change is set relative to a particular duration known as the 'critical day length'. The critical day length varies between species. obo:GO_0048573 obo:go.owl obo:GO_0048573 photoperiodic control of flowering time obo:GO_0048573 photoperiodic control of inflorescence development obo:GO_0048573 response to day length, flowering obo:GO_0048573 response to night length, flowering obo:GO_0048573 response to photoperiod, flowering obo:GO_0048573 biological_process obo:GO_0048573 GO:0048573 obo:GO_0048573 photoperiodism, flowering obo:GO_0048574 A change from the vegetative to the reproductive phase as a result of detection of, or exposure to, a period of light that exceeds the critical day length. The critical day length varies between species. Although the term is long-day is used, most species actually respond to the duration of the night, so that the response will occur when a period of darkness falls short of the number of hours defined by 24 minus the critical day length. obo:GO_0048574 obo:go.owl obo:GO_0048574 long-day photoperiodic control of flowering obo:GO_0048574 long-day photoperiodic control of flowering time obo:GO_0048574 long-day photoperiodic control of inflorescence development obo:GO_0048574 response to long-day, flowering obo:GO_0048574 response to short-night, flowering obo:GO_0048574 short-night photoperiodism, flowering obo:GO_0048574 biological_process obo:GO_0048574 GO:0048574 obo:GO_0048574 long-day photoperiodism, flowering obo:GO_0048575 A change from vegetative to reproductive phase as a result of detection of, or exposure to, a period of light that falls short of the critical day length. The critical day length varies between species. Although the term is short-day is used, most species actually respond to the duration of the night, so that the response will occur when a period of darkness exceeds the number of hours defined by 24 minus the critical day length. obo:GO_0048575 obo:go.owl obo:GO_0048575 long-night photoperiodism, flowering obo:GO_0048575 response to long-night, flowering obo:GO_0048575 response to short-day, flowering obo:GO_0048575 short-day photoperiodic control of flowering obo:GO_0048575 short-day photoperiodic control of flowering time obo:GO_0048575 short-day photoperiodic control of inflorescence development obo:GO_0048575 biological_process obo:GO_0048575 GO:0048575 obo:GO_0048575 short-day photoperiodism, flowering obo:GO_0048583 Any process that modulates the frequency, rate or extent of a response to a stimulus. Response to stimulus is a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus. obo:GO_0048583 obo:go.owl obo:GO_0048583 biological_process obo:GO_0048583 GO:0048583 obo:GO_0048583 http://purl.oboInOwllibrary.org/oboInOwl/go#gocheck_do_not_manually_annotate obo:GO_0048583 Note that this term is in the subset of terms that should not be used for direct gene product annotation. Instead, select a child term or, if no appropriate child term exists, please request a new term. Direct annotations to this term may be amended during annotation QC. obo:GO_0048583 regulation of response to stimulus obo:GO_0048584 Any process that activates, maintains or increases the rate of a response to a stimulus. Response to stimulus is a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus. obo:GO_0048584 obo:go.owl obo:GO_0048584 up regulation of response to stimulus obo:GO_0048584 up-regulation of response to stimulus obo:GO_0048584 upregulation of response to stimulus obo:GO_0048584 activation of response to stimulus obo:GO_0048584 stimulation of response to stimulus obo:GO_0048584 biological_process obo:GO_0048584 GO:0048584 obo:GO_0048584 http://purl.oboInOwllibrary.org/oboInOwl/go#gocheck_do_not_manually_annotate obo:GO_0048584 Note that this term is in the subset of terms that should not be used for direct gene product annotation. Instead, select a child term or, if no appropriate child term exists, please request a new term. Direct annotations to this term may be amended during annotation QC. obo:GO_0048584 positive regulation of response to stimulus obo:GO_0048585 Any process that stops, prevents, or reduces the frequency, rate or extent of a response to a stimulus. Response to stimulus is a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus. obo:GO_0048585 obo:go.owl obo:GO_0048585 down regulation of response to stimulus obo:GO_0048585 down-regulation of response to stimulus obo:GO_0048585 downregulation of response to stimulus obo:GO_0048585 inhibition of response to stimulus obo:GO_0048585 biological_process obo:GO_0048585 GO:0048585 obo:GO_0048585 http://purl.oboInOwllibrary.org/oboInOwl/go#gocheck_do_not_manually_annotate obo:GO_0048585 Note that this term is in the subset of terms that should not be used for direct gene product annotation. Instead, select a child term or, if no appropriate child term exists, please request a new term. Direct annotations to this term may be amended during annotation QC. obo:GO_0048585 negative regulation of response to stimulus obo:GO_0048660 Any process that modulates the frequency, rate or extent of smooth muscle cell proliferation. obo:GO_0048660 obo:go.owl obo:GO_0048660 regulation of SMC proliferation obo:GO_0048660 biological_process obo:GO_0048660 GO:0048660 obo:GO_0048660 regulation of smooth muscle cell proliferation obo:GO_0048661 Any process that activates or increases the rate or extent of smooth muscle cell proliferation. obo:GO_0048661 obo:go.owl obo:GO_0048661 positive regulation of SMC proliferation obo:GO_0048661 up regulation of smooth muscle cell proliferation obo:GO_0048661 up-regulation of smooth muscle cell proliferation obo:GO_0048661 upregulation of smooth muscle cell proliferation obo:GO_0048661 activation of smooth muscle cell proliferation obo:GO_0048661 stimulation of smooth muscle cell proliferation obo:GO_0048661 biological_process obo:GO_0048661 GO:0048661 obo:GO_0048661 positive regulation of smooth muscle cell proliferation obo:GO_0048662 Any process that stops, prevents or reduces the rate or extent of smooth muscle cell proliferation. obo:GO_0048662 obo:go.owl obo:GO_0048662 down regulation of smooth muscle cell proliferation obo:GO_0048662 down-regulation of smooth muscle cell proliferation obo:GO_0048662 downregulation of smooth muscle cell proliferation obo:GO_0048662 negative regulation of SMC proliferation obo:GO_0048662 inhibition of smooth muscle cell proliferation obo:GO_0048662 biological_process obo:GO_0048662 GO:0048662 obo:GO_0048662 negative regulation of smooth muscle cell proliferation obo:GO_0048878 Any biological process involved in the maintenance of an internal steady state of a chemical. obo:GO_0048878 obo:go.owl obo:GO_0048878 biological_process obo:GO_0048878 GO:0048878 obo:GO_0048878 chemical homeostasis obo:GO_0050115 Catalysis of the reaction: myosin light-chain phosphate + H2O = myosin light chain + phosphate. obo:GO_0050115 obo:go.owl obo:GO_0050115 EC:3.1.3.53 obo:GO_0050115 MetaCyc:MYOSIN-LIGHT-CHAIN-PHOSPHATASE-RXN obo:GO_0050115 Reactome:R-HSA-419232 obo:GO_0050115 [Myosin light-chain]-phosphatase activity obo:GO_0050115 myosin light chain kinase phosphatase activity obo:GO_0050115 myosin-light-chain phosphatase activity obo:GO_0050115 myosin-light-chain-phosphate phosphohydrolase activity obo:GO_0050115 molecular_function obo:GO_0050115 myosin light-chain kinase phosphatase activity obo:GO_0050115 protein phosphatase 2A obo:GO_0050115 GO:0050115 obo:GO_0050115 myosin-light-chain-phosphatase activity obo:GO_0050196 Catalysis of the reaction: [phosphorylase a] + 4 H2O = 2 [phosphorylase b] + 4 phosphate. obo:GO_0050196 obo:go.owl obo:GO_0050196 EC:3.1.3.17 obo:GO_0050196 MetaCyc:PHOSPHORYLASE-PHOSPHATASE-RXN obo:GO_0050196 glycogen phosphorylase phosphatase activity obo:GO_0050196 phosphorylase a phosphatase activity obo:GO_0050196 phosphorylase a phosphohydrolase activity obo:GO_0050196 phosphorylase phosphatase activity obo:GO_0050196 type 1 protein phosphatase activity obo:GO_0050196 molecular_function obo:GO_0050196 PR-enzyme obo:GO_0050196 protein phosphatase C obo:GO_0050196 GO:0050196 obo:GO_0050196 [phosphorylase] phosphatase activity obo:GO_0050254 Catalysis of the reaction: ATP + rhodopsin = ADP + phosphorhodopsin. obo:GO_0050254 obo:go.owl obo:GO_0050254 EC:2.7.11.14 obo:GO_0050254 MetaCyc:2.7.11.14-RXN obo:GO_0050254 Reactome:R-HSA-2581474 obo:GO_0050254 ATP:rhodopsin phosphotransferase activity obo:GO_0050254 opsin kinase (phosphorylating) activity obo:GO_0050254 opsin kinase activity obo:GO_0050254 rhodopsin kinase (phosphorylating) activity obo:GO_0050254 G-protein-coupled receptor kinase 1 activity obo:GO_0050254 GPCR kinase 1 activity obo:GO_0050254 cone opsin kinase activity obo:GO_0050254 molecular_function obo:GO_0050254 GRK1 obo:GO_0050254 GRK7 obo:GO_0050254 RK obo:GO_0050254 STK14 obo:GO_0050254 GO:0050254 obo:GO_0050254 rhodopsin kinase activity obo:GO_0050321 Catalysis of the reaction: ATP + tau-protein = ADP + O-phospho-tau-protein. obo:GO_0050321 obo:go.owl obo:GO_0050321 ATP:tau-protein O-phosphotransferase activity obo:GO_0050321 EC:2.7.11.26 obo:GO_0050321 MetaCyc:TAU-PROTEIN-KINASE-RXN obo:GO_0050321 [Tau protein] kinase activity obo:GO_0050321 glycogen synthase kinase-3beta activity obo:GO_0050321 protein tau kinase activity obo:GO_0050321 tau kinase activity obo:GO_0050321 tau protein kinase activity obo:GO_0050321 brain protein kinase PK40erk activity obo:GO_0050321 tau-protein kinase I activity obo:GO_0050321 tau-protein kinase II activity obo:GO_0050321 tau-tubulin kinase activity obo:GO_0050321 molecular_function obo:GO_0050321 CDK5/p23 obo:GO_0050321 GSK obo:GO_0050321 STK31 obo:GO_0050321 TPK obo:GO_0050321 TPK I obo:GO_0050321 TPK II obo:GO_0050321 TTK obo:GO_0050321 cdk5/p20 obo:GO_0050321 GO:0050321 obo:GO_0050321 tau-protein kinase activity obo:GO_0050359 Catalysis of the reaction: ATP + tropomyosin = ADP + O-phosphotropomyosin. obo:GO_0050359 obo:go.owl obo:GO_0050359 EC:2.7.11.28 obo:GO_0050359 MetaCyc:TROPOMYOSIN-KINASE-RXN obo:GO_0050359 ATP:tropomyosin O-phosphotransferase activity obo:GO_0050359 tropomyosin kinase (phosphorylating) activity obo:GO_0050359 molecular_function obo:GO_0050359 STK obo:GO_0050359 GO:0050359 obo:GO_0050359 tropomyosin kinase activity obo:GO_0050369 Catalysis of the reaction: ATP + [tyrosine-3-monooxygenase] = ADP + phospho-[tyrosine-3-monooxygenase]. obo:GO_0050369 obo:go.owl obo:GO_0050369 EC:2.7.11.6 obo:GO_0050369 MetaCyc:2.7.11.6-RXN obo:GO_0050369 ATP:tyrosine-3-monoxygenase phosphotransferase activity obo:GO_0050369 pheochromocytoma tyrosine hydroxylase-associated kinase activity obo:GO_0050369 tyrosine 3-monooxygenase kinase (phosphorylating) activity obo:GO_0050369 tyrosine 3-monooxygenase kinase activity obo:GO_0050369 molecular_function obo:GO_0050369 STK4 obo:GO_0050369 GO:0050369 obo:GO_0050369 [tyrosine 3-monooxygenase] kinase activity obo:GO_0050405 Catalysis of the reaction: ATP + [acetyl-CoA carboxylase] = ADP + [acetyl-CoA carboxylase] phosphate. obo:GO_0050405 obo:go.owl obo:GO_0050405 EC:2.7.11.27 obo:GO_0050405 MetaCyc:2.7.11.27-RXN obo:GO_0050405 ATP:acetyl-CoA carboxylase phosphotransferase activity obo:GO_0050405 acetyl coenzyme A carboxylase kinase (phosphorylating) activity obo:GO_0050405 acetyl-CoA carboxylase kinase (AMP-activated) activity obo:GO_0050405 acetyl-CoA carboxylase kinase (cAMP-independent) activity obo:GO_0050405 acetyl-CoA carboxylase kinase activity obo:GO_0050405 acetyl-coenzyme A carboxylase kinase activity obo:GO_0050405 I-peptide kinase activity obo:GO_0050405 acetyl-CoA carboxylase bound kinase activity obo:GO_0050405 acetyl-CoA carboxylase kinase 2 activity obo:GO_0050405 acetyl-CoA carboxylase kinase-2 activity obo:GO_0050405 acetyl-CoA carboxylase kinase-3 (AMP-activated) activity obo:GO_0050405 molecular_function obo:GO_0050405 ACK2 obo:GO_0050405 ACK3 obo:GO_0050405 AMPK obo:GO_0050405 STK5 obo:GO_0050405 GO:0050405 obo:GO_0050405 [acetyl-CoA carboxylase] kinase activity obo:GO_0050406 Catalysis of the reaction: [acetyl-CoA carboxylase]-phosphate + H2O = [acetyl-CoA carboxylase] + phosphate. obo:GO_0050406 obo:go.owl obo:GO_0050406 EC:3.1.3.44 obo:GO_0050406 MetaCyc:ACETYL-COA-CARBOXYLASE-PHOSPHATASE-RXN obo:GO_0050406 acetyl-CoA carboxylase-phosphatase activity obo:GO_0050406 acetyl-CoA:carbon-dioxide ligase (ADP-forming)-phosphate phosphohydrolase activity obo:GO_0050406 molecular_function obo:GO_0050406 GO:0050406 obo:GO_0050406 [acetyl-CoA carboxylase]-phosphatase activity obo:GO_0050407 Catalysis of the reaction: [glycogen-synthase D] + H2O = [glycogen-synthase I] + phosphate. obo:GO_0050407 obo:go.owl obo:GO_0050407 EC:3.1.3.42 obo:GO_0050407 MetaCyc:GLYCOGEN-SYNTHASE-D-PHOSPHATASE-RXN obo:GO_0050407 Mg2+ dependent glycogen synthase phosphatase activity obo:GO_0050407 UDP-glucose:glycogen 4-alpha-D-glucosyltransferase-D phosphohydrolase activity obo:GO_0050407 UDP-glycogen glucosyltransferase phosphatase activity obo:GO_0050407 UDPglucose-glycogen glucosyltransferase phosphatase activity obo:GO_0050407 UDPglucose:glycogen 4-alpha-D-glucosyltransferase-D phosphohydrolase activity obo:GO_0050407 glycogen glucosyltransferase phosphatase activity obo:GO_0050407 glycogen synthase D phosphatase activity obo:GO_0050407 glycogen synthase phosphatase activity obo:GO_0050407 glycogen synthetase phosphatase activity obo:GO_0050407 glycogen-synthase-D phosphatase activity obo:GO_0050407 uridine diphosphoglucose-glycogen glucosyltransferase phosphatase activity obo:GO_0050407 molecular_function obo:GO_0050407 phosphatase type 2oC obo:GO_0050407 GO:0050407 obo:GO_0050407 [glycogen-synthase-D] phosphatase activity obo:GO_0050408 Catalysis of the reaction: [pyruvate kinase] phosphate + H2O = [pyruvate kinase] + phosphate. obo:GO_0050408 obo:go.owl obo:GO_0050408 EC:3.1.3.49 obo:GO_0050408 MetaCyc:PYRUVATE-KINASE-PHOSPHATASE-RXN obo:GO_0050408 ATP:pyruvate 2-O-phosphotransferase-phosphate phosphohydrolase activity obo:GO_0050408 pyruvate kinase phosphatase activity obo:GO_0050408 pyruvate kinase-phosphatase activity obo:GO_0050408 molecular_function obo:GO_0050408 GO:0050408 obo:GO_0050408 [pyruvate kinase]-phosphatase activity obo:GO_0050431 Interacting selectively and non-covalently with TGF-beta, transforming growth factor beta, a multifunctional peptide that controls proliferation, differentiation and other functions in many cell types. obo:GO_0050431 obo:go.owl obo:GO_0050431 TGF-beta binding obo:GO_0050431 TGFbeta binding obo:GO_0050431 molecular_function obo:GO_0050431 transforming growth factor beta ligand binding to type I receptor obo:GO_0050431 transforming growth factor beta ligand binding to type II receptor obo:GO_0050431 GO:0050431 obo:GO_0050431 transforming growth factor beta binding obo:GO_0050497 Catalysis of the transfer of an alkylthio group from one compound (donor) to another (acceptor). obo:GO_0050497 obo:go.owl obo:GO_0050497 EC:2.8.4 obo:GO_0050497 molecular_function obo:GO_0050497 GO:0050497 obo:GO_0050497 transferase activity, transferring alkylthio groups obo:GO_0050542 Interacting selectively and non-covalently with icosanoids, any C20 polyunsaturated fatty acids or their derivatives, including the leukotrienes and the prostanoids. obo:GO_0050542 obo:go.owl obo:GO_0050542 eicosanoid binding obo:GO_0050542 molecular_function obo:GO_0050542 GO:0050542 obo:GO_0050542 icosanoid binding obo:GO_0050543 Interacting selectively and non-covalently with icosatetraenoic acid, any straight-chain fatty acid with twenty carbon atoms and four double bonds per molecule. obo:GO_0050543 obo:go.owl obo:GO_0050543 eicosatetraenoic acid binding obo:GO_0050543 molecular_function obo:GO_0050543 GO:0050543 obo:GO_0050543 icosatetraenoic acid binding obo:GO_0050544 Interacting selectively and non-covalently with arachidonic acid, a straight chain fatty acid with 20 carbon atoms and four double bonds per molecule. Arachidonic acid is the all-Z-(5,8,11,14)-isomer. obo:GO_0050544 obo:go.owl obo:GO_0050544 arachidonate binding obo:GO_0050544 molecular_function obo:GO_0050544 GO:0050544 obo:GO_0050544 arachidonic acid binding obo:GO_0050646 Interacting selectively and non-covalently with 5-oxo-6E,8Z,11Z,14Z-icosatetraenoic acid, a straight-chain fatty acid with twenty carbon atoms and four double bonds. obo:GO_0050646 obo:go.owl obo:GO_0050646 5-oxo-6E,8Z,11Z,14Z-eicosatetraenoic acid binding obo:GO_0050646 molecular_function obo:GO_0050646 GO:0050646 obo:GO_0050646 5-oxo-6E,8Z,11Z,14Z-icosatetraenoic acid binding obo:GO_0050647 Interacting selectively and non-covalently with 5-hydroxy-6E,8Z,11Z,14Z-icosatetraenoic acid, a straight-chain fatty acid with twenty carbon atoms and four double bonds. obo:GO_0050647 obo:go.owl obo:GO_0050647 5-hydroxy-6E,8Z,11Z,14Z-eicosatetraenoic acid binding obo:GO_0050647 molecular_function obo:GO_0050647 GO:0050647 obo:GO_0050647 5-hydroxy-6E,8Z,11Z,14Z-icosatetraenoic acid binding obo:GO_0050648 Interacting selectively and non-covalently with 5(S)-hydroxyperoxy-6E,8Z,11Z,14Z-icosatetraenoic acid, a straight-chain fatty acid with twenty carbon atoms and four double bonds. obo:GO_0050648 obo:go.owl obo:GO_0050648 5(S)-hydroxyperoxy-6E,8Z,11Z,14Z-eicosatetraenoic acid binding obo:GO_0050648 molecular_function obo:GO_0050648 GO:0050648 obo:GO_0050648 5(S)-hydroxyperoxy-6E,8Z,11Z,14Z-icosatetraenoic acid binding obo:GO_0050656 Interacting selectively and non-covalently with 3'-phosphoadenosine 5'-phosphosulfate (PAPS), a naturally occurring mixed anhydride. It is an intermediate in the formation of a variety of sulfo compounds in biological systems. obo:GO_0050656 obo:go.owl obo:GO_0050656 3'-phosphoadenosine 5'-phosphosulphate binding obo:GO_0050656 3'-phosphoadenylyl-sulfate binding obo:GO_0050656 PAPS binding obo:GO_0050656 adenosine 3'-phosphate 5'-phosphosulfate binding obo:GO_0050656 phosphoadenosine phosphosulfate binding obo:GO_0050656 molecular_function obo:GO_0050656 GO:0050656 obo:GO_0050656 3'-phosphoadenosine 5'-phosphosulfate binding obo:GO_0050660 Interacting selectively and non-covalently with FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2. obo:GO_0050660 obo:go.owl obo:GO_0050660 MIPS_funcat:16.21.05 obo:GO_0050660 FAD or FADH2 binding obo:GO_0050660 flavine-adenine dinucleotide binding obo:GO_0050660 molecular_function obo:GO_0050660 GO:0050660 obo:GO_0050660 flavin adenine dinucleotide binding obo:GO_0050661 Interacting selectively and non-covalently with nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH. obo:GO_0050661 obo:go.owl obo:GO_0050661 MIPS_funcat:16.21.07 obo:GO_0050661 nicotinamide adenine dinucleotide phosphate binding obo:GO_0050661 molecular_function obo:GO_0050661 NADP or NADPH binding obo:GO_0050661 NADP+ or NADPH binding obo:GO_0050661 GO:0050661 obo:GO_0050661 NADP binding obo:GO_0050662 Interacting selectively and non-covalently with a coenzyme, any of various nonprotein organic cofactors that are required, in addition to an enzyme and a substrate, for an enzymatic reaction to proceed. obo:GO_0050662 obo:go.owl obo:GO_0050662 molecular_function obo:GO_0050662 GO:0050662 obo:GO_0050662 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0050662 coenzyme binding obo:GO_0050675 Any process that modulates the frequency, rate or extent of urothelial cell proliferation. obo:GO_0050675 obo:go.owl obo:GO_0050675 biological_process obo:GO_0050675 GO:0050675 obo:GO_0050675 regulation of urothelial cell proliferation obo:GO_0050676 Any process that stops, prevents or reduces the rate or extent of urothelial cell proliferation. obo:GO_0050676 obo:go.owl obo:GO_0050676 down regulation of urothelial cell proliferation obo:GO_0050676 down-regulation of urothelial cell proliferation obo:GO_0050676 downregulation of urothelial cell proliferation obo:GO_0050676 inhibition of urothelial cell proliferation obo:GO_0050676 biological_process obo:GO_0050676 GO:0050676 obo:GO_0050676 negative regulation of urothelial cell proliferation obo:GO_0050677 Any process that activates or increases the rate or extent of urothelial cell proliferation. obo:GO_0050677 obo:go.owl obo:GO_0050677 up regulation of urothelial cell proliferation obo:GO_0050677 up-regulation of urothelial cell proliferation obo:GO_0050677 upregulation of urothelial cell proliferation obo:GO_0050677 activation of urothelial cell proliferation obo:GO_0050677 stimulation of urothelial cell proliferation obo:GO_0050677 biological_process obo:GO_0050677 GO:0050677 obo:GO_0050677 positive regulation of urothelial cell proliferation obo:GO_0050678 Any process that modulates the frequency, rate or extent of epithelial cell proliferation. obo:GO_0050678 obo:go.owl obo:GO_0050678 biological_process obo:GO_0050678 GO:0050678 obo:GO_0050678 regulation of epithelial cell proliferation obo:GO_0050679 Any process that activates or increases the rate or extent of epithelial cell proliferation. obo:GO_0050679 obo:go.owl obo:GO_0050679 up regulation of epithelial cell proliferation obo:GO_0050679 up-regulation of epithelial cell proliferation obo:GO_0050679 upregulation of epithelial cell proliferation obo:GO_0050679 activation of epithelial cell proliferation obo:GO_0050679 stimulation of epithelial cell proliferation obo:GO_0050679 biological_process obo:GO_0050679 GO:0050679 obo:GO_0050679 positive regulation of epithelial cell proliferation obo:GO_0050680 Any process that stops, prevents or reduces the rate or extent of epithelial cell proliferation. obo:GO_0050680 obo:go.owl obo:GO_0050680 down regulation of epithelial cell proliferation obo:GO_0050680 down-regulation of epithelial cell proliferation obo:GO_0050680 downregulation of epithelial cell proliferation obo:GO_0050680 inhibition of epithelial cell proliferation obo:GO_0050680 biological_process obo:GO_0050680 GO:0050680 obo:GO_0050680 negative regulation of epithelial cell proliferation obo:GO_0050681 Interacting selectively and non-covalently with an androgen receptor. obo:GO_0050681 obo:go.owl obo:GO_0050681 AR binding obo:GO_0050681 molecular_function obo:GO_0050681 GO:0050681 obo:GO_0050681 androgen receptor binding obo:GO_0050682 Interacting selectively and non-covalently with the AF-2 domain of a protein, a highly conserved ligand-dependent transactivation domain which is essential for receptor-mediated transcriptional activation. obo:GO_0050682 obo:go.owl obo:GO_0050682 molecular_function obo:GO_0050682 GO:0050682 obo:GO_0050682 AF-2 domain binding obo:GO_0050683 Interacting selectively and non-covalently with the AF-1 domain of a protein, a ligand-independent transactivation domain which is required for the full transcriptional activity of the receptor. obo:GO_0050683 obo:go.owl obo:GO_0050683 molecular_function obo:GO_0050683 GO:0050683 obo:GO_0050683 AF-1 domain binding obo:GO_0050692 Interacting selectively and non-covalently with the DBD, DNA binding domain, of a protein. The DNA binding domain of the vitamin D receptor, one of a family of receptors with the DBD, is split into three regions, the P, D and T boxes. Residues that are critical for target sequence selectivity form the P-box. The D-box contains residues that are important for homodimerization of class I nuclear receptors. The T-box is essential for both DNA-binding and transactivation of the VDR; this region may also be important for dimerization with RXR for class II nuclear receptors. obo:GO_0050692 obo:go.owl obo:GO_0050692 DNA binding domain binding obo:GO_0050692 molecular_function obo:GO_0050692 GO:0050692 obo:GO_0050692 DBD domain binding obo:GO_0050693 Interacting selectively and non-covalently with the LBD, the ligand binding domain found in nuclear receptors. In general, the LBDs consist of three layers comprised of twelve alpha-helices and several beta-strands that are organized around a lipophilic ligand-binding pocket. obo:GO_0050693 obo:go.owl obo:GO_0050693 ligand binding domain binding obo:GO_0050693 molecular_function obo:GO_0050693 GO:0050693 obo:GO_0050693 LBD domain binding obo:GO_0050699 Interacting selectively and non-covalently with a WW domain of a protein, a small module composed of 40 amino acids and plays a role in mediating protein-protein interactions via proline-rich regions. obo:GO_0050699 obo:go.owl obo:GO_0050699 molecular_function obo:GO_0050699 GO:0050699 obo:GO_0050699 WW domain binding obo:GO_0050700 Interacting selectively and non-covalently with a CARD (N-terminal caspase recruitment) domain, a protein-protein interaction domain that belongs to the death domain-fold superfamily. These protein molecule families are similar in structure with each consisting of six or seven anti-parallel alpha-helices that form highly specific homophilic interactions between signaling partners. CARD exists in the N-terminal prodomains of several caspases and in apoptosis-regulatory proteins and mediates the assembly of CARD-containing proteins that participate in activation or suppression of CARD carrying members of the caspase family. obo:GO_0050700 obo:go.owl obo:GO_0050700 molecular_function obo:GO_0050700 GO:0050700 obo:GO_0050700 CARD domain binding obo:GO_0050733 Interacting selectively and non-covalently with an RS domain of a protein; RS domains are usually highly phosphorylated and characterized by the presence of arginine (R)/serine (S) dipeptides. The RS domain promotes protein-protein interactions and directs subcellular localization and, in certain situations, nucleocytoplasmic shuttling of individual SR proteins. They also play a role in splicing. obo:GO_0050733 obo:go.owl obo:GO_0050733 molecular_function obo:GO_0050733 GO:0050733 obo:GO_0050733 RS domain binding obo:GO_0050750 Interacting selectively and non-covalently with a low-density lipoprotein receptor. obo:GO_0050750 obo:go.owl obo:GO_0050750 LDL receptor binding obo:GO_0050750 low-density lipoprotein receptor binding obo:GO_0050750 molecular_function obo:GO_0050750 GO:0050750 obo:GO_0050750 low-density lipoprotein particle receptor binding obo:GO_0050780 Interacting selectively and non-covalently with a dopamine receptor. obo:GO_0050780 obo:go.owl obo:GO_0050780 molecular_function obo:GO_0050780 GO:0050780 obo:GO_0050780 dopamine receptor binding obo:GO_0050786 Interacting selectively and non-covalently with the RAGE receptor, the receptor for advanced glycation end-products. obo:GO_0050786 obo:go.owl obo:GO_0050786 advanced glycation end-product receptor binding obo:GO_0050786 molecular_function obo:GO_0050786 GO:0050786 obo:GO_0050786 RAGE receptor binding obo:GO_0050789 Any process that modulates the frequency, rate or extent of a biological process. Biological processes are regulated by many means; examples include the control of gene expression, protein modification or interaction with a protein or substrate molecule. obo:GO_0050789 obo:go.owl obo:GO_0050789 GO:0050791 obo:GO_0050789 regulation of physiological process obo:GO_0050789 biological_process obo:GO_0050789 GO:0050789 obo:GO_0050789 http://purl.oboInOwllibrary.org/oboInOwl/go#gocheck_do_not_annotate obo:GO_0050789 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_agr obo:GO_0050789 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_aspergillus obo:GO_0050789 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_candida obo:GO_0050789 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0050789 regulation of biological process obo:GO_0050794 Any process that modulates the frequency, rate or extent of a cellular process, any of those that are carried out at the cellular level, but are not necessarily restricted to a single cell. For example, cell communication occurs among more than one cell, but occurs at the cellular level. obo:GO_0050794 obo:go.owl obo:GO_0050794 GO:0051244 obo:GO_0050794 regulation of cellular physiological process obo:GO_0050794 biological_process obo:GO_0050794 GO:0050794 obo:GO_0050794 regulation of cellular process obo:GO_0050809 Interacting selectively and non-covalently with diazepam, one of the most widely used benzodiazepine drugs. It is used as an anti-anxiety-hypnotic agent and has the proprietary name Valium. obo:GO_0050809 obo:go.owl obo:GO_0050809 Valium binding obo:GO_0050809 molecular_function obo:GO_0050809 diazepam binding inhibitor activity obo:GO_0050809 GO:0050809 obo:GO_0050809 diazepam binding obo:GO_0050811 Interacting selectively and non-covalently with the gamma-aminobutyric acid (GABA, 4-aminobutyrate) receptor. obo:GO_0050811 obo:go.owl obo:GO_0050811 4-aminobutanoate receptor binding obo:GO_0050811 4-aminobutyrate receptor binding obo:GO_0050811 gamma-aminobutyric acid receptor binding obo:GO_0050811 molecular_function obo:GO_0050811 diazepam binding inhibitor activity obo:GO_0050811 GO:0050811 obo:GO_0050811 GABA receptor binding obo:GO_0050815 Interacting selectively and non-covalently with a phosphorylated serine residue within a protein. obo:GO_0050815 obo:go.owl obo:GO_0050815 molecular_function obo:GO_0050815 phosphoserine binding obo:GO_0050815 GO:0050815 obo:GO_0050815 phosphoserine residue binding obo:GO_0050816 Interacting selectively and non-covalently with a phosphorylated threonine residue within a protein. obo:GO_0050816 obo:go.owl obo:GO_0050816 molecular_function obo:GO_0050816 phosphothreonine binding obo:GO_0050816 GO:0050816 obo:GO_0050816 phosphothreonine residue binding obo:GO_0050826 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a freezing stimulus, temperatures below 0 degrees Celsius. obo:GO_0050826 obo:go.owl obo:GO_0050826 biological_process obo:GO_0050826 antifreeze activity obo:GO_0050826 ice nucleation inhibitor activity obo:GO_0050826 GO:0050826 obo:GO_0050826 response to freezing obo:GO_0050839 Interacting selectively and non-covalently with a cell adhesion molecule. obo:GO_0050839 obo:go.owl obo:GO_0050839 CAM binding obo:GO_0050839 molecular_function obo:GO_0050839 adhesive extracellular matrix constituent obo:GO_0050839 cell adhesion molecule activity obo:GO_0050839 cell adhesion receptor activity obo:GO_0050839 GO:0050839 obo:GO_0050839 cell adhesion molecule binding obo:GO_0050896 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus. The process begins with detection of the stimulus and ends with a change in state or activity or the cell or organism. obo:GO_0050896 obo:go.owl obo:GO_0050896 GO:0051869 obo:GO_0050896 MIPS_funcat:34.11 obo:GO_0050896 physiological response to stimulus obo:GO_0050896 biological_process obo:GO_0050896 GO:0050896 obo:GO_0050896 http://purl.oboInOwllibrary.org/oboInOwl/go#gocheck_do_not_manually_annotate obo:GO_0050896 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_agr obo:GO_0050896 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_flybase_ribbon obo:GO_0050896 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_mouse obo:GO_0050896 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0050896 Note that this term is in the subset of terms that should not be used for direct gene product annotation. Instead, select a child term or, if no appropriate child term exists, please request a new term. Direct annotations to this term may be amended during annotation QC. obo:GO_0050896 response to stimulus obo:GO_0050897 Interacting selectively and non-covalently with a cobalt (Co) ion. obo:GO_0050897 obo:go.owl obo:GO_0050897 cobalt binding obo:GO_0050897 molecular_function obo:GO_0050897 GO:0050897 obo:GO_0050897 cobalt ion binding obo:GO_0050906 The series of events involved in sensory perception in which a sensory stimulus is received and converted into a molecular signal. obo:GO_0050906 obo:go.owl obo:GO_0050906 Wikipedia:Transduction_(physiology) obo:GO_0050906 sensory detection of stimulus obo:GO_0050906 sensory perception, sensory transduction of stimulus obo:GO_0050906 sensory perception, stimulus detection obo:GO_0050906 sensory transduction obo:GO_0050906 biological_process obo:GO_0050906 GO:0050906 obo:GO_0050906 detection of stimulus involved in sensory perception obo:GO_0050907 The series of events in which a chemical stimulus is received and converted into a molecular signal as part of sensory perception. obo:GO_0050907 obo:go.owl obo:GO_0050907 sensory detection of chemical stimulus obo:GO_0050907 sensory detection of chemical stimulus during sensory perception obo:GO_0050907 sensory perception, sensory detection of chemical stimulus obo:GO_0050907 sensory perception, sensory transduction of chemical stimulus obo:GO_0050907 sensory transduction of chemical stimulus obo:GO_0050907 sensory transduction of chemical stimulus during sensory perception obo:GO_0050907 biological_process obo:GO_0050907 GO:0050907 obo:GO_0050907 detection of chemical stimulus involved in sensory perception obo:GO_0050908 The series of events involved in visual perception in which a light stimulus is received and converted into a molecular signal. obo:GO_0050908 obo:go.owl obo:GO_0050908 sensory detection of light during visual perception obo:GO_0050908 sensory detection of light stimulus during visual perception obo:GO_0050908 sensory transduction of light during visual perception obo:GO_0050908 sensory transduction of light stimulus during visual perception obo:GO_0050908 visual perception, detection of light stimulus obo:GO_0050908 visual perception, sensory transduction during perception of light obo:GO_0050908 visual perception, sensory transduction of light stimulus obo:GO_0050908 biological_process obo:GO_0050908 GO:0050908 obo:GO_0050908 detection of light stimulus involved in visual perception obo:GO_0050911 The series of events involved in the perception of smell in which an olfactory chemical stimulus is received and converted into a molecular signal. obo:GO_0050911 obo:go.owl obo:GO_0050911 perception of smell, detection of chemical stimulus obo:GO_0050911 perception of smell, sensory detection of chemical stimulus obo:GO_0050911 perception of smell, sensory transduction of chemical stimulus obo:GO_0050911 sensory detection of chemical stimulus during perception of smell obo:GO_0050911 sensory detection of scent obo:GO_0050911 sensory detection of smell obo:GO_0050911 sensory transduction of chemical stimulus during perception of smell obo:GO_0050911 sensory transduction of scent obo:GO_0050911 sensory transduction of smell obo:GO_0050911 biological_process obo:GO_0050911 GO:0050911 obo:GO_0050911 detection of chemical stimulus involved in sensory perception of smell obo:GO_0050912 The series of events involved in the perception of taste in which a gustatory chemical stimulus is received and converted into a molecular signal. obo:GO_0050912 obo:go.owl obo:GO_0050912 taste perception obo:GO_0050912 perception of taste, detection of chemical stimulus obo:GO_0050912 perception of taste, sensory detection of chemical stimulus obo:GO_0050912 perception of taste, sensory transduction of chemical stimulus obo:GO_0050912 sensory detection of chemical stimulus during perception of taste obo:GO_0050912 sensory detection of taste obo:GO_0050912 sensory transduction of chemical stimulus during perception of taste obo:GO_0050912 sensory transduction of taste obo:GO_0050912 biological_process obo:GO_0050912 GO:0050912 obo:GO_0050912 detection of chemical stimulus involved in sensory perception of taste obo:GO_0050920 Any process that modulates the frequency, rate or extent of the directed movement of a motile cell or organism in response to a specific chemical concentration gradient. obo:GO_0050920 obo:go.owl obo:GO_0050920 biological_process obo:GO_0050920 GO:0050920 obo:GO_0050920 regulation of chemotaxis obo:GO_0050921 Any process that activates or increases the frequency, rate or extent of the directed movement of a motile cell or organism in response to a specific chemical concentration gradient. obo:GO_0050921 obo:go.owl obo:GO_0050921 up regulation of chemotaxis obo:GO_0050921 up-regulation of chemotaxis obo:GO_0050921 upregulation of chemotaxis obo:GO_0050921 activation of chemotaxis obo:GO_0050921 stimulation of chemotaxis obo:GO_0050921 biological_process obo:GO_0050921 GO:0050921 obo:GO_0050921 positive regulation of chemotaxis obo:GO_0050922 Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of a motile cell or organism in response to a specific chemical concentration gradient. obo:GO_0050922 obo:go.owl obo:GO_0050922 down regulation of chemotaxis obo:GO_0050922 down-regulation of chemotaxis obo:GO_0050922 downregulation of chemotaxis obo:GO_0050922 inhibition of chemotaxis obo:GO_0050922 biological_process obo:GO_0050922 GO:0050922 obo:GO_0050922 negative regulation of chemotaxis obo:GO_0050923 Any process that modulates the frequency, rate or extent of the directed movement of a motile cell or organism towards a lower concentration in a concentration gradient of a specific chemical. obo:GO_0050923 obo:go.owl obo:GO_0050923 biological_process obo:GO_0050923 GO:0050923 obo:GO_0050923 regulation of negative chemotaxis obo:GO_0050924 Any process that activates or increases the frequency, rate or extent of the directed movement of a motile cell or organism towards a lower concentration in a concentration gradient of a specific chemical. obo:GO_0050924 obo:go.owl obo:GO_0050924 up regulation of negative chemotaxis obo:GO_0050924 up-regulation of negative chemotaxis obo:GO_0050924 upregulation of negative chemotaxis obo:GO_0050924 activation of negative chemotaxis obo:GO_0050924 stimulation of negative chemotaxis obo:GO_0050924 biological_process obo:GO_0050924 GO:0050924 obo:GO_0050924 positive regulation of negative chemotaxis obo:GO_0050925 Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of a motile cell or organism towards a lower concentration in a concentration gradient of a specific chemical. obo:GO_0050925 obo:go.owl obo:GO_0050925 down regulation of negative chemotaxis obo:GO_0050925 down-regulation of negative chemotaxis obo:GO_0050925 downregulation of negative chemotaxis obo:GO_0050925 inhibition of negative chemotaxis obo:GO_0050925 biological_process obo:GO_0050925 GO:0050925 obo:GO_0050925 negative regulation of negative chemotaxis obo:GO_0050926 Any process that modulates the frequency, rate or extent of the directed movement of a motile cell or organism towards a higher concentration in a concentration gradient of a specific chemical. obo:GO_0050926 obo:go.owl obo:GO_0050926 biological_process obo:GO_0050926 GO:0050926 obo:GO_0050926 regulation of positive chemotaxis obo:GO_0050927 Any process that activates or increases the frequency, rate or extent of the directed movement of a motile cell or organism towards a higher concentration in a concentration gradient of a specific chemical. obo:GO_0050927 obo:go.owl obo:GO_0050927 up regulation of positive chemotaxis obo:GO_0050927 up-regulation of positive chemotaxis obo:GO_0050927 upregulation of positive chemotaxis obo:GO_0050927 activation of positive chemotaxis obo:GO_0050927 stimulation of positive chemotaxis obo:GO_0050927 biological_process obo:GO_0050927 GO:0050927 obo:GO_0050927 positive regulation of positive chemotaxis obo:GO_0050928 Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of a motile cell or organism towards a higher concentration in a concentration gradient of a specific chemical. obo:GO_0050928 obo:go.owl obo:GO_0050928 down regulation of positive chemotaxis obo:GO_0050928 down-regulation of positive chemotaxis obo:GO_0050928 downregulation of positive chemotaxis obo:GO_0050928 inhibition of positive chemotaxis obo:GO_0050928 biological_process obo:GO_0050928 GO:0050928 obo:GO_0050928 negative regulation of positive chemotaxis obo:GO_0050929 Any process that initiates the directed movement of a motile cell or organism towards a lower concentration in a concentration gradient of a specific chemical. obo:GO_0050929 obo:go.owl obo:GO_0050929 biological_process obo:GO_0050929 GO:0050929 obo:GO_0050929 induction of negative chemotaxis obo:GO_0050930 Any process that initiates the directed movement of a motile cell or organism towards a higher concentration in a concentration gradient of a specific chemical. obo:GO_0050930 obo:go.owl obo:GO_0050930 biological_process obo:GO_0050930 GO:0050930 obo:GO_0050930 induction of positive chemotaxis obo:GO_0050960 The series of events in which a temperature stimulus is received and converted into a molecular signal as part of thermoception. obo:GO_0050960 obo:go.owl obo:GO_0050960 sensory detection of temperature stimulus during thermoception obo:GO_0050960 sensory detection of thermal stimulus during thermoception obo:GO_0050960 sensory transduction of temperature stimulus during thermoception obo:GO_0050960 sensory transduction of thermal stimulus during thermoception obo:GO_0050960 thermoception, sensory detection of temperature stimulus obo:GO_0050960 thermoception, sensory detection of thermal stimulus obo:GO_0050960 thermoception, sensory transduction of temperature stimulus obo:GO_0050960 thermoception, sensory transduction of thermal stimulus obo:GO_0050960 biological_process obo:GO_0050960 GO:0050960 obo:GO_0050960 detection of temperature stimulus involved in thermoception obo:GO_0050961 The series of events in which a temperature stimulus is received and converted into a molecular signal as part of sensory perception. obo:GO_0050961 obo:go.owl obo:GO_0050961 sensory detection of temperature stimulus obo:GO_0050961 sensory detection of temperature stimulus during sensory perception obo:GO_0050961 sensory detection of thermal stimulus during sensory perception obo:GO_0050961 sensory perception, sensory detection of temperature stimulus obo:GO_0050961 sensory perception, sensory detection of thermal stimulus obo:GO_0050961 sensory perception, sensory transduction of temperature stimulus obo:GO_0050961 sensory perception, sensory transduction of thermal stimulus obo:GO_0050961 sensory transduction of temperature stimulus obo:GO_0050961 sensory transduction of temperature stimulus during sensory perception obo:GO_0050961 sensory transduction of thermal stimulus during sensory perception obo:GO_0050961 sensory detection of heat stimulus during sensory perception obo:GO_0050961 sensory perception, sensory detection of heat stimulus obo:GO_0050961 sensory perception, sensory transduction of heat stimulus obo:GO_0050961 sensory transduction of heat stimulus during sensory perception obo:GO_0050961 biological_process obo:GO_0050961 GO:0050961 obo:GO_0050961 detection of temperature stimulus involved in sensory perception obo:GO_0050962 The series of events in which a light stimulus is received by a cell and converted into a molecular signal as part of the sensory perception of light. obo:GO_0050962 obo:go.owl obo:GO_0050962 sensory detection of light stimulus obo:GO_0050962 sensory detection of light stimulus during sensory perception obo:GO_0050962 sensory perception, sensory detection of light stimulus obo:GO_0050962 sensory perception, sensory transduction of light stimulus obo:GO_0050962 sensory transduction of light stimulus obo:GO_0050962 sensory transduction of light stimulus during sensory perception obo:GO_0050962 biological_process obo:GO_0050962 GO:0050962 obo:GO_0050962 detection of light stimulus involved in sensory perception obo:GO_0050963 The series of events in which an electrical stimulus is received by a cell and converted into a molecular signal as part of sensory perception. obo:GO_0050963 obo:go.owl obo:GO_0050963 sensory detection of electrical stimulus obo:GO_0050963 sensory detection of electrical stimulus during sensory perception obo:GO_0050963 sensory perception, sensory detection of electrical stimulus obo:GO_0050963 sensory perception, sensory transduction of electrical stimulus obo:GO_0050963 sensory transduction of electrical stimulus obo:GO_0050963 sensory transduction of electrical stimulus during sensory perception obo:GO_0050963 biological_process obo:GO_0050963 GO:0050963 obo:GO_0050963 detection of electrical stimulus involved in sensory perception obo:GO_0050964 The series of events that contribute to electroception in which an electrical stimulus is received and converted into a molecular signal. obo:GO_0050964 obo:go.owl obo:GO_0050964 electroception, detection of electrical stimulus obo:GO_0050964 electroception, sensory detection of electrical stimulus obo:GO_0050964 electroception, sensory transduction obo:GO_0050964 electroception, sensory transduction of electrical stimulus obo:GO_0050964 biological_process obo:GO_0050964 detection of electrical stimulus during electroreception obo:GO_0050964 sensory detection of electrical stimulus during electroception obo:GO_0050964 sensory transduction of electrical stimulus during electroception obo:GO_0050964 GO:0050964 obo:GO_0050964 detection of electrical stimulus involved in electroception obo:GO_0050965 The series of events involved in the perception of pain in which a temperature stimulus is received and converted into a molecular signal. obo:GO_0050965 obo:go.owl obo:GO_0050965 perception of pain, detection of temperature stimulus obo:GO_0050965 perception of pain, sensory detection of temperature stimulus obo:GO_0050965 perception of pain, sensory transduction of temperature stimulus obo:GO_0050965 sensory detection of temperature stimulus during perception of pain obo:GO_0050965 sensory detection of thermal stimulus during sensory perception of pain obo:GO_0050965 sensory perception of pain, sensory detection of thermal stimulus obo:GO_0050965 sensory perception of pain, sensory transduction of thermal stimulus obo:GO_0050965 sensory transduction of temperature stimulus during perception of pain obo:GO_0050965 sensory transduction of thermal stimulus during sensory perception of pain obo:GO_0050965 biological_process obo:GO_0050965 thermal nociception obo:GO_0050965 GO:0050965 obo:GO_0050965 detection of temperature stimulus involved in sensory perception of pain obo:GO_0050967 The series of events that contribute to the perception of pain in which an electrical stimulus is received and converted into a molecular signal. obo:GO_0050967 obo:go.owl obo:GO_0050967 perception of pain, detection of electrical stimulus obo:GO_0050967 perception of pain, sensory detection of electrical stimulus obo:GO_0050967 perception of pain, sensory transduction of electrical stimulus obo:GO_0050967 biological_process obo:GO_0050967 detection of electrical stimulus during sensory perception of pain obo:GO_0050967 sensory detection of electrical stimulus during perception of pain obo:GO_0050967 sensory transduction of electrical stimulus during perception of pain obo:GO_0050967 GO:0050967 obo:GO_0050967 detection of electrical stimulus involved in sensory perception of pain obo:GO_0050968 The series of events involved in the perception of pain in which a chemical stimulus is received and converted into a molecular signal. obo:GO_0050968 obo:go.owl obo:GO_0050968 perception of pain, detection of chemical stimulus obo:GO_0050968 perception of pain, sensory detection of chemical stimulus obo:GO_0050968 perception of pain, sensory transduction of chemical stimulus obo:GO_0050968 sensory detection of chemical stimulus during perception of pain obo:GO_0050968 sensory transduction of chemical stimulus during perception of pain obo:GO_0050968 biological_process obo:GO_0050968 chemical nociception obo:GO_0050968 GO:0050968 obo:GO_0050968 detection of chemical stimulus involved in sensory perception of pain obo:GO_0050969 The series of events involved in magnetoception in which a chemical stimulus is received and converted into a molecular signal. It is believed that organisms such as birds and salamanders interpret product ratios in chemical reactions which involve transitions between different spin states. obo:GO_0050969 obo:go.owl obo:GO_0050969 magnetoception, sensory transduction of chemical stimulus obo:GO_0050969 magnetoreception, detection of chemical stimulus obo:GO_0050969 magnetoreception, sensory detection of chemical stimulus obo:GO_0050969 magnetoreception, sensory transduction of chemical stimulus obo:GO_0050969 sensory detection of chemical stimulus during magnetoreception obo:GO_0050969 sensory transduction of chemical stimulus during magnetoreception obo:GO_0050969 biological_process obo:GO_0050969 GO:0050969 obo:GO_0050969 detection of chemical stimulus involved in magnetoreception obo:GO_0050970 The series of events that contribute to magnetoception in which an electrical stimulus is received and converted into a molecular signal. The stimulus is in the form of an induced electric field resulting from movement in a magnetic field. obo:GO_0050970 obo:go.owl obo:GO_0050970 magnetoception, sensory transduction of electrical stimulus obo:GO_0050970 magnetoreception, detection of electrical stimulus obo:GO_0050970 magnetoreception, sensory detection of electrical stimulus obo:GO_0050970 magnetoreception, sensory transduction of electrical stimulus obo:GO_0050970 biological_process obo:GO_0050970 detection of electrical stimulus during magnetoreception obo:GO_0050970 sensory detection of electrical stimulus during magnetoreception obo:GO_0050970 sensory transduction of electrical stimulus during magnetoreception obo:GO_0050970 GO:0050970 obo:GO_0050970 detection of electrical stimulus involved in magnetoreception obo:GO_0050980 The series of events involved in magnetoception in which a light stimulus is received and converted into a molecular signal. Downstream processing of the light information in addition to other sensory data allows organisms to perceive the orientation of a magnetic field. obo:GO_0050980 obo:go.owl obo:GO_0050980 magnetoreception, detection of light stimulus obo:GO_0050980 magnetoreception, sensory detection of light stimulus obo:GO_0050980 magnetoreception, sensory transduction of light stimulus obo:GO_0050980 sensory detection of light stimulus during magnetoreception obo:GO_0050980 sensory transduction of light stimulus during magnetoreception obo:GO_0050980 biological_process obo:GO_0050980 GO:0050980 obo:GO_0050980 detection of light stimulus involved in magnetoreception obo:GO_0050981 The series of events by which an electrical stimulus is received and converted into a molecular signal. obo:GO_0050981 obo:go.owl obo:GO_0050981 MIPS_funcat:34.11.08 obo:GO_0050981 biological_process obo:GO_0050981 GO:0050981 obo:GO_0050981 detection of electrical stimulus obo:GO_0050998 Interacting selectively and non-covalently with the enzyme nitric-oxide synthase. obo:GO_0050998 obo:go.owl obo:GO_0050998 NOS binding obo:GO_0050998 molecular_function obo:GO_0050998 GO:0050998 obo:GO_0050998 nitric-oxide synthase binding obo:GO_0051008 Interacting selectively and non-covalently with Hsp27 proteins, a lightweight heat shock protein. obo:GO_0051008 obo:go.owl obo:GO_0051008 molecular_function obo:GO_0051008 GO:0051008 obo:GO_0051008 Hsp27 protein binding obo:GO_0051010 Interacting selectively and non-covalently with the plus end of a microtubule. obo:GO_0051010 obo:go.owl obo:GO_0051010 molecular_function obo:GO_0051010 GO:0051010 obo:GO_0051010 microtubule plus-end binding obo:GO_0051011 Interacting selectively and non-covalently with the minus end of a microtubule. obo:GO_0051011 obo:go.owl obo:GO_0051011 molecular_function obo:GO_0051011 GO:0051011 obo:GO_0051011 microtubule minus-end binding obo:GO_0051015 Interacting selectively and non-covalently with an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits. obo:GO_0051015 obo:go.owl obo:GO_0051015 F-actin binding obo:GO_0051015 molecular_function obo:GO_0051015 actin cross-linking activity obo:GO_0051015 GO:0051015 obo:GO_0051015 actin filament binding obo:GO_0051018 Interacting selectively and non-covalently with any subunit of protein kinase A. obo:GO_0051018 obo:go.owl obo:GO_0051018 PKA binding obo:GO_0051018 molecular_function obo:GO_0051018 protein kinase A anchoring activity obo:GO_0051018 GO:0051018 obo:GO_0051018 Note that this term is a direct child of 'protein binding ; GO:0005515' because it encompasses binding to either the catalytic or regulatory subunit of protein kinase A, and the latter does not have kinase activity. obo:GO_0051018 protein kinase A binding obo:GO_0051019 Interacting selectively and non-covalently with a mitogen-activated protein kinase. obo:GO_0051019 obo:go.owl obo:GO_0051019 MAP kinase binding obo:GO_0051019 MAPK binding obo:GO_0051019 molecular_function obo:GO_0051019 MAP-kinase anchoring activity obo:GO_0051019 GO:0051019 obo:GO_0051019 mitogen-activated protein kinase binding obo:GO_0051020 Interacting selectively and non-covalently with a GTPase, any enzyme that catalyzes the hydrolysis of GTP. obo:GO_0051020 obo:go.owl obo:GO_0051020 molecular_function obo:GO_0051020 GO:0051020 obo:GO_0051020 GTPase binding obo:GO_0051021 Interacting selectively and non-covalently with a GDP-dissociation inhibitor protein. obo:GO_0051021 obo:go.owl obo:GO_0051021 GDI binding obo:GO_0051021 molecular_function obo:GO_0051021 GO:0051021 obo:GO_0051021 GDP-dissociation inhibitor binding obo:GO_0051022 Interacting selectively and non-covalently with a Rho GDP-dissociation inhibitor protein. obo:GO_0051022 obo:go.owl obo:GO_0051022 Rho GDI binding obo:GO_0051022 molecular_function obo:GO_0051022 GO:0051022 obo:GO_0051022 Rho GDP-dissociation inhibitor binding obo:GO_0051040 Any process that modulates the frequency, rate or extent of the attachment of one cell to another cell via adhesion molecules that do not require the presence of calcium for the interaction. obo:GO_0051040 obo:go.owl obo:GO_0051040 biological_process obo:GO_0051040 GO:0051040 obo:GO_0051040 regulation of calcium-independent cell-cell adhesion obo:GO_0051041 Any process that activates or increases the frequency, rate or extent of calcium-independent cell-cell adhesion. obo:GO_0051041 obo:go.owl obo:GO_0051041 up regulation of calcium-independent cell-cell adhesion obo:GO_0051041 up-regulation of calcium-independent cell-cell adhesion obo:GO_0051041 upregulation of calcium-independent cell-cell adhesion obo:GO_0051041 activation of calcium-independent cell-cell adhesion obo:GO_0051041 stimulation of calcium-independent cell-cell adhesion obo:GO_0051041 biological_process obo:GO_0051041 GO:0051041 obo:GO_0051041 positive regulation of calcium-independent cell-cell adhesion obo:GO_0051042 Any process that stops, prevents, or reduces the frequency, rate or extent of calcium-independent cell-cell adhesion. obo:GO_0051042 obo:go.owl obo:GO_0051042 down regulation of calcium-independent cell-cell adhesion obo:GO_0051042 down-regulation of calcium-independent cell-cell adhesion obo:GO_0051042 downregulation of calcium-independent cell-cell adhesion obo:GO_0051042 inhibition of calcium-independent cell-cell adhesion obo:GO_0051042 biological_process obo:GO_0051042 GO:0051042 obo:GO_0051042 negative regulation of calcium-independent cell-cell adhesion obo:GO_0051046 Any process that modulates the frequency, rate or extent of the controlled release of a substance from a cell or a tissue. obo:GO_0051046 obo:go.owl obo:GO_0051046 biological_process obo:GO_0051046 GO:0051046 obo:GO_0051046 regulation of secretion obo:GO_0051047 Any process that activates or increases the frequency, rate or extent of the controlled release of a substance from a cell or a tissue. obo:GO_0051047 obo:go.owl obo:GO_0051047 up regulation of secretion obo:GO_0051047 up-regulation of secretion obo:GO_0051047 upregulation of secretion obo:GO_0051047 activation of secretion obo:GO_0051047 stimulation of secretion obo:GO_0051047 biological_process obo:GO_0051047 GO:0051047 obo:GO_0051047 positive regulation of secretion obo:GO_0051048 Any process that stops, prevents, or reduces the frequency, rate or extent of the controlled release of a substance from a cell or a tissue. obo:GO_0051048 obo:go.owl obo:GO_0051048 down regulation of secretion obo:GO_0051048 down-regulation of secretion obo:GO_0051048 downregulation of secretion obo:GO_0051048 inhibition of secretion obo:GO_0051048 biological_process obo:GO_0051048 GO:0051048 obo:GO_0051048 negative regulation of secretion obo:GO_0051049 Any process that modulates the frequency, rate or extent of the directed movement of substances (such as macromolecules, small molecules, ions) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0051049 obo:go.owl obo:GO_0051049 biological_process obo:GO_0051049 GO:0051049 obo:GO_0051049 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0051049 regulation of transport obo:GO_0051050 Any process that activates or increases the frequency, rate or extent of the directed movement of substances (such as macromolecules, small molecules, ions) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0051050 obo:go.owl obo:GO_0051050 up regulation of transport obo:GO_0051050 up-regulation of transport obo:GO_0051050 upregulation of transport obo:GO_0051050 activation of transport obo:GO_0051050 stimulation of transport obo:GO_0051050 biological_process obo:GO_0051050 GO:0051050 obo:GO_0051050 positive regulation of transport obo:GO_0051051 Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of substances (such as macromolecules, small molecules, ions) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0051051 obo:go.owl obo:GO_0051051 down regulation of transport obo:GO_0051051 down-regulation of transport obo:GO_0051051 downregulation of transport obo:GO_0051051 inhibition of transport obo:GO_0051051 biological_process obo:GO_0051051 GO:0051051 obo:GO_0051051 negative regulation of transport obo:GO_0051059 Interacting selectively and non-covalently with NF-kappaB, a transcription factor for eukaryotic RNA polymerase II promoters. obo:GO_0051059 obo:go.owl obo:GO_0051059 molecular_function obo:GO_0051059 GO:0051059 obo:GO_0051059 NF-kappaB binding obo:GO_0051082 Interacting selectively and non-covalently with an unfolded protein. obo:GO_0051082 obo:go.owl obo:GO_0051082 binding unfolded ER proteins obo:GO_0051082 molecular_function obo:GO_0051082 chaperone activity obo:GO_0051082 fimbrium-specific chaperone activity obo:GO_0051082 glycoprotein-specific chaperone activity obo:GO_0051082 histone-specific chaperone activity obo:GO_0051082 ribosomal chaperone activity obo:GO_0051082 tubulin-specific chaperone activity obo:GO_0051082 GO:0051082 obo:GO_0051082 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0051082 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_generic obo:GO_0051082 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0051082 unfolded protein binding obo:GO_0051087 Interacting selectively and non-covalently with a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport. obo:GO_0051087 obo:go.owl obo:GO_0051087 chaperone protein binding obo:GO_0051087 molecular_function obo:GO_0051087 co-chaperone activity obo:GO_0051087 co-chaperonin activity obo:GO_0051087 GO:0051087 obo:GO_0051087 chaperone binding obo:GO_0051117 Interacting selectively and non-covalently with an ATPase, any enzyme that catalyzes the hydrolysis of ATP. obo:GO_0051117 obo:go.owl obo:GO_0051117 molecular_function obo:GO_0051117 GO:0051117 obo:GO_0051117 ATPase binding obo:GO_0051179 Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation. obo:GO_0051179 obo:go.owl obo:GO_0051179 jl obo:GO_0051179 2013-12-18T13:51:04Z obo:GO_0051179 GO:1902578 obo:GO_0051179 establishment and maintenance of localization obo:GO_0051179 establishment and maintenance of position obo:GO_0051179 localisation obo:GO_0051179 establishment and maintenance of cellular component location obo:GO_0051179 establishment and maintenance of substance location obo:GO_0051179 establishment and maintenance of substrate location obo:GO_0051179 biological_process obo:GO_0051179 single organism localization obo:GO_0051179 single-organism localization obo:GO_0051179 GO:0051179 obo:GO_0051179 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0051179 localization obo:GO_0051192 Interacting selectively and non-covalently with a prosthetic group, the non-amino acid portion of certain protein molecules. Prosthetic groups may be inorganic or organic and are usually required for the biological activity of the protein. obo:GO_0051192 obo:go.owl obo:GO_0051192 molecular_function obo:GO_0051192 GO:0051192 obo:GO_0051192 prosthetic group binding obo:GO_0051212 Interacting selectively and non-covalently with vanadium (V) ions. obo:GO_0051212 obo:go.owl obo:GO_0051212 molecular_function obo:GO_0051212 GO:0051212 obo:GO_0051212 vanadium ion binding obo:GO_0051219 Interacting selectively and non-covalently with a phosphorylated protein. obo:GO_0051219 obo:go.owl obo:GO_0051219 phosphorylated protein binding obo:GO_0051219 molecular_function obo:GO_0051219 GO:0051219 obo:GO_0051219 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0051219 phosphoprotein binding obo:GO_0051234 Any process that localizes a substance or cellular component. This may occur via movement, tethering or selective degradation. obo:GO_0051234 obo:go.owl obo:GO_0051234 establishment of localisation obo:GO_0051234 biological_process obo:GO_0051234 GO:0051234 obo:GO_0051234 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_agr obo:GO_0051234 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_flybase_ribbon obo:GO_0051234 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_mouse obo:GO_0051234 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0051234 establishment of localization obo:GO_0051287 Interacting selectively and non-covalently with nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH. obo:GO_0051287 obo:go.owl obo:GO_0051287 GO:0051288 obo:GO_0051287 MIPS_funcat:16.21.07 obo:GO_0051287 nicotinamide adenine dinucleotide binding obo:GO_0051287 molecular_function obo:GO_0051287 NAD or NADH binding obo:GO_0051287 NAD+ or NADH binding obo:GO_0051287 GO:0051287 obo:GO_0051287 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0051287 NAD binding obo:GO_0051365 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of potassium ions. obo:GO_0051365 obo:go.owl obo:GO_0051365 cellular response to K+ ion deprivation obo:GO_0051365 cellular response to K+ ion starvation obo:GO_0051365 cellular response to potassium ion deprivation obo:GO_0051365 cellular response to potassium starvation obo:GO_0051365 biological_process obo:GO_0051365 GO:0051365 obo:GO_0051365 cellular response to potassium ion starvation obo:GO_0051371 Interacting selectively and non-covalently with muscle isoforms of actinin. Muscle alpha-actinin isoforms are found in skeletal and cardiac muscle and are localized to the Z-disc. obo:GO_0051371 obo:go.owl obo:GO_0051371 alpha-actinin 2 binding obo:GO_0051371 alpha-actinin 3 binding obo:GO_0051371 molecular_function obo:GO_0051371 GO:0051371 obo:GO_0051371 muscle alpha-actinin binding obo:GO_0051373 Interacting selectively and non-covalently with a member of the FATZ family of proteins, filamin-, actinin-, and telethonin-binding proteins of the Z-disc of striated muscle. FATZ proteins are located in the Z-disc of the sarcomere and are involved in a complex network of interactions with other Z-band components. obo:GO_0051373 obo:go.owl obo:GO_0051373 GO:0051374 obo:GO_0051373 GO:0051375 obo:GO_0051373 GO:0051376 obo:GO_0051373 FATZ 1 binding obo:GO_0051373 FATZ 2 binding obo:GO_0051373 FATZ 3 binding obo:GO_0051373 calsarcin 1 binding obo:GO_0051373 calsarcin 2 binding obo:GO_0051373 calsarcin 3 binding obo:GO_0051373 calsarcin binding obo:GO_0051373 filamin-, actinin- and telethonin-binding protein of the Z-disc of striated muscle obo:GO_0051373 molecular_function obo:GO_0051373 GO:0051373 obo:GO_0051373 FATZ binding obo:GO_0051379 Interacting selectively and non-covalently with epinephrine, a hormone produced by the medulla of the adrenal glands that increases heart activity, improves the power and prolongs the action of muscles, and increases the rate and depth of breathing. It is synthesized by the methylation of norepinephrine. obo:GO_0051379 obo:go.owl obo:GO_0051379 adrenaline binding obo:GO_0051379 molecular_function obo:GO_0051379 GO:0051379 obo:GO_0051379 epinephrine binding obo:GO_0051380 Interacting selectively and non-covalently with norepinephrine, (3,4-dihydroxyphenyl-2-aminoethanol), a hormone secreted by the adrenal medulla and a neurotransmitter in the sympathetic peripheral nervous system and in some tracts of the CNS. It is also the biosynthetic precursor of epinephrine. obo:GO_0051380 obo:go.owl obo:GO_0051380 noradrenaline binding obo:GO_0051380 molecular_function obo:GO_0051380 GO:0051380 obo:GO_0051380 norepinephrine binding obo:GO_0051393 Interacting selectively and non-covalently with alpha-actinin, one of a family of proteins that cross-link F-actin as antiparallel homodimers. Alpha-actinin has a molecular mass of 93-103 KDa; at the N-terminus there are two calponin homology domains, at the C-terminus there are two EF-hands. These two domains are connected by the rod domain. This domain is formed by triple-helical spectrin repeats. obo:GO_0051393 obo:go.owl obo:GO_0051393 GO:0051372 obo:GO_0051393 alpha-actinin 1 binding obo:GO_0051393 alpha-actinin 4 binding obo:GO_0051393 nonmuscle alpha-actinin binding obo:GO_0051393 molecular_function obo:GO_0051393 GO:0051393 obo:GO_0051393 alpha-actinin binding obo:GO_0051400 Interacting selectively and non-covalently with the Bcl-2 homology (BH) domain of a protein. Bcl-2-related proteins share homology in one to four conserved regions designated the Bcl-2 homology (BH) domains BH1, BH2, BH3 and BH4. These domains contribute at multiple levels to the function of these proteins in cell death and survival. Anti-apoptotic members of the Bcl-2 family have four BH domains (BH1-BH4). Pro-apoptotic members have fewer BH domains. obo:GO_0051400 obo:go.owl obo:GO_0051400 Bcl-2 homology domain binding obo:GO_0051400 molecular_function obo:GO_0051400 GO:0051400 obo:GO_0051400 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0051400 BH domain binding obo:GO_0051401 Interacting selectively and non-covalently with the calponin homology domain of a protein, a domain of 100 residues that occurs in signaling and cytoskeletal proteins. obo:GO_0051401 obo:go.owl obo:GO_0051401 calponin homology domain binding obo:GO_0051401 molecular_function obo:GO_0051401 GO:0051401 obo:GO_0051401 CH domain binding obo:GO_0051425 Interacting selectively and non-covalently with a phosphotyrosine-binding (PTB) domain of a protein. obo:GO_0051425 obo:go.owl obo:GO_0051425 PID binding obo:GO_0051425 phosphotyrosine-interacting domain binding obo:GO_0051425 molecular_function obo:GO_0051425 GO:0051425 obo:GO_0051425 PTB domain binding obo:GO_0051427 Interacting selectively and non-covalently with a receptor for hormones. obo:GO_0051427 obo:go.owl obo:GO_0051427 molecular_function obo:GO_0051427 GO:0051427 obo:GO_0051427 hormone receptor binding obo:GO_0051428 Interacting selectively and non-covalently with a receptor for peptide hormones. obo:GO_0051428 obo:go.owl obo:GO_0051428 polypeptide hormone receptor binding obo:GO_0051428 molecular_function obo:GO_0051428 GO:0051428 obo:GO_0051428 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0051428 peptide hormone receptor binding obo:GO_0051429 Interacting selectively and non-covalently with a receptor for corticotropin-releasing hormone (CRH), a polypeptide hormone involved in the stress response. It is released by the hypothalamus and stimulates the release of corticotropin by the anterior pituitary gland. obo:GO_0051429 obo:go.owl obo:GO_0051429 GO:0031742 obo:GO_0051429 CRF receptor binding obo:GO_0051429 CRH receptor binding obo:GO_0051429 CRHR binding obo:GO_0051429 corticotropin releasing factor receptor binding obo:GO_0051429 corticotropin-releasing factor receptor binding obo:GO_0051429 corticotropin releasing factor receptor ligand obo:GO_0051429 molecular_function obo:GO_0051429 GO:0051429 obo:GO_0051429 corticotropin-releasing hormone receptor binding obo:GO_0051430 Interacting selectively and non-covalently with the corticotropin-releasing hormone receptor 1 (CRHR1). CRHR1 is the major subtype in the pituitary corticotroph, and mediates the stimulatory actions of corticotropin-releasing hormone on corticotropin hormone secretion. CRHR1 are also located in cortical areas of the brain, cerebellum and limbic system. obo:GO_0051430 obo:go.owl obo:GO_0051430 GO:0031743 obo:GO_0051430 CRHR1 binding obo:GO_0051430 type 1 corticotropin releasing factor receptor binding obo:GO_0051430 type 1 corticotropin-releasing factor receptor binding obo:GO_0051430 type 1 corticotropin releasing factor receptor ligand obo:GO_0051430 molecular_function obo:GO_0051430 GO:0051430 obo:GO_0051430 corticotropin-releasing hormone receptor 1 binding obo:GO_0051431 Interacting selectively and non-covalently with the corticotropin-releasing hormone receptor type 2 (CRHR2). The CRHR2 has several splice variants that are located in sub-cortical areas of the brain and in the periphery. obo:GO_0051431 obo:go.owl obo:GO_0051431 GO:0031744 obo:GO_0051431 CRHR2 binding obo:GO_0051431 type 2 corticotropin releasing factor receptor binding obo:GO_0051431 type 2 corticotropin-releasing factor receptor binding obo:GO_0051431 type 2 corticotropin releasing factor receptor ligand obo:GO_0051431 molecular_function obo:GO_0051431 GO:0051431 obo:GO_0051431 corticotropin-releasing hormone receptor 2 binding obo:GO_0051432 Interacting selectively and non-covalently with the BH1 domain of a protein of the Bcl-2 family. Proteins that act as inhibitors of apoptosis harbour at least three BH domains: BH1, BH2 and BH3; the BH1 and BH2 domains are found in all death antagonists of the Bcl-2 family but only in one class of death agonists. obo:GO_0051432 obo:go.owl obo:GO_0051432 molecular_function obo:GO_0051432 GO:0051432 obo:GO_0051432 BH1 domain binding obo:GO_0051433 Interacting selectively and non-covalently with the BH2 domain of a protein of the Bcl-2 family. Proteins that act as inhibitors of apoptosis harbour at least three BH domains: BH1, BH2 and BH3; the BH1 and BH2 domains are found in all death antagonists of the Bcl-2 family but only in one class of death agonists. obo:GO_0051433 obo:go.owl obo:GO_0051433 molecular_function obo:GO_0051433 GO:0051433 obo:GO_0051433 BH2 domain binding obo:GO_0051434 Interacting selectively and non-covalently with the BH3 domain of a protein of the Bcl-2 family. The BH3 domain is a potent death domain and has an important role in protein-protein interactions and in cell death. obo:GO_0051434 obo:go.owl obo:GO_0051434 molecular_function obo:GO_0051434 GO:0051434 obo:GO_0051434 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0051434 BH3 domain binding obo:GO_0051435 Interacting selectively and non-covalently with the BH4 domain of a protein of the Bcl-2 family. All anti-apoptotic proteins contain BH1 and BH2 domains; some also contain an additional N-terminal BH4 domain, which is almost never seen in pro-apoptotic proteins. Loss of the BH4 domain can diminish or abrogate anti-apoptotic function or even impart outright death-promoting properties to the protein. obo:GO_0051435 obo:go.owl obo:GO_0051435 molecular_function obo:GO_0051435 GO:0051435 obo:GO_0051435 BH4 domain binding obo:GO_0051448 Interacting selectively and non-covalently with gonadotropin-releasing hormone (GnRH), a peptide hormone responsible for the release of follicle-stimulating hormone (FSH) and luteinizing hormone (LH) from the anterior pituitary. GnRH is synthesized and released by the hypothalamus. obo:GO_0051448 obo:go.owl obo:GO_0051448 GnRH binding obo:GO_0051448 gonadotrophin releasing hormone binding obo:GO_0051448 molecular_function obo:GO_0051448 GO:0051448 obo:GO_0051448 gonadotropin-releasing hormone binding obo:GO_0051449 Interacting selectively and non-covalently with thyrotropin-releasing hormone, a tripeptide hormone that stimulates the release of thyroid-stimulating hormone (TSH) and prolactin by the anterior pituitary and it is produced by the hypothalamus and travels across the median eminence to the pituitary via the pituitary portal system. obo:GO_0051449 obo:go.owl obo:GO_0051449 thyrotropin releasing hormone binding obo:GO_0051449 molecular_function obo:GO_0051449 GO:0051449 obo:GO_0051449 thyrotropin-releasing hormone binding obo:GO_0051525 Interacting selectively and non-covalently with NFAT (nuclear factor of activated T cells) proteins, a family of transcription factors. NFAT proteins have crucial roles in the development and function of the immune system. obo:GO_0051525 obo:go.owl obo:GO_0051525 GO:0051526 obo:GO_0051525 GO:0051527 obo:GO_0051525 GO:0051528 obo:GO_0051525 GO:0051529 obo:GO_0051525 GO:0051530 obo:GO_0051525 NFAT binding obo:GO_0051525 nuclear factor of activated T cell protein binding obo:GO_0051525 NFAT1 protein binding obo:GO_0051525 NFAT2 protein binding obo:GO_0051525 NFAT3 protein binding obo:GO_0051525 NFAT4 protein binding obo:GO_0051525 NFAT5 protein binding obo:GO_0051525 NFATc binding obo:GO_0051525 NFATc1 binding obo:GO_0051525 NFATc2 binding obo:GO_0051525 NFATc3 binding obo:GO_0051525 NFATc4 binding obo:GO_0051525 NFATp binding obo:GO_0051525 NFATx binding obo:GO_0051525 non-calcium-regulated NFAT protein binding obo:GO_0051525 molecular_function obo:GO_0051525 GO:0051525 obo:GO_0051525 NFAT protein binding obo:GO_0051536 Interacting selectively and non-covalently with an iron-sulfur cluster, a combination of iron and sulfur atoms. obo:GO_0051536 obo:go.owl obo:GO_0051536 MIPS_funcat:16.21.08 obo:GO_0051536 Fe/S binding obo:GO_0051536 iron sulfur cluster binding obo:GO_0051536 iron sulphur cluster binding obo:GO_0051536 iron-sulphur cluster binding obo:GO_0051536 molecular_function obo:GO_0051536 GO:0051536 obo:GO_0051536 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_metagenomics obo:GO_0051536 iron-sulfur cluster binding obo:GO_0051537 Interacting selectively and non-covalently with a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands. obo:GO_0051537 obo:go.owl obo:GO_0051537 2 Fe 2 S cluster binding obo:GO_0051537 2 iron, 2 sulphur cluster binding obo:GO_0051537 2Fe-2S cluster binding obo:GO_0051537 diiron disulfide cluster binding obo:GO_0051537 diiron disulphide cluster binding obo:GO_0051537 iron-sulfur cluster 2Fe-2S binding obo:GO_0051537 iron-sulphur cluster 2Fe-2S binding obo:GO_0051537 molecular_function obo:GO_0051537 GO:0051537 obo:GO_0051537 2 iron, 2 sulfur cluster binding obo:GO_0051538 Interacting selectively and non-covalently with a 3 iron, 4 sulfur (3Fe-4S) cluster; this cluster consists of three iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands. It is essentially a 4Fe-4S cluster with one iron missing. obo:GO_0051538 obo:go.owl obo:GO_0051538 3 Fe 4 S cluster binding obo:GO_0051538 3 iron, 4 sulphur cluster binding obo:GO_0051538 3Fe-4S cluster binding obo:GO_0051538 iron-sulfur cluster 3Fe-4S binding obo:GO_0051538 iron-sulphur cluster 3Fe-4S binding obo:GO_0051538 triiron tetrasulfide cluster binding obo:GO_0051538 triiron tetrasulphide cluster binding obo:GO_0051538 molecular_function obo:GO_0051538 GO:0051538 obo:GO_0051538 3 iron, 4 sulfur cluster binding obo:GO_0051539 Interacting selectively and non-covalently with a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands. obo:GO_0051539 obo:go.owl obo:GO_0051539 4 Fe 4 S cluster binding obo:GO_0051539 4 iron, 4 sulphur cluster binding obo:GO_0051539 4Fe-4S cluster binding obo:GO_0051539 iron-sulfur cluster 4Fe-4S binding obo:GO_0051539 iron-sulphur cluster 4Fe-4S binding obo:GO_0051539 tetrairon tetrasulfide cluster binding obo:GO_0051539 tetrairon tetrasulphide cluster binding obo:GO_0051539 molecular_function obo:GO_0051539 GO:0051539 obo:GO_0051539 4 iron, 4 sulfur cluster binding obo:GO_0051540 Interacting selectively and non-covalently with a cluster of atoms including both metal ions and nonmetal atoms, usually sulfur and oxygen. Examples include iron-sulfur clusters and nickel-iron-sulfur clusters. obo:GO_0051540 obo:go.owl obo:GO_0051540 molecular_function obo:GO_0051540 GO:0051540 obo:GO_0051540 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0051540 metal cluster binding obo:GO_0051594 The series of events in which a glucose stimulus is received by a cell and converted into a molecular signal. obo:GO_0051594 obo:go.owl obo:GO_0051594 glucose detection obo:GO_0051594 biological_process obo:GO_0051594 glucose perception obo:GO_0051594 glucose sensing obo:GO_0051594 GO:0051594 obo:GO_0051594 detection of glucose obo:GO_0051602 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an electrical stimulus. obo:GO_0051602 obo:go.owl obo:GO_0051602 MIPS_funcat:34.11.08 obo:GO_0051602 biological_process obo:GO_0051602 response to electricity obo:GO_0051602 GO:0051602 obo:GO_0051602 response to electrical stimulus obo:GO_0051603 The hydrolysis of a peptide bond or bonds within a protein as part of the chemical reactions and pathways resulting in the breakdown of a protein by individual cells. obo:GO_0051603 obo:go.owl obo:GO_0051603 peptidolysis involved in cellular protein catabolic process obo:GO_0051603 peptidolysis involved in cellular protein catabolism obo:GO_0051603 biological_process obo:GO_0051603 peptidolysis during cellular protein catabolic process obo:GO_0051603 peptidolysis during cellular protein catabolism obo:GO_0051603 proteolysis during cellular protein catabolic process obo:GO_0051603 proteolysis during cellular protein catabolism obo:GO_0051603 GO:0051603 obo:GO_0051603 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_yeast obo:GO_0051603 proteolysis involved in cellular protein catabolic process obo:GO_0051606 The series of events in which a stimulus is received by a cell or organism and converted into a molecular signal. obo:GO_0051606 obo:go.owl obo:GO_0051606 MIPS_funcat:34.11 obo:GO_0051606 stimulus detection obo:GO_0051606 biological_process obo:GO_0051606 perception of stimulus obo:GO_0051606 stimulus sensing obo:GO_0051606 GO:0051606 obo:GO_0051606 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0051606 detection of stimulus obo:GO_0051716 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus. The process begins with detection of the stimulus by a cell and ends with a change in state or activity or the cell. obo:GO_0051716 obo:go.owl obo:GO_0051716 biological_process obo:GO_0051716 GO:0051716 obo:GO_0051716 http://purl.oboInOwllibrary.org/oboInOwl/go#gocheck_do_not_manually_annotate obo:GO_0051716 Note that this term is in the subset of terms that should not be used for direct gene product annotation. Instead, select a child term or, if no appropriate child term exists, please request a new term. Direct annotations to this term may be amended during annotation QC. obo:GO_0051716 cellular response to stimulus obo:GO_0051721 Interacting selectively and non-covalently with the enzyme protein phosphatase 2A. obo:GO_0051721 obo:go.owl obo:GO_0051721 molecular_function obo:GO_0051721 protein phosphatase 2 binding obo:GO_0051721 GO:0051721 obo:GO_0051721 protein phosphatase 2A binding obo:GO_0051775 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating redox state. Redox state refers to the balance of oxidized versus reduced forms of electron donors and acceptors in an organelle, cell or organ; plastoquinone, glutathione (GSH/GSSG), and nicotinamide nucleotides (NAD+/NADH and NADP+/NADPH) are among the most important. obo:GO_0051775 obo:go.owl obo:GO_0051775 GO:0006980 obo:GO_0051775 redox signal response obo:GO_0051775 biological_process obo:GO_0051775 GO:0051775 obo:GO_0051775 response to redox state obo:GO_0051776 The series of events in which a chemical stimulus indicating redox state is received and converted into a molecular signal. Redox state refers to the balance of oxidized versus reduced forms of electron donors and acceptors in an organelle, cell or organ; plastoquinone, glutathione (GSH/GSSG), and nicotinamide nucleotides (NAD+/NADH and NADP+/NADPH) are among the most important. obo:GO_0051776 obo:go.owl obo:GO_0051776 redox sensing obo:GO_0051776 biological_process obo:GO_0051776 GO:0051776 obo:GO_0051776 detection of redox state obo:GO_0051787 Interacting selectively and non-covalently with a misfolded protein. obo:GO_0051787 obo:go.owl obo:GO_0051787 Reactome:R-HSA-5324632 obo:GO_0051787 molecular_function obo:GO_0051787 GO:0051787 obo:GO_0051787 misfolded protein binding obo:GO_0051861 Interacting selectively and non-covalently with a glycolipid, any compound containing one or more monosaccharide residues bound by a glycosidic linkage to a hydrophobic group such as an acylglycerol, a sphingoid, a ceramide (N-acylsphingoid) or a prenyl phosphate. obo:GO_0051861 obo:go.owl obo:GO_0051861 molecular_function obo:GO_0051861 GO:0051861 obo:GO_0051861 glycolipid binding obo:GO_0051870 Interacting selectively and non-covalently with methotrexate, an antineoplastic antimetabolite with immunosuppressant properties. It is an inhibitor of tetrahydrofolate reductase and prevents the formation of tetrahydrofolate, necessary for synthesis of thymidylate, an essential component of DNA. obo:GO_0051870 obo:go.owl obo:GO_0051870 molecular_function obo:GO_0051870 GO:0051870 obo:GO_0051870 methotrexate binding obo:GO_0051871 Interacting selectively and non-covalently with dihydrofolic acid, a folic acid in which the bicyclic pteridine structure is in the dihydro, partially reduced form; they are intermediates in folate metabolism and are reduced to their tetrahydro, reduced forms. obo:GO_0051871 obo:go.owl obo:GO_0051871 molecular_function obo:GO_0051871 DHF binding obo:GO_0051871 dihydrofolate binding obo:GO_0051871 GO:0051871 obo:GO_0051871 dihydrofolic acid binding obo:GO_0051879 Interacting selectively and non-covalently with Hsp90 proteins, any of a group of heat shock proteins around 90kDa in size. obo:GO_0051879 obo:go.owl obo:GO_0051879 Hsp90 binding obo:GO_0051879 Hsp90 class protein binding obo:GO_0051879 molecular_function obo:GO_0051879 GO:0051879 obo:GO_0051879 Hsp90 protein binding obo:GO_0051880 Interacting selectively and non-covalently with G-quadruplex DNA structures, in which groups of four guanines adopt a flat, cyclic Hoogsteen hydrogen-bonding arrangement known as a guanine tetrad. The stacking of guanine tetrads results in G-quadruplex DNA structures. G-quadruplex DNA can form under physiological conditions from some G-rich sequences, such as those found in telomeres, immunoglobulin switch regions, gene promoters, fragile X repeats, and the dimerization domain in the human immunodeficiency virus (HIV) genome. obo:GO_0051880 obo:go.owl obo:GO_0051880 G quartet binding obo:GO_0051880 G-quartet binding obo:GO_0051880 G quadruplex DNA binding obo:GO_0051880 G quartet DNA binding obo:GO_0051880 G-DNA binding obo:GO_0051880 G-quartet DNA binding obo:GO_0051880 quadruplex DNA binding obo:GO_0051880 tetraplex DNA binding obo:GO_0051880 molecular_function obo:GO_0051880 GO:0051880 obo:GO_0051880 G-quadruplex DNA binding obo:GO_0051916 Interacting selectively and non-covalently with granulocyte colony-stimulating factor, G-CSF. obo:GO_0051916 obo:go.owl obo:GO_0051916 G-CSF binding obo:GO_0051916 granulocyte colony stimulating factor binding obo:GO_0051916 molecular_function obo:GO_0051916 GO:0051916 obo:GO_0051916 granulocyte colony-stimulating factor binding obo:GO_0051924 Any process that modulates the frequency, rate or extent of the directed movement of calcium ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0051924 obo:go.owl obo:GO_0051924 regulation of calcium transport obo:GO_0051924 biological_process obo:GO_0051924 GO:0051924 obo:GO_0051924 regulation of calcium ion transport obo:GO_0051926 Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of calcium ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0051926 obo:go.owl obo:GO_0051926 down regulation of calcium ion transport obo:GO_0051926 down-regulation of calcium ion transport obo:GO_0051926 downregulation of calcium ion transport obo:GO_0051926 negative regulation of calcium transport obo:GO_0051926 inhibition of calcium ion transport obo:GO_0051926 biological_process obo:GO_0051926 GO:0051926 obo:GO_0051926 negative regulation of calcium ion transport obo:GO_0051928 Any process that activates or increases the frequency, rate or extent of the directed movement of calcium ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0051928 obo:go.owl obo:GO_0051928 positive regulation of calcium transport obo:GO_0051928 up regulation of calcium ion transport obo:GO_0051928 up-regulation of calcium ion transport obo:GO_0051928 upregulation of calcium ion transport obo:GO_0051928 activation of calcium ion transport obo:GO_0051928 stimulation of calcium ion transport obo:GO_0051928 biological_process obo:GO_0051928 GO:0051928 obo:GO_0051928 positive regulation of calcium ion transport obo:GO_0051959 Interacting selectively and non-covalently with a light intermediate chain of the dynein complex. obo:GO_0051959 obo:go.owl obo:GO_0051959 molecular_function obo:GO_0051959 GO:0051959 obo:GO_0051959 dynein light intermediate chain binding obo:GO_0052230 Any process in which an organism modulates the frequency, rate or extent of the directed movement of substances within the cell or cells of a second organism, where the two organisms are in a symbiotic interaction. obo:GO_0052230 obo:go.owl obo:GO_0052230 modulation of intracellular trafficking in other organism obo:GO_0052230 biological_process obo:GO_0052230 modulation of intracellular transport in other organism during symbiotic interaction obo:GO_0052230 GO:0052230 obo:GO_0052230 modulation of intracellular transport in other organism involved in symbiotic interaction obo:GO_0052386 A type of cell wall modification in which the cell wall is reinforced and made thicker. obo:GO_0052386 obo:go.owl obo:GO_0052386 biological_process obo:GO_0052386 GO:0052386 obo:GO_0052386 cell wall thickening obo:GO_0052689 Catalysis of the hydrolysis of a carboxylic ester bond. obo:GO_0052689 obo:go.owl obo:GO_0052689 GO:0004091 obo:GO_0052689 GO:0004302 obo:GO_0052689 GO:0004759 obo:GO_0052689 GO:0016789 obo:GO_0052689 EC:3.1.1 obo:GO_0052689 EC:3.1.1.1 obo:GO_0052689 KEGG:R00630 obo:GO_0052689 MetaCyc:CARBOXYLESTERASE-RXN obo:GO_0052689 Reactome:R-HSA-5693691 obo:GO_0052689 Reactome:R-HSA-8937442 obo:GO_0052689 Reactome:R-HSA-9619024 obo:GO_0052689 UM-BBD_reactionID:r1025 obo:GO_0052689 carboxyesterase activity obo:GO_0052689 carboxyl ester hydrolase activity obo:GO_0052689 carboxylate esterase activity obo:GO_0052689 carboxylesterase activity obo:GO_0052689 carboxylic acid esterase activity obo:GO_0052689 carboxylic esterase activity obo:GO_0052689 ali-esterase activity obo:GO_0052689 alpha-carboxylesterase activity obo:GO_0052689 cocaine esterase activity obo:GO_0052689 procaine esterase activity obo:GO_0052689 triacetin esterase obo:GO_0052689 vitamin A esterase obo:GO_0052689 molecular_function obo:GO_0052689 Ali-esterase activity obo:GO_0052689 B-esterase activity obo:GO_0052689 carboxylic ester hydrolase activity obo:GO_0052689 esterase A obo:GO_0052689 esterase B obo:GO_0052689 nonspecific carboxylesterase activity obo:GO_0052689 serine esterase activity obo:GO_0052689 GO:0052689 obo:GO_0052689 carboxylic ester hydrolase activity obo:GO_0055082 Any biological process involved in the maintenance of an internal steady state of a chemical at the level of the cell. obo:GO_0055082 obo:go.owl obo:GO_0055082 biological_process obo:GO_0055082 GO:0055082 obo:GO_0055082 cellular chemical homeostasis obo:GO_0055093 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating increased oxygen tension. obo:GO_0055093 obo:go.owl obo:GO_0055093 response to hyperoxic stress obo:GO_0055093 response to increased oxygen tension obo:GO_0055093 biological_process obo:GO_0055093 GO:0055093 obo:GO_0055093 response to hyperoxia obo:GO_0055100 Interacting selectively and non-covalently with adiponectin, a protein hormone produced by adipose tissue that modulates a number of metabolic processes, including glucose regulation and fatty acid catabolism. obo:GO_0055100 obo:go.owl obo:GO_0055100 molecular_function obo:GO_0055100 GO:0055100 obo:GO_0055100 adiponectin binding obo:GO_0055112 The splitting or migration of one epithelial sheet into two involved in the process of deuterostomic gastrulation. obo:GO_0055112 obo:go.owl obo:GO_0055112 biological_process obo:GO_0055112 GO:0055112 obo:GO_0055112 delamination involved in gastrulation with mouth forming second obo:GO_0055121 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of the detection of a high fluence blue light stimulus by the blue high-fluence system. Blue light is electromagnetic radiation with a wavelength of between 440 and 500nm. The blue high-fluence system responds to blue light at levels between 100 and 1000 micromols/m2. obo:GO_0055121 obo:go.owl obo:GO_0055121 response to high fluence blue light obo:GO_0055121 biological_process obo:GO_0055121 response to high fluence blue light by bhf system obo:GO_0055121 GO:0055121 obo:GO_0055121 response to high fluence blue light stimulus by blue high-fluence system obo:GO_0055122 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a very low light intensity stimulus. A very low light intensity stimulus is defined as a level of electromagnetic radiation below 0.001 mmol/m2/sec. obo:GO_0055122 obo:go.owl obo:GO_0055122 biological_process obo:GO_0055122 GO:0055122 obo:GO_0055122 response to very low light intensity stimulus obo:GO_0055131 Interacting selectively and non-covalently with a C3HC4-type zinc finger domain of a protein. The C3HC4-type zinc finger is a variant of RING finger, is a cysteine-rich domain of 40 to 60 residues that coordinates two zinc ions, and has the consensus sequence: C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C, where X is any amino acid. Many proteins containing a C3HC4-type RING finger play a key role in the ubiquitination pathway. obo:GO_0055131 obo:go.owl obo:GO_0055131 Jennifer I Deegan obo:GO_0055131 2009-10-22T02:20:33Z obo:GO_0055131 molecular_function obo:GO_0055131 GO:0055131 obo:GO_0055131 C3HC4-type RING finger domain binding obo:GO_0060003 The directed movement of copper ions out of a cell or organelle. obo:GO_0060003 obo:go.owl obo:GO_0060003 copper export obo:GO_0060003 biological_process obo:GO_0060003 GO:0060003 obo:GO_0060003 copper ion export obo:GO_0060054 Any process that activates or increases the rate or extent of epithelial cell proliferation, contributing to the restoration of integrity to a damaged tissue following an injury. obo:GO_0060054 obo:go.owl obo:GO_0060054 biological_process obo:GO_0060054 GO:0060054 obo:GO_0060054 positive regulation of epithelial cell proliferation involved in wound healing obo:GO_0060134 The process in which a startle magnitude is reduced when the startling stimulus is preceded by a low-intensity prepulse. obo:GO_0060134 obo:go.owl obo:GO_0060134 Wikipedia:Prepulse_inhibition obo:GO_0060134 pre-pulse inhibition obo:GO_0060134 biological_process obo:GO_0060134 PPI obo:GO_0060134 GO:0060134 obo:GO_0060134 prepulse inhibition obo:GO_0060178 Any process that modulates the localization of exocysts. An exocyst is a protein complex peripherally associated with the plasma membrane that determines where vesicles dock and fuse. obo:GO_0060178 obo:go.owl obo:GO_0060178 regulation of exocyst localisation obo:GO_0060178 biological_process obo:GO_0060178 GO:0060178 obo:GO_0060178 regulation of exocyst localization obo:GO_0060232 The process of negative regulation of cell adhesion that results in a cell or sheet of cells splitting off from an existing epithelial sheet. obo:GO_0060232 obo:go.owl obo:GO_0060232 biological_process obo:GO_0060232 GO:0060232 obo:GO_0060232 delamination obo:GO_0060233 The negative regulation of cell adhesion process in which an oenocyte splits off of an existing epithelial sheet. obo:GO_0060233 obo:go.owl obo:GO_0060233 biological_process obo:GO_0060233 GO:0060233 obo:GO_0060233 oenocyte delamination obo:GO_0060234 The negative regulation of cell adhesion process in which a neuroblast splits off of a neurectodermal sheet. obo:GO_0060234 obo:go.owl obo:GO_0060234 biological_process obo:GO_0060234 GO:0060234 obo:GO_0060234 neuroblast delamination obo:GO_0060244 Any process that stops, prevents or reduces the rate or extent of cell proliferation in response to cell density. obo:GO_0060244 obo:go.owl obo:GO_0060244 biological_process obo:GO_0060244 GO:0060244 obo:GO_0060244 negative regulation of cell proliferation involved in contact inhibition obo:GO_0060245 The series of events in which information about the density of cells in a population is received and converted into a molecular signal. obo:GO_0060245 obo:go.owl obo:GO_0060245 biological_process obo:GO_0060245 GO:0060245 obo:GO_0060245 detection of cell density obo:GO_0060246 The series of events in which information about the density of cells in a population is received by direct cell-cell contact and is converted into a molecular signal. obo:GO_0060246 obo:go.owl obo:GO_0060246 biological_process obo:GO_0060246 GO:0060246 obo:GO_0060246 detection of cell density by contact stimulus obo:GO_0060247 The series of events in which information about the density of cells in a population is received by the detection of a secreted molecule and is converted into a molecular signal. obo:GO_0060247 obo:go.owl obo:GO_0060247 biological_process obo:GO_0060247 GO:0060247 obo:GO_0060247 detection of cell density by secreted molecule obo:GO_0060248 The series of events in which information about the density of cells in a population is received by direct cell-cell contact and is converted into a molecular signal, resulting in the cessation of cell growth or proliferation. obo:GO_0060248 obo:go.owl obo:GO_0060248 biological_process obo:GO_0060248 GO:0060248 obo:GO_0060248 detection of cell density by contact stimulus involved in contact inhibition obo:GO_0060306 Any process that modulates the establishment or extent of a membrane potential in the polarizing direction towards the resting potential, usually from positive to negative. obo:GO_0060306 obo:go.owl obo:GO_0060306 biological_process obo:GO_0060306 GO:0060306 obo:GO_0060306 regulation of membrane repolarization obo:GO_0060307 Any process that modulates the establishment or extent of a membrane potential in the polarizing direction towards the resting potential in a ventricular cardiomyocyte. obo:GO_0060307 obo:go.owl obo:GO_0060307 regulation of ventricular cardiac muscle cell repolarization obo:GO_0060307 regulation of ventricular cardiomyocyte membrane repolarization obo:GO_0060307 biological_process obo:GO_0060307 electrocardiogram T wave obo:GO_0060307 regulation of ventricular cardiac muscle repolarization obo:GO_0060307 ventricular repolarization obo:GO_0060307 GO:0060307 obo:GO_0060307 regulation of ventricular cardiac muscle cell membrane repolarization obo:GO_0060341 Any process that modulates the frequency, rate or extent of a process in which a cell, a substance, or a cellular entity is transported to, or maintained in a specific location within or in the membrane of a cell. obo:GO_0060341 obo:go.owl obo:GO_0060341 regulation of cellular localisation obo:GO_0060341 biological_process obo:GO_0060341 GO:0060341 obo:GO_0060341 regulation of cellular localization obo:GO_0060372 Any process that modulates the establishment or extent of a membrane potential in the polarizing direction towards the resting potential in an atrial cardiomyocyte. obo:GO_0060372 obo:go.owl obo:GO_0060372 regulation of atrial cardiac muscle cell repolarization obo:GO_0060372 regulation of atrial cardiomyocyte membrane repolarization obo:GO_0060372 biological_process obo:GO_0060372 atrial repolarization obo:GO_0060372 electrocardiogram QRS complex obo:GO_0060372 GO:0060372 obo:GO_0060372 regulation of atrial cardiac muscle cell membrane repolarization obo:GO_0060401 The directed movement of calcium ions (Ca2+) into, out of or within the cytosol. obo:GO_0060401 obo:go.owl obo:GO_0060401 biological_process obo:GO_0060401 GO:0060401 obo:GO_0060401 cytosolic calcium ion transport obo:GO_0060402 The directed movement of calcium ions (Ca2+) into the cytosol. obo:GO_0060402 obo:go.owl obo:GO_0060402 biological_process obo:GO_0060402 GO:0060402 obo:GO_0060402 calcium ion transport into cytosol obo:GO_0060583 Any process that modulates the localization of an actin cortical patch. An actin cortical patch is a discrete actin-containing structure found just beneath the plasma membrane in fungal cells. obo:GO_0060583 obo:go.owl obo:GO_0060583 dph obo:GO_0060583 2009-05-08T01:58:42Z obo:GO_0060583 regulation of actin cortical patch localisation obo:GO_0060583 biological_process obo:GO_0060583 GO:0060583 obo:GO_0060583 regulation of actin cortical patch localization obo:GO_0060589 Modulates the rate of NTP hydrolysis by a NTPase. obo:GO_0060589 obo:go.owl obo:GO_0060589 dph obo:GO_0060589 2009-05-08T02:49:24Z obo:GO_0060589 NTPase regulator activity obo:GO_0060589 molecular_function obo:GO_0060589 GO:0060589 obo:GO_0060589 nucleoside-triphosphatase regulator activity obo:GO_0060784 Any process that modulates the frequency, rate or extent of cell proliferation resulting in the maintenance of a steady-state number of cells within a tissue. obo:GO_0060784 obo:go.owl obo:GO_0060784 dph obo:GO_0060784 2009-07-31T01:46:28Z obo:GO_0060784 biological_process obo:GO_0060784 GO:0060784 obo:GO_0060784 regulation of cell proliferation involved in tissue homeostasis obo:GO_0060904 Any process that modulates the rate, frequency or extent of the protein folding process that takes place in the endoplasmic reticulum (ER). Secreted, plasma membrane and organelle proteins are folded in the ER, assisted by chaperones and foldases (protein disulphide isomerases), and additional factors required for optimal folding (ATP, Ca2+ and an oxidizing environment to allow disulfide bond formation). obo:GO_0060904 obo:go.owl obo:GO_0060904 dph obo:GO_0060904 2009-08-14T01:12:00Z obo:GO_0060904 biological_process obo:GO_0060904 GO:0060904 obo:GO_0060904 regulation of protein folding in endoplasmic reticulum obo:GO_0060992 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a fungicide stimulus. Fungicides are chemicals used to kill fungi. obo:GO_0060992 obo:go.owl obo:GO_0060992 dph obo:GO_0060992 2010-01-13T08:05:58Z obo:GO_0060992 biological_process obo:GO_0060992 GO:0060992 obo:GO_0060992 response to fungicide obo:GO_0061006 Any process that modulates the frequency, rate or extent of cell proliferation that contributes to the shaping of the kidney. obo:GO_0061006 obo:go.owl obo:GO_0061006 dph obo:GO_0061006 2010-01-21T11:25:23Z obo:GO_0061006 biological_process obo:GO_0061006 GO:0061006 obo:GO_0061006 regulation of cell proliferation involved in kidney morphogenesis obo:GO_0061083 Any process that regulates the rate, frequency, or extent of protein refolding. Protein refolding is the process carried out by a cell that restores the biological activity of an unfolded or misfolded protein, using helper proteins such as chaperones. obo:GO_0061083 obo:go.owl obo:GO_0061083 dph obo:GO_0061083 2010-04-26T01:07:54Z obo:GO_0061083 biological_process obo:GO_0061083 GO:0061083 obo:GO_0061083 regulation of protein refolding obo:GO_0061084 Any process that decreases the rate, frequency, or extent of protein refolding. Protein refolding is the process carried out by a cell that restores the biological activity of an unfolded or misfolded protein, using helper proteins such as chaperones. obo:GO_0061084 obo:go.owl obo:GO_0061084 dph obo:GO_0061084 2010-04-26T01:11:29Z obo:GO_0061084 biological_process obo:GO_0061084 GO:0061084 obo:GO_0061084 negative regulation of protein refolding obo:GO_0061118 Any process that modulates the rate, frequency, or extent of directed movement of a motile cell or organism up a concentration gradient of 3',5'-cAMP. obo:GO_0061118 obo:go.owl obo:GO_0061118 dph obo:GO_0061118 2010-05-17T07:47:47Z obo:GO_0061118 biological_process obo:GO_0061118 GO:0061118 obo:GO_0061118 regulation of positive chemotaxis to cAMP obo:GO_0061119 Any process that modulates the rate, frequency, or extent of directed movement of a motile cell or organism up a concentration gradient of 3',5'-cAMP by the action of a chlorinated alkylphenone. An alkylphenone is an aromatic polyketide with methyl and chlorine substitutions. obo:GO_0061119 obo:go.owl obo:GO_0061119 dph obo:GO_0061119 2010-05-17T07:53:58Z obo:GO_0061119 biological_process obo:GO_0061119 GO:0061119 obo:GO_0061119 regulation of positive chemotaxis to cAMP by chlorinated alkylphenone obo:GO_0061120 Any process that modulates the rate, frequency, or extent of directed movement of a motile cell or organism up a concentration gradient of 3',5'-cAMP by the action of DIF-1. DIF-1 is a chlorinated alkylphenone. obo:GO_0061120 obo:go.owl obo:GO_0061120 dph obo:GO_0061120 2010-05-17T08:10:20Z obo:GO_0061120 biological_process obo:GO_0061120 GO:0061120 obo:GO_0061120 regulation of positive chemotaxis to cAMP by DIF-1 obo:GO_0061121 Any process that modulates the rate, frequency, or extent of directed movement of a motile cell or organism up a concentration gradient of 3',5'-cAMP by the action of DIF-2. DIF-2 is a chlorinated alkylphenone. obo:GO_0061121 obo:go.owl obo:GO_0061121 dph obo:GO_0061121 2010-05-17T08:16:21Z obo:GO_0061121 biological_process obo:GO_0061121 GO:0061121 obo:GO_0061121 regulation of positive chemotaxis to cAMP by DIF-2 obo:GO_0061122 Any process that increases the rate, frequency, or extent of directed movement of a motile cell or organism up a concentration gradient of 3',5'-cAMP. obo:GO_0061122 obo:go.owl obo:GO_0061122 dph obo:GO_0061122 2010-05-17T08:25:55Z obo:GO_0061122 biological_process obo:GO_0061122 GO:0061122 obo:GO_0061122 positive regulation of positive chemotaxis to cAMP obo:GO_0061123 Any process that decreases the rate, frequency, or extent of directed movement of a motile cell or organism up a concentration gradient of 3',5'-cAMP. obo:GO_0061123 obo:go.owl obo:GO_0061123 dph obo:GO_0061123 2010-05-17T08:27:20Z obo:GO_0061123 biological_process obo:GO_0061123 GO:0061123 obo:GO_0061123 negative regulation of positive chemotaxis to cAMP obo:GO_0061124 Any process that increases the rate, frequency, or extent of directed movement of a motile cell or organism up a concentration gradient of 3',5'-cAMP by the action of a chlorinated alkylphenone. An alkylphenone is an aromatic polyketide with methyl and chlorine substitutions. obo:GO_0061124 obo:go.owl obo:GO_0061124 dph obo:GO_0061124 2010-05-17T08:33:40Z obo:GO_0061124 biological_process obo:GO_0061124 GO:0061124 obo:GO_0061124 positive regulation of positive chemotaxis to cAMP by chlorinated alkylphenone obo:GO_0061125 Any process that decreases the rate, frequency, or extent of directed movement of a motile cell or organism up a concentration gradient of 3',5'-cAMP by the action of a chlorinated alkylphenone. An alkylphenone is an aromatic polyketide with methyl and chlorine substitutions. obo:GO_0061125 obo:go.owl obo:GO_0061125 dph obo:GO_0061125 2010-05-17T08:36:55Z obo:GO_0061125 biological_process obo:GO_0061125 GO:0061125 obo:GO_0061125 negative regulation of positive chemotaxis to cAMP by chlorinated alkylphenone obo:GO_0061126 Any process that increases the rate, frequency, or extent of directed movement of a motile cell or organism up a concentration gradient of 3',5'-cAMP by the action of DIF-1. DIF-1 is a chlorinated alkylphenone. obo:GO_0061126 obo:go.owl obo:GO_0061126 dph obo:GO_0061126 2010-05-17T08:41:04Z obo:GO_0061126 biological_process obo:GO_0061126 GO:0061126 obo:GO_0061126 positive regulation of positive chemotaxis to cAMP by DIF-1 obo:GO_0061127 Any process that decreases the rate, frequency, or extent of directed movement of a motile cell or organism up a concentration gradient of 3',5'-cAMP by the action of DIF-1. DIF-1 is a chlorinated alkylphenone. obo:GO_0061127 obo:go.owl obo:GO_0061127 dph obo:GO_0061127 2010-05-17T08:45:03Z obo:GO_0061127 biological_process obo:GO_0061127 GO:0061127 obo:GO_0061127 negative regulation of positive chemotaxis to cAMP by DIF-1 obo:GO_0061128 Any process that increases the rate, frequency, or extent of directed movement of a motile cell or organism up a concentration gradient of 3',5'-cAMP by the action of DIF-2. DIF-2 is a chlorinated alkylphenone. obo:GO_0061128 obo:go.owl obo:GO_0061128 dph obo:GO_0061128 2010-05-17T08:48:17Z obo:GO_0061128 biological_process obo:GO_0061128 GO:0061128 obo:GO_0061128 positive regulation of chemotaxis to cAMP by DIF-2 obo:GO_0061129 Any process that decreases the rate, frequency, or extent of directed movement of a motile cell or organism up a concentration gradient of 3',5'-cAMP by the action of DIF-2. DIF-2 is a chlorinated alkylphenone. obo:GO_0061129 obo:go.owl obo:GO_0061129 dph obo:GO_0061129 2010-05-17T08:50:33Z obo:GO_0061129 biological_process obo:GO_0061129 GO:0061129 obo:GO_0061129 negative regulation of positive chemotaxis to cAMP by DIF-2 obo:GO_0061469 Any process that modulates the frequency, rate or extent of type B pancreatic cell proliferation. obo:GO_0061469 obo:go.owl obo:GO_0061469 dph obo:GO_0061469 2012-11-01T13:16:23Z obo:GO_0061469 biological_process obo:GO_0061469 GO:0061469 obo:GO_0061469 regulation of type B pancreatic cell proliferation obo:GO_0061479 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a reverse transcriptase inhibitor stimulus. obo:GO_0061479 obo:go.owl obo:GO_0061479 dph obo:GO_0061479 2012-11-07T09:10:51Z obo:GO_0061479 biological_process obo:GO_0061479 GO:0061479 obo:GO_0061479 response to reverse transcriptase inhibitor obo:GO_0061507 Interacting selectively and non-covalently with cyclic-GMP-AMP (cGAMP) cyclic nucleotide. obo:GO_0061507 obo:go.owl obo:GO_0061507 dph obo:GO_0061507 2013-01-24T15:38:27Z obo:GO_0061507 molecular_function obo:GO_0061507 GO:0061507 obo:GO_0061507 cyclic-GMP-AMP binding obo:GO_0061577 A process in which a calcium ion is transported from one side of a membrane to the other by means of a high voltage-gated calcium channel. obo:GO_0061577 obo:go.owl obo:GO_0061577 dph obo:GO_0061577 2013-11-15T16:20:27Z obo:GO_0061577 biological_process obo:GO_0061577 generation of L-type calcium current obo:GO_0061577 GO:0061577 obo:GO_0061577 calcium ion transmembrane transport via high voltage-gated calcium channel obo:GO_0061628 Interacting selectively and non-covalently with a histone H3 in which the lysine residue at position 27 has been modified by trimethylation. obo:GO_0061628 obo:go.owl obo:GO_0061628 dph obo:GO_0061628 2014-05-14T15:36:53Z obo:GO_0061628 H3-K27me3 modified histone binding obo:GO_0061628 molecular_function obo:GO_0061628 GO:0061628 obo:GO_0061628 H3K27me3 modified histone binding obo:GO_0061629 Interacting selectively and non-covalently with a sequence-specific DNA binding RNA polymerase II transcription factor, any of the factors that interact selectively and non-covalently with a specific DNA sequence in order to modulate transcription. obo:GO_0061629 obo:go.owl obo:GO_0061629 dph obo:GO_0061629 2014-05-15T09:12:24Z obo:GO_0061629 RNA polymerase II sequence-specific DNA binding transcription factor binding obo:GO_0061629 RNA polymerase II sequence-specific DNA-binding transcription factor binding obo:GO_0061629 molecular_function obo:GO_0061629 GO:0061629 obo:GO_0061629 RNA polymerase II-specific DNA-binding transcription factor binding obo:GO_0061649 Interacting selectively and non-covalently with a histone protein in which a residue has been modified by ubiquitination. Histones are any of a group of water-soluble proteins found in association with the DNA of eukaroytic chromosomes. obo:GO_0061649 obo:go.owl obo:GO_0061649 dph obo:GO_0061649 2014-11-04T10:21:04Z obo:GO_0061649 molecular_function obo:GO_0061649 ubiquitinated histone binding obo:GO_0061649 GO:0061649 obo:GO_0061649 ubiquitin modification-dependent histone binding obo:GO_0061675 Interacting selectively and non-covalently with any member of the rhamnose-binding lectin (RBL) family, a family of animal lectins that show specific binding activities to L-rhamnose or D-galactose. obo:GO_0061675 obo:go.owl obo:GO_0061675 dph obo:GO_0061675 2015-01-10T18:22:42Z obo:GO_0061675 rhamnose-binding lectin family protein binding obo:GO_0061675 molecular_function obo:GO_0061675 GO:0061675 obo:GO_0061675 RBL family protein binding obo:GO_0061676 Interacting selectively and non-covalently with any member of the importin-alpha family. obo:GO_0061676 obo:go.owl obo:GO_0061676 dph obo:GO_0061676 2015-01-10T18:25:22Z obo:GO_0061676 molecular_function obo:GO_0061676 GO:0061676 obo:GO_0061676 importin-alpha family protein binding obo:GO_0061730 Interacting selectively and non-covalently with C-rich, single-stranded, telomere-associated DNA. obo:GO_0061730 obo:go.owl obo:GO_0061730 dph obo:GO_0061730 2015-08-20T09:08:27Z obo:GO_0061730 molecular_function obo:GO_0061730 GO:0061730 obo:GO_0061730 C-rich strand telomeric DNA binding obo:GO_0061752 Interacting selectively and non-covalently with long non-coding RNA molecules transcribed from subtelomeric regions in most eukaryotes. Telomeric repeat-containing RNA (TERRA) molecules consist of subtelomeric-derived sequences and G-rich telomeric repeats. obo:GO_0061752 obo:go.owl obo:GO_0061752 dph obo:GO_0061752 2015-11-13T07:55:06Z obo:GO_0061752 TERRA binding obo:GO_0061752 molecular_function obo:GO_0061752 GO:0061752 obo:GO_0061752 telomeric repeat-containing RNA binding obo:GO_0061761 Interacting selectively and non-covalently with an alpha-latrotoxin receptor. obo:GO_0061761 obo:go.owl obo:GO_0061761 dph obo:GO_0061761 2016-04-13T10:46:42Z obo:GO_0061761 lasso receptor binding obo:GO_0061761 latrophilin binding obo:GO_0061761 molecular_function obo:GO_0061761 GO:0061761 obo:GO_0061761 alpha-latrotoxin receptor binding obo:GO_0061770 Interacting selectively and non-covalently with a translation elongation factor, any polypeptide factor involved in the peptide elongation in ribosome-mediated translation. obo:GO_0061770 obo:go.owl obo:GO_0061770 dph obo:GO_0061770 2016-07-09T09:31:11Z obo:GO_0061770 molecular_function obo:GO_0061770 GO:0061770 obo:GO_0061770 translation elongation factor binding obo:GO_0061776 The DNA binding activity by which a protein complex interacts selectively and non-covalently with more than one DNA duplex to encircle the DNA molecules with a loose fitting ring. obo:GO_0061776 obo:go.owl obo:GO_0061776 dph obo:GO_0061776 2016-07-13T13:10:15Z obo:GO_0061776 molecular_function obo:GO_0061776 GO:0061776 obo:GO_0061776 topological DNA entrapment activity obo:GO_0061788 Interacting selectively and non-covalently with Epidermal Growth Factor (EGF) repeats. obo:GO_0061788 obo:go.owl obo:GO_0061788 dph obo:GO_0061788 2016-09-08T15:22:28Z obo:GO_0061788 Epidermal growth factor domain binding obo:GO_0061788 molecular_function obo:GO_0061788 Epidermal Growth Factor repeat binding obo:GO_0061788 GO:0061788 obo:GO_0061788 EGF repeat binding obo:GO_0061821 Interacting selectively and non-covalently with a telomeric D-loop. A telomeric D-loop is a three-stranded DNA displacement loop that forms at the site where the telomeric 3' single-stranded DNA overhang (formed of the repeat sequence TTAGGG in mammals) is tucked back inside the double-stranded component of telomeric DNA molecule, thus forming a t-loop or telomeric-loop and protecting the chromosome terminus. obo:GO_0061821 obo:go.owl obo:GO_0061821 dph obo:GO_0061821 telomeric Displacement-loop binding obo:GO_0061821 molecular_function obo:GO_0061821 GO:0061821 obo:GO_0061821 telomeric D-loop binding obo:GO_0061849 Interacting selectively and non-covalently with telomeric G-quadruplex DNA structures, in which groups of four guanines adopt a flat, cyclic Hoogsteen hydrogen-bonding arrangement known as a guanine tetrad. The stacking of guanine tetrads results in G-quadruplex DNA structures in telomeres. obo:GO_0061849 obo:go.owl obo:GO_0061849 molecular_function obo:GO_0061849 GO:0061849 obo:GO_0061849 telomeric G-quadruplex DNA binding obo:GO_0061856 A process in which a calcium ion is transported from one side of a Golgi membrane to the other by means of some agent such as a transporter or pore. obo:GO_0061856 obo:go.owl obo:GO_0061856 dph obo:GO_0061856 2017-03-14T16:08:23Z obo:GO_0061856 biological_process obo:GO_0061856 GO:0061856 obo:GO_0061856 Golgi calcium ion transmembrane transport obo:GO_0061860 Catalysis of the reaction: ATP + H2O = ADP + phosphate, to drive the opening of the ring structure of the PCNA complex, or any of the related sliding clamp complexes, and their removal from the DNA duplex. obo:GO_0061860 obo:go.owl obo:GO_0061860 dph obo:GO_0061860 2017-04-03T11:49:46Z obo:GO_0061860 molecular_function obo:GO_0061860 GO:0061860 obo:GO_0061860 DNA clamp unloader activity obo:GO_0061891 Interacting selectively and non-covalently with and responding, e.g. by conformational change, to changes in the cellular level of calcium ions (Ca2+). obo:GO_0061891 obo:go.owl obo:GO_0061891 dph obo:GO_0061891 2017-06-01T23:37:01Z obo:GO_0061891 molecular_function obo:GO_0061891 GO:0061891 obo:GO_0061891 calcium ion sensor activity obo:GO_0061980 Interacting selectively and non-covalently with a small regulatory RNA, a short RNA (usually 50-200 nt long) that is either independently transcribed or processed from a longer RNA by an RNAse enzyme. obo:GO_0061980 obo:go.owl obo:GO_0061980 dph obo:GO_0061980 2018-02-13T21:46:08Z obo:GO_0061980 molecular_function obo:GO_0061980 GO:0061980 obo:GO_0061980 regulatory RNA binding obo:GO_0061984 A process in which the presence of one nutrient source leads to a decrease in the frequency, rate, or extent of processes involved in the metabolism of other nutrient sources. obo:GO_0061984 obo:go.owl obo:GO_0061984 dph obo:GO_0061984 2018-02-15T16:34:14Z obo:GO_0061984 biological_process obo:GO_0061984 GO:0061984 obo:GO_0061984 catabolite repression obo:GO_0061985 A process in which the presence of one carbon source leads to the modulation of the frequency, rate, or extent of the metabolism of other carbon sources. obo:GO_0061985 obo:go.owl obo:GO_0061985 dph obo:GO_0061985 2018-02-15T16:49:48Z obo:GO_0061985 biological_process obo:GO_0061985 GO:0061985 obo:GO_0061985 carbon catabolite repression obo:GO_0062037 Interacting selectively and non-covalently with a DNA D-loop. A D-loop is a three-stranded DNA structure formed by the invasion of a single DNA strand that base pairs with one strand of duplex DNA, while the rest of the double-stranded DNA does not unwind. obo:GO_0062037 obo:go.owl obo:GO_0062037 dph obo:GO_0062037 2018-04-30T15:21:21Z obo:GO_0062037 DNA displacement loop binding obo:GO_0062037 molecular_function obo:GO_0062037 GO:0062037 obo:GO_0062037 D-loop DNA binding obo:GO_0062058 Interacting selectively and non-covalently with a transcription factor TFIIH holo complex. obo:GO_0062058 obo:go.owl obo:GO_0062058 dph obo:GO_0062058 2018-08-31T13:44:17Z obo:GO_0062058 molecular_function obo:GO_0062058 GO:0062058 obo:GO_0062058 transcription factor TFIIH holo complex binding obo:GO_0062059 Interacting selectively and non-covalently with a FACT complex. obo:GO_0062059 obo:go.owl obo:GO_0062059 dph obo:GO_0062059 2018-08-31T13:49:30Z obo:GO_0062059 molecular_function obo:GO_0062059 GO:0062059 obo:GO_0062059 FACT complex binding obo:GO_0062060 Interacting selectively and non-covalently with a NuA4 histone acetyltransferase complex. obo:GO_0062060 obo:go.owl obo:GO_0062060 dph obo:GO_0062060 2018-08-31T13:51:45Z obo:GO_0062060 molecular_function obo:GO_0062060 GO:0062060 obo:GO_0062060 NuA4 histone acetyltransferase complex binding obo:GO_0062061 Interacting selectively and non-covalently with a TAP complex. obo:GO_0062061 obo:go.owl obo:GO_0062061 dph obo:GO_0062061 2018-08-31T13:54:22Z obo:GO_0062061 molecular_function obo:GO_0062061 GO:0062061 obo:GO_0062061 TAP complex binding obo:GO_0062062 Interacting selectively and non-covalently with an oligosaccharyltransferase complex. obo:GO_0062062 obo:go.owl obo:GO_0062062 dph obo:GO_0062062 2018-08-31T13:56:32Z obo:GO_0062062 molecular_function obo:GO_0062062 GO:0062062 obo:GO_0062062 oligosaccharyltransferase complex binding obo:GO_0062063 Interacting selectively and non-covalently with a BBSome complex. obo:GO_0062063 obo:go.owl obo:GO_0062063 dph obo:GO_0062063 2018-08-31T13:59:18Z obo:GO_0062063 molecular_function obo:GO_0062063 GO:0062063 obo:GO_0062063 BBSome binding obo:GO_0062064 Interacting selectively and non-covalently with a box C/D snoRNP complex. obo:GO_0062064 obo:go.owl obo:GO_0062064 dph obo:GO_0062064 2018-08-31T14:01:03Z obo:GO_0062064 molecular_function obo:GO_0062064 GO:0062064 obo:GO_0062064 box C/D snoRNP complex binding obo:GO_0062065 Interacting selectively and non-covalently with a box H/ACA snoRNP complex. obo:GO_0062065 obo:go.owl obo:GO_0062065 dph obo:GO_0062065 2018-08-31T14:03:43Z obo:GO_0062065 molecular_function obo:GO_0062065 GO:0062065 obo:GO_0062065 box H/ACA snoRNP complex binding obo:GO_0062066 Interacting selectively and non-covalently with a PSII associated light-harvesting complex II. obo:GO_0062066 obo:go.owl obo:GO_0062066 dph obo:GO_0062066 2018-08-31T14:06:01Z obo:GO_0062066 molecular_function obo:GO_0062066 GO:0062066 obo:GO_0062066 PSII associated light-harvesting complex II binding obo:GO_0062067 Interacting selectively and non-covalently with a chloroplast photosystem I. obo:GO_0062067 obo:go.owl obo:GO_0062067 dph obo:GO_0062067 2018-08-31T14:07:46Z obo:GO_0062067 molecular_function obo:GO_0062067 GO:0062067 obo:GO_0062067 chloroplast photosystem I binding obo:GO_0062068 Interacting selectively and non-covalently with a chloroplast photosystem II. obo:GO_0062068 obo:go.owl obo:GO_0062068 dph obo:GO_0062068 2018-08-31T14:09:17Z obo:GO_0062068 molecular_function obo:GO_0062068 GO:0062068 obo:GO_0062068 chloroplast photosystem II binding obo:GO_0062069 Interacting selectively and non-covalently with a GARP complex. obo:GO_0062069 obo:go.owl obo:GO_0062069 dph obo:GO_0062069 2018-08-31T14:11:17Z obo:GO_0062069 molecular_function obo:GO_0062069 GO:0062069 obo:GO_0062069 GARP complex binding obo:GO_0062070 Interacting selectively and non-covalently with a SAGA complex. obo:GO_0062070 obo:go.owl obo:GO_0062070 dph obo:GO_0062070 2018-08-31T14:13:36Z obo:GO_0062070 molecular_function obo:GO_0062070 GO:0062070 obo:GO_0062070 SAGA complex binding obo:GO_0062072 Interacting selectively and non-covalently with a histone H3 in which the lysine residue at position 9 has been modified by trimethylation. obo:GO_0062072 obo:go.owl obo:GO_0062072 dph obo:GO_0062072 2018-09-05T12:58:43Z obo:GO_0062072 molecular_function obo:GO_0062072 GO:0062072 obo:GO_0062072 H3K9me3 modified histone binding obo:GO_0062078 Interacting selectively and non-covalently with a TSC1-TSC2 complex. obo:GO_0062078 obo:go.owl obo:GO_0062078 dph obo:GO_0062078 2018-10-11T12:31:42Z obo:GO_0062078 tuberin sclerosis complex binding obo:GO_0062078 tuberin-hamartin complex binding obo:GO_0062078 molecular_function obo:GO_0062078 GO:0062078 obo:GO_0062078 TSC1-TSC2 complex binding obo:GO_0062104 Interacting selectively and non-covalently with a region of RNA containing a Pumilio-response element element. The consensus sequence for the element is UGUAAAUA. obo:GO_0062104 obo:go.owl obo:GO_0062104 dph obo:GO_0062104 2019-01-11T13:38:26Z obo:GO_0062104 PRE binding obo:GO_0062104 molecular_function obo:GO_0062104 GO:0062104 obo:GO_0062104 pumilio-response element binding obo:GO_0062107 Any process that modulates the frequency, rate or extent of protein localization to a non-growing cell tip. obo:GO_0062107 obo:go.owl obo:GO_0062107 dph obo:GO_0062107 2019-02-05T12:59:18Z obo:GO_0062107 biological_process obo:GO_0062107 GO:0062107 obo:GO_0062107 regulation of protein localization to non-growing cell tip obo:GO_0062108 Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to a non-growing cell tip. obo:GO_0062108 obo:go.owl obo:GO_0062108 dph obo:GO_0062108 2019-02-05T13:03:52Z obo:GO_0062108 biological_process obo:GO_0062108 GO:0062108 obo:GO_0062108 negative regulation of protein localization to non-growing cell tip obo:GO_0062111 The directed import of zinc(2+) from the cytosol, across an organelle membrane, into the organelle. obo:GO_0062111 obo:go.owl obo:GO_0062111 dph obo:GO_0062111 2019-02-05T15:27:38Z obo:GO_0062111 biological_process obo:GO_0062111 GO:0062111 obo:GO_0062111 zinc ion import into organelle obo:GO_0065007 Any process that modulates a measurable attribute of any biological process, quality or function. obo:GO_0065007 obo:go.owl obo:GO_0065007 regulation obo:GO_0065007 biological_process obo:GO_0065007 GO:0065007 obo:GO_0065007 http://purl.oboInOwllibrary.org/oboInOwl/go#gocheck_do_not_annotate obo:GO_0065007 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0065007 biological regulation obo:GO_0065008 Any process that modulates a qualitative or quantitative trait of a biological quality. A biological quality is a measurable attribute of an organism or part of an organism, such as size, mass, shape, color, etc. obo:GO_0065008 obo:go.owl obo:GO_0065008 regulation of biological attribute obo:GO_0065008 regulation of biological characteristic obo:GO_0065008 biological_process obo:GO_0065008 GO:0065008 obo:GO_0065008 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0065008 regulation of biological quality obo:GO_0065009 Any process that modulates the frequency, rate or extent of a molecular function, an elemental biological activity occurring at the molecular level, such as catalysis or binding. obo:GO_0065009 obo:go.owl obo:GO_0065009 regulation of a molecular function obo:GO_0065009 biological_process obo:GO_0065009 GO:0065009 obo:GO_0065009 http://purl.oboInOwllibrary.org/oboInOwl/go#gocheck_do_not_annotate obo:GO_0065009 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_agr obo:GO_0065009 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0065009 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_plant obo:GO_0065009 regulation of molecular function obo:GO_0070016 Interacting selectively and non-covalently with the armadillo repeat domain of a protein, an approximately 40 amino acid long tandemly repeated sequence motif first identified in the Drosophila segment polarity protein armadillo. Arm-repeat proteins are involved in various processes, including intracellular signalling and cytoskeletal regulation. obo:GO_0070016 obo:go.owl obo:GO_0070016 Arm repeat domain binding obo:GO_0070016 armadillo domain binding obo:GO_0070016 armadillo repeat binding obo:GO_0070016 molecular_function obo:GO_0070016 GO:0070016 obo:GO_0070016 armadillo repeat domain binding obo:GO_0070026 Interacting selectively and non-covalently with nitric oxide (NO). obo:GO_0070026 obo:go.owl obo:GO_0070026 NO binding obo:GO_0070026 nitrogen monoxide binding obo:GO_0070026 nitrosyl binding obo:GO_0070026 molecular_function obo:GO_0070026 GO:0070026 obo:GO_0070026 nitric oxide binding obo:GO_0070034 Interacting selectively and non-covalently with the telomerase RNA template. obo:GO_0070034 obo:go.owl obo:GO_0070034 molecular_function obo:GO_0070034 TERC binding obo:GO_0070034 GO:0070034 obo:GO_0070034 telomerase RNA binding obo:GO_0070051 Interacting selectively and non-covalently with fibrinogen, a highly soluble hexameric glycoprotein complex that is found in blood plasma and is converted to fibrin by thrombin in the coagulation cascade. obo:GO_0070051 obo:go.owl obo:GO_0070051 molecular_function obo:GO_0070051 GO:0070051 obo:GO_0070051 fibrinogen binding obo:GO_0070052 Interacting selectively and non-covalently with a type V collagen trimer. obo:GO_0070052 obo:go.owl obo:GO_0070052 molecular_function obo:GO_0070052 GO:0070052 obo:GO_0070052 collagen V binding obo:GO_0070061 Interacting selectively and non-covalently with the D- or L-enantiomer of fructose, the ketohexose arabino-hex-2-ulose. obo:GO_0070061 obo:go.owl obo:GO_0070061 molecular_function obo:GO_0070061 GO:0070061 obo:GO_0070061 fructose binding obo:GO_0070063 Interacting selectively and non-covalently with an RNA polymerase molecule or complex. obo:GO_0070063 obo:go.owl obo:GO_0070063 molecular_function obo:GO_0070063 GO:0070063 obo:GO_0070063 RNA polymerase binding obo:GO_0070064 Interacting selectively and non-covalently with a proline-rich region, i.e. a region that contains a high proportion of proline residues, in a protein. obo:GO_0070064 obo:go.owl obo:GO_0070064 molecular_function obo:GO_0070064 GO:0070064 obo:GO_0070064 proline-rich region binding obo:GO_0070080 Interacting selectively and non-covalently with the titin Z domain, which recognizes and binds to the C-terminal calmodulin-like domain of alpha-actinin-2 (Act-EF34), adopts a helical structure, and binds in a groove formed by the two planes between the helix pairs of Act-EF34. obo:GO_0070080 obo:go.owl obo:GO_0070080 Z repeat domain binding obo:GO_0070080 molecular_function obo:GO_0070080 GO:0070080 obo:GO_0070080 titin Z domain binding obo:GO_0070087 Interacting selectively and non-covalently with a chromo shadow domain, a protein domain that is distantly related, and found in association with, the chromo domain. obo:GO_0070087 obo:go.owl obo:GO_0070087 chromoshadow domain binding obo:GO_0070087 molecular_function obo:GO_0070087 GO:0070087 obo:GO_0070087 chromo shadow domain binding obo:GO_0070095 Interacting selectively and non-covalently with fructose 6-phosphate. obo:GO_0070095 obo:go.owl obo:GO_0070095 fructose 6-phosphate binding obo:GO_0070095 D-fructose 6-phosphate binding obo:GO_0070095 molecular_function obo:GO_0070095 GO:0070095 obo:GO_0070095 fructose-6-phosphate binding obo:GO_0070097 Interacting selectively and non-covalently with the delta subunit of the catenin complex. obo:GO_0070097 obo:go.owl obo:GO_0070097 molecular_function obo:GO_0070097 GO:0070097 obo:GO_0070097 delta-catenin binding obo:GO_0070119 Interacting selectively and non-covalently with the cytokine ciliary neurotrophic factor. obo:GO_0070119 obo:go.owl obo:GO_0070119 CNTF binding obo:GO_0070119 molecular_function obo:GO_0070119 GO:0070119 obo:GO_0070119 ciliary neurotrophic factor binding obo:GO_0070141 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a UV-A radiation stimulus. UV-A radiation (UV-A light) spans the wavelengths 315 to 400 nm. obo:GO_0070141 obo:go.owl obo:GO_0070141 response to UV-A light stimulus obo:GO_0070141 response to UV-A radiation stimulus obo:GO_0070141 response to UVA light stimulus obo:GO_0070141 response to UVA radiation stimulus obo:GO_0070141 biological_process obo:GO_0070141 GO:0070141 obo:GO_0070141 response to UV-A obo:GO_0070180 Interacting selectively and non-covalently with the large ribosomal subunit RNA (LSU rRNA), a constituent of the large ribosomal subunit. In S. cerevisiae, this is the 25S rRNA. obo:GO_0070180 obo:go.owl obo:GO_0070180 25S rRNA binding obo:GO_0070180 LSU rRNA binding obo:GO_0070180 molecular_function obo:GO_0070180 GO:0070180 obo:GO_0070180 large ribosomal subunit rRNA binding obo:GO_0070181 Interacting selectively and non-covalently with the small ribosomal subunit RNA (SSU rRNA), a constituent of the small ribosomal subunit. In S. cerevisiae, this is the 18S rRNA. obo:GO_0070181 obo:go.owl obo:GO_0070181 18S rRNA binding obo:GO_0070181 SSU rRNA binding obo:GO_0070181 molecular_function obo:GO_0070181 GO:0070181 obo:GO_0070181 small ribosomal subunit rRNA binding obo:GO_0070182 Interacting selectively and non-covalently with a DNA polymerase. obo:GO_0070182 obo:go.owl obo:GO_0070182 molecular_function obo:GO_0070182 GO:0070182 obo:GO_0070182 DNA polymerase binding obo:GO_0070186 The action characteristic of growth hormone, a peptide hormone that is secreted by the anterior pituitary or the placenta into the circulation, and binds to membrane receptors in target tissues to stimulate body growth. obo:GO_0070186 obo:go.owl obo:GO_0070186 GH activity obo:GO_0070186 pituitary growth hormone activity obo:GO_0070186 placental growth hormone activity obo:GO_0070186 molecular_function obo:GO_0070186 GO:0070186 obo:GO_0070186 growth hormone activity obo:GO_0070201 Any process that modulates the frequency, rate or extent of the directed movement of a protein to a specific location. obo:GO_0070201 obo:go.owl obo:GO_0070201 regulation of establishment of protein localisation obo:GO_0070201 biological_process obo:GO_0070201 GO:0070201 obo:GO_0070201 regulation of establishment of protein localization obo:GO_0070202 Any process that modulates the frequency, rate or extent of the directed movement of a protein to a specific location on a chromosome. obo:GO_0070202 obo:go.owl obo:GO_0070202 regulation of establishment of protein localisation to chromosome obo:GO_0070202 biological_process obo:GO_0070202 GO:0070202 obo:GO_0070202 regulation of establishment of protein localization to chromosome obo:GO_0070203 Any process that modulates the frequency, rate or extent of the directed movement of a protein to a specific location in the telomeric region of a chromosome. obo:GO_0070203 obo:go.owl obo:GO_0070203 regulation of establishment of protein localisation to telomere obo:GO_0070203 biological_process obo:GO_0070203 GO:0070203 obo:GO_0070203 regulation of establishment of protein localization to telomere obo:GO_0070273 Interacting selectively and non-covalently with phosphatidylinositol-4-phosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 4' position. obo:GO_0070273 obo:go.owl obo:GO_0070273 molecular_function obo:GO_0070273 GO:0070273 obo:GO_0070273 phosphatidylinositol-4-phosphate binding obo:GO_0070279 Interacting selectively and non-covalently with any of the vitamin B6 compounds: pyridoxal, pyridoxamine and pyridoxine and the active form, pyridoxal phosphate. obo:GO_0070279 obo:go.owl obo:GO_0070279 molecular_function obo:GO_0070279 GO:0070279 obo:GO_0070279 vitamin B6 binding obo:GO_0070280 Interacting selectively and non-covalently with pyridoxal, 3-hydroxy-5-(hydroxymethyl)-2-methylpyridine-4-carbaldehyde, a form of vitamin B6. obo:GO_0070280 obo:go.owl obo:GO_0070280 molecular_function obo:GO_0070280 GO:0070280 obo:GO_0070280 pyridoxal binding obo:GO_0070281 Interacting selectively and non-covalently with pyridoxamine, 4-(aminomethyl)-5-(hydroxymethyl)-2-methylpyridin-3-ol, a form of vitamin B6. obo:GO_0070281 obo:go.owl obo:GO_0070281 molecular_function obo:GO_0070281 GO:0070281 obo:GO_0070281 pyridoxamine binding obo:GO_0070282 Interacting selectively and non-covalently with pyridoxine, 4,5-bis(hydroxymethyl)-2-methylpyridin-3-ol, a form of vitamin B6. obo:GO_0070282 obo:go.owl obo:GO_0070282 molecular_function obo:GO_0070282 GO:0070282 obo:GO_0070282 pyridoxine binding obo:GO_0070294 A renal system process in which sodium ions are taken up from the collecting ducts and proximal and distal loops of the nephron. In non-mammalian species, absorption may occur in related structures. obo:GO_0070294 obo:go.owl obo:GO_0070294 nephron sodium ion absorption obo:GO_0070294 renal sodium ion reabsorption obo:GO_0070294 biological_process obo:GO_0070294 GO:0070294 obo:GO_0070294 renal sodium ion absorption obo:GO_0070296 The directed movement of calcium ions (Ca2+) into, out of or within the sarcoplasmic reticulum. obo:GO_0070296 obo:go.owl obo:GO_0070296 biological_process obo:GO_0070296 GO:0070296 obo:GO_0070296 sarcoplasmic reticulum calcium ion transport obo:GO_0070300 Interacting selectively and non-covalently with phosphatidic acid, any of a class of glycerol phosphate in which both the remaining hydroxyl groups of the glycerol moiety are esterified with fatty acids. obo:GO_0070300 obo:go.owl obo:GO_0070300 phosphatidate binding obo:GO_0070300 molecular_function obo:GO_0070300 GO:0070300 obo:GO_0070300 phosphatidic acid binding obo:GO_0070324 Interacting selectively and non-covalently with thyroxine (T4) or triiodothyronine (T3), tyrosine-based hormones produced by the thyroid gland. obo:GO_0070324 obo:go.owl obo:GO_0070324 thyroxine binding obo:GO_0070324 triiodothyronine binding obo:GO_0070324 molecular_function obo:GO_0070324 GO:0070324 obo:GO_0070324 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0070324 thyroid hormone binding obo:GO_0070325 Interacting selectively and non-covalently with a lipoprotein particle receptor. obo:GO_0070325 obo:go.owl obo:GO_0070325 molecular_function obo:GO_0070325 GO:0070325 obo:GO_0070325 lipoprotein particle receptor binding obo:GO_0070326 Interacting selectively and non-covalently with a very-low-density lipoprotein receptor. obo:GO_0070326 obo:go.owl obo:GO_0070326 VLDL receptor binding obo:GO_0070326 VLDLR binding obo:GO_0070326 very-low-density lipoprotein receptor binding obo:GO_0070326 molecular_function obo:GO_0070326 apolipoprotein E receptor binding obo:GO_0070326 GO:0070326 obo:GO_0070326 very-low-density lipoprotein particle receptor binding obo:GO_0070335 Interacting selectively and non-covalently with aspartate, the alpha-amino-acid anion of 2-aminobutanedioic acid that has formula C4H5NO4. obo:GO_0070335 obo:go.owl obo:GO_0070335 aspartic acid binding obo:GO_0070335 molecular_function obo:GO_0070335 GO:0070335 obo:GO_0070335 aspartate binding obo:GO_0070336 Interacting selectively and non-covalently with a flap structure in DNA. A DNA flap structure is one in which a single-stranded length of DNA or RNA protrudes from a double-stranded DNA molecule. obo:GO_0070336 obo:go.owl obo:GO_0070336 molecular_function obo:GO_0070336 GO:0070336 obo:GO_0070336 flap-structured DNA binding obo:GO_0070337 Interacting selectively and non-covalently with a 3'-flap structure in DNA. A DNA flap structure is one in which a single-stranded 3'-end of DNA or RNA protrudes from a double-stranded DNA molecule. obo:GO_0070337 obo:go.owl obo:GO_0070337 molecular_function obo:GO_0070337 GO:0070337 obo:GO_0070337 3'-flap-structured DNA binding obo:GO_0070338 Interacting selectively and non-covalently with a 5'-flap structure in DNA. A DNA flap structure is one in which a single-stranded 5'-end of DNA or RNA protrudes from a double-stranded DNA molecule. 5'-flap structures can be formed during DNA repair or lagging strand synthesis; in the latter case RNA flaps form from lagging strand RNA primers. obo:GO_0070338 obo:go.owl obo:GO_0070338 molecular_function obo:GO_0070338 GO:0070338 obo:GO_0070338 5'-flap-structured DNA binding obo:GO_0070339 Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a bacterial lipopeptide stimulus. obo:GO_0070339 obo:go.owl obo:GO_0070339 biological_process obo:GO_0070339 GO:0070339 obo:GO_0070339 response to bacterial lipopeptide obo:GO_0070340 The series of events in which a bacterial lipopeptide stimulus is received by a cell and converted into a molecular signal. obo:GO_0070340 obo:go.owl obo:GO_0070340 biological_process obo:GO_0070340 GO:0070340 obo:GO_0070340 detection of bacterial lipopeptide obo:GO_0070344 Any process that modulates the frequency, rate or extent of fat cell proliferation. obo:GO_0070344 obo:go.owl obo:GO_0070344 regulation of adipocyte proliferation obo:GO_0070344 regulation of adipose cell proliferation obo:GO_0070344 biological_process obo:GO_0070344 GO:0070344 obo:GO_0070344 regulation of fat cell proliferation obo:GO_0070345 Any process that stops or decreases the rate or extent of fat cell proliferation. obo:GO_0070345 obo:go.owl obo:GO_0070345 down regulation of fat cell proliferation obo:GO_0070345 down-regulation of fat cell proliferation obo:GO_0070345 downregulation of fat cell proliferation obo:GO_0070345 negative regulation of adipocyte proliferation obo:GO_0070345 negative regulation of adipose cell proliferation obo:GO_0070345 inhibition of fat cell proliferation obo:GO_0070345 biological_process obo:GO_0070345 GO:0070345 obo:GO_0070345 negative regulation of fat cell proliferation obo:GO_0070346 Any process that activates or increases the rate or extent of fat cell proliferation. obo:GO_0070346 obo:go.owl obo:GO_0070346 positive regulation of adipocyte proliferation obo:GO_0070346 positive regulation of adipose cell proliferation obo:GO_0070346 up regulation of fat cell proliferation obo:GO_0070346 up-regulation of fat cell proliferation obo:GO_0070346 upregulation of fat cell proliferation obo:GO_0070346 activation of fat cell proliferation obo:GO_0070346 stimulation of fat cell proliferation obo:GO_0070346 biological_process obo:GO_0070346 GO:0070346 obo:GO_0070346 positive regulation of fat cell proliferation obo:GO_0070347 Any process that modulates the frequency, rate or extent of brown fat cell proliferation. obo:GO_0070347 obo:go.owl obo:GO_0070347 regulation of brown adipocyte proliferation obo:GO_0070347 regulation of brown adipose cell proliferation obo:GO_0070347 biological_process obo:GO_0070347 GO:0070347 obo:GO_0070347 regulation of brown fat cell proliferation obo:GO_0070348 Any process that stops or decreases the rate or extent of brown fat cell proliferation. obo:GO_0070348 obo:go.owl obo:GO_0070348 down regulation of brown fat cell proliferation obo:GO_0070348 down-regulation of brown fat cell proliferation obo:GO_0070348 downregulation of brown fat cell proliferation obo:GO_0070348 negative regulation of brown adipocyte proliferation obo:GO_0070348 negative regulation of brown adipose cell proliferation obo:GO_0070348 inhibition of brown fat cell proliferation obo:GO_0070348 biological_process obo:GO_0070348 GO:0070348 obo:GO_0070348 negative regulation of brown fat cell proliferation obo:GO_0070349 Any process that activates or increases the rate or extent of brown fat cell proliferation. obo:GO_0070349 obo:go.owl obo:GO_0070349 positive regulation of brown adipocyte proliferation obo:GO_0070349 positive regulation of brown adipose cell proliferation obo:GO_0070349 up regulation of brown fat cell proliferation obo:GO_0070349 up-regulation of brown fat cell proliferation obo:GO_0070349 upregulation of brown fat cell proliferation obo:GO_0070349 activation of brown fat cell proliferation obo:GO_0070349 stimulation of brown fat cell proliferation obo:GO_0070349 biological_process obo:GO_0070349 GO:0070349 obo:GO_0070349 positive regulation of brown fat cell proliferation obo:GO_0070350 Any process that modulates the frequency, rate or extent of white fat cell proliferation. obo:GO_0070350 obo:go.owl obo:GO_0070350 regulation of white adipocyte proliferation obo:GO_0070350 regulation of white adipose cell proliferation obo:GO_0070350 biological_process obo:GO_0070350 GO:0070350 obo:GO_0070350 regulation of white fat cell proliferation obo:GO_0070351 Any process that stops or decreases the rate or extent of white fat cell proliferation. obo:GO_0070351 obo:go.owl obo:GO_0070351 down regulation of white fat cell proliferation obo:GO_0070351 down-regulation of white fat cell proliferation obo:GO_0070351 downregulation of white fat cell proliferation obo:GO_0070351 negative regulation of white adipocyte proliferation obo:GO_0070351 negative regulation of white adipose cell proliferation obo:GO_0070351 inhibition of white fat cell proliferation obo:GO_0070351 biological_process obo:GO_0070351 GO:0070351 obo:GO_0070351 negative regulation of white fat cell proliferation obo:GO_0070352 Any process that activates or increases the rate or extent of white fat cell proliferation. obo:GO_0070352 obo:go.owl obo:GO_0070352 positive regulation of white adipocyte proliferation obo:GO_0070352 positive regulation of white adipose cell proliferation obo:GO_0070352 up regulation of white fat cell proliferation obo:GO_0070352 up-regulation of white fat cell proliferation obo:GO_0070352 upregulation of white fat cell proliferation obo:GO_0070352 activation of white fat cell proliferation obo:GO_0070352 stimulation of white fat cell proliferation obo:GO_0070352 biological_process obo:GO_0070352 GO:0070352 obo:GO_0070352 positive regulation of white fat cell proliferation obo:GO_0070379 Interacting selectively and non-covalently with high mobility group box 1 (HMBGB1). obo:GO_0070379 obo:go.owl obo:GO_0070379 HMGB1 binding obo:GO_0070379 molecular_function obo:GO_0070379 GO:0070379 obo:GO_0070379 high mobility group box 1 binding obo:GO_0070391 Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a lipoteichoic acid stimulus; lipoteichoic acid is a major component of the cell wall of gram-positive bacteria and typically consists of a chain of glycerol-phosphate repeating units linked to a glycolipid anchor. obo:GO_0070391 obo:go.owl obo:GO_0070391 response to LTA obo:GO_0070391 biological_process obo:GO_0070391 GO:0070391 obo:GO_0070391 response to lipoteichoic acid obo:GO_0070392 The series of events in which a lipoteichoic acid stimulus is received by a cell and converted into a molecular signal; lipoteichoic acid is a major component of the cell wall of gram-positive bacteria and typically consists of a chain of glycerol-phosphate repeating units linked to a glycolipid anchor. obo:GO_0070392 obo:go.owl obo:GO_0070392 detection of LTA obo:GO_0070392 biological_process obo:GO_0070392 GO:0070392 obo:GO_0070392 detection of lipoteichoic acid obo:GO_0070401 Interacting selectively and non-covalently with the oxidized form, NADP+, of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions. obo:GO_0070401 obo:go.owl obo:GO_0070401 NADP (oxidized) binding obo:GO_0070401 oxidized NADP binding obo:GO_0070401 oxidized nicotinamide adenine dinucleotide phosphate binding obo:GO_0070401 molecular_function obo:GO_0070401 NADP binding obo:GO_0070401 GO:0070401 obo:GO_0070401 NADP+ binding obo:GO_0070402 Interacting selectively and non-covalently with the reduced form, NADPH, of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions. obo:GO_0070402 obo:go.owl obo:GO_0070402 NADP (reduced) binding obo:GO_0070402 reduced NADP binding obo:GO_0070402 reduced nicotinamide adenine dinucleotide phosphate binding obo:GO_0070402 molecular_function obo:GO_0070402 GO:0070402 obo:GO_0070402 NADPH binding obo:GO_0070403 Interacting selectively and non-covalently with the oxidized form, NAD, of nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions. obo:GO_0070403 obo:go.owl obo:GO_0070403 NAD (oxidized) binding obo:GO_0070403 oxidized NAD binding obo:GO_0070403 oxidized nicotinamide adenine dinucleotide binding obo:GO_0070403 molecular_function obo:GO_0070403 NAD binding obo:GO_0070403 GO:0070403 obo:GO_0070403 NAD+ binding obo:GO_0070404 Interacting selectively and non-covalently with the reduced form, NADH, of nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions. obo:GO_0070404 obo:go.owl obo:GO_0070404 NAD (reduced) binding obo:GO_0070404 reduced NAD binding obo:GO_0070404 reduced nicotinamide adenine dinucleotide binding obo:GO_0070404 molecular_function obo:GO_0070404 GO:0070404 obo:GO_0070404 NADH binding obo:GO_0070405 Interacting selectively and non-covalently with ammonium ions (NH4+). obo:GO_0070405 obo:go.owl obo:GO_0070405 molecular_function obo:GO_0070405 ammonium binding obo:GO_0070405 GO:0070405 obo:GO_0070405 ammonium ion binding obo:GO_0070406 Interacting selectively and non-covalently with glutamine, 2,5-diamino-5-oxopentanoic acid. obo:GO_0070406 obo:go.owl obo:GO_0070406 molecular_function obo:GO_0070406 GO:0070406 obo:GO_0070406 glutamine binding obo:GO_0070410 Interacting selectively and non-covalently with a common mediator SMAD signaling protein. obo:GO_0070410 obo:go.owl obo:GO_0070410 common mediator SMAD binding obo:GO_0070410 common partner SMAD binding obo:GO_0070410 common-mediator SMAD binding obo:GO_0070410 common-partner SMAD binding obo:GO_0070410 molecular_function obo:GO_0070410 GO:0070410 obo:GO_0070410 co-SMAD binding obo:GO_0070411 Interacting selectively and non-covalently with an inhibitory SMAD signaling protein. obo:GO_0070411 obo:go.owl obo:GO_0070411 molecular_function obo:GO_0070411 GO:0070411 obo:GO_0070411 I-SMAD binding obo:GO_0070412 Interacting selectively and non-covalently with a receptor-regulated SMAD signaling protein. obo:GO_0070412 obo:go.owl obo:GO_0070412 pathway restricted SMAD binding obo:GO_0070412 pathway-restricted SMAD binding obo:GO_0070412 receptor regulated SMAD binding obo:GO_0070412 receptor-regulated SMAD binding obo:GO_0070412 molecular_function obo:GO_0070412 GO:0070412 obo:GO_0070412 R-SMAD binding obo:GO_0070413 The chemical reactions and pathways involving trehalose that occur as a result of a stimulus indicating the organism is under stress. obo:GO_0070413 obo:go.owl obo:GO_0070413 trehalose metabolic process involved in response to stress obo:GO_0070413 biological_process obo:GO_0070413 GO:0070413 obo:GO_0070413 trehalose metabolism in response to stress obo:GO_0070417 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cold stimulus, a temperature stimulus below the optimal temperature for that organism. obo:GO_0070417 obo:go.owl obo:GO_0070417 cellular response to cold stress obo:GO_0070417 biological_process obo:GO_0070417 GO:0070417 obo:GO_0070417 cellular response to cold obo:GO_0070482 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus reflecting the presence, absence, or concentration of oxygen. obo:GO_0070482 obo:go.owl obo:GO_0070482 biological_process obo:GO_0070482 GO:0070482 obo:GO_0070482 response to oxygen levels obo:GO_0070483 The series of events in which a stimulus indicating lowered oxygen tension is received by a cell and converted into a molecular signal. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level. obo:GO_0070483 obo:go.owl obo:GO_0070483 detection of reduced oxygen levels obo:GO_0070483 biological_process obo:GO_0070483 GO:0070483 obo:GO_0070483 detection of hypoxia obo:GO_0070491 Interacting selectively and non-covalently with a transcription repressor, any protein whose activity is required to prevent or downregulate transcription. obo:GO_0070491 obo:go.owl obo:GO_0070491 molecular_function obo:GO_0070491 GO:0070491 obo:GO_0070491 repressing transcription factor binding obo:GO_0070492 Interacting selectively and non-covalently with any oligosaccharide, a molecule with between two and (about) 20 monosaccharide residues connected by glycosidic linkages. obo:GO_0070492 obo:go.owl obo:GO_0070492 molecular_function obo:GO_0070492 GO:0070492 obo:GO_0070492 oligosaccharide binding obo:GO_0070509 The directed movement of calcium ions into a cell or organelle. obo:GO_0070509 obo:go.owl obo:GO_0070509 calcium ion uptake obo:GO_0070509 biological_process obo:GO_0070509 transmembrane calcium influx obo:GO_0070509 GO:0070509 obo:GO_0070509 calcium ion import obo:GO_0070513 Interacting selectively and non-covalently with a death domain of a protein. The death domain (DD) is a homotypic protein interaction module composed of a bundle of six alpha-helices. DD bind each other forming oligomers. Some DD-containing proteins are involved in the regulation of apoptosis and inflammation through their activation of caspases and NF-kappaB. obo:GO_0070513 obo:go.owl obo:GO_0070513 molecular_function obo:GO_0070513 GO:0070513 obo:GO_0070513 For binding to the death effector domain, consider instead the term 'death effector domain binding ; GO:0035877'. obo:GO_0070513 death domain binding obo:GO_0070530 Interacting selectively and non-covalently with a protein upon poly-ubiquitination formed by linkages between lysine residues at position 63 in the target protein. obo:GO_0070530 obo:go.owl obo:GO_0070530 molecular_function obo:GO_0070530 GO:0070530 obo:GO_0070530 K63-linked polyubiquitin modification-dependent protein binding obo:GO_0070538 Interacting selectively and non-covalently with oleic acid, the 18-carbon monounsaturated fatty acid (9Z)-octadec-9-enoic acid. obo:GO_0070538 obo:go.owl obo:GO_0070538 molecular_function obo:GO_0070538 GO:0070538 obo:GO_0070538 oleic acid binding obo:GO_0070539 Interacting selectively and non-covalently with linoleic acid, the 18-carbon unsaturated fatty acid (9Z,12Z)-octadeca-9,12-dienoic acid. obo:GO_0070539 obo:go.owl obo:GO_0070539 molecular_function obo:GO_0070539 GO:0070539 obo:GO_0070539 linoleic acid binding obo:GO_0070540 Interacting selectively and non-covalently with stearic acid, the 18-carbon saturated fatty acid octadecanoic acid. obo:GO_0070540 obo:go.owl obo:GO_0070540 molecular_function obo:GO_0070540 GO:0070540 obo:GO_0070540 stearic acid binding obo:GO_0070569 Catalysis of the transfer of an uridylyl group to an acceptor. obo:GO_0070569 obo:go.owl obo:GO_0070569 midori obo:GO_0070569 2009-04-15T11:06:07Z obo:GO_0070569 uridyl transferase activity obo:GO_0070569 uridyltransferase activity obo:GO_0070569 molecular_function obo:GO_0070569 GO:0070569 obo:GO_0070569 uridylyltransferase activity obo:GO_0070574 A process in which a cadmium ion is transported from one side of a membrane to the other by means of some agent such as a transporter or pore. obo:GO_0070574 obo:go.owl obo:GO_0070574 midori obo:GO_0070574 2009-04-20T03:31:47Z obo:GO_0070574 cadmium ion membrane transport obo:GO_0070574 transmembrane cadmium transport obo:GO_0070574 biological_process obo:GO_0070574 GO:0070574 obo:GO_0070574 Note that this term is not intended for use in annotating lateral movement within membranes. obo:GO_0070574 cadmium ion transmembrane transport obo:GO_0070577 Interacting selectively and non-covalently with a histone in which a lysine residue has been modified by acetylation. obo:GO_0070577 obo:go.owl obo:GO_0070577 midori obo:GO_0070577 2009-04-21T03:03:35Z obo:GO_0070577 acetylated histone residue binding obo:GO_0070577 molecular_function obo:GO_0070577 GO:0070577 obo:GO_0070577 lysine-acetylated histone binding obo:GO_0070588 A process in which a calcium ion is transported from one side of a membrane to the other by means of some agent such as a transporter or pore. obo:GO_0070588 obo:go.owl obo:GO_0070588 midori obo:GO_0070588 2009-04-28T10:44:09Z obo:GO_0070588 calcium ion membrane transport obo:GO_0070588 transmembrane calcium transport obo:GO_0070588 biological_process obo:GO_0070588 GO:0070588 obo:GO_0070588 Note that this term is not intended for use in annotating lateral movement within membranes. obo:GO_0070588 calcium ion transmembrane transport obo:GO_0070594 Interacting selectively and non-covalently with the juvenile hormone response element (JHRE), a conserved sequence found in the promoters of genes whose expression is regulated in response to juvenile hormone. obo:GO_0070594 obo:go.owl obo:GO_0070594 midori obo:GO_0070594 2009-04-28T03:31:27Z obo:GO_0070594 JHRE binding obo:GO_0070594 molecular_function obo:GO_0070594 GO:0070594 obo:GO_0070594 Note that as agreed during the transcription overhaul, terms specifying binding to specific transcription regulatory motifs are no longer being created. The level of specificity GO has decided to go to is the "core promoter", "core promoter proximal region" and "enhancer". To capture more detail, please consider using column 16. obo:GO_0070594 juvenile hormone response element binding obo:GO_0070628 Interacting selectively and non-covalently with a proteasome, a large multisubunit protein complex that catalyzes protein degradation. obo:GO_0070628 obo:go.owl obo:GO_0070628 midori obo:GO_0070628 2009-05-01T04:38:58Z obo:GO_0070628 molecular_function obo:GO_0070628 GO:0070628 obo:GO_0070628 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0070628 proteasome binding obo:GO_0070644 Interacting selectively and non-covalently with the vitamin D response element (VDRE), a short sequence with dyad symmetry found in the promoters of some of the cellular immediate-early genes, regulated by serum. obo:GO_0070644 obo:go.owl obo:GO_0070644 midori obo:GO_0070644 2009-05-08T04:23:44Z obo:GO_0070644 VDRE binding obo:GO_0070644 molecular_function obo:GO_0070644 GO:0070644 obo:GO_0070644 Note that as agreed during the transcription overhaul, terms specifying binding to specific transcription regulatory motifs are no longer being created. The level of specificity GO has decided to go to is the "core promoter", "core promoter proximal region" and "enhancer". To capture more detail, please consider using column 16. obo:GO_0070644 vitamin D response element binding obo:GO_0070653 Interacting selectively and non-covalently with a high-density lipoprotein receptor. obo:GO_0070653 obo:go.owl obo:GO_0070653 midori obo:GO_0070653 2009-05-28T03:44:33Z obo:GO_0070653 HDL receptor binding obo:GO_0070653 high-density lipoprotein receptor binding obo:GO_0070653 molecular_function obo:GO_0070653 GO:0070653 obo:GO_0070653 high-density lipoprotein particle receptor binding obo:GO_0070663 Any process that modulates the frequency, rate or extent of leukocyte proliferation. obo:GO_0070663 obo:go.owl obo:GO_0070663 midori obo:GO_0070663 2009-05-28T05:30:39Z obo:GO_0070663 biological_process obo:GO_0070663 GO:0070663 obo:GO_0070663 regulation of leukocyte proliferation obo:GO_0070664 Any process that stops, prevents, or reduces the frequency, rate or extent of leukocyte proliferation. obo:GO_0070664 obo:go.owl obo:GO_0070664 midori obo:GO_0070664 2009-05-28T05:34:50Z obo:GO_0070664 down regulation of leukocyte proliferation obo:GO_0070664 down-regulation of leukocyte proliferation obo:GO_0070664 downregulation of leukocyte proliferation obo:GO_0070664 inhibition of leukocyte proliferation obo:GO_0070664 biological_process obo:GO_0070664 GO:0070664 obo:GO_0070664 negative regulation of leukocyte proliferation obo:GO_0070665 Any process that activates or increases the frequency, rate or extent of leukocyte proliferation. obo:GO_0070665 obo:go.owl obo:GO_0070665 midori obo:GO_0070665 2009-05-28T05:36:46Z obo:GO_0070665 up regulation of leukocyte proliferation obo:GO_0070665 up-regulation of leukocyte proliferation obo:GO_0070665 upregulation of leukocyte proliferation obo:GO_0070665 activation of leukocyte proliferation obo:GO_0070665 stimulation of leukocyte proliferation obo:GO_0070665 biological_process obo:GO_0070665 GO:0070665 obo:GO_0070665 positive regulation of leukocyte proliferation obo:GO_0070666 Any process that modulates the frequency, rate or extent of mast cell proliferation. obo:GO_0070666 obo:go.owl obo:GO_0070666 midori obo:GO_0070666 2009-05-28T05:40:43Z obo:GO_0070666 biological_process obo:GO_0070666 GO:0070666 obo:GO_0070666 regulation of mast cell proliferation obo:GO_0070667 Any process that stops, prevents or reduces the rate or extent of mast cell proliferation. obo:GO_0070667 obo:go.owl obo:GO_0070667 midori obo:GO_0070667 2009-05-28T05:45:11Z obo:GO_0070667 down regulation of mast cell proliferation obo:GO_0070667 down-regulation of mast cell proliferation obo:GO_0070667 downregulation of mast cell proliferation obo:GO_0070667 inhibition of mast cell proliferation obo:GO_0070667 biological_process obo:GO_0070667 GO:0070667 obo:GO_0070667 negative regulation of mast cell proliferation obo:GO_0070668 Any process that activates or increases the rate or extent of mast cell proliferation. obo:GO_0070668 obo:go.owl obo:GO_0070668 midori obo:GO_0070668 2009-05-28T05:48:30Z obo:GO_0070668 up regulation of mast cell proliferation obo:GO_0070668 up-regulation of mast cell proliferation obo:GO_0070668 upregulation of mast cell proliferation obo:GO_0070668 activation of mast cell proliferation obo:GO_0070668 stimulation of mast cell proliferation obo:GO_0070668 biological_process obo:GO_0070668 GO:0070668 obo:GO_0070668 positive regulation of mast cell proliferation obo:GO_0070678 Interacting selectively and non-covalently with a preprotein, the unprocessed form of a protein destined to undergo co- or post-translational processing. obo:GO_0070678 obo:go.owl obo:GO_0070678 midori obo:GO_0070678 2009-05-29T03:41:54Z obo:GO_0070678 unprocessed protein binding obo:GO_0070678 molecular_function obo:GO_0070678 GO:0070678 obo:GO_0070678 preprotein binding obo:GO_0070679 Interacting selectively and non-covalently with inositol 1,4,5 trisphosphate. obo:GO_0070679 obo:go.owl obo:GO_0070679 midori obo:GO_0070679 2009-05-29T04:07:00Z obo:GO_0070679 IP3 binding obo:GO_0070679 InsP3 binding obo:GO_0070679 molecular_function obo:GO_0070679 GO:0070679 obo:GO_0070679 inositol 1,4,5 trisphosphate binding obo:GO_0070696 Interacting selectively and non-covalently with a receptor that spans a cell membrane and possesses protein serine/threonine kinase activity. obo:GO_0070696 obo:go.owl obo:GO_0070696 midori obo:GO_0070696 2009-06-04T03:57:42Z obo:GO_0070696 molecular_function obo:GO_0070696 GO:0070696 obo:GO_0070696 transmembrane receptor protein serine/threonine kinase binding obo:GO_0070697 Interacting selectively and non-covalently with an activin receptor. obo:GO_0070697 obo:go.owl obo:GO_0070697 midori obo:GO_0070697 2009-06-04T04:02:13Z obo:GO_0070697 molecular_function obo:GO_0070697 GO:0070697 obo:GO_0070697 activin receptor binding obo:GO_0070698 Interacting selectively and non-covalently with a type I activin receptor. obo:GO_0070698 obo:go.owl obo:GO_0070698 midori obo:GO_0070698 2009-06-04T04:15:21Z obo:GO_0070698 molecular_function obo:GO_0070698 GO:0070698 obo:GO_0070698 type I activin receptor binding obo:GO_0070699 Interacting selectively and non-covalently with a type II activin receptor. obo:GO_0070699 obo:go.owl obo:GO_0070699 midori obo:GO_0070699 2009-06-04T04:16:26Z obo:GO_0070699 molecular_function obo:GO_0070699 GO:0070699 obo:GO_0070699 type II activin receptor binding obo:GO_0070700 Interacting selectively and non-covalently with a BMP receptor. obo:GO_0070700 obo:go.owl obo:GO_0070700 midori obo:GO_0070700 2009-06-04T04:24:16Z obo:GO_0070700 bone morphogenetic protein receptor binding obo:GO_0070700 molecular_function obo:GO_0070700 GO:0070700 obo:GO_0070700 BMP receptor binding obo:GO_0070716 A mismatch repair process that corrects errors introduced that ensures the accuracy of DNA replication. obo:GO_0070716 obo:go.owl obo:GO_0070716 midori obo:GO_0070716 2009-06-09T04:00:29Z obo:GO_0070716 biological_process obo:GO_0070716 mismatch repair involved in maintenance of fidelity during DNA-dependent DNA replication obo:GO_0070716 GO:0070716 obo:GO_0070716 mismatch repair involved in maintenance of fidelity involved in DNA-dependent DNA replication obo:GO_0070717 Interacting selectively and non-covalently with any stretch of purines (adenine or guanine) in an RNA molecule. obo:GO_0070717 obo:go.owl obo:GO_0070717 midori obo:GO_0070717 2009-06-10T03:32:15Z obo:GO_0070717 molecular_function obo:GO_0070717 GO:0070717 obo:GO_0070717 poly-purine tract binding obo:GO_0070728 Interacting selectively and non-covalently with 2-amino-4-methylpentanoic acid. obo:GO_0070728 obo:go.owl obo:GO_0070728 midori obo:GO_0070728 2009-06-17T03:16:30Z obo:GO_0070728 Leu binding obo:GO_0070728 molecular_function obo:GO_0070728 GO:0070728 obo:GO_0070728 leucine binding obo:GO_0070730 The directed movement of cyclic AMP (cAMP), into, out of or within a cell. obo:GO_0070730 obo:go.owl obo:GO_0070730 midori obo:GO_0070730 2009-06-17T03:53:45Z obo:GO_0070730 cyclic AMP transport obo:GO_0070730 biological_process obo:GO_0070730 GO:0070730 obo:GO_0070730 cAMP transport obo:GO_0070731 The directed movement of cyclic GMP (cGMP), into, out of or within a cell. obo:GO_0070731 obo:go.owl obo:GO_0070731 midori obo:GO_0070731 2009-06-17T04:40:27Z obo:GO_0070731 cyclic GMP transport obo:GO_0070731 biological_process obo:GO_0070731 GO:0070731 obo:GO_0070731 cGMP transport obo:GO_0070742 Interacting selectively and non-covalently with a C2H2-type zinc finger domain of a protein. The C2H2 zinc finger is the classical zinc finger domain, in which two conserved cysteines and histidines co-ordinate a zinc ion. obo:GO_0070742 obo:go.owl obo:GO_0070742 midori obo:GO_0070742 2009-06-23T11:26:02Z obo:GO_0070742 molecular_function obo:GO_0070742 GO:0070742 obo:GO_0070742 C2H2 zinc finger domain binding obo:GO_0070746 Interacting selectively and non-covalently with interleukin-35. obo:GO_0070746 obo:go.owl obo:GO_0070746 midori obo:GO_0070746 2009-06-23T01:15:36Z obo:GO_0070746 IL-35 binding obo:GO_0070746 molecular_function obo:GO_0070746 GO:0070746 obo:GO_0070746 interleukin-35 binding obo:GO_0070748 Interacting selectively and non-covalently with the interleukin-35 receptor. obo:GO_0070748 obo:go.owl obo:GO_0070748 midori obo:GO_0070748 2009-06-23T01:21:54Z obo:GO_0070748 IL-35 obo:GO_0070748 interleukin-35 receptor ligand obo:GO_0070748 molecular_function obo:GO_0070748 GO:0070748 obo:GO_0070748 interleukin-35 receptor binding obo:GO_0070838 The directed movement of divalent metal cations, any metal ion with a +2 electric charge, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0070838 obo:go.owl obo:GO_0070838 midori obo:GO_0070838 2009-07-31T01:02:39Z obo:GO_0070838 biological_process obo:GO_0070838 GO:0070838 obo:GO_0070838 divalent metal ion transport obo:GO_0070839 The directed movement of divalent metal cations, any metal ion with a +2 electric charge, out of a cell or organelle. obo:GO_0070839 obo:go.owl obo:GO_0070839 midori obo:GO_0070839 2009-07-31T01:07:46Z obo:GO_0070839 biological_process obo:GO_0070839 GO:0070839 obo:GO_0070839 divalent metal ion export obo:GO_0070840 Interacting selectively and non-covalently with a dynein complex, a protein complex that contains two or three dynein heavy chains and several light chains, and has microtubule motor activity. obo:GO_0070840 obo:go.owl obo:GO_0070840 midori obo:GO_0070840 2009-07-31T01:22:47Z obo:GO_0070840 GO:0045502 obo:GO_0070840 molecular_function obo:GO_0070840 dynein binding obo:GO_0070840 GO:0070840 obo:GO_0070840 dynein complex binding obo:GO_0070851 Interacting selectively and non-covalently with a growth factor receptor. obo:GO_0070851 obo:go.owl obo:GO_0070851 midori obo:GO_0070851 2009-08-07T11:23:02Z obo:GO_0070851 molecular_function obo:GO_0070851 GO:0070851 obo:GO_0070851 growth factor receptor binding obo:GO_0070853 Interacting selectively and non-covalently with a class VI myosin. The myosin VI heavy chain has a single IQ motif in the neck and a tail region with a coiled coil domain followed by a unique globular domain, a unique insertion that enables myosin VI to move towards the pointed or minus end of actin filaments. obo:GO_0070853 obo:go.owl obo:GO_0070853 midori obo:GO_0070853 2009-08-13T01:28:36Z obo:GO_0070853 molecular_function obo:GO_0070853 GO:0070853 obo:GO_0070853 myosin VI binding obo:GO_0070854 Interacting selectively and non-covalently with a heavy chain of a myosin VI complex. obo:GO_0070854 obo:go.owl obo:GO_0070854 midori obo:GO_0070854 2009-08-13T01:44:05Z obo:GO_0070854 molecular_function obo:GO_0070854 GO:0070854 obo:GO_0070854 myosin VI heavy chain binding obo:GO_0070855 Interacting selectively and non-covalently with the head/neck region of a myosin VI heavy chain. obo:GO_0070855 obo:go.owl obo:GO_0070855 midori obo:GO_0070855 2009-08-13T01:45:08Z obo:GO_0070855 molecular_function obo:GO_0070855 GO:0070855 obo:GO_0070855 myosin VI head/neck binding obo:GO_0070856 Interacting selectively and non-covalently with a light chain of a myosin VI complex. obo:GO_0070856 obo:go.owl obo:GO_0070856 midori obo:GO_0070856 2009-08-13T01:46:13Z obo:GO_0070856 molecular_function obo:GO_0070856 GO:0070856 obo:GO_0070856 myosin VI light chain binding obo:GO_0070866 Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules) in the presence of sterols. obo:GO_0070866 obo:go.owl obo:GO_0070866 midori obo:GO_0070866 2009-08-19T01:43:35Z obo:GO_0070866 molecular_function obo:GO_0070866 GO:0070866 obo:GO_0070866 sterol-dependent protein binding obo:GO_0070878 Interacting selectively and non-covalently with a primary microRNA (pri-miRNA) transcript, an RNA molecule that is processed into a short hairpin-shaped structure called a pre-miRNA and finally into a functional miRNA. Both double-stranded and single-stranded regions of a pri-miRNA are required for binding. obo:GO_0070878 obo:go.owl obo:GO_0070878 midori obo:GO_0070878 2009-08-20T04:11:36Z obo:GO_0070878 pri-miRNA binding obo:GO_0070878 primary microRNA binding obo:GO_0070878 molecular_function obo:GO_0070878 GO:0070878 obo:GO_0070878 primary miRNA binding obo:GO_0070883 Interacting selectively and non-covalently with a precursor microRNA (pre-miRNA) transcript, a stem-loop-containing precursor of microRNA. obo:GO_0070883 obo:go.owl obo:GO_0070883 midori obo:GO_0070883 2009-08-24T04:36:24Z obo:GO_0070883 pre-microRNA binding obo:GO_0070883 precursor microRNA binding obo:GO_0070883 molecular_function obo:GO_0070883 GO:0070883 obo:GO_0070883 pre-miRNA binding obo:GO_0070887 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a chemical stimulus. obo:GO_0070887 obo:go.owl obo:GO_0070887 midori obo:GO_0070887 2009-08-27T04:41:45Z obo:GO_0070887 biological_process obo:GO_0070887 GO:0070887 obo:GO_0070887 http://purl.oboInOwllibrary.org/oboInOwl/go#gocheck_do_not_manually_annotate obo:GO_0070887 Note that this term is in the subset of terms that should not be used for direct gene product annotation. Instead, select a child term or, if no appropriate child term exists, please request a new term. Direct annotations to this term may be amended during annotation QC. obo:GO_0070887 cellular response to chemical stimulus obo:GO_0070888 Interacting selectively and non-covalently with an E-box, a DNA motif with the consensus sequence CANNTG that is found in the promoters of a wide array of genes expressed in neurons, muscle and other tissues. obo:GO_0070888 obo:go.owl obo:GO_0070888 midori obo:GO_0070888 2009-08-28T10:37:01Z obo:GO_0070888 E-box promoter binding obo:GO_0070888 molecular_function obo:GO_0070888 GO:0070888 obo:GO_0070888 Note that as agreed during the transcription overhaul, terms specifying binding to specific transcription regulatory motifs are no longer being created. The level of specificity GO has decided to go to is the "core promoter", "core promoter proximal region" and "enhancer". To capture more detail, please consider using column 16. obo:GO_0070888 E-box binding obo:GO_0070891 Interacting selectively and non-covalently with lipoteichoic acid. obo:GO_0070891 obo:go.owl obo:GO_0070891 midori obo:GO_0070891 2009-09-01T02:56:36Z obo:GO_0070891 molecular_function obo:GO_0070891 GO:0070891 obo:GO_0070891 lipoteichoic acid binding obo:GO_0070905 Interacting selectively and non-covalently with 2-amino-3-hydroxypropanoic acid. obo:GO_0070905 obo:go.owl obo:GO_0070905 midori obo:GO_0070905 2009-09-04T03:28:29Z obo:GO_0070905 Ser binding obo:GO_0070905 molecular_function obo:GO_0070905 GO:0070905 obo:GO_0070905 serine binding obo:GO_0070911 The nucleotide-excision repair process in which DNA lesions are removed from nontranscribed strands and from transcriptionally silent regions over the entire genome. obo:GO_0070911 obo:go.owl obo:GO_0070911 midori obo:GO_0070911 2009-09-09T03:13:11Z obo:GO_0070911 GG-NER obo:GO_0070911 GGR obo:GO_0070911 global genome NER obo:GO_0070911 global genomic nucleotide-excision repair obo:GO_0070911 global genomic repair obo:GO_0070911 biological_process obo:GO_0070911 GO:0070911 obo:GO_0070911 global genome nucleotide-excision repair obo:GO_0070914 A DNA repair process that is initiated by an endonuclease that introduces a single-strand incision immediately 5' of a UV-induced damage site. UV-damage excision repair acts on both cyclobutane pyrimidine dimers (CPDs) and pyrimidine-pyrimidone 6-4 photoproducts (6-4PPs). obo:GO_0070914 obo:go.owl obo:GO_0070914 midori obo:GO_0070914 2009-09-10T03:14:06Z obo:GO_0070914 UV-damaged DNA endonuclease-dependent excision repair obo:GO_0070914 UVDE-dependent excision repair obo:GO_0070914 UVER obo:GO_0070914 biological_process obo:GO_0070914 AER obo:GO_0070914 alternative excision repair obo:GO_0070914 GO:0070914 obo:GO_0070914 UV-damage excision repair obo:GO_0070967 Interacting selectively and non-covalently with F420, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. obo:GO_0070967 obo:go.owl obo:GO_0070967 midori obo:GO_0070967 2009-10-02T11:33:26Z obo:GO_0070967 molecular_function obo:GO_0070967 GO:0070967 obo:GO_0070967 coenzyme F420 binding obo:GO_0070968 Interacting selectively and non-covalently with pyrroloquinoline quinone, PQQ, the coenzyme or the prosthetic group of certain alcohol dehydrogenases and glucose dehydrogenases. obo:GO_0070968 obo:go.owl obo:GO_0070968 midori obo:GO_0070968 2009-10-02T11:39:13Z obo:GO_0070968 PQQ binding obo:GO_0070968 molecular_function obo:GO_0070968 GO:0070968 obo:GO_0070968 pyrroloquinoline quinone binding obo:GO_0070974 Interacting selectively and non-covalently with a POU domain of a protein. The POU domain is a bipartite DNA binding domain composed of two subunits separated by a non-conserved region of 15-55 amino acids; it is found in several eukaryotic transcription factors. obo:GO_0070974 obo:go.owl obo:GO_0070974 midori obo:GO_0070974 2009-10-02T12:53:02Z obo:GO_0070974 molecular_function obo:GO_0070974 GO:0070974 obo:GO_0070974 POU domain binding obo:GO_0070975 Interacting selectively and non-covalently with a FHA domain of a protein. The FHA domain is a phosphopeptide recognition domain found in many regulatory proteins, and consists of approximately 80-100 amino acid residues folded into an 11-stranded beta sandwich. obo:GO_0070975 obo:go.owl obo:GO_0070975 midori obo:GO_0070975 2009-10-02T01:09:20Z obo:GO_0070975 Forkhead-associated domain binding obo:GO_0070975 molecular_function obo:GO_0070975 GO:0070975 obo:GO_0070975 FHA domain binding obo:GO_0070976 Interacting selectively and non-covalently with a Toll-Interleukin receptor (TIR) domain of a protein. The TIR domain is an intracellular 200 residue domain that is found in the Toll protein, the interleukin-1 receptor (IL-1R), and MyD88; it contains three highly-conserved regions, and mediates protein-protein interactions between the Toll-like receptors (TLRs) and signal-transduction components. obo:GO_0070976 obo:go.owl obo:GO_0070976 midori obo:GO_0070976 2009-10-02T01:17:29Z obo:GO_0070976 Toll-Interleukin receptor domain binding obo:GO_0070976 molecular_function obo:GO_0070976 GO:0070976 obo:GO_0070976 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_chembl obo:GO_0070976 TIR domain binding obo:GO_0070984 Interacting selectively and non-covalently with a SET domain of a protein. SET domains are named after three Drosophila proteins that contain this domain: Su(var), E(z) and trithorax. SET domains are associated with histone lysine methylation. obo:GO_0070984 obo:go.owl obo:GO_0070984 midori obo:GO_0070984 2009-10-27T04:09:28Z obo:GO_0070984 SET binding obo:GO_0070984 molecular_function obo:GO_0070984 GO:0070984 obo:GO_0070984 SET domain binding obo:GO_0070987 The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA after replication by using a specialized DNA polymerase or replication complex to insert a defined nucleotide across the lesion. This process does not remove the replication-blocking lesions but does not causes an increase in the endogenous mutation level. For S. cerevisiae, RAD30 encodes DNA polymerase eta, which incorporates two adenines. When incorporated across a thymine-thymine dimer, it does not increase the endogenous mutation level. obo:GO_0070987 obo:go.owl obo:GO_0070987 midori obo:GO_0070987 2009-10-29T02:45:42Z obo:GO_0070987 biological_process obo:GO_0070987 GO:0070987 obo:GO_0070987 Note that 'error-free' does not mean that literally zero errors occur during DNA synthesis, but that the error rate is low, comparable to that of DNA synthesis during replication. obo:GO_0070987 error-free translesion synthesis obo:GO_0070990 Interacting selectively and non-covalently with any part of a small nuclear ribonucleoprotein particle. obo:GO_0070990 obo:go.owl obo:GO_0070990 midori obo:GO_0070990 2009-10-29T03:54:25Z obo:GO_0070990 molecular_function obo:GO_0070990 GO:0070990 obo:GO_0070990 snRNP binding obo:GO_0070994 The series of events in which a stimulus indicating oxidative stress is received and converted into a molecular signal. obo:GO_0070994 obo:go.owl obo:GO_0070994 midori obo:GO_0070994 2009-10-30T02:54:35Z obo:GO_0070994 biological_process obo:GO_0070994 GO:0070994 obo:GO_0070994 detection of oxidative stress obo:GO_0070996 Interacting selectively and non-covalently with a type 1 melanocortin receptor. obo:GO_0070996 obo:go.owl obo:GO_0070996 midori obo:GO_0070996 2009-11-03T01:50:53Z obo:GO_0070996 type 1 melanocortin receptor ligand obo:GO_0070996 molecular_function obo:GO_0070996 GO:0070996 obo:GO_0070996 type 1 melanocortin receptor binding obo:GO_0071000 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a magnetic stimulus. obo:GO_0071000 obo:go.owl obo:GO_0071000 midori obo:GO_0071000 2009-11-04T12:02:03Z obo:GO_0071000 response to magnetic stimulus obo:GO_0071000 biological_process obo:GO_0071000 GO:0071000 obo:GO_0071000 response to magnetism obo:GO_0071074 Interacting selectively and non-covalently with eukaryotic initiation factor eIF2, a protein complex involved in the initiation of ribosome-mediated translation. obo:GO_0071074 obo:go.owl obo:GO_0071074 midori obo:GO_0071074 2009-11-06T01:39:02Z obo:GO_0071074 molecular_function obo:GO_0071074 GO:0071074 obo:GO_0071074 eukaryotic initiation factor eIF2 binding obo:GO_0071207 Interacting selectively and non-covalently with a conserved stem-loop structure found in histone pre-mRNAs. obo:GO_0071207 obo:go.owl obo:GO_0071207 midori obo:GO_0071207 2009-11-25T01:25:15Z obo:GO_0071207 molecular_function obo:GO_0071207 GO:0071207 obo:GO_0071207 histone pre-mRNA stem-loop binding obo:GO_0071208 Interacting selectively and non-covalently with the downstream cleavage product (DCP) generated by histone pre-mRNA 3'-end processing. obo:GO_0071208 obo:go.owl obo:GO_0071208 midori obo:GO_0071208 2009-11-25T01:41:35Z obo:GO_0071208 molecular_function obo:GO_0071208 GO:0071208 obo:GO_0071208 histone pre-mRNA DCP binding obo:GO_0071209 Interacting selectively and non-covalently with the U7 small nuclear RNA (U7 snRNA). obo:GO_0071209 obo:go.owl obo:GO_0071209 midori obo:GO_0071209 2009-11-25T01:46:50Z obo:GO_0071209 molecular_function obo:GO_0071209 GO:0071209 obo:GO_0071209 Note that this term may be useful for annotating other small nuclear RNAs (snRNAs). obo:GO_0071209 U7 snRNA binding obo:GO_0071214 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an abiotic (non-living) stimulus. obo:GO_0071214 obo:go.owl obo:GO_0071214 midori obo:GO_0071214 2009-12-03T01:02:11Z obo:GO_0071214 cellular response to abiotic stress obo:GO_0071214 biological_process obo:GO_0071214 GO:0071214 obo:GO_0071214 http://purl.oboInOwllibrary.org/oboInOwl/go#gocheck_do_not_manually_annotate obo:GO_0071214 Note that this term is in the subset of terms that should not be used for direct gene product annotation. Instead, select a child term or, if no appropriate child term exists, please request a new term. Direct annotations to this term may be amended during annotation QC. obo:GO_0071214 cellular response to abiotic stimulus obo:GO_0071216 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a biotic stimulus, a stimulus caused or produced by a living organism. obo:GO_0071216 obo:go.owl obo:GO_0071216 midori obo:GO_0071216 2009-12-03T01:09:08Z obo:GO_0071216 cellular response to biotic stress obo:GO_0071216 biological_process obo:GO_0071216 GO:0071216 obo:GO_0071216 http://purl.oboInOwllibrary.org/oboInOwl/go#gocheck_do_not_manually_annotate obo:GO_0071216 Note that this term is in the subset of terms that should not be used for direct gene product annotation. Instead, select a child term or, if no appropriate child term exists, please request a new term. Direct annotations to this term may be amended during annotation QC. obo:GO_0071216 cellular response to biotic stimulus obo:GO_0071217 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an external biotic stimulus, an external stimulus caused by, or produced by living things. obo:GO_0071217 obo:go.owl obo:GO_0071217 midori obo:GO_0071217 2009-12-03T01:14:27Z obo:GO_0071217 biological_process obo:GO_0071217 GO:0071217 obo:GO_0071217 cellular response to external biotic stimulus obo:GO_0071219 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus by molecules of bacterial origin such as peptides derived from bacterial flagellin. obo:GO_0071219 obo:go.owl obo:GO_0071219 midori obo:GO_0071219 2009-12-03T01:22:00Z obo:GO_0071219 cellular response to bacteria associated molecule obo:GO_0071219 cellular response to bacterial associated molecule obo:GO_0071219 cellular response to bacterium associated molecule obo:GO_0071219 biological_process obo:GO_0071219 GO:0071219 obo:GO_0071219 cellular response to molecule of bacterial origin obo:GO_0071220 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a bacterial lipoprotein stimulus. obo:GO_0071220 obo:go.owl obo:GO_0071220 midori obo:GO_0071220 2009-12-03T01:26:36Z obo:GO_0071220 biological_process obo:GO_0071220 GO:0071220 obo:GO_0071220 cellular response to bacterial lipoprotein obo:GO_0071221 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a bacterial lipopeptide stimulus. obo:GO_0071221 obo:go.owl obo:GO_0071221 midori obo:GO_0071221 2009-12-03T01:28:03Z obo:GO_0071221 biological_process obo:GO_0071221 GO:0071221 obo:GO_0071221 cellular response to bacterial lipopeptide obo:GO_0071222 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a lipopolysaccharide stimulus; lipopolysaccharide is a major component of the cell wall of gram-negative bacteria. obo:GO_0071222 obo:go.owl obo:GO_0071222 midori obo:GO_0071222 2009-12-03T01:29:29Z obo:GO_0071222 cellular response to endotoxin obo:GO_0071222 cellular response to LPS obo:GO_0071222 biological_process obo:GO_0071222 GO:0071222 obo:GO_0071222 cellular response to lipopolysaccharide obo:GO_0071223 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a lipoteichoic acid stimulus; lipoteichoic acid is a major component of the cell wall of gram-positive bacteria and typically consists of a chain of glycerol-phosphate repeating units linked to a glycolipid anchor. obo:GO_0071223 obo:go.owl obo:GO_0071223 midori obo:GO_0071223 2009-12-03T01:31:00Z obo:GO_0071223 cellular response to LTA obo:GO_0071223 biological_process obo:GO_0071223 GO:0071223 obo:GO_0071223 cellular response to lipoteichoic acid obo:GO_0071226 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus by molecules of fungal origin such as chito-octamer oligosaccharide. obo:GO_0071226 obo:go.owl obo:GO_0071226 midori obo:GO_0071226 2009-12-03T01:50:01Z obo:GO_0071226 cellular response to fungus associated molecule obo:GO_0071226 biological_process obo:GO_0071226 GO:0071226 obo:GO_0071226 cellular response to molecule of fungal origin obo:GO_0071227 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus by molecules of oomycetes origin. obo:GO_0071227 obo:go.owl obo:GO_0071227 midori obo:GO_0071227 2009-12-03T01:55:09Z obo:GO_0071227 cellular response to oomycetes associated molecule obo:GO_0071227 biological_process obo:GO_0071227 GO:0071227 obo:GO_0071227 cellular response to molecule of oomycetes origin obo:GO_0071236 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an antibiotic stimulus. An antibiotic is a chemical substance produced by a microorganism which has the capacity to inhibit the growth of or to kill other microorganisms. obo:GO_0071236 obo:go.owl obo:GO_0071236 midori obo:GO_0071236 2009-12-03T02:23:49Z obo:GO_0071236 biological_process obo:GO_0071236 GO:0071236 obo:GO_0071236 cellular response to antibiotic obo:GO_0071238 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a brefeldin A stimulus. obo:GO_0071238 obo:go.owl obo:GO_0071238 midori obo:GO_0071238 2009-12-03T02:25:52Z obo:GO_0071238 biological_process obo:GO_0071238 GO:0071238 obo:GO_0071238 cellular response to brefeldin A obo:GO_0071239 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a streptomycin stimulus. Streptomycin is a commonly used antibiotic in cell culture media which acts only on prokaryotes and blocks transition from initiation complex to chain elongating ribosome. obo:GO_0071239 obo:go.owl obo:GO_0071239 midori obo:GO_0071239 2009-12-03T02:25:59Z obo:GO_0071239 biological_process obo:GO_0071239 GO:0071239 obo:GO_0071239 cellular response to streptomycin obo:GO_0071253 Interacting selectively and non-covalently with a connexin, any of a group of related proteins that assemble to form gap junctions. obo:GO_0071253 obo:go.owl obo:GO_0071253 midori obo:GO_0071253 2009-12-04T10:07:54Z obo:GO_0071253 molecular_function obo:GO_0071253 GO:0071253 obo:GO_0071253 connexin binding obo:GO_0071257 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an electrical stimulus. obo:GO_0071257 obo:go.owl obo:GO_0071257 midori obo:GO_0071257 2009-12-04T03:27:03Z obo:GO_0071257 biological_process obo:GO_0071257 cellular response to electricity obo:GO_0071257 GO:0071257 obo:GO_0071257 cellular response to electrical stimulus obo:GO_0071258 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a gravitational stimulus. obo:GO_0071258 obo:go.owl obo:GO_0071258 midori obo:GO_0071258 2009-12-04T03:31:36Z obo:GO_0071258 cellular response to gravitational stimulus obo:GO_0071258 biological_process obo:GO_0071258 GO:0071258 obo:GO_0071258 cellular response to gravity obo:GO_0071259 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a magnetic stimulus. obo:GO_0071259 obo:go.owl obo:GO_0071259 midori obo:GO_0071259 2009-12-04T03:54:53Z obo:GO_0071259 cellular response to magnetic stimulus obo:GO_0071259 biological_process obo:GO_0071259 GO:0071259 obo:GO_0071259 cellular response to magnetism obo:GO_0071299 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a vitamin A stimulus. obo:GO_0071299 obo:go.owl obo:GO_0071299 midori obo:GO_0071299 2009-12-10T04:29:30Z obo:GO_0071299 cellular response to retinol obo:GO_0071299 biological_process obo:GO_0071299 GO:0071299 obo:GO_0071299 cellular response to vitamin A obo:GO_0071303 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a vitamin B3 stimulus. obo:GO_0071303 obo:go.owl obo:GO_0071303 midori obo:GO_0071303 2009-12-10T04:35:04Z obo:GO_0071303 cellular response to niacin obo:GO_0071303 cellular response to nicotinamide obo:GO_0071303 biological_process obo:GO_0071303 GO:0071303 obo:GO_0071303 cellular response to vitamin B3 obo:GO_0071305 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a vitamin D stimulus. obo:GO_0071305 obo:go.owl obo:GO_0071305 midori obo:GO_0071305 2009-12-10T04:35:37Z obo:GO_0071305 cellular response to calciferol obo:GO_0071305 cellular response to cholecalciferol obo:GO_0071305 cellular response to ergocalciferol obo:GO_0071305 biological_process obo:GO_0071305 GO:0071305 obo:GO_0071305 cellular response to vitamin D obo:GO_0071306 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a vitamin E stimulus. obo:GO_0071306 obo:go.owl obo:GO_0071306 midori obo:GO_0071306 2009-12-10T04:35:58Z obo:GO_0071306 cellular response to DL-alpha-tocopherol acetate obo:GO_0071306 cellular response to DL-alpha-tocopheryl acetate obo:GO_0071306 cellular response to O-Acetyl-alpha-tocopherol obo:GO_0071306 biological_process obo:GO_0071306 GO:0071306 obo:GO_0071306 cellular response to vitamin E obo:GO_0071307 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a vitamin K stimulus. obo:GO_0071307 obo:go.owl obo:GO_0071307 midori obo:GO_0071307 2009-12-10T04:36:09Z obo:GO_0071307 biological_process obo:GO_0071307 GO:0071307 obo:GO_0071307 cellular response to vitamin K obo:GO_0071336 Any process that modulates the frequency, rate or extent of hair follicle cell proliferation. obo:GO_0071336 obo:go.owl obo:GO_0071336 midori obo:GO_0071336 2009-12-11T10:53:40Z obo:GO_0071336 biological_process obo:GO_0071336 GO:0071336 obo:GO_0071336 regulation of hair follicle cell proliferation obo:GO_0071337 Any process that stops, prevents or reduces the rate or extent of hair follicle cell proliferation. obo:GO_0071337 obo:go.owl obo:GO_0071337 midori obo:GO_0071337 2009-12-11T10:59:20Z obo:GO_0071337 down regulation of hair follicle cell proliferation obo:GO_0071337 down-regulation of hair follicle cell proliferation obo:GO_0071337 downregulation of hair follicle cell proliferation obo:GO_0071337 inhibition of hair follicle cell proliferation obo:GO_0071337 biological_process obo:GO_0071337 GO:0071337 obo:GO_0071337 negative regulation of hair follicle cell proliferation obo:GO_0071338 Any process that activates or increases the rate or extent of hair follicle cell proliferation. obo:GO_0071338 obo:go.owl obo:GO_0071338 midori obo:GO_0071338 2009-12-11T11:00:57Z obo:GO_0071338 up regulation of hair follicle cell proliferation obo:GO_0071338 up-regulation of hair follicle cell proliferation obo:GO_0071338 upregulation of hair follicle cell proliferation obo:GO_0071338 activation of hair follicle cell proliferation obo:GO_0071338 stimulation of hair follicle cell proliferation obo:GO_0071338 biological_process obo:GO_0071338 GO:0071338 obo:GO_0071338 positive regulation of hair follicle cell proliferation obo:GO_0071361 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an ethanol stimulus. obo:GO_0071361 obo:go.owl obo:GO_0071361 midori obo:GO_0071361 2009-12-11T03:02:59Z obo:GO_0071361 biological_process obo:GO_0071361 GO:0071361 obo:GO_0071361 cellular response to ethanol obo:GO_0071421 A process in which a manganese ion is transported from one side of a membrane to the other by means of some agent such as a transporter or pore. obo:GO_0071421 obo:go.owl obo:GO_0071421 midori obo:GO_0071421 2009-12-15T02:41:31Z obo:GO_0071421 manganese ion membrane transport obo:GO_0071421 transmembrane manganese transport obo:GO_0071421 biological_process obo:GO_0071421 GO:0071421 obo:GO_0071421 Note that this term is not intended for use in annotating lateral movement within membranes. obo:GO_0071421 manganese ion transmembrane transport obo:GO_0071443 Interacting selectively and non-covalently with DNA sequences encoding transfer RNA. obo:GO_0071443 obo:go.owl obo:GO_0071443 midori obo:GO_0071443 2009-12-16T03:47:31Z obo:GO_0071443 molecular_function obo:GO_0071443 GO:0071443 obo:GO_0071443 tDNA binding obo:GO_0071447 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a hydroperoxide stimulus. Hydroperoxides are monosubstitution products of hydrogen peroxide, HOOH. obo:GO_0071447 obo:go.owl obo:GO_0071447 midori obo:GO_0071447 2009-12-16T04:16:42Z obo:GO_0071447 biological_process obo:GO_0071447 GO:0071447 obo:GO_0071447 cellular response to hydroperoxide obo:GO_0071448 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an alkyl hydroperoxide stimulus. Alkyl hydroperoxides are monosubstitution products of hydrogen peroxide, HOOH, where the substituent is an alkyl group. obo:GO_0071448 obo:go.owl obo:GO_0071448 midori obo:GO_0071448 2009-12-16T04:17:52Z obo:GO_0071448 biological_process obo:GO_0071448 GO:0071448 obo:GO_0071448 cellular response to alkyl hydroperoxide obo:GO_0071449 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a lipid hydroperoxide stimulus. Lipid hydroperoxide is the highly reactive primary oxygenated products of polyunsaturated fatty acids. obo:GO_0071449 obo:go.owl obo:GO_0071449 midori obo:GO_0071449 2009-12-16T04:17:57Z obo:GO_0071449 cellular response to LHPO obo:GO_0071449 biological_process obo:GO_0071449 GO:0071449 obo:GO_0071449 cellular response to lipid hydroperoxide obo:GO_0071453 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus reflecting the presence, absence, or concentration of oxygen. obo:GO_0071453 obo:go.owl obo:GO_0071453 midori obo:GO_0071453 2009-12-16T04:43:59Z obo:GO_0071453 biological_process obo:GO_0071453 cellular response to oxygen obo:GO_0071453 GO:0071453 obo:GO_0071453 cellular response to oxygen levels obo:GO_0071455 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating increased oxygen tension. obo:GO_0071455 obo:go.owl obo:GO_0071455 midori obo:GO_0071455 2009-12-16T04:44:41Z obo:GO_0071455 cellular response to hyperoxic stress obo:GO_0071455 cellular response to increased oxygen tension obo:GO_0071455 biological_process obo:GO_0071455 GO:0071455 obo:GO_0071455 cellular response to hyperoxia obo:GO_0071456 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level. obo:GO_0071456 obo:go.owl obo:GO_0071456 midori obo:GO_0071456 2009-12-16T04:45:20Z obo:GO_0071456 cellular response to hypoxic stress obo:GO_0071456 cellular response to lowered oxygen tension obo:GO_0071456 biological_process obo:GO_0071456 GO:0071456 obo:GO_0071456 Note that this term should not be confused with 'cellular response to anoxia ; GO:0071454'. Note that in laboratory studies, hypoxia is typically studied at O2 concentrations ranging from 0.1 - 5%. obo:GO_0071456 cellular response to hypoxia obo:GO_0071460 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of cell-matrix adhesion. obo:GO_0071460 obo:go.owl obo:GO_0071460 midori obo:GO_0071460 2009-12-17T02:25:45Z obo:GO_0071460 biological_process obo:GO_0071460 GO:0071460 obo:GO_0071460 cellular response to cell-matrix adhesion obo:GO_0071461 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating redox state. Redox state refers to the balance of oxidized versus reduced forms of electron donors and acceptors in an organelle, cell or organ; plastoquinone, glutathione (GSH/GSSG), and nicotinamide nucleotides (NAD+/NADH and NADP+/NADPH) are among the most important. obo:GO_0071461 obo:go.owl obo:GO_0071461 midori obo:GO_0071461 2009-12-18T11:30:21Z obo:GO_0071461 cellular redox signal response obo:GO_0071461 biological_process obo:GO_0071461 GO:0071461 obo:GO_0071461 cellular response to redox state obo:GO_0071467 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a pH stimulus. pH is a measure of the acidity or basicity of an aqueous solution. obo:GO_0071467 obo:go.owl obo:GO_0071467 midori obo:GO_0071467 2009-12-18T11:41:54Z obo:GO_0071467 biological_process obo:GO_0071467 GO:0071467 obo:GO_0071467 cellular response to pH obo:GO_0071468 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a pH stimulus with pH < 7. pH is a measure of the acidity or basicity of an aqueous solution. obo:GO_0071468 obo:go.owl obo:GO_0071468 midori obo:GO_0071468 2009-12-18T11:42:35Z obo:GO_0071468 cellular response to acidity obo:GO_0071468 biological_process obo:GO_0071468 GO:0071468 obo:GO_0071468 This term should be used to annotate instances where a cell is responding to a chemical that is playing the role of an acid (e.g. proton donor) and therefore lowering the pH. If instead you wish to describe a response to a specific acid as a chemical, such as the anion portion of glutamate, please annotate to the appropriate child of GO:0071229 'cellular response to acid chemical'. obo:GO_0071468 cellular response to acidic pH obo:GO_0071469 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a pH stimulus with pH > 7. pH is a measure of the acidity or basicity of an aqueous solution. obo:GO_0071469 obo:go.owl obo:GO_0071469 midori obo:GO_0071469 2009-12-18T11:42:47Z obo:GO_0071469 cellular response to alkalinity obo:GO_0071469 cellular response to basic pH obo:GO_0071469 biological_process obo:GO_0071469 GO:0071469 obo:GO_0071469 cellular response to alkaline pH obo:GO_0071470 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating an increase or decrease in the concentration of solutes outside the organism or cell. obo:GO_0071470 obo:go.owl obo:GO_0071470 midori obo:GO_0071470 2009-12-18T11:45:33Z obo:GO_0071470 cellular osmotic response obo:GO_0071470 cellular osmotic stress response obo:GO_0071470 biological_process obo:GO_0071470 GO:0071470 obo:GO_0071470 cellular response to osmotic stress obo:GO_0071471 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating an increase or decrease in the concentration of non-ionic solutes (e.g. mannitol, sorbitol) in the environment. obo:GO_0071471 obo:go.owl obo:GO_0071471 midori obo:GO_0071471 2009-12-18T11:47:59Z obo:GO_0071471 biological_process obo:GO_0071471 GO:0071471 obo:GO_0071471 cellular response to non-ionic osmotic stress obo:GO_0071472 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating an increase or decrease in the concentration of salt (particularly but not exclusively sodium and chloride ions) in the environment. obo:GO_0071472 obo:go.owl obo:GO_0071472 midori obo:GO_0071472 2009-12-18T11:48:23Z obo:GO_0071472 cellular response to ionic osmotic stress obo:GO_0071472 cellular salinity response obo:GO_0071472 biological_process obo:GO_0071472 GO:0071472 obo:GO_0071472 cellular response to salt stress obo:GO_0071473 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of cation stress, an increase or decrease in the concentration of positively charged ions in the environment. obo:GO_0071473 obo:go.owl obo:GO_0071473 midori obo:GO_0071473 2009-12-18T11:49:46Z obo:GO_0071473 biological_process obo:GO_0071473 GO:0071473 obo:GO_0071473 cellular response to cation stress obo:GO_0071474 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, a hyperosmotic environment, i.e. an environment with a higher concentration of solutes than the organism or cell. obo:GO_0071474 obo:go.owl obo:GO_0071474 midori obo:GO_0071474 2009-12-18T11:51:36Z obo:GO_0071474 cellular HOG response obo:GO_0071474 cellular hypertonic response obo:GO_0071474 cellular response to hypertonicity obo:GO_0071474 biological_process obo:GO_0071474 GO:0071474 obo:GO_0071474 cellular hyperosmotic response obo:GO_0071475 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, an increase in the concentration of salt (particularly but not exclusively sodium and chloride ions) in the environment. obo:GO_0071475 obo:go.owl obo:GO_0071475 midori obo:GO_0071475 2009-12-18T11:52:06Z obo:GO_0071475 cellular response to hyperosmotic salt stress obo:GO_0071475 biological_process obo:GO_0071475 GO:0071475 obo:GO_0071475 cellular hyperosmotic salinity response obo:GO_0071476 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, a hypotonic environment, i.e. an environment with a lower concentration of solutes than the organism or cell. obo:GO_0071476 obo:go.owl obo:GO_0071476 midori obo:GO_0071476 2009-12-18T11:52:59Z obo:GO_0071476 cellular hypo-osmotic response obo:GO_0071476 biological_process obo:GO_0071476 GO:0071476 obo:GO_0071476 cellular hypotonic response obo:GO_0071477 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, a decrease in the concentration of salt (particularly but not exclusively sodium and chloride ions) in the environment. obo:GO_0071477 obo:go.owl obo:GO_0071477 midori obo:GO_0071477 2009-12-18T11:53:20Z obo:GO_0071477 cellular response to hypotonic salt stress obo:GO_0071477 biological_process obo:GO_0071477 GO:0071477 obo:GO_0071477 cellular hypotonic salinity response obo:GO_0071478 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an electromagnetic radiation stimulus. Electromagnetic radiation is a propagating wave in space with electric and magnetic components. These components oscillate at right angles to each other and to the direction of propagation. obo:GO_0071478 obo:go.owl obo:GO_0071478 midori obo:GO_0071478 2009-12-18T01:59:37Z obo:GO_0071478 cellular response to electromagnetic radiation stimulus obo:GO_0071478 cellular response to radiation stimulus obo:GO_0071478 biological_process obo:GO_0071478 GO:0071478 obo:GO_0071478 Note that 'radiation' refers to electromagnetic radiation of any wavelength. obo:GO_0071478 cellular response to radiation obo:GO_0071479 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a ionizing radiation stimulus. Ionizing radiation is radiation with sufficient energy to remove electrons from atoms and may arise from spontaneous decay of unstable isotopes, resulting in alpha and beta particles and gamma rays. Ionizing radiation also includes X-rays. obo:GO_0071479 obo:go.owl obo:GO_0071479 midori obo:GO_0071479 2009-12-18T02:00:31Z obo:GO_0071479 cellular response to ionising radiation obo:GO_0071479 cellular response to ionizing radiation stimulus obo:GO_0071479 biological_process obo:GO_0071479 GO:0071479 obo:GO_0071479 cellular response to ionizing radiation obo:GO_0071480 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a gamma radiation stimulus. Gamma radiation is a form of electromagnetic radiation (EMR) or light emission of a specific frequency produced from sub-atomic particle interaction, such as electron-positron annihilation and radioactive decay. Gamma rays are generally characterized as EMR having the highest frequency and energy, and also the shortest wavelength, within the electromagnetic radiation spectrum. obo:GO_0071480 obo:go.owl obo:GO_0071480 midori obo:GO_0071480 2009-12-18T02:00:50Z obo:GO_0071480 biological_process obo:GO_0071480 cellular response to gamma ray obo:GO_0071480 cellular response to gamma-ray photon obo:GO_0071480 GO:0071480 obo:GO_0071480 cellular response to gamma radiation obo:GO_0071481 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of X-ray radiation. An X-ray is a form of electromagnetic radiation with a wavelength in the range of 10 nanometers to 100 picometers (corresponding to frequencies in the range 30 PHz to 3 EHz). obo:GO_0071481 obo:go.owl obo:GO_0071481 midori obo:GO_0071481 2009-12-18T02:00:59Z obo:GO_0071481 cellular response to X-ray radiation stimulus obo:GO_0071481 biological_process obo:GO_0071481 GO:0071481 obo:GO_0071481 cellular response to X-ray obo:GO_0071482 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a light stimulus, electromagnetic radiation of wavelengths classified as infrared, visible or ultraviolet light. obo:GO_0071482 obo:go.owl obo:GO_0071482 midori obo:GO_0071482 2009-12-18T02:03:49Z obo:GO_0071482 biological_process obo:GO_0071482 GO:0071482 obo:GO_0071482 cellular response to light stimulus obo:GO_0071483 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a blue light stimulus. Blue light is electromagnetic radiation with a wavelength of between 440 and 500nm. obo:GO_0071483 obo:go.owl obo:GO_0071483 midori obo:GO_0071483 2009-12-18T02:09:48Z obo:GO_0071483 cellular response to blue light stimulus obo:GO_0071483 biological_process obo:GO_0071483 GO:0071483 obo:GO_0071483 cellular response to blue light obo:GO_0071484 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a light intensity stimulus. obo:GO_0071484 obo:go.owl obo:GO_0071484 midori obo:GO_0071484 2009-12-18T02:11:03Z obo:GO_0071484 biological_process obo:GO_0071484 GO:0071484 obo:GO_0071484 cellular response to light intensity obo:GO_0071485 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an absence of light stimuli. obo:GO_0071485 obo:go.owl obo:GO_0071485 midori obo:GO_0071485 2009-12-18T02:13:12Z obo:GO_0071485 biological_process obo:GO_0071485 cellular response to darkness obo:GO_0071485 GO:0071485 obo:GO_0071485 cellular response to absence of light obo:GO_0071486 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a high light intensity stimulus. obo:GO_0071486 obo:go.owl obo:GO_0071486 midori obo:GO_0071486 2009-12-18T02:13:23Z obo:GO_0071486 biological_process obo:GO_0071486 GO:0071486 obo:GO_0071486 cellular response to high light intensity obo:GO_0071487 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a low light intensity stimulus. Low light intensity is defined as a level of electromagnetic radiation at or below 0.1 micromols/m2. obo:GO_0071487 obo:go.owl obo:GO_0071487 midori obo:GO_0071487 2009-12-18T02:13:29Z obo:GO_0071487 biological_process obo:GO_0071487 GO:0071487 obo:GO_0071487 cellular response to low light intensity stimulus obo:GO_0071488 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a very low light intensity stimulus. A very low light intensity stimulus is defined as a level of electromagnetic radiation below 0.001 mmol/m2/sec. obo:GO_0071488 obo:go.owl obo:GO_0071488 midori obo:GO_0071488 2009-12-18T02:13:40Z obo:GO_0071488 biological_process obo:GO_0071488 GO:0071488 obo:GO_0071488 cellular response to very low light intensity stimulus obo:GO_0071489 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a red or far red light stimulus. Red light is electromagnetic radiation of wavelength of 580-700nm. Far red light is electromagnetic radiation of wavelength 700-800nm. An example of this response is seen at the beginning of many plant species developmental stages. These include germination, and the point when cotyledon expansion is triggered. In certain species these processes take place in response to absorption of red light by the pigment molecule phytochrome, but the signal can be reversed by exposure to far red light. During the initial phase the phytochrome molecule is only present in the red light absorbing form, but on absorption of red light it changes to a far red light absorbing form, triggering progress through development. An immediate short period of exposure to far red light entirely returns the pigment to its initial state and prevents triggering of the developmental process. A thirty minute break between red and subsequent far red light exposure renders the red light effect irreversible, and development then occurs regardless of whether far red light exposure subsequently occurs. obo:GO_0071489 obo:go.owl obo:GO_0071489 midori obo:GO_0071489 2009-12-18T02:18:25Z obo:GO_0071489 biological_process obo:GO_0071489 GO:0071489 obo:GO_0071489 cellular response to red or far red light obo:GO_0071490 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of far red light stimulus. Far red light is electromagnetic radiation of wavelength 700-800nm. An example of this response is seen at the beginning of many plant species developmental stages. These include germination, and the point when cotyledon expansion is triggered. In certain species these processes take place in response to absorption of red light by the pigment molecule phytochrome, but the signal can be reversed by exposure to far red light. During the initial phase the phytochrome molecule is only present in the red light absorbing form, but on absorption of red light it changes to a far red light absorbing form, triggering progress through development. An immediate short period of exposure to far red light entirely returns the pigment to its initial state and prevents triggering of the developmental process. A thirty minute break between red and subsequent far red light exposure renders the red light effect irreversible, and development then occurs regardless of whether far red light exposure subsequently occurs. obo:GO_0071490 obo:go.owl obo:GO_0071490 midori obo:GO_0071490 2009-12-18T02:19:40Z obo:GO_0071490 cellular response to far red light stimulus obo:GO_0071490 biological_process obo:GO_0071490 GO:0071490 obo:GO_0071490 cellular response to far red light obo:GO_0071491 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a red light stimulus. Red light is electromagnetic radiation of wavelength of 580-700nm. An example of this response is seen at the beginning of many plant species developmental stages. These include germination, and the point when cotyledon expansion is triggered. In certain species these processes take place in response to absorption of red light by the pigment molecule phytochrome, but the signal can be reversed by exposure to far red light. During the initial phase the phytochrome molecule is only present in the red light absorbing form, but on absorption of red light it changes to a far red light absorbing form, triggering progress through development. An immediate short period of exposure to far red light entirely returns the pigment to its initial state and prevents triggering of the developmental process. A thirty minute break between red and subsequent far red light exposure renders the red light effect irreversible, and development then occurs regardless of whether far red light exposure subsequently occurs. obo:GO_0071491 obo:go.owl obo:GO_0071491 midori obo:GO_0071491 2009-12-18T02:19:47Z obo:GO_0071491 cellular response to red light stimulus obo:GO_0071491 biological_process obo:GO_0071491 GO:0071491 obo:GO_0071491 cellular response to red light obo:GO_0071492 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a UV-A radiation stimulus. UV-A radiation (UV-A light) spans the wavelengths 315 to 400 nm. obo:GO_0071492 obo:go.owl obo:GO_0071492 midori obo:GO_0071492 2009-12-18T02:21:51Z obo:GO_0071492 cellular response to UV-A light stimulus obo:GO_0071492 cellular response to UV-A radiation stimulus obo:GO_0071492 cellular response to UVA light stimulus obo:GO_0071492 cellular response to UVA radiation stimulus obo:GO_0071492 biological_process obo:GO_0071492 GO:0071492 obo:GO_0071492 cellular response to UV-A obo:GO_0071493 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a UV-B radiation stimulus. UV-B radiation (UV-B light) spans the wavelengths 280 to 315 nm. obo:GO_0071493 obo:go.owl obo:GO_0071493 midori obo:GO_0071493 2009-12-18T02:21:56Z obo:GO_0071493 cellular response to UV-B light stimulus obo:GO_0071493 cellular response to UV-B radiation stimulus obo:GO_0071493 cellular response to UVB light stimulus obo:GO_0071493 cellular response to UVB radiation stimulus obo:GO_0071493 cellular response to medium wave ultraviolet light stimulus obo:GO_0071493 cellular response to medium wave ultraviolet radiation stimulus obo:GO_0071493 biological_process obo:GO_0071493 GO:0071493 obo:GO_0071493 cellular response to UV-B obo:GO_0071494 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a UV-C radiation stimulus. UV-C radiation (UV-C light) spans the wavelengths 100 to 280 nm. obo:GO_0071494 obo:go.owl obo:GO_0071494 midori obo:GO_0071494 2009-12-18T02:22:01Z obo:GO_0071494 cellular response to UV-C light stimulus obo:GO_0071494 cellular response to UV-C radiation stimulus obo:GO_0071494 cellular response to UVC light stimulus obo:GO_0071494 cellular response to UVC radiation stimulus obo:GO_0071494 cellular response to germicidal ultraviolet light stimulus obo:GO_0071494 cellular response to germicidal ultraviolet radiation stimulus obo:GO_0071494 cellular response to shortwave ultraviolet light stimulus obo:GO_0071494 cellular response to shortwave ultraviolet radiation stimulus obo:GO_0071494 biological_process obo:GO_0071494 GO:0071494 obo:GO_0071494 cellular response to UV-C obo:GO_0071496 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an external stimulus. obo:GO_0071496 obo:go.owl obo:GO_0071496 midori obo:GO_0071496 2009-12-18T02:36:52Z obo:GO_0071496 biological_process obo:GO_0071496 GO:0071496 obo:GO_0071496 http://purl.oboInOwllibrary.org/oboInOwl/go#gocheck_do_not_manually_annotate obo:GO_0071496 Note that this term is in the subset of terms that should not be used for direct gene product annotation. Instead, select a child term or, if no appropriate child term exists, please request a new term. Direct annotations to this term may be amended during annotation QC. obo:GO_0071496 cellular response to external stimulus obo:GO_0071497 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a freezing stimulus, temperatures below 0 degrees Celsius. obo:GO_0071497 obo:go.owl obo:GO_0071497 midori obo:GO_0071497 2009-12-18T02:41:02Z obo:GO_0071497 biological_process obo:GO_0071497 antifreeze activity obo:GO_0071497 ice nucleation inhibitor activity obo:GO_0071497 GO:0071497 obo:GO_0071497 cellular response to freezing obo:GO_0071502 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a temperature stimulus. obo:GO_0071502 obo:go.owl obo:GO_0071502 midori obo:GO_0071502 2009-12-18T02:56:45Z obo:GO_0071502 cellular response to thermal stimulus obo:GO_0071502 biological_process obo:GO_0071502 GO:0071502 obo:GO_0071502 cellular response to temperature stimulus obo:GO_0071532 Interacting selectively and non-covalently with an ankyrin repeat of a protein. Ankyrin repeats are tandemly repeated modules of about 33 amino acids; each repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90-degree angle, and repeats stack to form an L-shaped structure. obo:GO_0071532 obo:go.owl obo:GO_0071532 midori obo:GO_0071532 2010-01-08T02:21:02Z obo:GO_0071532 ANK repeat binding obo:GO_0071532 molecular_function obo:GO_0071532 GO:0071532 obo:GO_0071532 ankyrin repeat binding obo:GO_0071535 Interacting selectively and non-covalently with a RING-like zinc finger domain domain of a protein. The RING-like domain is a zinc finger domain that is related to the C3HC4 RING finger domain. obo:GO_0071535 obo:go.owl obo:GO_0071535 midori obo:GO_0071535 2010-01-08T03:10:14Z obo:GO_0071535 molecular_function obo:GO_0071535 GO:0071535 obo:GO_0071535 RING-like zinc finger domain binding obo:GO_0071551 Interacting selectively and non-covalently with a RIP homotypic interaction motif (RHIM) of a protein. The RHIM is a 16-amino-acid motif found in some members, including RIP3, of a family of related kinases. obo:GO_0071551 obo:go.owl obo:GO_0071551 midori obo:GO_0071551 2010-01-13T03:03:51Z obo:GO_0071551 RHIM binding obo:GO_0071551 molecular_function obo:GO_0071551 GO:0071551 obo:GO_0071551 RIP homotypic interaction motif binding obo:GO_0071555 A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis. obo:GO_0071555 obo:go.owl obo:GO_0071555 midori obo:GO_0071555 2010-01-13T03:33:07Z obo:GO_0071555 GO:0007047 obo:GO_0071555 GO:0044234 obo:GO_0071555 cell wall organisation obo:GO_0071555 cell wall organisation in other organism obo:GO_0071555 cell wall organization at cellular level obo:GO_0071555 cell wall organization in other organism obo:GO_0071555 cellular cell wall organisation obo:GO_0071555 cellular cell wall organization obo:GO_0071555 biological_process obo:GO_0071555 cell wall organization and biogenesis obo:GO_0071555 GO:0071555 obo:GO_0071555 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_candida obo:GO_0071555 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_0071555 cell wall organization obo:GO_0071576 Interacting selectively and non-covalently with tetrahydrodictyopterin, the pterin 2-amino-6-[(1R,2R)-1,2-dihydroxypropyl]-5,6,7,8-tetrahydropteridin-4(3H)-one. obo:GO_0071576 obo:go.owl obo:GO_0071576 midori obo:GO_0071576 2010-01-26T05:24:59Z obo:GO_0071576 D-threo-tetrahydrobiopterin obo:GO_0071576 DH4 binding obo:GO_0071576 molecular_function obo:GO_0071576 GO:0071576 obo:GO_0071576 tetrahydrodictyopterin binding obo:GO_0071577 A process in which a zinc II ion is transported from one side of a membrane to the other by means of some agent such as a transporter or pore. obo:GO_0071577 obo:go.owl obo:GO_0071577 midori obo:GO_0071577 2010-01-28T02:17:12Z obo:GO_0071577 zinc II ion transmembrane transport obo:GO_0071577 zinc ion membrane transport obo:GO_0071577 zinc transmembrane transport obo:GO_0071577 biological_process obo:GO_0071577 GO:0071577 obo:GO_0071577 Note that this term is not intended for use in annotating lateral movement within membranes. obo:GO_0071577 zinc ion transmembrane transport obo:GO_0071578 The directed movement of zinc(2+) ions from outside of a cell, across the plasma membrane and into the cytosol. obo:GO_0071578 obo:go.owl obo:GO_0071578 janelomax obo:GO_0071578 2010-01-28T02:22:02Z obo:GO_0071578 GO:0006830 obo:GO_0071578 GO:0006831 obo:GO_0071578 GO:0044749 obo:GO_0071578 GO:0140160 obo:GO_0071578 zinc II ion plasma membrane import obo:GO_0071578 zinc II ion transmembrane import obo:GO_0071578 zinc import obo:GO_0071578 zinc uptake obo:GO_0071578 high-affinity zinc II ion transmembrane import obo:GO_0071578 high-affinity zinc II ion transport obo:GO_0071578 low-affinity zinc II ion transport obo:GO_0071578 biological_process obo:GO_0071578 zinc ion transmembrane import obo:GO_0071578 GO:0071578 obo:GO_0071578 zinc ion import across plasma membrane obo:GO_0071579 Any process that modulates the frequency, rate or extent of the directed movement of zinc ions (Zn2+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0071579 obo:go.owl obo:GO_0071579 midori obo:GO_0071579 2010-01-28T03:02:15Z obo:GO_0071579 biological_process obo:GO_0071579 GO:0071579 obo:GO_0071579 regulation of zinc ion transport obo:GO_0071580 Any process that modulates the frequency, rate or extent of the directed movement of zinc ions (Zn2+) from one side of a membrane to the other. obo:GO_0071580 obo:go.owl obo:GO_0071580 midori obo:GO_0071580 2010-01-28T03:05:53Z obo:GO_0071580 regulation of zinc ion membrane transport obo:GO_0071580 biological_process obo:GO_0071580 GO:0071580 obo:GO_0071580 regulation of zinc ion transmembrane transport obo:GO_0071581 Any process that modulates the frequency, rate or extent of zinc ion import. obo:GO_0071581 obo:go.owl obo:GO_0071581 midori obo:GO_0071581 2010-01-28T03:09:19Z obo:GO_0071581 biological_process obo:GO_0071581 GO:0071581 obo:GO_0071581 regulation of zinc ion transmembrane import obo:GO_0071582 Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of zinc ions (Zn2+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0071582 obo:go.owl obo:GO_0071582 midori obo:GO_0071582 2010-01-28T03:14:25Z obo:GO_0071582 biological_process obo:GO_0071582 GO:0071582 obo:GO_0071582 negative regulation of zinc ion transport obo:GO_0071583 Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of zinc ions (Zn2+) from one side of a membrane to the other. obo:GO_0071583 obo:go.owl obo:GO_0071583 midori obo:GO_0071583 2010-01-28T03:15:54Z obo:GO_0071583 negative regulation of zinc ion membrane transport obo:GO_0071583 biological_process obo:GO_0071583 GO:0071583 obo:GO_0071583 negative regulation of zinc ion transmembrane transport obo:GO_0071584 Any process that stops, prevents, or reduces the frequency, rate or extent of zinc ion import. obo:GO_0071584 obo:go.owl obo:GO_0071584 midori obo:GO_0071584 2010-01-28T03:17:21Z obo:GO_0071584 biological_process obo:GO_0071584 GO:0071584 obo:GO_0071584 negative regulation of zinc ion transmembrane import obo:GO_0071588 A series of molecular signals mediated by the detection of hydrogen peroxide (H2O2). obo:GO_0071588 obo:go.owl obo:GO_0071588 midori obo:GO_0071588 2010-01-29T11:18:58Z obo:GO_0071588 H2O2 mediated signaling pathway obo:GO_0071588 hydrogen peroxide mediated signalling pathway obo:GO_0071588 biological_process obo:GO_0071588 GO:0071588 obo:GO_0071588 hydrogen peroxide mediated signaling pathway obo:GO_0071667 Interacting selectively and non-covalently with a RNA/DNA hybrid. obo:GO_0071667 obo:go.owl obo:GO_0071667 midori obo:GO_0071667 2010-02-15T01:51:44Z obo:GO_0071667 RNA/DNA hybrid binding obo:GO_0071667 molecular_function obo:GO_0071667 GO:0071667 obo:GO_0071667 DNA/RNA hybrid binding obo:GO_0071703 The series of events in which an organic substance stimulus is received by a cell and converted into a molecular signal. obo:GO_0071703 obo:go.owl obo:GO_0071703 midori obo:GO_0071703 2010-03-08T03:18:44Z obo:GO_0071703 biological_process obo:GO_0071703 GO:0071703 obo:GO_0071703 detection of organic substance obo:GO_0071704 The chemical reactions and pathways involving an organic substance, any molecular entity containing carbon. obo:GO_0071704 obo:go.owl obo:GO_0071704 midori obo:GO_0071704 2010-03-08T03:32:18Z obo:GO_0071704 organic molecular entity metabolic process obo:GO_0071704 organic molecular entity metabolism obo:GO_0071704 organic substance metabolism obo:GO_0071704 biological_process obo:GO_0071704 GO:0071704 obo:GO_0071704 organic substance metabolic process obo:GO_0071723 Interacting selectively and non-covalently with a lipopeptide, any of a group of organic compounds comprising two or more amino acids linked by peptide bonds and containing a nonprotein group consisting of a lipid or lipids. obo:GO_0071723 obo:go.owl obo:GO_0071723 midori obo:GO_0071723 2010-03-17T02:13:21Z obo:GO_0071723 bacterial lipopeptide binding obo:GO_0071723 molecular_function obo:GO_0071723 bacterial lipoprotein binding obo:GO_0071723 GO:0071723 obo:GO_0071723 Note that bacterial lipopeptides are derived from bacterial lipoproteins, but the two terms are sometimes used interchangeably in the literature. obo:GO_0071723 lipopeptide binding obo:GO_0071724 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a diacylated bacterial lipopeptide stimulus. obo:GO_0071724 obo:go.owl obo:GO_0071724 midori obo:GO_0071724 2010-03-17T02:14:41Z obo:GO_0071724 response to diacylated bacterial lipoprotein obo:GO_0071724 biological_process obo:GO_0071724 GO:0071724 obo:GO_0071724 Note that bacterial lipopeptides are derived from bacterial lipoproteins, but the two terms are sometimes used interchangeably in the literature. obo:GO_0071724 response to diacyl bacterial lipopeptide obo:GO_0071725 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a triacylated bacterial lipopeptide stimulus. obo:GO_0071725 obo:go.owl obo:GO_0071725 midori obo:GO_0071725 2010-03-17T02:16:40Z obo:GO_0071725 response to triacylated bacterial lipoprotein obo:GO_0071725 biological_process obo:GO_0071725 GO:0071725 obo:GO_0071725 Note that bacterial lipopeptides are derived from bacterial lipoproteins, but the two terms are sometimes used interchangeably in the literature. obo:GO_0071725 response to triacyl bacterial lipopeptide obo:GO_0071726 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a diacylated bacterial lipopeptide stimulus. obo:GO_0071726 obo:go.owl obo:GO_0071726 midori obo:GO_0071726 2010-03-17T02:17:02Z obo:GO_0071726 cellular response to diacylated bacterial lipoprotein obo:GO_0071726 biological_process obo:GO_0071726 GO:0071726 obo:GO_0071726 Note that bacterial lipopeptides are derived from bacterial lipoproteins, but the two terms are sometimes used interchangeably in the literature. obo:GO_0071726 cellular response to diacyl bacterial lipopeptide obo:GO_0071727 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a triacylated bacterial lipopeptide stimulus. obo:GO_0071727 obo:go.owl obo:GO_0071727 midori obo:GO_0071727 2010-03-17T02:17:49Z obo:GO_0071727 cellular response to triacylated bacterial lipoprotein obo:GO_0071727 biological_process obo:GO_0071727 GO:0071727 obo:GO_0071727 Note that bacterial lipopeptides are derived from bacterial lipoproteins, but the two terms are sometimes used interchangeably in the literature. obo:GO_0071727 cellular response to triacyl bacterial lipopeptide obo:GO_0071791 Interacting selectively and non-covalently with chemokine (C-C motif) ligand 5. obo:GO_0071791 obo:go.owl obo:GO_0071791 midori obo:GO_0071791 2010-09-01T02:28:22Z obo:GO_0071791 CCL5 binding obo:GO_0071791 RANTES binding obo:GO_0071791 Regulated upon Activation, Normal T-cell Expressed, and Secreted binding obo:GO_0071791 molecular_function obo:GO_0071791 GO:0071791 obo:GO_0071791 chemokine (C-C motif) ligand 5 binding obo:GO_0071794 Interacting selectively and non-covalently with a CAP-Gly domain of a protein. The CAP_Gly domain is a conserved, glycine-rich domain of about 42 residues found in some cytoskeleton-associated proteins, and features a novel protein fold containing three beta-sheets. obo:GO_0071794 obo:go.owl obo:GO_0071794 midori obo:GO_0071794 2010-09-02T02:02:53Z obo:GO_0071794 molecular_function obo:GO_0071794 GO:0071794 obo:GO_0071794 CAP-Gly domain binding obo:GO_0071795 Interacting selectively and non-covalently with a protein upon poly-ubiquitination formed by linkages between lysine residues at position 11 in the target protein. obo:GO_0071795 obo:go.owl obo:GO_0071795 midori obo:GO_0071795 2010-09-02T02:11:41Z obo:GO_0071795 molecular_function obo:GO_0071795 GO:0071795 obo:GO_0071795 K11-linked polyubiquitin modification-dependent protein binding obo:GO_0071796 Interacting selectively and non-covalently with a protein upon poly-ubiquitination formed by linkages between lysine residues at position 6 in the target protein. obo:GO_0071796 obo:go.owl obo:GO_0071796 midori obo:GO_0071796 2010-09-02T02:13:07Z obo:GO_0071796 molecular_function obo:GO_0071796 GO:0071796 obo:GO_0071796 K6-linked polyubiquitin modification-dependent protein binding obo:GO_0071805 A process in which a potassium ion is transported from one side of a membrane to the other. obo:GO_0071805 obo:go.owl obo:GO_0071805 midori obo:GO_0071805 2010-09-03T02:43:49Z obo:GO_0071805 GO:0010163 obo:GO_0071805 potassium ion membrane transport obo:GO_0071805 high affinity potassium ion import obo:GO_0071805 high affinity potassium ion uptake obo:GO_0071805 high-affinity potassium ion import obo:GO_0071805 high-affinity potassium ion uptake obo:GO_0071805 biological_process obo:GO_0071805 GO:0071805 obo:GO_0071805 Note that this term is not intended for use in annotating lateral movement within membranes. obo:GO_0071805 potassium ion transmembrane transport obo:GO_0071813 Interacting selectively and non-covalently with a lipoprotein particle. A lipoprotein particle, also known as a lipoprotein, is a clathrate complex consisting of a lipid enwrapped in a protein host without covalent binding in such a way that the complex has a hydrophilic outer surface consisting of all the protein and the polar ends of any phospholipids. obo:GO_0071813 obo:go.owl obo:GO_0071813 midori obo:GO_0071813 2010-09-06T03:16:01Z obo:GO_0071813 plasma lipoprotein particle binding obo:GO_0071813 molecular_function obo:GO_0071813 lipoprotein binding obo:GO_0071813 plasma lipoprotein binding obo:GO_0071813 GO:0071813 obo:GO_0071813 lipoprotein particle binding obo:GO_0071814 Interacting selectively and non-covalently with a protein-lipid complex, any macromolecular complex that contains both protein and lipid molecules. obo:GO_0071814 obo:go.owl obo:GO_0071814 midori obo:GO_0071814 2010-09-06T04:26:27Z obo:GO_0071814 molecular_function obo:GO_0071814 GO:0071814 obo:GO_0071814 protein-lipid complex binding obo:GO_0071815 Interacting selectively and non-covalently with a intermediate-density lipoprotein particle, a triglyceride-rich lipoprotein particle that typically contains APOB100, APOE and APOCs and has a density of 1.006-1.019 g/ml and a diameter of between 25-30 nm. obo:GO_0071815 obo:go.owl obo:GO_0071815 midori obo:GO_0071815 2010-09-06T04:28:35Z obo:GO_0071815 IDL binding obo:GO_0071815 intermediate-density lipoprotein binding obo:GO_0071815 molecular_function obo:GO_0071815 GO:0071815 obo:GO_0071815 intermediate-density lipoprotein particle binding obo:GO_0071820 Interacting selectively and non-covalently with an N-box, a DNA motif with the consensus sequence CACNAG that is found in the promoters of genes expressed preferentially at synapses. obo:GO_0071820 obo:go.owl obo:GO_0071820 midori obo:GO_0071820 2010-09-07T11:55:32Z obo:GO_0071820 N box binding obo:GO_0071820 N-box promoter binding obo:GO_0071820 molecular_function obo:GO_0071820 GO:0071820 obo:GO_0071820 Note that as agreed during the transcription overhaul, terms specifying binding to specific transcription regulatory motifs are no longer being created. The level of specificity GO has decided to go to is the "core promoter", "core promoter proximal region" and "enhancer". To capture more detail, please consider using column 16. obo:GO_0071820 N-box binding obo:GO_0071837 Interacting selectively and non-covalently with an HMG box domain, a protein domain that consists of three helices in an irregular array. HMG-box domains are found in one or more copies in HMG-box proteins, which form a large, diverse family involved in the regulation of DNA-dependent processes such as transcription, replication, and strand repair, all of which require the bending and unwinding of chromatin. obo:GO_0071837 obo:go.owl obo:GO_0071837 midori obo:GO_0071837 2010-09-10T12:05:45Z obo:GO_0071837 molecular_function obo:GO_0071837 GO:0071837 obo:GO_0071837 HMG box domain binding obo:GO_0071855 Interacting selectively and non-covalently with a neuropeptide receptor. obo:GO_0071855 obo:go.owl obo:GO_0071855 midori obo:GO_0071855 2010-09-10T03:21:43Z obo:GO_0071855 molecular_function obo:GO_0071855 GO:0071855 obo:GO_0071855 neuropeptide receptor binding obo:GO_0071857 Interacting selectively and non-covalently with a beta-endorphin receptor. obo:GO_0071857 obo:go.owl obo:GO_0071857 midori obo:GO_0071857 2010-09-10T03:23:01Z obo:GO_0071857 molecular_function obo:GO_0071857 GO:0071857 obo:GO_0071857 beta-endorphin receptor binding obo:GO_0071858 Interacting selectively and non-covalently with a corazonin receptor. obo:GO_0071858 obo:go.owl obo:GO_0071858 midori obo:GO_0071858 2010-09-10T03:23:40Z obo:GO_0071858 molecular_function obo:GO_0071858 GO:0071858 obo:GO_0071858 corazonin receptor binding obo:GO_0071859 Interacting selectively and non-covalently with a neuropeptide F receptor. obo:GO_0071859 obo:go.owl obo:GO_0071859 midori obo:GO_0071859 2010-09-10T03:23:56Z obo:GO_0071859 molecular_function obo:GO_0071859 GO:0071859 obo:GO_0071859 neuropeptide F receptor binding obo:GO_0071860 Interacting selectively and non-covalently with a proctolin receptor. obo:GO_0071860 obo:go.owl obo:GO_0071860 midori obo:GO_0071860 2010-09-10T03:24:19Z obo:GO_0071860 molecular_function obo:GO_0071860 GO:0071860 obo:GO_0071860 proctolin receptor binding obo:GO_0071861 Interacting selectively and non-covalently with a tachykinin receptor. obo:GO_0071861 obo:go.owl obo:GO_0071861 midori obo:GO_0071861 2010-09-10T03:24:34Z obo:GO_0071861 molecular_function obo:GO_0071861 GO:0071861 obo:GO_0071861 tachykinin receptor binding obo:GO_0071863 A process that modulates the frequency, rate or extent of cell proliferation in the bone marrow. obo:GO_0071863 obo:go.owl obo:GO_0071863 midori obo:GO_0071863 2010-09-13T02:11:08Z obo:GO_0071863 regulation of bone marrow cell proliferation obo:GO_0071863 biological_process obo:GO_0071863 GO:0071863 obo:GO_0071863 regulation of cell proliferation in bone marrow obo:GO_0071864 A process that activates or increases the frequency, rate or extent of cell proliferation in the bone marrow. obo:GO_0071864 obo:go.owl obo:GO_0071864 midori obo:GO_0071864 2010-09-13T02:12:36Z obo:GO_0071864 positive regulation of bone marrow cell proliferation obo:GO_0071864 up regulation of cell proliferation in bone marrow obo:GO_0071864 up-regulation of cell proliferation in bone marrow obo:GO_0071864 upregulation of cell proliferation in bone marrow obo:GO_0071864 activation of cell proliferation in bone marrow obo:GO_0071864 stimulation of cell proliferation in bone marrow obo:GO_0071864 biological_process obo:GO_0071864 GO:0071864 obo:GO_0071864 positive regulation of cell proliferation in bone marrow obo:GO_0071889 Interacting selectively and non-covalently with a 14-3-3 protein. A 14-3-3 protein is any of a large family of approximately 30kDa acidic proteins which exist primarily as homo- and heterodimers within all eukaryotic cells, and have been implicated in the modulation of distinct biological processes by binding to specific phosphorylated sites on diverse target proteins, thereby forcing conformational changes or influencing interactions between their targets and other molecules. Each 14-3-3 protein sequence can be roughly divided into three sections: a divergent amino terminus, the conserved core region and a divergent carboxy-terminus. The conserved middle core region of the 14-3-3s encodes an amphipathic groove that forms the main functional domain, a cradle for interacting with client proteins. obo:GO_0071889 obo:go.owl obo:GO_0071889 midori obo:GO_0071889 2010-09-14T01:21:50Z obo:GO_0071889 molecular_function obo:GO_0071889 GO:0071889 obo:GO_0071889 14-3-3 protein binding obo:GO_0071890 Interacting selectively and non-covalently with bicarbonate (CHO3-) ions. obo:GO_0071890 obo:go.owl obo:GO_0071890 midori obo:GO_0071890 2010-09-14T01:47:43Z obo:GO_0071890 hydrogencarbonate binding obo:GO_0071890 molecular_function obo:GO_0071890 GO:0071890 obo:GO_0071890 bicarbonate binding obo:GO_0071897 The cellular DNA metabolic process resulting in the formation of DNA, deoxyribonucleic acid, one of the two main types of nucleic acid, consisting of a long unbranched macromolecule formed from one or two strands of linked deoxyribonucleotides, the 3'-phosphate group of each constituent deoxyribonucleotide being joined in 3',5'-phosphodiester linkage to the 5'-hydroxyl group of the deoxyribose moiety of the next one. obo:GO_0071897 obo:go.owl obo:GO_0071897 midori obo:GO_0071897 2010-09-15T02:14:33Z obo:GO_0071897 DNA anabolism obo:GO_0071897 DNA biosynthesis obo:GO_0071897 DNA formation obo:GO_0071897 DNA synthesis obo:GO_0071897 biological_process obo:GO_0071897 GO:0071897 obo:GO_0071897 DNA biosynthetic process obo:GO_0071906 Interacting selectively and non-covalently with a CRD (context dependent regulatory) domain, a domain of about 130 residues that is the most divergent region among the LEF/TCF proteins. obo:GO_0071906 obo:go.owl obo:GO_0071906 midori obo:GO_0071906 2010-09-21T04:08:53Z obo:GO_0071906 context dependent regulatory domain binding obo:GO_0071906 molecular_function obo:GO_0071906 GO:0071906 obo:GO_0071906 CRD domain binding obo:GO_0071933 Interacting selectively and non-covalently with an Arp2/3 complex, a protein complex that contains two actin-related proteins, Arp2 and Arp3, and five novel proteins (ARPC1-5). obo:GO_0071933 obo:go.owl obo:GO_0071933 midori obo:GO_0071933 2010-09-29T02:48:41Z obo:GO_0071933 molecular_function obo:GO_0071933 GO:0071933 obo:GO_0071933 Arp2/3 complex binding obo:GO_0071949 Interacting selectively and non-covalently with the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. obo:GO_0071949 obo:go.owl obo:GO_0071949 midori obo:GO_0071949 2010-10-07T12:30:28Z obo:GO_0071949 oxidized flavin adenine dinucleotide binding obo:GO_0071949 oxidized flavine-adenine dinucleotide binding obo:GO_0071949 molecular_function obo:GO_0071949 GO:0071949 obo:GO_0071949 FAD binding obo:GO_0071950 Interacting selectively and non-covalently with the reduced form, FADH2, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. obo:GO_0071950 obo:go.owl obo:GO_0071950 midori obo:GO_0071950 2010-10-07T12:31:34Z obo:GO_0071950 reduced flavin adenine dinucleotide binding obo:GO_0071950 reduced flavine-adenine dinucleotide binding obo:GO_0071950 molecular_function obo:GO_0071950 GO:0071950 obo:GO_0071950 FADH2 binding obo:GO_0071987 Interacting selectively and non-covalently with a WD40 repeat domain of a protein. The WD40 repeat is a short structural motif of approximately 40 amino acids, often terminating in a tryptophan-aspartic acid (W-D) dipeptide. Several of these repeats are combined to form a type of protein domain called the WD domain. obo:GO_0071987 obo:go.owl obo:GO_0071987 midori obo:GO_0071987 2010-10-22T02:53:29Z obo:GO_0071987 WD domain binding obo:GO_0071987 beta-transducin repeat domain binding obo:GO_0071987 molecular_function obo:GO_0071987 GO:0071987 obo:GO_0071987 WD40-repeat domain binding obo:GO_0072042 Any process that modulates the frequency, rate or extent of mesenchymal stem cell proliferation and contributes to the shaping of a nephron. obo:GO_0072042 obo:go.owl obo:GO_0072042 midori obo:GO_0072042 2010-01-25T03:11:26Z obo:GO_0072042 biological_process obo:GO_0072042 GO:0072042 obo:GO_0072042 regulation of mesenchymal stem cell proliferation involved in nephron morphogenesis obo:GO_0072091 Any process that modulates the frequency, rate or extent of stem cell proliferation. A stem cell is a cell that retains the ability to divide and proliferate throughout life to provide progenitor cells that can differentiate into specialized cells. obo:GO_0072091 obo:go.owl obo:GO_0072091 midori obo:GO_0072091 2010-02-08T02:09:03Z obo:GO_0072091 biological_process obo:GO_0072091 GO:0072091 obo:GO_0072091 regulation of stem cell proliferation obo:GO_0072201 Any process that decreases the frequency, rate or extent of mesenchymal cell proliferation. A mesenchymal cell is a cell that normally gives rise to other cells that are organized as three-dimensional masses, rather than sheets. obo:GO_0072201 obo:go.owl obo:GO_0072201 midori obo:GO_0072201 2010-03-01T03:43:29Z obo:GO_0072201 biological_process obo:GO_0072201 GO:0072201 obo:GO_0072201 negative regulation of mesenchymal cell proliferation obo:GO_0072341 Interacting selectively and non-covalently with a modified amino acid. obo:GO_0072341 obo:go.owl obo:GO_0072341 midori obo:GO_0072341 2010-11-04T05:45:32Z obo:GO_0072341 amino acid derivative binding obo:GO_0072341 molecular_function obo:GO_0072341 GO:0072341 obo:GO_0072341 modified amino acid binding obo:GO_0072342 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of anion stress, an increase or decrease in the concentration of negatively charged ions in the environment. obo:GO_0072342 obo:go.owl obo:GO_0072342 midori obo:GO_0072342 2010-11-05T02:25:28Z obo:GO_0072342 biological_process obo:GO_0072342 GO:0072342 obo:GO_0072342 response to anion stress obo:GO_0072354 Catalysis of the transfer of a phosphate group to the threonine-3 residue of the N-terminal tail of histone H3. obo:GO_0072354 obo:go.owl obo:GO_0072354 midori obo:GO_0072354 2010-11-12T04:27:57Z obo:GO_0072354 histone threonine kinase activity (H3-T3 specific) obo:GO_0072354 histone-threonine kinase activity (H3-T3 specific) obo:GO_0072354 molecular_function obo:GO_0072354 GO:0072354 obo:GO_0072354 histone kinase activity (H3-T3 specific) obo:GO_0072371 Catalysis of the transfer of a phosphate group to the serine-121 residue of the N-terminal tail of histone H2A. obo:GO_0072371 obo:go.owl obo:GO_0072371 midori obo:GO_0072371 2010-11-16T03:42:59Z obo:GO_0072371 histone serine kinase activity (H2A-S121 specific) obo:GO_0072371 histone-serine kinase activity (H2A-S121 specific) obo:GO_0072371 molecular_function obo:GO_0072371 GO:0072371 obo:GO_0072371 histone kinase activity (H2A-S121 specific) obo:GO_0072421 The series of events in which information about damage to DNA is received and converted into a molecular signal, contributing to a DNA damage checkpoint. obo:GO_0072421 obo:go.owl obo:GO_0072421 midori obo:GO_0072421 2010-12-08T04:16:04Z obo:GO_0072421 biological_process obo:GO_0072421 DNA damage checkpoint sensor mechanism obo:GO_0072421 DNA damage checkpoint sensor process obo:GO_0072421 sensing involved in DNA damage checkpoint obo:GO_0072421 GO:0072421 obo:GO_0072421 detection of DNA damage stimulus involved in DNA damage checkpoint obo:GO_0072424 The series of events in which information about damage to DNA is received and converted into a molecular signal, contributing to a G2/M transition DNA damage checkpoint. obo:GO_0072424 obo:go.owl obo:GO_0072424 midori obo:GO_0072424 2010-12-08T04:24:59Z obo:GO_0072424 detection of DNA damage stimulus involved in G2/M transition DNA damage checkpoint obo:GO_0072424 biological_process obo:GO_0072424 G2/M transition DNA damage checkpoint sensor mechanism obo:GO_0072424 G2/M transition DNA damage checkpoint sensor process obo:GO_0072424 sensing involved in G2/M transition DNA damage checkpoint obo:GO_0072424 GO:0072424 obo:GO_0072424 detection of DNA damage stimulus involved in G2 DNA damage checkpoint obo:GO_0072436 The series of events in which information about whether DNA replication is complete is received and converted into a molecular signal, contributing to a DNA replication checkpoint. obo:GO_0072436 obo:go.owl obo:GO_0072436 midori obo:GO_0072436 2010-12-08T04:52:09Z obo:GO_0072436 biological_process obo:GO_0072436 DNA replication checkpoint sensor mechanism obo:GO_0072436 DNA replication checkpoint sensor process obo:GO_0072436 sensing involved in DNA replication checkpoint obo:GO_0072436 GO:0072436 obo:GO_0072436 detection of stimulus involved in DNA replication checkpoint obo:GO_0072511 The directed movement of inorganic cations with a valency of two into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Inorganic cations are atoms or small molecules with a positive charge which do not contain carbon in covalent linkage. obo:GO_0072511 obo:go.owl obo:GO_0072511 midori obo:GO_0072511 2010-12-16T04:11:02Z obo:GO_0072511 biological_process obo:GO_0072511 GO:0072511 obo:GO_0072511 divalent inorganic cation transport obo:GO_0072518 Catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein. This reaction requires binding of the GTPase Rho. obo:GO_0072518 obo:go.owl obo:GO_0072518 midori obo:GO_0072518 2010-12-22T11:07:29Z obo:GO_0072518 ROCK kinase activity obo:GO_0072518 Rho-associated protein kinase activity obo:GO_0072518 molecular_function obo:GO_0072518 GO:0072518 obo:GO_0072518 Rho-dependent protein serine/threonine kinase activity obo:GO_0072544 Interacting selectively and non-covalently with L-DOPA, the modified amino acid (2S)-2-amino-3-(3,4-dihydroxyphenyl)propanoic acid. obo:GO_0072544 obo:go.owl obo:GO_0072544 midori obo:GO_0072544 2011-01-19T05:40:04Z obo:GO_0072544 L-dopa binding obo:GO_0072544 molecular_function obo:GO_0072544 GO:0072544 obo:GO_0072544 L-DOPA binding obo:GO_0072545 Interacting selectively and non-covalently with2-amino-3-(4-hydroxyphenyl)propanoic acid. obo:GO_0072545 obo:go.owl obo:GO_0072545 midori obo:GO_0072545 2011-01-19T05:43:55Z obo:GO_0072545 Tyr binding obo:GO_0072545 molecular_function obo:GO_0072545 GO:0072545 obo:GO_0072545 tyrosine binding obo:GO_0072570 Interacting selectively and non-covalently with ADP-D-ribose, an ADP-aldose having ribose as the aldose fragment. obo:GO_0072570 obo:go.owl obo:GO_0072570 midori obo:GO_0072570 2011-01-31T02:37:30Z obo:GO_0072570 ADP-ribose binding obo:GO_0072570 molecular_function obo:GO_0072570 GO:0072570 obo:GO_0072570 ADP-D-ribose binding obo:GO_0072571 Interacting selectively and non-covalently with monomeric ADP-D-ribose, an ADP-aldose having ribose as the aldose fragment. obo:GO_0072571 obo:go.owl obo:GO_0072571 midori obo:GO_0072571 2011-01-31T02:39:12Z obo:GO_0072571 mono-ADP-ribose binding obo:GO_0072571 mADPr binding obo:GO_0072571 molecular_function obo:GO_0072571 GO:0072571 obo:GO_0072571 mono-ADP-D-ribose binding obo:GO_0072572 Interacting selectively and non-covalently with polymeric ADP-D-ribose, a polymer that is composed of poly-ADP-D-ribose units linked through 1,2-glycosidic bonds at the ribose ring. obo:GO_0072572 obo:go.owl obo:GO_0072572 midori obo:GO_0072572 2011-01-31T02:49:04Z obo:GO_0072572 poly-ADP-ribose binding obo:GO_0072572 pADPr binding obo:GO_0072572 molecular_function obo:GO_0072572 GO:0072572 obo:GO_0072572 poly-ADP-D-ribose binding obo:GO_0072706 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a sodium dodecyl sulfate (SDS) stimulus. obo:GO_0072706 obo:go.owl obo:GO_0072706 midori obo:GO_0072706 2012-04-11T03:35:07Z obo:GO_0072706 response to SDS obo:GO_0072706 biological_process obo:GO_0072706 GO:0072706 obo:GO_0072706 response to sodium dodecyl sulfate obo:GO_0072707 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a sodium dodecyl sulfate (SDS) stimulus. obo:GO_0072707 obo:go.owl obo:GO_0072707 midori obo:GO_0072707 2012-04-11T03:35:15Z obo:GO_0072707 cellular response to SDS obo:GO_0072707 biological_process obo:GO_0072707 GO:0072707 obo:GO_0072707 cellular response to sodium dodecyl sulfate obo:GO_0072730 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a papulacandin B stimulus. obo:GO_0072730 obo:go.owl obo:GO_0072730 midori obo:GO_0072730 2012-05-31T11:30:32Z obo:GO_0072730 biological_process obo:GO_0072730 GO:0072730 obo:GO_0072730 response to papulacandin B obo:GO_0072731 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a papulacandin B stimulus. obo:GO_0072731 obo:go.owl obo:GO_0072731 midori obo:GO_0072731 2012-05-31T11:30:39Z obo:GO_0072731 biological_process obo:GO_0072731 GO:0072731 obo:GO_0072731 cellular response to papulacandin B obo:GO_0072732 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of calcium ions. obo:GO_0072732 obo:go.owl obo:GO_0072732 midori obo:GO_0072732 2012-07-06T02:42:26Z obo:GO_0072732 cellular response to calcium starvation obo:GO_0072732 biological_process obo:GO_0072732 GO:0072732 obo:GO_0072732 cellular response to calcium ion starvation obo:GO_0072735 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a tert-butyl hydroperoxide (t-BOOH) stimulus. obo:GO_0072735 obo:go.owl obo:GO_0072735 midori obo:GO_0072735 2012-07-17T10:33:00Z obo:GO_0072735 response to 2-methyl-prop-2-yl-hydroperoxide obo:GO_0072735 response to tert-butyl hydroperoxide obo:GO_0072735 biological_process obo:GO_0072735 GO:0072735 obo:GO_0072735 response to t-BOOH obo:GO_0072736 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a tert-butyl hydroperoxide (t-BOOH) stimulus. obo:GO_0072736 obo:go.owl obo:GO_0072736 midori obo:GO_0072736 2012-07-17T10:33:00Z obo:GO_0072736 cellular response to 2-methyl-prop-2-yl-hydroperoxide obo:GO_0072736 cellular response to tert-butyl hydroperoxide obo:GO_0072736 biological_process obo:GO_0072736 GO:0072736 obo:GO_0072736 cellular response to t-BOOH obo:GO_0072744 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a trichodermin stimulus. obo:GO_0072744 obo:go.owl obo:GO_0072744 midori obo:GO_0072744 2012-08-31T12:29:38Z obo:GO_0072744 biological_process obo:GO_0072744 GO:0072744 obo:GO_0072744 cellular response to trichodermin obo:GO_0072746 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a tetracycline stimulus. obo:GO_0072746 obo:go.owl obo:GO_0072746 midori obo:GO_0072746 2012-08-31T12:32:43Z obo:GO_0072746 biological_process obo:GO_0072746 GO:0072746 obo:GO_0072746 cellular response to tetracycline obo:GO_0080025 Interacting selectively and non-covalently with phosphatidylinositol-3,5-bisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3' and 5' positions. obo:GO_0080025 obo:go.owl obo:GO_0080025 PtdIns(3,5)P2 binding obo:GO_0080025 molecular_function obo:GO_0080025 GO:0080025 obo:GO_0080025 phosphatidylinositol-3,5-bisphosphate binding obo:GO_0080084 Interacting selectively and non-covalently with the 5S rDNA sequence encoding ribosomal 5S rRNA, which is individually transcribed by RNA polymerase III, rather than by RNA polymerase I, in species where it exists. obo:GO_0080084 obo:go.owl obo:GO_0080084 donghui obo:GO_0080084 2009-04-22T02:32:20Z obo:GO_0080084 molecular_function obo:GO_0080084 GO:0080084 obo:GO_0080084 5S rDNA binding obo:GO_0080115 Interacting selectively and non-covalently with the tail region of a myosin XI heavy chain. obo:GO_0080115 obo:go.owl obo:GO_0080115 donghui obo:GO_0080115 2009-04-27T03:31:45Z obo:GO_0080115 molecular_function obo:GO_0080115 GO:0080115 obo:GO_0080115 myosin XI tail binding obo:GO_0080157 Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving plant-type cell wall organization or biogenesis. Plant-type cell wall organization or biogenesis is a process that results in the biosynthesis of constituent macromolecules, assembly, arrangement of constituent parts, or disassembly of a cellulose- and pectin-containing cell wall. obo:GO_0080157 obo:go.owl obo:GO_0080157 donghui obo:GO_0080157 2010-09-01T04:02:37Z obo:GO_0080157 regulation of plant-type cell wall organisation or biogenesis obo:GO_0080157 biological_process obo:GO_0080157 GO:0080157 obo:GO_0080157 regulation of plant-type cell wall organization or biogenesis obo:GO_0080160 The directed movement of selenate into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_0080160 obo:go.owl obo:GO_0080160 donghui obo:GO_0080160 2010-09-01T04:17:38Z obo:GO_0080160 biological_process obo:GO_0080160 GO:0080160 obo:GO_0080160 selenate transport obo:GO_0080167 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a karrikin stimulus. Karrikins are signaling molecules in smoke from burning vegetation that trigger seed germination for many angiosperms (flowering plants). obo:GO_0080167 obo:go.owl obo:GO_0080167 donghui obo:GO_0080167 2010-09-23T05:07:22Z obo:GO_0080167 biological_process obo:GO_0080167 GO:0080167 obo:GO_0080167 response to karrikin obo:GO_0086080 Interacting selectively and non-covalently with any protein or protein complex contributing to the adhesion of two different types of cells. obo:GO_0086080 obo:go.owl obo:GO_0086080 dph obo:GO_0086080 2011-11-22T10:53:52Z obo:GO_0086080 molecular_function obo:GO_0086080 GO:0086080 obo:GO_0086080 protein binding involved in heterotypic cell-cell adhesion obo:GO_0086081 Interacting selectively and non-covalently with any protein or protein complex that results in the connection of an atrial cardiomyocyte with an AV node cell and contributes to the communication between the two cells. obo:GO_0086081 obo:go.owl obo:GO_0086081 dph obo:GO_0086081 2011-11-22T11:00:47Z obo:GO_0086081 cell adhesive protein binding involved in atrial cardiomyocyte-AV node cell communication obo:GO_0086081 cell adhesive protein binding involved in atrial cardiomyocyte-atrioventricular node cell communication obo:GO_0086081 molecular_function obo:GO_0086081 GO:0086081 obo:GO_0086081 cell adhesive protein binding involved in atrial cardiac muscle cell-AV node cell communication obo:GO_0086082 Interacting selectively and non-covalently with any protein or protein complex that results in the connection of an AV node cell with a bundle of His cell and contributes to the communication between the two cells. obo:GO_0086082 obo:go.owl obo:GO_0086082 dph obo:GO_0086082 2011-11-22T11:09:37Z obo:GO_0086082 cell adhesive protein binding involved in atrioventricular node cell-bundle of His cell communication obo:GO_0086082 molecular_function obo:GO_0086082 GO:0086082 obo:GO_0086082 cell adhesive protein binding involved in AV node cell-bundle of His cell communication obo:GO_0086083 Interacting selectively and non-covalently with any protein or protein complex that results in the connection of a bundle of His cell with a Purkinje myocyte and contributes to the communication between the two cells. obo:GO_0086083 obo:go.owl obo:GO_0086083 dph obo:GO_0086083 2011-11-22T11:11:03Z obo:GO_0086083 molecular_function obo:GO_0086083 GO:0086083 obo:GO_0086083 cell adhesive protein binding involved in bundle of His cell-Purkinje myocyte communication obo:GO_0086084 Interacting selectively and non-covalently with any protein or protein complex that results in the connection of a Purkinje myocyte with an ventricular cardiac muscle cell and contributes to the communication between the two cells. obo:GO_0086084 obo:go.owl obo:GO_0086084 dph obo:GO_0086084 2011-11-22T11:13:16Z obo:GO_0086084 molecular_function obo:GO_0086084 GO:0086084 obo:GO_0086084 cell adhesive protein binding involved in Purkinje myocyte-ventricular cardiac muscle cell communication obo:GO_0086085 Interacting selectively and non-covalently with any protein or protein complex that results in the connection of an SA cardiomyocyte with an atrial cardiomyocyte and contributes to the communication between the two cells. obo:GO_0086085 obo:go.owl obo:GO_0086085 dph obo:GO_0086085 2011-11-22T11:15:07Z obo:GO_0086085 cell adhesive protein binding involved in SA cardiomyocyte-atrial cardiomyocyte communication obo:GO_0086085 molecular_function obo:GO_0086085 GO:0086085 obo:GO_0086085 cell adhesive protein binding involved in SA cardiac muscle cell-atrial cardiac muscle cell communication obo:GO_0089710 Interacting selectively and non-covalently with a endocytic signal sequence, a specific peptide sequence, of 4-6 amino acids with an essential tyrosine (Y), found on cytoplasmic tails of some cell surface membrane proteins, which directs internalization by clathrin-coated pits. obo:GO_0089710 obo:go.owl obo:GO_0089710 molecular_function obo:GO_0089710 GO:0089710 obo:GO_0089710 endocytic targeting sequence binding obo:GO_0089719 Interacting selectively and non-covalently with an RHG (reaper/hid/grimm) domain/motif (AKA iap binding motif). obo:GO_0089719 obo:go.owl obo:GO_0089719 RHG domain binding obo:GO_0089719 iap binding domain binding obo:GO_0089719 inhibitor of apoptosis binding domain binding obo:GO_0089719 reaper hid grim domain binding obo:GO_0089719 molecular_function obo:GO_0089719 GO:0089719 obo:GO_0089719 RHG protein domain binding obo:GO_0089720 Interacting selectively and non-covalently with a caspase family protein. obo:GO_0089720 obo:go.owl obo:GO_0089720 molecular_function obo:GO_0089720 GO:0089720 obo:GO_0089720 caspase binding obo:GO_0090069 Any process that modulates the rate, frequency or extent of ribosome biogenesis. Ribosome biogenesis is the cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of ribosome subunits. obo:GO_0090069 obo:go.owl obo:GO_0090069 tanyaberardini obo:GO_0090069 2009-09-11T10:32:17Z obo:GO_0090069 biological_process obo:GO_0090069 GO:0090069 obo:GO_0090069 regulation of ribosome biogenesis obo:GO_0090070 Any process that increases the rate, frequency or extent of ribosome biogenesis. Ribosome biogenesis is the cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of ribosome subunits. obo:GO_0090070 obo:go.owl obo:GO_0090070 tanyaberardini obo:GO_0090070 2009-09-11T10:32:17Z obo:GO_0090070 biological_process obo:GO_0090070 GO:0090070 obo:GO_0090070 positive regulation of ribosome biogenesis obo:GO_0090071 Any process that decreases the rate, frequency or extent of ribosome biogenesis. Ribosome biogenesis is the cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of ribosome subunits. obo:GO_0090071 obo:go.owl obo:GO_0090071 tanyaberardini obo:GO_0090071 2009-09-11T10:32:17Z obo:GO_0090071 biological_process obo:GO_0090071 GO:0090071 obo:GO_0090071 negative regulation of ribosome biogenesis obo:GO_0090165 The asymmetric formation of a continuous ribbon of interconnected Golgi stacks of flat cisternae that modulates the controlled release of a substance from a polarized epithelial cell. obo:GO_0090165 obo:go.owl obo:GO_0090165 tanyaberardini obo:GO_0090165 2009-12-08T09:05:16Z obo:GO_0090165 biological_process obo:GO_0090165 GO:0090165 obo:GO_0090165 regulation of secretion by asymmetric Golgi ribbon formation obo:GO_0090279 Any process that modulates the rate, frequency, or extent of the directed movement of calcium ions into a cell or organelle. obo:GO_0090279 obo:go.owl obo:GO_0090279 tanyaberardini obo:GO_0090279 2010-02-08T05:11:20Z obo:GO_0090279 biological_process obo:GO_0090279 regulation of transmembrane calcium influx obo:GO_0090279 GO:0090279 obo:GO_0090279 regulation of calcium ion import obo:GO_0090280 Any process that increases the rate, frequency, or extent of the directed movement of calcium ions into a cell or organelle. obo:GO_0090280 obo:go.owl obo:GO_0090280 tanyaberardini obo:GO_0090280 2010-02-08T05:11:20Z obo:GO_0090280 biological_process obo:GO_0090280 positive regulation of transmembrane calcium influx obo:GO_0090280 GO:0090280 obo:GO_0090280 positive regulation of calcium ion import obo:GO_0090281 Any process that decreases the rate, frequency, or extent of the directed movement of calcium ions into a cell or organelle. obo:GO_0090281 obo:go.owl obo:GO_0090281 tanyaberardini obo:GO_0090281 2010-02-08T05:11:20Z obo:GO_0090281 biological_process obo:GO_0090281 negative regulation of transmembrane calcium influx obo:GO_0090281 GO:0090281 obo:GO_0090281 negative regulation of calcium ion import obo:GO_0090289 Any process that modulates the rate, frequency, or extent of the multiplication or reproduction of osteoclasts, resulting in the expansion of an osteoclast cell population. obo:GO_0090289 obo:go.owl obo:GO_0090289 tanyaberardini obo:GO_0090289 2010-02-18T03:11:03Z obo:GO_0090289 biological_process obo:GO_0090289 GO:0090289 obo:GO_0090289 regulation of osteoclast proliferation obo:GO_0090290 Any process that increases the rate, frequency, or extent of the multiplication or reproduction of osteoclasts, resulting in the expansion of an osteoclast cell population. obo:GO_0090290 obo:go.owl obo:GO_0090290 tanyaberardini obo:GO_0090290 2010-02-18T03:11:03Z obo:GO_0090290 biological_process obo:GO_0090290 GO:0090290 obo:GO_0090290 positive regulation of osteoclast proliferation obo:GO_0090291 Any process that decreases the rate, frequency, or extent of the multiplication or reproduction of osteoclasts, resulting in the expansion of an osteoclast cell population. obo:GO_0090291 obo:go.owl obo:GO_0090291 tanyaberardini obo:GO_0090291 2010-02-18T03:11:03Z obo:GO_0090291 biological_process obo:GO_0090291 GO:0090291 obo:GO_0090291 negative regulation of osteoclast proliferation obo:GO_0090304 Any cellular metabolic process involving nucleic acids. obo:GO_0090304 obo:go.owl obo:GO_0090304 tanyaberardini obo:GO_0090304 2010-04-07T10:18:47Z obo:GO_0090304 biological_process obo:GO_0090304 GO:0090304 obo:GO_0090304 nucleic acid metabolic process obo:GO_0090408 The process of loading nitrate into the sieve tube or companion cell of the phloem for long distance transport from source to sink. obo:GO_0090408 obo:go.owl obo:GO_0090408 tanyaberardini obo:GO_0090408 2011-06-01T10:06:21Z obo:GO_0090408 biological_process obo:GO_0090408 GO:0090408 obo:GO_0090408 phloem nitrate loading obo:GO_0090411 Interacting selectively and non-covalently with a brassinosteroid. obo:GO_0090411 obo:go.owl obo:GO_0090411 tanyaberardini obo:GO_0090411 2011-08-11T02:25:30Z obo:GO_0090411 molecular_function obo:GO_0090411 GO:0090411 obo:GO_0090411 brassinosteroid binding obo:GO_0090452 The directed movement of lithium ions across a membrane. obo:GO_0090452 obo:go.owl obo:GO_0090452 tanyaberardini obo:GO_0090452 2012-09-24T14:04:41Z obo:GO_0090452 lithium ion uptake obo:GO_0090452 lithium ion import obo:GO_0090452 biological_process obo:GO_0090452 GO:0090452 obo:GO_0090452 lithium ion transmembrane transport obo:GO_0090488 Interacting selectively and non-covalently with a polo box domain of a protein. The polo box domain is involved in binding substrates of polo kinases. obo:GO_0090488 obo:go.owl obo:GO_0090488 tanyaberardini obo:GO_0090488 2012-10-16T10:47:30Z obo:GO_0090488 molecular_function obo:GO_0090488 GO:0090488 obo:GO_0090488 polo box domain specific binding obo:GO_0090541 Interacting selectively and non-covalently with the MIT domain of a protein. The MIT domain is found in vacuolar sorting proteins, spastin (probable ATPase involved in the assembly or function of nuclear protein complexes), and a sorting nexin, which may play a role in intracellular trafficking. obo:GO_0090541 obo:go.owl obo:GO_0090541 tanyaberardini obo:GO_0090541 2013-02-14T17:11:29Z obo:GO_0090541 molecular_function obo:GO_0090541 GO:0090541 obo:GO_0090541 MIT domain binding obo:GO_0090542 Interacting selectively and non-covalently with the ELYC domain of a protein. The ELYC domain is an approximately 150 amino acid sequence which contains a highly conserved tetrapeptide sequence, ELYC. obo:GO_0090542 obo:go.owl obo:GO_0090542 tanyaberardini obo:GO_0090542 2013-02-14T17:11:29Z obo:GO_0090542 molecular_function obo:GO_0090542 GO:0090542 obo:GO_0090542 ELYC domain binding obo:GO_0090546 The process by which excess light energy absorbed by chlorophyll and not used to drive photosynthesis is re-emitted as light. obo:GO_0090546 obo:go.owl obo:GO_0090546 tanyaberardini obo:GO_0090546 2013-03-27T14:23:27Z obo:GO_0090546 biological_process obo:GO_0090546 GO:0090546 obo:GO_0090546 chlorophyll fluorescence obo:GO_0090548 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a starvation stimulus, deprivation of nitrate. obo:GO_0090548 obo:go.owl obo:GO_0090548 tanyaberardini obo:GO_0090548 2013-04-22T13:57:16Z obo:GO_0090548 biological_process obo:GO_0090548 GO:0090548 obo:GO_0090548 response to nitrate starvation obo:GO_0090549 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a starvation stimulus, deprivation of a carbon source. obo:GO_0090549 obo:go.owl obo:GO_0090549 tanyaberardini obo:GO_0090549 2013-04-22T13:57:16Z obo:GO_0090549 biological_process obo:GO_0090549 GO:0090549 obo:GO_0090549 response to carbon starvation obo:GO_0090551 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a starvation stimulus, deprivation of manganese. obo:GO_0090551 obo:go.owl obo:GO_0090551 tanyaberardini obo:GO_0090551 2013-04-22T13:57:16Z obo:GO_0090551 biological_process obo:GO_0090551 GO:0090551 obo:GO_0090551 response to manganese starvation obo:GO_0090593 The phosphorylation by a protein of one or more of its own histidine residues, or a histidine residue on an identical protein. obo:GO_0090593 obo:go.owl obo:GO_0090593 tanyaberardini obo:GO_0090593 2014-06-06T14:19:46Z obo:GO_0090593 biological_process obo:GO_0090593 GO:0090593 obo:GO_0090593 peptidyl-histidine autophosphorylation obo:GO_0090648 Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of the provision of a combination of complex inanimate and social stimulations in the organism's housing environment. obo:GO_0090648 obo:go.owl obo:GO_0090648 tanyaberardini obo:GO_0090648 2015-07-01T10:20:37Z obo:GO_0090648 response to the introduction of novel objects obo:GO_0090648 biological_process obo:GO_0090648 GO:0090648 obo:GO_0090648 response to environmental enrichment obo:GO_0090649 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of the deprivation of oxygen and glucose. obo:GO_0090649 obo:go.owl obo:GO_0090649 tanyaberardini obo:GO_0090649 2015-07-01T10:27:29Z obo:GO_0090649 response to OGD obo:GO_0090649 biological_process obo:GO_0090649 GO:0090649 obo:GO_0090649 response to oxygen-glucose deprivation obo:GO_0090650 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of the deprivation of oxygen and glucose. obo:GO_0090650 obo:go.owl obo:GO_0090650 tanyaberardini obo:GO_0090650 2015-07-01T10:27:29Z obo:GO_0090650 cellular response to OGD obo:GO_0090650 biological_process obo:GO_0090650 GO:0090650 obo:GO_0090650 cellular response to oxygen-glucose deprivation obo:GO_0090655 Interacting selectively and non-covalently with the junction formed at the point where double-stranded telomeric DNA becomes a single-stranded G-rich telomeric DNA 3' overhang. obo:GO_0090655 obo:go.owl obo:GO_0090655 tanyaberardini obo:GO_0090655 2015-07-02T11:33:39Z obo:GO_0090655 molecular_function obo:GO_0090655 GO:0090655 obo:GO_0090655 double-stranded/single-stranded junction telomeric DNA binding obo:GO_0090676 A process in which a calcium ion is transported from one side of a membrane to the other by means of a low voltage-gated calcium channel. obo:GO_0090676 obo:go.owl obo:GO_0090676 tanyaberardini obo:GO_0090676 2016-03-23T10:15:23Z obo:GO_0090676 biological_process obo:GO_0090676 generation of T-type calcium current obo:GO_0090676 GO:0090676 obo:GO_0090676 calcium ion transmembrane transport via low voltage-gated calcium channel obo:GO_0090722 The aggregation, arrangement and bonding together of two or more different receptor complexes that individually undergo combination with a hormone, neurotransmitter, drug or intracellular messenger to form a higher level receptor complex. The formation of the higher level complex initiates a change in cell function. obo:GO_0090722 obo:go.owl obo:GO_0090722 tanyaberardini obo:GO_0090722 2016-11-11T17:41:56Z obo:GO_0090722 hetero-receptor complex formation obo:GO_0090722 molecular_function obo:GO_0090722 GO:0090722 obo:GO_0090722 receptor-receptor interaction obo:GO_0090736 Interacting selectively and non-covalently with a meprin and TRAF homology (MATH) domain. obo:GO_0090736 obo:go.owl obo:GO_0090736 tanyaberardini obo:GO_0090736 2017-02-06T17:08:28Z obo:GO_0090736 molecular_function obo:GO_0090736 GO:0090736 obo:GO_0090736 MATH domain binding obo:GO_0097001 Interacting selectively and non-covalently with any ceramide, a class of lipids that is composed of sphingosine linked to a fatty acid. Ceramides are a major component of cell membranes. obo:GO_0097001 obo:go.owl obo:GO_0097001 paola obo:GO_0097001 2011-03-09T11:34:09Z obo:GO_0097001 molecular_function obo:GO_0097001 GO:0097001 obo:GO_0097001 ceramide binding obo:GO_0097004 Interacting selectively and non-covalently with an adipokinetic hormone. Adipokinetic hormones (AKHs) are peptide hormones that are involved in the mobilization of sugar and lipids from the insect fat body during energy-requiring activities such as flight and locomotion. They also contribute to hemolymph sugar homeostasis. obo:GO_0097004 obo:go.owl obo:GO_0097004 paola obo:GO_0097004 2011-03-14T12:50:02Z obo:GO_0097004 AKH binding obo:GO_0097004 molecular_function obo:GO_0097004 GO:0097004 obo:GO_0097004 adipokinetic hormone binding obo:GO_0097005 Interacting selectively and non-covalently with an adipokinetic hormone receptor. Adipokinetic hormones (AKHs) are peptide hormones that are involved in the mobilization of sugar and lipids from the insect fat body during energy-requiring activities such as flight and locomotion. They also contribute to hemolymph sugar homeostasis. obo:GO_0097005 obo:go.owl obo:GO_0097005 paola obo:GO_0097005 2011-03-14T12:58:19Z obo:GO_0097005 AKH receptor binding obo:GO_0097005 molecular_function obo:GO_0097005 GO:0097005 obo:GO_0097005 adipokinetic hormone receptor binding obo:GO_0097016 Interacting selectively and non-covalently with a L27 domain of a protein. L27 is composed of conserved negatively charged amino acids and a conserved aromatic amino acid. L27 domains can assemble proteins involved in signaling and establishment and maintenance of cell polarity into complexes by interacting in a heterodimeric manner. obo:GO_0097016 obo:go.owl obo:GO_0097016 paola obo:GO_0097016 2011-03-23T02:17:51Z obo:GO_0097016 molecular_function obo:GO_0097016 GO:0097016 obo:GO_0097016 L27 domain binding obo:GO_0097037 The directed movement of heme out of a cell or organelle. obo:GO_0097037 obo:go.owl obo:GO_0097037 paola obo:GO_0097037 2011-04-11T10:39:22Z obo:GO_0097037 biological_process obo:GO_0097037 GO:0097037 obo:GO_0097037 heme export obo:GO_0097063 Interacting selectively and non-covalently with and responding, e.g. by conformational change, to changes in the cellular level of cadmium (Cd++). obo:GO_0097063 obo:go.owl obo:GO_0097063 paola obo:GO_0097063 2011-06-08T09:46:14Z obo:GO_0097063 molecular_function obo:GO_0097063 GO:0097063 obo:GO_0097063 cadmium ion sensor activity obo:GO_0097077 Interacting selectively and non-covalently with and responding, e.g. by conformational change, to changes in the cellular level of copper(I) (Cu+). obo:GO_0097077 obo:go.owl obo:GO_0097077 paola obo:GO_0097077 2011-06-17T09:57:11Z obo:GO_0097077 molecular_function obo:GO_0097077 GO:0097077 obo:GO_0097077 copper ion sensor activity obo:GO_0097098 Facilitates the base-pairing of single-stranded RNA to double-stranded DNA resulting in the formation of R-loops. obo:GO_0097098 obo:go.owl obo:GO_0097098 paola obo:GO_0097098 2011-07-07T11:20:44Z obo:GO_0097098 molecular_function obo:GO_0097098 GO:0097098 obo:GO_0097098 DNA/RNA hybrid annealing activity obo:GO_0097100 Interacting selectively and non-covalently with supercoiled DNA. For example, during replication and transcription, template DNA is negatively supercoiled in the receding downstream DNA and positively supercoiled in the approaching downstream DNA. obo:GO_0097100 obo:go.owl obo:GO_0097100 paola obo:GO_0097100 2011-07-12T03:28:57Z obo:GO_0097100 molecular_function obo:GO_0097100 GO:0097100 obo:GO_0097100 supercoiled DNA binding obo:GO_0097108 Interacting selectively and non-covalently with a member of the hedgehog protein family, signaling proteins involved in development. obo:GO_0097108 obo:go.owl obo:GO_0097108 paola obo:GO_0097108 2011-07-28T10:06:45Z obo:GO_0097108 molecular_function obo:GO_0097108 GO:0097108 obo:GO_0097108 hedgehog family protein binding obo:GO_0097109 Interacting selectively and non-covalently with a member of the neuroligin protein family, neuronal cell surface proteins that mediate synapse formation. obo:GO_0097109 obo:go.owl obo:GO_0097109 paola obo:GO_0097109 2011-07-28T05:15:22Z obo:GO_0097109 molecular_function obo:GO_0097109 GO:0097109 obo:GO_0097109 neuroligin family protein binding obo:GO_0097110 Interacting selectively and non-covalently with a scaffold protein. Scaffold proteins are crucial regulators of many key signaling pathways. Although not strictly defined in function, they are known to interact and/or bind with multiple members of a signaling pathway, tethering them into complexes. obo:GO_0097110 obo:go.owl obo:GO_0097110 paola obo:GO_0097110 2011-07-28T05:16:53Z obo:GO_0097110 molecular_function obo:GO_0097110 GO:0097110 obo:GO_0097110 scaffold protein binding obo:GO_0097157 Interacting selectively and non-covalently with an intronic sequence of a pre-messenger RNA (pre-mRNA). obo:GO_0097157 obo:go.owl obo:GO_0097157 paola obo:GO_0097157 2011-09-23T11:27:01Z obo:GO_0097157 pre-messenger RNA intronic binding obo:GO_0097157 molecular_function obo:GO_0097157 GO:0097157 obo:GO_0097157 pre-mRNA intronic binding obo:GO_0097158 Interacting selectively and non-covalently with a pyrimidine-rich (CU-rich) intronic sequence of a pre-messenger RNA (pre-mRNA). obo:GO_0097158 obo:go.owl obo:GO_0097158 paola obo:GO_0097158 2011-09-23T11:29:03Z obo:GO_0097158 pre-messenger RNA intronic pyrimidine-rich binding obo:GO_0097158 molecular_function obo:GO_0097158 GO:0097158 obo:GO_0097158 pre-mRNA intronic pyrimidine-rich binding obo:GO_0097159 Interacting selectively and non-covalently with an organic cyclic compound, any molecular entity that contains carbon arranged in a cyclic molecular structure. obo:GO_0097159 obo:go.owl obo:GO_0097159 paola obo:GO_0097159 2011-09-23T02:31:01Z obo:GO_0097159 molecular_function obo:GO_0097159 GO:0097159 obo:GO_0097159 organic cyclic compound binding obo:GO_0097160 Interacting selectively and non-covalently with a polychlorinated biphenyl (PCB), a biphenyl compound containing between 2 and 10 chlorine atoms attached to the two benzene rings. obo:GO_0097160 obo:go.owl obo:GO_0097160 paola obo:GO_0097160 2011-09-23T02:33:22Z obo:GO_0097160 PCB binding obo:GO_0097160 polychlorobiphenyl binding obo:GO_0097160 molecular_function obo:GO_0097160 GO:0097160 obo:GO_0097160 polychlorinated biphenyl binding obo:GO_0097161 Interacting selectively and non-covalently with a DH (Dbl homology) domain of a protein. The DH domain contains three structurally conserved regions separated by more variable regions. It is composed of 11 alpha helices that are folded into a flattened, elongated alpha-helix bundle in which two of the three conserved regions, conserved region 1 (CR1) and conserved region 3 (CR3), are exposed near the centre of one surface. CR1 and CR3, together with a part of alpha-6 and the DH/PH (pleckstrin homology) junction site, constitute the Rho GTPase interacting pocket. obo:GO_0097161 obo:go.owl obo:GO_0097161 paola obo:GO_0097161 2011-09-27T10:06:09Z obo:GO_0097161 molecular_function obo:GO_0097161 GO:0097161 obo:GO_0097161 DH domain binding obo:GO_0097162 Interacting selectively and non-covalently with a MADS box domain, a protein domain that encodes the DNA-binding MADS domain. The MADS domain binds to DNA sequences of high similarity to the motif CC[A/T]6GG termed the CArG-box. MADS-domain proteins are generally transcription factors. The length of the MADS-box is in the range of 168 to 180 base pairs. obo:GO_0097162 obo:go.owl obo:GO_0097162 paola obo:GO_0097162 2011-09-27T10:10:59Z obo:GO_0097162 molecular_function obo:GO_0097162 GO:0097162 obo:GO_0097162 MADS box domain binding obo:GO_0097177 Interacting selectively and non-covalently with any part of a mitochondrial ribosome, a ribosome found in the mitochondrion of a eukaryotic cell. obo:GO_0097177 obo:go.owl obo:GO_0097177 paola obo:GO_0097177 2011-10-11T03:03:03Z obo:GO_0097177 molecular_function obo:GO_0097177 GO:0097177 obo:GO_0097177 mitochondrial ribosome binding obo:GO_0097216 Interacting selectively and non-covalently with guanosine tetraphosphate (5'-ppGpp-3'), a guanosine bisphosphate having diphosphate groups at both the 3' and 5'-positions. obo:GO_0097216 obo:go.owl obo:GO_0097216 paola obo:GO_0097216 2012-01-13T08:35:50Z obo:GO_0097216 5'-ppGpp-3' binding obo:GO_0097216 molecular_function obo:GO_0097216 GO:0097216 obo:GO_0097216 guanosine tetraphosphate binding obo:GO_0097243 Interacting selectively and non-covalently with a flavonoid, a compound containing two or more aromatic rings, each bearing at least one aromatic hydroxyl and connected with a carbon bridge. obo:GO_0097243 obo:go.owl obo:GO_0097243 paola obo:GO_0097243 2012-02-17T03:49:16Z obo:GO_0097243 molecular_function obo:GO_0097243 GO:0097243 obo:GO_0097243 flavonoid binding obo:GO_0097244 Interacting selectively and non-covalently with a flavonol, a flavonoid that contains a 3-hydroxy-2-phenylchromen-4-one backbone. obo:GO_0097244 obo:go.owl obo:GO_0097244 paola obo:GO_0097244 2012-02-17T03:50:45Z obo:GO_0097244 molecular_function obo:GO_0097244 GO:0097244 obo:GO_0097244 flavonol binding obo:GO_0097245 Interacting selectively and non-covalently with a flavanol. obo:GO_0097245 obo:go.owl obo:GO_0097245 paola obo:GO_0097245 2012-02-17T03:52:10Z obo:GO_0097245 flavan-3-ol binding obo:GO_0097245 molecular_function obo:GO_0097245 GO:0097245 obo:GO_0097245 flavanol binding obo:GO_0097246 Interacting selectively and non-covalently with a catechin, a polyphenolic antioxidant plant metabolite with a flavonoid or flavan-3-ol structure. obo:GO_0097246 obo:go.owl obo:GO_0097246 paola obo:GO_0097246 2012-02-17T03:53:54Z obo:GO_0097246 molecular_function obo:GO_0097246 GO:0097246 obo:GO_0097246 catechin binding obo:GO_0097247 Interacting selectively and non-covalently with epigallocatechin 3-gallate, a compound that is a gallic acid ester of a catechin. obo:GO_0097247 obo:go.owl obo:GO_0097247 paola obo:GO_0097247 2012-02-17T03:55:05Z obo:GO_0097247 catechin gallate binding obo:GO_0097247 EGCG binding obo:GO_0097247 molecular_function obo:GO_0097247 GO:0097247 obo:GO_0097247 epigallocatechin 3-gallate binding obo:GO_0097307 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a farnesol stimulus. obo:GO_0097307 obo:go.owl obo:GO_0097307 paola obo:GO_0097307 2012-05-15T03:51:31Z obo:GO_0097307 biological_process obo:GO_0097307 GO:0097307 obo:GO_0097307 response to farnesol obo:GO_0097308 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a farnesol stimulus. obo:GO_0097308 obo:go.owl obo:GO_0097308 paola obo:GO_0097308 2012-05-15T03:54:01Z obo:GO_0097308 biological_process obo:GO_0097308 GO:0097308 obo:GO_0097308 cellular response to farnesol obo:GO_0097322 Interacting selectively and non-covalently with a 7SK small nuclear RNA (7SK snRNA). obo:GO_0097322 obo:go.owl obo:GO_0097322 paola obo:GO_0097322 2012-06-05T11:42:23Z obo:GO_0097322 7SK small nuclear RNA binding obo:GO_0097322 molecular_function obo:GO_0097322 GO:0097322 obo:GO_0097322 7SK snRNA binding obo:GO_0097351 Interacting selectively and non-covalently with a toxic protein, disabling its function. There may be more than one antitoxin to a toxic protein. Instances of this activity are known only in prokaryotes, where the toxic protein may be a ribonuclease, a DNA gyrase, or other. obo:GO_0097351 obo:go.owl obo:GO_0097351 paola obo:GO_0097351 2012-06-28T11:41:38Z obo:GO_0097351 molecular_function obo:GO_0097351 GO:0097351 obo:GO_0097351 toxin-antitoxin pair type II binding obo:GO_0097367 Interacting selectively and non-covalently with a carbohydrate derivative. obo:GO_0097367 obo:go.owl obo:GO_0097367 paola obo:GO_0097367 2012-08-02T13:03:39Z obo:GO_0097367 molecular_function obo:GO_0097367 GO:0097367 obo:GO_0097367 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_agr obo:GO_0097367 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_mouse obo:GO_0097367 carbohydrate derivative binding obo:GO_0097371 Interacting selectively and non-covalently with any isoform of the MDM2/MDM4 protein family, comprising negative regulators of p53. obo:GO_0097371 obo:go.owl obo:GO_0097371 paola obo:GO_0097371 2012-08-08T16:20:59Z obo:GO_0097371 molecular_function obo:GO_0097371 GO:0097371 obo:GO_0097371 MDM2/MDM4 family protein binding obo:GO_0097401 The acidification of the synaptic vesicle lumen via transport of protons into the vesicle. The resulting electrochemical gradient powers neurotransmitter loading. obo:GO_0097401 obo:go.owl obo:GO_0097401 paola obo:GO_0097401 2012-10-25T09:03:34Z obo:GO_0097401 synaptic vesicle lumen pH reduction obo:GO_0097401 synaptic vesicle proton loading obo:GO_0097401 biological_process obo:GO_0097401 GO:0097401 obo:GO_0097401 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_synapse obo:GO_0097401 synaptic vesicle lumen acidification obo:GO_0097430 The directed movement of copper ions from outside of a cell, across an ascospore-type prospore membrane and into the cytosol. obo:GO_0097430 obo:go.owl obo:GO_0097430 paola obo:GO_0097430 2012-11-16T12:37:05Z obo:GO_0097430 copper ion import across prospore membrane obo:GO_0097430 biological_process obo:GO_0097430 copper ion import into ascospore-type prospore obo:GO_0097430 copper ion transport into forespores obo:GO_0097430 GO:0097430 obo:GO_0097430 copper ion import across prospore membrane obo:GO_0097497 The process of negative regulation of cell adhesion that results in blood vessel endothelial cells splitting off from an existing endothelial sheet. obo:GO_0097497 obo:go.owl obo:GO_0097497 paola obo:GO_0097497 2013-08-12T13:48:34Z obo:GO_0097497 biological_process obo:GO_0097497 GO:0097497 obo:GO_0097497 blood vessel endothelial cell delamination obo:GO_0097551 The repair of double-strand breaks in mitochondrial DNA via homologous and nonhomologous mechanisms to reform a continuous DNA helix. obo:GO_0097551 obo:go.owl obo:GO_0097551 paola obo:GO_0097551 2014-01-22T10:06:54Z obo:GO_0097551 mtDSB repair obo:GO_0097551 biological_process obo:GO_0097551 GO:0097551 obo:GO_0097551 Note that the processes of nuclear double-strand break repair and mitochondrial double-strand break repair are genetically separable. obo:GO_0097551 mitochondrial double-strand break repair obo:GO_0097552 The repair of a double-strand break in mitochondrial DNA in which the broken DNA molecule is repaired using homologous sequences. obo:GO_0097552 obo:go.owl obo:GO_0097552 paola obo:GO_0097552 2014-01-22T10:09:10Z obo:GO_0097552 mtDSB repair via homologous recombination obo:GO_0097552 biological_process obo:GO_0097552 GO:0097552 obo:GO_0097552 Note that the processes of nuclear double-strand break repair and mitochondrial double-strand break repair are genetically separable. obo:GO_0097552 mitochondrial double-strand break repair via homologous recombination obo:GO_0097553 A process in which a calcium ion is transported from one side of a membrane to the other into the cytosol by means of some agent such as a transporter or pore. obo:GO_0097553 obo:go.owl obo:GO_0097553 paola obo:GO_0097553 2014-01-23T11:05:13Z obo:GO_0097553 calcium transmembrane import into cytosol obo:GO_0097553 biological_process obo:GO_0097553 GO:0097553 obo:GO_0097553 calcium ion transmembrane import into cytosol obo:GO_0097602 Interacting selectively and non-covalently with any member of the cullin family, hydrophobic proteins that act as scaffolds for ubiquitin ligases (E3). obo:GO_0097602 obo:go.owl obo:GO_0097602 paola obo:GO_0097602 2014-05-11T20:41:10Z obo:GO_0097602 cullin binding obo:GO_0097602 molecular_function obo:GO_0097602 GO:0097602 obo:GO_0097602 cullin family protein binding obo:GO_0097617 A nucleic acid binding activity that brings together complementary sequences of nucleic acids so that they pair by hydrogen bonds to form a double-stranded polynucleotide. obo:GO_0097617 obo:go.owl obo:GO_0097617 paola obo:GO_0097617 2014-06-13T10:18:43Z obo:GO_0097617 Reactome:R-HSA-5686642 obo:GO_0097617 molecular_function obo:GO_0097617 renaturation obo:GO_0097617 GO:0097617 obo:GO_0097617 The term 'annealing' is often used to describe the binding of a DNA probe, or the binding of a primer to a DNA strand during a polymerase chain reaction. The term is also often used to describe the reformation (renaturation) of complementary strands that were separated by heat (thermally denatured). For example, proteins such as RAD52 can help DNA anneal. If at all possible, please annotate to the more specific terms GO:0036310 'annealing helicase activity', GO:0097098 'DNA/RNA hybrid annealing activity' or GO:0033592 'RNA strand annealing activity'. obo:GO_0097617 annealing activity obo:GO_0097623 The directed movement of potassium ions from inside of a cell, across the plasma membrane and into the extracellular region. obo:GO_0097623 obo:go.owl obo:GO_0097623 paola obo:GO_0097623 2009-12-16T11:10:45Z obo:GO_0097623 GO:0071435 obo:GO_0097623 GO:0098668 obo:GO_0097623 potassium export obo:GO_0097623 potassium ion export obo:GO_0097623 potassium export across plasma membrane obo:GO_0097623 potassium ion export from cell obo:GO_0097623 biological_process obo:GO_0097623 GO:0097623 obo:GO_0097623 Merged as of ticket of related term https://github.com/geneontology/go-ontology/issues/14265 obo:GO_0097623 potassium ion export across plasma membrane obo:GO_0097644 Interacting selectively and non-covalently with any member of the calcitonin family (e.g. adrenomedullin, adrenomedullin 2 (intermedin), amylin, calcitonin and calcitonin gene-related peptides (CGRPs)). obo:GO_0097644 obo:go.owl obo:GO_0097644 paola obo:GO_0097644 2014-09-08T20:50:52Z obo:GO_0097644 molecular_function obo:GO_0097644 GO:0097644 obo:GO_0097644 calcitonin family binding obo:GO_0097645 Interacting selectively and non-covalently with amylin. obo:GO_0097645 obo:go.owl obo:GO_0097645 paola obo:GO_0097645 2014-09-08T20:53:03Z obo:GO_0097645 molecular_function obo:GO_0097645 GO:0097645 obo:GO_0097645 amylin binding obo:GO_0097655 Interacting selectively and non-covalently with any member of the serpin protein family (serine protease inhibitors or classified inhibitor family I4). Serpins are a broadly distributed family of protease inhibitors that use a conformational change to inhibit target enzymes. They are central in controlling many important proteolytic cascades. The majority of serpins inhibit serine proteases, but serpins that inhibit caspases and papain-like cysteine proteases have also been identified. Rarely, serpins perform a non-inhibitory function; for example, several human serpins function as hormone transporters and certain serpins function as molecular chaperones or tumor suppressors. obo:GO_0097655 obo:go.owl obo:GO_0097655 paola obo:GO_0097655 2014-09-24T16:19:31Z obo:GO_0097655 SERPIN family protein binding obo:GO_0097655 molecular_function obo:GO_0097655 GO:0097655 obo:GO_0097655 serpin family protein binding obo:GO_0097677 Interacting selectively and non-covalently with any member of the signal transducers and activators of transcription (STAT) protein family. STATs are, as the name indicates, both signal transducers and transcription factors. STATs are activated by cytokines and some growth factors and thus control important biological processes including cell growth, cell differentiation, apoptosis and immune responses. obo:GO_0097677 obo:go.owl obo:GO_0097677 paola obo:GO_0097677 2014-11-04T11:31:03Z obo:GO_0097677 signal transducers and activators of transcription family protein binding obo:GO_0097677 molecular_function obo:GO_0097677 GO:0097677 obo:GO_0097677 STAT family protein binding obo:GO_0097678 Interacting selectively and non-covalently with any member of the suppressor of cytokine signaling (SOCS) family of proteins. SOCS represent an important mechanism to extinguish cytokine and growth factor receptor signaling. Individual SOCS proteins are typically induced by specific cytokines and growth factors, thereby generating a negative feedback loop. SOCS proteins have important functions in development and homeostasis, and in disease, particularly tumor suppression and anti-inflammatory functions. obo:GO_0097678 obo:go.owl obo:GO_0097678 paola obo:GO_0097678 2014-11-04T11:32:49Z obo:GO_0097678 suppressor of cytokine signaling family protein binding obo:GO_0097678 molecular_function obo:GO_0097678 GO:0097678 obo:GO_0097678 SOCS family protein binding obo:GO_0097680 An instance of double-strand break repair via nonhomologous end joining that requires a number of factors important for V(D)J recombination, including the KU70/80 heterodimer (KU), XRCC4, ligase IV, and DNA-PKcs in mammals. It does not produce translocations (as opposed to the alternative nonhomologous end joining). obo:GO_0097680 obo:go.owl obo:GO_0097680 paola obo:GO_0097680 2014-12-17T15:15:18Z obo:GO_0097680 canonical nonhomologous end joining obo:GO_0097680 biological_process obo:GO_0097680 C-NHEJ obo:GO_0097680 GO:0097680 obo:GO_0097680 double-strand break repair via classical nonhomologous end joining obo:GO_0097681 An instance of double-strand break repair via nonhomologous end joining that is independent of factors important for V(D)J recombination (as opposed to classical nonhomologous end joining). It often results in a deletion with microhomology (i.e. 5-25bp homology) at the repair junction. Among different subclasses of nonhomologous end joining (NHEJ), alternative NHEJ appears to play a significant role in the etiology of mutations that arise during cancer development and treatment. obo:GO_0097681 obo:go.owl obo:GO_0097681 paola obo:GO_0097681 2014-12-17T15:17:45Z obo:GO_0097681 double-strand break repair via microhomology-mediated end joining obo:GO_0097681 biological_process obo:GO_0097681 A-NHEJ obo:GO_0097681 MMEJ obo:GO_0097681 alt-NHEJ obo:GO_0097681 GO:0097681 obo:GO_0097681 double-strand break repair via alternative nonhomologous end joining obo:GO_0097714 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a viscosity stimulus. obo:GO_0097714 obo:go.owl obo:GO_0097714 paola obo:GO_0097714 2016-08-23T14:32:46Z obo:GO_0097714 biological_process obo:GO_0097714 GO:0097714 obo:GO_0097714 response to viscosity obo:GO_0097715 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a viscosity stimulus. obo:GO_0097715 obo:go.owl obo:GO_0097715 paola obo:GO_0097715 2016-08-23T14:34:05Z obo:GO_0097715 biological_process obo:GO_0097715 GO:0097715 obo:GO_0097715 cellular response to viscosity obo:GO_0097716 The directed movement of copper (Cu) ions passing through the blood-brain barrier. obo:GO_0097716 obo:go.owl obo:GO_0097716 paola obo:GO_0097716 2016-08-23T14:35:54Z obo:GO_0097716 biological_process obo:GO_0097716 copper ion transport across BBB obo:GO_0097716 GO:0097716 obo:GO_0097716 copper ion transport across blood-brain barrier obo:GO_0097717 The directed movement of copper (Cu) ions passing through the blood-cerebrospinal fluid barrier. obo:GO_0097717 obo:go.owl obo:GO_0097717 paola obo:GO_0097717 2016-08-23T14:37:33Z obo:GO_0097717 copper ion transport across blood-CSF barrier obo:GO_0097717 biological_process obo:GO_0097717 copper ion transport across BCB obo:GO_0097717 GO:0097717 obo:GO_0097717 copper ion transport across blood-cerebrospinal fluid barrier obo:GO_0097718 Interacting selectively and non-covalently with a disordered domain of a protein. obo:GO_0097718 obo:go.owl obo:GO_0097718 paola obo:GO_0097718 2016-08-23T16:42:51Z obo:GO_0097718 molecular_function obo:GO_0097718 disordered protein domain specific binding obo:GO_0097718 GO:0097718 obo:GO_0097718 disordered domain specific binding obo:GO_0097726 Interacting selectively and non-covalently with a LEM domain. The LEM domain (for lamina-associated polypeptide, emerin, MAN1 domain) is present in a group of nuclear proteins that bind chromatin through interaction of the LEM motif with the conserved DNA crosslinking protein, barrier-to-autointegration factor (BAF). obo:GO_0097726 obo:go.owl obo:GO_0097726 paola obo:GO_0097726 2016-09-19T10:19:02Z obo:GO_0097726 LAP2, emerin, MAN1 domain binding obo:GO_0097726 lamina-associated polypeptide, emerin, MAN1 domain binding obo:GO_0097726 molecular_function obo:GO_0097726 GO:0097726 obo:GO_0097726 LEM domain binding obo:GO_0098505 Interacting selectively and non-covalently with G-rich, single-stranded, telomere-associated DNA. obo:GO_0098505 obo:go.owl obo:GO_0098505 davidos obo:GO_0098505 2013-09-23T13:16:24Z obo:GO_0098505 molecular_function obo:GO_0098505 GO:0098505 obo:GO_0098505 G-rich strand telomeric DNA binding obo:GO_0098508 The generation of hematopoietic stem cells from hemogenic endothelial cells by a process that includes tight-junction dissolution and loss of cell polarity followed by delamination from the endothelium. obo:GO_0098508 obo:go.owl obo:GO_0098508 davidos obo:GO_0098508 2013-09-24T15:20:39Z obo:GO_0098508 biological_process obo:GO_0098508 GO:0098508 obo:GO_0098508 endothelial to hematopoietic transition obo:GO_0098512 The series of events in which a humidity stimulus is received and converted into a molecular signal as part of the sensory perception of humidity. obo:GO_0098512 obo:go.owl obo:GO_0098512 davidos obo:GO_0098512 2013-09-25T14:09:25Z obo:GO_0098512 biological_process obo:GO_0098512 GO:0098512 obo:GO_0098512 detection of humidity stimulus involved in sensory perception obo:GO_0098514 The series of events in which a high humidity stimulus is detected and converted into a molecular signal as a part of the sensory detection of high humidity. obo:GO_0098514 obo:go.owl obo:GO_0098514 davidos obo:GO_0098514 2013-09-25T14:20:54Z obo:GO_0098514 biological_process obo:GO_0098514 GO:0098514 obo:GO_0098514 detection of high humidity stimulus involved in sensory perception obo:GO_0098515 The series of events in which a low humidity stimulus is detected and converted into a molecular signal as a part of the sensory detection of low humidity. obo:GO_0098515 obo:go.owl obo:GO_0098515 davidos obo:GO_0098515 2013-09-25T14:24:29Z obo:GO_0098515 biological_process obo:GO_0098515 GO:0098515 obo:GO_0098515 detection of low humidity stimulus involved in sensory perception obo:GO_0098546 Interacting selectively and non-covalently with c[G(2',5')pA(2',5')p], a cyclic purine dinucleotide that consists of AMP and GMP units cyclized via 2',5' and 3',5' linkages. obo:GO_0098546 obo:go.owl obo:GO_0098546 davidos obo:GO_0098546 2013-12-03T15:31:39Z obo:GO_0098546 c[G(2',5')pA(3',5')p] binding obo:GO_0098546 molecular_function obo:GO_0098546 GO:0098546 obo:GO_0098546 2',5-3',5'-cyclic GMP-AMP binding obo:GO_0098581 The series of events in which an external biotic stimulus is detected and converted into a molecular signal. An external biotic stimulus is defined as one caused or produced by a living organism other than the one being stimulated. obo:GO_0098581 obo:go.owl obo:GO_0098581 davidos obo:GO_0098581 2014-01-22T14:20:16Z obo:GO_0098581 detection of exogenous biotic stimulus obo:GO_0098581 biological_process obo:GO_0098581 GO:0098581 obo:GO_0098581 detection of external biotic stimulus obo:GO_0098599 Catalysis of a hydrolase reaction that removes a palmitoyl moiety from some substrate. obo:GO_0098599 obo:go.owl obo:GO_0098599 davidos obo:GO_0098599 2014-04-11T17:57:36Z obo:GO_0098599 Reactome:R-HSA-5690046 obo:GO_0098599 Reactome:R-HSA-9027670 obo:GO_0098599 molecular_function obo:GO_0098599 GO:0098599 obo:GO_0098599 palmitoyl hydrolase activity obo:GO_0098627 Catalysis of the reaction: protein arginine phosphate + H2O = protein arginine + phosphate. obo:GO_0098627 obo:go.owl obo:GO_0098627 davidos obo:GO_0098627 2014-04-17T17:57:39Z obo:GO_0098627 molecular_function obo:GO_0098627 GO:0098627 obo:GO_0098627 Made part of peptidyl-N-phospho-arginine phosphatase activity on the assumption that arginine phosphorylation in proteins occurs via an N link. obo:GO_0098627 protein arginine phosphatase activity obo:GO_0098631 The binding by a cell-adhesion protein on the cell surface to an extracellular matrix component, to mediate adhesion of the cell to the external substrate or to another cell. obo:GO_0098631 obo:go.owl obo:GO_0098631 cell adhesion molecule obo:GO_0098631 protein binding involved in cell adhesion obo:GO_0098631 molecular_function obo:GO_0098631 GO:0098631 obo:GO_0098631 cell adhesion mediator activity obo:GO_0098632 The binding by a cell-adhesion protein on the cell surface to an extracellular matrix component, to mediate adhesion of the cell to another cell. obo:GO_0098632 obo:go.owl obo:GO_0098632 cell-cell adhesion molecule obo:GO_0098632 protein binding involved in cell-cell adhesion obo:GO_0098632 molecular_function obo:GO_0098632 GO:0098632 obo:GO_0098632 cell-cell adhesion mediator activity obo:GO_0098633 Interacting selectively and non-covalently with a collagen fibril. obo:GO_0098633 obo:go.owl obo:GO_0098633 molecular_function obo:GO_0098633 GO:0098633 obo:GO_0098633 collagen fibril binding obo:GO_0098634 The binding by a cell-adhesion protein on the cell surface to an extracellular matrix component, to mediate adhesion of the cell to the extracellular matrix. obo:GO_0098634 obo:go.owl obo:GO_0098634 cell-matrix adhesion molecule obo:GO_0098634 protein binding involved in cell-matrix adhesion obo:GO_0098634 molecular_function obo:GO_0098634 GO:0098634 obo:GO_0098634 cell-matrix adhesion mediator activity obo:GO_0098639 Any collagen binding that occurs as part of cell-matrix adhesion. obo:GO_0098639 obo:go.owl obo:GO_0098639 molecular_function obo:GO_0098639 GO:0098639 obo:GO_0098639 collagen binding involved in cell-matrix adhesion obo:GO_0098640 Any integrin binding that occurs as part of the process of cell-matrix adhesion. obo:GO_0098640 obo:go.owl obo:GO_0098640 molecular_function obo:GO_0098640 GO:0098640 obo:GO_0098640 integrin binding involved in cell-matrix adhesion obo:GO_0098641 Any cadherin binding that occurs as part of the process of cell-cell adhesion. obo:GO_0098641 obo:go.owl obo:GO_0098641 molecular_function obo:GO_0098641 GO:0098641 obo:GO_0098641 cadherin binding involved in cell-cell adhesion obo:GO_0098650 Interacting selectively and non-covalently with a peptidyl-proline 4-dioxygenase. obo:GO_0098650 obo:go.owl obo:GO_0098650 molecular_function obo:GO_0098650 GO:0098650 obo:GO_0098650 peptidyl-proline 4-dioxygenase binding obo:GO_0098655 The process in which a cation is transported across a membrane. obo:GO_0098655 obo:go.owl obo:GO_0098655 GO:0099132 obo:GO_0098655 ATP hydrolysis coupled cation transmembrane transport obo:GO_0098655 biological_process obo:GO_0098655 GO:0098655 obo:GO_0098655 cation transmembrane transport obo:GO_0098659 The directed movement of inorganic cations from outside of a cell, across the plasma membrane and into the cytosol. obo:GO_0098659 obo:go.owl obo:GO_0098659 inorganic cation import into cell obo:GO_0098659 biological_process obo:GO_0098659 GO:0098659 obo:GO_0098659 inorganic cation import across plasma membrane obo:GO_0098660 The process in which an inorganic ion is transported across a membrane. obo:GO_0098660 obo:go.owl obo:GO_0098660 inorganic ion membrane transport obo:GO_0098660 transmembrane inorganic ion transport obo:GO_0098660 biological_process obo:GO_0098660 GO:0098660 obo:GO_0098660 Note that this term is not intended for use in annotating lateral movement within membranes. obo:GO_0098660 inorganic ion transmembrane transport obo:GO_0098662 A process in which an inorganic cation is transported from one side of a membrane to the other by means of some agent such as a transporter or pore. obo:GO_0098662 obo:go.owl obo:GO_0098662 inorganic cation membrane transport obo:GO_0098662 transmembrane inorganic cation transport obo:GO_0098662 biological_process obo:GO_0098662 GO:0098662 obo:GO_0098662 Note that this term is not intended for use in annotating lateral movement within membranes. obo:GO_0098662 inorganic cation transmembrane transport obo:GO_0098696 Any process that modulates the frequency, rate or extent of neurotransmitter receptor localization to postsynaptic specialization membrane. obo:GO_0098696 obo:go.owl obo:GO_0098696 dos obo:GO_0098696 2017-04-04T16:33:38Z obo:GO_0098696 biological_process obo:GO_0098696 GO:0098696 obo:GO_0098696 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_synapse obo:GO_0098696 regulation of neurotransmitter receptor localization to postsynaptic specialization membrane obo:GO_0098703 The directed movement of calcium ions from outside of a cell, across the plasma membrane and into the cytosol. obo:GO_0098703 obo:go.owl obo:GO_0098703 mah obo:GO_0098703 2013-02-07T13:07:59Z obo:GO_0098703 GO:1990035 obo:GO_0098703 calcium ion import into cell obo:GO_0098703 calcium ion uptake into cell obo:GO_0098703 biological_process obo:GO_0098703 GO:0098703 obo:GO_0098703 calcium ion import across plasma membrane obo:GO_0098705 The directed movement of copper ions from outside of a cell, across the plasma membrane and into the cytosol. obo:GO_0098705 obo:go.owl obo:GO_0098705 mah obo:GO_0098705 2014-04-03T13:26:04Z obo:GO_0098705 GO:0015678 obo:GO_0098705 GO:1902861 obo:GO_0098705 copper cation import into cell obo:GO_0098705 copper ion import into cell obo:GO_0098705 high affinity copper ion transport obo:GO_0098705 high affinity copper transport obo:GO_0098705 high-affinity copper ion transport obo:GO_0098705 biological_process obo:GO_0098705 GO:0098705 obo:GO_0098705 copper ion import across plasma membrane obo:GO_0098706 The directed movement of iron ions from outside of a cell, across the cell outer membrane and into the periplasmic space. obo:GO_0098706 obo:go.owl obo:GO_0098706 paola obo:GO_0098706 2012-12-20T08:33:03Z obo:GO_0098706 GO:0015683 obo:GO_0098706 GO:0097461 obo:GO_0098706 ferric iron transmembrane transport obo:GO_0098706 ferric ion import into cell obo:GO_0098706 ferric iron import into cell obo:GO_0098706 ferric iron import across cell outer membrane obo:GO_0098706 high affinity ferric iron transport obo:GO_0098706 high-affinity ferric iron transmembrane transport obo:GO_0098706 biological_process obo:GO_0098706 GO:0098706 obo:GO_0098706 iron ion import across cell outer membrane obo:GO_0098711 The directed movement of iron ions from outside of a cell, across the plasma membrane and into the cytosol. obo:GO_0098711 obo:go.owl obo:GO_0098711 paola obo:GO_0098711 2012-12-20T08:29:00Z obo:GO_0098711 GO:0097459 obo:GO_0098711 GO:0097460 obo:GO_0098711 GO:0098707 obo:GO_0098711 iron ion import into cell obo:GO_0098711 biological_process obo:GO_0098711 ferrous ion import into cell obo:GO_0098711 ferrous iron import across plasma membrane obo:GO_0098711 ferrous iron import into cell obo:GO_0098711 iron import into cell obo:GO_0098711 GO:0098711 obo:GO_0098711 iron ion import across plasma membrane obo:GO_0098716 The directed movement of nickel cations from outside of a cell, across the plasma membrane and into the cytosol. obo:GO_0098716 obo:go.owl obo:GO_0098716 tanyaberardini obo:GO_0098716 2012-11-16T16:12:53Z obo:GO_0098716 GO:0090509 obo:GO_0098716 nickel cation import into cell obo:GO_0098716 biological_process obo:GO_0098716 GO:0098716 obo:GO_0098716 nickel cation import across plasma membrane obo:GO_0098719 The directed movement of sodium ions from outside of a cell, across the plasma membrane and into the cytosol. obo:GO_0098719 obo:go.owl obo:GO_0098719 pr obo:GO_0098719 2012-08-03T16:55:52Z obo:GO_0098719 GO:0097369 obo:GO_0098719 GO:1990118 obo:GO_0098719 sodium import obo:GO_0098719 sodium ion import into cell obo:GO_0098719 biological_process obo:GO_0098719 sodium ion import obo:GO_0098719 GO:0098719 obo:GO_0098719 sodium ion import across plasma membrane obo:GO_0098750 Interacting selectively and non-covalently with a FXYD domain. obo:GO_0098750 obo:go.owl obo:GO_0098750 molecular_function obo:GO_0098750 GO:0098750 obo:GO_0098750 FYXD domain binding obo:GO_0098769 Interacting selectively and non-covalently with any member of the Tissue inhibitors of metalloproteinases (TIMPs) family. TIMPs are endogenous protein regulators of the matrix metalloproteinase (MMPs) family obo:GO_0098769 obo:go.owl obo:GO_0098769 molecular_function obo:GO_0098769 GO:0098769 obo:GO_0098769 TIMP family protein binding obo:GO_0098770 Interacting selectively and non-covalently with any member of the FBXO protein family. Members of this family have an F-box protein motif of approximately 50 amino acids that functions as a site of protein-protein interaction. obo:GO_0098770 obo:go.owl obo:GO_0098770 molecular_function obo:GO_0098770 GO:0098770 obo:GO_0098770 FBXO family protein binding obo:GO_0098772 A molecular function that modulates the activity of a gene product or complex. Examples include enzyme regulators and channel regulators. obo:GO_0098772 obo:go.owl obo:GO_0098772 molecular_function obo:GO_0098772 GO:0098772 obo:GO_0098772 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_flybase_ribbon obo:GO_0098772 molecular function regulator obo:GO_0098808 Interacting selectively and non-covalently with a 7-methylguanosine (m7G) group or derivative located at the 5' end of an mRNA molecule. obo:GO_0098808 obo:go.owl obo:GO_0098808 molecular_function obo:GO_0098808 GO:0098808 obo:GO_0098808 mRNA cap binding obo:GO_0098847 Interacting selectively and non-covalently with single-stranded DNA of a specific nucleotide composition. obo:GO_0098847 obo:go.owl obo:GO_0098847 molecular_function obo:GO_0098847 GO:0098847 obo:GO_0098847 sequence-specific single stranded DNA binding obo:GO_0098851 Interacting selectively and non-covalently with double-stranded miRNA. double-stranded miRNA is formed by processing of pre-miRNA stem-loop structures. obo:GO_0098851 obo:go.owl obo:GO_0098851 miRNA duplex binding obo:GO_0098851 molecular_function obo:GO_0098851 GO:0098851 obo:GO_0098851 double-stranded miRNA binding obo:GO_0099077 DNA-binding activity that is dependent on binding to a histone. obo:GO_0099077 obo:go.owl obo:GO_0099077 molecular_function obo:GO_0099077 GO:0099077 obo:GO_0099077 histone-dependent DNA binding obo:GO_0099122 Interacting selectively and non-covalently with the C-terminal domain (CTD) of the largest subunit of RNA polymerase II. The CTD is comprised of repeats of a heptapeptide with the consensus sequence YSPTSPS. The number of repeats varies with the species and a minimum number of repeats is required for RNAP II function. obo:GO_0099122 obo:go.owl obo:GO_0099122 RNAP II C-terminal binding obo:GO_0099122 molecular_function obo:GO_0099122 GO:0099122 obo:GO_0099122 RNA polymerase II C-terminal domain binding obo:GO_0099130 Interacting selectively and non-covalently with any estrogen. obo:GO_0099130 obo:go.owl obo:GO_0099130 molecular_function obo:GO_0099130 GO:0099130 obo:GO_0099130 estrogen binding obo:GO_0099180 The directed movement of Zn2+ ions from the cytoplasm into the lumen of a cytoplasmic vesicle. obo:GO_0099180 obo:go.owl obo:GO_0099180 Zn2+ import into synaptic vesicle obo:GO_0099180 zinc import into synaptic vesicle obo:GO_0099180 biological_process obo:GO_0099180 GO:0099180 obo:GO_0099180 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_synapse obo:GO_0099180 zinc ion import into synaptic vesicle obo:GO_0099510 The directed change of cytosolic calcium ion concentration in the cytosol via the reversible binding of calcium ions to calcium-binding proteins in the cytosol thereby modulating the spatial and temporal dynamics of changes in cytosolic calcium concentrations. obo:GO_0099510 obo:go.owl obo:GO_0099510 regulation of cytosolic calcium ion concentration by calcium ion buffering obo:GO_0099510 molecular_function obo:GO_0099510 GO:0099510 obo:GO_0099510 calcium ion binding involved in regulation of cytosolic calcium ion concentration obo:GO_0099534 The directed change of presynaptic cytosolic free calcium ion concentration in the cytosol via the reversible binding of calcium ions to calcium-binding proteins in the cytosol thereby modulating the spatial and temporal dynamics of changes in presynaptic cytosolic calcium concentrations. obo:GO_0099534 obo:go.owl obo:GO_0099534 calcium ion binding involved in regulation of presynaptic cytosolic calcium levels obo:GO_0099534 presynaptic calcium ion buffering obo:GO_0099534 regulation of presynaptic cytosolic calcium ion concentration by calcium ion buffering obo:GO_0099534 molecular_function obo:GO_0099534 GO:0099534 obo:GO_0099534 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_synapse obo:GO_0099534 calcium ion binding involved in regulation of presynaptic cytosolic calcium ion concentration obo:GO_0099567 The directed change of free calcium ion concentration in the postsynaptic cytosol via the reversible binding of calcium ions to calcium-binding proteins in the cytosol thereby modulating the spatial and temporal dynamics of changes in postsynaptic cytosolic calcium concentrations. obo:GO_0099567 obo:go.owl obo:GO_0099567 calcium ion binding involved in regulation of postsynaptic cytosolic calcium levels obo:GO_0099567 postsynaptic calcium ion buffering obo:GO_0099567 molecular_function obo:GO_0099567 regulation of postsynaptic cytosolic calcium ion concentration by calcium ion buffering obo:GO_0099567 GO:0099567 obo:GO_0099567 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_synapse obo:GO_0099567 calcium ion binding involved in regulation of postsynaptic cytosolic calcium ion concentration obo:GO_0099587 The directed movement of inorganic ions from outside of a cell, across the plasma membrane and into the cytosol. obo:GO_0099587 obo:go.owl obo:GO_0099587 inorganic ion import into cell obo:GO_0099587 biological_process obo:GO_0099587 GO:0099587 obo:GO_0099587 inorganic ion import across plasma membrane obo:GO_0099609 Interacting selectively and non-covalently with the side of a microtubule. obo:GO_0099609 obo:go.owl obo:GO_0099609 molecular_function obo:GO_0099609 GO:0099609 obo:GO_0099609 microtubule lateral binding obo:GO_0099623 Any process that modulates the establishment or extent of a change in membrane potential in the polarizing direction towards the resting potential in a cardiomyocyte. obo:GO_0099623 obo:go.owl obo:GO_0099623 regulation of cardiac muscle cell repolarization obo:GO_0099623 regulation of cardiomyocyte membrane repolarization obo:GO_0099623 biological_process obo:GO_0099623 heart repolarization obo:GO_0099623 GO:0099623 obo:GO_0099623 regulation of cardiac muscle cell membrane repolarization obo:GO_0100017 Any transcription from RNA polymerase II promoter process that negatively_regulates single organismal cell-cell adhesion obo:GO_0100017 obo:go.owl obo:GO_0100017 cjm obo:GO_0100017 2015-04-02T04:13:19Z obo:GO_0100017 biological_process obo:GO_0100017 GO:0100017 obo:GO_0100017 negative regulation of cell-cell adhesion by transcription from RNA polymerase II promoter obo:GO_0101006 Catalysis of the reaction: protein histidine phosphate + H2O = protein histidine + phosphate obo:GO_0101006 obo:go.owl obo:GO_0101006 GO:0008969 obo:GO_0101006 phosphohistidine phosphatase activity obo:GO_0101006 molecular_function obo:GO_0101006 GO:0101006 obo:GO_0101006 protein histidine phosphatase activity obo:GO_0101014 Catalysis of the reaction: [isocitrate dehydrogenase] phosphate + H2O = [isocitrate dehydrogenase] + phosphate. obo:GO_0101014 obo:go.owl obo:GO_0101014 isocitrate dehydrogenase kinase/phosphatase activity obo:GO_0101014 MetaCyc:ICITDEHASE-KIN-PHOSPHA obo:GO_0101014 molecular_function obo:GO_0101014 GO:0101014 obo:GO_0101014 [isocitrate dehydrogenase (NADP+)] phosphatase activity obo:GO_0101016 Interacting selectively and non-covalently with the FMN-binding domain of a protein. obo:GO_0101016 obo:go.owl obo:GO_0101016 molecular_function obo:GO_0101016 GO:0101016 obo:GO_0101016 FMN-binding domain binding obo:GO_0104004 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an environmental stimulus. obo:GO_0104004 obo:go.owl obo:GO_0104004 dos obo:GO_0104004 2017-02-17T16:02:42Z obo:GO_0104004 biological_process obo:GO_0104004 GO:0104004 obo:GO_0104004 cellular response to environmental stimulus obo:GO_0106011 Any process that regulates the localization of a protein to the medial cortex. obo:GO_0106011 obo:go.owl obo:GO_0106011 hjd obo:GO_0106011 2017-04-27T17:29:56Z obo:GO_0106011 biological_process obo:GO_0106011 GO:0106011 obo:GO_0106011 regulation of protein localization to medial cortex obo:GO_0106012 Any process that activates or increases the frequency, rate or extent of protein localization to the medial cortex. obo:GO_0106012 obo:go.owl obo:GO_0106012 hjd obo:GO_0106012 2017-04-27T17:36:17Z obo:GO_0106012 biological_process obo:GO_0106012 GO:0106012 obo:GO_0106012 positive regulation of protein localization to medial cortex obo:GO_0106013 Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to the cell cortex of the cell tip. obo:GO_0106013 obo:go.owl obo:GO_0106013 hjd obo:GO_0106013 2017-04-28T13:45:38Z obo:GO_0106013 biological_process obo:GO_0106013 GO:0106013 obo:GO_0106013 negative regulation of protein localization to cell cortex of cell tip obo:GO_0106080 Interacting selectively and non-covalently with the GATOR1 complex. obo:GO_0106080 obo:go.owl obo:GO_0106080 hjd obo:GO_0106080 2017-12-22T14:49:54Z obo:GO_0106080 molecular_function obo:GO_0106080 GO:0106080 obo:GO_0106080 GATOR1 complex binding obo:GO_0106128 Any process that stops, prevents or reduces the frequency, rate or extent of store-operated calcium entry. obo:GO_0106128 obo:go.owl obo:GO_0106128 hjd obo:GO_0106128 2018-05-10T18:59:12Z obo:GO_0106128 biological_process obo:GO_0106128 GO:0106128 obo:GO_0106128 negative regulation of store-operated calcium entry obo:GO_0106129 Any process that activates or increases the frequency, rate or extent of store-operated calcium entry. obo:GO_0106129 obo:go.owl obo:GO_0106129 hjd obo:GO_0106129 2018-05-10T19:02:40Z obo:GO_0106129 biological_process obo:GO_0106129 GO:0106129 obo:GO_0106129 positive regulation of store-operated calcium entry obo:GO_0106137 Interacting selectively and non-covalently with the IkappaB kinase complex. obo:GO_0106137 obo:go.owl obo:GO_0106137 hjd obo:GO_0106137 2018-08-15T14:05:10Z obo:GO_0106137 molecular_function obo:GO_0106137 GO:0106137 obo:GO_0106137 IkappaB kinase complex binding obo:GO_0106138 Interacting selectively and non-covalently with a Sec61 translocon complex. obo:GO_0106138 obo:go.owl obo:GO_0106138 hjd obo:GO_0106138 2018-08-15T14:50:29Z obo:GO_0106138 molecular_function obo:GO_0106138 GO:0106138 obo:GO_0106138 Sec61 translocon complex binding obo:GO_0106140 Interacting selectively and non-covalently with the P-TEFb complex. obo:GO_0106140 obo:go.owl obo:GO_0106140 hjd obo:GO_0106140 2018-08-17T18:17:50Z obo:GO_0106140 molecular_function obo:GO_0106140 GO:0106140 obo:GO_0106140 P-TEFb complex binding obo:GO_0106151 nteracting selectivity and noncovalently with a cyclic nucleotide mimicking protein motif that is part of the same protein. The CNBHD is a domain on KCNH channels that creates a binding pocket on the KCNH channel that resembles the cyclic nucleotide- binding domain on other ion channels. It binds to a peptide motif that is part of the same protein rather than a cyclic nucleotide. obo:GO_0106151 obo:go.owl obo:GO_0106151 hjd obo:GO_0106151 2018-09-18T20:47:35Z obo:GO_0106151 molecular_function obo:GO_0106151 GO:0106151 obo:GO_0106151 It is unclear if the motif bound by CNBHD is a specific motif or just a beta sheet with the appropriate amino acids. obo:GO_0106151 CNBH domain intrinsic ligand binding obo:GO_0106153 Interacting selectively and non-covalently with a histone in which a residue has been modified by phosphorylation. Histones are any of a group of water-soluble proteins found in association with the DNA of eukaroytic chromosomes. obo:GO_0106153 obo:go.owl obo:GO_0106153 hjd obo:GO_0106153 2018-09-19T17:23:06Z obo:GO_0106153 molecular_function obo:GO_0106153 GO:0106153 obo:GO_0106153 phosphorylated histone binding obo:GO_0110022 Any process that modulates the frequency, rate or extent of cardiac muscle myoblast proliferation. obo:GO_0110022 obo:go.owl obo:GO_0110022 kmv obo:GO_0110022 2017-06-29T15:11:47Z obo:GO_0110022 biological_process obo:GO_0110022 GO:0110022 obo:GO_0110022 regulation of cardiac muscle myoblast proliferation obo:GO_0110023 Any process that stops, prevents, or reduces the frequency, rate or extent of cardiac muscle myoblast proliferation. obo:GO_0110023 obo:go.owl obo:GO_0110023 kmv obo:GO_0110023 2017-06-29T15:18:30Z obo:GO_0110023 biological_process obo:GO_0110023 GO:0110023 obo:GO_0110023 negative regulation of cardiac muscle myoblast proliferation obo:GO_0110024 Any process that activates or increases the frequency, rate or extent of cardiac muscle myoblast proliferation. obo:GO_0110024 obo:go.owl obo:GO_0110024 kmv obo:GO_0110024 2017-06-29T15:24:16Z obo:GO_0110024 biological_process obo:GO_0110024 GO:0110024 obo:GO_0110024 positive regulation of cardiac muscle myoblast proliferation obo:GO_0110035 The activity of binding selectively, and in a sequence-specific manner, a replication fork barrier found in rDNA spacers, and distorting the original structure of DNA, typically a straight helix, into a bend, or increasing the bend if the original structure was intrinsically bent due to its sequence. obo:GO_0110035 obo:go.owl obo:GO_0110035 kmv obo:GO_0110035 2017-07-17T21:09:50Z obo:GO_0110035 molecular_function obo:GO_0110035 GO:0110035 obo:GO_0110035 rDNA spacer replication fork barrier binding, bending obo:GO_0110036 Interacting selectively and non-covalently with the C2 domain of a protein, a protein structural domain involved in targeting proteins to cell membranes. obo:GO_0110036 obo:go.owl obo:GO_0110036 kmv obo:GO_0110036 2017-07-20T20:45:56Z obo:GO_0110036 molecular_function obo:GO_0110036 GO:0110036 obo:GO_0110036 C2 domain binding obo:GO_0110065 Any process that modulates the frequency, rate or extent of mitotic telomere clustering during interphase. obo:GO_0110065 obo:go.owl obo:GO_0110065 kmv obo:GO_0110065 2017-11-17T22:03:40Z obo:GO_0110065 regulation of mitotic telomere clustering during interphase obo:GO_0110065 biological_process obo:GO_0110065 GO:0110065 obo:GO_0110065 regulation of interphase mitotic telomere clustering obo:GO_0110066 Any process that stops, prevents, or reduces the frequency, rate or extent of mitotic telomere clustering during interphase. obo:GO_0110066 obo:go.owl obo:GO_0110066 kmv obo:GO_0110066 2017-11-17T22:11:59Z obo:GO_0110066 negative regulation of mitotic telomere clustering during interphase obo:GO_0110066 telomere dispersion during interphase obo:GO_0110066 biological_process obo:GO_0110066 GO:0110066 obo:GO_0110066 negative regulation of interphase mitotic telomere clustering obo:GO_0110097 Any process that modulates the frequency, rate or extent of calcium import into the mitochondrion. obo:GO_0110097 obo:go.owl obo:GO_0110097 kmv obo:GO_0110097 2018-02-28T00:33:51Z obo:GO_0110097 biological_process obo:GO_0110097 GO:0110097 obo:GO_0110097 regulation of calcium import into the mitochondrion obo:GO_0110098 Any process that activates or increases the frequency, rate or extent of calcium import into the mitochondrion. obo:GO_0110098 obo:go.owl obo:GO_0110098 kmv obo:GO_0110098 2018-02-28T00:39:13Z obo:GO_0110098 biological_process obo:GO_0110098 GO:0110098 obo:GO_0110098 positive regulation of calcium import into the mitochondrion obo:GO_0110099 Any process that stops, prevents or reduces the frequency, rate or extent of calcium ion import into the mitochondrion. obo:GO_0110099 obo:go.owl obo:GO_0110099 kmv obo:GO_0110099 2018-02-28T00:42:06Z obo:GO_0110099 biological_process obo:GO_0110099 GO:0110099 obo:GO_0110099 negative regulation of calcium import into the mitochondrion obo:GO_0120022 Interacting selectively and non-covalently with glucagon, a polypeptide hormone involved in glucose response. It is produced by pancreatic alpha cells and raises the concentration of glucose in the blood. obo:GO_0120022 obo:go.owl obo:GO_0120022 kchris obo:GO_0120022 2017-03-17T14:46:29Z obo:GO_0120022 molecular_function obo:GO_0120022 GO:0120022 obo:GO_0120022 glucagon binding obo:GO_0120023 Interacting selectively and non-covalently with somatostatin, a polypeptide hormone involved in regulating pancreatic alpha and pancreatic beta cells and controlling growth hormone secretion as well as many other functions. Somatostatin is produced by several cell types including pancreatic delta cells. There are several different mature forms of somatostatin. obo:GO_0120023 obo:go.owl obo:GO_0120023 kchris obo:GO_0120023 2017-03-17T14:54:21Z obo:GO_0120023 molecular_function obo:GO_0120023 GO:0120023 obo:GO_0120023 somatostatin binding obo:GO_0120024 Interacting selectively and non-covalently with glucagon-like peptide, a antihyperglycemic hormone. Glucagon-like peptide is derived from the glucagon gene produced by pancreatic alpha cells. obo:GO_0120024 obo:go.owl obo:GO_0120024 kchris obo:GO_0120024 2017-03-17T14:57:26Z obo:GO_0120024 molecular_function obo:GO_0120024 GO:0120024 obo:GO_0120024 glucagon-like peptide binding obo:GO_0120029 The directed movement of hydrogen ions (protons) from inside a cell, across the plasma membrane and into the extracellular region. obo:GO_0120029 obo:go.owl obo:GO_0120029 kchris obo:GO_0120029 2017-03-31T17:39:03Z obo:GO_0120029 hydrogen ion export from cell obo:GO_0120029 proton export from cell obo:GO_0120029 hydrogen ion export across plasma membrane obo:GO_0120029 proton export across plasma membrane obo:GO_0120029 biological_process obo:GO_0120029 GO:0120029 obo:GO_0120029 proton export across plasma membrane obo:GO_0120040 Any process that modulates the frequency, rate or extent of macrophage proliferation. obo:GO_0120040 obo:go.owl obo:GO_0120040 kchris obo:GO_0120040 2017-05-10T20:38:19Z obo:GO_0120040 biological_process obo:GO_0120040 GO:0120040 obo:GO_0120040 regulation of macrophage proliferation obo:GO_0120041 Any process that activates or increases the frequency, rate or extent of macrophage proliferation. obo:GO_0120041 obo:go.owl obo:GO_0120041 kchris obo:GO_0120041 2017-05-10T20:45:01Z obo:GO_0120041 biological_process obo:GO_0120041 GO:0120041 obo:GO_0120041 positive regulation of macrophage proliferation obo:GO_0120042 Any process that stops, prevents, or reduces the frequency, rate or extent of macrophage proliferation. obo:GO_0120042 obo:go.owl obo:GO_0120042 kchris obo:GO_0120042 2017-05-10T20:51:40Z obo:GO_0120042 biological_process obo:GO_0120042 GO:0120042 obo:GO_0120042 negative regulation of macrophage proliferation obo:GO_0120046 Any process that modulates the frequency, rate or extent of protein localization to a medial cortical node. obo:GO_0120046 obo:go.owl obo:GO_0120046 kchris obo:GO_0120046 2017-06-02T17:29:23Z obo:GO_0120046 biological_process obo:GO_0120046 GO:0120046 obo:GO_0120046 regulation of protein localization to medial cortical node obo:GO_0120047 Any process that activates or increases the frequency, rate or extent of protein localization to a medial cortical node. obo:GO_0120047 obo:go.owl obo:GO_0120047 kchris obo:GO_0120047 2017-06-02T17:30:38Z obo:GO_0120047 biological_process obo:GO_0120047 GO:0120047 obo:GO_0120047 positive regulation of protein localization to medial cortical node obo:GO_0120126 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a starvation stimulus, deprivation of copper ion. obo:GO_0120126 obo:go.owl obo:GO_0120126 kchris obo:GO_0120126 2018-02-12T19:49:19Z obo:GO_0120126 biological_process obo:GO_0120126 GO:0120126 obo:GO_0120126 response to copper ion starvation obo:GO_0120127 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a starvation stimulus, deprivation of zinc ion. obo:GO_0120127 obo:go.owl obo:GO_0120127 kchris obo:GO_0120127 2018-02-12T19:57:02Z obo:GO_0120127 biological_process obo:GO_0120127 GO:0120127 obo:GO_0120127 response to zinc ion starvation obo:GO_0120146 Interacting selectively and non-covalently with sulfatide, also known as 3-O-sulfogalactosylceramide, SM4, or sulfated galactocerebroside. Sulfatide is a class of sulfoglycolipid, which are glycolipids that contain a sulfate group. obo:GO_0120146 obo:go.owl obo:GO_0120146 kchris obo:GO_0120146 2018-03-30T20:44:03Z obo:GO_0120146 3-O-sulfogalactosylceramide binding obo:GO_0120146 SM4 binding obo:GO_0120146 sulfated galactocerebroside binding obo:GO_0120146 molecular_function obo:GO_0120146 GO:0120146 obo:GO_0120146 sulfatide binding obo:GO_0120152 Interacting selectively and non-covalently with an outer dynein arm in the presence of calcium. obo:GO_0120152 obo:go.owl obo:GO_0120152 kchris obo:GO_0120152 2018-04-27T16:33:39Z obo:GO_0120152 molecular_function obo:GO_0120152 GO:0120152 obo:GO_0120152 calcium-dependent outer dynein arm binding obo:GO_0120153 Interacting selectively and non-covalently with any carbohydrate in the presence of calcium. obo:GO_0120153 obo:go.owl obo:GO_0120153 kchris obo:GO_0120153 2018-04-27T16:42:21Z obo:GO_0120153 molecular_function obo:GO_0120153 GO:0120153 obo:GO_0120153 calcium-dependent carbohydrate binding obo:GO_0120160 Interacting selectively and non-covalently with an intraciliary transport particle A (IFT A) complex. obo:GO_0120160 obo:go.owl obo:GO_0120160 kchris obo:GO_0120160 2018-05-11T22:28:11Z obo:GO_0120160 intraciliary transport complex A binding obo:GO_0120160 intraflagellar transport complex A binding obo:GO_0120160 intraflagellar transport particle A binding obo:GO_0120160 molecular_function obo:GO_0120160 IFT A complex binding obo:GO_0120160 GO:0120160 obo:GO_0120160 intraciliary transport particle A binding obo:GO_0120168 The series of events in which a hot stimulus is received and converted into a molecular signal as part of thermoception. obo:GO_0120168 obo:go.owl obo:GO_0120168 kchris obo:GO_0120168 2018-05-21T20:35:47Z obo:GO_0120168 sensory detection of heat stimulus during thermoception obo:GO_0120168 sensory detection of hot stimulus during thermoception obo:GO_0120168 sensory transduction of heat stimulus during thermoception obo:GO_0120168 sensory transduction of hot stimulus during thermoception obo:GO_0120168 thermoception, sensory detection of heat stimulus obo:GO_0120168 thermoception, sensory detection of hot stimulus obo:GO_0120168 thermoception, sensory transduction of heat stimulus obo:GO_0120168 thermoception, sensory transduction of hot stimulus obo:GO_0120168 biological_process obo:GO_0120168 GO:0120168 obo:GO_0120168 detection of hot stimulus involved in thermoception obo:GO_0120169 The series of events in which a cold stimulus is received and converted into a molecular signal as part of thermoception. obo:GO_0120169 obo:go.owl obo:GO_0120169 kchris obo:GO_0120169 2018-05-21T20:36:05Z obo:GO_0120169 sensory detection of cold stimulus during thermoception obo:GO_0120169 sensory transduction of cold stimulus during thermoception obo:GO_0120169 thermoception, sensory detection of cold stimulus obo:GO_0120169 thermoception, sensory transduction of cold stimulus obo:GO_0120169 biological_process obo:GO_0120169 GO:0120169 obo:GO_0120169 detection of cold stimulus involved in thermoception obo:GO_0120170 Interacting selectively and non-covalently with an intraciliary transport particle B (IFT B) complex. obo:GO_0120170 obo:go.owl obo:GO_0120170 kchris obo:GO_0120170 2018-05-11T22:28:11Z obo:GO_0120170 intraciliary transport complex B binding obo:GO_0120170 intraflagellar transport complex B binding obo:GO_0120170 intraflagellar transport particle B binding obo:GO_0120170 molecular_function obo:GO_0120170 IFT B complex binding obo:GO_0120170 GO:0120170 obo:GO_0120170 intraciliary transport particle B binding obo:GO_0120186 Any process that stops, prevents, or reduces the frequency, rate or extent of protein localization to chromatin. obo:GO_0120186 obo:go.owl obo:GO_0120186 kchris obo:GO_0120186 2018-07-14T00:19:32Z obo:GO_0120186 negative regulation of protein localisation to chromatin obo:GO_0120186 biological_process obo:GO_0120186 GO:0120186 obo:GO_0120186 negative regulation of protein localization to chromatin obo:GO_0120187 Any process that activates or increases the frequency, rate or extent of protein localization to chromatin. obo:GO_0120187 obo:go.owl obo:GO_0120187 kchris obo:GO_0120187 2018-07-14T00:21:28Z obo:GO_0120187 positive regulation of protein localisation to chromatin obo:GO_0120187 biological_process obo:GO_0120187 GO:0120187 obo:GO_0120187 positive regulation of protein localization to chromatin obo:GO_0120188 Any process that modulates the frequency, rate or extent of the controlled release of bile acid from a cell or a tissue. obo:GO_0120188 obo:go.owl obo:GO_0120188 kchris obo:GO_0120188 2018-07-16T22:28:58Z obo:GO_0120188 biological_process obo:GO_0120188 GO:0120188 obo:GO_0120188 regulation of bile acid secretion obo:GO_0120189 Any process that activates or increases the frequency, rate or extent of the controlled release of bile acid from a cell or a tissue. obo:GO_0120189 obo:go.owl obo:GO_0120189 kchris obo:GO_0120189 2018-07-16T22:36:17Z obo:GO_0120189 biological_process obo:GO_0120189 GO:0120189 obo:GO_0120189 positive regulation of bile acid secretion obo:GO_0120190 Any process that stops, prevents or reduces the frequency, rate or extent of the controlled release of bile acid from a cell or a tissue. obo:GO_0120190 obo:go.owl obo:GO_0120190 kchris obo:GO_0120190 2018-07-16T22:38:34Z obo:GO_0120190 biological_process obo:GO_0120190 GO:0120190 obo:GO_0120190 negative regulation of bile acid secretion obo:GO_0140030 Interacting selectively and non-covalently with a protein upon post-translation modification of the target protein. obo:GO_0140030 obo:go.owl obo:GO_0140030 pg obo:GO_0140030 2017-05-17T11:50:41Z obo:GO_0140030 molecular_function obo:GO_0140030 modified protein binding obo:GO_0140030 GO:0140030 obo:GO_0140030 This term should only be used when the binding is shown to require a post-translational modification: the interaction needs to be tested with and without the PTM. The binding does not need to be at the site of the modification. It may be that the PTM causes a conformational change that allows binding of the protein to another region; this type of modification-dependent protein binding is valid for annotation to this term. obo:GO_0140030 modification-dependent protein binding obo:GO_0140031 Interacting selectively and non-covalently with a protein upon phosphorylation of the target protein. obo:GO_0140031 obo:go.owl obo:GO_0140031 pg obo:GO_0140031 2017-05-17T15:15:19Z obo:GO_0140031 molecular_function obo:GO_0140031 GO:0140031 obo:GO_0140031 This term should only be used when the binding is shown to require phosphorylation of the target protein: the interaction needs to be tested with and without the PTM. The binding does not need to be at the site of phosphorylation. It may be that the phosphorylation causes a conformational change that allows binding of the protein to another region; this type of phosphorylation-dependent protein binding is valid for annotation to this term. obo:GO_0140031 phosphorylation-dependent protein binding obo:GO_0140032 Interacting selectively and non-covalently with a protein upon glycosylation of the target protein. obo:GO_0140032 obo:go.owl obo:GO_0140032 pg obo:GO_0140032 2017-05-17T15:20:50Z obo:GO_0140032 molecular_function obo:GO_0140032 GO:0140032 obo:GO_0140032 This term should only be used when the binding is shown to require glycosylation of the target protein: the interaction needs to be tested with and without the PTM. The binding does not need to be at the site of glycosylation. It may be that the glycosylation causes a conformational change that allows binding of the protein to another region; this type of glycosylation-dependent protein binding is valid for annotation to this term. obo:GO_0140032 glycosylation-dependent protein binding obo:GO_0140033 Interacting selectively and non-covalently with a protein upon acetylation of the target protein. obo:GO_0140033 obo:go.owl obo:GO_0140033 pg obo:GO_0140033 2017-05-17T15:35:43Z obo:GO_0140033 molecular_function obo:GO_0140033 GO:0140033 obo:GO_0140033 This term should only be used when the binding is shown to require acetylation of the target protein: the interaction needs to be tested with and without the PTM. The binding does not need to be at the site of acetylation. It may be that the acetylation causes a conformational change that allows binding of the protein to another region; this type of acetylation-dependent protein binding is valid for annotation to this term. obo:GO_0140033 acetylation-dependent protein binding obo:GO_0140034 Interacting selectively and non-covalently with a protein upon methylation of the target protein. obo:GO_0140034 obo:go.owl obo:GO_0140034 pg obo:GO_0140034 2017-05-17T15:40:02Z obo:GO_0140034 molecular_function obo:GO_0140034 GO:0140034 obo:GO_0140034 This term should only be used when the binding is shown to require methylation of the target protein: the interaction needs to be tested with and without the PTM. The binding does not need to be at the site of methylation. It may be that the methylation causes a conformational change that allows binding of the protein to another region; this type of methylation-dependent protein binding is valid for annotation to this term. obo:GO_0140034 methylation-dependent protein binding obo:GO_0140035 Interacting selectively and non-covalently with a protein upon modification by a ubiquitin-like protein of the target protein. obo:GO_0140035 obo:go.owl obo:GO_0140035 pg obo:GO_0140035 2017-05-18T06:11:27Z obo:GO_0140035 molecular_function obo:GO_0140035 GO:0140035 obo:GO_0140035 This term should only be used when the binding is shown to require a ubiquitin-like modification in the target protein: the interaction needs to be tested with and without the PTM. The binding does not need to be at the site of ubiquitin-like modification. It may be that the modification causes a conformational change that allows binding of the protein to another region; this type of modification-dependent protein binding is valid for annotation to this term. obo:GO_0140035 ubiquitination-like modification-dependent protein binding obo:GO_0140036 Interacting selectively and non-covalently with a protein upon ubiquitination of the target protein. obo:GO_0140036 obo:go.owl obo:GO_0140036 pg obo:GO_0140036 2017-05-18T06:29:14Z obo:GO_0140036 molecular_function obo:GO_0140036 GO:0140036 obo:GO_0140036 This term should only be used when the binding is shown to require ubiquitination of the target protein: the interaction needs to be tested with and without the PTM. The binding does not need to be at the site of ubiquitination. It may be that the ubiquitination causes a conformational change that allows binding of the protein to another region; this type of ubiquitination-dependent protein binding is valid for annotation to this term. obo:GO_0140036 ubiquitin-dependent protein binding obo:GO_0140037 Interacting selectively and non-covalently with a protein upon sumoylation of the target protein. obo:GO_0140037 obo:go.owl obo:GO_0140037 pg obo:GO_0140037 2017-05-18T06:29:27Z obo:GO_0140037 molecular_function obo:GO_0140037 GO:0140037 obo:GO_0140037 This term should only be used when the binding is shown to require sumoylation of the target protein: the interaction needs to be tested with and without the PTM. The binding does not need to be at the site of sumoylation. It may be that the sumoylation causes a conformational change that allows binding of the protein to another region; this type of sumoylation-dependent protein binding is valid for annotation to this term. obo:GO_0140037 sumo-dependent protein binding obo:GO_0140048 The directed movement of manganese ions from inside of a cell, across the plasma membrane and into the extracellular region. obo:GO_0140048 obo:go.owl obo:GO_0140048 pg obo:GO_0140048 2017-06-23T14:25:00Z obo:GO_0140048 manganese ion export from cell obo:GO_0140048 biological_process obo:GO_0140048 GO:0140048 obo:GO_0140048 manganese ion export across plasma membrane obo:GO_0140081 Interacting selectively and non-covalently with a glycosylated region of a protein. obo:GO_0140081 obo:go.owl obo:GO_0140081 pg obo:GO_0140081 2017-07-25T10:58:31Z obo:GO_0140081 molecular_function obo:GO_0140081 GO:0140081 obo:GO_0140081 glycosylated region protein binding obo:GO_0140090 Preferential binding of proteins on curved membranes. The binding to curved membranes by insertion (aka wedging) to curved membranes is mediated by both the hydrophobic and hydrophilic faces of the helix of membrane curvature sensing (MCS) proteins. obo:GO_0140090 obo:go.owl obo:GO_0140090 pg obo:GO_0140090 2017-08-19T20:37:54Z obo:GO_0140090 molecular_function obo:GO_0140090 GO:0140090 obo:GO_0140090 membrane curvature sensor activity obo:GO_0140096 Catalytic activity that acts to modify a protein. obo:GO_0140096 obo:go.owl obo:GO_0140096 pg obo:GO_0140096 2017-09-14T10:32:59Z obo:GO_0140096 molecular_function obo:GO_0140096 GO:0140096 obo:GO_0140096 https://github.com/geneontology/go-ontology/issues/14225 obo:GO_0140096 catalytic activity, acting on a protein obo:GO_0140098 Catalytic activity that acts to modify RNA. obo:GO_0140098 obo:go.owl obo:GO_0140098 pg obo:GO_0140098 2017-09-14T12:05:21Z obo:GO_0140098 molecular_function obo:GO_0140098 GO:0140098 obo:GO_0140098 https://github.com/geneontology/go-ontology/issues/14225 obo:GO_0140098 catalytic activity, acting on RNA obo:GO_0140101 Catalytic activity that acts to modify a tRNA. obo:GO_0140101 obo:go.owl obo:GO_0140101 pg obo:GO_0140101 2017-09-15T18:41:41Z obo:GO_0140101 molecular_function obo:GO_0140101 GO:0140101 obo:GO_0140101 catalytic activity, acting on a tRNA obo:GO_0140141 The process in which a potassium ion is transported across a mitochondrial membrane, into or out of the mitochondrion. obo:GO_0140141 obo:go.owl obo:GO_0140141 pg obo:GO_0140141 2017-11-24T13:26:42Z obo:GO_0140141 biological_process obo:GO_0140141 GO:0140141 obo:GO_0140141 mitochondrial potassium ion transmembrane transport obo:GO_0140145 The directed movement of copper ions out of the vacuole across the vacuolar membrane. obo:GO_0140145 obo:go.owl obo:GO_0140145 pg obo:GO_0140145 2017-12-13T15:02:39Z obo:GO_0140145 biological_process obo:GO_0140145 GO:0140145 obo:GO_0140145 copper ion export from vacuole obo:GO_0140146 The directed movement of calcium cations into the vacuole across the vacuolar membrane. obo:GO_0140146 obo:go.owl obo:GO_0140146 pg obo:GO_0140146 2017-12-13T15:15:29Z obo:GO_0140146 biological_process obo:GO_0140146 GO:0140146 obo:GO_0140146 calcium ion import into vacuole obo:GO_0140147 The directed movement of zinc ions from inside the vacuole across the vacuolar membrane and into the cytosol. obo:GO_0140147 obo:go.owl obo:GO_0140147 pg obo:GO_0140147 2017-12-13T15:21:10Z obo:GO_0140147 biological_process obo:GO_0140147 GO:0140147 obo:GO_0140147 zinc ion export from vacuole obo:GO_0140164 Interacting selectively and non-covalently with the Golgi transport complex, a multisubunit tethering complex of the CATCHR family. obo:GO_0140164 obo:go.owl obo:GO_0140164 pg obo:GO_0140164 2018-02-08T11:49:38Z obo:GO_0140164 COG complex binding obo:GO_0140164 molecular_function obo:GO_0140164 GO:0140164 obo:GO_0140164 Golgi transport complex binding obo:GO_0140209 The directed import of zinc(2+) from the cytosol, across the endoplasmic reticulum membrane, into the endoplasmic reticulum. obo:GO_0140209 obo:go.owl obo:GO_0140209 pg obo:GO_0140209 2018-03-19T10:40:01Z obo:GO_0140209 zinc ion import across endoplasmic reticulum obo:GO_0140209 zinc ion import into ER obo:GO_0140209 zinc(2+) import across endoplasmic reticulum obo:GO_0140209 zinc(2+) import into endoplasmic reticulum obo:GO_0140209 biological_process obo:GO_0140209 GO:0140209 obo:GO_0140209 This term covers zinc(2+) import *across* the endoplasmic reticulum membrane through a channel or pore. It does not cover import via vesicle fusion with endoplasmic reticulum membrane, as in this case transport does not involve crossing the membrane. obo:GO_0140209 zinc ion import into endoplasmic reticulum obo:GO_0140259 Interacting selectively and non-covalently with a PRC1 complex. obo:GO_0140259 obo:go.owl obo:GO_0140259 pg obo:GO_0140259 2018-09-10T16:48:18Z obo:GO_0140259 molecular_function obo:GO_0140259 GO:0140259 obo:GO_0140259 PRC1 complex binding obo:GO_0140260 Interacting selectively and non-covalently with a mitochondrial proton-transporting ATP synthase complex. obo:GO_0140260 obo:go.owl obo:GO_0140260 pg obo:GO_0140260 2018-09-10T19:38:26Z obo:GO_0140260 molecular_function obo:GO_0140260 GO:0140260 obo:GO_0140260 mitochondrial proton-transporting ATP synthase complex binding obo:GO_0140262 Interacting selectively and non-covalently with a mRNA cap binding complex. obo:GO_0140262 obo:go.owl obo:GO_0140262 pg obo:GO_0140262 2018-09-12T12:56:16Z obo:GO_0140262 molecular_function obo:GO_0140262 GO:0140262 obo:GO_0140262 mRNA cap binding complex binding obo:GO_0140295 The activity of a pathogen-derived entity that interacts with a host receptor to activate effector-triggered immunity. obo:GO_0140295 obo:go.owl obo:GO_0140295 pg obo:GO_0140295 2018-11-26T13:30:21Z obo:GO_0140295 molecular_function obo:GO_0140295 innate receptor ligand activity obo:GO_0140295 GO:0140295 obo:GO_0140295 pathogen-derived receptor ligand activity obo:GO_0140296 Interacting selectively and non-covalently with a general transcription initiation factor, a protein that contributes to transcription start site selection and transcription initiation. obo:GO_0140296 obo:go.owl obo:GO_0140296 pg obo:GO_0140296 2018-11-28T12:48:06Z obo:GO_0140296 molecular_function obo:GO_0140296 GO:0140296 obo:GO_0140296 general transcription initiation factor binding obo:GO_0140297 Interacting selectively and non-covalently with a DNA-binding transcription factor, a protein that interacts with a specific DNA sequence (sometimes referred to as a motif) within the regulatory region of a gene to modulate transcription. obo:GO_0140297 obo:go.owl obo:GO_0140297 pg obo:GO_0140297 2018-11-28T12:48:20Z obo:GO_0140297 molecular_function obo:GO_0140297 GO:0140297 obo:GO_0140297 DNA-binding transcription factor binding obo:GO_0140298 Uptake of iron into a cell via binding to an extracellular receptor, which is internalized by endocytosis. obo:GO_0140298 obo:go.owl obo:GO_0140298 pg obo:GO_0140298 2018-12-10T10:31:31Z obo:GO_0140298 iron import into cell by endocytosis obo:GO_0140298 biological_process obo:GO_0140298 GO:0140298 obo:GO_0140298 endocytic iron import into cell obo:GO_0140299 Binding to a small molecule and eliciting a change in the protein's activity in response to the intracellular level of that small molecule. obo:GO_0140299 obo:go.owl obo:GO_0140299 pg obo:GO_0140299 2018-12-10T14:30:28Z obo:GO_0140299 small molecular sensor activity obo:GO_0140299 molecular_function obo:GO_0140299 GO:0140299 obo:GO_0140299 small molecule sensor activity obo:GO_0140325 Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to the medial cortex. obo:GO_0140325 obo:go.owl obo:GO_0140325 pg obo:GO_0140325 2019-04-17T11:58:27Z obo:GO_0140325 biological_process obo:GO_0140325 GO:0140325 obo:GO_0140325 negative regulation of protein localization to medial cortex obo:GO_0140357 The directed movement of heme from inside the vacuole across the vacuolar membrane and into the cytosol. obo:GO_0140357 obo:go.owl obo:GO_0140357 pg obo:GO_0140357 2019-05-28T07:40:48Z obo:GO_0140357 biological_process obo:GO_0140357 GO:0140357 obo:GO_0140357 Create new term see https://github.com/geneontology/go-ontology/issues/17407 obo:GO_0140357 heme export from vacuole to cytoplasm obo:GO_0150031 Any process that modulates the frequency, rate or extent of protein localization to lysosome. obo:GO_0150031 obo:go.owl obo:GO_0150031 BarbaraCzub obo:GO_0150031 2018-02-06T17:07:03Z obo:GO_0150031 biological_process obo:GO_0150031 GO:0150031 obo:GO_0150031 regulation of protein localization to lysosome obo:GO_0150032 Any process that activates or increases the frequency, rate or extent of protein localization to lysosome. obo:GO_0150032 obo:go.owl obo:GO_0150032 BarbaraCzub obo:GO_0150032 2018-02-06T17:11:02Z obo:GO_0150032 biological_process obo:GO_0150032 GO:0150032 obo:GO_0150032 positive regulation of protein localization to lysosome obo:GO_0150033 Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to lysosome. obo:GO_0150033 obo:go.owl obo:GO_0150033 BarbaraCzub obo:GO_0150033 2018-02-06T17:14:16Z obo:GO_0150033 biological_process obo:GO_0150033 GO:0150033 obo:GO_0150033 negative regulation of protein localization to lysosome obo:GO_0150054 Any process that modulates the frequency, rate or extent of postsynaptic neurotransmitter receptor diffusion trapping. obo:GO_0150054 obo:go.owl obo:GO_0150054 BarbaraCzub obo:GO_0150054 2018-05-10T14:26:59Z obo:GO_0150054 biological_process obo:GO_0150054 GO:0150054 obo:GO_0150054 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_synapse obo:GO_0150054 regulation of postsynaptic neurotransmitter receptor diffusion trapping obo:GO_0150100 Any RNA binding that is involved in posttranscriptional gene silencing. obo:GO_0150100 obo:go.owl obo:GO_0150100 BarbaraCzub obo:GO_0150100 2019-03-11T11:48:27Z obo:GO_0150100 RNA binding involved in PTGS obo:GO_0150100 RNA binding involved in post-transcriptional gene silencing obo:GO_0150100 RNA binding involved in quelling obo:GO_0150100 molecular_function obo:GO_0150100 RNA binding involved in cosuppression obo:GO_0150100 GO:0150100 obo:GO_0150100 RNA binding involved in posttranscriptional gene silencing obo:GO_1900046 Any process that modulates the frequency, rate or extent of hemostasis. obo:GO_1900046 obo:go.owl obo:GO_1900046 jl obo:GO_1900046 2012-01-19T03:23:38Z obo:GO_1900046 biological_process obo:GO_1900046 GO:1900046 obo:GO_1900046 regulation of hemostasis obo:GO_1900047 Any process that stops, prevents or reduces the frequency, rate or extent of hemostasis. obo:GO_1900047 obo:go.owl obo:GO_1900047 jl obo:GO_1900047 2012-01-19T03:23:42Z obo:GO_1900047 down regulation of hemostasis obo:GO_1900047 down-regulation of hemostasis obo:GO_1900047 downregulation of hemostasis obo:GO_1900047 inhibition of hemostasis obo:GO_1900047 biological_process obo:GO_1900047 GO:1900047 obo:GO_1900047 negative regulation of hemostasis obo:GO_1900048 Any process that activates or increases the frequency, rate or extent of hemostasis. obo:GO_1900048 obo:go.owl obo:GO_1900048 jl obo:GO_1900048 2012-01-19T03:23:45Z obo:GO_1900048 up regulation of hemostasis obo:GO_1900048 up-regulation of hemostasis obo:GO_1900048 upregulation of hemostasis obo:GO_1900048 activation of hemostasis obo:GO_1900048 biological_process obo:GO_1900048 GO:1900048 obo:GO_1900048 positive regulation of hemostasis obo:GO_1900067 Any process that modulates the frequency, rate or extent of cellular response to alkalinity. obo:GO_1900067 obo:go.owl obo:GO_1900067 pr obo:GO_1900067 2012-01-26T02:34:59Z obo:GO_1900067 regulation of cellular response to alkalinity obo:GO_1900067 regulation of cellular response to basic pH obo:GO_1900067 biological_process obo:GO_1900067 GO:1900067 obo:GO_1900067 regulation of cellular response to alkaline pH obo:GO_1900071 Any process that modulates the frequency, rate or extent of sulfite transport. obo:GO_1900071 obo:go.owl obo:GO_1900071 dph obo:GO_1900071 2012-01-26T08:41:10Z obo:GO_1900071 regulation of sulphite transport obo:GO_1900071 biological_process obo:GO_1900071 GO:1900071 obo:GO_1900071 regulation of sulfite transport obo:GO_1900072 Any process that activates or increases the frequency, rate or extent of sulfite transport. obo:GO_1900072 obo:go.owl obo:GO_1900072 dph obo:GO_1900072 2012-01-26T08:41:16Z obo:GO_1900072 positive regulation of sulphite transport obo:GO_1900072 up regulation of sulphite transport obo:GO_1900072 up-regulation of sulphite transport obo:GO_1900072 upregulation of sulphite transport obo:GO_1900072 activation of sulfite transport obo:GO_1900072 activation of sulphite transport obo:GO_1900072 biological_process obo:GO_1900072 up regulation of sulfite transport obo:GO_1900072 up-regulation of sulfite transport obo:GO_1900072 upregulation of sulfite transport obo:GO_1900072 GO:1900072 obo:GO_1900072 positive regulation of sulfite transport obo:GO_1900128 Any process that modulates the frequency, rate or extent of G-protein activated inward rectifier potassium channel activity. obo:GO_1900128 obo:go.owl obo:GO_1900128 bf obo:GO_1900128 2012-02-23T03:12:53Z obo:GO_1900128 regulation of G protein activated inward rectifier potassium channel activity obo:GO_1900128 regulation of G protein enhanced inward rectifier potassium channel activity obo:GO_1900128 regulation of G-protein enhanced inward rectifier potassium channel activity obo:GO_1900128 regulation of G-protein-activated inward rectifier potassium channel activity obo:GO_1900128 regulation of G-protein-enhanced inward rectifier potassium channel activity obo:GO_1900128 biological_process obo:GO_1900128 GO:1900128 obo:GO_1900128 regulation of G-protein activated inward rectifier potassium channel activity obo:GO_1900129 Any process that activates or increases the frequency, rate or extent of G-protein activated inward rectifier potassium channel activity. obo:GO_1900129 obo:go.owl obo:GO_1900129 bf obo:GO_1900129 2012-02-23T03:12:58Z obo:GO_1900129 positive regulation of G protein activated inward rectifier potassium channel activity obo:GO_1900129 positive regulation of G protein enhanced inward rectifier potassium channel activity obo:GO_1900129 positive regulation of G-protein enhanced inward rectifier potassium channel activity obo:GO_1900129 positive regulation of G-protein-activated inward rectifier potassium channel activity obo:GO_1900129 positive regulation of G-protein-enhanced inward rectifier potassium channel activity obo:GO_1900129 up regulation of G protein activated inward rectifier potassium channel activity obo:GO_1900129 up regulation of G protein enhanced inward rectifier potassium channel activity obo:GO_1900129 up regulation of G-protein activated inward rectifier potassium channel activity obo:GO_1900129 up regulation of G-protein enhanced inward rectifier potassium channel activity obo:GO_1900129 up regulation of G-protein-activated inward rectifier potassium channel activity obo:GO_1900129 up regulation of G-protein-enhanced inward rectifier potassium channel activity obo:GO_1900129 up-regulation of G protein activated inward rectifier potassium channel activity obo:GO_1900129 up-regulation of G protein enhanced inward rectifier potassium channel activity obo:GO_1900129 up-regulation of G-protein activated inward rectifier potassium channel activity obo:GO_1900129 up-regulation of G-protein enhanced inward rectifier potassium channel activity obo:GO_1900129 up-regulation of G-protein-activated inward rectifier potassium channel activity obo:GO_1900129 up-regulation of G-protein-enhanced inward rectifier potassium channel activity obo:GO_1900129 upregulation of G protein activated inward rectifier potassium channel activity obo:GO_1900129 upregulation of G protein enhanced inward rectifier potassium channel activity obo:GO_1900129 upregulation of G-protein activated inward rectifier potassium channel activity obo:GO_1900129 upregulation of G-protein enhanced inward rectifier potassium channel activity obo:GO_1900129 upregulation of G-protein-activated inward rectifier potassium channel activity obo:GO_1900129 upregulation of G-protein-enhanced inward rectifier potassium channel activity obo:GO_1900129 activation of G protein activated inward rectifier potassium channel activity obo:GO_1900129 activation of G protein enhanced inward rectifier potassium channel activity obo:GO_1900129 activation of G-protein activated inward rectifier potassium channel activity obo:GO_1900129 activation of G-protein enhanced inward rectifier potassium channel activity obo:GO_1900129 activation of G-protein-activated inward rectifier potassium channel activity obo:GO_1900129 activation of G-protein-enhanced inward rectifier potassium channel activity obo:GO_1900129 biological_process obo:GO_1900129 GO:1900129 obo:GO_1900129 positive regulation of G-protein activated inward rectifier potassium channel activity obo:GO_1900180 Any process that modulates the frequency, rate or extent of protein localization to nucleus. obo:GO_1900180 obo:go.owl obo:GO_1900180 bf obo:GO_1900180 2012-03-12T01:23:44Z obo:GO_1900180 regulation of protein localisation to nucleus obo:GO_1900180 regulation of protein localization in cell nucleus obo:GO_1900180 regulation of protein localization in nucleus obo:GO_1900180 biological_process obo:GO_1900180 GO:1900180 obo:GO_1900180 regulation of protein localization to nucleus obo:GO_1900181 Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to nucleus. obo:GO_1900181 obo:go.owl obo:GO_1900181 bf obo:GO_1900181 2012-03-12T01:23:48Z obo:GO_1900181 down regulation of protein localisation to nucleus obo:GO_1900181 down regulation of protein localization in cell nucleus obo:GO_1900181 down regulation of protein localization in nucleus obo:GO_1900181 down regulation of protein localization to nucleus obo:GO_1900181 down-regulation of protein localisation to nucleus obo:GO_1900181 down-regulation of protein localization in cell nucleus obo:GO_1900181 down-regulation of protein localization in nucleus obo:GO_1900181 down-regulation of protein localization to nucleus obo:GO_1900181 downregulation of protein localisation to nucleus obo:GO_1900181 downregulation of protein localization in cell nucleus obo:GO_1900181 downregulation of protein localization in nucleus obo:GO_1900181 downregulation of protein localization to nucleus obo:GO_1900181 negative regulation of protein localisation to nucleus obo:GO_1900181 negative regulation of protein localization in cell nucleus obo:GO_1900181 negative regulation of protein localization in nucleus obo:GO_1900181 inhibition of protein localisation to nucleus obo:GO_1900181 inhibition of protein localization in cell nucleus obo:GO_1900181 inhibition of protein localization in nucleus obo:GO_1900181 inhibition of protein localization to nucleus obo:GO_1900181 biological_process obo:GO_1900181 GO:1900181 obo:GO_1900181 negative regulation of protein localization to nucleus obo:GO_1900182 Any process that activates or increases the frequency, rate or extent of protein localization to nucleus. obo:GO_1900182 obo:go.owl obo:GO_1900182 bf obo:GO_1900182 2012-03-12T01:23:52Z obo:GO_1900182 activation of protein localization in nucleus obo:GO_1900182 positive regulation of protein localisation to nucleus obo:GO_1900182 positive regulation of protein localization in cell nucleus obo:GO_1900182 positive regulation of protein localization in nucleus obo:GO_1900182 up regulation of protein localisation to nucleus obo:GO_1900182 up regulation of protein localization in cell nucleus obo:GO_1900182 up regulation of protein localization in nucleus obo:GO_1900182 up regulation of protein localization to nucleus obo:GO_1900182 up-regulation of protein localisation to nucleus obo:GO_1900182 up-regulation of protein localization in cell nucleus obo:GO_1900182 up-regulation of protein localization in nucleus obo:GO_1900182 up-regulation of protein localization to nucleus obo:GO_1900182 upregulation of protein localisation to nucleus obo:GO_1900182 upregulation of protein localization in cell nucleus obo:GO_1900182 upregulation of protein localization in nucleus obo:GO_1900182 upregulation of protein localization to nucleus obo:GO_1900182 activation of protein localisation to nucleus obo:GO_1900182 activation of protein localization in cell nucleus obo:GO_1900182 activation of protein localization to nucleus obo:GO_1900182 biological_process obo:GO_1900182 GO:1900182 obo:GO_1900182 positive regulation of protein localization to nucleus obo:GO_1900623 Any process that modulates the frequency, rate or extent of monocyte aggregation. obo:GO_1900623 obo:go.owl obo:GO_1900623 vk obo:GO_1900623 2012-05-21T01:07:17Z obo:GO_1900623 regulation of mononuclear phagocyte aggregation obo:GO_1900623 biological_process obo:GO_1900623 GO:1900623 obo:GO_1900623 regulation of monocyte aggregation obo:GO_1900624 Any process that stops, prevents or reduces the frequency, rate or extent of monocyte aggregation. obo:GO_1900624 obo:go.owl obo:GO_1900624 vk obo:GO_1900624 2012-05-21T01:07:37Z obo:GO_1900624 down regulation of monocyte aggregation obo:GO_1900624 down regulation of mononuclear phagocyte aggregation obo:GO_1900624 down-regulation of monocyte aggregation obo:GO_1900624 down-regulation of mononuclear phagocyte aggregation obo:GO_1900624 downregulation of monocyte aggregation obo:GO_1900624 downregulation of mononuclear phagocyte aggregation obo:GO_1900624 inhibition of mononuclear phagocyte aggregation obo:GO_1900624 negative regulation of mononuclear phagocyte aggregation obo:GO_1900624 inhibition of monocyte aggregation obo:GO_1900624 biological_process obo:GO_1900624 GO:1900624 obo:GO_1900624 negative regulation of monocyte aggregation obo:GO_1900625 Any process that activates or increases the frequency, rate or extent of monocyte aggregation. obo:GO_1900625 obo:go.owl obo:GO_1900625 vk obo:GO_1900625 2012-05-21T01:07:44Z obo:GO_1900625 activation of mononuclear phagocyte aggregation obo:GO_1900625 positive regulation of mononuclear phagocyte aggregation obo:GO_1900625 up regulation of monocyte aggregation obo:GO_1900625 up regulation of mononuclear phagocyte aggregation obo:GO_1900625 up-regulation of monocyte aggregation obo:GO_1900625 up-regulation of mononuclear phagocyte aggregation obo:GO_1900625 upregulation of monocyte aggregation obo:GO_1900625 upregulation of mononuclear phagocyte aggregation obo:GO_1900625 activation of monocyte aggregation obo:GO_1900625 biological_process obo:GO_1900625 GO:1900625 obo:GO_1900625 positive regulation of monocyte aggregation obo:GO_1900728 Any cardiac neural crest cell delamination that is involved in outflow tract morphogenesis. obo:GO_1900728 obo:go.owl obo:GO_1900728 bf obo:GO_1900728 2012-05-25T09:50:24Z obo:GO_1900728 biological_process obo:GO_1900728 GO:1900728 obo:GO_1900728 cardiac neural crest cell delamination involved in outflow tract morphogenesis obo:GO_1900750 Interacting selectively and non-covalently with an oligopeptide. obo:GO_1900750 obo:go.owl obo:GO_1900750 jl obo:GO_1900750 2012-05-29T02:13:31Z obo:GO_1900750 oligopeptides binding obo:GO_1900750 molecular_function obo:GO_1900750 Oligopeptid binding obo:GO_1900750 oligopeptido binding obo:GO_1900750 GO:1900750 obo:GO_1900750 oligopeptide binding obo:GO_1900995 Interacting selectively and non-covalently with ubiquinone-6. Ubiquinone-6 is a ubiquinone compound having a (2E,6E,10E,14E,18E)-3,7,11,15,19,23-hexamethyltetracosa-2,6,10,14,18,22-hexaen-1-yl substituent at position 2. obo:GO_1900995 obo:go.owl obo:GO_1900995 bf obo:GO_1900995 2012-06-14T02:49:15Z obo:GO_1900995 molecular_function obo:GO_1900995 GO:1900995 obo:GO_1900995 ubiquinone-6 binding obo:GO_1901016 Any process that modulates the frequency, rate or extent of potassium ion transmembrane transporter activity. obo:GO_1901016 obo:go.owl obo:GO_1901016 rl obo:GO_1901016 2012-06-15T01:13:49Z obo:GO_1901016 regulation of potassium transporter activity obo:GO_1901016 biological_process obo:GO_1901016 GO:1901016 obo:GO_1901016 regulation of potassium ion transmembrane transporter activity obo:GO_1901017 Any process that stops, prevents or reduces the frequency, rate or extent of potassium ion transmembrane transporter activity. obo:GO_1901017 obo:go.owl obo:GO_1901017 rl obo:GO_1901017 2012-06-15T01:14:10Z obo:GO_1901017 down regulation of potassium ion transmembrane transporter activity obo:GO_1901017 down regulation of potassium transporter activity obo:GO_1901017 down-regulation of potassium ion transmembrane transporter activity obo:GO_1901017 down-regulation of potassium transporter activity obo:GO_1901017 downregulation of potassium ion transmembrane transporter activity obo:GO_1901017 downregulation of potassium transporter activity obo:GO_1901017 inhibition of potassium transporter activity obo:GO_1901017 negative regulation of potassium transporter activity obo:GO_1901017 inhibition of potassium ion transmembrane transporter activity obo:GO_1901017 biological_process obo:GO_1901017 GO:1901017 obo:GO_1901017 negative regulation of potassium ion transmembrane transporter activity obo:GO_1901018 Any process that activates or increases the frequency, rate or extent of potassium ion transmembrane transporter activity. obo:GO_1901018 obo:go.owl obo:GO_1901018 rl obo:GO_1901018 2012-06-15T01:14:18Z obo:GO_1901018 activation of potassium transporter activity obo:GO_1901018 positive regulation of potassium transporter activity obo:GO_1901018 up regulation of potassium ion transmembrane transporter activity obo:GO_1901018 up regulation of potassium transporter activity obo:GO_1901018 up-regulation of potassium ion transmembrane transporter activity obo:GO_1901018 up-regulation of potassium transporter activity obo:GO_1901018 upregulation of potassium ion transmembrane transporter activity obo:GO_1901018 upregulation of potassium transporter activity obo:GO_1901018 activation of potassium ion transmembrane transporter activity obo:GO_1901018 biological_process obo:GO_1901018 GO:1901018 obo:GO_1901018 positive regulation of potassium ion transmembrane transporter activity obo:GO_1901019 Any process that modulates the frequency, rate or extent of calcium ion transmembrane transporter activity. obo:GO_1901019 obo:go.owl obo:GO_1901019 rl obo:GO_1901019 2012-06-15T07:54:12Z obo:GO_1901019 biological_process obo:GO_1901019 GO:1901019 obo:GO_1901019 regulation of calcium ion transmembrane transporter activity obo:GO_1901020 Any process that stops, prevents or reduces the frequency, rate or extent of calcium ion transmembrane transporter activity. obo:GO_1901020 obo:go.owl obo:GO_1901020 rl obo:GO_1901020 2012-06-15T07:54:32Z obo:GO_1901020 down regulation of calcium ion transmembrane transporter activity obo:GO_1901020 down-regulation of calcium ion transmembrane transporter activity obo:GO_1901020 downregulation of calcium ion transmembrane transporter activity obo:GO_1901020 inhibition of calcium ion transmembrane transporter activity obo:GO_1901020 biological_process obo:GO_1901020 GO:1901020 obo:GO_1901020 negative regulation of calcium ion transmembrane transporter activity obo:GO_1901021 Any process that activates or increases the frequency, rate or extent of calcium ion transmembrane transporter activity. obo:GO_1901021 obo:go.owl obo:GO_1901021 rl obo:GO_1901021 2012-06-15T07:54:40Z obo:GO_1901021 up regulation of calcium ion transmembrane transporter activity obo:GO_1901021 up-regulation of calcium ion transmembrane transporter activity obo:GO_1901021 upregulation of calcium ion transmembrane transporter activity obo:GO_1901021 activation of calcium ion transmembrane transporter activity obo:GO_1901021 biological_process obo:GO_1901021 GO:1901021 obo:GO_1901021 positive regulation of calcium ion transmembrane transporter activity obo:GO_1901135 The chemical reactions and pathways involving carbohydrate derivative. obo:GO_1901135 obo:go.owl obo:GO_1901135 bf obo:GO_1901135 2012-07-12T04:05:09Z obo:GO_1901135 carbohydrate derivative metabolism obo:GO_1901135 biological_process obo:GO_1901135 GO:1901135 obo:GO_1901135 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_agr obo:GO_1901135 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_mouse obo:GO_1901135 carbohydrate derivative metabolic process obo:GO_1901136 The chemical reactions and pathways resulting in the breakdown of carbohydrate derivative. obo:GO_1901136 obo:go.owl obo:GO_1901136 bf obo:GO_1901136 2012-07-12T04:05:31Z obo:GO_1901136 carbohydrate derivative breakdown obo:GO_1901136 carbohydrate derivative catabolism obo:GO_1901136 carbohydrate derivative degradation obo:GO_1901136 biological_process obo:GO_1901136 GO:1901136 obo:GO_1901136 carbohydrate derivative catabolic process obo:GO_1901149 Interacting selectively and non-covalently with salicylic acid. obo:GO_1901149 obo:go.owl obo:GO_1901149 dhl obo:GO_1901149 2012-07-16T05:26:38Z obo:GO_1901149 salicylic acid receptor obo:GO_1901149 molecular_function obo:GO_1901149 GO:1901149 obo:GO_1901149 salicylic acid binding obo:GO_1901198 Any positive regulation of calcium ion transport into cytosol that is involved in cellular response to calcium ion. obo:GO_1901198 obo:go.owl obo:GO_1901198 al obo:GO_1901198 2012-07-27T11:07:43Z obo:GO_1901198 positive regulation of calcium ion transport into cytosol involved in cellular response to Ca2+ ion obo:GO_1901198 biological_process obo:GO_1901198 GO:1901198 obo:GO_1901198 positive regulation of calcium ion transport into cytosol involved in cellular response to calcium ion obo:GO_1901199 Any positive regulation of calcium ion transport into cytosol that is involved in cellular response to salt stress. obo:GO_1901199 obo:go.owl obo:GO_1901199 al obo:GO_1901199 2012-07-27T11:09:37Z obo:GO_1901199 positive regulation of calcium ion transport into cytosol involved in cellular response to ionic osmotic stress obo:GO_1901199 positive regulation of calcium ion transport into cytosol involved in cellular salinity response obo:GO_1901199 biological_process obo:GO_1901199 GO:1901199 obo:GO_1901199 positive regulation of calcium ion transport into cytosol involved in cellular response to salt stress obo:GO_1901200 Any negative regulation of calcium ion transport into cytosol that is involved in cellular response to salt stress. obo:GO_1901200 obo:go.owl obo:GO_1901200 al obo:GO_1901200 2012-07-27T11:11:09Z obo:GO_1901200 negative regulation of calcium ion transport into cytosol involved in cellular response to ionic osmotic stress obo:GO_1901200 negative regulation of calcium ion transport into cytosol involved in cellular salinity response obo:GO_1901200 biological_process obo:GO_1901200 GO:1901200 obo:GO_1901200 negative regulation of calcium ion transport into cytosol involved in cellular response to salt stress obo:GO_1901255 Any nucleotide-excision repair that is involved in interstrand cross-link repair. obo:GO_1901255 obo:go.owl obo:GO_1901255 vw obo:GO_1901255 2012-08-09T06:09:50Z obo:GO_1901255 NER involved in ICL repair obo:GO_1901255 NER involved in interstrand cross-link repair obo:GO_1901255 nucleotide-excision repair involved in ICL repair obo:GO_1901255 biological_process obo:GO_1901255 GO:1901255 obo:GO_1901255 nucleotide-excision repair involved in interstrand cross-link repair obo:GO_1901265 Interacting selectively and non-covalently with nucleoside phosphate. obo:GO_1901265 obo:go.owl obo:GO_1901265 bf obo:GO_1901265 2012-08-17T12:59:58Z obo:GO_1901265 molecular_function obo:GO_1901265 GO:1901265 obo:GO_1901265 nucleoside phosphate binding obo:GO_1901324 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a trichodermin stimulus. obo:GO_1901324 obo:go.owl obo:GO_1901324 mah obo:GO_1901324 2012-08-30T10:11:07Z obo:GO_1901324 biological_process obo:GO_1901324 GO:1901324 obo:GO_1901324 response to trichodermin obo:GO_1901326 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a tetracycline stimulus. obo:GO_1901326 obo:go.owl obo:GO_1901326 mah obo:GO_1901326 2012-08-30T10:13:26Z obo:GO_1901326 biological_process obo:GO_1901326 GO:1901326 obo:GO_1901326 response to tetracycline obo:GO_1901338 Interacting selectively and non-covalently with catecholamine. obo:GO_1901338 obo:go.owl obo:GO_1901338 bf obo:GO_1901338 2012-09-03T14:08:44Z obo:GO_1901338 molecular_function obo:GO_1901338 GO:1901338 obo:GO_1901338 catecholamine binding obo:GO_1901339 Any process that modulates the frequency, rate or extent of store-operated calcium channel activity. obo:GO_1901339 obo:go.owl obo:GO_1901339 pr obo:GO_1901339 2012-09-03T14:23:10Z obo:GO_1901339 biological_process obo:GO_1901339 GO:1901339 obo:GO_1901339 regulation of store-operated calcium channel activity obo:GO_1901340 Any process that stops, prevents or reduces the frequency, rate or extent of store-operated calcium channel activity. obo:GO_1901340 obo:go.owl obo:GO_1901340 pr obo:GO_1901340 2012-09-03T14:24:21Z obo:GO_1901340 down regulation of store-operated calcium channel activity obo:GO_1901340 down-regulation of store-operated calcium channel activity obo:GO_1901340 downregulation of store-operated calcium channel activity obo:GO_1901340 inhibition of store-operated calcium channel activity obo:GO_1901340 biological_process obo:GO_1901340 GO:1901340 obo:GO_1901340 negative regulation of store-operated calcium channel activity obo:GO_1901341 Any process that activates or increases the frequency, rate or extent of store-operated calcium channel activity. obo:GO_1901341 obo:go.owl obo:GO_1901341 pr obo:GO_1901341 2012-09-03T14:24:38Z obo:GO_1901341 up regulation of store-operated calcium channel activity obo:GO_1901341 up-regulation of store-operated calcium channel activity obo:GO_1901341 upregulation of store-operated calcium channel activity obo:GO_1901341 activation of store-operated calcium channel activity obo:GO_1901341 biological_process obo:GO_1901341 GO:1901341 obo:GO_1901341 positive regulation of store-operated calcium channel activity obo:GO_1901359 Interacting selectively and non-covalently with tungstate. obo:GO_1901359 obo:go.owl obo:GO_1901359 cdasilva obo:GO_1901359 2012-09-14T08:33:56Z obo:GO_1901359 molecular_function obo:GO_1901359 GO:1901359 obo:GO_1901359 tungstate binding obo:GO_1901360 The chemical reactions and pathways involving organic cyclic compound. obo:GO_1901360 obo:go.owl obo:GO_1901360 bf obo:GO_1901360 2012-09-14T09:03:51Z obo:GO_1901360 organic cyclic compound metabolism obo:GO_1901360 biological_process obo:GO_1901360 GO:1901360 obo:GO_1901360 organic cyclic compound metabolic process obo:GO_1901362 The chemical reactions and pathways resulting in the formation of organic cyclic compound. obo:GO_1901362 obo:go.owl obo:GO_1901362 bf obo:GO_1901362 2012-09-14T09:05:22Z obo:GO_1901362 organic cyclic compound anabolism obo:GO_1901362 organic cyclic compound biosynthesis obo:GO_1901362 organic cyclic compound formation obo:GO_1901362 organic cyclic compound synthesis obo:GO_1901362 biological_process obo:GO_1901362 GO:1901362 obo:GO_1901362 organic cyclic compound biosynthetic process obo:GO_1901363 Interacting selectively and non-covalently with heterocyclic compound. obo:GO_1901363 obo:go.owl obo:GO_1901363 bf obo:GO_1901363 2012-09-14T13:53:50Z obo:GO_1901363 molecular_function obo:GO_1901363 GO:1901363 obo:GO_1901363 heterocyclic compound binding obo:GO_1901379 Any process that modulates the frequency, rate or extent of potassium ion transmembrane transport. obo:GO_1901379 obo:go.owl obo:GO_1901379 rl obo:GO_1901379 2012-09-28T15:58:00Z obo:GO_1901379 regulation of potassium ion membrane transport obo:GO_1901379 biological_process obo:GO_1901379 GO:1901379 obo:GO_1901379 regulation of potassium ion transmembrane transport obo:GO_1901380 Any process that stops, prevents or reduces the frequency, rate or extent of potassium ion transmembrane transport. obo:GO_1901380 obo:go.owl obo:GO_1901380 rl obo:GO_1901380 2012-09-28T15:59:08Z obo:GO_1901380 down regulation of potassium ion transmembrane transport obo:GO_1901380 down-regulation of potassium ion transmembrane transport obo:GO_1901380 downregulation of potassium ion transmembrane transport obo:GO_1901380 negative regulation of potassium ion membrane transport obo:GO_1901380 inhibition of potassium ion transmembrane transport obo:GO_1901380 biological_process obo:GO_1901380 GO:1901380 obo:GO_1901380 negative regulation of potassium ion transmembrane transport obo:GO_1901381 Any process that activates or increases the frequency, rate or extent of potassium ion transmembrane transport. obo:GO_1901381 obo:go.owl obo:GO_1901381 rl obo:GO_1901381 2012-09-28T15:59:25Z obo:GO_1901381 positive regulation of potassium ion membrane transport obo:GO_1901381 up regulation of potassium ion transmembrane transport obo:GO_1901381 up-regulation of potassium ion transmembrane transport obo:GO_1901381 upregulation of potassium ion transmembrane transport obo:GO_1901381 activation of potassium ion transmembrane transport obo:GO_1901381 biological_process obo:GO_1901381 GO:1901381 obo:GO_1901381 positive regulation of potassium ion transmembrane transport obo:GO_1901382 Any process that modulates the frequency, rate or extent of chorionic trophoblast cell proliferation. obo:GO_1901382 obo:go.owl obo:GO_1901382 vk obo:GO_1901382 2012-10-01T10:03:13Z obo:GO_1901382 biological_process obo:GO_1901382 GO:1901382 obo:GO_1901382 regulation of chorionic trophoblast cell proliferation obo:GO_1901383 Any process that stops, prevents or reduces the frequency, rate or extent of chorionic trophoblast cell proliferation. obo:GO_1901383 obo:go.owl obo:GO_1901383 vk obo:GO_1901383 2012-10-01T10:04:23Z obo:GO_1901383 down regulation of chorionic trophoblast cell proliferation obo:GO_1901383 down-regulation of chorionic trophoblast cell proliferation obo:GO_1901383 downregulation of chorionic trophoblast cell proliferation obo:GO_1901383 inhibition of chorionic trophoblast cell proliferation obo:GO_1901383 biological_process obo:GO_1901383 GO:1901383 obo:GO_1901383 negative regulation of chorionic trophoblast cell proliferation obo:GO_1901384 Any process that activates or increases the frequency, rate or extent of chorionic trophoblast cell proliferation. obo:GO_1901384 obo:go.owl obo:GO_1901384 vk obo:GO_1901384 2012-10-01T10:04:41Z obo:GO_1901384 up regulation of chorionic trophoblast cell proliferation obo:GO_1901384 up-regulation of chorionic trophoblast cell proliferation obo:GO_1901384 upregulation of chorionic trophoblast cell proliferation obo:GO_1901384 activation of chorionic trophoblast cell proliferation obo:GO_1901384 biological_process obo:GO_1901384 GO:1901384 obo:GO_1901384 positive regulation of chorionic trophoblast cell proliferation obo:GO_1901385 Any process that modulates the frequency, rate or extent of voltage-gated calcium channel activity. obo:GO_1901385 obo:go.owl obo:GO_1901385 vk obo:GO_1901385 2012-10-01T10:34:08Z obo:GO_1901385 regulation of depolarization-activated calcium channel obo:GO_1901385 regulation of depolarization-activated voltage gated calcium channel activity obo:GO_1901385 regulation of depolarization-activated voltage-gated calcium channel obo:GO_1901385 regulation of depolarization-activated voltage-gated calcium channel activity obo:GO_1901385 regulation of voltage gated calcium channel activity obo:GO_1901385 regulation of voltage-dependent calcium channel activity obo:GO_1901385 regulation of voltage-gated calcium ion channel activity obo:GO_1901385 regulation of voltage-sensitive calcium channel obo:GO_1901385 regulation of dihydropyridine-sensitive calcium channel activity obo:GO_1901385 biological_process obo:GO_1901385 GO:1901385 obo:GO_1901385 regulation of voltage-gated calcium channel activity obo:GO_1901386 Any process that stops, prevents or reduces the frequency, rate or extent of voltage-gated calcium channel activity. obo:GO_1901386 obo:go.owl obo:GO_1901386 vk obo:GO_1901386 2012-10-01T10:35:15Z obo:GO_1901386 down regulation of depolarization-activated calcium channel obo:GO_1901386 down-regulation of depolarization-activated calcium channel obo:GO_1901386 downregulation of depolarization-activated calcium channel obo:GO_1901386 inhibition of depolarization-activated calcium channel obo:GO_1901386 negative regulation of depolarization-activated calcium channel obo:GO_1901386 down regulation of depolarization-activated voltage gated calcium channel activity obo:GO_1901386 down regulation of depolarization-activated voltage-gated calcium channel obo:GO_1901386 down regulation of depolarization-activated voltage-gated calcium channel activity obo:GO_1901386 down regulation of voltage gated calcium channel activity obo:GO_1901386 down regulation of voltage-dependent calcium channel activity obo:GO_1901386 down regulation of voltage-gated calcium channel activity obo:GO_1901386 down regulation of voltage-gated calcium ion channel activity obo:GO_1901386 down regulation of voltage-sensitive calcium channel obo:GO_1901386 down-regulation of depolarization-activated voltage gated calcium channel activity obo:GO_1901386 down-regulation of depolarization-activated voltage-gated calcium channel obo:GO_1901386 down-regulation of depolarization-activated voltage-gated calcium channel activity obo:GO_1901386 down-regulation of voltage gated calcium channel activity obo:GO_1901386 down-regulation of voltage-dependent calcium channel activity obo:GO_1901386 down-regulation of voltage-gated calcium channel activity obo:GO_1901386 down-regulation of voltage-gated calcium ion channel activity obo:GO_1901386 down-regulation of voltage-sensitive calcium channel obo:GO_1901386 downregulation of depolarization-activated voltage gated calcium channel activity obo:GO_1901386 downregulation of depolarization-activated voltage-gated calcium channel obo:GO_1901386 downregulation of depolarization-activated voltage-gated calcium channel activity obo:GO_1901386 downregulation of voltage gated calcium channel activity obo:GO_1901386 downregulation of voltage-dependent calcium channel activity obo:GO_1901386 downregulation of voltage-gated calcium channel activity obo:GO_1901386 downregulation of voltage-gated calcium ion channel activity obo:GO_1901386 downregulation of voltage-sensitive calcium channel obo:GO_1901386 inhibition of depolarization-activated voltage gated calcium channel activity obo:GO_1901386 inhibition of depolarization-activated voltage-gated calcium channel obo:GO_1901386 inhibition of depolarization-activated voltage-gated calcium channel activity obo:GO_1901386 inhibition of voltage gated calcium channel activity obo:GO_1901386 inhibition of voltage-dependent calcium channel activity obo:GO_1901386 inhibition of voltage-gated calcium ion channel activity obo:GO_1901386 inhibition of voltage-sensitive calcium channel obo:GO_1901386 negative regulation of depolarization-activated voltage gated calcium channel activity obo:GO_1901386 negative regulation of depolarization-activated voltage-gated calcium channel obo:GO_1901386 negative regulation of depolarization-activated voltage-gated calcium channel activity obo:GO_1901386 negative regulation of voltage gated calcium channel activity obo:GO_1901386 negative regulation of voltage-dependent calcium channel activity obo:GO_1901386 negative regulation of voltage-gated calcium ion channel activity obo:GO_1901386 negative regulation of voltage-sensitive calcium channel obo:GO_1901386 down regulation of dihydropyridine-sensitive calcium channel activity obo:GO_1901386 down-regulation of dihydropyridine-sensitive calcium channel activity obo:GO_1901386 downregulation of dihydropyridine-sensitive calcium channel activity obo:GO_1901386 inhibition of dihydropyridine-sensitive calcium channel activity obo:GO_1901386 inhibition of voltage-gated calcium channel activity obo:GO_1901386 negative regulation of dihydropyridine-sensitive calcium channel activity obo:GO_1901386 biological_process obo:GO_1901386 GO:1901386 obo:GO_1901386 negative regulation of voltage-gated calcium channel activity obo:GO_1901387 Any process that activates or increases the frequency, rate or extent of voltage-gated calcium channel activity. obo:GO_1901387 obo:go.owl obo:GO_1901387 vk obo:GO_1901387 2012-10-01T10:35:32Z obo:GO_1901387 activation of depolarization-activated calcium channel obo:GO_1901387 positive regulation of depolarization-activated calcium channel obo:GO_1901387 up regulation of depolarization-activated calcium channel obo:GO_1901387 up-regulation of depolarization-activated calcium channel obo:GO_1901387 upregulation of depolarization-activated calcium channel obo:GO_1901387 activation of depolarization-activated voltage gated calcium channel activity obo:GO_1901387 activation of depolarization-activated voltage-gated calcium channel obo:GO_1901387 activation of depolarization-activated voltage-gated calcium channel activity obo:GO_1901387 activation of voltage gated calcium channel activity obo:GO_1901387 activation of voltage-dependent calcium channel activity obo:GO_1901387 activation of voltage-gated calcium ion channel activity obo:GO_1901387 activation of voltage-sensitive calcium channel obo:GO_1901387 positive regulation of depolarization-activated voltage gated calcium channel activity obo:GO_1901387 positive regulation of depolarization-activated voltage-gated calcium channel obo:GO_1901387 positive regulation of depolarization-activated voltage-gated calcium channel activity obo:GO_1901387 positive regulation of voltage gated calcium channel activity obo:GO_1901387 positive regulation of voltage-dependent calcium channel activity obo:GO_1901387 positive regulation of voltage-gated calcium ion channel activity obo:GO_1901387 positive regulation of voltage-sensitive calcium channel obo:GO_1901387 up regulation of depolarization-activated voltage gated calcium channel activity obo:GO_1901387 up regulation of depolarization-activated voltage-gated calcium channel obo:GO_1901387 up regulation of depolarization-activated voltage-gated calcium channel activity obo:GO_1901387 up regulation of voltage gated calcium channel activity obo:GO_1901387 up regulation of voltage-dependent calcium channel activity obo:GO_1901387 up regulation of voltage-gated calcium channel activity obo:GO_1901387 up regulation of voltage-gated calcium ion channel activity obo:GO_1901387 up regulation of voltage-sensitive calcium channel obo:GO_1901387 up-regulation of depolarization-activated voltage gated calcium channel activity obo:GO_1901387 up-regulation of depolarization-activated voltage-gated calcium channel obo:GO_1901387 up-regulation of depolarization-activated voltage-gated calcium channel activity obo:GO_1901387 up-regulation of voltage gated calcium channel activity obo:GO_1901387 up-regulation of voltage-dependent calcium channel activity obo:GO_1901387 up-regulation of voltage-gated calcium channel activity obo:GO_1901387 up-regulation of voltage-gated calcium ion channel activity obo:GO_1901387 up-regulation of voltage-sensitive calcium channel obo:GO_1901387 upregulation of depolarization-activated voltage gated calcium channel activity obo:GO_1901387 upregulation of depolarization-activated voltage-gated calcium channel obo:GO_1901387 upregulation of depolarization-activated voltage-gated calcium channel activity obo:GO_1901387 upregulation of voltage gated calcium channel activity obo:GO_1901387 upregulation of voltage-dependent calcium channel activity obo:GO_1901387 upregulation of voltage-gated calcium channel activity obo:GO_1901387 upregulation of voltage-gated calcium ion channel activity obo:GO_1901387 upregulation of voltage-sensitive calcium channel obo:GO_1901387 activation of dihydropyridine-sensitive calcium channel activity obo:GO_1901387 activation of voltage-gated calcium channel activity obo:GO_1901387 positive regulation of dihydropyridine-sensitive calcium channel activity obo:GO_1901387 up regulation of dihydropyridine-sensitive calcium channel activity obo:GO_1901387 up-regulation of dihydropyridine-sensitive calcium channel activity obo:GO_1901387 upregulation of dihydropyridine-sensitive calcium channel activity obo:GO_1901387 biological_process obo:GO_1901387 GO:1901387 obo:GO_1901387 positive regulation of voltage-gated calcium channel activity obo:GO_1901528 Any hydrogen peroxide mediated signaling pathway that is involved in stomatal movement. obo:GO_1901528 obo:go.owl obo:GO_1901528 tb obo:GO_1901528 2012-10-23T23:15:25Z obo:GO_1901528 H2O2 mediated signaling pathway involved in stomatal movement obo:GO_1901528 hydrogen peroxide mediated signalling pathway involved in stomatal movement obo:GO_1901528 biological_process obo:GO_1901528 GO:1901528 obo:GO_1901528 hydrogen peroxide mediated signaling pathway involved in stomatal movement obo:GO_1901529 Any process that activates or increases the frequency, rate or extent of anion channel activity. obo:GO_1901529 obo:go.owl obo:GO_1901529 tb obo:GO_1901529 2012-10-23T23:38:50Z obo:GO_1901529 up regulation of anion channel activity obo:GO_1901529 up-regulation of anion channel activity obo:GO_1901529 upregulation of anion channel activity obo:GO_1901529 activation of anion channel activity obo:GO_1901529 biological_process obo:GO_1901529 GO:1901529 obo:GO_1901529 positive regulation of anion channel activity obo:GO_1901531 Interacting selectively and non-covalently with hypochlorite. obo:GO_1901531 obo:go.owl obo:GO_1901531 pr obo:GO_1901531 2012-10-24T07:15:22Z obo:GO_1901531 molecular_function obo:GO_1901531 GO:1901531 obo:GO_1901531 hypochlorite binding obo:GO_1901564 The chemical reactions and pathways involving organonitrogen compound. obo:GO_1901564 obo:go.owl obo:GO_1901564 pr obo:GO_1901564 2012-11-04T15:17:52Z obo:GO_1901564 organonitrogen compound metabolism obo:GO_1901564 biological_process obo:GO_1901564 GO:1901564 obo:GO_1901564 organonitrogen compound metabolic process obo:GO_1901565 The chemical reactions and pathways resulting in the breakdown of organonitrogen compound. obo:GO_1901565 obo:go.owl obo:GO_1901565 pr obo:GO_1901565 2012-11-04T15:17:56Z obo:GO_1901565 organonitrogen compound breakdown obo:GO_1901565 organonitrogen compound catabolism obo:GO_1901565 organonitrogen compound degradation obo:GO_1901565 biological_process obo:GO_1901565 GO:1901565 obo:GO_1901565 organonitrogen compound catabolic process obo:GO_1901567 Interacting selectively and non-covalently with fatty acid derivative. obo:GO_1901567 obo:go.owl obo:GO_1901567 pr obo:GO_1901567 2012-11-04T17:13:28Z obo:GO_1901567 molecular_function obo:GO_1901567 GO:1901567 obo:GO_1901567 fatty acid derivative binding obo:GO_1901575 The chemical reactions and pathways resulting in the breakdown of an organic substance, any molecular entity containing carbon. obo:GO_1901575 obo:go.owl obo:GO_1901575 pr obo:GO_1901575 2012-11-05T11:04:36Z obo:GO_1901575 organic molecular entity breakdown obo:GO_1901575 organic molecular entity catabolic process obo:GO_1901575 organic molecular entity catabolism obo:GO_1901575 organic molecular entity degradation obo:GO_1901575 organic substance breakdown obo:GO_1901575 organic substance catabolism obo:GO_1901575 organic substance degradation obo:GO_1901575 biological_process obo:GO_1901575 GO:1901575 obo:GO_1901575 organic substance catabolic process obo:GO_1901576 The chemical reactions and pathways resulting in the formation of an organic substance, any molecular entity containing carbon. obo:GO_1901576 obo:go.owl obo:GO_1901576 pr obo:GO_1901576 2012-11-05T11:04:40Z obo:GO_1901576 organic molecular entity anabolism obo:GO_1901576 organic molecular entity biosynthesis obo:GO_1901576 organic molecular entity biosynthetic process obo:GO_1901576 organic molecular entity formation obo:GO_1901576 organic molecular entity synthesis obo:GO_1901576 organic substance anabolism obo:GO_1901576 organic substance biosynthesis obo:GO_1901576 organic substance formation obo:GO_1901576 organic substance synthesis obo:GO_1901576 biological_process obo:GO_1901576 GO:1901576 obo:GO_1901576 organic substance biosynthetic process obo:GO_1901585 Any process that modulates the frequency, rate or extent of acid-sensing ion channel activity. obo:GO_1901585 obo:go.owl obo:GO_1901585 jl obo:GO_1901585 2012-11-07T13:37:24Z obo:GO_1901585 regulation of ASIC activity obo:GO_1901585 biological_process obo:GO_1901585 GO:1901585 obo:GO_1901585 regulation of acid-sensing ion channel activity obo:GO_1901586 Any process that stops, prevents or reduces the frequency, rate or extent of acid-sensing ion channel activity. obo:GO_1901586 obo:go.owl obo:GO_1901586 jl obo:GO_1901586 2012-11-07T13:37:32Z obo:GO_1901586 down regulation of ASIC activity obo:GO_1901586 down regulation of acid-sensing ion channel activity obo:GO_1901586 down-regulation of ASIC activity obo:GO_1901586 down-regulation of acid-sensing ion channel activity obo:GO_1901586 downregulation of ASIC activity obo:GO_1901586 downregulation of acid-sensing ion channel activity obo:GO_1901586 inhibition of ASIC activity obo:GO_1901586 negative regulation of ASIC activity obo:GO_1901586 inhibition of acid-sensing ion channel activity obo:GO_1901586 biological_process obo:GO_1901586 GO:1901586 obo:GO_1901586 negative regulation of acid-sensing ion channel activity obo:GO_1901587 Any process that activates or increases the frequency, rate or extent of acid-sensing ion channel activity. obo:GO_1901587 obo:go.owl obo:GO_1901587 jl obo:GO_1901587 2012-11-07T13:37:37Z obo:GO_1901587 activation of ASIC activity obo:GO_1901587 positive regulation of ASIC activity obo:GO_1901587 up regulation of ASIC activity obo:GO_1901587 up regulation of acid-sensing ion channel activity obo:GO_1901587 up-regulation of ASIC activity obo:GO_1901587 up-regulation of acid-sensing ion channel activity obo:GO_1901587 upregulation of ASIC activity obo:GO_1901587 upregulation of acid-sensing ion channel activity obo:GO_1901587 activation of acid-sensing ion channel activity obo:GO_1901587 biological_process obo:GO_1901587 GO:1901587 obo:GO_1901587 positive regulation of acid-sensing ion channel activity obo:GO_1901602 Interacting selectively and non-covalently with dethiobiotin. obo:GO_1901602 obo:go.owl obo:GO_1901602 al obo:GO_1901602 2012-11-08T14:09:14Z obo:GO_1901602 molecular_function obo:GO_1901602 GO:1901602 obo:GO_1901602 dethiobiotin binding obo:GO_1901611 Interacting selectively and non-covalently with phosphatidylglycerol. obo:GO_1901611 obo:go.owl obo:GO_1901611 kmv obo:GO_1901611 2012-11-12T21:18:24Z obo:GO_1901611 molecular_function obo:GO_1901611 GO:1901611 obo:GO_1901611 phosphatidylglycerol binding obo:GO_1901612 Interacting selectively and non-covalently with cardiolipin. obo:GO_1901612 obo:go.owl obo:GO_1901612 kmv obo:GO_1901612 2012-11-12T21:19:50Z obo:GO_1901612 molecular_function obo:GO_1901612 GO:1901612 obo:GO_1901612 cardiolipin binding obo:GO_1901640 Interacting selectively and non-covalently with XTP. obo:GO_1901640 obo:go.owl obo:GO_1901640 tb obo:GO_1901640 2012-11-15T22:56:35Z obo:GO_1901640 molecular_function obo:GO_1901640 GO:1901640 obo:GO_1901640 XTP binding obo:GO_1901641 Interacting selectively and non-covalently with ITP. obo:GO_1901641 obo:go.owl obo:GO_1901641 tb obo:GO_1901641 2012-11-15T22:56:39Z obo:GO_1901641 molecular_function obo:GO_1901641 GO:1901641 obo:GO_1901641 ITP binding obo:GO_1901645 Any process that modulates the frequency, rate or extent of synoviocyte proliferation. obo:GO_1901645 obo:go.owl obo:GO_1901645 hjd obo:GO_1901645 2012-11-16T20:16:23Z obo:GO_1901645 biological_process obo:GO_1901645 GO:1901645 obo:GO_1901645 regulation of synoviocyte proliferation obo:GO_1901646 Any process that stops, prevents or reduces the frequency, rate or extent of synoviocyte proliferation. obo:GO_1901646 obo:go.owl obo:GO_1901646 hjd obo:GO_1901646 2012-11-16T20:16:27Z obo:GO_1901646 down regulation of synoviocyte proliferation obo:GO_1901646 down-regulation of synoviocyte proliferation obo:GO_1901646 downregulation of synoviocyte proliferation obo:GO_1901646 inhibition of synoviocyte proliferation obo:GO_1901646 biological_process obo:GO_1901646 GO:1901646 obo:GO_1901646 negative regulation of synoviocyte proliferation obo:GO_1901647 Any process that activates or increases the frequency, rate or extent of synoviocyte proliferation. obo:GO_1901647 obo:go.owl obo:GO_1901647 hjd obo:GO_1901647 2012-11-16T20:16:32Z obo:GO_1901647 up regulation of synoviocyte proliferation obo:GO_1901647 up-regulation of synoviocyte proliferation obo:GO_1901647 upregulation of synoviocyte proliferation obo:GO_1901647 activation of synoviocyte proliferation obo:GO_1901647 biological_process obo:GO_1901647 GO:1901647 obo:GO_1901647 positive regulation of synoviocyte proliferation obo:GO_1901660 The directed movement of calcium ion out of a cell or organelle. obo:GO_1901660 obo:go.owl obo:GO_1901660 jl obo:GO_1901660 2012-11-20T14:33:07Z obo:GO_1901660 biological_process obo:GO_1901660 GO:1901660 obo:GO_1901660 calcium ion export obo:GO_1901678 The directed movement of an iron coordination entity into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_1901678 obo:go.owl obo:GO_1901678 pr obo:GO_1901678 2012-11-22T15:43:15Z obo:GO_1901678 biological_process obo:GO_1901678 GO:1901678 obo:GO_1901678 iron coordination entity transport obo:GO_1901681 Interacting selectively and non-covalently with a sulfur compound. obo:GO_1901681 obo:go.owl obo:GO_1901681 pr obo:GO_1901681 2012-11-26T20:45:23Z obo:GO_1901681 sulfur molecular entity binding obo:GO_1901681 molecular_function obo:GO_1901681 GO:1901681 obo:GO_1901681 sulfur compound binding obo:GO_1901691 Interacting selectively and non-covalently with proton. obo:GO_1901691 obo:go.owl obo:GO_1901691 al obo:GO_1901691 2012-12-07T13:50:53Z obo:GO_1901691 hydrogen ion binding obo:GO_1901691 molecular_function obo:GO_1901691 GO:1901691 obo:GO_1901691 proton binding obo:GO_1901707 Interacting selectively and non-covalently with leptomycin B. obo:GO_1901707 obo:go.owl obo:GO_1901707 mah obo:GO_1901707 2012-12-18T15:10:04Z obo:GO_1901707 molecular_function obo:GO_1901707 GO:1901707 obo:GO_1901707 leptomycin B binding obo:GO_1901841 Any process that modulates the frequency, rate or extent of high voltage-gated calcium channel activity. obo:GO_1901841 obo:go.owl obo:GO_1901841 rl obo:GO_1901841 2013-01-24T19:02:15Z obo:GO_1901841 regulation of high voltage gated calcium channel activity obo:GO_1901841 regulation of high voltage-dependent calcium channel activity obo:GO_1901841 biological_process obo:GO_1901841 GO:1901841 obo:GO_1901841 regulation of high voltage-gated calcium channel activity obo:GO_1901842 Any process that stops, prevents or reduces the frequency, rate or extent of high voltage-gated calcium channel activity. obo:GO_1901842 obo:go.owl obo:GO_1901842 rl obo:GO_1901842 2013-01-24T19:02:20Z obo:GO_1901842 down regulation of high voltage gated calcium channel activity obo:GO_1901842 down regulation of high voltage-dependent calcium channel activity obo:GO_1901842 down regulation of high voltage-gated calcium channel activity obo:GO_1901842 down-regulation of high voltage gated calcium channel activity obo:GO_1901842 down-regulation of high voltage-dependent calcium channel activity obo:GO_1901842 down-regulation of high voltage-gated calcium channel activity obo:GO_1901842 downregulation of high voltage gated calcium channel activity obo:GO_1901842 downregulation of high voltage-dependent calcium channel activity obo:GO_1901842 downregulation of high voltage-gated calcium channel activity obo:GO_1901842 inhibition of high voltage gated calcium channel activity obo:GO_1901842 inhibition of high voltage-dependent calcium channel activity obo:GO_1901842 negative regulation of high voltage gated calcium channel activity obo:GO_1901842 negative regulation of high voltage-dependent calcium channel activity obo:GO_1901842 inhibition of high voltage-gated calcium channel activity obo:GO_1901842 biological_process obo:GO_1901842 GO:1901842 obo:GO_1901842 negative regulation of high voltage-gated calcium channel activity obo:GO_1901843 Any process that activates or increases the frequency, rate or extent of high voltage-gated calcium channel activity. obo:GO_1901843 obo:go.owl obo:GO_1901843 rl obo:GO_1901843 2013-01-24T19:02:25Z obo:GO_1901843 activation of high voltage gated calcium channel activity obo:GO_1901843 activation of high voltage-dependent calcium channel activity obo:GO_1901843 positive regulation of high voltage gated calcium channel activity obo:GO_1901843 positive regulation of high voltage-dependent calcium channel activity obo:GO_1901843 up regulation of high voltage gated calcium channel activity obo:GO_1901843 up regulation of high voltage-dependent calcium channel activity obo:GO_1901843 up regulation of high voltage-gated calcium channel activity obo:GO_1901843 up-regulation of high voltage gated calcium channel activity obo:GO_1901843 up-regulation of high voltage-dependent calcium channel activity obo:GO_1901843 up-regulation of high voltage-gated calcium channel activity obo:GO_1901843 upregulation of high voltage gated calcium channel activity obo:GO_1901843 upregulation of high voltage-dependent calcium channel activity obo:GO_1901843 upregulation of high voltage-gated calcium channel activity obo:GO_1901843 activation of high voltage-gated calcium channel activity obo:GO_1901843 biological_process obo:GO_1901843 GO:1901843 obo:GO_1901843 positive regulation of high voltage-gated calcium channel activity obo:GO_1901894 Any process that modulates the frequency, rate or extent of an ATPase-coupled calcium transmembrane transporter activity. obo:GO_1901894 obo:go.owl obo:GO_1901894 rl obo:GO_1901894 2013-02-06T21:18:16Z obo:GO_1901894 regulation of calcium pump obo:GO_1901894 regulation of ATP phosphohydrolase (Ca2+-transporting) obo:GO_1901894 regulation of Ca(2+)-transporting ATPase activity obo:GO_1901894 regulation of Ca2+-pumping ATPase activity obo:GO_1901894 regulation of Ca2+-transporting ATPase activity obo:GO_1901894 regulation of calcium transporting ATPase activity obo:GO_1901894 regulation of calcium-transporting ATPase activity obo:GO_1901894 regulation of calcium ABC transporter obo:GO_1901894 regulation of calcium efflux ATPase obo:GO_1901894 regulation of calcium-translocating P-type ATPase activity obo:GO_1901894 regulation of plasma membrane Ca-ATPase obo:GO_1901894 regulation of sarco(endo)plasmic reticulum Ca2+-ATPase obo:GO_1901894 regulation of sarcoplasmic reticulum ATPase obo:GO_1901894 biological_process obo:GO_1901894 GO:1901894 obo:GO_1901894 regulation of ATPase-coupled calcium transmembrane transporter activity obo:GO_1901895 Any process that stops, prevents or reduces the frequency, rate or extent of an ATPase-coupled calcium transmembrane transporter activity. obo:GO_1901895 obo:go.owl obo:GO_1901895 rl obo:GO_1901895 2013-02-06T21:18:25Z obo:GO_1901895 down regulation of calcium pump obo:GO_1901895 down-regulation of calcium pump obo:GO_1901895 downregulation of calcium pump obo:GO_1901895 inhibition of calcium pump obo:GO_1901895 negative regulation of calcium pump obo:GO_1901895 down regulation of ATP phosphohydrolase (Ca2+-transporting) obo:GO_1901895 down regulation of Ca(2+)-transporting ATPase activity obo:GO_1901895 down regulation of Ca2+-pumping ATPase activity obo:GO_1901895 down regulation of Ca2+-transporting ATPase activity obo:GO_1901895 down regulation of calcium transporting ATPase activity obo:GO_1901895 down regulation of calcium-transporting ATPase activity obo:GO_1901895 down-regulation of ATP phosphohydrolase (Ca2+-transporting) obo:GO_1901895 down-regulation of Ca(2+)-transporting ATPase activity obo:GO_1901895 down-regulation of Ca2+-pumping ATPase activity obo:GO_1901895 down-regulation of Ca2+-transporting ATPase activity obo:GO_1901895 down-regulation of calcium transporting ATPase activity obo:GO_1901895 down-regulation of calcium-transporting ATPase activity obo:GO_1901895 downregulation of ATP phosphohydrolase (Ca2+-transporting) obo:GO_1901895 downregulation of Ca(2+)-transporting ATPase activity obo:GO_1901895 downregulation of Ca2+-pumping ATPase activity obo:GO_1901895 downregulation of Ca2+-transporting ATPase activity obo:GO_1901895 downregulation of calcium transporting ATPase activity obo:GO_1901895 downregulation of calcium-transporting ATPase activity obo:GO_1901895 inhibition of ATP phosphohydrolase (Ca2+-transporting) obo:GO_1901895 inhibition of Ca(2+)-transporting ATPase activity obo:GO_1901895 inhibition of Ca2+-pumping ATPase activity obo:GO_1901895 inhibition of Ca2+-transporting ATPase activity obo:GO_1901895 inhibition of calcium transporting ATPase activity obo:GO_1901895 negative regulation of ATP phosphohydrolase (Ca2+-transporting) obo:GO_1901895 negative regulation of Ca(2+)-transporting ATPase activity obo:GO_1901895 negative regulation of Ca2+-pumping ATPase activity obo:GO_1901895 negative regulation of Ca2+-transporting ATPase activity obo:GO_1901895 negative regulation of calcium transporting ATPase activity obo:GO_1901895 negative regulation of calcium-transporting ATPase activity obo:GO_1901895 down regulation of calcium ABC transporter obo:GO_1901895 down regulation of calcium efflux ATPase obo:GO_1901895 down regulation of calcium-translocating P-type ATPase activity obo:GO_1901895 down regulation of plasma membrane Ca-ATPase obo:GO_1901895 down regulation of sarco(endo)plasmic reticulum Ca2+-ATPase obo:GO_1901895 down regulation of sarcoplasmic reticulum ATPase obo:GO_1901895 down-regulation of calcium ABC transporter obo:GO_1901895 down-regulation of calcium efflux ATPase obo:GO_1901895 down-regulation of calcium-translocating P-type ATPase activity obo:GO_1901895 down-regulation of plasma membrane Ca-ATPase obo:GO_1901895 down-regulation of sarco(endo)plasmic reticulum Ca2+-ATPase obo:GO_1901895 down-regulation of sarcoplasmic reticulum ATPase obo:GO_1901895 downregulation of calcium ABC transporter obo:GO_1901895 downregulation of calcium efflux ATPase obo:GO_1901895 downregulation of calcium-translocating P-type ATPase activity obo:GO_1901895 downregulation of plasma membrane Ca-ATPase obo:GO_1901895 downregulation of sarco(endo)plasmic reticulum Ca2+-ATPase obo:GO_1901895 downregulation of sarcoplasmic reticulum ATPase obo:GO_1901895 inhibition of calcium ABC transporter obo:GO_1901895 inhibition of calcium efflux ATPase obo:GO_1901895 inhibition of calcium-translocating P-type ATPase activity obo:GO_1901895 inhibition of calcium-transporting ATPase activity obo:GO_1901895 inhibition of plasma membrane Ca-ATPase obo:GO_1901895 inhibition of sarco(endo)plasmic reticulum Ca2+-ATPase obo:GO_1901895 inhibition of sarcoplasmic reticulum ATPase obo:GO_1901895 negative regulation of calcium ABC transporter obo:GO_1901895 negative regulation of calcium efflux ATPase obo:GO_1901895 negative regulation of calcium-translocating P-type ATPase activity obo:GO_1901895 negative regulation of plasma membrane Ca-ATPase obo:GO_1901895 negative regulation of sarco(endo)plasmic reticulum Ca2+-ATPase obo:GO_1901895 negative regulation of sarcoplasmic reticulum ATPase obo:GO_1901895 biological_process obo:GO_1901895 GO:1901895 obo:GO_1901895 negative regulation of ATPase-coupled calcium transmembrane transporter activity obo:GO_1901896 Any process that activates or increases the frequency, rate or extent of an ATPase-coupled calcium transmembrane transporter activity. obo:GO_1901896 obo:go.owl obo:GO_1901896 rl obo:GO_1901896 2013-02-06T21:18:29Z obo:GO_1901896 activation of calcium pump obo:GO_1901896 positive regulation of calcium pump obo:GO_1901896 up regulation of calcium pump obo:GO_1901896 up-regulation of calcium pump obo:GO_1901896 upregulation of calcium pump obo:GO_1901896 activation of ATP phosphohydrolase (Ca2+-transporting) obo:GO_1901896 activation of Ca(2+)-transporting ATPase activity obo:GO_1901896 activation of Ca2+-pumping ATPase activity obo:GO_1901896 activation of Ca2+-transporting ATPase activity obo:GO_1901896 activation of calcium transporting ATPase activity obo:GO_1901896 positive regulation of ATP phosphohydrolase (Ca2+-transporting) obo:GO_1901896 positive regulation of Ca(2+)-transporting ATPase activity obo:GO_1901896 positive regulation of Ca2+-pumping ATPase activity obo:GO_1901896 positive regulation of Ca2+-transporting ATPase activity obo:GO_1901896 positive regulation of calcium transporting ATPase activity obo:GO_1901896 positive regulation of calcium-transporting ATPase activity obo:GO_1901896 up regulation of ATP phosphohydrolase (Ca2+-transporting) obo:GO_1901896 up regulation of Ca(2+)-transporting ATPase activity obo:GO_1901896 up regulation of Ca2+-pumping ATPase activity obo:GO_1901896 up regulation of Ca2+-transporting ATPase activity obo:GO_1901896 up regulation of calcium transporting ATPase activity obo:GO_1901896 up regulation of calcium-transporting ATPase activity obo:GO_1901896 up-regulation of ATP phosphohydrolase (Ca2+-transporting) obo:GO_1901896 up-regulation of Ca(2+)-transporting ATPase activity obo:GO_1901896 up-regulation of Ca2+-pumping ATPase activity obo:GO_1901896 up-regulation of Ca2+-transporting ATPase activity obo:GO_1901896 up-regulation of calcium transporting ATPase activity obo:GO_1901896 up-regulation of calcium-transporting ATPase activity obo:GO_1901896 upregulation of ATP phosphohydrolase (Ca2+-transporting) obo:GO_1901896 upregulation of Ca(2+)-transporting ATPase activity obo:GO_1901896 upregulation of Ca2+-pumping ATPase activity obo:GO_1901896 upregulation of Ca2+-transporting ATPase activity obo:GO_1901896 upregulation of calcium transporting ATPase activity obo:GO_1901896 upregulation of calcium-transporting ATPase activity obo:GO_1901896 activation of calcium ABC transporter obo:GO_1901896 activation of calcium efflux ATPase obo:GO_1901896 activation of calcium-translocating P-type ATPase activity obo:GO_1901896 activation of calcium-transporting ATPase activity obo:GO_1901896 activation of plasma membrane Ca-ATPase obo:GO_1901896 activation of sarco(endo)plasmic reticulum Ca2+-ATPase obo:GO_1901896 activation of sarcoplasmic reticulum ATPase obo:GO_1901896 positive regulation of calcium ABC transporter obo:GO_1901896 positive regulation of calcium efflux ATPase obo:GO_1901896 positive regulation of calcium-translocating P-type ATPase activity obo:GO_1901896 positive regulation of plasma membrane Ca-ATPase obo:GO_1901896 positive regulation of sarco(endo)plasmic reticulum Ca2+-ATPase obo:GO_1901896 positive regulation of sarcoplasmic reticulum ATPase obo:GO_1901896 up regulation of calcium ABC transporter obo:GO_1901896 up regulation of calcium efflux ATPase obo:GO_1901896 up regulation of calcium-translocating P-type ATPase activity obo:GO_1901896 up regulation of plasma membrane Ca-ATPase obo:GO_1901896 up regulation of sarco(endo)plasmic reticulum Ca2+-ATPase obo:GO_1901896 up regulation of sarcoplasmic reticulum ATPase obo:GO_1901896 up-regulation of calcium ABC transporter obo:GO_1901896 up-regulation of calcium efflux ATPase obo:GO_1901896 up-regulation of calcium-translocating P-type ATPase activity obo:GO_1901896 up-regulation of plasma membrane Ca-ATPase obo:GO_1901896 up-regulation of sarco(endo)plasmic reticulum Ca2+-ATPase obo:GO_1901896 up-regulation of sarcoplasmic reticulum ATPase obo:GO_1901896 upregulation of calcium ABC transporter obo:GO_1901896 upregulation of calcium efflux ATPase obo:GO_1901896 upregulation of calcium-translocating P-type ATPase activity obo:GO_1901896 upregulation of plasma membrane Ca-ATPase obo:GO_1901896 upregulation of sarco(endo)plasmic reticulum Ca2+-ATPase obo:GO_1901896 upregulation of sarcoplasmic reticulum ATPase obo:GO_1901896 biological_process obo:GO_1901896 GO:1901896 obo:GO_1901896 positive regulation of ATPase-coupled calcium transmembrane transporter activity obo:GO_1901900 Any process that modulates the frequency, rate or extent of protein localization to cell division site. obo:GO_1901900 obo:go.owl obo:GO_1901900 dph obo:GO_1901900 2013-02-11T12:27:55Z obo:GO_1901900 regulation of protein localisation to cell division site obo:GO_1901900 biological_process obo:GO_1901900 GO:1901900 obo:GO_1901900 regulation of protein localization to cell division site obo:GO_1901901 Any regulation of protein localization to cell division site that is involved in cytokinesis. obo:GO_1901901 obo:go.owl obo:GO_1901901 dph obo:GO_1901901 2013-02-12T18:01:34Z obo:GO_1901901 regulation of protein localisation to cell division site involved in cytokinesis obo:GO_1901901 biological_process obo:GO_1901901 GO:1901901 obo:GO_1901901 regulation of protein localization to cell division site involved in cytokinesis obo:GO_1901916 Any protein kinase activity that is involved in regulation of protein localization to cell division site involved in cytokinesis. obo:GO_1901916 obo:go.owl obo:GO_1901916 dph obo:GO_1901916 2013-02-14T15:30:37Z obo:GO_1901916 protein kinase activity involved in regulation of protein localisation to cell division site involved in cytokinesis obo:GO_1901916 protamine kinase activity involved in regulation of protein localisation to cell division site involved in cytokinesis obo:GO_1901916 protamine kinase activity involved in regulation of protein localization to cell division site involved in cytokinesis obo:GO_1901916 molecular_function obo:GO_1901916 GO:1901916 obo:GO_1901916 protein kinase activity involved in regulation of protein localization to cell division site involved in cytokinesis obo:GO_1901973 Interacting selectively and non-covalently with proline. obo:GO_1901973 obo:go.owl obo:GO_1901973 pm obo:GO_1901973 2013-02-26T14:58:01Z obo:GO_1901973 molecular_function obo:GO_1901973 GO:1901973 obo:GO_1901973 proline binding obo:GO_1901979 Any process that modulates the frequency, rate or extent of inward rectifier potassium channel activity. obo:GO_1901979 obo:go.owl obo:GO_1901979 tb obo:GO_1901979 2013-03-12T18:21:12Z obo:GO_1901979 regulation of Kir channel activity obo:GO_1901979 biological_process obo:GO_1901979 GO:1901979 obo:GO_1901979 regulation of inward rectifier potassium channel activity obo:GO_1901980 Any process that activates or increases the frequency, rate or extent of inward rectifier potassium channel activity. obo:GO_1901980 obo:go.owl obo:GO_1901980 tb obo:GO_1901980 2013-03-12T18:21:17Z obo:GO_1901980 activation of Kir channel activity obo:GO_1901980 positive regulation of Kir channel activity obo:GO_1901980 up regulation of Kir channel activity obo:GO_1901980 up regulation of inward rectifier potassium channel activity obo:GO_1901980 up-regulation of Kir channel activity obo:GO_1901980 up-regulation of inward rectifier potassium channel activity obo:GO_1901980 upregulation of Kir channel activity obo:GO_1901980 upregulation of inward rectifier potassium channel activity obo:GO_1901980 activation of inward rectifier potassium channel activity obo:GO_1901980 biological_process obo:GO_1901980 GO:1901980 obo:GO_1901980 positive regulation of inward rectifier potassium channel activity obo:GO_1901981 Interacting selectively and non-covalently with phosphatidylinositol phosphate. obo:GO_1901981 obo:go.owl obo:GO_1901981 tb obo:GO_1901981 2013-03-12T18:21:22Z obo:GO_1901981 molecular_function obo:GO_1901981 GO:1901981 obo:GO_1901981 phosphatidylinositol phosphate binding obo:GO_1901982 Interacting selectively and non-covalently with maltose. obo:GO_1901982 obo:go.owl obo:GO_1901982 tb obo:GO_1901982 2013-03-13T18:17:19Z obo:GO_1901982 molecular_function obo:GO_1901982 GO:1901982 obo:GO_1901982 maltose binding obo:GO_1902025 The directed movement of nitrate into a cell or organelle. obo:GO_1902025 obo:go.owl obo:GO_1902025 tb obo:GO_1902025 2013-03-27T21:32:58Z obo:GO_1902025 nitrate influx obo:GO_1902025 nitrate uptake obo:GO_1902025 biological_process obo:GO_1902025 GO:1902025 obo:GO_1902025 nitrate import obo:GO_1902051 Interacting selectively and non-covalently with (25S)-Delta(4)-dafachronate. obo:GO_1902051 obo:go.owl obo:GO_1902051 ab obo:GO_1902051 2013-04-11T08:33:41Z obo:GO_1902051 molecular_function obo:GO_1902051 GO:1902051 obo:GO_1902051 (25S)-Delta(4)-dafachronate binding obo:GO_1902052 Interacting selectively and non-covalently with (25S)-Delta(7)-dafachronate. obo:GO_1902052 obo:go.owl obo:GO_1902052 ab obo:GO_1902052 2013-04-11T08:34:38Z obo:GO_1902052 molecular_function obo:GO_1902052 GO:1902052 obo:GO_1902052 (25S)-Delta(7)-dafachronate binding obo:GO_1902074 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a salt stimulus. obo:GO_1902074 obo:go.owl obo:GO_1902074 mls obo:GO_1902074 2013-04-22T15:41:57Z obo:GO_1902074 response to salinity obo:GO_1902074 biological_process obo:GO_1902074 GO:1902074 obo:GO_1902074 response to salt obo:GO_1902080 Any process that modulates the frequency, rate or extent of calcium ion import into sarcoplasmic reticulum. obo:GO_1902080 obo:go.owl obo:GO_1902080 rl obo:GO_1902080 2013-04-24T16:07:50Z obo:GO_1902080 biological_process obo:GO_1902080 GO:1902080 obo:GO_1902080 regulation of calcium ion import into sarcoplasmic reticulum obo:GO_1902081 Any process that stops, prevents or reduces the frequency, rate or extent of calcium ion import into sarcoplasmic reticulum. obo:GO_1902081 obo:go.owl obo:GO_1902081 rl obo:GO_1902081 2013-04-24T16:07:59Z obo:GO_1902081 down regulation of calcium ion import into sarcoplasmic reticulum obo:GO_1902081 down-regulation of calcium ion import into sarcoplasmic reticulum obo:GO_1902081 downregulation of calcium ion import into sarcoplasmic reticulum obo:GO_1902081 inhibition of calcium ion import into sarcoplasmic reticulum obo:GO_1902081 biological_process obo:GO_1902081 GO:1902081 obo:GO_1902081 negative regulation of calcium ion import into sarcoplasmic reticulum obo:GO_1902082 Any process that activates or increases the frequency, rate or extent of calcium ion import into sarcoplasmic reticulum. obo:GO_1902082 obo:go.owl obo:GO_1902082 rl obo:GO_1902082 2013-04-24T16:08:03Z obo:GO_1902082 up regulation of calcium ion import into sarcoplasmic reticulum obo:GO_1902082 up-regulation of calcium ion import into sarcoplasmic reticulum obo:GO_1902082 upregulation of calcium ion import into sarcoplasmic reticulum obo:GO_1902082 activation of calcium ion import into sarcoplasmic reticulum obo:GO_1902082 biological_process obo:GO_1902082 GO:1902082 obo:GO_1902082 positive regulation of calcium ion import into sarcoplasmic reticulum obo:GO_1902098 Interacting selectively and non-covalently with calcitriol. Calcitriol (1,25-dihydroxycholecalciferol) is the hormonally active form of vitamin D3. obo:GO_1902098 obo:go.owl obo:GO_1902098 bf obo:GO_1902098 2013-05-02T09:41:15Z obo:GO_1902098 1,25-dihydroxycholecalciferol binding obo:GO_1902098 1,25-dihydroxyvitamin D3 binding obo:GO_1902098 1alpha,25(OH)2 vitamin D3 binding obo:GO_1902098 1alpha,25(OH)2D3 binding obo:GO_1902098 1alpha,25-dihydroxycholecalciferol binding obo:GO_1902098 1alpha,25-dihydroxyvitamin D3 binding obo:GO_1902098 hormonally active vitamin D3 binding obo:GO_1902098 molecular_function obo:GO_1902098 GO:1902098 obo:GO_1902098 calcitriol binding obo:GO_1902118 Interacting selectively and non-covalently with calcidiol. obo:GO_1902118 obo:go.owl obo:GO_1902118 bf obo:GO_1902118 2013-05-15T14:55:58Z obo:GO_1902118 25(OH)D3 binding obo:GO_1902118 25-hydroxycholecalciferol binding obo:GO_1902118 25-hydroxyvitamin D3 binding obo:GO_1902118 25OHD3 binding obo:GO_1902118 calcifediol binding obo:GO_1902118 molecular_function obo:GO_1902118 GO:1902118 obo:GO_1902118 calcidiol binding obo:GO_1902121 Interacting selectively and non-covalently with lithocholic acid. obo:GO_1902121 obo:go.owl obo:GO_1902121 bf obo:GO_1902121 2013-05-15T16:05:12Z obo:GO_1902121 LCA binding obo:GO_1902121 molecular_function obo:GO_1902121 GO:1902121 obo:GO_1902121 lithocholic acid binding obo:GO_1902122 Interacting selectively and non-covalently with chenodeoxycholic acid. obo:GO_1902122 obo:go.owl obo:GO_1902122 bf obo:GO_1902122 2013-05-16T09:17:19Z obo:GO_1902122 CDCA binding obo:GO_1902122 molecular_function obo:GO_1902122 GO:1902122 obo:GO_1902122 chenodeoxycholic acid binding obo:GO_1902159 Any process that modulates the frequency, rate or extent of cyclic nucleotide-gated ion channel activity. obo:GO_1902159 obo:go.owl obo:GO_1902159 sl obo:GO_1902159 2013-05-21T19:24:30Z obo:GO_1902159 regulation of cyclic nucleotide activated ion channel activity obo:GO_1902159 regulation of cyclic nucleotide gated ion channel activity obo:GO_1902159 regulation of cyclic nucleotide-activated ion channel activity obo:GO_1902159 biological_process obo:GO_1902159 GO:1902159 obo:GO_1902159 regulation of cyclic nucleotide-gated ion channel activity obo:GO_1902160 Any process that stops, prevents or reduces the frequency, rate or extent of cyclic nucleotide-gated ion channel activity. obo:GO_1902160 obo:go.owl obo:GO_1902160 sl obo:GO_1902160 2013-05-21T19:24:35Z obo:GO_1902160 down regulation of cyclic nucleotide activated ion channel activity obo:GO_1902160 down regulation of cyclic nucleotide gated ion channel activity obo:GO_1902160 down regulation of cyclic nucleotide-activated ion channel activity obo:GO_1902160 down regulation of cyclic nucleotide-gated ion channel activity obo:GO_1902160 down-regulation of cyclic nucleotide activated ion channel activity obo:GO_1902160 down-regulation of cyclic nucleotide gated ion channel activity obo:GO_1902160 down-regulation of cyclic nucleotide-activated ion channel activity obo:GO_1902160 down-regulation of cyclic nucleotide-gated ion channel activity obo:GO_1902160 downregulation of cyclic nucleotide activated ion channel activity obo:GO_1902160 downregulation of cyclic nucleotide gated ion channel activity obo:GO_1902160 downregulation of cyclic nucleotide-activated ion channel activity obo:GO_1902160 downregulation of cyclic nucleotide-gated ion channel activity obo:GO_1902160 inhibition of cyclic nucleotide activated ion channel activity obo:GO_1902160 inhibition of cyclic nucleotide gated ion channel activity obo:GO_1902160 inhibition of cyclic nucleotide-activated ion channel activity obo:GO_1902160 negative regulation of cyclic nucleotide activated ion channel activity obo:GO_1902160 negative regulation of cyclic nucleotide gated ion channel activity obo:GO_1902160 negative regulation of cyclic nucleotide-activated ion channel activity obo:GO_1902160 inhibition of cyclic nucleotide-gated ion channel activity obo:GO_1902160 biological_process obo:GO_1902160 GO:1902160 obo:GO_1902160 negative regulation of cyclic nucleotide-gated ion channel activity obo:GO_1902161 Any process that activates or increases the frequency, rate or extent of cyclic nucleotide-gated ion channel activity. obo:GO_1902161 obo:go.owl obo:GO_1902161 sl obo:GO_1902161 2013-05-21T19:24:48Z obo:GO_1902161 activation of cyclic nucleotide activated ion channel activity obo:GO_1902161 activation of cyclic nucleotide gated ion channel activity obo:GO_1902161 activation of cyclic nucleotide-activated ion channel activity obo:GO_1902161 positive regulation of cyclic nucleotide activated ion channel activity obo:GO_1902161 positive regulation of cyclic nucleotide gated ion channel activity obo:GO_1902161 positive regulation of cyclic nucleotide-activated ion channel activity obo:GO_1902161 up regulation of cyclic nucleotide activated ion channel activity obo:GO_1902161 up regulation of cyclic nucleotide gated ion channel activity obo:GO_1902161 up regulation of cyclic nucleotide-activated ion channel activity obo:GO_1902161 up regulation of cyclic nucleotide-gated ion channel activity obo:GO_1902161 up-regulation of cyclic nucleotide activated ion channel activity obo:GO_1902161 up-regulation of cyclic nucleotide gated ion channel activity obo:GO_1902161 up-regulation of cyclic nucleotide-activated ion channel activity obo:GO_1902161 up-regulation of cyclic nucleotide-gated ion channel activity obo:GO_1902161 upregulation of cyclic nucleotide activated ion channel activity obo:GO_1902161 upregulation of cyclic nucleotide gated ion channel activity obo:GO_1902161 upregulation of cyclic nucleotide-activated ion channel activity obo:GO_1902161 upregulation of cyclic nucleotide-gated ion channel activity obo:GO_1902161 activation of cyclic nucleotide-gated ion channel activity obo:GO_1902161 biological_process obo:GO_1902161 GO:1902161 obo:GO_1902161 positive regulation of cyclic nucleotide-gated ion channel activity obo:GO_1902248 Interacting selectively and non-covalently with 5-O-phosphono-alpha-D-ribofuranosyl diphosphate. obo:GO_1902248 obo:go.owl obo:GO_1902248 mah obo:GO_1902248 2013-06-20T16:20:29Z obo:GO_1902248 5-phosphoribose 1-diphosphate binding obo:GO_1902248 phosphoribosylpyrophosphate binding obo:GO_1902248 molecular_function obo:GO_1902248 GO:1902248 obo:GO_1902248 5-O-phosphono-alpha-D-ribofuranosyl diphosphate binding obo:GO_1902249 Interacting selectively and non-covalently with IMP, inosine monophosphate. obo:GO_1902249 obo:go.owl obo:GO_1902249 mah obo:GO_1902249 2013-06-20T16:20:35Z obo:GO_1902249 molecular_function obo:GO_1902249 GO:1902249 obo:GO_1902249 IMP binding obo:GO_1902259 Any process that modulates the frequency, rate or extent of delayed rectifier potassium channel activity. obo:GO_1902259 obo:go.owl obo:GO_1902259 rl obo:GO_1902259 2013-06-25T12:16:19Z obo:GO_1902259 biological_process obo:GO_1902259 GO:1902259 obo:GO_1902259 regulation of delayed rectifier potassium channel activity obo:GO_1902260 Any process that stops, prevents or reduces the frequency, rate or extent of delayed rectifier potassium channel activity. obo:GO_1902260 obo:go.owl obo:GO_1902260 rl obo:GO_1902260 2013-06-25T12:16:24Z obo:GO_1902260 down regulation of delayed rectifier potassium channel activity obo:GO_1902260 down-regulation of delayed rectifier potassium channel activity obo:GO_1902260 downregulation of delayed rectifier potassium channel activity obo:GO_1902260 inhibition of delayed rectifier potassium channel activity obo:GO_1902260 biological_process obo:GO_1902260 GO:1902260 obo:GO_1902260 negative regulation of delayed rectifier potassium channel activity obo:GO_1902261 Any process that activates or increases the frequency, rate or extent of delayed rectifier potassium channel activity. obo:GO_1902261 obo:go.owl obo:GO_1902261 rl obo:GO_1902261 2013-06-25T12:16:30Z obo:GO_1902261 up regulation of delayed rectifier potassium channel activity obo:GO_1902261 up-regulation of delayed rectifier potassium channel activity obo:GO_1902261 upregulation of delayed rectifier potassium channel activity obo:GO_1902261 activation of delayed rectifier potassium channel activity obo:GO_1902261 biological_process obo:GO_1902261 GO:1902261 obo:GO_1902261 positive regulation of delayed rectifier potassium channel activity obo:GO_1902267 Any process that modulates the frequency, rate or extent of polyamine transmembrane transport. obo:GO_1902267 obo:go.owl obo:GO_1902267 mcc obo:GO_1902267 2013-06-28T21:34:36Z obo:GO_1902267 biological_process obo:GO_1902267 GO:1902267 obo:GO_1902267 regulation of polyamine transmembrane transport obo:GO_1902268 Any process that stops, prevents or reduces the frequency, rate or extent of polyamine transmembrane transport. obo:GO_1902268 obo:go.owl obo:GO_1902268 mcc obo:GO_1902268 2013-06-28T21:34:42Z obo:GO_1902268 down regulation of polyamine transmembrane transport obo:GO_1902268 down-regulation of polyamine transmembrane transport obo:GO_1902268 downregulation of polyamine transmembrane transport obo:GO_1902268 inhibition of polyamine transmembrane transport obo:GO_1902268 biological_process obo:GO_1902268 GO:1902268 obo:GO_1902268 negative regulation of polyamine transmembrane transport obo:GO_1902269 Any process that activates or increases the frequency, rate or extent of polyamine transmembrane transport. obo:GO_1902269 obo:go.owl obo:GO_1902269 mcc obo:GO_1902269 2013-06-28T21:34:47Z obo:GO_1902269 up regulation of polyamine transmembrane transport obo:GO_1902269 up-regulation of polyamine transmembrane transport obo:GO_1902269 upregulation of polyamine transmembrane transport obo:GO_1902269 activation of polyamine transmembrane transport obo:GO_1902269 biological_process obo:GO_1902269 GO:1902269 obo:GO_1902269 positive regulation of polyamine transmembrane transport obo:GO_1902271 Interacting selectively and non-covalently with D3 vitamins. obo:GO_1902271 obo:go.owl obo:GO_1902271 bf obo:GO_1902271 2013-07-01T12:54:37Z obo:GO_1902271 molecular_function obo:GO_1902271 GO:1902271 obo:GO_1902271 D3 vitamins binding obo:GO_1902305 Any process that modulates the frequency, rate or extent of sodium ion transmembrane transport. obo:GO_1902305 obo:go.owl obo:GO_1902305 rl obo:GO_1902305 2013-07-18T13:33:53Z obo:GO_1902305 regulation of sodium ion membrane transport obo:GO_1902305 biological_process obo:GO_1902305 GO:1902305 obo:GO_1902305 regulation of sodium ion transmembrane transport obo:GO_1902306 Any process that stops, prevents or reduces the frequency, rate or extent of sodium ion transmembrane transport. obo:GO_1902306 obo:go.owl obo:GO_1902306 rl obo:GO_1902306 2013-07-18T13:34:01Z obo:GO_1902306 down regulation of sodium ion membrane transport obo:GO_1902306 down regulation of sodium ion transmembrane transport obo:GO_1902306 down-regulation of sodium ion membrane transport obo:GO_1902306 down-regulation of sodium ion transmembrane transport obo:GO_1902306 downregulation of sodium ion membrane transport obo:GO_1902306 downregulation of sodium ion transmembrane transport obo:GO_1902306 negative regulation of sodium ion membrane transport obo:GO_1902306 inhibition of sodium ion membrane transport obo:GO_1902306 inhibition of sodium ion transmembrane transport obo:GO_1902306 biological_process obo:GO_1902306 GO:1902306 obo:GO_1902306 negative regulation of sodium ion transmembrane transport obo:GO_1902307 Any process that activates or increases the frequency, rate or extent of sodium ion transmembrane transport. obo:GO_1902307 obo:go.owl obo:GO_1902307 rl obo:GO_1902307 2013-07-18T13:34:18Z obo:GO_1902307 positive regulation of sodium ion membrane transport obo:GO_1902307 up regulation of sodium ion membrane transport obo:GO_1902307 up regulation of sodium ion transmembrane transport obo:GO_1902307 up-regulation of sodium ion membrane transport obo:GO_1902307 up-regulation of sodium ion transmembrane transport obo:GO_1902307 upregulation of sodium ion membrane transport obo:GO_1902307 upregulation of sodium ion transmembrane transport obo:GO_1902307 activation of sodium ion membrane transport obo:GO_1902307 activation of sodium ion transmembrane transport obo:GO_1902307 biological_process obo:GO_1902307 GO:1902307 obo:GO_1902307 positive regulation of sodium ion transmembrane transport obo:GO_1902311 Any process that modulates the frequency, rate or extent of copper ion transmembrane transport. obo:GO_1902311 obo:go.owl obo:GO_1902311 di obo:GO_1902311 2013-07-19T20:59:28Z obo:GO_1902311 regulation of copper cation transmembrane transport obo:GO_1902311 regulation of copper ion membrane transport obo:GO_1902311 biological_process obo:GO_1902311 GO:1902311 obo:GO_1902311 regulation of copper ion transmembrane transport obo:GO_1902312 Any process that stops, prevents or reduces the frequency, rate or extent of copper ion transmembrane transport. obo:GO_1902312 obo:go.owl obo:GO_1902312 di obo:GO_1902312 2013-07-19T20:59:37Z obo:GO_1902312 down regulation of copper cation transmembrane transport obo:GO_1902312 down regulation of copper ion membrane transport obo:GO_1902312 down regulation of copper ion transmembrane transport obo:GO_1902312 down-regulation of copper cation transmembrane transport obo:GO_1902312 down-regulation of copper ion membrane transport obo:GO_1902312 down-regulation of copper ion transmembrane transport obo:GO_1902312 downregulation of copper cation transmembrane transport obo:GO_1902312 downregulation of copper ion membrane transport obo:GO_1902312 downregulation of copper ion transmembrane transport obo:GO_1902312 negative regulation of copper cation transmembrane transport obo:GO_1902312 negative regulation of copper ion membrane transport obo:GO_1902312 inhibition of copper cation transmembrane transport obo:GO_1902312 inhibition of copper ion membrane transport obo:GO_1902312 inhibition of copper ion transmembrane transport obo:GO_1902312 biological_process obo:GO_1902312 GO:1902312 obo:GO_1902312 negative regulation of copper ion transmembrane transport obo:GO_1902313 Any process that activates or increases the frequency, rate or extent of copper ion transmembrane transport. obo:GO_1902313 obo:go.owl obo:GO_1902313 di obo:GO_1902313 2013-07-19T20:59:45Z obo:GO_1902313 positive regulation of copper cation transmembrane transport obo:GO_1902313 positive regulation of copper ion membrane transport obo:GO_1902313 up regulation of copper cation transmembrane transport obo:GO_1902313 up regulation of copper ion membrane transport obo:GO_1902313 up regulation of copper ion transmembrane transport obo:GO_1902313 up-regulation of copper cation transmembrane transport obo:GO_1902313 up-regulation of copper ion membrane transport obo:GO_1902313 up-regulation of copper ion transmembrane transport obo:GO_1902313 upregulation of copper cation transmembrane transport obo:GO_1902313 upregulation of copper ion membrane transport obo:GO_1902313 upregulation of copper ion transmembrane transport obo:GO_1902313 activation of copper cation transmembrane transport obo:GO_1902313 activation of copper ion membrane transport obo:GO_1902313 activation of copper ion transmembrane transport obo:GO_1902313 biological_process obo:GO_1902313 GO:1902313 obo:GO_1902313 positive regulation of copper ion transmembrane transport obo:GO_1902314 Interacting selectively and non-covalently with hydroquinone. obo:GO_1902314 obo:go.owl obo:GO_1902314 bhm obo:GO_1902314 2013-07-22T10:10:12Z obo:GO_1902314 quinol binding obo:GO_1902314 molecular_function obo:GO_1902314 GO:1902314 obo:GO_1902314 hydroquinone binding obo:GO_1902354 Any blood vessel endothelial cell delamination that is involved in blood vessel lumen ensheathment. obo:GO_1902354 obo:go.owl obo:GO_1902354 pr obo:GO_1902354 2013-08-14T10:22:00Z obo:GO_1902354 biological_process obo:GO_1902354 GO:1902354 obo:GO_1902354 blood vessel endothelial cell delamination involved in blood vessel lumen ensheathment obo:GO_1902363 Any process that modulates the frequency, rate or extent of protein localization to spindle pole body. obo:GO_1902363 obo:go.owl obo:GO_1902363 vw obo:GO_1902363 2013-08-15T16:38:07Z obo:GO_1902363 regulation of protein localisation to spindle pole body obo:GO_1902363 biological_process obo:GO_1902363 GO:1902363 obo:GO_1902363 regulation of protein localization to spindle pole body obo:GO_1902364 Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to spindle pole body. obo:GO_1902364 obo:go.owl obo:GO_1902364 vw obo:GO_1902364 2013-08-15T16:38:23Z obo:GO_1902364 down regulation of protein localisation to spindle pole body obo:GO_1902364 down regulation of protein localization to spindle pole body obo:GO_1902364 down-regulation of protein localisation to spindle pole body obo:GO_1902364 down-regulation of protein localization to spindle pole body obo:GO_1902364 downregulation of protein localisation to spindle pole body obo:GO_1902364 downregulation of protein localization to spindle pole body obo:GO_1902364 negative regulation of protein localisation to spindle pole body obo:GO_1902364 inhibition of protein localisation to spindle pole body obo:GO_1902364 inhibition of protein localization to spindle pole body obo:GO_1902364 biological_process obo:GO_1902364 GO:1902364 obo:GO_1902364 negative regulation of protein localization to spindle pole body obo:GO_1902365 Any process that activates or increases the frequency, rate or extent of protein localization to spindle pole body. obo:GO_1902365 obo:go.owl obo:GO_1902365 vw obo:GO_1902365 2013-08-15T16:38:31Z obo:GO_1902365 positive regulation of protein localisation to spindle pole body obo:GO_1902365 up regulation of protein localisation to spindle pole body obo:GO_1902365 up regulation of protein localization to spindle pole body obo:GO_1902365 up-regulation of protein localisation to spindle pole body obo:GO_1902365 up-regulation of protein localization to spindle pole body obo:GO_1902365 upregulation of protein localisation to spindle pole body obo:GO_1902365 upregulation of protein localization to spindle pole body obo:GO_1902365 activation of protein localisation to spindle pole body obo:GO_1902365 activation of protein localization to spindle pole body obo:GO_1902365 biological_process obo:GO_1902365 GO:1902365 obo:GO_1902365 positive regulation of protein localization to spindle pole body obo:GO_1902379 Any chemoattractant activity that is involved in axon guidance. obo:GO_1902379 obo:go.owl obo:GO_1902379 bf obo:GO_1902379 2013-09-02T13:49:35Z obo:GO_1902379 chemoattractant activity involved in axon pathfinding obo:GO_1902379 chemoattractant activity involved in axon growth cone guidance obo:GO_1902379 molecular_function obo:GO_1902379 chemoattractant activity involved in axon chemotaxis obo:GO_1902379 GO:1902379 obo:GO_1902379 chemoattractant activity involved in axon guidance obo:GO_1902387 Interacting selectively and non-covalently with ceramide 1-phosphate. obo:GO_1902387 obo:go.owl obo:GO_1902387 uh obo:GO_1902387 2013-09-05T05:51:08Z obo:GO_1902387 molecular_function obo:GO_1902387 GO:1902387 obo:GO_1902387 ceramide 1-phosphate binding obo:GO_1902397 Any detection of stimulus that is involved in meiotic spindle checkpoint. obo:GO_1902397 obo:go.owl obo:GO_1902397 jl obo:GO_1902397 2013-09-12T12:01:32Z obo:GO_1902397 stimulus detection involved in meiotic spindle checkpoint obo:GO_1902397 biological_process obo:GO_1902397 perception of stimulus involved in meiotic spindle checkpoint obo:GO_1902397 stimulus sensing involved in meiotic spindle checkpoint obo:GO_1902397 GO:1902397 obo:GO_1902397 detection of stimulus involved in meiotic spindle checkpoint obo:GO_1902399 Any detection of stimulus that is involved in G1 DNA damage checkpoint. obo:GO_1902399 obo:go.owl obo:GO_1902399 jl obo:GO_1902399 2013-09-12T12:01:49Z obo:GO_1902399 detection of stimulus involved in G1/S DNA damage checkpoint obo:GO_1902399 stimulus detection involved in G1 DNA damage checkpoint obo:GO_1902399 stimulus detection involved in G1/S DNA damage checkpoint obo:GO_1902399 biological_process obo:GO_1902399 perception of stimulus involved in G1 DNA damage checkpoint obo:GO_1902399 perception of stimulus involved in G1/S DNA damage checkpoint obo:GO_1902399 stimulus sensing involved in G1 DNA damage checkpoint obo:GO_1902399 stimulus sensing involved in G1/S DNA damage checkpoint obo:GO_1902399 GO:1902399 obo:GO_1902399 detection of stimulus involved in G1 DNA damage checkpoint obo:GO_1902427 Any process that modulates the frequency, rate or extent of water channel activity. obo:GO_1902427 obo:go.owl obo:GO_1902427 bf obo:GO_1902427 2013-09-23T12:56:31Z obo:GO_1902427 regulation of aquaporin obo:GO_1902427 regulation of aquaporin permeability obo:GO_1902427 biological_process obo:GO_1902427 GO:1902427 obo:GO_1902427 regulation of water channel activity obo:GO_1902428 Any process that stops, prevents or reduces the frequency, rate or extent of water channel activity. obo:GO_1902428 obo:go.owl obo:GO_1902428 bf obo:GO_1902428 2013-09-23T12:56:40Z obo:GO_1902428 down regulation of water channel activity obo:GO_1902428 down-regulation of water channel activity obo:GO_1902428 downregulation of water channel activity obo:GO_1902428 down regulation of aquaporin obo:GO_1902428 down-regulation of aquaporin obo:GO_1902428 downregulation of aquaporin obo:GO_1902428 inhibition of aquaporin obo:GO_1902428 inhibition of water channel activity obo:GO_1902428 negative regulation of aquaporin obo:GO_1902428 biological_process obo:GO_1902428 GO:1902428 obo:GO_1902428 negative regulation of water channel activity obo:GO_1902429 Any process that activates or increases the frequency, rate or extent of water channel activity. obo:GO_1902429 obo:go.owl obo:GO_1902429 bf obo:GO_1902429 2013-09-23T12:56:49Z obo:GO_1902429 up regulation of water channel activity obo:GO_1902429 up-regulation of water channel activity obo:GO_1902429 upregulation of water channel activity obo:GO_1902429 activation of aquaporin obo:GO_1902429 activation of water channel activity obo:GO_1902429 aquaporin activation obo:GO_1902429 positive regulation of aquaporin obo:GO_1902429 up regulation of aquaporin obo:GO_1902429 up-regulation of aquaporin obo:GO_1902429 upregulation of aquaporin obo:GO_1902429 biological_process obo:GO_1902429 GO:1902429 obo:GO_1902429 positive regulation of water channel activity obo:GO_1902433 Any positive regulation of water channel activity that is involved in maintenance of lens transparency. obo:GO_1902433 obo:go.owl obo:GO_1902433 bf obo:GO_1902433 2013-10-02T12:58:00Z obo:GO_1902433 positive regulation of water channel activity involved in maintenance of ocular lens transparency obo:GO_1902433 positive regulation of water channel activity involved in preservation of lens transparency obo:GO_1902433 up regulation of water channel activity involved in maintenance of lens transparency obo:GO_1902433 up regulation of water channel activity involved in maintenance of ocular lens transparency obo:GO_1902433 up regulation of water channel activity involved in preservation of lens transparency obo:GO_1902433 up-regulation of water channel activity involved in maintenance of lens transparency obo:GO_1902433 up-regulation of water channel activity involved in maintenance of ocular lens transparency obo:GO_1902433 up-regulation of water channel activity involved in preservation of lens transparency obo:GO_1902433 upregulation of water channel activity involved in maintenance of lens transparency obo:GO_1902433 upregulation of water channel activity involved in maintenance of ocular lens transparency obo:GO_1902433 upregulation of water channel activity involved in preservation of lens transparency obo:GO_1902433 activation of aquaporin involved in maintenance of lens transparency obo:GO_1902433 activation of aquaporin involved in maintenance of ocular lens transparency obo:GO_1902433 activation of aquaporin involved in preservation of lens transparency obo:GO_1902433 activation of water channel activity involved in maintenance of lens transparency obo:GO_1902433 activation of water channel activity involved in maintenance of ocular lens transparency obo:GO_1902433 activation of water channel activity involved in preservation of lens transparency obo:GO_1902433 aquaporin activation involved in maintenance of lens transparency obo:GO_1902433 aquaporin activation involved in maintenance of ocular lens transparency obo:GO_1902433 aquaporin activation involved in preservation of lens transparency obo:GO_1902433 positive regulation of aquaporin involved in maintenance of lens transparency obo:GO_1902433 positive regulation of aquaporin involved in maintenance of ocular lens transparency obo:GO_1902433 positive regulation of aquaporin involved in preservation of lens transparency obo:GO_1902433 up regulation of aquaporin involved in maintenance of lens transparency obo:GO_1902433 up regulation of aquaporin involved in maintenance of ocular lens transparency obo:GO_1902433 up regulation of aquaporin involved in preservation of lens transparency obo:GO_1902433 up-regulation of aquaporin involved in maintenance of lens transparency obo:GO_1902433 up-regulation of aquaporin involved in maintenance of ocular lens transparency obo:GO_1902433 up-regulation of aquaporin involved in preservation of lens transparency obo:GO_1902433 upregulation of aquaporin involved in maintenance of lens transparency obo:GO_1902433 upregulation of aquaporin involved in maintenance of ocular lens transparency obo:GO_1902433 upregulation of aquaporin involved in preservation of lens transparency obo:GO_1902433 biological_process obo:GO_1902433 GO:1902433 obo:GO_1902433 positive regulation of water channel activity involved in maintenance of lens transparency obo:GO_1902444 Interacting selectively and non-covalently with riboflavin. obo:GO_1902444 obo:go.owl obo:GO_1902444 al obo:GO_1902444 2013-10-11T08:44:52Z obo:GO_1902444 molecular_function obo:GO_1902444 GO:1902444 obo:GO_1902444 riboflavin binding obo:GO_1902460 Any process that modulates the frequency, rate or extent of mesenchymal stem cell proliferation. obo:GO_1902460 obo:go.owl obo:GO_1902460 pm obo:GO_1902460 2013-10-22T10:01:00Z obo:GO_1902460 regulation of MSC proliferation obo:GO_1902460 biological_process obo:GO_1902460 GO:1902460 obo:GO_1902460 regulation of mesenchymal stem cell proliferation obo:GO_1902461 Any process that stops, prevents or reduces the frequency, rate or extent of mesenchymal stem cell proliferation. obo:GO_1902461 obo:go.owl obo:GO_1902461 pm obo:GO_1902461 2013-10-22T10:01:08Z obo:GO_1902461 down regulation of MSC proliferation obo:GO_1902461 down regulation of mesenchymal stem cell proliferation obo:GO_1902461 down-regulation of MSC proliferation obo:GO_1902461 down-regulation of mesenchymal stem cell proliferation obo:GO_1902461 downregulation of MSC proliferation obo:GO_1902461 downregulation of mesenchymal stem cell proliferation obo:GO_1902461 negative regulation of MSC proliferation obo:GO_1902461 inhibition of MSC proliferation obo:GO_1902461 inhibition of mesenchymal stem cell proliferation obo:GO_1902461 biological_process obo:GO_1902461 GO:1902461 obo:GO_1902461 negative regulation of mesenchymal stem cell proliferation obo:GO_1902462 Any process that activates or increases the frequency, rate or extent of mesenchymal stem cell proliferation. obo:GO_1902462 obo:go.owl obo:GO_1902462 pm obo:GO_1902462 2013-10-22T10:01:17Z obo:GO_1902462 positive regulation of MSC proliferation obo:GO_1902462 up regulation of MSC proliferation obo:GO_1902462 up regulation of mesenchymal stem cell proliferation obo:GO_1902462 up-regulation of MSC proliferation obo:GO_1902462 up-regulation of mesenchymal stem cell proliferation obo:GO_1902462 upregulation of MSC proliferation obo:GO_1902462 upregulation of mesenchymal stem cell proliferation obo:GO_1902462 activation of MSC proliferation obo:GO_1902462 activation of mesenchymal stem cell proliferation obo:GO_1902462 biological_process obo:GO_1902462 GO:1902462 obo:GO_1902462 positive regulation of mesenchymal stem cell proliferation obo:GO_1902473 Any process that modulates the frequency, rate or extent of protein localization to synapse. obo:GO_1902473 obo:go.owl obo:GO_1902473 kmv obo:GO_1902473 2013-10-25T15:09:09Z obo:GO_1902473 regulation of protein localisation to synapse obo:GO_1902473 biological_process obo:GO_1902473 GO:1902473 obo:GO_1902473 regulation of protein localization to synapse obo:GO_1902474 Any process that activates or increases the frequency, rate or extent of protein localization to synapse. obo:GO_1902474 obo:go.owl obo:GO_1902474 kmv obo:GO_1902474 2013-10-25T15:09:18Z obo:GO_1902474 positive regulation of protein localisation to synapse obo:GO_1902474 up regulation of protein localisation to synapse obo:GO_1902474 up regulation of protein localization to synapse obo:GO_1902474 up-regulation of protein localisation to synapse obo:GO_1902474 up-regulation of protein localization to synapse obo:GO_1902474 upregulation of protein localisation to synapse obo:GO_1902474 upregulation of protein localization to synapse obo:GO_1902474 activation of protein localisation to synapse obo:GO_1902474 activation of protein localization to synapse obo:GO_1902474 biological_process obo:GO_1902474 GO:1902474 obo:GO_1902474 positive regulation of protein localization to synapse obo:GO_1902485 Interacting selectively and non-covalently with L-cysteine. obo:GO_1902485 obo:go.owl obo:GO_1902485 bhm obo:GO_1902485 2013-11-12T09:06:28Z obo:GO_1902485 molecular_function obo:GO_1902485 GO:1902485 obo:GO_1902485 L-cysteine binding obo:GO_1902496 Any protein binding that is involved in negative regulation of telomere maintenance via telomerase. obo:GO_1902496 obo:go.owl obo:GO_1902496 dph obo:GO_1902496 2013-11-13T16:22:49Z obo:GO_1902496 protein binding involved in down regulation of telomere maintenance via telomerase activity obo:GO_1902496 protein binding involved in down-regulation of telomere maintenance via telomerase activity obo:GO_1902496 protein binding involved in downregulation of telomere maintenance via telomerase activity obo:GO_1902496 protein binding involved in inhibition of telomere maintenance via telomerase obo:GO_1902496 molecular_function obo:GO_1902496 GO:1902496 obo:GO_1902496 protein binding involved in negative regulation of telomere maintenance via telomerase obo:GO_1902497 The directed movement of an iron-sulfur cluster into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. obo:GO_1902497 obo:go.owl obo:GO_1902497 dph obo:GO_1902497 2013-11-13T16:33:00Z obo:GO_1902497 biological_process obo:GO_1902497 GO:1902497 obo:GO_1902497 iron-sulfur cluster transport obo:GO_1902514 Any process that modulates the frequency, rate or extent of generation of calcium ion transmembrane transport via high voltage-gated calcium channel. obo:GO_1902514 obo:go.owl obo:GO_1902514 dph obo:GO_1902514 2013-11-16T00:04:42Z obo:GO_1902514 biological_process obo:GO_1902514 regulation of generation of L-type calcium current obo:GO_1902514 GO:1902514 obo:GO_1902514 regulation of calcium ion transmembrane transport via high voltage-gated calcium channel obo:GO_1902516 Interacting selectively and non-covalently with sn-glycerol 3-phosphate. obo:GO_1902516 obo:go.owl obo:GO_1902516 bhm obo:GO_1902516 2013-11-27T16:50:55Z obo:GO_1902516 molecular_function obo:GO_1902516 GO:1902516 obo:GO_1902516 An example of this is UgpB in E. coli [P0AG80] - see PMID:23013274. obo:GO_1902516 sn-glycerol 3-phosphate binding obo:GO_1902531 Any process that modulates the frequency, rate or extent of intracellular signal transduction. obo:GO_1902531 obo:go.owl obo:GO_1902531 bf obo:GO_1902531 2013-12-02T11:32:52Z obo:GO_1902531 GO:0010627 obo:GO_1902531 regulation of intracellular signaling cascade obo:GO_1902531 regulation of intracellular signaling chain obo:GO_1902531 regulation of intracellular protein kinase cascade obo:GO_1902531 regulation of intracellular signal transduction pathway obo:GO_1902531 regulation of signal transmission via intracellular cascade obo:GO_1902531 biological_process obo:GO_1902531 regulation of intracellular signaling pathway obo:GO_1902531 regulation of signal transduction via intracellular signaling cascade obo:GO_1902531 GO:1902531 obo:GO_1902531 regulation of intracellular signal transduction obo:GO_1902542 Any process that modulates the frequency, rate or extent of protein localization to mitotic spindle pole body. obo:GO_1902542 obo:go.owl obo:GO_1902542 al obo:GO_1902542 2013-12-04T13:47:09Z obo:GO_1902542 regulation of protein localisation to mitotic spindle pole body obo:GO_1902542 biological_process obo:GO_1902542 GO:1902542 obo:GO_1902542 regulation of protein localization to mitotic spindle pole body obo:GO_1902543 Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to mitotic spindle pole body. obo:GO_1902543 obo:go.owl obo:GO_1902543 al obo:GO_1902543 2013-12-04T13:47:18Z obo:GO_1902543 down regulation of protein localisation to mitotic spindle pole body obo:GO_1902543 down regulation of protein localization to mitotic spindle pole body obo:GO_1902543 down-regulation of protein localisation in mitotic spindle pole body obo:GO_1902543 down-regulation of protein localisation to mitotic spindle pole body obo:GO_1902543 down-regulation of protein localization to mitotic spindle pole body obo:GO_1902543 downregulation of protein localisation to mitotic spindle pole body obo:GO_1902543 downregulation of protein localization to mitotic spindle pole body obo:GO_1902543 negative regulation of protein localisation to mitotic spindle pole body obo:GO_1902543 inhibition of protein localisation to mitotic spindle pole body obo:GO_1902543 inhibition of protein localization to mitotic spindle pole body obo:GO_1902543 biological_process obo:GO_1902543 GO:1902543 obo:GO_1902543 negative regulation of protein localization to mitotic spindle pole body obo:GO_1902600 The directed movement of a proton across a membrane. obo:GO_1902600 obo:go.owl obo:GO_1902600 pr obo:GO_1902600 2013-12-20T11:08:37Z obo:GO_1902600 GO:0006818 obo:GO_1902600 GO:0015991 obo:GO_1902600 GO:0015992 obo:GO_1902600 hydrogen transport obo:GO_1902600 proton transport obo:GO_1902600 hydrogen ion transmembrane transport obo:GO_1902600 hydrogen transmembrane transport obo:GO_1902600 proton transmembrane transport obo:GO_1902600 ATP hydrolysis coupled proton transport obo:GO_1902600 passive proton transport, down the electrochemical gradient obo:GO_1902600 biological_process obo:GO_1902600 hydrogen ion transport obo:GO_1902600 GO:1902600 obo:GO_1902600 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_pir obo:GO_1902600 proton transmembrane transport obo:GO_1902601 The directed movement of silver ion across a membrane. obo:GO_1902601 obo:go.owl obo:GO_1902601 pr obo:GO_1902601 2013-12-20T11:08:46Z obo:GO_1902601 silver transmembrane transport obo:GO_1902601 biological_process obo:GO_1902601 GO:1902601 obo:GO_1902601 silver ion transmembrane transport obo:GO_1902602 The process in which an aluminium ion is transported across a membrane. obo:GO_1902602 obo:go.owl obo:GO_1902602 pr obo:GO_1902602 2013-12-20T11:09:01Z obo:GO_1902602 aluminium transmembrane transport obo:GO_1902602 aluminum transmembrane transport obo:GO_1902602 aluminium ion transmembrane transport obo:GO_1902602 biological_process obo:GO_1902602 GO:1902602 obo:GO_1902602 aluminum ion transmembrane transport obo:GO_1902606 Any process that modulates the frequency, rate or extent of large conductance calcium-activated potassium channel activity. obo:GO_1902606 obo:go.owl obo:GO_1902606 sl obo:GO_1902606 2014-01-02T18:51:03Z obo:GO_1902606 regulation of BK KCa channels obo:GO_1902606 regulation of BK calcium-activated potassium channel activity obo:GO_1902606 regulation of large conductance KCa channels obo:GO_1902606 biological_process obo:GO_1902606 regulation of BK channel activity obo:GO_1902606 GO:1902606 obo:GO_1902606 regulation of large conductance calcium-activated potassium channel activity obo:GO_1902607 Any process that stops, prevents or reduces the frequency, rate or extent of large conductance calcium-activated potassium channel activity. obo:GO_1902607 obo:go.owl obo:GO_1902607 sl obo:GO_1902607 2014-01-02T18:51:12Z obo:GO_1902607 down regulation of BK KCa channels obo:GO_1902607 down regulation of BK calcium-activated potassium channel activity obo:GO_1902607 down regulation of large conductance KCa channels obo:GO_1902607 down regulation of large conductance calcium-activated potassium channel activity obo:GO_1902607 down-regulation of BK KCa channels obo:GO_1902607 down-regulation of BK calcium-activated potassium channel activity obo:GO_1902607 down-regulation of large conductance KCa channels obo:GO_1902607 down-regulation of large conductance calcium-activated potassium channel activity obo:GO_1902607 downregulation of BK KCa channels obo:GO_1902607 downregulation of BK calcium-activated potassium channel activity obo:GO_1902607 downregulation of large conductance KCa channels obo:GO_1902607 downregulation of large conductance calcium-activated potassium channel activity obo:GO_1902607 negative regulation of BK KCa channels obo:GO_1902607 negative regulation of BK calcium-activated potassium channel activity obo:GO_1902607 negative regulation of large conductance KCa channels obo:GO_1902607 inhibition of BK KCa channels obo:GO_1902607 inhibition of BK calcium-activated potassium channel activity obo:GO_1902607 inhibition of large conductance KCa channels obo:GO_1902607 inhibition of large conductance calcium-activated potassium channel activity obo:GO_1902607 biological_process obo:GO_1902607 down regulation of BK channel activity obo:GO_1902607 down-regulation of BK channel activity obo:GO_1902607 downregulation of BK channel activity obo:GO_1902607 inhibition of BK channel activity obo:GO_1902607 negative regulation of BK channel activity obo:GO_1902607 GO:1902607 obo:GO_1902607 negative regulation of large conductance calcium-activated potassium channel activity obo:GO_1902608 Any process that activates or increases the frequency, rate or extent of large conductance calcium-activated potassium channel activity. obo:GO_1902608 obo:go.owl obo:GO_1902608 sl obo:GO_1902608 2014-01-02T18:51:21Z obo:GO_1902608 positive regulation of BK KCa channels obo:GO_1902608 positive regulation of BK calcium-activated potassium channel activity obo:GO_1902608 positive regulation of large conductance KCa channels obo:GO_1902608 up regulation of BK KCa channels obo:GO_1902608 up regulation of BK calcium-activated potassium channel activity obo:GO_1902608 up regulation of large conductance KCa channels obo:GO_1902608 up regulation of large conductance calcium-activated potassium channel activity obo:GO_1902608 up-regulation of BK KCa channels obo:GO_1902608 up-regulation of BK calcium-activated potassium channel activity obo:GO_1902608 up-regulation of large conductance KCa channels obo:GO_1902608 up-regulation of large conductance calcium-activated potassium channel activity obo:GO_1902608 upregulation of BK KCa channels obo:GO_1902608 upregulation of BK calcium-activated potassium channel activity obo:GO_1902608 upregulation of large conductance KCa channels obo:GO_1902608 upregulation of large conductance calcium-activated potassium channel activity obo:GO_1902608 activation of BK KCa channels obo:GO_1902608 activation of BK calcium-activated potassium channel activity obo:GO_1902608 activation of large conductance KCa channels obo:GO_1902608 activation of large conductance calcium-activated potassium channel activity obo:GO_1902608 biological_process obo:GO_1902608 activation of BK channel activity obo:GO_1902608 positive regulation of BK channel activity obo:GO_1902608 up regulation of BK channel activity obo:GO_1902608 up-regulation of BK channel activity obo:GO_1902608 upregulation of BK channel activity obo:GO_1902608 GO:1902608 obo:GO_1902608 positive regulation of large conductance calcium-activated potassium channel activity obo:GO_1902656 The directed movement of calcium ion into a cytosol. obo:GO_1902656 obo:go.owl obo:GO_1902656 pr obo:GO_1902656 2014-01-22T13:41:11Z obo:GO_1902656 calcium import into cytosol obo:GO_1902656 biological_process obo:GO_1902656 GO:1902656 obo:GO_1902656 calcium ion import into cytosol obo:GO_1902670 Interacting selectively and non-covalently with carbon dioxide. obo:GO_1902670 obo:go.owl obo:GO_1902670 bhm obo:GO_1902670 2014-02-04T10:38:41Z obo:GO_1902670 CO2 binding obo:GO_1902670 molecular_function obo:GO_1902670 GO:1902670 obo:GO_1902670 carbon dioxide binding obo:GO_1902683 Any process that modulates the frequency, rate or extent of receptor localization to synapse. obo:GO_1902683 obo:go.owl obo:GO_1902683 kmv obo:GO_1902683 2014-02-07T17:38:31Z obo:GO_1902683 regulation of receptor localisation to synapse obo:GO_1902683 biological_process obo:GO_1902683 GO:1902683 obo:GO_1902683 regulation of receptor localization to synapse obo:GO_1902684 Any process that stops, prevents or reduces the frequency, rate or extent of receptor localization to synapse. obo:GO_1902684 obo:go.owl obo:GO_1902684 kmv obo:GO_1902684 2014-02-07T17:38:41Z obo:GO_1902684 down regulation of receptor localisation to synapse obo:GO_1902684 down regulation of receptor localization to synapse obo:GO_1902684 down-regulation of receptor localisation to synapse obo:GO_1902684 down-regulation of receptor localization to synapse obo:GO_1902684 downregulation of receptor localisation to synapse obo:GO_1902684 downregulation of receptor localization to synapse obo:GO_1902684 negative regulation of receptor localisation to synapse obo:GO_1902684 inhibition of receptor localisation to synapse obo:GO_1902684 inhibition of receptor localization to synapse obo:GO_1902684 biological_process obo:GO_1902684 GO:1902684 obo:GO_1902684 negative regulation of receptor localization to synapse obo:GO_1902685 Any process that activates or increases the frequency, rate or extent of receptor localization to synapse. obo:GO_1902685 obo:go.owl obo:GO_1902685 kmv obo:GO_1902685 2014-02-07T17:38:51Z obo:GO_1902685 positive regulation of receptor localisation to synapse obo:GO_1902685 up regulation of receptor localisation to synapse obo:GO_1902685 up regulation of receptor localization to synapse obo:GO_1902685 up-regulation of receptor localisation to synapse obo:GO_1902685 up-regulation of receptor localization to synapse obo:GO_1902685 upregulation of receptor localisation to synapse obo:GO_1902685 upregulation of receptor localization to synapse obo:GO_1902685 activation of receptor localisation to synapse obo:GO_1902685 activation of receptor localization to synapse obo:GO_1902685 biological_process obo:GO_1902685 GO:1902685 obo:GO_1902685 positive regulation of receptor localization to synapse obo:GO_1902723 Any process that stops, prevents or reduces the frequency, rate or extent of satellite cell proliferation. obo:GO_1902723 obo:go.owl obo:GO_1902723 mrice obo:GO_1902723 2014-02-24T16:09:46Z obo:GO_1902723 down regulation of satellite cell proliferation obo:GO_1902723 down-regulation of satellite cell proliferation obo:GO_1902723 downregulation of satellite cell proliferation obo:GO_1902723 inhibition of satellite cell proliferation obo:GO_1902723 biological_process obo:GO_1902723 GO:1902723 obo:GO_1902723 negative regulation of skeletal muscle satellite cell proliferation obo:GO_1902724 Any process that activates or increases the frequency, rate or extent of skeletal muscle satellite cell proliferation. obo:GO_1902724 obo:go.owl obo:GO_1902724 mrice obo:GO_1902724 2014-02-24T16:09:56Z obo:GO_1902724 up regulation of satellite cell proliferation obo:GO_1902724 up-regulation of satellite cell proliferation obo:GO_1902724 upregulation of satellite cell proliferation obo:GO_1902724 activation of satellite cell proliferation obo:GO_1902724 biological_process obo:GO_1902724 GO:1902724 obo:GO_1902724 positive regulation of skeletal muscle satellite cell proliferation obo:GO_1902727 Any process that stops, prevents or reduces the frequency, rate or extent of satellite cell proliferation; dependent on specific growth factor activity such as fibroblast growth factors and transforming growth factor beta. obo:GO_1902727 obo:go.owl obo:GO_1902727 mrice obo:GO_1902727 2014-02-24T16:10:24Z obo:GO_1902727 biological_process obo:GO_1902727 GO:1902727 obo:GO_1902727 negative regulation of growth factor dependent skeletal muscle satellite cell proliferation obo:GO_1902728 Any process that activates or increases the frequency, rate or extent of satellite cell proliferation; dependent on specific growth factor activity such as fibroblast growth factors and transforming growth factor beta. obo:GO_1902728 obo:go.owl obo:GO_1902728 mrice obo:GO_1902728 2014-02-24T16:10:33Z obo:GO_1902728 biological_process obo:GO_1902728 GO:1902728 obo:GO_1902728 positive regulation of growth factor dependent skeletal muscle satellite cell proliferation obo:GO_1902731 Any process that stops, prevents, or reduces the frequency, rate or extent of the multiplication or reproduction of chondrocytes by cell division, resulting in the expansion of their population. A chondrocyte is a polymorphic cell that forms cartilage. obo:GO_1902731 obo:go.owl obo:GO_1902731 mrice obo:GO_1902731 2014-02-24T16:11:02Z obo:GO_1902731 down regulation of cartilage cell proliferation obo:GO_1902731 down regulation of chondrocyte cell proliferation obo:GO_1902731 down regulation of chondrocyte proliferation obo:GO_1902731 down-regulation of cartilage cell proliferation obo:GO_1902731 down-regulation of chondrocyte cell proliferation obo:GO_1902731 down-regulation of chondrocyte proliferation obo:GO_1902731 downregulation of cartilage cell proliferation obo:GO_1902731 downregulation of chondrocyte cell proliferation obo:GO_1902731 downregulation of chondrocyte proliferation obo:GO_1902731 negative regulation of cartilage cell proliferation obo:GO_1902731 negative regulation of chondrocyte cell proliferation obo:GO_1902731 inhibition of cartilage cell proliferation obo:GO_1902731 inhibition of chondrocyte cell proliferation obo:GO_1902731 inhibition of chondrocyte proliferation obo:GO_1902731 biological_process obo:GO_1902731 GO:1902731 obo:GO_1902731 negative regulation of chondrocyte proliferation obo:GO_1902732 Any process that increases the frequency, rate or extent of the multiplication or reproduction of chondrocytes by cell division, resulting in the expansion of their population. A chondrocyte is a polymorphic cell that forms cartilage. obo:GO_1902732 obo:go.owl obo:GO_1902732 mrice obo:GO_1902732 2014-02-24T16:11:18Z obo:GO_1902732 positive regulation of cartilage cell proliferation obo:GO_1902732 positive regulation of chondrocyte cell proliferation obo:GO_1902732 up regulation of cartilage cell proliferation obo:GO_1902732 up regulation of chondrocyte cell proliferation obo:GO_1902732 up regulation of chondrocyte proliferation obo:GO_1902732 up-regulation of cartilage cell proliferation obo:GO_1902732 up-regulation of chondrocyte cell proliferation obo:GO_1902732 up-regulation of chondrocyte proliferation obo:GO_1902732 upregulation of cartilage cell proliferation obo:GO_1902732 upregulation of chondrocyte cell proliferation obo:GO_1902732 upregulation of chondrocyte proliferation obo:GO_1902732 activation of cartilage cell proliferation obo:GO_1902732 activation of chondrocyte cell proliferation obo:GO_1902732 activation of chondrocyte proliferation obo:GO_1902732 biological_process obo:GO_1902732 GO:1902732 obo:GO_1902732 positive regulation of chondrocyte proliferation obo:GO_1902816 Any process that modulates the frequency, rate or extent of protein localization to microtubule. obo:GO_1902816 obo:go.owl obo:GO_1902816 tb obo:GO_1902816 2014-03-27T22:07:12Z obo:GO_1902816 regulation of protein localisation to microtubule obo:GO_1902816 biological_process obo:GO_1902816 GO:1902816 obo:GO_1902816 regulation of protein localization to microtubule obo:GO_1902817 Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to microtubule. obo:GO_1902817 obo:go.owl obo:GO_1902817 tb obo:GO_1902817 2014-03-27T22:07:18Z obo:GO_1902817 down regulation of protein localisation to microtubule obo:GO_1902817 down regulation of protein localization to microtubule obo:GO_1902817 down-regulation of protein localisation to microtubule obo:GO_1902817 down-regulation of protein localization to microtubule obo:GO_1902817 downregulation of protein localisation to microtubule obo:GO_1902817 downregulation of protein localization to microtubule obo:GO_1902817 negative regulation of protein localisation to microtubule obo:GO_1902817 inhibition of protein localisation to microtubule obo:GO_1902817 inhibition of protein localization to microtubule obo:GO_1902817 biological_process obo:GO_1902817 GO:1902817 obo:GO_1902817 negative regulation of protein localization to microtubule obo:GO_1902832 Any process that stops, prevents or reduces the frequency, rate or extent of cell proliferation in dorsal spinal cord. obo:GO_1902832 obo:go.owl obo:GO_1902832 mr obo:GO_1902832 2014-03-31T17:42:50Z obo:GO_1902832 down regulation of cell proliferation in dorsal spinal cord obo:GO_1902832 down-regulation of cell proliferation in dorsal spinal cord obo:GO_1902832 downregulation of cell proliferation in dorsal spinal cord obo:GO_1902832 inhibition of cell proliferation in dorsal spinal cord obo:GO_1902832 biological_process obo:GO_1902832 GO:1902832 obo:GO_1902832 negative regulation of cell proliferation in dorsal spinal cord obo:GO_1902833 Any process that activates or increases the frequency, rate or extent of cell proliferation in dorsal spinal cord. obo:GO_1902833 obo:go.owl obo:GO_1902833 mr obo:GO_1902833 2014-03-31T17:43:33Z obo:GO_1902833 up regulation of cell proliferation in dorsal spinal cord obo:GO_1902833 up-regulation of cell proliferation in dorsal spinal cord obo:GO_1902833 upregulation of cell proliferation in dorsal spinal cord obo:GO_1902833 activation of cell proliferation in dorsal spinal cord obo:GO_1902833 biological_process obo:GO_1902833 GO:1902833 obo:GO_1902833 positive regulation of cell proliferation in dorsal spinal cord obo:GO_1902936 Interacting selectively and non-covalently with phosphatidylinositol bisphosphate. obo:GO_1902936 obo:go.owl obo:GO_1902936 bhm obo:GO_1902936 2014-04-25T15:14:12Z obo:GO_1902936 molecular_function obo:GO_1902936 GO:1902936 obo:GO_1902936 An example of this is KCNJ2 in human (P63252) in PMID:18690034 (inferred from direct assay) obo:GO_1902936 phosphatidylinositol bisphosphate binding obo:GO_1902938 Any process that modulates the frequency, rate or extent of intracellular calcium activated chloride channel activity. obo:GO_1902938 obo:go.owl obo:GO_1902938 als obo:GO_1902938 2014-04-28T08:49:08Z obo:GO_1902938 biological_process obo:GO_1902938 GO:1902938 obo:GO_1902938 regulation of intracellular calcium activated chloride channel activity obo:GO_1902939 Any process that stops, prevents or reduces the frequency, rate or extent of intracellular calcium activated chloride channel activity. obo:GO_1902939 obo:go.owl obo:GO_1902939 als obo:GO_1902939 2014-04-28T08:49:14Z obo:GO_1902939 down regulation of intracellular calcium activated chloride channel activity obo:GO_1902939 down-regulation of intracellular calcium activated chloride channel activity obo:GO_1902939 downregulation of intracellular calcium activated chloride channel activity obo:GO_1902939 inhibition of intracellular calcium activated chloride channel activity obo:GO_1902939 biological_process obo:GO_1902939 GO:1902939 obo:GO_1902939 negative regulation of intracellular calcium activated chloride channel activity obo:GO_1902940 Any process that activates or increases the frequency, rate or extent of intracellular calcium activated chloride channel activity. obo:GO_1902940 obo:go.owl obo:GO_1902940 als obo:GO_1902940 2014-04-28T08:49:20Z obo:GO_1902940 up regulation of intracellular calcium activated chloride channel activity obo:GO_1902940 up-regulation of intracellular calcium activated chloride channel activity obo:GO_1902940 upregulation of intracellular calcium activated chloride channel activity obo:GO_1902940 activation of intracellular calcium activated chloride channel activity obo:GO_1902940 biological_process obo:GO_1902940 GO:1902940 obo:GO_1902940 positive regulation of intracellular calcium activated chloride channel activity obo:GO_1902941 Any process that modulates the frequency, rate or extent of voltage-gated chloride channel activity. obo:GO_1902941 obo:go.owl obo:GO_1902941 als obo:GO_1902941 2014-04-28T08:55:31Z obo:GO_1902941 regulation of voltage gated chloride channel activity obo:GO_1902941 regulation of voltage-dependent chloride channel activity obo:GO_1902941 biological_process obo:GO_1902941 GO:1902941 obo:GO_1902941 regulation of voltage-gated chloride channel activity obo:GO_1902942 Any process that stops, prevents or reduces the frequency, rate or extent of voltage-gated chloride channel activity. obo:GO_1902942 obo:go.owl obo:GO_1902942 als obo:GO_1902942 2014-04-28T08:55:37Z obo:GO_1902942 down regulation of voltage gated chloride channel activity obo:GO_1902942 down regulation of voltage-dependent chloride channel activity obo:GO_1902942 down regulation of voltage-gated chloride channel activity obo:GO_1902942 down-regulation of voltage gated chloride channel activity obo:GO_1902942 down-regulation of voltage-dependent chloride channel activity obo:GO_1902942 down-regulation of voltage-gated chloride channel activity obo:GO_1902942 downregulation of voltage gated chloride channel activity obo:GO_1902942 downregulation of voltage-dependent chloride channel activity obo:GO_1902942 downregulation of voltage-gated chloride channel activity obo:GO_1902942 negative regulation of voltage gated chloride channel activity obo:GO_1902942 negative regulation of voltage-dependent chloride channel activity obo:GO_1902942 inhibition of voltage gated chloride channel activity obo:GO_1902942 inhibition of voltage-dependent chloride channel activity obo:GO_1902942 inhibition of voltage-gated chloride channel activity obo:GO_1902942 biological_process obo:GO_1902942 GO:1902942 obo:GO_1902942 negative regulation of voltage-gated chloride channel activity obo:GO_1902943 Any process that activates or increases the frequency, rate or extent of voltage-gated chloride channel activity. obo:GO_1902943 obo:go.owl obo:GO_1902943 als obo:GO_1902943 2014-04-28T08:55:43Z obo:GO_1902943 positive regulation of voltage gated chloride channel activity obo:GO_1902943 positive regulation of voltage-dependent chloride channel activity obo:GO_1902943 up regulation of voltage gated chloride channel activity obo:GO_1902943 up regulation of voltage-dependent chloride channel activity obo:GO_1902943 up regulation of voltage-gated chloride channel activity obo:GO_1902943 up-regulation of voltage gated chloride channel activity obo:GO_1902943 up-regulation of voltage-dependent chloride channel activity obo:GO_1902943 up-regulation of voltage-gated chloride channel activity obo:GO_1902943 upregulation of voltage gated chloride channel activity obo:GO_1902943 upregulation of voltage-dependent chloride channel activity obo:GO_1902943 upregulation of voltage-gated chloride channel activity obo:GO_1902943 activation of voltage gated chloride channel activity obo:GO_1902943 activation of voltage-dependent chloride channel activity obo:GO_1902943 activation of voltage-gated chloride channel activity obo:GO_1902943 biological_process obo:GO_1902943 GO:1902943 obo:GO_1902943 positive regulation of voltage-gated chloride channel activity obo:GO_1902965 Any process that modulates the frequency, rate or extent of protein localization to early endosome. obo:GO_1902965 obo:go.owl obo:GO_1902965 sjp obo:GO_1902965 2014-05-06T09:28:24Z obo:GO_1902965 regulation of protein localisation in early endosome obo:GO_1902965 regulation of protein localisation to early endosome obo:GO_1902965 regulation of protein localization in early endosome obo:GO_1902965 biological_process obo:GO_1902965 GO:1902965 obo:GO_1902965 regulation of protein localization to early endosome obo:GO_1902966 Any process that activates or increases the frequency, rate or extent of protein localization to early endosome. obo:GO_1902966 obo:go.owl obo:GO_1902966 sjp obo:GO_1902966 2014-05-06T09:28:30Z obo:GO_1902966 positive regulation of protein localisation in early endosome obo:GO_1902966 positive regulation of protein localisation to early endosome obo:GO_1902966 positive regulation of protein localization in early endosome obo:GO_1902966 up regulation of protein localisation in early endosome obo:GO_1902966 up regulation of protein localisation to early endosome obo:GO_1902966 up regulation of protein localization in early endosome obo:GO_1902966 up regulation of protein localization to early endosome obo:GO_1902966 up-regulation of protein localisation in early endosome obo:GO_1902966 up-regulation of protein localisation to early endosome obo:GO_1902966 up-regulation of protein localization in early endosome obo:GO_1902966 up-regulation of protein localization to early endosome obo:GO_1902966 upregulation of protein localisation in early endosome obo:GO_1902966 upregulation of protein localisation to early endosome obo:GO_1902966 upregulation of protein localization in early endosome obo:GO_1902966 upregulation of protein localization to early endosome obo:GO_1902966 activation of protein localisation in early endosome obo:GO_1902966 activation of protein localisation to early endosome obo:GO_1902966 activation of protein localization in early endosome obo:GO_1902966 activation of protein localization to early endosome obo:GO_1902966 biological_process obo:GO_1902966 GO:1902966 obo:GO_1902966 positive regulation of protein localization to early endosome obo:GO_1903037 Any process that modulates the frequency, rate or extent of leukocyte cell-cell adhesion. obo:GO_1903037 obo:go.owl obo:GO_1903037 rl obo:GO_1903037 2014-05-19T15:29:58Z obo:GO_1903037 regulation of leukocyte adhesion obo:GO_1903037 regulation of leukocyte cell adhesion obo:GO_1903037 biological_process obo:GO_1903037 GO:1903037 obo:GO_1903037 Exogenous expression of ASS1 or NOS3 in HUVECs enhances NO production and inhibits monocyte adhesion obo:GO_1903037 regulation of leukocyte cell-cell adhesion obo:GO_1903038 Any process that stops, prevents or reduces the frequency, rate or extent of leukocyte cell-cell adhesion. obo:GO_1903038 obo:go.owl obo:GO_1903038 rl obo:GO_1903038 2014-05-19T15:30:05Z obo:GO_1903038 down regulation of leukocyte adhesion obo:GO_1903038 down regulation of leukocyte cell adhesion obo:GO_1903038 down regulation of leukocyte cell-cell adhesion obo:GO_1903038 down-regulation of leukocyte adhesion obo:GO_1903038 down-regulation of leukocyte cell adhesion obo:GO_1903038 down-regulation of leukocyte cell-cell adhesion obo:GO_1903038 downregulation of leukocyte adhesion obo:GO_1903038 downregulation of leukocyte cell adhesion obo:GO_1903038 downregulation of leukocyte cell-cell adhesion obo:GO_1903038 negative regulation of leukocyte adhesion obo:GO_1903038 negative regulation of leukocyte cell adhesion obo:GO_1903038 inhibition of leukocyte adhesion obo:GO_1903038 inhibition of leukocyte cell adhesion obo:GO_1903038 inhibition of leukocyte cell-cell adhesion obo:GO_1903038 biological_process obo:GO_1903038 GO:1903038 obo:GO_1903038 Exogenous expression of ASS1 or NOS3 in HUVECs enhances NO production and inhibits monocyte adhesion obo:GO_1903038 negative regulation of leukocyte cell-cell adhesion obo:GO_1903039 Any process that activates or increases the frequency, rate or extent of leukocyte cell-cell adhesion. obo:GO_1903039 obo:go.owl obo:GO_1903039 rl obo:GO_1903039 2014-05-19T15:30:15Z obo:GO_1903039 positive regulation of leukocyte adhesion obo:GO_1903039 positive regulation of leukocyte cell adhesion obo:GO_1903039 up regulation of leukocyte adhesion obo:GO_1903039 up regulation of leukocyte cell adhesion obo:GO_1903039 up regulation of leukocyte cell-cell adhesion obo:GO_1903039 up-regulation of leukocyte adhesion obo:GO_1903039 up-regulation of leukocyte cell adhesion obo:GO_1903039 up-regulation of leukocyte cell-cell adhesion obo:GO_1903039 upregulation of leukocyte adhesion obo:GO_1903039 upregulation of leukocyte cell adhesion obo:GO_1903039 upregulation of leukocyte cell-cell adhesion obo:GO_1903039 activation of leukocyte adhesion obo:GO_1903039 activation of leukocyte cell adhesion obo:GO_1903039 activation of leukocyte cell-cell adhesion obo:GO_1903039 biological_process obo:GO_1903039 GO:1903039 obo:GO_1903039 Exogenous expression of ASS1 or NOS3 in HUVECs enhances NO production and inhibits monocyte adhesion obo:GO_1903039 positive regulation of leukocyte cell-cell adhesion obo:GO_1903066 Any process that modulates the frequency, rate or extent of protein localization to cell tip. obo:GO_1903066 obo:go.owl obo:GO_1903066 vw obo:GO_1903066 2014-05-28T15:48:42Z obo:GO_1903066 regulation of protein localisation to cell tip obo:GO_1903066 biological_process obo:GO_1903066 GO:1903066 obo:GO_1903066 regulation of protein localization to cell tip obo:GO_1903067 Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to cell tip. obo:GO_1903067 obo:go.owl obo:GO_1903067 vw obo:GO_1903067 2014-05-28T15:48:48Z obo:GO_1903067 down regulation of protein localisation to cell tip obo:GO_1903067 down regulation of protein localization to cell tip obo:GO_1903067 down-regulation of protein localisation to cell tip obo:GO_1903067 down-regulation of protein localization to cell tip obo:GO_1903067 downregulation of protein localisation to cell tip obo:GO_1903067 downregulation of protein localization to cell tip obo:GO_1903067 negative regulation of protein localisation to cell tip obo:GO_1903067 inhibition of protein localisation to cell tip obo:GO_1903067 inhibition of protein localization to cell tip obo:GO_1903067 biological_process obo:GO_1903067 GO:1903067 obo:GO_1903067 negative regulation of protein localization to cell tip obo:GO_1903068 Any process that activates or increases the frequency, rate or extent of protein localization to cell tip. obo:GO_1903068 obo:go.owl obo:GO_1903068 vw obo:GO_1903068 2014-05-28T15:48:54Z obo:GO_1903068 positive regulation of protein localisation to cell tip obo:GO_1903068 up regulation of protein localisation to cell tip obo:GO_1903068 up regulation of protein localization to cell tip obo:GO_1903068 up-regulation of protein localisation to cell tip obo:GO_1903068 up-regulation of protein localization to cell tip obo:GO_1903068 upregulation of protein localisation to cell tip obo:GO_1903068 upregulation of protein localization to cell tip obo:GO_1903068 activation of protein localisation to cell tip obo:GO_1903068 activation of protein localization to cell tip obo:GO_1903068 biological_process obo:GO_1903068 GO:1903068 obo:GO_1903068 positive regulation of protein localization to cell tip obo:GO_1903076 Any process that modulates the frequency, rate or extent of protein localization to plasma membrane. obo:GO_1903076 obo:go.owl obo:GO_1903076 tanyaberardini obo:GO_1903076 2009-07-10T10:32:44Z obo:GO_1903076 GO:0090003 obo:GO_1903076 GO:1905963 obo:GO_1903076 regulation of protein localization in plasma membrane obo:GO_1903076 biological_process obo:GO_1903076 regulation of establishment of protein localisation in plasma membrane obo:GO_1903076 regulation of establishment of protein localization in plasma membrane obo:GO_1903076 regulation of establishment of protein localization to plasma membrane obo:GO_1903076 regulation of protein localisation in plasma membrane obo:GO_1903076 regulation of protein targeting to plasma membrane obo:GO_1903076 regulation of protein-plasma membrane targeting obo:GO_1903076 GO:1903076 obo:GO_1903076 regulation of protein localization to plasma membrane obo:GO_1903077 Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to plasma membrane. obo:GO_1903077 obo:go.owl obo:GO_1903077 tanyaberardini obo:GO_1903077 2014-05-29T17:10:16Z obo:GO_1903077 GO:0090005 obo:GO_1903077 GO:1905964 obo:GO_1903077 down regulation of protein localisation in plasma membrane obo:GO_1903077 down regulation of protein localization in plasma membrane obo:GO_1903077 down regulation of protein localization to plasma membrane obo:GO_1903077 down-regulation of protein localisation in plasma membrane obo:GO_1903077 down-regulation of protein localization in plasma membrane obo:GO_1903077 down-regulation of protein localization to plasma membrane obo:GO_1903077 downregulation of protein localisation in plasma membrane obo:GO_1903077 downregulation of protein localization in plasma membrane obo:GO_1903077 downregulation of protein localization to plasma membrane obo:GO_1903077 negative regulation of protein localization in plasma membrane obo:GO_1903077 inhibition of protein localisation in plasma membrane obo:GO_1903077 inhibition of protein localization in plasma membrane obo:GO_1903077 inhibition of protein localization to plasma membrane obo:GO_1903077 inhibition of protein targeting to plasma membrane obo:GO_1903077 inhibition of protein-plasma membrane targeting obo:GO_1903077 biological_process obo:GO_1903077 down regulation of protein targeting to plasma membrane obo:GO_1903077 down regulation of protein-plasma membrane targeting obo:GO_1903077 down-regulation of protein targeting to plasma membrane obo:GO_1903077 down-regulation of protein-plasma membrane targeting obo:GO_1903077 downregulation of protein targeting to plasma membrane obo:GO_1903077 downregulation of protein-plasma membrane targeting obo:GO_1903077 negative regulation of establishment of protein localisation in plasma membrane obo:GO_1903077 negative regulation of establishment of protein localization in plasma membrane obo:GO_1903077 negative regulation of establishment of protein localization to plasma membrane obo:GO_1903077 negative regulation of protein localisation in plasma membrane obo:GO_1903077 negative regulation of protein targeting to plasma membrane obo:GO_1903077 negative regulation of protein-plasma membrane targeting obo:GO_1903077 GO:1903077 obo:GO_1903077 negative regulation of protein localization to plasma membrane obo:GO_1903078 Any process that activates or increases the frequency, rate or extent of protein localization to plasma membrane. obo:GO_1903078 obo:go.owl obo:GO_1903078 tanyaberardini obo:GO_1903078 2009-07-10T10:34:17Z obo:GO_1903078 GO:0090004 obo:GO_1903078 GO:1905965 obo:GO_1903078 positive regulation of protein localisation in plasma membrane obo:GO_1903078 positive regulation of protein localization in plasma membrane obo:GO_1903078 up regulation of protein localisation in plasma membrane obo:GO_1903078 up regulation of protein localization in plasma membrane obo:GO_1903078 up regulation of protein localization to plasma membrane obo:GO_1903078 up-regulation of protein localisation in plasma membrane obo:GO_1903078 up-regulation of protein localization in plasma membrane obo:GO_1903078 up-regulation of protein localization to plasma membrane obo:GO_1903078 upregulation of protein localisation in plasma membrane obo:GO_1903078 upregulation of protein localization in plasma membrane obo:GO_1903078 upregulation of protein localization to plasma membrane obo:GO_1903078 activation of protein localisation in plasma membrane obo:GO_1903078 activation of protein localization in plasma membrane obo:GO_1903078 activation of protein localization to plasma membrane obo:GO_1903078 activation of protein targeting to plasma membrane obo:GO_1903078 activation of protein-plasma membrane targeting obo:GO_1903078 biological_process obo:GO_1903078 positive regulation of establishment of protein localisation in plasma membrane obo:GO_1903078 positive regulation of establishment of protein localization to plasma membrane obo:GO_1903078 positive regulation of protein targeting to plasma membrane obo:GO_1903078 positive regulation of protein-plasma membrane targeting obo:GO_1903078 up regulation of protein targeting to plasma membrane obo:GO_1903078 up regulation of protein-plasma membrane targeting obo:GO_1903078 up-regulation of protein targeting to plasma membrane obo:GO_1903078 up-regulation of protein-plasma membrane targeting obo:GO_1903078 upregulation of protein targeting to plasma membrane obo:GO_1903078 upregulation of protein-plasma membrane targeting obo:GO_1903078 GO:1903078 obo:GO_1903078 positive regulation of protein localization to plasma membrane obo:GO_1903135 Interacting selectively and non-covalently with cupric ion, copper(2+). obo:GO_1903135 obo:go.owl obo:GO_1903135 bf obo:GO_1903135 2014-06-26T14:38:16Z obo:GO_1903135 Cu(2+) binding obo:GO_1903135 Cu(II) binding obo:GO_1903135 copper(2+)binding obo:GO_1903135 molecular_function obo:GO_1903135 GO:1903135 obo:GO_1903135 cupric ion binding obo:GO_1903136 Interacting selectively and non-covalently with cuprous ion, copper(1+). obo:GO_1903136 obo:go.owl obo:GO_1903136 bf obo:GO_1903136 2014-06-26T14:38:23Z obo:GO_1903136 Cu(+) binding obo:GO_1903136 Cu(I) binding obo:GO_1903136 copper(1+) binding obo:GO_1903136 molecular_function obo:GO_1903136 GO:1903136 obo:GO_1903136 cuprous ion binding obo:GO_1903169 Any process that modulates the frequency, rate or extent of calcium ion transmembrane transport. obo:GO_1903169 obo:go.owl obo:GO_1903169 rl obo:GO_1903169 2014-07-11T17:09:26Z obo:GO_1903169 regulation of calcium ion membrane transport obo:GO_1903169 regulation of transmembrane calcium transport obo:GO_1903169 biological_process obo:GO_1903169 GO:1903169 obo:GO_1903169 human HRC regulates RYR2 and thus regulates transmembrane transport of calcium from SR to cytosol obo:GO_1903169 regulation of calcium ion transmembrane transport obo:GO_1903170 Any process that stops, prevents or reduces the frequency, rate or extent of calcium ion transmembrane transport. obo:GO_1903170 obo:go.owl obo:GO_1903170 rl obo:GO_1903170 2014-07-11T17:09:32Z obo:GO_1903170 down regulation of calcium ion membrane transport obo:GO_1903170 down regulation of calcium ion transmembrane transport obo:GO_1903170 down regulation of transmembrane calcium transport obo:GO_1903170 down-regulation of calcium ion membrane transport obo:GO_1903170 down-regulation of calcium ion transmembrane transport obo:GO_1903170 down-regulation of transmembrane calcium transport obo:GO_1903170 downregulation of calcium ion membrane transport obo:GO_1903170 downregulation of calcium ion transmembrane transport obo:GO_1903170 downregulation of transmembrane calcium transport obo:GO_1903170 negative regulation of calcium ion membrane transport obo:GO_1903170 negative regulation of transmembrane calcium transport obo:GO_1903170 inhibition of calcium ion membrane transport obo:GO_1903170 inhibition of calcium ion transmembrane transport obo:GO_1903170 inhibition of transmembrane calcium transport obo:GO_1903170 biological_process obo:GO_1903170 GO:1903170 obo:GO_1903170 human HRC regulates RYR2 and thus regulates transmembrane transport of calcium from SR to cytosol obo:GO_1903170 negative regulation of calcium ion transmembrane transport obo:GO_1903231 Any mRNA binding that is involved in posttranscriptional gene silencing. obo:GO_1903231 obo:go.owl obo:GO_1903231 jl obo:GO_1903231 2014-07-31T10:30:43Z obo:GO_1903231 mRNA binding involved in PTGS obo:GO_1903231 mRNA binding involved in post-transcriptional gene silencing obo:GO_1903231 mRNA binding involved in quelling obo:GO_1903231 molecular_function obo:GO_1903231 mRNA binding involved in cosuppression obo:GO_1903231 GO:1903231 obo:GO_1903231 mRNA binding involved in posttranscriptional gene silencing obo:GO_1903279 Any process that modulates the frequency, rate or extent of calcium:sodium antiporter activity. obo:GO_1903279 obo:go.owl obo:GO_1903279 rl obo:GO_1903279 2014-08-11T12:53:30Z obo:GO_1903279 regulation of sodium/calcium exchanger obo:GO_1903279 biological_process obo:GO_1903279 regulation of mitochondrial sodium/calcium ion exchange obo:GO_1903279 regulation of sodium:calcium exchange obo:GO_1903279 GO:1903279 obo:GO_1903279 regulation of calcium:sodium antiporter activity obo:GO_1903280 Any process that stops, prevents or reduces the frequency, rate or extent of calcium:sodium antiporter activity. obo:GO_1903280 obo:go.owl obo:GO_1903280 rl obo:GO_1903280 2014-08-11T12:53:38Z obo:GO_1903280 down regulation of calcium:sodium antiporter activity obo:GO_1903280 down regulation of sodium/calcium exchanger obo:GO_1903280 down-regulation of calcium:sodium antiporter activity obo:GO_1903280 down-regulation of sodium/calcium exchanger obo:GO_1903280 downregulation of calcium:sodium antiporter activity obo:GO_1903280 downregulation of sodium/calcium exchanger obo:GO_1903280 negative regulation of sodium/calcium exchanger obo:GO_1903280 inhibition of calcium:sodium antiporter activity obo:GO_1903280 inhibition of sodium/calcium exchanger obo:GO_1903280 biological_process obo:GO_1903280 down regulation of mitochondrial sodium/calcium ion exchange obo:GO_1903280 down regulation of sodium:calcium exchange obo:GO_1903280 down-regulation of mitochondrial sodium/calcium ion exchange obo:GO_1903280 down-regulation of sodium:calcium exchange obo:GO_1903280 downregulation of mitochondrial sodium/calcium ion exchange obo:GO_1903280 downregulation of sodium:calcium exchange obo:GO_1903280 inhibition of mitochondrial sodium/calcium ion exchange obo:GO_1903280 inhibition of sodium:calcium exchange obo:GO_1903280 negative regulation of mitochondrial sodium/calcium ion exchange obo:GO_1903280 negative regulation of sodium:calcium exchange obo:GO_1903280 GO:1903280 obo:GO_1903280 negative regulation of calcium:sodium antiporter activity obo:GO_1903281 Any process that activates or increases the frequency, rate or extent of calcium:sodium antiporter activity. obo:GO_1903281 obo:go.owl obo:GO_1903281 rl obo:GO_1903281 2014-08-11T12:53:47Z obo:GO_1903281 positive regulation of sodium/calcium exchanger obo:GO_1903281 up regulation of calcium:sodium antiporter activity obo:GO_1903281 up regulation of sodium/calcium exchanger obo:GO_1903281 up-regulation of calcium:sodium antiporter activity obo:GO_1903281 up-regulation of sodium/calcium exchanger obo:GO_1903281 upregulation of calcium:sodium antiporter activity obo:GO_1903281 upregulation of sodium/calcium exchanger obo:GO_1903281 activation of calcium:sodium antiporter activity obo:GO_1903281 activation of sodium/calcium exchanger obo:GO_1903281 biological_process obo:GO_1903281 activation of mitochondrial sodium/calcium ion exchange obo:GO_1903281 activation of sodium:calcium exchange obo:GO_1903281 positive regulation of mitochondrial sodium/calcium ion exchange obo:GO_1903281 positive regulation of sodium:calcium exchange obo:GO_1903281 up regulation of mitochondrial sodium/calcium ion exchange obo:GO_1903281 up regulation of sodium:calcium exchange obo:GO_1903281 up-regulation of mitochondrial sodium/calcium ion exchange obo:GO_1903281 up-regulation of sodium:calcium exchange obo:GO_1903281 upregulation of mitochondrial sodium/calcium ion exchange obo:GO_1903281 upregulation of sodium:calcium exchange obo:GO_1903281 GO:1903281 obo:GO_1903281 positive regulation of calcium:sodium antiporter activity obo:GO_1903286 Any process that modulates the frequency, rate or extent of potassium ion import. obo:GO_1903286 obo:go.owl obo:GO_1903286 rl obo:GO_1903286 2014-08-11T14:26:16Z obo:GO_1903286 regulation of potassium import obo:GO_1903286 regulation of potassium ion uptake obo:GO_1903286 biological_process obo:GO_1903286 GO:1903286 obo:GO_1903286 regulation of potassium ion import obo:GO_1903287 Any process that stops, prevents or reduces the frequency, rate or extent of potassium ion import across the plasma membrane. obo:GO_1903287 obo:go.owl obo:GO_1903287 rl obo:GO_1903287 2014-08-11T14:26:24Z obo:GO_1903287 down regulation of potassium import obo:GO_1903287 down regulation of potassium ion import obo:GO_1903287 down regulation of potassium ion uptake obo:GO_1903287 down-regulation of potassium import obo:GO_1903287 down-regulation of potassium ion import obo:GO_1903287 down-regulation of potassium ion uptake obo:GO_1903287 downregulation of potassium import obo:GO_1903287 downregulation of potassium ion import obo:GO_1903287 downregulation of potassium ion uptake obo:GO_1903287 negative regulation of potassium import obo:GO_1903287 negative regulation of potassium ion import obo:GO_1903287 negative regulation of potassium ion uptake obo:GO_1903287 inhibition of potassium import obo:GO_1903287 inhibition of potassium ion import obo:GO_1903287 inhibition of potassium ion uptake obo:GO_1903287 biological_process obo:GO_1903287 GO:1903287 obo:GO_1903287 negative regulation of potassium ion import across plasma membrane obo:GO_1903288 Any process that activates or increases the frequency, rate or extent of potassium ion import across the plasma membrane. obo:GO_1903288 obo:go.owl obo:GO_1903288 rl obo:GO_1903288 2014-08-11T14:26:32Z obo:GO_1903288 positive regulation of potassium ion import obo:GO_1903288 positive regulation of potassium import obo:GO_1903288 positive regulation of potassium ion uptake obo:GO_1903288 up regulation of potassium import obo:GO_1903288 up regulation of potassium ion import obo:GO_1903288 up regulation of potassium ion uptake obo:GO_1903288 up-regulation of potassium import obo:GO_1903288 up-regulation of potassium ion import obo:GO_1903288 up-regulation of potassium ion uptake obo:GO_1903288 upregulation of potassium import obo:GO_1903288 upregulation of potassium ion import obo:GO_1903288 upregulation of potassium ion uptake obo:GO_1903288 activation of potassium import obo:GO_1903288 activation of potassium ion import obo:GO_1903288 activation of potassium ion uptake obo:GO_1903288 biological_process obo:GO_1903288 GO:1903288 obo:GO_1903288 positive regulation of potassium ion import across plasma membrane obo:GO_1903332 Any process that modulates the frequency, rate or extent of protein folding. obo:GO_1903332 obo:go.owl obo:GO_1903332 vw obo:GO_1903332 2014-08-18T13:14:34Z obo:GO_1903332 regulation of alpha-tubulin folding obo:GO_1903332 regulation of beta-tubulin folding obo:GO_1903332 regulation of chaperonin-mediated tubulin folding obo:GO_1903332 biological_process obo:GO_1903332 regulation of chaperone activity obo:GO_1903332 regulation of chaperonin ATPase activity obo:GO_1903332 regulation of co-chaperone activity obo:GO_1903332 regulation of co-chaperonin activity obo:GO_1903332 regulation of glycoprotein-specific chaperone activity obo:GO_1903332 regulation of non-chaperonin molecular chaperone ATPase activity obo:GO_1903332 regulation of protein complex assembly, multichaperone pathway obo:GO_1903332 GO:1903332 obo:GO_1903332 regulation of protein folding obo:GO_1903333 Any process that stops, prevents or reduces the frequency, rate or extent of protein folding. obo:GO_1903333 obo:go.owl obo:GO_1903333 vw obo:GO_1903333 2014-08-18T13:14:42Z obo:GO_1903333 down regulation of protein folding obo:GO_1903333 down-regulation of protein folding obo:GO_1903333 downregulation of protein folding obo:GO_1903333 down regulation of alpha-tubulin folding obo:GO_1903333 down regulation of beta-tubulin folding obo:GO_1903333 down regulation of chaperonin-mediated tubulin folding obo:GO_1903333 down-regulation of alpha-tubulin folding obo:GO_1903333 down-regulation of beta-tubulin folding obo:GO_1903333 down-regulation of chaperonin-mediated tubulin folding obo:GO_1903333 downregulation of alpha-tubulin folding obo:GO_1903333 downregulation of beta-tubulin folding obo:GO_1903333 downregulation of chaperonin-mediated tubulin folding obo:GO_1903333 inhibition of alpha-tubulin folding obo:GO_1903333 inhibition of beta-tubulin folding obo:GO_1903333 inhibition of chaperonin-mediated tubulin folding obo:GO_1903333 inhibition of protein folding obo:GO_1903333 negative regulation of alpha-tubulin folding obo:GO_1903333 negative regulation of beta-tubulin folding obo:GO_1903333 negative regulation of chaperonin-mediated tubulin folding obo:GO_1903333 biological_process obo:GO_1903333 down regulation of chaperone activity obo:GO_1903333 down regulation of chaperonin ATPase activity obo:GO_1903333 down regulation of co-chaperone activity obo:GO_1903333 down regulation of co-chaperonin activity obo:GO_1903333 down regulation of glycoprotein-specific chaperone activity obo:GO_1903333 down regulation of non-chaperonin molecular chaperone ATPase activity obo:GO_1903333 down regulation of protein complex assembly, multichaperone pathway obo:GO_1903333 down-regulation of chaperone activity obo:GO_1903333 down-regulation of chaperonin ATPase activity obo:GO_1903333 down-regulation of co-chaperone activity obo:GO_1903333 down-regulation of co-chaperonin activity obo:GO_1903333 down-regulation of glycoprotein-specific chaperone activity obo:GO_1903333 down-regulation of non-chaperonin molecular chaperone ATPase activity obo:GO_1903333 down-regulation of protein complex assembly, multichaperone pathway obo:GO_1903333 downregulation of chaperone activity obo:GO_1903333 downregulation of chaperonin ATPase activity obo:GO_1903333 downregulation of co-chaperone activity obo:GO_1903333 downregulation of co-chaperonin activity obo:GO_1903333 downregulation of glycoprotein-specific chaperone activity obo:GO_1903333 downregulation of non-chaperonin molecular chaperone ATPase activity obo:GO_1903333 downregulation of protein complex assembly, multichaperone pathway obo:GO_1903333 inhibition of chaperone activity obo:GO_1903333 inhibition of chaperonin ATPase activity obo:GO_1903333 inhibition of co-chaperone activity obo:GO_1903333 inhibition of co-chaperonin activity obo:GO_1903333 inhibition of glycoprotein-specific chaperone activity obo:GO_1903333 inhibition of non-chaperonin molecular chaperone ATPase activity obo:GO_1903333 inhibition of protein complex assembly, multichaperone pathway obo:GO_1903333 negative regulation of chaperone activity obo:GO_1903333 negative regulation of chaperonin ATPase activity obo:GO_1903333 negative regulation of co-chaperone activity obo:GO_1903333 negative regulation of co-chaperonin activity obo:GO_1903333 negative regulation of glycoprotein-specific chaperone activity obo:GO_1903333 negative regulation of non-chaperonin molecular chaperone ATPase activity obo:GO_1903333 negative regulation of protein complex assembly, multichaperone pathway obo:GO_1903333 GO:1903333 obo:GO_1903333 negative regulation of protein folding obo:GO_1903334 Any process that activates or increases the frequency, rate or extent of protein folding. obo:GO_1903334 obo:go.owl obo:GO_1903334 vw obo:GO_1903334 2014-08-18T13:14:50Z obo:GO_1903334 up regulation of protein folding obo:GO_1903334 up-regulation of protein folding obo:GO_1903334 upregulation of protein folding obo:GO_1903334 activation of alpha-tubulin folding obo:GO_1903334 activation of beta-tubulin folding obo:GO_1903334 activation of chaperonin-mediated tubulin folding obo:GO_1903334 activation of protein folding obo:GO_1903334 positive regulation of alpha-tubulin folding obo:GO_1903334 positive regulation of beta-tubulin folding obo:GO_1903334 positive regulation of chaperonin-mediated tubulin folding obo:GO_1903334 up regulation of alpha-tubulin folding obo:GO_1903334 up regulation of beta-tubulin folding obo:GO_1903334 up regulation of chaperonin-mediated tubulin folding obo:GO_1903334 up-regulation of alpha-tubulin folding obo:GO_1903334 up-regulation of beta-tubulin folding obo:GO_1903334 up-regulation of chaperonin-mediated tubulin folding obo:GO_1903334 upregulation of alpha-tubulin folding obo:GO_1903334 upregulation of beta-tubulin folding obo:GO_1903334 upregulation of chaperonin-mediated tubulin folding obo:GO_1903334 biological_process obo:GO_1903334 activation of chaperone activity obo:GO_1903334 activation of chaperonin ATPase activity obo:GO_1903334 activation of co-chaperone activity obo:GO_1903334 activation of co-chaperonin activity obo:GO_1903334 activation of glycoprotein-specific chaperone activity obo:GO_1903334 activation of non-chaperonin molecular chaperone ATPase activity obo:GO_1903334 activation of protein complex assembly, multichaperone pathway obo:GO_1903334 positive regulation of chaperone activity obo:GO_1903334 positive regulation of chaperonin ATPase activity obo:GO_1903334 positive regulation of co-chaperone activity obo:GO_1903334 positive regulation of co-chaperonin activity obo:GO_1903334 positive regulation of glycoprotein-specific chaperone activity obo:GO_1903334 positive regulation of non-chaperonin molecular chaperone ATPase activity obo:GO_1903334 positive regulation of protein complex assembly, multichaperone pathway obo:GO_1903334 up regulation of chaperone activity obo:GO_1903334 up regulation of chaperonin ATPase activity obo:GO_1903334 up regulation of co-chaperone activity obo:GO_1903334 up regulation of co-chaperonin activity obo:GO_1903334 up regulation of glycoprotein-specific chaperone activity obo:GO_1903334 up regulation of non-chaperonin molecular chaperone ATPase activity obo:GO_1903334 up regulation of protein complex assembly, multichaperone pathway obo:GO_1903334 up-regulation of chaperone activity obo:GO_1903334 up-regulation of chaperonin ATPase activity obo:GO_1903334 up-regulation of co-chaperone activity obo:GO_1903334 up-regulation of co-chaperonin activity obo:GO_1903334 up-regulation of glycoprotein-specific chaperone activity obo:GO_1903334 up-regulation of non-chaperonin molecular chaperone ATPase activity obo:GO_1903334 up-regulation of protein complex assembly, multichaperone pathway obo:GO_1903334 upregulation of chaperone activity obo:GO_1903334 upregulation of chaperonin ATPase activity obo:GO_1903334 upregulation of co-chaperone activity obo:GO_1903334 upregulation of co-chaperonin activity obo:GO_1903334 upregulation of glycoprotein-specific chaperone activity obo:GO_1903334 upregulation of non-chaperonin molecular chaperone ATPase activity obo:GO_1903334 upregulation of protein complex assembly, multichaperone pathway obo:GO_1903334 GO:1903334 obo:GO_1903334 positive regulation of protein folding obo:GO_1903338 Any process that modulates the frequency, rate or extent of cell wall organization or biogenesis. obo:GO_1903338 obo:go.owl obo:GO_1903338 vw obo:GO_1903338 2014-08-18T13:20:50Z obo:GO_1903338 regulation of cell wall organisation or biogenesis obo:GO_1903338 regulation of cell wall organization or biogenesis at cellular level obo:GO_1903338 regulation of cellular cell wall organisation or biogenesis obo:GO_1903338 regulation of cellular cell wall organization or biogenesis obo:GO_1903338 biological_process obo:GO_1903338 GO:1903338 obo:GO_1903338 regulation of cell wall organization or biogenesis obo:GO_1903339 Any process that stops, prevents or reduces the frequency, rate or extent of cell wall organization or biogenesis. obo:GO_1903339 obo:go.owl obo:GO_1903339 vw obo:GO_1903339 2014-08-18T13:20:58Z obo:GO_1903339 down regulation of cell wall organisation or biogenesis obo:GO_1903339 down regulation of cell wall organization or biogenesis obo:GO_1903339 down regulation of cell wall organization or biogenesis at cellular level obo:GO_1903339 down regulation of cellular cell wall organisation or biogenesis obo:GO_1903339 down regulation of cellular cell wall organization or biogenesis obo:GO_1903339 down-regulation of cell wall organisation or biogenesis obo:GO_1903339 down-regulation of cell wall organization or biogenesis obo:GO_1903339 down-regulation of cell wall organization or biogenesis at cellular level obo:GO_1903339 down-regulation of cellular cell wall organisation or biogenesis obo:GO_1903339 down-regulation of cellular cell wall organization or biogenesis obo:GO_1903339 downregulation of cell wall organisation or biogenesis obo:GO_1903339 downregulation of cell wall organization or biogenesis obo:GO_1903339 downregulation of cell wall organization or biogenesis at cellular level obo:GO_1903339 downregulation of cellular cell wall organisation or biogenesis obo:GO_1903339 downregulation of cellular cell wall organization or biogenesis obo:GO_1903339 negative regulation of cell wall organisation or biogenesis obo:GO_1903339 negative regulation of cell wall organization or biogenesis at cellular level obo:GO_1903339 negative regulation of cellular cell wall organisation or biogenesis obo:GO_1903339 negative regulation of cellular cell wall organization or biogenesis obo:GO_1903339 inhibition of cell wall organisation or biogenesis obo:GO_1903339 inhibition of cell wall organization or biogenesis obo:GO_1903339 inhibition of cell wall organization or biogenesis at cellular level obo:GO_1903339 inhibition of cellular cell wall organisation or biogenesis obo:GO_1903339 inhibition of cellular cell wall organization or biogenesis obo:GO_1903339 biological_process obo:GO_1903339 GO:1903339 obo:GO_1903339 negative regulation of cell wall organization or biogenesis obo:GO_1903340 Any process that activates or increases the frequency, rate or extent of cell wall organization or biogenesis. obo:GO_1903340 obo:go.owl obo:GO_1903340 vw obo:GO_1903340 2014-08-18T13:21:06Z obo:GO_1903340 positive regulation of cell wall organisation or biogenesis obo:GO_1903340 positive regulation of cell wall organization or biogenesis at cellular level obo:GO_1903340 positive regulation of cellular cell wall organisation or biogenesis obo:GO_1903340 positive regulation of cellular cell wall organization or biogenesis obo:GO_1903340 up regulation of cell wall organisation or biogenesis obo:GO_1903340 up regulation of cell wall organization or biogenesis obo:GO_1903340 up regulation of cell wall organization or biogenesis at cellular level obo:GO_1903340 up regulation of cellular cell wall organisation or biogenesis obo:GO_1903340 up regulation of cellular cell wall organization or biogenesis obo:GO_1903340 up-regulation of cell wall organisation or biogenesis obo:GO_1903340 up-regulation of cell wall organization or biogenesis obo:GO_1903340 up-regulation of cell wall organization or biogenesis at cellular level obo:GO_1903340 up-regulation of cellular cell wall organisation or biogenesis obo:GO_1903340 up-regulation of cellular cell wall organization or biogenesis obo:GO_1903340 upregulation of cell wall organisation or biogenesis obo:GO_1903340 upregulation of cell wall organization or biogenesis obo:GO_1903340 upregulation of cell wall organization or biogenesis at cellular level obo:GO_1903340 upregulation of cellular cell wall organisation or biogenesis obo:GO_1903340 upregulation of cellular cell wall organization or biogenesis obo:GO_1903340 activation of cell wall organisation or biogenesis obo:GO_1903340 activation of cell wall organization or biogenesis obo:GO_1903340 activation of cell wall organization or biogenesis at cellular level obo:GO_1903340 activation of cellular cell wall organisation or biogenesis obo:GO_1903340 activation of cellular cell wall organization or biogenesis obo:GO_1903340 biological_process obo:GO_1903340 GO:1903340 obo:GO_1903340 positive regulation of cell wall organization or biogenesis obo:GO_1903385 Any process that modulates the frequency, rate or extent of homophilic cell adhesion. obo:GO_1903385 obo:go.owl obo:GO_1903385 als obo:GO_1903385 2014-08-27T09:57:30Z obo:GO_1903385 biological_process obo:GO_1903385 GO:1903385 obo:GO_1903385 regulation of homophilic cell adhesion obo:GO_1903386 Any process that stops, prevents or reduces the frequency, rate or extent of homophilic cell adhesion. obo:GO_1903386 obo:go.owl obo:GO_1903386 als obo:GO_1903386 2014-08-27T09:57:38Z obo:GO_1903386 down regulation of homophilic cell adhesion obo:GO_1903386 down-regulation of homophilic cell adhesion obo:GO_1903386 downregulation of homophilic cell adhesion obo:GO_1903386 inhibition of homophilic cell adhesion obo:GO_1903386 biological_process obo:GO_1903386 GO:1903386 obo:GO_1903386 negative regulation of homophilic cell adhesion obo:GO_1903387 Any process that activates or increases the frequency, rate or extent of homophilic cell adhesion. obo:GO_1903387 obo:go.owl obo:GO_1903387 als obo:GO_1903387 2014-08-27T09:57:46Z obo:GO_1903387 up regulation of homophilic cell adhesion obo:GO_1903387 up-regulation of homophilic cell adhesion obo:GO_1903387 upregulation of homophilic cell adhesion obo:GO_1903387 activation of homophilic cell adhesion obo:GO_1903387 biological_process obo:GO_1903387 GO:1903387 obo:GO_1903387 positive regulation of homophilic cell adhesion obo:GO_1903406 Any process that modulates the frequency, rate or extent of sodium:potassium-exchanging ATPase activity. obo:GO_1903406 obo:go.owl obo:GO_1903406 mr obo:GO_1903406 2014-09-02T19:45:08Z obo:GO_1903406 regulation of sodium pump obo:GO_1903406 regulation of (Na+ + K+)-ATPase activity obo:GO_1903406 regulation of (Na+ + K+)-activated ATPase activity obo:GO_1903406 regulation of ATP phosphohydrolase (Na+/K+-exchanging) obo:GO_1903406 regulation of Na(+)/K(+)-ATPase activity obo:GO_1903406 regulation of Na(+)/K(+)-exchanging ATPase activity obo:GO_1903406 regulation of Na+,K+-ATPase activity obo:GO_1903406 regulation of Na+/K+-ATPase activity obo:GO_1903406 regulation of Na+/K+-exchanging ATPase activity obo:GO_1903406 regulation of Na,K-activated ATPase activity obo:GO_1903406 regulation of sodium/potassium-exchanging ATPase activity obo:GO_1903406 regulation of sodium/potassium-transporting ATPase activity obo:GO_1903406 regulation of sodium:potassium exchanging ATPase activity obo:GO_1903406 biological_process obo:GO_1903406 regulation of Na+,K+ pump obo:GO_1903406 regulation of Na,K-pump obo:GO_1903406 GO:1903406 obo:GO_1903406 regulation of sodium:potassium-exchanging ATPase activity obo:GO_1903407 Any process that stops, prevents or reduces the frequency, rate or extent of sodium:potassium-exchanging ATPase activity. obo:GO_1903407 obo:go.owl obo:GO_1903407 mr obo:GO_1903407 2014-09-02T19:45:16Z obo:GO_1903407 down regulation of (Na+ + K+)-ATPase activity obo:GO_1903407 down regulation of (Na+ + K+)-activated ATPase activity obo:GO_1903407 down regulation of ATP phosphohydrolase (Na+/K+-exchanging) obo:GO_1903407 down regulation of Na(+)/K(+)-ATPase activity obo:GO_1903407 down regulation of Na(+)/K(+)-exchanging ATPase activity obo:GO_1903407 down regulation of Na+,K+-ATPase activity obo:GO_1903407 down regulation of Na+/K+-ATPase activity obo:GO_1903407 down regulation of Na+/K+-exchanging ATPase activity obo:GO_1903407 down regulation of Na,K-activated ATPase activity obo:GO_1903407 down regulation of sodium/potassium-exchanging ATPase activity obo:GO_1903407 down regulation of sodium/potassium-transporting ATPase activity obo:GO_1903407 down regulation of sodium:potassium exchanging ATPase activity obo:GO_1903407 down regulation of sodium:potassium-exchanging ATPase activity obo:GO_1903407 down-regulation of (Na+ + K+)-ATPase activity obo:GO_1903407 down-regulation of (Na+ + K+)-activated ATPase activity obo:GO_1903407 down-regulation of ATP phosphohydrolase (Na+/K+-exchanging) obo:GO_1903407 down-regulation of Na(+)/K(+)-ATPase activity obo:GO_1903407 down-regulation of Na(+)/K(+)-exchanging ATPase activity obo:GO_1903407 down-regulation of Na+,K+-ATPase activity obo:GO_1903407 down-regulation of Na+/K+-ATPase activity obo:GO_1903407 down-regulation of Na+/K+-exchanging ATPase activity obo:GO_1903407 down-regulation of Na,K-activated ATPase activity obo:GO_1903407 down-regulation of sodium/potassium-exchanging ATPase activity obo:GO_1903407 down-regulation of sodium/potassium-transporting ATPase activity obo:GO_1903407 down-regulation of sodium:potassium exchanging ATPase activity obo:GO_1903407 down-regulation of sodium:potassium-exchanging ATPase activity obo:GO_1903407 downregulation of (Na+ + K+)-ATPase activity obo:GO_1903407 downregulation of (Na+ + K+)-activated ATPase activity obo:GO_1903407 downregulation of ATP phosphohydrolase (Na+/K+-exchanging) obo:GO_1903407 downregulation of Na(+)/K(+)-ATPase activity obo:GO_1903407 downregulation of Na(+)/K(+)-exchanging ATPase activity obo:GO_1903407 downregulation of Na+,K+-ATPase activity obo:GO_1903407 downregulation of Na+/K+-ATPase activity obo:GO_1903407 downregulation of Na+/K+-exchanging ATPase activity obo:GO_1903407 downregulation of Na,K-activated ATPase activity obo:GO_1903407 downregulation of sodium/potassium-exchanging ATPase activity obo:GO_1903407 downregulation of sodium/potassium-transporting ATPase activity obo:GO_1903407 downregulation of sodium:potassium exchanging ATPase activity obo:GO_1903407 downregulation of sodium:potassium-exchanging ATPase activity obo:GO_1903407 negative regulation of (Na+ + K+)-ATPase activity obo:GO_1903407 negative regulation of (Na+ + K+)-activated ATPase activity obo:GO_1903407 negative regulation of ATP phosphohydrolase (Na+/K+-exchanging) obo:GO_1903407 negative regulation of Na(+)/K(+)-ATPase activity obo:GO_1903407 negative regulation of Na(+)/K(+)-exchanging ATPase activity obo:GO_1903407 negative regulation of Na+,K+-ATPase activity obo:GO_1903407 negative regulation of Na+/K+-ATPase activity obo:GO_1903407 negative regulation of Na+/K+-exchanging ATPase activity obo:GO_1903407 negative regulation of Na,K-activated ATPase activity obo:GO_1903407 negative regulation of sodium/potassium-exchanging ATPase activity obo:GO_1903407 negative regulation of sodium/potassium-transporting ATPase activity obo:GO_1903407 negative regulation of sodium:potassium exchanging ATPase activity obo:GO_1903407 inhibition of (Na+ + K+)-ATPase activity obo:GO_1903407 inhibition of (Na+ + K+)-activated ATPase activity obo:GO_1903407 inhibition of ATP phosphohydrolase (Na+/K+-exchanging) obo:GO_1903407 inhibition of Na(+)/K(+)-ATPase activity obo:GO_1903407 inhibition of Na(+)/K(+)-exchanging ATPase activity obo:GO_1903407 inhibition of Na+,K+-ATPase activity obo:GO_1903407 inhibition of Na+/K+-ATPase activity obo:GO_1903407 inhibition of Na+/K+-exchanging ATPase activity obo:GO_1903407 inhibition of Na,K-activated ATPase activity obo:GO_1903407 inhibition of sodium/potassium-exchanging ATPase activity obo:GO_1903407 inhibition of sodium/potassium-transporting ATPase activity obo:GO_1903407 inhibition of sodium:potassium exchanging ATPase activity obo:GO_1903407 inhibition of sodium:potassium-exchanging ATPase activity obo:GO_1903407 biological_process obo:GO_1903407 down regulation of Na+,K+ pump obo:GO_1903407 down regulation of Na,K-pump obo:GO_1903407 down-regulation of Na+,K+ pump obo:GO_1903407 down-regulation of Na,K-pump obo:GO_1903407 downregulation of Na+,K+ pump obo:GO_1903407 downregulation of Na,K-pump obo:GO_1903407 inhibition of Na+,K+ pump obo:GO_1903407 inhibition of Na,K-pump obo:GO_1903407 negative regulation of Na+,K+ pump obo:GO_1903407 negative regulation of Na,K-pump obo:GO_1903407 GO:1903407 obo:GO_1903407 negative regulation of sodium:potassium-exchanging ATPase activity obo:GO_1903408 Any process that activates or increases the frequency, rate or extent of sodium:potassium-exchanging ATPase activity. obo:GO_1903408 obo:go.owl obo:GO_1903408 mr obo:GO_1903408 2014-09-02T19:45:24Z obo:GO_1903408 positive regulation of (Na+ + K+)-ATPase activity obo:GO_1903408 positive regulation of (Na+ + K+)-activated ATPase activity obo:GO_1903408 positive regulation of ATP phosphohydrolase (Na+/K+-exchanging) obo:GO_1903408 positive regulation of Na(+)/K(+)-ATPase activity obo:GO_1903408 positive regulation of Na(+)/K(+)-exchanging ATPase activity obo:GO_1903408 positive regulation of Na+,K+-ATPase activity obo:GO_1903408 positive regulation of Na+/K+-ATPase activity obo:GO_1903408 positive regulation of Na+/K+-exchanging ATPase activity obo:GO_1903408 positive regulation of Na,K-activated ATPase activity obo:GO_1903408 positive regulation of sodium/potassium-exchanging ATPase activity obo:GO_1903408 positive regulation of sodium/potassium-transporting ATPase activity obo:GO_1903408 positive regulation of sodium:potassium exchanging ATPase activity obo:GO_1903408 up regulation of (Na+ + K+)-ATPase activity obo:GO_1903408 up regulation of (Na+ + K+)-activated ATPase activity obo:GO_1903408 up regulation of ATP phosphohydrolase (Na+/K+-exchanging) obo:GO_1903408 up regulation of Na(+)/K(+)-ATPase activity obo:GO_1903408 up regulation of Na(+)/K(+)-exchanging ATPase activity obo:GO_1903408 up regulation of Na+,K+-ATPase activity obo:GO_1903408 up regulation of Na+/K+-ATPase activity obo:GO_1903408 up regulation of Na+/K+-exchanging ATPase activity obo:GO_1903408 up regulation of Na,K-activated ATPase activity obo:GO_1903408 up regulation of sodium/potassium-exchanging ATPase activity obo:GO_1903408 up regulation of sodium/potassium-transporting ATPase activity obo:GO_1903408 up regulation of sodium:potassium exchanging ATPase activity obo:GO_1903408 up regulation of sodium:potassium-exchanging ATPase activity obo:GO_1903408 up-regulation of (Na+ + K+)-ATPase activity obo:GO_1903408 up-regulation of (Na+ + K+)-activated ATPase activity obo:GO_1903408 up-regulation of ATP phosphohydrolase (Na+/K+-exchanging) obo:GO_1903408 up-regulation of Na(+)/K(+)-ATPase activity obo:GO_1903408 up-regulation of Na(+)/K(+)-exchanging ATPase activity obo:GO_1903408 up-regulation of Na+,K+-ATPase activity obo:GO_1903408 up-regulation of Na+/K+-ATPase activity obo:GO_1903408 up-regulation of Na+/K+-exchanging ATPase activity obo:GO_1903408 up-regulation of Na,K-activated ATPase activity obo:GO_1903408 up-regulation of sodium/potassium-exchanging ATPase activity obo:GO_1903408 up-regulation of sodium/potassium-transporting ATPase activity obo:GO_1903408 up-regulation of sodium:potassium exchanging ATPase activity obo:GO_1903408 up-regulation of sodium:potassium-exchanging ATPase activity obo:GO_1903408 upregulation of (Na+ + K+)-ATPase activity obo:GO_1903408 upregulation of (Na+ + K+)-activated ATPase activity obo:GO_1903408 upregulation of ATP phosphohydrolase (Na+/K+-exchanging) obo:GO_1903408 upregulation of Na(+)/K(+)-ATPase activity obo:GO_1903408 upregulation of Na(+)/K(+)-exchanging ATPase activity obo:GO_1903408 upregulation of Na+,K+-ATPase activity obo:GO_1903408 upregulation of Na+/K+-ATPase activity obo:GO_1903408 upregulation of Na+/K+-exchanging ATPase activity obo:GO_1903408 upregulation of Na,K-activated ATPase activity obo:GO_1903408 upregulation of sodium/potassium-exchanging ATPase activity obo:GO_1903408 upregulation of sodium/potassium-transporting ATPase activity obo:GO_1903408 upregulation of sodium:potassium exchanging ATPase activity obo:GO_1903408 upregulation of sodium:potassium-exchanging ATPase activity obo:GO_1903408 activation of (Na+ + K+)-ATPase activity obo:GO_1903408 activation of (Na+ + K+)-activated ATPase activity obo:GO_1903408 activation of ATP phosphohydrolase (Na+/K+-exchanging) obo:GO_1903408 activation of Na(+)/K(+)-ATPase activity obo:GO_1903408 activation of Na(+)/K(+)-exchanging ATPase activity obo:GO_1903408 activation of Na+,K+-ATPase activity obo:GO_1903408 activation of Na+/K+-ATPase activity obo:GO_1903408 activation of Na+/K+-exchanging ATPase activity obo:GO_1903408 activation of Na,K-activated ATPase activity obo:GO_1903408 activation of sodium/potassium-exchanging ATPase activity obo:GO_1903408 activation of sodium/potassium-transporting ATPase activity obo:GO_1903408 activation of sodium:potassium exchanging ATPase activity obo:GO_1903408 activation of sodium:potassium-exchanging ATPase activity obo:GO_1903408 biological_process obo:GO_1903408 activation of Na+,K+ pump obo:GO_1903408 activation of Na,K-pump obo:GO_1903408 positive regulation of Na+,K+ pump obo:GO_1903408 positive regulation of Na,K-pump obo:GO_1903408 up regulation of Na+,K+ pump obo:GO_1903408 up regulation of Na,K-pump obo:GO_1903408 up-regulation of Na+,K+ pump obo:GO_1903408 up-regulation of Na,K-pump obo:GO_1903408 upregulation of Na+,K+ pump obo:GO_1903408 upregulation of Na,K-pump obo:GO_1903408 GO:1903408 obo:GO_1903408 positive regulation of sodium:potassium-exchanging ATPase activity obo:GO_1903515 The directed movement of calcium ion from cytosol to endoplasmic reticulum. obo:GO_1903515 obo:go.owl obo:GO_1903515 rl obo:GO_1903515 2014-10-02T14:51:20Z obo:GO_1903515 biological_process obo:GO_1903515 GO:1903515 obo:GO_1903515 calcium ion transport from cytosol to endoplasmic reticulum obo:GO_1903564 Any process that modulates the frequency, rate or extent of protein localization to cilium. obo:GO_1903564 obo:go.owl obo:GO_1903564 krc obo:GO_1903564 2014-10-24T20:58:11Z obo:GO_1903564 biological_process obo:GO_1903564 GO:1903564 obo:GO_1903564 regulation of protein localization to cilium obo:GO_1903565 Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to cilium. obo:GO_1903565 obo:go.owl obo:GO_1903565 krc obo:GO_1903565 2014-10-24T20:58:20Z obo:GO_1903565 down regulation of protein localization to cilium obo:GO_1903565 down-regulation of protein localization to cilium obo:GO_1903565 downregulation of protein localization to cilium obo:GO_1903565 inhibition of protein localization to cilium obo:GO_1903565 biological_process obo:GO_1903565 GO:1903565 obo:GO_1903565 negative regulation of protein localization to cilium obo:GO_1903566 Any process that activates or increases the frequency, rate or extent of protein localization to cilium. obo:GO_1903566 obo:go.owl obo:GO_1903566 krc obo:GO_1903566 2014-10-24T20:58:28Z obo:GO_1903566 up regulation of protein localization to cilium obo:GO_1903566 up-regulation of protein localization to cilium obo:GO_1903566 upregulation of protein localization to cilium obo:GO_1903566 activation of protein localization to cilium obo:GO_1903566 biological_process obo:GO_1903566 GO:1903566 obo:GO_1903566 positive regulation of protein localization to cilium obo:GO_1903567 Any process that modulates the frequency, rate or extent of protein localization to ciliary membrane. obo:GO_1903567 obo:go.owl obo:GO_1903567 krc obo:GO_1903567 2014-10-24T21:32:51Z obo:GO_1903567 regulation of protein localisation in ciliary membrane obo:GO_1903567 regulation of protein localisation to ciliary membrane obo:GO_1903567 regulation of protein localization in ciliary membrane obo:GO_1903567 biological_process obo:GO_1903567 GO:1903567 obo:GO_1903567 regulation of protein localization to ciliary membrane obo:GO_1903568 Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to ciliary membrane. obo:GO_1903568 obo:go.owl obo:GO_1903568 krc obo:GO_1903568 2014-10-24T21:32:59Z obo:GO_1903568 down regulation of protein localisation in ciliary membrane obo:GO_1903568 down regulation of protein localisation to ciliary membrane obo:GO_1903568 down regulation of protein localization in ciliary membrane obo:GO_1903568 down regulation of protein localization to ciliary membrane obo:GO_1903568 down-regulation of protein localisation in ciliary membrane obo:GO_1903568 down-regulation of protein localisation to ciliary membrane obo:GO_1903568 down-regulation of protein localization in ciliary membrane obo:GO_1903568 down-regulation of protein localization to ciliary membrane obo:GO_1903568 downregulation of protein localisation in ciliary membrane obo:GO_1903568 downregulation of protein localisation to ciliary membrane obo:GO_1903568 downregulation of protein localization in ciliary membrane obo:GO_1903568 downregulation of protein localization to ciliary membrane obo:GO_1903568 negative regulation of protein localisation in ciliary membrane obo:GO_1903568 negative regulation of protein localisation to ciliary membrane obo:GO_1903568 negative regulation of protein localization in ciliary membrane obo:GO_1903568 inhibition of protein localisation in ciliary membrane obo:GO_1903568 inhibition of protein localisation to ciliary membrane obo:GO_1903568 inhibition of protein localization in ciliary membrane obo:GO_1903568 inhibition of protein localization to ciliary membrane obo:GO_1903568 biological_process obo:GO_1903568 GO:1903568 obo:GO_1903568 negative regulation of protein localization to ciliary membrane obo:GO_1903569 Any process that activates or increases the frequency, rate or extent of protein localization to ciliary membrane. obo:GO_1903569 obo:go.owl obo:GO_1903569 krc obo:GO_1903569 2014-10-24T21:33:08Z obo:GO_1903569 positive regulation of protein localisation in ciliary membrane obo:GO_1903569 positive regulation of protein localisation to ciliary membrane obo:GO_1903569 positive regulation of protein localization in ciliary membrane obo:GO_1903569 up regulation of protein localisation in ciliary membrane obo:GO_1903569 up regulation of protein localisation to ciliary membrane obo:GO_1903569 up regulation of protein localization in ciliary membrane obo:GO_1903569 up regulation of protein localization to ciliary membrane obo:GO_1903569 up-regulation of protein localisation in ciliary membrane obo:GO_1903569 up-regulation of protein localisation to ciliary membrane obo:GO_1903569 up-regulation of protein localization in ciliary membrane obo:GO_1903569 up-regulation of protein localization to ciliary membrane obo:GO_1903569 upregulation of protein localisation in ciliary membrane obo:GO_1903569 upregulation of protein localisation to ciliary membrane obo:GO_1903569 upregulation of protein localization in ciliary membrane obo:GO_1903569 upregulation of protein localization to ciliary membrane obo:GO_1903569 activation of protein localisation in ciliary membrane obo:GO_1903569 activation of protein localisation to ciliary membrane obo:GO_1903569 activation of protein localization in ciliary membrane obo:GO_1903569 activation of protein localization to ciliary membrane obo:GO_1903569 biological_process obo:GO_1903569 GO:1903569 obo:GO_1903569 positive regulation of protein localization to ciliary membrane obo:GO_1903609 Any process that stops, prevents or reduces the frequency, rate or extent of inward rectifier potassium channel activity. obo:GO_1903609 obo:go.owl obo:GO_1903609 rl obo:GO_1903609 2014-11-14T20:29:14Z obo:GO_1903609 down regulation of Kir channel activity obo:GO_1903609 down regulation of inward rectifier potassium channel activity obo:GO_1903609 down-regulation of Kir channel activity obo:GO_1903609 down-regulation of inward rectifier potassium channel activity obo:GO_1903609 downregulation of Kir channel activity obo:GO_1903609 downregulation of inward rectifier potassium channel activity obo:GO_1903609 negative regulation of Kir channel activity obo:GO_1903609 inhibition of Kir channel activity obo:GO_1903609 inhibition of inward rectifier potassium channel activity obo:GO_1903609 biological_process obo:GO_1903609 GO:1903609 obo:GO_1903609 negative regulation of inward rectifier potassium channel activity obo:GO_1903644 Any process that modulates the frequency, rate or extent of chaperone-mediated protein folding. obo:GO_1903644 obo:go.owl obo:GO_1903644 pga obo:GO_1903644 2014-11-21T15:25:27Z obo:GO_1903644 biological_process obo:GO_1903644 GO:1903644 obo:GO_1903644 regulation of chaperone-mediated protein folding obo:GO_1903645 Any process that stops, prevents or reduces the frequency, rate or extent of chaperone-mediated protein folding. obo:GO_1903645 obo:go.owl obo:GO_1903645 pga obo:GO_1903645 2014-11-21T15:25:35Z obo:GO_1903645 down regulation of chaperone-mediated protein folding obo:GO_1903645 down-regulation of chaperone-mediated protein folding obo:GO_1903645 downregulation of chaperone-mediated protein folding obo:GO_1903645 inhibition of chaperone-mediated protein folding obo:GO_1903645 biological_process obo:GO_1903645 GO:1903645 obo:GO_1903645 negative regulation of chaperone-mediated protein folding obo:GO_1903646 Any process that activates or increases the frequency, rate or extent of chaperone-mediated protein folding. obo:GO_1903646 obo:go.owl obo:GO_1903646 pga obo:GO_1903646 2014-11-21T15:25:44Z obo:GO_1903646 up regulation of chaperone-mediated protein folding obo:GO_1903646 up-regulation of chaperone-mediated protein folding obo:GO_1903646 upregulation of chaperone-mediated protein folding obo:GO_1903646 activation of chaperone-mediated protein folding obo:GO_1903646 biological_process obo:GO_1903646 GO:1903646 obo:GO_1903646 positive regulation of chaperone-mediated protein folding obo:GO_1903649 Any process that modulates the frequency, rate or extent of cytoplasmic transport. obo:GO_1903649 obo:go.owl obo:GO_1903649 jl obo:GO_1903649 2014-11-24T13:38:17Z obo:GO_1903649 regulation of cytoplasmic streaming obo:GO_1903649 biological_process obo:GO_1903649 GO:1903649 obo:GO_1903649 regulation of cytoplasmic transport obo:GO_1903650 Any process that stops, prevents or reduces the frequency, rate or extent of cytoplasmic transport. obo:GO_1903650 obo:go.owl obo:GO_1903650 jl obo:GO_1903650 2014-11-24T13:38:26Z obo:GO_1903650 down regulation of cytoplasmic transport obo:GO_1903650 down-regulation of cytoplasmic transport obo:GO_1903650 downregulation of cytoplasmic transport obo:GO_1903650 down regulation of cytoplasmic streaming obo:GO_1903650 down-regulation of cytoplasmic streaming obo:GO_1903650 downregulation of cytoplasmic streaming obo:GO_1903650 inhibition of cytoplasmic streaming obo:GO_1903650 inhibition of cytoplasmic transport obo:GO_1903650 negative regulation of cytoplasmic streaming obo:GO_1903650 biological_process obo:GO_1903650 GO:1903650 obo:GO_1903650 negative regulation of cytoplasmic transport obo:GO_1903651 Any process that activates or increases the frequency, rate or extent of cytoplasmic transport. obo:GO_1903651 obo:go.owl obo:GO_1903651 jl obo:GO_1903651 2014-11-24T13:38:34Z obo:GO_1903651 up regulation of cytoplasmic transport obo:GO_1903651 up-regulation of cytoplasmic transport obo:GO_1903651 upregulation of cytoplasmic transport obo:GO_1903651 activation of cytoplasmic streaming obo:GO_1903651 activation of cytoplasmic transport obo:GO_1903651 positive regulation of cytoplasmic streaming obo:GO_1903651 up regulation of cytoplasmic streaming obo:GO_1903651 up-regulation of cytoplasmic streaming obo:GO_1903651 upregulation of cytoplasmic streaming obo:GO_1903651 biological_process obo:GO_1903651 GO:1903651 obo:GO_1903651 positive regulation of cytoplasmic transport obo:GO_1903747 Any process that modulates the frequency, rate or extent of establishment of protein localization to mitochondrion. obo:GO_1903747 obo:go.owl obo:GO_1903747 krc obo:GO_1903747 2014-12-12T22:18:09Z obo:GO_1903747 regulation of establishment of protein localisation to mitochondrion obo:GO_1903747 regulation of establishment of protein localization in mitochondrion obo:GO_1903747 biological_process obo:GO_1903747 GO:1903747 obo:GO_1903747 regulation of establishment of protein localization to mitochondrion obo:GO_1903748 Any process that stops, prevents or reduces the frequency, rate or extent of establishment of protein localization to mitochondrion. obo:GO_1903748 obo:go.owl obo:GO_1903748 krc obo:GO_1903748 2014-12-12T22:18:18Z obo:GO_1903748 down regulation of establishment of protein localisation to mitochondrion obo:GO_1903748 down regulation of establishment of protein localization in mitochondrion obo:GO_1903748 down regulation of establishment of protein localization to mitochondrion obo:GO_1903748 down-regulation of establishment of protein localisation to mitochondrion obo:GO_1903748 down-regulation of establishment of protein localization in mitochondrion obo:GO_1903748 down-regulation of establishment of protein localization to mitochondrion obo:GO_1903748 downregulation of establishment of protein localisation to mitochondrion obo:GO_1903748 downregulation of establishment of protein localization in mitochondrion obo:GO_1903748 downregulation of establishment of protein localization to mitochondrion obo:GO_1903748 negative regulation of establishment of protein localisation to mitochondrion obo:GO_1903748 negative regulation of establishment of protein localization in mitochondrion obo:GO_1903748 inhibition of establishment of protein localisation to mitochondrion obo:GO_1903748 inhibition of establishment of protein localization in mitochondrion obo:GO_1903748 inhibition of establishment of protein localization to mitochondrion obo:GO_1903748 biological_process obo:GO_1903748 GO:1903748 obo:GO_1903748 negative regulation of establishment of protein localization to mitochondrion obo:GO_1903749 Any process that activates or increases the frequency, rate or extent of establishment of protein localization to mitochondrion. obo:GO_1903749 obo:go.owl obo:GO_1903749 krc obo:GO_1903749 2014-12-12T22:18:26Z obo:GO_1903749 positive regulation of establishment of protein localisation to mitochondrion obo:GO_1903749 positive regulation of establishment of protein localization in mitochondrion obo:GO_1903749 up regulation of establishment of protein localisation to mitochondrion obo:GO_1903749 up regulation of establishment of protein localization in mitochondrion obo:GO_1903749 up regulation of establishment of protein localization to mitochondrion obo:GO_1903749 up-regulation of establishment of protein localisation to mitochondrion obo:GO_1903749 up-regulation of establishment of protein localization in mitochondrion obo:GO_1903749 up-regulation of establishment of protein localization to mitochondrion obo:GO_1903749 upregulation of establishment of protein localisation to mitochondrion obo:GO_1903749 upregulation of establishment of protein localization in mitochondrion obo:GO_1903749 upregulation of establishment of protein localization to mitochondrion obo:GO_1903749 activation of establishment of protein localisation to mitochondrion obo:GO_1903749 activation of establishment of protein localization in mitochondrion obo:GO_1903749 activation of establishment of protein localization to mitochondrion obo:GO_1903749 biological_process obo:GO_1903749 GO:1903749 obo:GO_1903749 positive regulation of establishment of protein localization to mitochondrion obo:GO_1903759 Any signal transduction that is involved in regulation of aerobic respiration. obo:GO_1903759 obo:go.owl obo:GO_1903759 al obo:GO_1903759 2014-12-18T16:37:50Z obo:GO_1903759 signaling cascade involved in regulation of aerobic respiration obo:GO_1903759 signalling cascade involved in regulation of aerobic respiration obo:GO_1903759 biological_process obo:GO_1903759 signaling pathway involved in regulation of aerobic respiration obo:GO_1903759 signalling pathway involved in regulation of aerobic respiration obo:GO_1903759 GO:1903759 obo:GO_1903759 signal transduction involved in regulation of aerobic respiration obo:GO_1903769 Any process that stops, prevents or reduces the frequency, rate or extent of cell proliferation in bone marrow. obo:GO_1903769 obo:go.owl obo:GO_1903769 sl obo:GO_1903769 2014-12-29T19:46:26Z obo:GO_1903769 down regulation of bone marrow cell proliferation obo:GO_1903769 down regulation of cell proliferation in bone marrow obo:GO_1903769 down-regulation of bone marrow cell proliferation obo:GO_1903769 down-regulation of cell proliferation in bone marrow obo:GO_1903769 downregulation of bone marrow cell proliferation obo:GO_1903769 downregulation of cell proliferation in bone marrow obo:GO_1903769 negative regulation of bone marrow cell proliferation obo:GO_1903769 inhibition of bone marrow cell proliferation obo:GO_1903769 inhibition of cell proliferation in bone marrow obo:GO_1903769 biological_process obo:GO_1903769 GO:1903769 obo:GO_1903769 negative regulation of cell proliferation in bone marrow obo:GO_1903777 Interacting selectively and non-covalently with melibiose. obo:GO_1903777 obo:go.owl obo:GO_1903777 mr obo:GO_1903777 2015-01-06T21:05:29Z obo:GO_1903777 molecular_function obo:GO_1903777 GO:1903777 obo:GO_1903777 melibiose binding obo:GO_1903782 Any process that modulates the frequency, rate or extent of sodium ion import across the plasma membrane. obo:GO_1903782 obo:go.owl obo:GO_1903782 nc obo:GO_1903782 2015-01-07T16:48:43Z obo:GO_1903782 biological_process obo:GO_1903782 GO:1903782 obo:GO_1903782 regulation of sodium ion import across plasma membrane obo:GO_1903783 Any process that stops, prevents or reduces the frequency, rate or extent of sodium ion import across the plasma membrane. obo:GO_1903783 obo:go.owl obo:GO_1903783 nc obo:GO_1903783 2015-01-07T16:48:51Z obo:GO_1903783 down regulation of sodium ion import across plasma membrane obo:GO_1903783 down-regulation of sodium ion import across plasma membrane obo:GO_1903783 downregulation of sodium ion import across plasma membrane obo:GO_1903783 inhibition of sodium ion import across plasma membrane obo:GO_1903783 biological_process obo:GO_1903783 GO:1903783 obo:GO_1903783 negative regulation of sodium ion import across plasma membrane obo:GO_1903784 Any process that activates or increases the frequency, rate or extent of sodium ion import across the plasma membrane. obo:GO_1903784 obo:go.owl obo:GO_1903784 nc obo:GO_1903784 2015-01-07T16:49:00Z obo:GO_1903784 up regulation of sodium ion import across plasma membrane obo:GO_1903784 up-regulation of sodium ion import across plasma membrane obo:GO_1903784 upregulation of sodium ion import across plasma membrane obo:GO_1903784 activation of sodium ion import across plasma membrane obo:GO_1903784 biological_process obo:GO_1903784 GO:1903784 obo:GO_1903784 positive regulation of sodium ion import across plasma membrane obo:GO_1903792 Any process that stops, prevents or reduces the frequency, rate or extent of anion transport. obo:GO_1903792 obo:go.owl obo:GO_1903792 sl obo:GO_1903792 2015-01-12T21:50:20Z obo:GO_1903792 down regulation of anion transport obo:GO_1903792 down-regulation of anion transport obo:GO_1903792 downregulation of anion transport obo:GO_1903792 inhibition of anion transport obo:GO_1903792 biological_process obo:GO_1903792 GO:1903792 obo:GO_1903792 negative regulation of anion transport obo:GO_1903793 Any process that activates or increases the frequency, rate or extent of anion transport. obo:GO_1903793 obo:go.owl obo:GO_1903793 sl obo:GO_1903793 2015-01-12T21:50:30Z obo:GO_1903793 up regulation of anion transport obo:GO_1903793 up-regulation of anion transport obo:GO_1903793 upregulation of anion transport obo:GO_1903793 activation of anion transport obo:GO_1903793 biological_process obo:GO_1903793 GO:1903793 obo:GO_1903793 positive regulation of anion transport obo:GO_1903794 Interacting selectively and non-covalently with cortisol. obo:GO_1903794 obo:go.owl obo:GO_1903794 mr obo:GO_1903794 2015-01-14T19:02:31Z obo:GO_1903794 molecular_function obo:GO_1903794 GO:1903794 obo:GO_1903794 cortisol binding obo:GO_1903795 Any process that modulates the frequency, rate or extent of inorganic anion transmembrane transport. obo:GO_1903795 obo:go.owl obo:GO_1903795 sl obo:GO_1903795 2015-01-14T21:44:49Z obo:GO_1903795 regulation of inorganic anion membrane transport obo:GO_1903795 regulation of transmembrane inorganic anion transport obo:GO_1903795 biological_process obo:GO_1903795 GO:1903795 obo:GO_1903795 regulation of inorganic anion transmembrane transport obo:GO_1903796 Any process that stops, prevents or reduces the frequency, rate or extent of inorganic anion transmembrane transport. obo:GO_1903796 obo:go.owl obo:GO_1903796 sl obo:GO_1903796 2015-01-14T21:44:59Z obo:GO_1903796 down regulation of inorganic anion membrane transport obo:GO_1903796 down regulation of inorganic anion transmembrane transport obo:GO_1903796 down regulation of transmembrane inorganic anion transport obo:GO_1903796 down-regulation of inorganic anion membrane transport obo:GO_1903796 down-regulation of inorganic anion transmembrane transport obo:GO_1903796 down-regulation of transmembrane inorganic anion transport obo:GO_1903796 downregulation of inorganic anion membrane transport obo:GO_1903796 downregulation of inorganic anion transmembrane transport obo:GO_1903796 downregulation of transmembrane inorganic anion transport obo:GO_1903796 negative regulation of inorganic anion membrane transport obo:GO_1903796 negative regulation of transmembrane inorganic anion transport obo:GO_1903796 inhibition of inorganic anion membrane transport obo:GO_1903796 inhibition of inorganic anion transmembrane transport obo:GO_1903796 inhibition of transmembrane inorganic anion transport obo:GO_1903796 biological_process obo:GO_1903796 GO:1903796 obo:GO_1903796 negative regulation of inorganic anion transmembrane transport obo:GO_1903797 Any process that activates or increases the frequency, rate or extent of inorganic anion transmembrane transport. obo:GO_1903797 obo:go.owl obo:GO_1903797 sl obo:GO_1903797 2015-01-14T21:45:08Z obo:GO_1903797 positive regulation of inorganic anion membrane transport obo:GO_1903797 positive regulation of transmembrane inorganic anion transport obo:GO_1903797 up regulation of inorganic anion membrane transport obo:GO_1903797 up regulation of inorganic anion transmembrane transport obo:GO_1903797 up regulation of transmembrane inorganic anion transport obo:GO_1903797 up-regulation of inorganic anion membrane transport obo:GO_1903797 up-regulation of inorganic anion transmembrane transport obo:GO_1903797 up-regulation of transmembrane inorganic anion transport obo:GO_1903797 upregulation of inorganic anion membrane transport obo:GO_1903797 upregulation of inorganic anion transmembrane transport obo:GO_1903797 upregulation of transmembrane inorganic anion transport obo:GO_1903797 activation of inorganic anion membrane transport obo:GO_1903797 activation of inorganic anion transmembrane transport obo:GO_1903797 activation of transmembrane inorganic anion transport obo:GO_1903797 biological_process obo:GO_1903797 GO:1903797 obo:GO_1903797 positive regulation of inorganic anion transmembrane transport obo:GO_1903817 Any process that stops, prevents or reduces the frequency, rate or extent of voltage-gated potassium channel activity. obo:GO_1903817 obo:go.owl obo:GO_1903817 sl obo:GO_1903817 2015-01-16T17:22:08Z obo:GO_1903817 down regulation of voltage gated potassium channel activity obo:GO_1903817 down regulation of voltage-dependent potassium channel activity obo:GO_1903817 down regulation of voltage-gated potassium channel activity obo:GO_1903817 down regulation of voltage-gated potassium ion channel activity obo:GO_1903817 down regulation of voltage-sensitive potassium channel obo:GO_1903817 down-regulation of voltage gated potassium channel activity obo:GO_1903817 down-regulation of voltage-dependent potassium channel activity obo:GO_1903817 down-regulation of voltage-gated potassium channel activity obo:GO_1903817 down-regulation of voltage-gated potassium ion channel activity obo:GO_1903817 down-regulation of voltage-sensitive potassium channel obo:GO_1903817 downregulation of voltage gated potassium channel activity obo:GO_1903817 downregulation of voltage-dependent potassium channel activity obo:GO_1903817 downregulation of voltage-gated potassium channel activity obo:GO_1903817 downregulation of voltage-gated potassium ion channel activity obo:GO_1903817 downregulation of voltage-sensitive potassium channel obo:GO_1903817 negative regulation of voltage gated potassium channel activity obo:GO_1903817 negative regulation of voltage-dependent potassium channel activity obo:GO_1903817 negative regulation of voltage-gated potassium ion channel activity obo:GO_1903817 negative regulation of voltage-sensitive potassium channel obo:GO_1903817 inhibition of voltage gated potassium channel activity obo:GO_1903817 inhibition of voltage-dependent potassium channel activity obo:GO_1903817 inhibition of voltage-gated potassium channel activity obo:GO_1903817 inhibition of voltage-gated potassium ion channel activity obo:GO_1903817 inhibition of voltage-sensitive potassium channel obo:GO_1903817 biological_process obo:GO_1903817 GO:1903817 obo:GO_1903817 negative regulation of voltage-gated potassium channel activity obo:GO_1903818 Any process that activates or increases the frequency, rate or extent of voltage-gated potassium channel activity. obo:GO_1903818 obo:go.owl obo:GO_1903818 sl obo:GO_1903818 2015-01-16T17:22:18Z obo:GO_1903818 positive regulation of voltage gated potassium channel activity obo:GO_1903818 positive regulation of voltage-dependent potassium channel activity obo:GO_1903818 positive regulation of voltage-gated potassium ion channel activity obo:GO_1903818 positive regulation of voltage-sensitive potassium channel obo:GO_1903818 up regulation of voltage gated potassium channel activity obo:GO_1903818 up regulation of voltage-dependent potassium channel activity obo:GO_1903818 up regulation of voltage-gated potassium channel activity obo:GO_1903818 up regulation of voltage-gated potassium ion channel activity obo:GO_1903818 up regulation of voltage-sensitive potassium channel obo:GO_1903818 up-regulation of voltage gated potassium channel activity obo:GO_1903818 up-regulation of voltage-dependent potassium channel activity obo:GO_1903818 up-regulation of voltage-gated potassium channel activity obo:GO_1903818 up-regulation of voltage-gated potassium ion channel activity obo:GO_1903818 up-regulation of voltage-sensitive potassium channel obo:GO_1903818 upregulation of voltage gated potassium channel activity obo:GO_1903818 upregulation of voltage-dependent potassium channel activity obo:GO_1903818 upregulation of voltage-gated potassium channel activity obo:GO_1903818 upregulation of voltage-gated potassium ion channel activity obo:GO_1903818 upregulation of voltage-sensitive potassium channel obo:GO_1903818 activation of voltage gated potassium channel activity obo:GO_1903818 activation of voltage-dependent potassium channel activity obo:GO_1903818 activation of voltage-gated potassium channel activity obo:GO_1903818 activation of voltage-gated potassium ion channel activity obo:GO_1903818 activation of voltage-sensitive potassium channel obo:GO_1903818 biological_process obo:GO_1903818 GO:1903818 obo:GO_1903818 positive regulation of voltage-gated potassium channel activity obo:GO_1903823 Single strand break repair that takes place in a telomere. obo:GO_1903823 obo:go.owl obo:GO_1903823 jl obo:GO_1903823 2015-01-19T16:12:29Z obo:GO_1903823 single strand break repair in telomere obo:GO_1903823 telomere single-strand break repair obo:GO_1903823 telomeric single strand break repair obo:GO_1903823 biological_process obo:GO_1903823 telomere SSBR obo:GO_1903823 GO:1903823 obo:GO_1903823 telomere single strand break repair obo:GO_1903827 Any process that modulates the frequency, rate or extent of cellular protein localization. Cellular protein localization is any process in which a protein is transported to, and/or maintained in, a specific location and encompasses movement within the cell, from within the cell to the cell surface, or from one location to another at the surface of a cell. obo:GO_1903827 obo:go.owl obo:GO_1903827 jl obo:GO_1903827 2015-01-20T14:32:14Z obo:GO_1903827 regulation of cellular protein localisation obo:GO_1903827 regulation of channel localizer activity obo:GO_1903827 biological_process obo:GO_1903827 GO:1903827 obo:GO_1903827 regulation of cellular protein localization obo:GO_1903828 Any process that stops, prevents or reduces the frequency, rate or extent of cellular protein localization. Cellular protein localization is any process in which a protein is transported to, and/or maintained in, a specific location and encompasses movement within the cell, from within the cell to the cell surface, or from one location to another at the surface of a cell. obo:GO_1903828 obo:go.owl obo:GO_1903828 jl obo:GO_1903828 2015-01-20T14:32:24Z obo:GO_1903828 down regulation of cellular protein localisation obo:GO_1903828 down regulation of cellular protein localization obo:GO_1903828 down-regulation of cellular protein localisation obo:GO_1903828 down-regulation of cellular protein localization obo:GO_1903828 downregulation of cellular protein localisation obo:GO_1903828 downregulation of cellular protein localization obo:GO_1903828 negative regulation of cellular protein localisation obo:GO_1903828 down regulation of channel localizer activity obo:GO_1903828 down-regulation of channel localizer activity obo:GO_1903828 downregulation of channel localizer activity obo:GO_1903828 inhibition of cellular protein localisation obo:GO_1903828 inhibition of cellular protein localization obo:GO_1903828 inhibition of channel localizer activity obo:GO_1903828 negative regulation of channel localizer activity obo:GO_1903828 biological_process obo:GO_1903828 GO:1903828 obo:GO_1903828 negative regulation of cellular protein localization obo:GO_1903829 Any process that activates or increases the frequency, rate or extent of cellular protein localization. Cellular protein localization is any process in which a protein is transported to, and/or maintained in, a specific location and encompasses movement within the cell, from within the cell to the cell surface, or from one location to another at the surface of a cell. obo:GO_1903829 obo:go.owl obo:GO_1903829 jl obo:GO_1903829 2015-01-20T14:32:33Z obo:GO_1903829 positive regulation of cellular protein localisation obo:GO_1903829 up regulation of cellular protein localisation obo:GO_1903829 up regulation of cellular protein localization obo:GO_1903829 up-regulation of cellular protein localisation obo:GO_1903829 up-regulation of cellular protein localization obo:GO_1903829 upregulation of cellular protein localisation obo:GO_1903829 upregulation of cellular protein localization obo:GO_1903829 activation of cellular protein localisation obo:GO_1903829 activation of cellular protein localization obo:GO_1903829 activation of channel localizer activity obo:GO_1903829 positive regulation of channel localizer activity obo:GO_1903829 up regulation of channel localizer activity obo:GO_1903829 up-regulation of channel localizer activity obo:GO_1903829 upregulation of channel localizer activity obo:GO_1903829 biological_process obo:GO_1903829 GO:1903829 obo:GO_1903829 positive regulation of cellular protein localization obo:GO_1903830 The directed movement of magnesium ion across a membrane. obo:GO_1903830 obo:go.owl obo:GO_1903830 mcc obo:GO_1903830 2015-01-21T17:38:30Z obo:GO_1903830 biological_process obo:GO_1903830 GO:1903830 obo:GO_1903830 magnesium ion transmembrane transport obo:GO_1903875 Interacting selectively and non-covalently with corticosterone. obo:GO_1903875 obo:go.owl obo:GO_1903875 mr obo:GO_1903875 2015-02-06T16:02:35Z obo:GO_1903875 molecular_function obo:GO_1903875 GO:1903875 obo:GO_1903875 corticosterone binding obo:GO_1903876 Interacting selectively and non-covalently with 11-deoxycortisol. obo:GO_1903876 obo:go.owl obo:GO_1903876 mr obo:GO_1903876 2015-02-06T16:02:44Z obo:GO_1903876 molecular_function obo:GO_1903876 GO:1903876 obo:GO_1903876 11-deoxycortisol binding obo:GO_1903877 Interacting selectively and non-covalently with 21-deoxycortisol. obo:GO_1903877 obo:go.owl obo:GO_1903877 mr obo:GO_1903877 2015-02-06T16:02:54Z obo:GO_1903877 molecular_function obo:GO_1903877 GO:1903877 obo:GO_1903877 21-deoxycortisol binding obo:GO_1903878 Interacting selectively and non-covalently with 11-deoxycorticosterone. obo:GO_1903878 obo:go.owl obo:GO_1903878 mr obo:GO_1903878 2015-02-06T16:03:03Z obo:GO_1903878 molecular_function obo:GO_1903878 GO:1903878 obo:GO_1903878 11-deoxycorticosterone binding obo:GO_1903879 Interacting selectively and non-covalently with 11beta-hydroxyprogesterone. obo:GO_1903879 obo:go.owl obo:GO_1903879 mr obo:GO_1903879 2015-02-06T16:03:12Z obo:GO_1903879 molecular_function obo:GO_1903879 GO:1903879 obo:GO_1903879 11beta-hydroxyprogesterone binding obo:GO_1903880 Interacting selectively and non-covalently with 17alpha-hydroxyprogesterone. obo:GO_1903880 obo:go.owl obo:GO_1903880 mr obo:GO_1903880 2015-02-06T16:03:22Z obo:GO_1903880 molecular_function obo:GO_1903880 GO:1903880 obo:GO_1903880 17alpha-hydroxyprogesterone binding obo:GO_1903909 Any process that modulates the frequency, rate or extent of receptor clustering. obo:GO_1903909 obo:go.owl obo:GO_1903909 als obo:GO_1903909 2015-02-09T10:56:33Z obo:GO_1903909 biological_process obo:GO_1903909 GO:1903909 obo:GO_1903909 regulation of receptor clustering obo:GO_1903910 Any process that stops, prevents or reduces the frequency, rate or extent of receptor clustering. obo:GO_1903910 obo:go.owl obo:GO_1903910 als obo:GO_1903910 2015-02-09T10:56:42Z obo:GO_1903910 down regulation of receptor clustering obo:GO_1903910 down-regulation of receptor clustering obo:GO_1903910 downregulation of receptor clustering obo:GO_1903910 inhibition of receptor clustering obo:GO_1903910 biological_process obo:GO_1903910 GO:1903910 obo:GO_1903910 negative regulation of receptor clustering obo:GO_1903911 Any process that activates or increases the frequency, rate or extent of receptor clustering. obo:GO_1903911 obo:go.owl obo:GO_1903911 als obo:GO_1903911 2015-02-09T10:56:51Z obo:GO_1903911 up regulation of receptor clustering obo:GO_1903911 up-regulation of receptor clustering obo:GO_1903911 upregulation of receptor clustering obo:GO_1903911 activation of receptor clustering obo:GO_1903911 biological_process obo:GO_1903911 GO:1903911 obo:GO_1903911 positive regulation of receptor clustering obo:GO_1903924 Interacting selectively and non-covalently with estradiol. obo:GO_1903924 obo:go.owl obo:GO_1903924 sl obo:GO_1903924 2015-02-11T00:11:34Z obo:GO_1903924 molecular_function obo:GO_1903924 GO:1903924 obo:GO_1903924 estradiol binding obo:GO_1903959 Any process that modulates the frequency, rate or extent of anion transmembrane transport. obo:GO_1903959 obo:go.owl obo:GO_1903959 pr obo:GO_1903959 2015-02-25T13:52:25Z obo:GO_1903959 biological_process obo:GO_1903959 GO:1903959 obo:GO_1903959 regulation of anion transmembrane transport obo:GO_1903960 Any process that stops, prevents or reduces the frequency, rate or extent of anion transmembrane transport. obo:GO_1903960 obo:go.owl obo:GO_1903960 pr obo:GO_1903960 2015-02-25T13:52:35Z obo:GO_1903960 down regulation of anion transmembrane transport obo:GO_1903960 down-regulation of anion transmembrane transport obo:GO_1903960 downregulation of anion transmembrane transport obo:GO_1903960 inhibition of anion transmembrane transport obo:GO_1903960 biological_process obo:GO_1903960 GO:1903960 obo:GO_1903960 negative regulation of anion transmembrane transport obo:GO_1903961 Any process that activates or increases the frequency, rate or extent of anion transmembrane transport. obo:GO_1903961 obo:go.owl obo:GO_1903961 pr obo:GO_1903961 2015-02-25T13:52:44Z obo:GO_1903961 up regulation of anion transmembrane transport obo:GO_1903961 up-regulation of anion transmembrane transport obo:GO_1903961 upregulation of anion transmembrane transport obo:GO_1903961 activation of anion transmembrane transport obo:GO_1903961 biological_process obo:GO_1903961 GO:1903961 obo:GO_1903961 positive regulation of anion transmembrane transport obo:GO_1903981 Interacting selectively and non-covalently with enterobactin. obo:GO_1903981 obo:go.owl obo:GO_1903981 mr obo:GO_1903981 2015-03-02T17:21:54Z obo:GO_1903981 siderophore binding obo:GO_1903981 enterochelin binding obo:GO_1903981 molecular_function obo:GO_1903981 GO:1903981 obo:GO_1903981 enterobactin binding obo:GO_1903988 The directed movement of iron ions from inside of a cell, across the plasma membrane and into the extracellular region. obo:GO_1903988 obo:go.owl obo:GO_1903988 rl obo:GO_1903988 2014-09-03T13:01:37Z obo:GO_1903988 GO:1903414 obo:GO_1903988 ferrous iron export obo:GO_1903988 ferrous iron export across plasma membrane obo:GO_1903988 biological_process obo:GO_1903988 iron cation export obo:GO_1903988 iron(2+) export obo:GO_1903988 GO:1903988 obo:GO_1903988 An example of this is mouse ferroportin (symbol Slc40a1, UniProtKB identifier: Q9JHI9). obo:GO_1903988 iron ion export across plasma membrane obo:GO_1904002 Any process that modulates the frequency, rate or extent of sebum secreting cell proliferation. obo:GO_1904002 obo:go.owl obo:GO_1904002 hjd obo:GO_1904002 2015-03-06T16:19:44Z obo:GO_1904002 biological_process obo:GO_1904002 regulation of sebocyte proliferation obo:GO_1904002 GO:1904002 obo:GO_1904002 regulation of sebum secreting cell proliferation obo:GO_1904003 Any process that stops, prevents or reduces the frequency, rate or extent of sebum secreting cell proliferation. obo:GO_1904003 obo:go.owl obo:GO_1904003 hjd obo:GO_1904003 2015-03-06T16:19:50Z obo:GO_1904003 down regulation of sebum secreting cell proliferation obo:GO_1904003 down-regulation of sebum secreting cell proliferation obo:GO_1904003 downregulation of sebum secreting cell proliferation obo:GO_1904003 inhibition of sebum secreting cell proliferation obo:GO_1904003 biological_process obo:GO_1904003 down regulation of sebocyte proliferation obo:GO_1904003 down-regulation of sebocyte proliferation obo:GO_1904003 downregulation of sebocyte proliferation obo:GO_1904003 inhibition of sebocyte proliferation obo:GO_1904003 negative regulation of sebocyte proliferation obo:GO_1904003 GO:1904003 obo:GO_1904003 negative regulation of sebum secreting cell proliferation obo:GO_1904004 Any process that activates or increases the frequency, rate or extent of sebum secreting cell proliferation. obo:GO_1904004 obo:go.owl obo:GO_1904004 hjd obo:GO_1904004 2015-03-06T16:19:56Z obo:GO_1904004 up regulation of sebum secreting cell proliferation obo:GO_1904004 up-regulation of sebum secreting cell proliferation obo:GO_1904004 upregulation of sebum secreting cell proliferation obo:GO_1904004 activation of sebum secreting cell proliferation obo:GO_1904004 biological_process obo:GO_1904004 activation of sebocyte proliferation obo:GO_1904004 positive regulation of sebocyte proliferation obo:GO_1904004 up regulation of sebocyte proliferation obo:GO_1904004 up-regulation of sebocyte proliferation obo:GO_1904004 upregulation of sebocyte proliferation obo:GO_1904004 GO:1904004 obo:GO_1904004 positive regulation of sebum secreting cell proliferation obo:GO_1904008 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a monosodium glutamate stimulus. obo:GO_1904008 obo:go.owl obo:GO_1904008 sl obo:GO_1904008 2015-03-06T18:26:34Z obo:GO_1904008 biological_process obo:GO_1904008 GO:1904008 obo:GO_1904008 response to monosodium glutamate obo:GO_1904009 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a monosodium glutamate stimulus. obo:GO_1904009 obo:go.owl obo:GO_1904009 sl obo:GO_1904009 2015-03-06T18:26:40Z obo:GO_1904009 biological_process obo:GO_1904009 GO:1904009 obo:GO_1904009 cellular response to monosodium glutamate obo:GO_1904032 Any process that modulates the frequency, rate or extent of t-SNARE clustering. obo:GO_1904032 obo:go.owl obo:GO_1904032 sl obo:GO_1904032 2015-03-13T21:21:38Z obo:GO_1904032 biological_process obo:GO_1904032 GO:1904032 obo:GO_1904032 regulation of t-SNARE clustering obo:GO_1904033 Any process that stops, prevents or reduces the frequency, rate or extent of t-SNARE clustering. obo:GO_1904033 obo:go.owl obo:GO_1904033 sl obo:GO_1904033 2015-03-13T21:21:44Z obo:GO_1904033 down regulation of t-SNARE clustering obo:GO_1904033 down-regulation of t-SNARE clustering obo:GO_1904033 downregulation of t-SNARE clustering obo:GO_1904033 inhibition of t-SNARE clustering obo:GO_1904033 biological_process obo:GO_1904033 GO:1904033 obo:GO_1904033 negative regulation of t-SNARE clustering obo:GO_1904034 Any process that activates or increases the frequency, rate or extent of t-SNARE clustering. obo:GO_1904034 obo:go.owl obo:GO_1904034 sl obo:GO_1904034 2015-03-13T21:21:50Z obo:GO_1904034 up regulation of t-SNARE clustering obo:GO_1904034 up-regulation of t-SNARE clustering obo:GO_1904034 upregulation of t-SNARE clustering obo:GO_1904034 activation of t-SNARE clustering obo:GO_1904034 biological_process obo:GO_1904034 GO:1904034 obo:GO_1904034 positive regulation of t-SNARE clustering obo:GO_1904047 Interacting selectively and non-covalently with S-adenosyl-L-methionine. obo:GO_1904047 obo:go.owl obo:GO_1904047 hadil.alrohaif.14 obo:GO_1904047 2015-03-17T10:32:16Z obo:GO_1904047 GO:0070283 obo:GO_1904047 Reactome:R-HSA-947535 obo:GO_1904047 radical SAM enzyme activity obo:GO_1904047 molecular_function obo:GO_1904047 GO:1904047 obo:GO_1904047 S-adenosyl-L-methionine binding obo:GO_1904054 Any process that modulates the frequency, rate or extent of cholangiocyte proliferation. obo:GO_1904054 obo:go.owl obo:GO_1904054 sl obo:GO_1904054 2015-03-18T17:56:14Z obo:GO_1904054 regulation of hepatoblast proliferation obo:GO_1904054 biological_process obo:GO_1904054 GO:1904054 obo:GO_1904054 regulation of cholangiocyte proliferation obo:GO_1904055 Any process that stops, prevents or reduces the frequency, rate or extent of cholangiocyte proliferation. obo:GO_1904055 obo:go.owl obo:GO_1904055 sl obo:GO_1904055 2015-03-18T17:56:20Z obo:GO_1904055 down regulation of cholangiocyte proliferation obo:GO_1904055 down regulation of hepatoblast proliferation obo:GO_1904055 down-regulation of cholangiocyte proliferation obo:GO_1904055 down-regulation of hepatoblast proliferation obo:GO_1904055 downregulation of cholangiocyte proliferation obo:GO_1904055 downregulation of hepatoblast proliferation obo:GO_1904055 negative regulation of hepatoblast proliferation obo:GO_1904055 inhibition of cholangiocyte proliferation obo:GO_1904055 inhibition of hepatoblast proliferation obo:GO_1904055 biological_process obo:GO_1904055 GO:1904055 obo:GO_1904055 negative regulation of cholangiocyte proliferation obo:GO_1904056 Any process that activates or increases the frequency, rate or extent of cholangiocyte proliferation. obo:GO_1904056 obo:go.owl obo:GO_1904056 sl obo:GO_1904056 2015-03-18T17:56:26Z obo:GO_1904056 positive regulation of hepatoblast proliferation obo:GO_1904056 up regulation of cholangiocyte proliferation obo:GO_1904056 up regulation of hepatoblast proliferation obo:GO_1904056 up-regulation of cholangiocyte proliferation obo:GO_1904056 up-regulation of hepatoblast proliferation obo:GO_1904056 upregulation of cholangiocyte proliferation obo:GO_1904056 upregulation of hepatoblast proliferation obo:GO_1904056 activation of cholangiocyte proliferation obo:GO_1904056 activation of hepatoblast proliferation obo:GO_1904056 biological_process obo:GO_1904056 GO:1904056 obo:GO_1904056 positive regulation of cholangiocyte proliferation obo:GO_1904062 Any process that modulates the frequency, rate or extent of cation transmembrane transport. obo:GO_1904062 obo:go.owl obo:GO_1904062 sl obo:GO_1904062 2015-03-18T21:11:43Z obo:GO_1904062 biological_process obo:GO_1904062 GO:1904062 obo:GO_1904062 regulation of cation transmembrane transport obo:GO_1904063 Any process that stops, prevents or reduces the frequency, rate or extent of cation transmembrane transport. obo:GO_1904063 obo:go.owl obo:GO_1904063 sl obo:GO_1904063 2015-03-18T21:11:50Z obo:GO_1904063 down regulation of cation transmembrane transport obo:GO_1904063 down-regulation of cation transmembrane transport obo:GO_1904063 downregulation of cation transmembrane transport obo:GO_1904063 inhibition of cation transmembrane transport obo:GO_1904063 biological_process obo:GO_1904063 GO:1904063 obo:GO_1904063 negative regulation of cation transmembrane transport obo:GO_1904064 Any process that activates or increases the frequency, rate or extent of cation transmembrane transport. obo:GO_1904064 obo:go.owl obo:GO_1904064 sl obo:GO_1904064 2015-03-18T21:11:55Z obo:GO_1904064 up regulation of cation transmembrane transport obo:GO_1904064 up-regulation of cation transmembrane transport obo:GO_1904064 upregulation of cation transmembrane transport obo:GO_1904064 activation of cation transmembrane transport obo:GO_1904064 biological_process obo:GO_1904064 GO:1904064 obo:GO_1904064 positive regulation of cation transmembrane transport obo:GO_1904195 Any process that modulates the frequency, rate or extent of granulosa cell proliferation. obo:GO_1904195 obo:go.owl obo:GO_1904195 sl obo:GO_1904195 2015-05-07T17:02:25Z obo:GO_1904195 biological_process obo:GO_1904195 GO:1904195 obo:GO_1904195 regulation of granulosa cell proliferation obo:GO_1904196 Any process that stops, prevents or reduces the frequency, rate or extent of granulosa cell proliferation. obo:GO_1904196 obo:go.owl obo:GO_1904196 sl obo:GO_1904196 2015-05-07T17:02:34Z obo:GO_1904196 down regulation of granulosa cell proliferation obo:GO_1904196 down-regulation of granulosa cell proliferation obo:GO_1904196 downregulation of granulosa cell proliferation obo:GO_1904196 inhibition of granulosa cell proliferation obo:GO_1904196 biological_process obo:GO_1904196 GO:1904196 obo:GO_1904196 negative regulation of granulosa cell proliferation obo:GO_1904197 Any process that activates or increases the frequency, rate or extent of granulosa cell proliferation. obo:GO_1904197 obo:go.owl obo:GO_1904197 sl obo:GO_1904197 2015-05-07T17:02:40Z obo:GO_1904197 up regulation of granulosa cell proliferation obo:GO_1904197 up-regulation of granulosa cell proliferation obo:GO_1904197 upregulation of granulosa cell proliferation obo:GO_1904197 activation of granulosa cell proliferation obo:GO_1904197 biological_process obo:GO_1904197 GO:1904197 obo:GO_1904197 positive regulation of granulosa cell proliferation obo:GO_1904201 Any process that modulates the frequency, rate or extent of iodide transport. obo:GO_1904201 obo:go.owl obo:GO_1904201 sl obo:GO_1904201 2015-05-08T15:19:57Z obo:GO_1904201 biological_process obo:GO_1904201 GO:1904201 obo:GO_1904201 regulation of iodide transport obo:GO_1904202 Any process that stops, prevents or reduces the frequency, rate or extent of iodide transport. obo:GO_1904202 obo:go.owl obo:GO_1904202 sl obo:GO_1904202 2015-05-08T15:20:03Z obo:GO_1904202 down regulation of iodide transport obo:GO_1904202 down-regulation of iodide transport obo:GO_1904202 downregulation of iodide transport obo:GO_1904202 inhibition of iodide transport obo:GO_1904202 biological_process obo:GO_1904202 GO:1904202 obo:GO_1904202 negative regulation of iodide transport obo:GO_1904203 Any process that activates or increases the frequency, rate or extent of iodide transport. obo:GO_1904203 obo:go.owl obo:GO_1904203 sl obo:GO_1904203 2015-05-08T15:20:09Z obo:GO_1904203 up regulation of iodide transport obo:GO_1904203 up-regulation of iodide transport obo:GO_1904203 upregulation of iodide transport obo:GO_1904203 activation of iodide transport obo:GO_1904203 biological_process obo:GO_1904203 GO:1904203 obo:GO_1904203 positive regulation of iodide transport obo:GO_1904212 Any process that modulates the frequency, rate or extent of iodide transmembrane transport. obo:GO_1904212 obo:go.owl obo:GO_1904212 sl obo:GO_1904212 2015-05-14T19:00:02Z obo:GO_1904212 biological_process obo:GO_1904212 GO:1904212 obo:GO_1904212 regulation of iodide transmembrane transport obo:GO_1904213 Any process that stops, prevents or reduces the frequency, rate or extent of iodide transmembrane transport. obo:GO_1904213 obo:go.owl obo:GO_1904213 sl obo:GO_1904213 2015-05-14T19:00:08Z obo:GO_1904213 down regulation of iodide transmembrane transport obo:GO_1904213 down-regulation of iodide transmembrane transport obo:GO_1904213 downregulation of iodide transmembrane transport obo:GO_1904213 inhibition of iodide transmembrane transport obo:GO_1904213 biological_process obo:GO_1904213 GO:1904213 obo:GO_1904213 negative regulation of iodide transmembrane transport obo:GO_1904214 Any process that activates or increases the frequency, rate or extent of iodide transmembrane transport. obo:GO_1904214 obo:go.owl obo:GO_1904214 sl obo:GO_1904214 2015-05-14T19:00:14Z obo:GO_1904214 up regulation of iodide transmembrane transport obo:GO_1904214 up-regulation of iodide transmembrane transport obo:GO_1904214 upregulation of iodide transmembrane transport obo:GO_1904214 activation of iodide transmembrane transport obo:GO_1904214 biological_process obo:GO_1904214 GO:1904214 obo:GO_1904214 positive regulation of iodide transmembrane transport obo:GO_1904254 Any process that modulates the frequency, rate or extent of an iron transmembrane transporter activity. obo:GO_1904254 obo:go.owl obo:GO_1904254 kom obo:GO_1904254 2015-05-20T14:05:00Z obo:GO_1904254 regulation of iron cation channel activity obo:GO_1904254 regulation of iron channel activity obo:GO_1904254 regulation of iron-specific channel activity obo:GO_1904254 biological_process obo:GO_1904254 GO:1904254 obo:GO_1904254 regulation of iron ion transmembrane transporter activity obo:GO_1904255 Any process that stops, prevents or reduces the frequency, rate or extent of an iron transmembrane transporter activity. obo:GO_1904255 obo:go.owl obo:GO_1904255 kom obo:GO_1904255 2015-05-20T14:05:06Z obo:GO_1904255 down regulation of iron cation channel activity obo:GO_1904255 down regulation of iron channel activity obo:GO_1904255 down regulation of iron-specific channel activity obo:GO_1904255 down-regulation of iron cation channel activity obo:GO_1904255 down-regulation of iron channel activity obo:GO_1904255 down-regulation of iron-specific channel activity obo:GO_1904255 downregulation of iron cation channel activity obo:GO_1904255 downregulation of iron channel activity obo:GO_1904255 downregulation of iron-specific channel activity obo:GO_1904255 negative regulation of iron cation channel activity obo:GO_1904255 negative regulation of iron channel activity obo:GO_1904255 negative regulation of iron-specific channel activity obo:GO_1904255 inhibition of iron cation channel activity obo:GO_1904255 inhibition of iron channel activity obo:GO_1904255 inhibition of iron-specific channel activity obo:GO_1904255 biological_process obo:GO_1904255 GO:1904255 obo:GO_1904255 negative regulation of iron ion transmembrane transporter activity obo:GO_1904256 Any process that activates or increases the frequency, rate or extent of an iron transmembrane transporter activity. obo:GO_1904256 obo:go.owl obo:GO_1904256 kom obo:GO_1904256 2015-05-20T14:05:12Z obo:GO_1904256 positive regulation of iron cation channel activity obo:GO_1904256 positive regulation of iron channel activity obo:GO_1904256 positive regulation of iron transmembrane transporter activity obo:GO_1904256 positive regulation of iron-specific channel activity obo:GO_1904256 up regulation of iron cation channel activity obo:GO_1904256 up regulation of iron channel activity obo:GO_1904256 up regulation of iron-specific channel activity obo:GO_1904256 up-regulation of iron cation channel activity obo:GO_1904256 up-regulation of iron channel activity obo:GO_1904256 up-regulation of iron-specific channel activity obo:GO_1904256 upregulation of iron cation channel activity obo:GO_1904256 upregulation of iron channel activity obo:GO_1904256 upregulation of iron-specific channel activity obo:GO_1904256 activation of iron cation channel activity obo:GO_1904256 activation of iron channel activity obo:GO_1904256 activation of iron-specific channel activity obo:GO_1904256 biological_process obo:GO_1904256 GO:1904256 obo:GO_1904256 positive regulation of iron ion transmembrane transporter activity obo:GO_1904257 The directed import of zinc(2+) from the cytosol across the Golgi membrane into the Golgi apparatus. obo:GO_1904257 obo:go.owl obo:GO_1904257 tb obo:GO_1904257 2015-05-20T19:56:18Z obo:GO_1904257 zinc II ion import across Golgi membrane obo:GO_1904257 zinc ion import across Golgi membrane obo:GO_1904257 zinc(2+) import across Golgi membrane obo:GO_1904257 biological_process obo:GO_1904257 GO:1904257 obo:GO_1904257 This term covers zinc(2+) import *across* the Golgi membrane through a channel or pore. It does not cover import via vesicle fusion with Golgi membrane, as in this case transport does not involve crossing the membrane. obo:GO_1904257 zinc ion import into Golgi membrane obo:GO_1904288 Interacting selectively and non-covalently with a BAT3 complex. obo:GO_1904288 obo:go.owl obo:GO_1904288 bf obo:GO_1904288 2015-06-07T19:48:55Z obo:GO_1904288 BAG6-UBL4A-TRC35 complex binding obo:GO_1904288 Bag6 complex binding obo:GO_1904288 molecular_function obo:GO_1904288 BAT3-TRC35-UBL4A complex binding obo:GO_1904288 GO:1904288 obo:GO_1904288 BAT3 complex binding obo:GO_1904313 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a methamphetamine hydrochloride stimulus. obo:GO_1904313 obo:go.owl obo:GO_1904313 sl obo:GO_1904313 2015-06-10T17:47:09Z obo:GO_1904313 response to methamphetamine HCL obo:GO_1904313 biological_process obo:GO_1904313 GO:1904313 obo:GO_1904313 response to methamphetamine hydrochloride obo:GO_1904314 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a methamphetamine hydrochloride stimulus. obo:GO_1904314 obo:go.owl obo:GO_1904314 sl obo:GO_1904314 2015-06-10T17:47:15Z obo:GO_1904314 cellular response to methamphetamine HCL obo:GO_1904314 biological_process obo:GO_1904314 GO:1904314 obo:GO_1904314 cellular response to methamphetamine hydrochloride obo:GO_1904321 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a forskolin stimulus. obo:GO_1904321 obo:go.owl obo:GO_1904321 sl obo:GO_1904321 2015-06-10T19:01:27Z obo:GO_1904321 biological_process obo:GO_1904321 GO:1904321 obo:GO_1904321 response to forskolin obo:GO_1904322 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a forskolin stimulus. obo:GO_1904322 obo:go.owl obo:GO_1904322 sl obo:GO_1904322 2015-06-10T19:01:33Z obo:GO_1904322 biological_process obo:GO_1904322 GO:1904322 obo:GO_1904322 cellular response to forskolin obo:GO_1904334 The directed movement of heme from outside of a cell, across the plasma membrane and into the cytosol. obo:GO_1904334 obo:go.owl obo:GO_1904334 al obo:GO_1904334 2015-06-11T16:56:21Z obo:GO_1904334 biological_process obo:GO_1904334 GO:1904334 obo:GO_1904334 heme import across plasma membrane obo:GO_1904365 Any process that modulates the frequency, rate or extent of chemokinesis. obo:GO_1904365 obo:go.owl obo:GO_1904365 sl obo:GO_1904365 2015-06-15T22:44:06Z obo:GO_1904365 biological_process obo:GO_1904365 GO:1904365 obo:GO_1904365 regulation of chemokinesis obo:GO_1904366 Any process that stops, prevents or reduces the frequency, rate or extent of chemokinesis. obo:GO_1904366 obo:go.owl obo:GO_1904366 sl obo:GO_1904366 2015-06-15T22:44:12Z obo:GO_1904366 down regulation of chemokinesis obo:GO_1904366 down-regulation of chemokinesis obo:GO_1904366 downregulation of chemokinesis obo:GO_1904366 inhibition of chemokinesis obo:GO_1904366 biological_process obo:GO_1904366 GO:1904366 obo:GO_1904366 negative regulation of chemokinesis obo:GO_1904367 Any process that activates or increases the frequency, rate or extent of chemokinesis. obo:GO_1904367 obo:go.owl obo:GO_1904367 sl obo:GO_1904367 2015-06-15T22:44:18Z obo:GO_1904367 up regulation of chemokinesis obo:GO_1904367 up-regulation of chemokinesis obo:GO_1904367 upregulation of chemokinesis obo:GO_1904367 activation of chemokinesis obo:GO_1904367 biological_process obo:GO_1904367 GO:1904367 obo:GO_1904367 positive regulation of chemokinesis obo:GO_1904370 Any process that modulates the frequency, rate or extent of protein localization to actin cortical patch. obo:GO_1904370 obo:go.owl obo:GO_1904370 sl obo:GO_1904370 2015-06-18T22:23:31Z obo:GO_1904370 regulation of protein localisation to actin cortical patch obo:GO_1904370 biological_process obo:GO_1904370 GO:1904370 obo:GO_1904370 regulation of protein localization to actin cortical patch obo:GO_1904371 Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to actin cortical patch. obo:GO_1904371 obo:go.owl obo:GO_1904371 sl obo:GO_1904371 2015-06-18T22:23:37Z obo:GO_1904371 down regulation of protein localisation to actin cortical patch obo:GO_1904371 down regulation of protein localization to actin cortical patch obo:GO_1904371 down-regulation of protein localisation to actin cortical patch obo:GO_1904371 down-regulation of protein localization to actin cortical patch obo:GO_1904371 downregulation of protein localisation to actin cortical patch obo:GO_1904371 downregulation of protein localization to actin cortical patch obo:GO_1904371 negative regulation of protein localisation to actin cortical patch obo:GO_1904371 inhibition of protein localisation to actin cortical patch obo:GO_1904371 inhibition of protein localization to actin cortical patch obo:GO_1904371 biological_process obo:GO_1904371 GO:1904371 obo:GO_1904371 negative regulation of protein localization to actin cortical patch obo:GO_1904372 Any process that activates or increases the frequency, rate or extent of protein localization to actin cortical patch. obo:GO_1904372 obo:go.owl obo:GO_1904372 sl obo:GO_1904372 2015-06-18T22:23:43Z obo:GO_1904372 positive regulation of protein localisation to actin cortical patch obo:GO_1904372 up regulation of protein localisation to actin cortical patch obo:GO_1904372 up regulation of protein localization to actin cortical patch obo:GO_1904372 up-regulation of protein localisation to actin cortical patch obo:GO_1904372 up-regulation of protein localization to actin cortical patch obo:GO_1904372 upregulation of protein localisation to actin cortical patch obo:GO_1904372 upregulation of protein localization to actin cortical patch obo:GO_1904372 activation of protein localisation to actin cortical patch obo:GO_1904372 activation of protein localization to actin cortical patch obo:GO_1904372 biological_process obo:GO_1904372 GO:1904372 obo:GO_1904372 positive regulation of protein localization to actin cortical patch obo:GO_1904375 Any process that modulates the frequency, rate or extent of protein localization to cell periphery. obo:GO_1904375 obo:go.owl obo:GO_1904375 sl obo:GO_1904375 2015-06-22T22:09:25Z obo:GO_1904375 biological_process obo:GO_1904375 GO:1904375 obo:GO_1904375 regulation of protein localization to cell periphery obo:GO_1904376 Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to cell periphery. obo:GO_1904376 obo:go.owl obo:GO_1904376 sl obo:GO_1904376 2015-06-22T22:09:32Z obo:GO_1904376 down regulation of protein localization to cell periphery obo:GO_1904376 down-regulation of protein localization to cell periphery obo:GO_1904376 downregulation of protein localization to cell periphery obo:GO_1904376 inhibition of protein localization to cell periphery obo:GO_1904376 biological_process obo:GO_1904376 GO:1904376 obo:GO_1904376 negative regulation of protein localization to cell periphery obo:GO_1904377 Any process that activates or increases the frequency, rate or extent of protein localization to cell periphery. obo:GO_1904377 obo:go.owl obo:GO_1904377 sl obo:GO_1904377 2015-06-22T22:09:37Z obo:GO_1904377 up regulation of protein localization to cell periphery obo:GO_1904377 up-regulation of protein localization to cell periphery obo:GO_1904377 upregulation of protein localization to cell periphery obo:GO_1904377 activation of protein localization to cell periphery obo:GO_1904377 biological_process obo:GO_1904377 GO:1904377 obo:GO_1904377 positive regulation of protein localization to cell periphery obo:GO_1904399 Interacting selectively and non-covalently with heparan sulfate. obo:GO_1904399 obo:go.owl obo:GO_1904399 sl obo:GO_1904399 2015-06-23T19:56:54Z obo:GO_1904399 molecular_function obo:GO_1904399 GO:1904399 obo:GO_1904399 heparan sulfate binding obo:GO_1904404 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a formaldehyde stimulus. obo:GO_1904404 obo:go.owl obo:GO_1904404 sl obo:GO_1904404 2015-06-23T21:14:04Z obo:GO_1904404 biological_process obo:GO_1904404 GO:1904404 obo:GO_1904404 response to formaldehyde obo:GO_1904405 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a formaldehyde stimulus. obo:GO_1904405 obo:go.owl obo:GO_1904405 sl obo:GO_1904405 2015-06-23T21:14:10Z obo:GO_1904405 biological_process obo:GO_1904405 GO:1904405 obo:GO_1904405 cellular response to formaldehyde obo:GO_1904408 Interacting selectively and non-covalently with melatonin. obo:GO_1904408 obo:go.owl obo:GO_1904408 mr obo:GO_1904408 2015-06-25T19:19:53Z obo:GO_1904408 molecular_function obo:GO_1904408 GO:1904408 obo:GO_1904408 melatonin binding obo:GO_1904427 Any process that activates or increases the frequency, rate or extent of calcium ion transmembrane transport. obo:GO_1904427 obo:go.owl obo:GO_1904427 sl obo:GO_1904427 2015-07-02T20:44:25Z obo:GO_1904427 positive regulation of calcium ion membrane transport obo:GO_1904427 positive regulation of transmembrane calcium transport obo:GO_1904427 up regulation of calcium ion membrane transport obo:GO_1904427 up regulation of calcium ion transmembrane transport obo:GO_1904427 up regulation of transmembrane calcium transport obo:GO_1904427 up-regulation of calcium ion membrane transport obo:GO_1904427 up-regulation of calcium ion transmembrane transport obo:GO_1904427 up-regulation of transmembrane calcium transport obo:GO_1904427 upregulation of calcium ion membrane transport obo:GO_1904427 upregulation of calcium ion transmembrane transport obo:GO_1904427 upregulation of transmembrane calcium transport obo:GO_1904427 activation of calcium ion membrane transport obo:GO_1904427 activation of calcium ion transmembrane transport obo:GO_1904427 activation of transmembrane calcium transport obo:GO_1904427 biological_process obo:GO_1904427 GO:1904427 obo:GO_1904427 positive regulation of calcium ion transmembrane transport obo:GO_1904451 Any process that modulates the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity. obo:GO_1904451 obo:go.owl obo:GO_1904451 sl obo:GO_1904451 2015-07-08T23:00:03Z obo:GO_1904451 regulation of proton pump activity obo:GO_1904451 regulation of (K+ + H+)-ATPase activity obo:GO_1904451 regulation of ATP phosphohydrolase (H+/K+-exchanging) obo:GO_1904451 regulation of H(+)/K(+)-ATPase activity obo:GO_1904451 regulation of H(+)/K(+)-exchanging ATPase activity obo:GO_1904451 regulation of H+-K+-ATPase activity obo:GO_1904451 regulation of H+/K+-ATPase activity obo:GO_1904451 regulation of H+/K+-exchanging ATPase activity obo:GO_1904451 regulation of H,K-ATPase activity obo:GO_1904451 regulation of hydrogen/potassium-exchanging ATPase activity obo:GO_1904451 regulation of hydrogen:potassium exchanging ATPase activity obo:GO_1904451 regulation of hydrogen:potassium-exchanging ATPase activity obo:GO_1904451 regulation of gastric H(+)/K(+) ATPase activity obo:GO_1904451 regulation of gastric H+/K+ ATPase obo:GO_1904451 biological_process obo:GO_1904451 GO:1904451 obo:GO_1904451 regulation of potassium:proton exchanging ATPase activity obo:GO_1904452 Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity. obo:GO_1904452 obo:go.owl obo:GO_1904452 sl obo:GO_1904452 2015-07-08T23:00:09Z obo:GO_1904452 down regulation of (K+ + H+)-ATPase activity obo:GO_1904452 down regulation of ATP phosphohydrolase (H+/K+-exchanging) obo:GO_1904452 down regulation of H(+)/K(+)-ATPase activity obo:GO_1904452 down regulation of H(+)/K(+)-exchanging ATPase activity obo:GO_1904452 down regulation of H+-K+-ATPase activity obo:GO_1904452 down regulation of H+/K+-ATPase activity obo:GO_1904452 down regulation of H+/K+-exchanging ATPase activity obo:GO_1904452 down regulation of H,K-ATPase activity obo:GO_1904452 down regulation of hydrogen/potassium-exchanging ATPase activity obo:GO_1904452 down regulation of hydrogen:potassium exchanging ATPase activity obo:GO_1904452 down regulation of hydrogen:potassium-exchanging ATPase activity obo:GO_1904452 down-regulation of (K+ + H+)-ATPase activity obo:GO_1904452 down-regulation of ATP phosphohydrolase (H+/K+-exchanging) obo:GO_1904452 down-regulation of H(+)/K(+)-ATPase activity obo:GO_1904452 down-regulation of H(+)/K(+)-exchanging ATPase activity obo:GO_1904452 down-regulation of H+-K+-ATPase activity obo:GO_1904452 down-regulation of H+/K+-ATPase activity obo:GO_1904452 down-regulation of H+/K+-exchanging ATPase activity obo:GO_1904452 down-regulation of H,K-ATPase activity obo:GO_1904452 down-regulation of hydrogen/potassium-exchanging ATPase activity obo:GO_1904452 down-regulation of hydrogen:potassium exchanging ATPase activity obo:GO_1904452 down-regulation of hydrogen:potassium-exchanging ATPase activity obo:GO_1904452 downregulation of (K+ + H+)-ATPase activity obo:GO_1904452 downregulation of ATP phosphohydrolase (H+/K+-exchanging) obo:GO_1904452 downregulation of H(+)/K(+)-ATPase activity obo:GO_1904452 downregulation of H(+)/K(+)-exchanging ATPase activity obo:GO_1904452 downregulation of H+-K+-ATPase activity obo:GO_1904452 downregulation of H+/K+-ATPase activity obo:GO_1904452 downregulation of H+/K+-exchanging ATPase activity obo:GO_1904452 downregulation of H,K-ATPase activity obo:GO_1904452 downregulation of hydrogen/potassium-exchanging ATPase activity obo:GO_1904452 downregulation of hydrogen:potassium exchanging ATPase activity obo:GO_1904452 downregulation of hydrogen:potassium-exchanging ATPase activity obo:GO_1904452 negative regulation of (K+ + H+)-ATPase activity obo:GO_1904452 negative regulation of ATP phosphohydrolase (H+/K+-exchanging) obo:GO_1904452 negative regulation of H(+)/K(+)-ATPase activity obo:GO_1904452 negative regulation of H(+)/K(+)-exchanging ATPase activity obo:GO_1904452 negative regulation of H+-K+-ATPase activity obo:GO_1904452 negative regulation of H+/K+-ATPase activity obo:GO_1904452 negative regulation of H+/K+-exchanging ATPase activity obo:GO_1904452 negative regulation of H,K-ATPase activity obo:GO_1904452 negative regulation of hydrogen/potassium-exchanging ATPase activity obo:GO_1904452 negative regulation of hydrogen:potassium exchanging ATPase activity obo:GO_1904452 negative regulation of hydrogen:potassium-exchanging ATPase activity obo:GO_1904452 down regulation of gastric H(+)/K(+) ATPase activity obo:GO_1904452 down regulation of gastric H+/K+ ATPase obo:GO_1904452 down-regulation of gastric H(+)/K(+) ATPase activity obo:GO_1904452 down-regulation of gastric H+/K+ ATPase obo:GO_1904452 downregulation of gastric H(+)/K(+) ATPase activity obo:GO_1904452 downregulation of gastric H+/K+ ATPase obo:GO_1904452 inhibition of (K+ + H+)-ATPase activity obo:GO_1904452 inhibition of ATP phosphohydrolase (H+/K+-exchanging) obo:GO_1904452 inhibition of H(+)/K(+)-ATPase activity obo:GO_1904452 inhibition of H(+)/K(+)-exchanging ATPase activity obo:GO_1904452 inhibition of H+-K+-ATPase activity obo:GO_1904452 inhibition of H+/K+-ATPase activity obo:GO_1904452 inhibition of H+/K+-exchanging ATPase activity obo:GO_1904452 inhibition of H,K-ATPase activity obo:GO_1904452 inhibition of gastric H(+)/K(+) ATPase activity obo:GO_1904452 inhibition of gastric H+/K+ ATPase obo:GO_1904452 inhibition of hydrogen/potassium-exchanging ATPase activity obo:GO_1904452 inhibition of hydrogen:potassium exchanging ATPase activity obo:GO_1904452 inhibition of hydrogen:potassium-exchanging ATPase activity obo:GO_1904452 negative regulation of gastric H(+)/K(+) ATPase activity obo:GO_1904452 negative regulation of gastric H+/K+ ATPase obo:GO_1904452 biological_process obo:GO_1904452 GO:1904452 obo:GO_1904452 negative regulation of potassium:proton exchanging ATPase activity obo:GO_1904453 Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity. obo:GO_1904453 obo:go.owl obo:GO_1904453 sl obo:GO_1904453 2015-07-08T23:00:15Z obo:GO_1904453 positive regulation of (K+ + H+)-ATPase activity obo:GO_1904453 positive regulation of ATP phosphohydrolase (H+/K+-exchanging) obo:GO_1904453 positive regulation of H(+)/K(+)-ATPase activity obo:GO_1904453 positive regulation of H(+)/K(+)-exchanging ATPase activity obo:GO_1904453 positive regulation of H+-K+-ATPase activity obo:GO_1904453 positive regulation of H+/K+-ATPase activity obo:GO_1904453 positive regulation of H+/K+-exchanging ATPase activity obo:GO_1904453 positive regulation of H,K-ATPase activity obo:GO_1904453 positive regulation of hydrogen/potassium-exchanging ATPase activity obo:GO_1904453 positive regulation of hydrogen:potassium exchanging ATPase activity obo:GO_1904453 positive regulation of hydrogen:potassium-exchanging ATPase activity obo:GO_1904453 up regulation of (K+ + H+)-ATPase activity obo:GO_1904453 up regulation of ATP phosphohydrolase (H+/K+-exchanging) obo:GO_1904453 up regulation of H(+)/K(+)-ATPase activity obo:GO_1904453 up regulation of H(+)/K(+)-exchanging ATPase activity obo:GO_1904453 up regulation of H+-K+-ATPase activity obo:GO_1904453 up regulation of H+/K+-ATPase activity obo:GO_1904453 up regulation of H+/K+-exchanging ATPase activity obo:GO_1904453 up regulation of H,K-ATPase activity obo:GO_1904453 up regulation of hydrogen/potassium-exchanging ATPase activity obo:GO_1904453 up regulation of hydrogen:potassium exchanging ATPase activity obo:GO_1904453 up regulation of hydrogen:potassium-exchanging ATPase activity obo:GO_1904453 up-regulation of (K+ + H+)-ATPase activity obo:GO_1904453 up-regulation of ATP phosphohydrolase (H+/K+-exchanging) obo:GO_1904453 up-regulation of H(+)/K(+)-ATPase activity obo:GO_1904453 up-regulation of H(+)/K(+)-exchanging ATPase activity obo:GO_1904453 up-regulation of H+-K+-ATPase activity obo:GO_1904453 up-regulation of H+/K+-ATPase activity obo:GO_1904453 up-regulation of H+/K+-exchanging ATPase activity obo:GO_1904453 up-regulation of H,K-ATPase activity obo:GO_1904453 up-regulation of hydrogen/potassium-exchanging ATPase activity obo:GO_1904453 up-regulation of hydrogen:potassium exchanging ATPase activity obo:GO_1904453 up-regulation of hydrogen:potassium-exchanging ATPase activity obo:GO_1904453 upregulation of (K+ + H+)-ATPase activity obo:GO_1904453 upregulation of ATP phosphohydrolase (H+/K+-exchanging) obo:GO_1904453 upregulation of H(+)/K(+)-ATPase activity obo:GO_1904453 upregulation of H(+)/K(+)-exchanging ATPase activity obo:GO_1904453 upregulation of H+-K+-ATPase activity obo:GO_1904453 upregulation of H+/K+-ATPase activity obo:GO_1904453 upregulation of H+/K+-exchanging ATPase activity obo:GO_1904453 upregulation of H,K-ATPase activity obo:GO_1904453 upregulation of hydrogen/potassium-exchanging ATPase activity obo:GO_1904453 upregulation of hydrogen:potassium exchanging ATPase activity obo:GO_1904453 upregulation of hydrogen:potassium-exchanging ATPase activity obo:GO_1904453 activation of (K+ + H+)-ATPase activity obo:GO_1904453 activation of ATP phosphohydrolase (H+/K+-exchanging) obo:GO_1904453 activation of H(+)/K(+)-ATPase activity obo:GO_1904453 activation of H(+)/K(+)-exchanging ATPase activity obo:GO_1904453 activation of H+-K+-ATPase activity obo:GO_1904453 activation of H+/K+-ATPase activity obo:GO_1904453 activation of H+/K+-exchanging ATPase activity obo:GO_1904453 activation of H,K-ATPase activity obo:GO_1904453 activation of gastric H(+)/K(+) ATPase activity obo:GO_1904453 activation of gastric H+/K+ ATPase obo:GO_1904453 activation of hydrogen/potassium-exchanging ATPase activity obo:GO_1904453 activation of hydrogen:potassium exchanging ATPase activity obo:GO_1904453 activation of hydrogen:potassium-exchanging ATPase activity obo:GO_1904453 positive regulation of gastric H(+)/K(+) ATPase activity obo:GO_1904453 positive regulation of gastric H+/K+ ATPase obo:GO_1904453 up regulation of gastric H(+)/K(+) ATPase activity obo:GO_1904453 up regulation of gastric H+/K+ ATPase obo:GO_1904453 up-regulation of gastric H(+)/K(+) ATPase activity obo:GO_1904453 up-regulation of gastric H+/K+ ATPase obo:GO_1904453 upregulation of gastric H(+)/K(+) ATPase activity obo:GO_1904453 upregulation of gastric H+/K+ ATPase obo:GO_1904453 biological_process obo:GO_1904453 GO:1904453 obo:GO_1904453 positive regulation of potassium:proton exchanging ATPase activity obo:GO_1904492 Interacting selectively and non-covalently with Ac-Asp-Glu. obo:GO_1904492 obo:go.owl obo:GO_1904492 hal obo:GO_1904492 2015-07-20T10:32:49Z obo:GO_1904492 molecular_function obo:GO_1904492 GO:1904492 obo:GO_1904492 Ac-Asp-Glu binding obo:GO_1904508 Any process that modulates the frequency, rate or extent of protein localization to basolateral plasma membrane. obo:GO_1904508 obo:go.owl obo:GO_1904508 kmv obo:GO_1904508 2015-07-24T17:56:26Z obo:GO_1904508 regulation of protein localisation in basolateral plasma membrane obo:GO_1904508 regulation of protein localisation to basolateral plasma membrane obo:GO_1904508 regulation of protein localization in basolateral plasma membrane obo:GO_1904508 biological_process obo:GO_1904508 GO:1904508 obo:GO_1904508 regulation of protein localization to basolateral plasma membrane obo:GO_1904509 Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to basolateral plasma membrane. obo:GO_1904509 obo:go.owl obo:GO_1904509 kmv obo:GO_1904509 2015-07-24T17:56:32Z obo:GO_1904509 down regulation of protein localisation in basolateral plasma membrane obo:GO_1904509 down regulation of protein localisation to basolateral plasma membrane obo:GO_1904509 down regulation of protein localization in basolateral plasma membrane obo:GO_1904509 down regulation of protein localization to basolateral plasma membrane obo:GO_1904509 down-regulation of protein localisation in basolateral plasma membrane obo:GO_1904509 down-regulation of protein localisation to basolateral plasma membrane obo:GO_1904509 down-regulation of protein localization in basolateral plasma membrane obo:GO_1904509 down-regulation of protein localization to basolateral plasma membrane obo:GO_1904509 downregulation of protein localisation in basolateral plasma membrane obo:GO_1904509 downregulation of protein localisation to basolateral plasma membrane obo:GO_1904509 downregulation of protein localization in basolateral plasma membrane obo:GO_1904509 downregulation of protein localization to basolateral plasma membrane obo:GO_1904509 negative regulation of protein localisation in basolateral plasma membrane obo:GO_1904509 negative regulation of protein localisation to basolateral plasma membrane obo:GO_1904509 negative regulation of protein localization in basolateral plasma membrane obo:GO_1904509 inhibition of protein localisation in basolateral plasma membrane obo:GO_1904509 inhibition of protein localisation to basolateral plasma membrane obo:GO_1904509 inhibition of protein localization in basolateral plasma membrane obo:GO_1904509 inhibition of protein localization to basolateral plasma membrane obo:GO_1904509 biological_process obo:GO_1904509 GO:1904509 obo:GO_1904509 negative regulation of protein localization to basolateral plasma membrane obo:GO_1904510 Any process that activates or increases the frequency, rate or extent of protein localization to basolateral plasma membrane. obo:GO_1904510 obo:go.owl obo:GO_1904510 kmv obo:GO_1904510 2015-07-24T17:56:38Z obo:GO_1904510 positive regulation of protein localisation in basolateral plasma membrane obo:GO_1904510 positive regulation of protein localisation to basolateral plasma membrane obo:GO_1904510 positive regulation of protein localization in basolateral plasma membrane obo:GO_1904510 up regulation of protein localisation in basolateral plasma membrane obo:GO_1904510 up regulation of protein localisation to basolateral plasma membrane obo:GO_1904510 up regulation of protein localization in basolateral plasma membrane obo:GO_1904510 up regulation of protein localization to basolateral plasma membrane obo:GO_1904510 up-regulation of protein localisation in basolateral plasma membrane obo:GO_1904510 up-regulation of protein localisation to basolateral plasma membrane obo:GO_1904510 up-regulation of protein localization in basolateral plasma membrane obo:GO_1904510 up-regulation of protein localization to basolateral plasma membrane obo:GO_1904510 upregulation of protein localisation in basolateral plasma membrane obo:GO_1904510 upregulation of protein localisation to basolateral plasma membrane obo:GO_1904510 upregulation of protein localization in basolateral plasma membrane obo:GO_1904510 upregulation of protein localization to basolateral plasma membrane obo:GO_1904510 activation of protein localisation in basolateral plasma membrane obo:GO_1904510 activation of protein localisation to basolateral plasma membrane obo:GO_1904510 activation of protein localization in basolateral plasma membrane obo:GO_1904510 activation of protein localization to basolateral plasma membrane obo:GO_1904510 biological_process obo:GO_1904510 GO:1904510 obo:GO_1904510 positive regulation of protein localization to basolateral plasma membrane obo:GO_1904536 Any process that modulates the frequency, rate or extent of mitotic telomere tethering at nuclear periphery. obo:GO_1904536 obo:go.owl obo:GO_1904536 al obo:GO_1904536 2015-08-04T14:24:26Z obo:GO_1904536 biological_process obo:GO_1904536 GO:1904536 obo:GO_1904536 regulation of mitotic telomere tethering at nuclear periphery obo:GO_1904537 Any process that stops, prevents or reduces the frequency, rate or extent of mitotic telomere tethering at nuclear periphery. obo:GO_1904537 obo:go.owl obo:GO_1904537 al obo:GO_1904537 2015-08-04T14:24:32Z obo:GO_1904537 down regulation of mitotic telomere tethering at nuclear periphery obo:GO_1904537 down-regulation of mitotic telomere tethering at nuclear periphery obo:GO_1904537 downregulation of mitotic telomere tethering at nuclear periphery obo:GO_1904537 inhibition of mitotic telomere tethering at nuclear periphery obo:GO_1904537 biological_process obo:GO_1904537 GO:1904537 obo:GO_1904537 negative regulation of mitotic telomere tethering at nuclear periphery obo:GO_1904552 Any process that modulates the frequency, rate or extent of chemotaxis to arachidonic acid. obo:GO_1904552 obo:go.owl obo:GO_1904552 sl obo:GO_1904552 2015-08-13T21:08:14Z obo:GO_1904552 biological_process obo:GO_1904552 GO:1904552 obo:GO_1904552 regulation of chemotaxis to arachidonic acid obo:GO_1904553 Any process that stops, prevents or reduces the frequency, rate or extent of chemotaxis to arachidonic acid. obo:GO_1904553 obo:go.owl obo:GO_1904553 sl obo:GO_1904553 2015-08-13T21:08:20Z obo:GO_1904553 down regulation of chemotaxis to arachidonic acid obo:GO_1904553 down-regulation of chemotaxis to arachidonic acid obo:GO_1904553 downregulation of chemotaxis to arachidonic acid obo:GO_1904553 inhibition of chemotaxis to arachidonic acid obo:GO_1904553 biological_process obo:GO_1904553 GO:1904553 obo:GO_1904553 negative regulation of chemotaxis to arachidonic acid obo:GO_1904554 Any process that activates or increases the frequency, rate or extent of chemotaxis to arachidonic acid. obo:GO_1904554 obo:go.owl obo:GO_1904554 sl obo:GO_1904554 2015-08-13T21:08:27Z obo:GO_1904554 up regulation of chemotaxis to arachidonic acid obo:GO_1904554 up-regulation of chemotaxis to arachidonic acid obo:GO_1904554 upregulation of chemotaxis to arachidonic acid obo:GO_1904554 activation of chemotaxis to arachidonic acid obo:GO_1904554 biological_process obo:GO_1904554 GO:1904554 obo:GO_1904554 positive regulation of chemotaxis to arachidonic acid obo:GO_1904576 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a tunicamycin stimulus. obo:GO_1904576 obo:go.owl obo:GO_1904576 sl obo:GO_1904576 2015-08-19T18:01:52Z obo:GO_1904576 biological_process obo:GO_1904576 GO:1904576 obo:GO_1904576 response to tunicamycin obo:GO_1904577 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a tunicamycin stimulus. obo:GO_1904577 obo:go.owl obo:GO_1904577 sl obo:GO_1904577 2015-08-19T18:01:58Z obo:GO_1904577 biological_process obo:GO_1904577 GO:1904577 obo:GO_1904577 cellular response to tunicamycin obo:GO_1904580 Any process that modulates the frequency, rate or extent of intracellular mRNA localization. obo:GO_1904580 obo:go.owl obo:GO_1904580 sl obo:GO_1904580 2015-08-19T23:40:25Z obo:GO_1904580 regulation of establishment and maintenance of intracellular RNA localization obo:GO_1904580 regulation of intracellular mRNA localisation obo:GO_1904580 regulation of mRNA localization, intracellular obo:GO_1904580 regulation of intracellular mRNA positioning obo:GO_1904580 regulation of mRNA positioning, intracellular obo:GO_1904580 biological_process obo:GO_1904580 GO:1904580 obo:GO_1904580 regulation of intracellular mRNA localization obo:GO_1904581 Any process that stops, prevents or reduces the frequency, rate or extent of intracellular mRNA localization. obo:GO_1904581 obo:go.owl obo:GO_1904581 sl obo:GO_1904581 2015-08-19T23:40:32Z obo:GO_1904581 down regulation of establishment and maintenance of intracellular RNA localization obo:GO_1904581 down regulation of intracellular mRNA localisation obo:GO_1904581 down regulation of intracellular mRNA localization obo:GO_1904581 down regulation of mRNA localization, intracellular obo:GO_1904581 down-regulation of establishment and maintenance of intracellular RNA localization obo:GO_1904581 down-regulation of intracellular mRNA localisation obo:GO_1904581 down-regulation of intracellular mRNA localization obo:GO_1904581 down-regulation of mRNA localization, intracellular obo:GO_1904581 downregulation of establishment and maintenance of intracellular RNA localization obo:GO_1904581 downregulation of intracellular mRNA localisation obo:GO_1904581 downregulation of intracellular mRNA localization obo:GO_1904581 downregulation of mRNA localization, intracellular obo:GO_1904581 negative regulation of establishment and maintenance of intracellular RNA localization obo:GO_1904581 negative regulation of intracellular mRNA localisation obo:GO_1904581 negative regulation of mRNA localization, intracellular obo:GO_1904581 down regulation of intracellular mRNA positioning obo:GO_1904581 down regulation of mRNA positioning, intracellular obo:GO_1904581 down-regulation of intracellular mRNA positioning obo:GO_1904581 down-regulation of mRNA positioning, intracellular obo:GO_1904581 downregulation of intracellular mRNA positioning obo:GO_1904581 downregulation of mRNA positioning, intracellular obo:GO_1904581 inhibition of establishment and maintenance of intracellular RNA localization obo:GO_1904581 inhibition of intracellular mRNA localisation obo:GO_1904581 inhibition of intracellular mRNA localization obo:GO_1904581 inhibition of intracellular mRNA positioning obo:GO_1904581 inhibition of mRNA localization, intracellular obo:GO_1904581 inhibition of mRNA positioning, intracellular obo:GO_1904581 negative regulation of intracellular mRNA positioning obo:GO_1904581 negative regulation of mRNA positioning, intracellular obo:GO_1904581 biological_process obo:GO_1904581 GO:1904581 obo:GO_1904581 negative regulation of intracellular mRNA localization obo:GO_1904582 Any process that activates or increases the frequency, rate or extent of intracellular mRNA localization. obo:GO_1904582 obo:go.owl obo:GO_1904582 sl obo:GO_1904582 2015-08-19T23:40:38Z obo:GO_1904582 positive regulation of establishment and maintenance of intracellular RNA localization obo:GO_1904582 positive regulation of intracellular mRNA localisation obo:GO_1904582 positive regulation of mRNA localization, intracellular obo:GO_1904582 up regulation of establishment and maintenance of intracellular RNA localization obo:GO_1904582 up regulation of intracellular mRNA localisation obo:GO_1904582 up regulation of intracellular mRNA localization obo:GO_1904582 up regulation of mRNA localization, intracellular obo:GO_1904582 up-regulation of establishment and maintenance of intracellular RNA localization obo:GO_1904582 up-regulation of intracellular mRNA localisation obo:GO_1904582 up-regulation of intracellular mRNA localization obo:GO_1904582 up-regulation of mRNA localization, intracellular obo:GO_1904582 upregulation of establishment and maintenance of intracellular RNA localization obo:GO_1904582 upregulation of intracellular mRNA localisation obo:GO_1904582 upregulation of intracellular mRNA localization obo:GO_1904582 upregulation of mRNA localization, intracellular obo:GO_1904582 activation of establishment and maintenance of intracellular RNA localization obo:GO_1904582 activation of intracellular mRNA localisation obo:GO_1904582 activation of intracellular mRNA localization obo:GO_1904582 activation of intracellular mRNA positioning obo:GO_1904582 activation of mRNA localization, intracellular obo:GO_1904582 activation of mRNA positioning, intracellular obo:GO_1904582 positive regulation of intracellular mRNA positioning obo:GO_1904582 positive regulation of mRNA positioning, intracellular obo:GO_1904582 up regulation of intracellular mRNA positioning obo:GO_1904582 up regulation of mRNA positioning, intracellular obo:GO_1904582 up-regulation of intracellular mRNA positioning obo:GO_1904582 up-regulation of mRNA positioning, intracellular obo:GO_1904582 upregulation of intracellular mRNA positioning obo:GO_1904582 upregulation of mRNA positioning, intracellular obo:GO_1904582 biological_process obo:GO_1904582 GO:1904582 obo:GO_1904582 positive regulation of intracellular mRNA localization obo:GO_1904592 Any process that activates or increases the frequency, rate or extent of protein refolding. obo:GO_1904592 obo:go.owl obo:GO_1904592 sl obo:GO_1904592 2015-08-21T18:11:16Z obo:GO_1904592 up regulation of protein refolding obo:GO_1904592 up-regulation of protein refolding obo:GO_1904592 upregulation of protein refolding obo:GO_1904592 activation of protein refolding obo:GO_1904592 biological_process obo:GO_1904592 activation of heat shock protein activity obo:GO_1904592 positive regulation of heat shock protein activity obo:GO_1904592 up regulation of heat shock protein activity obo:GO_1904592 up-regulation of heat shock protein activity obo:GO_1904592 upregulation of heat shock protein activity obo:GO_1904592 GO:1904592 obo:GO_1904592 positive regulation of protein refolding obo:GO_1904593 Interacting selectively and non-covalently with prostaglandin. obo:GO_1904593 obo:go.owl obo:GO_1904593 sl obo:GO_1904593 2015-08-21T18:53:31Z obo:GO_1904593 molecular_function obo:GO_1904593 GO:1904593 obo:GO_1904593 prostaglandin binding obo:GO_1904599 Interacting selectively and non-covalently with advanced glycation end-product. obo:GO_1904599 obo:go.owl obo:GO_1904599 krc obo:GO_1904599 2015-08-25T23:39:32Z obo:GO_1904599 molecular_function obo:GO_1904599 GO:1904599 obo:GO_1904599 advanced glycation end-product binding obo:GO_1904608 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a monosodium L-glutamate stimulus. obo:GO_1904608 obo:go.owl obo:GO_1904608 sl obo:GO_1904608 2015-08-27T18:43:08Z obo:GO_1904608 biological_process obo:GO_1904608 GO:1904608 obo:GO_1904608 response to monosodium L-glutamate obo:GO_1904609 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a monosodium L-glutamate stimulus. obo:GO_1904609 obo:go.owl obo:GO_1904609 sl obo:GO_1904609 2015-08-27T18:43:14Z obo:GO_1904609 biological_process obo:GO_1904609 GO:1904609 obo:GO_1904609 cellular response to monosodium L-glutamate obo:GO_1904614 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a biphenyl stimulus. obo:GO_1904614 obo:go.owl obo:GO_1904614 sl obo:GO_1904614 2015-08-27T19:08:43Z obo:GO_1904614 biological_process obo:GO_1904614 GO:1904614 obo:GO_1904614 response to biphenyl obo:GO_1904615 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a biphenyl stimulus. obo:GO_1904615 obo:go.owl obo:GO_1904615 sl obo:GO_1904615 2015-08-27T19:08:49Z obo:GO_1904615 biological_process obo:GO_1904615 GO:1904615 obo:GO_1904615 cellular response to biphenyl obo:GO_1904643 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a curcumin stimulus. obo:GO_1904643 obo:go.owl obo:GO_1904643 sl obo:GO_1904643 2015-08-31T20:38:11Z obo:GO_1904643 biological_process obo:GO_1904643 GO:1904643 obo:GO_1904643 response to curcumin obo:GO_1904644 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a curcumin stimulus. obo:GO_1904644 obo:go.owl obo:GO_1904644 sl obo:GO_1904644 2015-08-31T20:38:17Z obo:GO_1904644 biological_process obo:GO_1904644 GO:1904644 obo:GO_1904644 cellular response to curcumin obo:GO_1904669 The directed movement of ATP out of a cell or organelle. obo:GO_1904669 obo:go.owl obo:GO_1904669 tb obo:GO_1904669 2015-09-09T16:33:06Z obo:GO_1904669 biological_process obo:GO_1904669 ATP efflux obo:GO_1904669 GO:1904669 obo:GO_1904669 ATP export obo:GO_1904678 Interacting selectively and non-covalently with alpha-aminoacyl-tRNA. obo:GO_1904678 obo:go.owl obo:GO_1904678 hjd obo:GO_1904678 2015-09-18T16:44:17Z obo:GO_1904678 molecular_function obo:GO_1904678 aminoacyl-tRNA binding obo:GO_1904678 GO:1904678 obo:GO_1904678 alpha-aminoacyl-tRNA binding obo:GO_1904691 Any process that stops, prevents or reduces the frequency, rate or extent of type B pancreatic cell proliferation. obo:GO_1904691 obo:go.owl obo:GO_1904691 sl obo:GO_1904691 2015-09-25T15:23:38Z obo:GO_1904691 down regulation of pancreatic B cell proliferation obo:GO_1904691 down regulation of pancreatic beta cell proliferation obo:GO_1904691 down regulation of type B pancreatic cell proliferation obo:GO_1904691 down-regulation of pancreatic B cell proliferation obo:GO_1904691 down-regulation of pancreatic beta cell proliferation obo:GO_1904691 down-regulation of type B pancreatic cell proliferation obo:GO_1904691 downregulation of pancreatic B cell proliferation obo:GO_1904691 downregulation of pancreatic beta cell proliferation obo:GO_1904691 downregulation of type B pancreatic cell proliferation obo:GO_1904691 negative regulation of pancreatic B cell proliferation obo:GO_1904691 negative regulation of pancreatic beta cell proliferation obo:GO_1904691 inhibition of pancreatic B cell proliferation obo:GO_1904691 inhibition of pancreatic beta cell proliferation obo:GO_1904691 inhibition of type B pancreatic cell proliferation obo:GO_1904691 biological_process obo:GO_1904691 GO:1904691 obo:GO_1904691 negative regulation of type B pancreatic cell proliferation obo:GO_1904692 Any process that activates or increases the frequency, rate or extent of type B pancreatic cell proliferation. obo:GO_1904692 obo:go.owl obo:GO_1904692 sl obo:GO_1904692 2015-09-25T15:23:44Z obo:GO_1904692 positive regulation of pancreatic B cell proliferation obo:GO_1904692 positive regulation of pancreatic beta cell proliferation obo:GO_1904692 up regulation of pancreatic B cell proliferation obo:GO_1904692 up regulation of pancreatic beta cell proliferation obo:GO_1904692 up regulation of type B pancreatic cell proliferation obo:GO_1904692 up-regulation of pancreatic B cell proliferation obo:GO_1904692 up-regulation of pancreatic beta cell proliferation obo:GO_1904692 up-regulation of type B pancreatic cell proliferation obo:GO_1904692 upregulation of pancreatic B cell proliferation obo:GO_1904692 upregulation of pancreatic beta cell proliferation obo:GO_1904692 upregulation of type B pancreatic cell proliferation obo:GO_1904692 activation of pancreatic B cell proliferation obo:GO_1904692 activation of pancreatic beta cell proliferation obo:GO_1904692 activation of type B pancreatic cell proliferation obo:GO_1904692 biological_process obo:GO_1904692 GO:1904692 obo:GO_1904692 positive regulation of type B pancreatic cell proliferation obo:GO_1904697 Any process that modulates the frequency, rate or extent of acinar cell proliferation. obo:GO_1904697 obo:go.owl obo:GO_1904697 sl obo:GO_1904697 2015-09-30T15:19:50Z obo:GO_1904697 regulation of acinic cell proliferation obo:GO_1904697 regulation of acinous cell proliferation obo:GO_1904697 biological_process obo:GO_1904697 GO:1904697 obo:GO_1904697 regulation of acinar cell proliferation obo:GO_1904698 Any process that stops, prevents or reduces the frequency, rate or extent of acinar cell proliferation. obo:GO_1904698 obo:go.owl obo:GO_1904698 sl obo:GO_1904698 2015-09-30T15:19:57Z obo:GO_1904698 down regulation of acinar cell proliferation obo:GO_1904698 down regulation of acinic cell proliferation obo:GO_1904698 down regulation of acinous cell proliferation obo:GO_1904698 down-regulation of acinar cell proliferation obo:GO_1904698 down-regulation of acinic cell proliferation obo:GO_1904698 down-regulation of acinous cell proliferation obo:GO_1904698 downregulation of acinar cell proliferation obo:GO_1904698 downregulation of acinic cell proliferation obo:GO_1904698 downregulation of acinous cell proliferation obo:GO_1904698 negative regulation of acinic cell proliferation obo:GO_1904698 negative regulation of acinous cell proliferation obo:GO_1904698 inhibition of acinar cell proliferation obo:GO_1904698 inhibition of acinic cell proliferation obo:GO_1904698 inhibition of acinous cell proliferation obo:GO_1904698 biological_process obo:GO_1904698 GO:1904698 obo:GO_1904698 negative regulation of acinar cell proliferation obo:GO_1904699 Any process that activates or increases the frequency, rate or extent of acinar cell proliferation. obo:GO_1904699 obo:go.owl obo:GO_1904699 sl obo:GO_1904699 2015-09-30T15:20:03Z obo:GO_1904699 positive regulation of acinic cell proliferation obo:GO_1904699 positive regulation of acinous cell proliferation obo:GO_1904699 up regulation of acinar cell proliferation obo:GO_1904699 up regulation of acinic cell proliferation obo:GO_1904699 up regulation of acinous cell proliferation obo:GO_1904699 up-regulation of acinar cell proliferation obo:GO_1904699 up-regulation of acinic cell proliferation obo:GO_1904699 up-regulation of acinous cell proliferation obo:GO_1904699 upregulation of acinar cell proliferation obo:GO_1904699 upregulation of acinic cell proliferation obo:GO_1904699 upregulation of acinous cell proliferation obo:GO_1904699 activation of acinar cell proliferation obo:GO_1904699 activation of acinic cell proliferation obo:GO_1904699 activation of acinous cell proliferation obo:GO_1904699 biological_process obo:GO_1904699 GO:1904699 obo:GO_1904699 positive regulation of acinar cell proliferation obo:GO_1904702 Any process that modulates the frequency, rate or extent of protein localization to cell-cell adherens junction. obo:GO_1904702 obo:go.owl obo:GO_1904702 kmv obo:GO_1904702 2015-10-01T15:11:49Z obo:GO_1904702 regulation of protein localisation in cell-cell adherens junction obo:GO_1904702 regulation of protein localisation to cell-cell adherens junction obo:GO_1904702 regulation of protein localization in cell-cell adherens junction obo:GO_1904702 biological_process obo:GO_1904702 GO:1904702 obo:GO_1904702 regulation of protein localization to cell-cell adherens junction obo:GO_1904703 Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to cell-cell adherens junction. obo:GO_1904703 obo:go.owl obo:GO_1904703 kmv obo:GO_1904703 2015-10-01T15:11:56Z obo:GO_1904703 down regulation of protein localisation in cell-cell adherens junction obo:GO_1904703 down regulation of protein localisation to cell-cell adherens junction obo:GO_1904703 down regulation of protein localization in cell-cell adherens junction obo:GO_1904703 down regulation of protein localization to cell-cell adherens junction obo:GO_1904703 down-regulation of protein localisation in cell-cell adherens junction obo:GO_1904703 down-regulation of protein localisation to cell-cell adherens junction obo:GO_1904703 down-regulation of protein localization in cell-cell adherens junction obo:GO_1904703 down-regulation of protein localization to cell-cell adherens junction obo:GO_1904703 downregulation of protein localisation in cell-cell adherens junction obo:GO_1904703 downregulation of protein localisation to cell-cell adherens junction obo:GO_1904703 downregulation of protein localization in cell-cell adherens junction obo:GO_1904703 downregulation of protein localization to cell-cell adherens junction obo:GO_1904703 negative regulation of protein localisation in cell-cell adherens junction obo:GO_1904703 negative regulation of protein localisation to cell-cell adherens junction obo:GO_1904703 negative regulation of protein localization in cell-cell adherens junction obo:GO_1904703 inhibition of protein localisation in cell-cell adherens junction obo:GO_1904703 inhibition of protein localisation to cell-cell adherens junction obo:GO_1904703 inhibition of protein localization in cell-cell adherens junction obo:GO_1904703 inhibition of protein localization to cell-cell adherens junction obo:GO_1904703 biological_process obo:GO_1904703 GO:1904703 obo:GO_1904703 negative regulation of protein localization to cell-cell adherens junction obo:GO_1904704 Any process that activates or increases the frequency, rate or extent of protein localization to cell-cell adherens junction. obo:GO_1904704 obo:go.owl obo:GO_1904704 kmv obo:GO_1904704 2015-10-01T15:12:02Z obo:GO_1904704 positive regulation of protein localisation in cell-cell adherens junction obo:GO_1904704 positive regulation of protein localisation to cell-cell adherens junction obo:GO_1904704 positive regulation of protein localization in cell-cell adherens junction obo:GO_1904704 up regulation of protein localisation in cell-cell adherens junction obo:GO_1904704 up regulation of protein localisation to cell-cell adherens junction obo:GO_1904704 up regulation of protein localization in cell-cell adherens junction obo:GO_1904704 up regulation of protein localization to cell-cell adherens junction obo:GO_1904704 up-regulation of protein localisation in cell-cell adherens junction obo:GO_1904704 up-regulation of protein localisation to cell-cell adherens junction obo:GO_1904704 up-regulation of protein localization in cell-cell adherens junction obo:GO_1904704 up-regulation of protein localization to cell-cell adherens junction obo:GO_1904704 upregulation of protein localisation in cell-cell adherens junction obo:GO_1904704 upregulation of protein localisation to cell-cell adherens junction obo:GO_1904704 upregulation of protein localization in cell-cell adherens junction obo:GO_1904704 upregulation of protein localization to cell-cell adherens junction obo:GO_1904704 activation of protein localisation in cell-cell adherens junction obo:GO_1904704 activation of protein localisation to cell-cell adherens junction obo:GO_1904704 activation of protein localization in cell-cell adherens junction obo:GO_1904704 activation of protein localization to cell-cell adherens junction obo:GO_1904704 biological_process obo:GO_1904704 GO:1904704 obo:GO_1904704 positive regulation of protein localization to cell-cell adherens junction obo:GO_1904705 Any process that modulates the frequency, rate or extent of vascular smooth muscle cell proliferation. obo:GO_1904705 obo:go.owl obo:GO_1904705 sl obo:GO_1904705 2015-10-01T16:05:20Z obo:GO_1904705 regulation of VSMC proliferation obo:GO_1904705 biological_process obo:GO_1904705 GO:1904705 obo:GO_1904705 regulation of vascular smooth muscle cell proliferation obo:GO_1904706 Any process that stops, prevents or reduces the frequency, rate or extent of vascular smooth muscle cell proliferation. obo:GO_1904706 obo:go.owl obo:GO_1904706 sl obo:GO_1904706 2015-10-01T16:05:26Z obo:GO_1904706 down regulation of VSMC proliferation obo:GO_1904706 down regulation of vascular smooth muscle cell proliferation obo:GO_1904706 down-regulation of VSMC proliferation obo:GO_1904706 down-regulation of vascular smooth muscle cell proliferation obo:GO_1904706 downregulation of VSMC proliferation obo:GO_1904706 downregulation of vascular smooth muscle cell proliferation obo:GO_1904706 negative regulation of VSMC proliferation obo:GO_1904706 inhibition of VSMC proliferation obo:GO_1904706 inhibition of vascular smooth muscle cell proliferation obo:GO_1904706 biological_process obo:GO_1904706 GO:1904706 obo:GO_1904706 negative regulation of vascular smooth muscle cell proliferation obo:GO_1904707 Any process that activates or increases the frequency, rate or extent of vascular smooth muscle cell proliferation. obo:GO_1904707 obo:go.owl obo:GO_1904707 sl obo:GO_1904707 2015-10-01T16:05:32Z obo:GO_1904707 positive regulation of VSMC proliferation obo:GO_1904707 up regulation of VSMC proliferation obo:GO_1904707 up regulation of vascular smooth muscle cell proliferation obo:GO_1904707 up-regulation of VSMC proliferation obo:GO_1904707 up-regulation of vascular smooth muscle cell proliferation obo:GO_1904707 upregulation of VSMC proliferation obo:GO_1904707 upregulation of vascular smooth muscle cell proliferation obo:GO_1904707 activation of VSMC proliferation obo:GO_1904707 activation of vascular smooth muscle cell proliferation obo:GO_1904707 biological_process obo:GO_1904707 GO:1904707 obo:GO_1904707 positive regulation of vascular smooth muscle cell proliferation obo:GO_1904713 Interacting selectively and non-covalently with a beta-catenin destruction complex. obo:GO_1904713 obo:go.owl obo:GO_1904713 bf obo:GO_1904713 2015-10-05T14:34:14Z obo:GO_1904713 APC-Axin-1-beta-catenin complex binding obo:GO_1904713 Axin-APC-beta-catenin-GSK3B complex binding obo:GO_1904713 BDC binding obo:GO_1904713 beta-catenin degradation complex binding obo:GO_1904713 23S APC complex binding obo:GO_1904713 molecular_function obo:GO_1904713 GO:1904713 obo:GO_1904713 beta-catenin destruction complex binding obo:GO_1904749 Any process that modulates the frequency, rate or extent of protein localization to nucleolus. obo:GO_1904749 obo:go.owl obo:GO_1904749 nc obo:GO_1904749 2015-10-19T15:16:17Z obo:GO_1904749 regulation of protein localisation in nucleolus obo:GO_1904749 regulation of protein localisation to nucleolus obo:GO_1904749 regulation of protein localization in nucleolus obo:GO_1904749 biological_process obo:GO_1904749 GO:1904749 obo:GO_1904749 regulation of protein localization to nucleolus obo:GO_1904750 Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to nucleolus. obo:GO_1904750 obo:go.owl obo:GO_1904750 nc obo:GO_1904750 2015-10-19T15:16:24Z obo:GO_1904750 down regulation of protein localisation in nucleolus obo:GO_1904750 down regulation of protein localisation to nucleolus obo:GO_1904750 down regulation of protein localization in nucleolus obo:GO_1904750 down regulation of protein localization to nucleolus obo:GO_1904750 down-regulation of protein localisation in nucleolus obo:GO_1904750 down-regulation of protein localisation to nucleolus obo:GO_1904750 down-regulation of protein localization in nucleolus obo:GO_1904750 down-regulation of protein localization to nucleolus obo:GO_1904750 downregulation of protein localisation in nucleolus obo:GO_1904750 downregulation of protein localisation to nucleolus obo:GO_1904750 downregulation of protein localization in nucleolus obo:GO_1904750 downregulation of protein localization to nucleolus obo:GO_1904750 negative regulation of protein localisation in nucleolus obo:GO_1904750 negative regulation of protein localisation to nucleolus obo:GO_1904750 negative regulation of protein localization in nucleolus obo:GO_1904750 inhibition of protein localisation in nucleolus obo:GO_1904750 inhibition of protein localisation to nucleolus obo:GO_1904750 inhibition of protein localization in nucleolus obo:GO_1904750 inhibition of protein localization to nucleolus obo:GO_1904750 biological_process obo:GO_1904750 GO:1904750 obo:GO_1904750 negative regulation of protein localization to nucleolus obo:GO_1904751 Any process that activates or increases the frequency, rate or extent of protein localization to nucleolus. obo:GO_1904751 obo:go.owl obo:GO_1904751 nc obo:GO_1904751 2015-10-19T15:16:30Z obo:GO_1904751 positive regulation of protein localisation in nucleolus obo:GO_1904751 positive regulation of protein localisation to nucleolus obo:GO_1904751 positive regulation of protein localization in nucleolus obo:GO_1904751 up regulation of protein localisation in nucleolus obo:GO_1904751 up regulation of protein localisation to nucleolus obo:GO_1904751 up regulation of protein localization in nucleolus obo:GO_1904751 up regulation of protein localization to nucleolus obo:GO_1904751 up-regulation of protein localisation in nucleolus obo:GO_1904751 up-regulation of protein localisation to nucleolus obo:GO_1904751 up-regulation of protein localization in nucleolus obo:GO_1904751 up-regulation of protein localization to nucleolus obo:GO_1904751 upregulation of protein localisation in nucleolus obo:GO_1904751 upregulation of protein localisation to nucleolus obo:GO_1904751 upregulation of protein localization in nucleolus obo:GO_1904751 upregulation of protein localization to nucleolus obo:GO_1904751 activation of protein localisation in nucleolus obo:GO_1904751 activation of protein localisation to nucleolus obo:GO_1904751 activation of protein localization in nucleolus obo:GO_1904751 activation of protein localization to nucleolus obo:GO_1904751 biological_process obo:GO_1904751 GO:1904751 obo:GO_1904751 positive regulation of protein localization to nucleolus obo:GO_1904767 Interacting selectively and non-covalently with octanoic acid. obo:GO_1904767 obo:go.owl obo:GO_1904767 kmv obo:GO_1904767 2015-10-27T21:11:49Z obo:GO_1904767 caprylic acid binding obo:GO_1904767 molecular_function obo:GO_1904767 GO:1904767 obo:GO_1904767 octanoic acid binding obo:GO_1904768 Interacting selectively and non-covalently with all-trans-retinol. obo:GO_1904768 obo:go.owl obo:GO_1904768 kmv obo:GO_1904768 2015-10-27T21:14:47Z obo:GO_1904768 molecular_function obo:GO_1904768 GO:1904768 obo:GO_1904768 all-trans-retinol binding obo:GO_1904769 Interacting selectively and non-covalently with isopentadecanoic acid. obo:GO_1904769 obo:go.owl obo:GO_1904769 kmv obo:GO_1904769 2015-10-27T21:33:38Z obo:GO_1904769 13-methylmyristic acid binding obo:GO_1904769 molecular_function obo:GO_1904769 GO:1904769 obo:GO_1904769 isopentadecanoic acid binding obo:GO_1904776 Any process that modulates the frequency, rate or extent of protein localization to cell cortex. obo:GO_1904776 obo:go.owl obo:GO_1904776 es obo:GO_1904776 2015-10-29T16:55:01Z obo:GO_1904776 regulation of protein localisation to cell cortex obo:GO_1904776 biological_process obo:GO_1904776 GO:1904776 obo:GO_1904776 An example is cye-1 in C. elegans, UniProt ID O01501 in PMID:17115027. obo:GO_1904776 regulation of protein localization to cell cortex obo:GO_1904777 Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to cell cortex. obo:GO_1904777 obo:go.owl obo:GO_1904777 es obo:GO_1904777 2015-10-29T16:55:08Z obo:GO_1904777 down regulation of protein localisation to cell cortex obo:GO_1904777 down regulation of protein localization to cell cortex obo:GO_1904777 down-regulation of protein localisation to cell cortex obo:GO_1904777 down-regulation of protein localization to cell cortex obo:GO_1904777 downregulation of protein localisation to cell cortex obo:GO_1904777 downregulation of protein localization to cell cortex obo:GO_1904777 negative regulation of protein localisation to cell cortex obo:GO_1904777 inhibition of protein localisation to cell cortex obo:GO_1904777 inhibition of protein localization to cell cortex obo:GO_1904777 biological_process obo:GO_1904777 GO:1904777 obo:GO_1904777 An example is cye-1 in C. elegans, UniProt ID O01501 in PMID:17115027. obo:GO_1904777 negative regulation of protein localization to cell cortex obo:GO_1904778 Any process that activates or increases the frequency, rate or extent of protein localization to cell cortex. obo:GO_1904778 obo:go.owl obo:GO_1904778 es obo:GO_1904778 2015-10-29T16:55:15Z obo:GO_1904778 positive regulation of protein localisation to cell cortex obo:GO_1904778 up regulation of protein localisation to cell cortex obo:GO_1904778 up regulation of protein localization to cell cortex obo:GO_1904778 up-regulation of protein localisation to cell cortex obo:GO_1904778 up-regulation of protein localization to cell cortex obo:GO_1904778 upregulation of protein localisation to cell cortex obo:GO_1904778 upregulation of protein localization to cell cortex obo:GO_1904778 activation of protein localisation to cell cortex obo:GO_1904778 activation of protein localization to cell cortex obo:GO_1904778 biological_process obo:GO_1904778 GO:1904778 obo:GO_1904778 An example is cye-1 in C. elegans, UniProt ID O01501 in PMID:17115027. obo:GO_1904778 positive regulation of protein localization to cell cortex obo:GO_1904779 Any process that modulates the frequency, rate or extent of protein localization to centrosome. obo:GO_1904779 obo:go.owl obo:GO_1904779 es obo:GO_1904779 2015-10-30T11:54:30Z obo:GO_1904779 regulation of protein localisation to centrosome obo:GO_1904779 biological_process obo:GO_1904779 GO:1904779 obo:GO_1904779 An example is cdk-2 in C. elegans (UniProt ID O61847) in PMID:17115027 (inferred from mutant phenotype). obo:GO_1904779 regulation of protein localization to centrosome obo:GO_1904780 Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to centrosome. obo:GO_1904780 obo:go.owl obo:GO_1904780 es obo:GO_1904780 2015-10-30T11:54:47Z obo:GO_1904780 down regulation of protein localisation to centrosome obo:GO_1904780 down regulation of protein localization to centrosome obo:GO_1904780 down-regulation of protein localisation to centrosome obo:GO_1904780 down-regulation of protein localization to centrosome obo:GO_1904780 downregulation of protein localisation to centrosome obo:GO_1904780 downregulation of protein localization to centrosome obo:GO_1904780 negative regulation of protein localisation to centrosome obo:GO_1904780 inhibition of protein localisation to centrosome obo:GO_1904780 inhibition of protein localization to centrosome obo:GO_1904780 biological_process obo:GO_1904780 GO:1904780 obo:GO_1904780 An example is cdk-2 in C. elegans (UniProt ID O61847) in PMID:17115027 (inferred from mutant phenotype). obo:GO_1904780 negative regulation of protein localization to centrosome obo:GO_1904781 Any process that activates or increases the frequency, rate or extent of protein localization to centrosome. obo:GO_1904781 obo:go.owl obo:GO_1904781 es obo:GO_1904781 2015-10-30T11:54:53Z obo:GO_1904781 positive regulation of protein localisation to centrosome obo:GO_1904781 up regulation of protein localisation to centrosome obo:GO_1904781 up regulation of protein localization to centrosome obo:GO_1904781 up-regulation of protein localisation to centrosome obo:GO_1904781 up-regulation of protein localization to centrosome obo:GO_1904781 upregulation of protein localisation to centrosome obo:GO_1904781 upregulation of protein localization to centrosome obo:GO_1904781 activation of protein localisation to centrosome obo:GO_1904781 activation of protein localization to centrosome obo:GO_1904781 biological_process obo:GO_1904781 GO:1904781 obo:GO_1904781 An example is cdk-2 in C. elegans (UniProt ID O61847) in PMID:17115027 (inferred from mutant phenotype). obo:GO_1904781 positive regulation of protein localization to centrosome obo:GO_1904809 Any process that modulates the frequency, rate or extent of dense core granule transport. obo:GO_1904809 obo:go.owl obo:GO_1904809 es obo:GO_1904809 2015-11-11T10:40:10Z obo:GO_1904809 regulation of dense core vesicle transport obo:GO_1904809 biological_process obo:GO_1904809 GO:1904809 obo:GO_1904809 cdk-5 in C.elegans (G5ECH7) in PMID:22699897 (inferred from mutant phenotype). obo:GO_1904809 regulation of dense core granule transport obo:GO_1904810 Any process that stops, prevents or reduces the frequency, rate or extent of dense core granule transport. obo:GO_1904810 obo:go.owl obo:GO_1904810 es obo:GO_1904810 2015-11-11T10:40:18Z obo:GO_1904810 down regulation of dense core granule transport obo:GO_1904810 down regulation of dense core vesicle transport obo:GO_1904810 down-regulation of dense core granule transport obo:GO_1904810 down-regulation of dense core vesicle transport obo:GO_1904810 downregulation of dense core granule transport obo:GO_1904810 downregulation of dense core vesicle transport obo:GO_1904810 negative regulation of dense core vesicle transport obo:GO_1904810 inhibition of dense core granule transport obo:GO_1904810 inhibition of dense core vesicle transport obo:GO_1904810 biological_process obo:GO_1904810 GO:1904810 obo:GO_1904810 cdk-5 in C.elegans (G5ECH7) in PMID:22699897 (inferred from mutant phenotype). obo:GO_1904810 negative regulation of dense core granule transport obo:GO_1904811 Any process that activates or increases the frequency, rate or extent of dense core granule transport. obo:GO_1904811 obo:go.owl obo:GO_1904811 es obo:GO_1904811 2015-11-11T10:40:25Z obo:GO_1904811 positive regulation of dense core vesicle transport obo:GO_1904811 up regulation of dense core granule transport obo:GO_1904811 up regulation of dense core vesicle transport obo:GO_1904811 up-regulation of dense core granule transport obo:GO_1904811 up-regulation of dense core vesicle transport obo:GO_1904811 upregulation of dense core granule transport obo:GO_1904811 upregulation of dense core vesicle transport obo:GO_1904811 activation of dense core granule transport obo:GO_1904811 activation of dense core vesicle transport obo:GO_1904811 biological_process obo:GO_1904811 GO:1904811 obo:GO_1904811 cdk-5 in C.elegans (G5ECH7) in PMID:22699897 (inferred from mutant phenotype). obo:GO_1904811 positive regulation of dense core granule transport obo:GO_1904814 Any process that modulates the frequency, rate or extent of protein localization to chromosome, telomeric region. obo:GO_1904814 obo:go.owl obo:GO_1904814 nc obo:GO_1904814 2015-11-16T12:18:43Z obo:GO_1904814 regulation of protein localisation to chromosome, telomeric region obo:GO_1904814 regulation of protein localization to telomere obo:GO_1904814 biological_process obo:GO_1904814 GO:1904814 obo:GO_1904814 regulation of protein localization to chromosome, telomeric region obo:GO_1904815 Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to chromosome, telomeric region. obo:GO_1904815 obo:go.owl obo:GO_1904815 nc obo:GO_1904815 2015-11-16T12:18:51Z obo:GO_1904815 down regulation of protein localisation to chromosome, telomeric region obo:GO_1904815 down regulation of protein localization to chromosome, telomeric region obo:GO_1904815 down regulation of protein localization to telomere obo:GO_1904815 down-regulation of protein localisation to chromosome, telomeric region obo:GO_1904815 down-regulation of protein localization to chromosome, telomeric region obo:GO_1904815 down-regulation of protein localization to telomere obo:GO_1904815 downregulation of protein localisation to chromosome, telomeric region obo:GO_1904815 downregulation of protein localization to chromosome, telomeric region obo:GO_1904815 downregulation of protein localization to telomere obo:GO_1904815 negative regulation of protein localisation to chromosome, telomeric region obo:GO_1904815 negative regulation of protein localization to telomere obo:GO_1904815 inhibition of protein localisation to chromosome, telomeric region obo:GO_1904815 inhibition of protein localization to chromosome, telomeric region obo:GO_1904815 inhibition of protein localization to telomere obo:GO_1904815 biological_process obo:GO_1904815 GO:1904815 obo:GO_1904815 negative regulation of protein localization to chromosome, telomeric region obo:GO_1904816 Any process that activates or increases the frequency, rate or extent of protein localization to chromosome, telomeric region. obo:GO_1904816 obo:go.owl obo:GO_1904816 nc obo:GO_1904816 2015-11-16T12:18:58Z obo:GO_1904816 positive regulation of protein localisation to chromosome, telomeric region obo:GO_1904816 positive regulation of protein localization to telomere obo:GO_1904816 up regulation of protein localisation to chromosome, telomeric region obo:GO_1904816 up regulation of protein localization to chromosome, telomeric region obo:GO_1904816 up regulation of protein localization to telomere obo:GO_1904816 up-regulation of protein localisation to chromosome, telomeric region obo:GO_1904816 up-regulation of protein localization to chromosome, telomeric region obo:GO_1904816 up-regulation of protein localization to telomere obo:GO_1904816 upregulation of protein localisation to chromosome, telomeric region obo:GO_1904816 upregulation of protein localization to chromosome, telomeric region obo:GO_1904816 upregulation of protein localization to telomere obo:GO_1904816 activation of protein localisation to chromosome, telomeric region obo:GO_1904816 activation of protein localization to chromosome, telomeric region obo:GO_1904816 activation of protein localization to telomere obo:GO_1904816 biological_process obo:GO_1904816 GO:1904816 obo:GO_1904816 positive regulation of protein localization to chromosome, telomeric region obo:GO_1904841 Interacting selectively and non-covalently with a TORC2 complex. obo:GO_1904841 obo:go.owl obo:GO_1904841 pf obo:GO_1904841 2015-12-07T16:59:44Z obo:GO_1904841 TOR complex 2 binding obo:GO_1904841 TORC 2 complex binding obo:GO_1904841 TORC2 binding obo:GO_1904841 rapamycin and nutrient-insensitive TOR complex binding obo:GO_1904841 mTORC2 binding obo:GO_1904841 molecular_function obo:GO_1904841 GO:1904841 obo:GO_1904841 Interacting selectively and non-covalently with a TORC2 complex, a protein complex that mediates the phosphorylation of protein kinase B obo:GO_1904841 TORC2 complex binding obo:GO_1904850 Any process that stops, prevents or reduces the frequency, rate or extent of establishment of protein localization to telomere. obo:GO_1904850 obo:go.owl obo:GO_1904850 nc obo:GO_1904850 2015-12-10T15:37:51Z obo:GO_1904850 down regulation of establishment of protein localisation to telomere obo:GO_1904850 down regulation of establishment of protein localization to chromosome, telomeric region obo:GO_1904850 down regulation of establishment of protein localization to telomere obo:GO_1904850 down-regulation of establishment of protein localisation to telomere obo:GO_1904850 down-regulation of establishment of protein localization to chromosome, telomeric region obo:GO_1904850 down-regulation of establishment of protein localization to telomere obo:GO_1904850 downregulation of establishment of protein localisation to telomere obo:GO_1904850 downregulation of establishment of protein localization to chromosome, telomeric region obo:GO_1904850 downregulation of establishment of protein localization to telomere obo:GO_1904850 negative regulation of establishment of protein localisation to telomere obo:GO_1904850 negative regulation of establishment of protein localization to chromosome, telomeric region obo:GO_1904850 inhibition of establishment of protein localisation to telomere obo:GO_1904850 inhibition of establishment of protein localization to chromosome, telomeric region obo:GO_1904850 inhibition of establishment of protein localization to telomere obo:GO_1904850 biological_process obo:GO_1904850 GO:1904850 obo:GO_1904850 negative regulation of establishment of protein localization to telomere obo:GO_1904851 Any process that activates or increases the frequency, rate or extent of establishment of protein localization to telomere. obo:GO_1904851 obo:go.owl obo:GO_1904851 nc obo:GO_1904851 2015-12-10T15:37:58Z obo:GO_1904851 positive regulation of establishment of protein localisation to telomere obo:GO_1904851 positive regulation of establishment of protein localization to chromosome, telomeric region obo:GO_1904851 up regulation of establishment of protein localisation to telomere obo:GO_1904851 up regulation of establishment of protein localization to chromosome, telomeric region obo:GO_1904851 up regulation of establishment of protein localization to telomere obo:GO_1904851 up-regulation of establishment of protein localisation to telomere obo:GO_1904851 up-regulation of establishment of protein localization to chromosome, telomeric region obo:GO_1904851 up-regulation of establishment of protein localization to telomere obo:GO_1904851 upregulation of establishment of protein localisation to telomere obo:GO_1904851 upregulation of establishment of protein localization to chromosome, telomeric region obo:GO_1904851 upregulation of establishment of protein localization to telomere obo:GO_1904851 activation of establishment of protein localisation to telomere obo:GO_1904851 activation of establishment of protein localization to chromosome, telomeric region obo:GO_1904851 activation of establishment of protein localization to telomere obo:GO_1904851 biological_process obo:GO_1904851 GO:1904851 obo:GO_1904851 positive regulation of establishment of protein localization to telomere obo:GO_1904854 Interacting selectively and non-covalently with a proteasome core complex. obo:GO_1904854 obo:go.owl obo:GO_1904854 mah obo:GO_1904854 2015-12-15T11:54:19Z obo:GO_1904854 macropain binding obo:GO_1904854 20S core complex binding obo:GO_1904854 20S proteasome binding obo:GO_1904854 PA28gamma-20S proteasome binding obo:GO_1904854 molecular_function obo:GO_1904854 GO:1904854 obo:GO_1904854 proteasome core complex binding obo:GO_1904855 Interacting selectively and non-covalently with a proteasome regulatory particle. obo:GO_1904855 obo:go.owl obo:GO_1904855 mah obo:GO_1904855 2015-12-15T11:54:27Z obo:GO_1904855 PA700-dependent proteasome activator binding obo:GO_1904855 19S regulatory particle binding obo:GO_1904855 PA700 proteasome activator binding obo:GO_1904855 molecular_function obo:GO_1904855 modulator complex binding obo:GO_1904855 GO:1904855 obo:GO_1904855 proteasome regulatory particle binding obo:GO_1904869 Any process that modulates the frequency, rate or extent of protein localization to Cajal body. obo:GO_1904869 obo:go.owl obo:GO_1904869 nc obo:GO_1904869 2015-12-18T11:17:31Z obo:GO_1904869 regulation of protein localisation in Cajal body obo:GO_1904869 regulation of protein localisation to Cajal body obo:GO_1904869 regulation of protein localization in Cajal body obo:GO_1904869 biological_process obo:GO_1904869 GO:1904869 obo:GO_1904869 regulation of protein localization to Cajal body obo:GO_1904870 Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to Cajal body. obo:GO_1904870 obo:go.owl obo:GO_1904870 nc obo:GO_1904870 2015-12-18T11:17:38Z obo:GO_1904870 down regulation of protein localisation in Cajal body obo:GO_1904870 down regulation of protein localisation to Cajal body obo:GO_1904870 down regulation of protein localization in Cajal body obo:GO_1904870 down regulation of protein localization to Cajal body obo:GO_1904870 down-regulation of protein localisation in Cajal body obo:GO_1904870 down-regulation of protein localisation to Cajal body obo:GO_1904870 down-regulation of protein localization in Cajal body obo:GO_1904870 down-regulation of protein localization to Cajal body obo:GO_1904870 downregulation of protein localisation in Cajal body obo:GO_1904870 downregulation of protein localisation to Cajal body obo:GO_1904870 downregulation of protein localization in Cajal body obo:GO_1904870 downregulation of protein localization to Cajal body obo:GO_1904870 negative regulation of protein localisation in Cajal body obo:GO_1904870 negative regulation of protein localisation to Cajal body obo:GO_1904870 negative regulation of protein localization in Cajal body obo:GO_1904870 inhibition of protein localisation in Cajal body obo:GO_1904870 inhibition of protein localisation to Cajal body obo:GO_1904870 inhibition of protein localization in Cajal body obo:GO_1904870 inhibition of protein localization to Cajal body obo:GO_1904870 biological_process obo:GO_1904870 GO:1904870 obo:GO_1904870 negative regulation of protein localization to Cajal body obo:GO_1904871 Any process that activates or increases the frequency, rate or extent of protein localization to Cajal body. obo:GO_1904871 obo:go.owl obo:GO_1904871 nc obo:GO_1904871 2015-12-18T11:17:45Z obo:GO_1904871 positive regulation of protein localisation in Cajal body obo:GO_1904871 positive regulation of protein localisation to Cajal body obo:GO_1904871 positive regulation of protein localization in Cajal body obo:GO_1904871 up regulation of protein localisation in Cajal body obo:GO_1904871 up regulation of protein localisation to Cajal body obo:GO_1904871 up regulation of protein localization in Cajal body obo:GO_1904871 up regulation of protein localization to Cajal body obo:GO_1904871 up-regulation of protein localisation in Cajal body obo:GO_1904871 up-regulation of protein localisation to Cajal body obo:GO_1904871 up-regulation of protein localization in Cajal body obo:GO_1904871 up-regulation of protein localization to Cajal body obo:GO_1904871 upregulation of protein localisation in Cajal body obo:GO_1904871 upregulation of protein localisation to Cajal body obo:GO_1904871 upregulation of protein localization in Cajal body obo:GO_1904871 upregulation of protein localization to Cajal body obo:GO_1904871 activation of protein localisation in Cajal body obo:GO_1904871 activation of protein localisation to Cajal body obo:GO_1904871 activation of protein localization in Cajal body obo:GO_1904871 activation of protein localization to Cajal body obo:GO_1904871 biological_process obo:GO_1904871 GO:1904871 obo:GO_1904871 positive regulation of protein localization to Cajal body obo:GO_1904878 Any process that stops, prevents or reduces the frequency, rate or extent of calcium ion transmembrane transport via high voltage-gated calcium channel. obo:GO_1904878 obo:go.owl obo:GO_1904878 sl obo:GO_1904878 2015-12-18T22:30:37Z obo:GO_1904878 down regulation of generation of L-type calcium current obo:GO_1904878 down-regulation of generation of L-type calcium current obo:GO_1904878 downregulation of generation of L-type calcium current obo:GO_1904878 inhibition of generation of L-type calcium current obo:GO_1904878 biological_process obo:GO_1904878 negative regulation of generation of L-type calcium current obo:GO_1904878 GO:1904878 obo:GO_1904878 negative regulation of calcium ion transmembrane transport via high voltage-gated calcium channel obo:GO_1904879 Any process that activates or increases the frequency, rate or extent of calcium ion transmembrane transport via high voltage-gated calcium channel. obo:GO_1904879 obo:go.owl obo:GO_1904879 sl obo:GO_1904879 2015-12-18T22:30:44Z obo:GO_1904879 up regulation of generation of L-type calcium current obo:GO_1904879 up-regulation of generation of L-type calcium current obo:GO_1904879 upregulation of generation of L-type calcium current obo:GO_1904879 activation of generation of L-type calcium current obo:GO_1904879 biological_process obo:GO_1904879 positive regulation of generation of L-type calcium current obo:GO_1904879 GO:1904879 obo:GO_1904879 positive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel obo:GO_1904897 Any process that modulates the frequency, rate or extent of hepatic stellate cell proliferation. obo:GO_1904897 obo:go.owl obo:GO_1904897 sl obo:GO_1904897 2016-01-14T15:56:59Z obo:GO_1904897 regulation of Ito cell proliferation obo:GO_1904897 regulation of hepatic perisinusoidal cell proliferation obo:GO_1904897 regulation of perisinusoidal cell proliferation obo:GO_1904897 biological_process obo:GO_1904897 GO:1904897 obo:GO_1904897 regulation of hepatic stellate cell proliferation obo:GO_1904898 Any process that stops, prevents or reduces the frequency, rate or extent of hepatic stellate cell proliferation. obo:GO_1904898 obo:go.owl obo:GO_1904898 sl obo:GO_1904898 2016-01-14T15:57:06Z obo:GO_1904898 down regulation of Ito cell proliferation obo:GO_1904898 down regulation of hepatic perisinusoidal cell proliferation obo:GO_1904898 down regulation of hepatic stellate cell proliferation obo:GO_1904898 down regulation of perisinusoidal cell proliferation obo:GO_1904898 down-regulation of Ito cell proliferation obo:GO_1904898 down-regulation of hepatic perisinusoidal cell proliferation obo:GO_1904898 down-regulation of hepatic stellate cell proliferation obo:GO_1904898 down-regulation of perisinusoidal cell proliferation obo:GO_1904898 downregulation of Ito cell proliferation obo:GO_1904898 downregulation of hepatic perisinusoidal cell proliferation obo:GO_1904898 downregulation of hepatic stellate cell proliferation obo:GO_1904898 downregulation of perisinusoidal cell proliferation obo:GO_1904898 negative regulation of Ito cell proliferation obo:GO_1904898 negative regulation of hepatic perisinusoidal cell proliferation obo:GO_1904898 negative regulation of perisinusoidal cell proliferation obo:GO_1904898 inhibition of Ito cell proliferation obo:GO_1904898 inhibition of hepatic perisinusoidal cell proliferation obo:GO_1904898 inhibition of hepatic stellate cell proliferation obo:GO_1904898 inhibition of perisinusoidal cell proliferation obo:GO_1904898 biological_process obo:GO_1904898 GO:1904898 obo:GO_1904898 negative regulation of hepatic stellate cell proliferation obo:GO_1904899 Any process that activates or increases the frequency, rate or extent of hepatic stellate cell proliferation. obo:GO_1904899 obo:go.owl obo:GO_1904899 sl obo:GO_1904899 2016-01-14T15:57:13Z obo:GO_1904899 positive regulation of Ito cell proliferation obo:GO_1904899 positive regulation of hepatic perisinusoidal cell proliferation obo:GO_1904899 positive regulation of perisinusoidal cell proliferation obo:GO_1904899 up regulation of Ito cell proliferation obo:GO_1904899 up regulation of hepatic perisinusoidal cell proliferation obo:GO_1904899 up regulation of hepatic stellate cell proliferation obo:GO_1904899 up regulation of perisinusoidal cell proliferation obo:GO_1904899 up-regulation of Ito cell proliferation obo:GO_1904899 up-regulation of hepatic perisinusoidal cell proliferation obo:GO_1904899 up-regulation of hepatic stellate cell proliferation obo:GO_1904899 up-regulation of perisinusoidal cell proliferation obo:GO_1904899 upregulation of Ito cell proliferation obo:GO_1904899 upregulation of hepatic perisinusoidal cell proliferation obo:GO_1904899 upregulation of hepatic stellate cell proliferation obo:GO_1904899 upregulation of perisinusoidal cell proliferation obo:GO_1904899 activation of Ito cell proliferation obo:GO_1904899 activation of hepatic perisinusoidal cell proliferation obo:GO_1904899 activation of hepatic stellate cell proliferation obo:GO_1904899 activation of perisinusoidal cell proliferation obo:GO_1904899 biological_process obo:GO_1904899 GO:1904899 obo:GO_1904899 positive regulation of hepatic stellate cell proliferation obo:GO_1904910 Any process that modulates the frequency, rate or extent of establishment of RNA localization to telomere. obo:GO_1904910 obo:go.owl obo:GO_1904910 rph obo:GO_1904910 2016-01-19T10:34:21Z obo:GO_1904910 regulation of establishment of RNA localisation to telomere obo:GO_1904910 biological_process obo:GO_1904910 GO:1904910 obo:GO_1904910 regulation of establishment of RNA localization to telomere obo:GO_1904911 Any process that stops, prevents or reduces the frequency, rate or extent of establishment of RNA localization to telomere. obo:GO_1904911 obo:go.owl obo:GO_1904911 rph obo:GO_1904911 2016-01-19T10:34:28Z obo:GO_1904911 down regulation of establishment of RNA localisation to telomere obo:GO_1904911 down regulation of establishment of RNA localization to telomere obo:GO_1904911 down-regulation of establishment of RNA localisation to telomere obo:GO_1904911 down-regulation of establishment of RNA localization to telomere obo:GO_1904911 downregulation of establishment of RNA localisation to telomere obo:GO_1904911 downregulation of establishment of RNA localization to telomere obo:GO_1904911 negative regulation of establishment of RNA localisation to telomere obo:GO_1904911 inhibition of establishment of RNA localisation to telomere obo:GO_1904911 inhibition of establishment of RNA localization to telomere obo:GO_1904911 biological_process obo:GO_1904911 GO:1904911 obo:GO_1904911 negative regulation of establishment of RNA localization to telomere obo:GO_1904912 Any process that activates or increases the frequency, rate or extent of establishment of RNA localization to telomere. obo:GO_1904912 obo:go.owl obo:GO_1904912 rph obo:GO_1904912 2016-01-19T10:34:35Z obo:GO_1904912 positive regulation of establishment of RNA localisation to telomere obo:GO_1904912 up regulation of establishment of RNA localisation to telomere obo:GO_1904912 up regulation of establishment of RNA localization to telomere obo:GO_1904912 up-regulation of establishment of RNA localisation to telomere obo:GO_1904912 up-regulation of establishment of RNA localization to telomere obo:GO_1904912 upregulation of establishment of RNA localisation to telomere obo:GO_1904912 upregulation of establishment of RNA localization to telomere obo:GO_1904912 activation of establishment of RNA localisation to telomere obo:GO_1904912 activation of establishment of RNA localization to telomere obo:GO_1904912 biological_process obo:GO_1904912 GO:1904912 obo:GO_1904912 positive regulation of establishment of RNA localization to telomere obo:GO_1904913 Any process that modulates the frequency, rate or extent of establishment of the localization of a protein-containing macromolecular complex to a telomere. obo:GO_1904913 obo:go.owl obo:GO_1904913 rph obo:GO_1904913 2016-01-19T10:38:22Z obo:GO_1904913 regulation of establishment of macromolecular complex localisation to telomere obo:GO_1904913 biological_process obo:GO_1904913 regulation of establishment of macromolecular complex localization to telomere obo:GO_1904913 GO:1904913 obo:GO_1904913 regulation of establishment of protein-containing complex localization to telomere obo:GO_1904914 Any process that stops, prevents or reduces the frequency, rate or extent of establishment of the localization of a protein-containing macromolecular complex to a telomere. obo:GO_1904914 obo:go.owl obo:GO_1904914 rph obo:GO_1904914 2016-01-19T10:38:29Z obo:GO_1904914 down regulation of establishment of macromolecular complex localisation to telomere obo:GO_1904914 down regulation of establishment of macromolecular complex localization to telomere obo:GO_1904914 down-regulation of establishment of macromolecular complex localisation to telomere obo:GO_1904914 down-regulation of establishment of macromolecular complex localization to telomere obo:GO_1904914 downregulation of establishment of macromolecular complex localisation to telomere obo:GO_1904914 downregulation of establishment of macromolecular complex localization to telomere obo:GO_1904914 negative regulation of establishment of macromolecular complex localisation to telomere obo:GO_1904914 inhibition of establishment of macromolecular complex localisation to telomere obo:GO_1904914 inhibition of establishment of macromolecular complex localization to telomere obo:GO_1904914 biological_process obo:GO_1904914 negative regulation of establishment of macromolecular complex localization to telomere obo:GO_1904914 GO:1904914 obo:GO_1904914 negative regulation of establishment of protein-containing complex localization to telomere obo:GO_1904915 Any process that activates or increases the frequency, rate or extent of establishment of the localization of a protein-containing macromolecular complex to a telomere. obo:GO_1904915 obo:go.owl obo:GO_1904915 rph obo:GO_1904915 2016-01-19T10:38:36Z obo:GO_1904915 positive regulation of establishment of macromolecular complex localisation to telomere obo:GO_1904915 up regulation of establishment of macromolecular complex localisation to telomere obo:GO_1904915 up regulation of establishment of macromolecular complex localization to telomere obo:GO_1904915 up-regulation of establishment of macromolecular complex localisation to telomere obo:GO_1904915 up-regulation of establishment of macromolecular complex localization to telomere obo:GO_1904915 upregulation of establishment of macromolecular complex localisation to telomere obo:GO_1904915 upregulation of establishment of macromolecular complex localization to telomere obo:GO_1904915 activation of establishment of macromolecular complex localisation to telomere obo:GO_1904915 activation of establishment of macromolecular complex localization to telomere obo:GO_1904915 biological_process obo:GO_1904915 positive regulation of establishment of macromolecular complex localization to telomere obo:GO_1904915 GO:1904915 obo:GO_1904915 positive regulation of establishment of protein-containing complex localization to telomere obo:GO_1904931 Interacting selectively and non-covalently with an MCM complex. obo:GO_1904931 obo:go.owl obo:GO_1904931 mah obo:GO_1904931 2016-01-29T11:48:10Z obo:GO_1904931 mini-chromosome maintenance complex binding obo:GO_1904931 molecular_function obo:GO_1904931 GO:1904931 obo:GO_1904931 MCM complex binding obo:GO_1904950 Any process that stops, prevents or reduces the frequency, rate or extent of establishment of protein localization. obo:GO_1904950 obo:go.owl obo:GO_1904950 mec obo:GO_1904950 2016-02-05T09:59:24Z obo:GO_1904950 down regulation of establishment of protein localisation obo:GO_1904950 down regulation of establishment of protein localization obo:GO_1904950 down regulation of protein positioning obo:GO_1904950 down regulation of protein recruitment obo:GO_1904950 down-regulation of establishment of protein localisation obo:GO_1904950 down-regulation of establishment of protein localization obo:GO_1904950 down-regulation of protein positioning obo:GO_1904950 down-regulation of protein recruitment obo:GO_1904950 downregulation of establishment of protein localisation obo:GO_1904950 downregulation of establishment of protein localization obo:GO_1904950 downregulation of protein positioning obo:GO_1904950 downregulation of protein recruitment obo:GO_1904950 negative regulation of establishment of protein localisation obo:GO_1904950 negative regulation of protein positioning obo:GO_1904950 negative regulation of protein recruitment obo:GO_1904950 inhibition of establishment of protein localisation obo:GO_1904950 inhibition of establishment of protein localization obo:GO_1904950 inhibition of protein positioning obo:GO_1904950 inhibition of protein recruitment obo:GO_1904950 biological_process obo:GO_1904950 GO:1904950 obo:GO_1904950 negative regulation of establishment of protein localization obo:GO_1904951 Any process that activates or increases the frequency, rate or extent of establishment of protein localization. obo:GO_1904951 obo:go.owl obo:GO_1904951 mec obo:GO_1904951 2016-02-05T09:59:32Z obo:GO_1904951 positive regulation of establishment of protein localisation obo:GO_1904951 positive regulation of protein positioning obo:GO_1904951 positive regulation of protein recruitment obo:GO_1904951 up regulation of establishment of protein localisation obo:GO_1904951 up regulation of establishment of protein localization obo:GO_1904951 up regulation of protein positioning obo:GO_1904951 up regulation of protein recruitment obo:GO_1904951 up-regulation of establishment of protein localisation obo:GO_1904951 up-regulation of establishment of protein localization obo:GO_1904951 up-regulation of protein positioning obo:GO_1904951 up-regulation of protein recruitment obo:GO_1904951 upregulation of establishment of protein localisation obo:GO_1904951 upregulation of establishment of protein localization obo:GO_1904951 upregulation of protein positioning obo:GO_1904951 upregulation of protein recruitment obo:GO_1904951 activation of establishment of protein localisation obo:GO_1904951 activation of establishment of protein localization obo:GO_1904951 activation of protein positioning obo:GO_1904951 activation of protein recruitment obo:GO_1904951 biological_process obo:GO_1904951 GO:1904951 obo:GO_1904951 positive regulation of establishment of protein localization obo:GO_1904994 Any process that modulates the frequency, rate or extent of leukocyte adhesion to vascular endothelial cell. obo:GO_1904994 obo:go.owl obo:GO_1904994 bc obo:GO_1904994 2016-03-01T10:59:00Z obo:GO_1904994 biological_process obo:GO_1904994 GO:1904994 obo:GO_1904994 regulation of leukocyte adhesion to vascular endothelial cell obo:GO_1904995 Any process that stops, prevents or reduces the frequency, rate or extent of leukocyte adhesion to vascular endothelial cell. obo:GO_1904995 obo:go.owl obo:GO_1904995 bc obo:GO_1904995 2016-03-01T10:59:08Z obo:GO_1904995 down regulation of leukocyte adhesion to vascular endothelial cell obo:GO_1904995 down-regulation of leukocyte adhesion to vascular endothelial cell obo:GO_1904995 downregulation of leukocyte adhesion to vascular endothelial cell obo:GO_1904995 inhibition of leukocyte adhesion to vascular endothelial cell obo:GO_1904995 biological_process obo:GO_1904995 GO:1904995 obo:GO_1904995 negative regulation of leukocyte adhesion to vascular endothelial cell obo:GO_1904996 Any process that activates or increases the frequency, rate or extent of leukocyte adhesion to vascular endothelial cell. obo:GO_1904996 obo:go.owl obo:GO_1904996 bc obo:GO_1904996 2016-03-01T10:59:22Z obo:GO_1904996 up regulation of leukocyte adhesion to vascular endothelial cell obo:GO_1904996 up-regulation of leukocyte adhesion to vascular endothelial cell obo:GO_1904996 upregulation of leukocyte adhesion to vascular endothelial cell obo:GO_1904996 activation of leukocyte adhesion to vascular endothelial cell obo:GO_1904996 biological_process obo:GO_1904996 GO:1904996 obo:GO_1904996 positive regulation of leukocyte adhesion to vascular endothelial cell obo:GO_1904997 Any process that modulates the frequency, rate or extent of leukocyte adhesion to arterial endothelial cell. obo:GO_1904997 obo:go.owl obo:GO_1904997 bc obo:GO_1904997 2016-03-01T11:04:49Z obo:GO_1904997 biological_process obo:GO_1904997 GO:1904997 obo:GO_1904997 regulation of leukocyte adhesion to arterial endothelial cell obo:GO_1904998 Any process that stops, prevents or reduces the frequency, rate or extent of leukocyte adhesion to arterial endothelial cell. obo:GO_1904998 obo:go.owl obo:GO_1904998 bc obo:GO_1904998 2016-03-01T11:04:57Z obo:GO_1904998 down regulation of leukocyte adhesion to arterial endothelial cell obo:GO_1904998 down-regulation of leukocyte adhesion to arterial endothelial cell obo:GO_1904998 downregulation of leukocyte adhesion to arterial endothelial cell obo:GO_1904998 inhibition of leukocyte adhesion to arterial endothelial cell obo:GO_1904998 biological_process obo:GO_1904998 GO:1904998 obo:GO_1904998 negative regulation of leukocyte adhesion to arterial endothelial cell obo:GO_1904999 Any process that activates or increases the frequency, rate or extent of leukocyte adhesion to arterial endothelial cell. obo:GO_1904999 obo:go.owl obo:GO_1904999 bc obo:GO_1904999 2016-03-01T11:05:05Z obo:GO_1904999 up regulation of leukocyte adhesion to arterial endothelial cell obo:GO_1904999 up-regulation of leukocyte adhesion to arterial endothelial cell obo:GO_1904999 upregulation of leukocyte adhesion to arterial endothelial cell obo:GO_1904999 activation of leukocyte adhesion to arterial endothelial cell obo:GO_1904999 biological_process obo:GO_1904999 GO:1904999 obo:GO_1904999 positive regulation of leukocyte adhesion to arterial endothelial cell obo:GO_1905092 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a diosgenin stimulus. obo:GO_1905092 obo:go.owl obo:GO_1905092 bc obo:GO_1905092 2016-03-31T11:04:28Z obo:GO_1905092 biological_process obo:GO_1905092 GO:1905092 obo:GO_1905092 response to diosgenin obo:GO_1905108 Interacting selectively and non-covalently with guanosine. obo:GO_1905108 obo:go.owl obo:GO_1905108 al obo:GO_1905108 2016-04-05T08:30:47Z obo:GO_1905108 molecular_function obo:GO_1905108 GO:1905108 obo:GO_1905108 guanosine binding obo:GO_1905150 Any process that modulates the frequency, rate or extent of voltage-gated sodium channel activity. obo:GO_1905150 obo:go.owl obo:GO_1905150 sl obo:GO_1905150 2016-04-15T21:47:40Z obo:GO_1905150 regulation of voltage gated sodium channel activity obo:GO_1905150 regulation of voltage-dependent sodium channel activity obo:GO_1905150 regulation of voltage-gated sodium ion channel activity obo:GO_1905150 regulation of voltage-sensitive sodium channel obo:GO_1905150 biological_process obo:GO_1905150 GO:1905150 obo:GO_1905150 regulation of voltage-gated sodium channel activity obo:GO_1905151 Any process that stops, prevents or reduces the frequency, rate or extent of voltage-gated sodium channel activity. obo:GO_1905151 obo:go.owl obo:GO_1905151 sl obo:GO_1905151 2016-04-15T21:47:49Z obo:GO_1905151 down regulation of voltage gated sodium channel activity obo:GO_1905151 down regulation of voltage-dependent sodium channel activity obo:GO_1905151 down regulation of voltage-gated sodium channel activity obo:GO_1905151 down regulation of voltage-gated sodium ion channel activity obo:GO_1905151 down regulation of voltage-sensitive sodium channel obo:GO_1905151 down-regulation of voltage gated sodium channel activity obo:GO_1905151 down-regulation of voltage-dependent sodium channel activity obo:GO_1905151 down-regulation of voltage-gated sodium channel activity obo:GO_1905151 down-regulation of voltage-gated sodium ion channel activity obo:GO_1905151 down-regulation of voltage-sensitive sodium channel obo:GO_1905151 downregulation of voltage gated sodium channel activity obo:GO_1905151 downregulation of voltage-dependent sodium channel activity obo:GO_1905151 downregulation of voltage-gated sodium channel activity obo:GO_1905151 downregulation of voltage-gated sodium ion channel activity obo:GO_1905151 downregulation of voltage-sensitive sodium channel obo:GO_1905151 negative regulation of voltage gated sodium channel activity obo:GO_1905151 negative regulation of voltage-dependent sodium channel activity obo:GO_1905151 negative regulation of voltage-gated sodium ion channel activity obo:GO_1905151 negative regulation of voltage-sensitive sodium channel obo:GO_1905151 inhibition of voltage gated sodium channel activity obo:GO_1905151 inhibition of voltage-dependent sodium channel activity obo:GO_1905151 inhibition of voltage-gated sodium channel activity obo:GO_1905151 inhibition of voltage-gated sodium ion channel activity obo:GO_1905151 inhibition of voltage-sensitive sodium channel obo:GO_1905151 biological_process obo:GO_1905151 GO:1905151 obo:GO_1905151 negative regulation of voltage-gated sodium channel activity obo:GO_1905152 Any process that activates or increases the frequency, rate or extent of voltage-gated sodium channel activity. obo:GO_1905152 obo:go.owl obo:GO_1905152 sl obo:GO_1905152 2016-04-15T21:47:57Z obo:GO_1905152 positive regulation of voltage gated sodium channel activity obo:GO_1905152 positive regulation of voltage-dependent sodium channel activity obo:GO_1905152 positive regulation of voltage-gated sodium ion channel activity obo:GO_1905152 positive regulation of voltage-sensitive sodium channel obo:GO_1905152 up regulation of voltage gated sodium channel activity obo:GO_1905152 up regulation of voltage-dependent sodium channel activity obo:GO_1905152 up regulation of voltage-gated sodium channel activity obo:GO_1905152 up regulation of voltage-gated sodium ion channel activity obo:GO_1905152 up regulation of voltage-sensitive sodium channel obo:GO_1905152 up-regulation of voltage gated sodium channel activity obo:GO_1905152 up-regulation of voltage-dependent sodium channel activity obo:GO_1905152 up-regulation of voltage-gated sodium channel activity obo:GO_1905152 up-regulation of voltage-gated sodium ion channel activity obo:GO_1905152 up-regulation of voltage-sensitive sodium channel obo:GO_1905152 upregulation of voltage gated sodium channel activity obo:GO_1905152 upregulation of voltage-dependent sodium channel activity obo:GO_1905152 upregulation of voltage-gated sodium channel activity obo:GO_1905152 upregulation of voltage-gated sodium ion channel activity obo:GO_1905152 upregulation of voltage-sensitive sodium channel obo:GO_1905152 activation of voltage gated sodium channel activity obo:GO_1905152 activation of voltage-dependent sodium channel activity obo:GO_1905152 activation of voltage-gated sodium channel activity obo:GO_1905152 activation of voltage-gated sodium ion channel activity obo:GO_1905152 activation of voltage-sensitive sodium channel obo:GO_1905152 biological_process obo:GO_1905152 GO:1905152 obo:GO_1905152 positive regulation of voltage-gated sodium channel activity obo:GO_1905169 Any process that modulates the frequency, rate or extent of protein localization to phagocytic vesicle. obo:GO_1905169 obo:go.owl obo:GO_1905169 bf obo:GO_1905169 2016-05-02T18:38:13Z obo:GO_1905169 regulation of protein localisation in phagocytic vesicle obo:GO_1905169 regulation of protein localisation to phagocytic vesicle obo:GO_1905169 regulation of protein localisation to phagosome obo:GO_1905169 regulation of protein localization in phagocytic vesicle obo:GO_1905169 regulation of protein recruitment to phagosome obo:GO_1905169 biological_process obo:GO_1905169 GO:1905169 obo:GO_1905169 regulation of protein localization to phagocytic vesicle obo:GO_1905170 Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to phagocytic vesicle. obo:GO_1905170 obo:go.owl obo:GO_1905170 bf obo:GO_1905170 2016-05-02T18:38:22Z obo:GO_1905170 down regulation of protein localisation in phagocytic vesicle obo:GO_1905170 down regulation of protein localisation to phagocytic vesicle obo:GO_1905170 down regulation of protein localisation to phagosome obo:GO_1905170 down regulation of protein localization in phagocytic vesicle obo:GO_1905170 down regulation of protein localization to phagocytic vesicle obo:GO_1905170 down regulation of protein recruitment to phagosome obo:GO_1905170 down-regulation of protein localisation in phagocytic vesicle obo:GO_1905170 down-regulation of protein localisation to phagocytic vesicle obo:GO_1905170 down-regulation of protein localisation to phagosome obo:GO_1905170 down-regulation of protein localization in phagocytic vesicle obo:GO_1905170 down-regulation of protein localization to phagocytic vesicle obo:GO_1905170 down-regulation of protein recruitment to phagosome obo:GO_1905170 downregulation of protein localisation in phagocytic vesicle obo:GO_1905170 downregulation of protein localisation to phagocytic vesicle obo:GO_1905170 downregulation of protein localisation to phagosome obo:GO_1905170 downregulation of protein localization in phagocytic vesicle obo:GO_1905170 downregulation of protein localization to phagocytic vesicle obo:GO_1905170 downregulation of protein recruitment to phagosome obo:GO_1905170 negative regulation of protein localisation in phagocytic vesicle obo:GO_1905170 negative regulation of protein localisation to phagocytic vesicle obo:GO_1905170 negative regulation of protein localisation to phagosome obo:GO_1905170 negative regulation of protein localization in phagocytic vesicle obo:GO_1905170 negative regulation of protein recruitment to phagosome obo:GO_1905170 inhibition of protein localisation in phagocytic vesicle obo:GO_1905170 inhibition of protein localisation to phagocytic vesicle obo:GO_1905170 inhibition of protein localisation to phagosome obo:GO_1905170 inhibition of protein localization in phagocytic vesicle obo:GO_1905170 inhibition of protein localization to phagocytic vesicle obo:GO_1905170 inhibition of protein recruitment to phagosome obo:GO_1905170 biological_process obo:GO_1905170 GO:1905170 obo:GO_1905170 negative regulation of protein localization to phagocytic vesicle obo:GO_1905171 Any process that activates or increases the frequency, rate or extent of protein localization to phagocytic vesicle. obo:GO_1905171 obo:go.owl obo:GO_1905171 bf obo:GO_1905171 2016-05-02T18:38:30Z obo:GO_1905171 positive regulation of protein localisation in phagocytic vesicle obo:GO_1905171 positive regulation of protein localisation to phagocytic vesicle obo:GO_1905171 positive regulation of protein localisation to phagosome obo:GO_1905171 positive regulation of protein localization in phagocytic vesicle obo:GO_1905171 positive regulation of protein recruitment to phagosome obo:GO_1905171 up regulation of protein localisation in phagocytic vesicle obo:GO_1905171 up regulation of protein localisation to phagocytic vesicle obo:GO_1905171 up regulation of protein localisation to phagosome obo:GO_1905171 up regulation of protein localization in phagocytic vesicle obo:GO_1905171 up regulation of protein localization to phagocytic vesicle obo:GO_1905171 up regulation of protein recruitment to phagosome obo:GO_1905171 up-regulation of protein localisation in phagocytic vesicle obo:GO_1905171 up-regulation of protein localisation to phagocytic vesicle obo:GO_1905171 up-regulation of protein localisation to phagosome obo:GO_1905171 up-regulation of protein localization in phagocytic vesicle obo:GO_1905171 up-regulation of protein localization to phagocytic vesicle obo:GO_1905171 up-regulation of protein recruitment to phagosome obo:GO_1905171 upregulation of protein localisation in phagocytic vesicle obo:GO_1905171 upregulation of protein localisation to phagocytic vesicle obo:GO_1905171 upregulation of protein localisation to phagosome obo:GO_1905171 upregulation of protein localization in phagocytic vesicle obo:GO_1905171 upregulation of protein localization to phagocytic vesicle obo:GO_1905171 upregulation of protein recruitment to phagosome obo:GO_1905171 activation of protein localisation in phagocytic vesicle obo:GO_1905171 activation of protein localisation to phagocytic vesicle obo:GO_1905171 activation of protein localisation to phagosome obo:GO_1905171 activation of protein localization in phagocytic vesicle obo:GO_1905171 activation of protein localization to phagocytic vesicle obo:GO_1905171 activation of protein recruitment to phagosome obo:GO_1905171 biological_process obo:GO_1905171 GO:1905171 obo:GO_1905171 positive regulation of protein localization to phagocytic vesicle obo:GO_1905172 Interacting selectively and non-covalently with a RISC complex. obo:GO_1905172 obo:go.owl obo:GO_1905172 bf obo:GO_1905172 2016-05-02T19:27:02Z obo:GO_1905172 RNA-induced silencing complex binding obo:GO_1905172 molecular_function obo:GO_1905172 GO:1905172 obo:GO_1905172 RISC complex binding obo:GO_1905271 Any process that modulates the frequency, rate or extent of proton-transporting ATP synthase activity, rotational mechanism. obo:GO_1905271 obo:go.owl obo:GO_1905271 als obo:GO_1905271 2016-06-16T12:09:49Z obo:GO_1905271 regulation of H+-transporting ATP synthase activity obo:GO_1905271 regulation of hydrogen ion translocating F-type ATPase activity obo:GO_1905271 regulation of hydrogen ion transporting ATP synthase activity, rotational mechanism obo:GO_1905271 regulation of hydrogen ion transporting two-sector ATPase activity obo:GO_1905271 biological_process obo:GO_1905271 GO:1905271 obo:GO_1905271 regulation of proton-transporting ATP synthase activity, rotational mechanism obo:GO_1905272 Any process that stops, prevents or reduces the frequency, rate or extent of proton-transporting ATP synthase activity, rotational mechanism. obo:GO_1905272 obo:go.owl obo:GO_1905272 als obo:GO_1905272 2016-06-16T12:09:57Z obo:GO_1905272 down regulation of H+-transporting ATP synthase activity obo:GO_1905272 down regulation of hydrogen ion translocating F-type ATPase activity obo:GO_1905272 down regulation of hydrogen ion transporting ATP synthase activity, rotational mechanism obo:GO_1905272 down regulation of hydrogen ion transporting two-sector ATPase activity obo:GO_1905272 down regulation of proton-transporting ATP synthase activity, rotational mechanism obo:GO_1905272 down-regulation of H+-transporting ATP synthase activity obo:GO_1905272 down-regulation of hydrogen ion translocating F-type ATPase activity obo:GO_1905272 down-regulation of hydrogen ion transporting ATP synthase activity, rotational mechanism obo:GO_1905272 down-regulation of hydrogen ion transporting two-sector ATPase activity obo:GO_1905272 down-regulation of proton-transporting ATP synthase activity, rotational mechanism obo:GO_1905272 downregulation of H+-transporting ATP synthase activity obo:GO_1905272 downregulation of hydrogen ion translocating F-type ATPase activity obo:GO_1905272 downregulation of hydrogen ion transporting ATP synthase activity, rotational mechanism obo:GO_1905272 downregulation of hydrogen ion transporting two-sector ATPase activity obo:GO_1905272 downregulation of proton-transporting ATP synthase activity, rotational mechanism obo:GO_1905272 negative regulation of H+-transporting ATP synthase activity obo:GO_1905272 negative regulation of hydrogen ion translocating F-type ATPase activity obo:GO_1905272 negative regulation of hydrogen ion transporting ATP synthase activity, rotational mechanism obo:GO_1905272 negative regulation of hydrogen ion transporting two-sector ATPase activity obo:GO_1905272 inhibition of H+-transporting ATP synthase activity obo:GO_1905272 inhibition of hydrogen ion translocating F-type ATPase activity obo:GO_1905272 inhibition of hydrogen ion transporting ATP synthase activity, rotational mechanism obo:GO_1905272 inhibition of hydrogen ion transporting two-sector ATPase activity obo:GO_1905272 inhibition of proton-transporting ATP synthase activity, rotational mechanism obo:GO_1905272 biological_process obo:GO_1905272 GO:1905272 obo:GO_1905272 negative regulation of proton-transporting ATP synthase activity, rotational mechanism obo:GO_1905273 Any process that activates or increases the frequency, rate or extent of proton-transporting ATP synthase activity, rotational mechanism. obo:GO_1905273 obo:go.owl obo:GO_1905273 als obo:GO_1905273 2016-06-16T12:10:05Z obo:GO_1905273 positive regulation of H+-transporting ATP synthase activity obo:GO_1905273 positive regulation of hydrogen ion translocating F-type ATPase activity obo:GO_1905273 positive regulation of hydrogen ion transporting ATP synthase activity, rotational mechanism obo:GO_1905273 positive regulation of hydrogen ion transporting two-sector ATPase activity obo:GO_1905273 up regulation of H+-transporting ATP synthase activity obo:GO_1905273 up regulation of hydrogen ion translocating F-type ATPase activity obo:GO_1905273 up regulation of hydrogen ion transporting ATP synthase activity, rotational mechanism obo:GO_1905273 up regulation of hydrogen ion transporting two-sector ATPase activity obo:GO_1905273 up regulation of proton-transporting ATP synthase activity, rotational mechanism obo:GO_1905273 up-regulation of H+-transporting ATP synthase activity obo:GO_1905273 up-regulation of hydrogen ion translocating F-type ATPase activity obo:GO_1905273 up-regulation of hydrogen ion transporting ATP synthase activity, rotational mechanism obo:GO_1905273 up-regulation of hydrogen ion transporting two-sector ATPase activity obo:GO_1905273 up-regulation of proton-transporting ATP synthase activity, rotational mechanism obo:GO_1905273 upregulation of H+-transporting ATP synthase activity obo:GO_1905273 upregulation of hydrogen ion translocating F-type ATPase activity obo:GO_1905273 upregulation of hydrogen ion transporting ATP synthase activity, rotational mechanism obo:GO_1905273 upregulation of hydrogen ion transporting two-sector ATPase activity obo:GO_1905273 upregulation of proton-transporting ATP synthase activity, rotational mechanism obo:GO_1905273 activation of H+-transporting ATP synthase activity obo:GO_1905273 activation of hydrogen ion translocating F-type ATPase activity obo:GO_1905273 activation of hydrogen ion transporting ATP synthase activity, rotational mechanism obo:GO_1905273 activation of hydrogen ion transporting two-sector ATPase activity obo:GO_1905273 activation of proton-transporting ATP synthase activity, rotational mechanism obo:GO_1905273 biological_process obo:GO_1905273 GO:1905273 obo:GO_1905273 positive regulation of proton-transporting ATP synthase activity, rotational mechanism obo:GO_1905334 Interacting selectively and non-covalently with a Swi5-Sfr1 complex. obo:GO_1905334 obo:go.owl obo:GO_1905334 al obo:GO_1905334 2016-07-25T16:18:58Z obo:GO_1905334 Sae3-Mei5 complex binding obo:GO_1905334 molecular_function obo:GO_1905334 GO:1905334 obo:GO_1905334 Swi5-Sfr1 complex binding obo:GO_1905340 Any process that modulates the frequency, rate or extent of protein localization to kinetochore. obo:GO_1905340 obo:go.owl obo:GO_1905340 es obo:GO_1905340 2016-07-27T15:26:36Z obo:GO_1905340 regulation of protein localisation to kinetochore obo:GO_1905340 regulation of condensin localization to kinetochore obo:GO_1905340 biological_process obo:GO_1905340 GO:1905340 obo:GO_1905340 Q9H211 in Human in PMID:22581055 obo:GO_1905340 regulation of protein localization to kinetochore obo:GO_1905341 Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to kinetochore. obo:GO_1905341 obo:go.owl obo:GO_1905341 es obo:GO_1905341 2016-07-27T15:26:44Z obo:GO_1905341 down regulation of protein localisation to kinetochore obo:GO_1905341 down regulation of protein localization to kinetochore obo:GO_1905341 down-regulation of protein localisation to kinetochore obo:GO_1905341 down-regulation of protein localization to kinetochore obo:GO_1905341 downregulation of protein localisation to kinetochore obo:GO_1905341 downregulation of protein localization to kinetochore obo:GO_1905341 negative regulation of protein localisation to kinetochore obo:GO_1905341 down regulation of condensin localization to kinetochore obo:GO_1905341 down-regulation of condensin localization to kinetochore obo:GO_1905341 downregulation of condensin localization to kinetochore obo:GO_1905341 inhibition of condensin localization to kinetochore obo:GO_1905341 inhibition of protein localisation to kinetochore obo:GO_1905341 inhibition of protein localization to kinetochore obo:GO_1905341 negative regulation of condensin localization to kinetochore obo:GO_1905341 biological_process obo:GO_1905341 GO:1905341 obo:GO_1905341 Q9H211 in Human in PMID:22581055 obo:GO_1905341 negative regulation of protein localization to kinetochore obo:GO_1905342 Any process that activates or increases the frequency, rate or extent of protein localization to kinetochore. obo:GO_1905342 obo:go.owl obo:GO_1905342 es obo:GO_1905342 2016-07-27T15:26:51Z obo:GO_1905342 positive regulation of protein localisation to kinetochore obo:GO_1905342 up regulation of protein localisation to kinetochore obo:GO_1905342 up regulation of protein localization to kinetochore obo:GO_1905342 up-regulation of protein localisation to kinetochore obo:GO_1905342 up-regulation of protein localization to kinetochore obo:GO_1905342 upregulation of protein localisation to kinetochore obo:GO_1905342 upregulation of protein localization to kinetochore obo:GO_1905342 activation of condensin localization to kinetochore obo:GO_1905342 activation of protein localisation to kinetochore obo:GO_1905342 activation of protein localization to kinetochore obo:GO_1905342 positive regulation of condensin localization to kinetochore obo:GO_1905342 up regulation of condensin localization to kinetochore obo:GO_1905342 up-regulation of condensin localization to kinetochore obo:GO_1905342 upregulation of condensin localization to kinetochore obo:GO_1905342 biological_process obo:GO_1905342 GO:1905342 obo:GO_1905342 Q9H211 in Human in PMID:22581055 obo:GO_1905342 positive regulation of protein localization to kinetochore obo:GO_1905384 Any process that modulates the frequency, rate or extent of protein localization to presynapse. obo:GO_1905384 obo:go.owl obo:GO_1905384 dos obo:GO_1905384 2016-08-18T14:56:00Z obo:GO_1905384 regulation of protein localisation in presynapse obo:GO_1905384 regulation of protein localisation to presynapse obo:GO_1905384 regulation of protein localization in presynapse obo:GO_1905384 regulation of recruitment of presynaptic proteins obo:GO_1905384 biological_process obo:GO_1905384 GO:1905384 obo:GO_1905384 regulation of protein localization to presynapse obo:GO_1905385 Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to presynapse. obo:GO_1905385 obo:go.owl obo:GO_1905385 dos obo:GO_1905385 2016-08-18T14:56:08Z obo:GO_1905385 down regulation of protein localisation in presynapse obo:GO_1905385 down regulation of protein localisation to presynapse obo:GO_1905385 down regulation of protein localization in presynapse obo:GO_1905385 down regulation of protein localization to presynapse obo:GO_1905385 down regulation of recruitment of presynaptic proteins obo:GO_1905385 down-regulation of protein localisation in presynapse obo:GO_1905385 down-regulation of protein localisation to presynapse obo:GO_1905385 down-regulation of protein localization in presynapse obo:GO_1905385 down-regulation of protein localization to presynapse obo:GO_1905385 down-regulation of recruitment of presynaptic proteins obo:GO_1905385 downregulation of protein localisation in presynapse obo:GO_1905385 downregulation of protein localisation to presynapse obo:GO_1905385 downregulation of protein localization in presynapse obo:GO_1905385 downregulation of protein localization to presynapse obo:GO_1905385 downregulation of recruitment of presynaptic proteins obo:GO_1905385 negative regulation of protein localisation in presynapse obo:GO_1905385 negative regulation of protein localisation to presynapse obo:GO_1905385 negative regulation of protein localization in presynapse obo:GO_1905385 negative regulation of recruitment of presynaptic proteins obo:GO_1905385 inhibition of protein localisation in presynapse obo:GO_1905385 inhibition of protein localisation to presynapse obo:GO_1905385 inhibition of protein localization in presynapse obo:GO_1905385 inhibition of protein localization to presynapse obo:GO_1905385 inhibition of recruitment of presynaptic proteins obo:GO_1905385 biological_process obo:GO_1905385 GO:1905385 obo:GO_1905385 negative regulation of protein localization to presynapse obo:GO_1905386 Any process that activates or increases the frequency, rate or extent of protein localization to presynapse. obo:GO_1905386 obo:go.owl obo:GO_1905386 dos obo:GO_1905386 2016-08-18T14:56:21Z obo:GO_1905386 positive regulation of protein localisation in presynapse obo:GO_1905386 positive regulation of protein localisation to presynapse obo:GO_1905386 positive regulation of protein localization in presynapse obo:GO_1905386 positive regulation of recruitment of presynaptic proteins obo:GO_1905386 up regulation of protein localisation in presynapse obo:GO_1905386 up regulation of protein localisation to presynapse obo:GO_1905386 up regulation of protein localization in presynapse obo:GO_1905386 up regulation of protein localization to presynapse obo:GO_1905386 up regulation of recruitment of presynaptic proteins obo:GO_1905386 up-regulation of protein localisation in presynapse obo:GO_1905386 up-regulation of protein localisation to presynapse obo:GO_1905386 up-regulation of protein localization in presynapse obo:GO_1905386 up-regulation of protein localization to presynapse obo:GO_1905386 up-regulation of recruitment of presynaptic proteins obo:GO_1905386 upregulation of protein localisation in presynapse obo:GO_1905386 upregulation of protein localisation to presynapse obo:GO_1905386 upregulation of protein localization in presynapse obo:GO_1905386 upregulation of protein localization to presynapse obo:GO_1905386 upregulation of recruitment of presynaptic proteins obo:GO_1905386 activation of protein localisation in presynapse obo:GO_1905386 activation of protein localisation to presynapse obo:GO_1905386 activation of protein localization in presynapse obo:GO_1905386 activation of protein localization to presynapse obo:GO_1905386 activation of recruitment of presynaptic proteins obo:GO_1905386 biological_process obo:GO_1905386 GO:1905386 obo:GO_1905386 positive regulation of protein localization to presynapse obo:GO_1905391 Any regulation of protein localization to cell division site that is involved in cell separation after cytokinesis. obo:GO_1905391 obo:go.owl obo:GO_1905391 vw obo:GO_1905391 2016-08-22T09:40:47Z obo:GO_1905391 regulation of protein localisation to cell division site involved in cell separation after cytokinesis obo:GO_1905391 regulation of protein localisation to cell division site involved in cell separation following cytokinesis obo:GO_1905391 regulation of protein localisation to cell division site involved in mitotic cytokinetic cell separation obo:GO_1905391 biological_process obo:GO_1905391 regulation of protein localisation to cell division site involved in cytokinetic cell separation obo:GO_1905391 GO:1905391 obo:GO_1905391 regulation of protein localization to cell division site involved in cell separation after cytokinesis obo:GO_1905394 Interacting selectively and non-covalently with a retromer complex. obo:GO_1905394 obo:go.owl obo:GO_1905394 bc obo:GO_1905394 2016-08-24T14:00:32Z obo:GO_1905394 molecular_function obo:GO_1905394 GO:1905394 obo:GO_1905394 retromer complex binding obo:GO_1905475 Any process that modulates the frequency, rate or extent of protein localization to membrane. obo:GO_1905475 obo:go.owl obo:GO_1905475 bc obo:GO_1905475 2016-09-21T16:20:03Z obo:GO_1905475 regulation of protein localisation in membrane obo:GO_1905475 regulation of protein localization in membrane obo:GO_1905475 biological_process obo:GO_1905475 GO:1905475 obo:GO_1905475 regulation of protein localization to membrane obo:GO_1905476 Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to membrane. obo:GO_1905476 obo:go.owl obo:GO_1905476 bc obo:GO_1905476 2016-09-21T16:20:10Z obo:GO_1905476 down regulation of protein localisation in membrane obo:GO_1905476 down regulation of protein localization in membrane obo:GO_1905476 down regulation of protein localization to membrane obo:GO_1905476 down-regulation of protein localisation in membrane obo:GO_1905476 down-regulation of protein localization in membrane obo:GO_1905476 down-regulation of protein localization to membrane obo:GO_1905476 downregulation of protein localisation in membrane obo:GO_1905476 downregulation of protein localization in membrane obo:GO_1905476 downregulation of protein localization to membrane obo:GO_1905476 negative regulation of protein localisation in membrane obo:GO_1905476 negative regulation of protein localization in membrane obo:GO_1905476 inhibition of protein localisation in membrane obo:GO_1905476 inhibition of protein localization in membrane obo:GO_1905476 inhibition of protein localization to membrane obo:GO_1905476 biological_process obo:GO_1905476 GO:1905476 obo:GO_1905476 negative regulation of protein localization to membrane obo:GO_1905477 Any process that activates or increases the frequency, rate or extent of protein localization to membrane. obo:GO_1905477 obo:go.owl obo:GO_1905477 bc obo:GO_1905477 2016-09-21T16:20:18Z obo:GO_1905477 positive regulation of protein localisation in membrane obo:GO_1905477 positive regulation of protein localization in membrane obo:GO_1905477 up regulation of protein localisation in membrane obo:GO_1905477 up regulation of protein localization in membrane obo:GO_1905477 up regulation of protein localization to membrane obo:GO_1905477 up-regulation of protein localisation in membrane obo:GO_1905477 up-regulation of protein localization in membrane obo:GO_1905477 up-regulation of protein localization to membrane obo:GO_1905477 upregulation of protein localisation in membrane obo:GO_1905477 upregulation of protein localization in membrane obo:GO_1905477 upregulation of protein localization to membrane obo:GO_1905477 activation of protein localisation in membrane obo:GO_1905477 activation of protein localization in membrane obo:GO_1905477 activation of protein localization to membrane obo:GO_1905477 biological_process obo:GO_1905477 GO:1905477 obo:GO_1905477 positive regulation of protein localization to membrane obo:GO_1905502 Interacting selectively and non-covalently with acetyl-CoA. obo:GO_1905502 obo:go.owl obo:GO_1905502 bc obo:GO_1905502 2016-09-27T16:33:44Z obo:GO_1905502 molecular_function obo:GO_1905502 GO:1905502 obo:GO_1905502 acetyl-CoA binding obo:GO_1905538 Interacting selectively and non-covalently with a polysome. obo:GO_1905538 obo:go.owl obo:GO_1905538 bc obo:GO_1905538 2016-10-07T14:02:53Z obo:GO_1905538 polyribosome binding obo:GO_1905538 molecular_function obo:GO_1905538 GO:1905538 obo:GO_1905538 polysome binding obo:GO_1905550 Any process that modulates the frequency, rate or extent of protein localization to endoplasmic reticulum. obo:GO_1905550 obo:go.owl obo:GO_1905550 rz obo:GO_1905550 2016-10-12T11:37:01Z obo:GO_1905550 regulation of protein localisation in endoplasmic reticulum obo:GO_1905550 regulation of protein localization in ER obo:GO_1905550 regulation of protein localization in endoplasmic reticulum obo:GO_1905550 biological_process obo:GO_1905550 GO:1905550 obo:GO_1905550 regulation of protein localization to endoplasmic reticulum obo:GO_1905551 Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to endoplasmic reticulum. obo:GO_1905551 obo:go.owl obo:GO_1905551 rz obo:GO_1905551 2016-10-12T11:37:08Z obo:GO_1905551 down regulation of protein localisation in endoplasmic reticulum obo:GO_1905551 down regulation of protein localization in ER obo:GO_1905551 down regulation of protein localization in endoplasmic reticulum obo:GO_1905551 down regulation of protein localization to endoplasmic reticulum obo:GO_1905551 down-regulation of protein localisation in endoplasmic reticulum obo:GO_1905551 down-regulation of protein localization in ER obo:GO_1905551 down-regulation of protein localization in endoplasmic reticulum obo:GO_1905551 down-regulation of protein localization to endoplasmic reticulum obo:GO_1905551 downregulation of protein localisation in endoplasmic reticulum obo:GO_1905551 downregulation of protein localization in ER obo:GO_1905551 downregulation of protein localization in endoplasmic reticulum obo:GO_1905551 downregulation of protein localization to endoplasmic reticulum obo:GO_1905551 negative regulation of protein localisation in endoplasmic reticulum obo:GO_1905551 negative regulation of protein localization in ER obo:GO_1905551 negative regulation of protein localization in endoplasmic reticulum obo:GO_1905551 inhibition of protein localisation in endoplasmic reticulum obo:GO_1905551 inhibition of protein localization in ER obo:GO_1905551 inhibition of protein localization in endoplasmic reticulum obo:GO_1905551 inhibition of protein localization to endoplasmic reticulum obo:GO_1905551 biological_process obo:GO_1905551 GO:1905551 obo:GO_1905551 negative regulation of protein localization to endoplasmic reticulum obo:GO_1905552 Any process that activates or increases the frequency, rate or extent of protein localization to endoplasmic reticulum. obo:GO_1905552 obo:go.owl obo:GO_1905552 rz obo:GO_1905552 2016-10-12T11:37:16Z obo:GO_1905552 positive regulation of protein localisation in endoplasmic reticulum obo:GO_1905552 positive regulation of protein localization in ER obo:GO_1905552 positive regulation of protein localization in endoplasmic reticulum obo:GO_1905552 up regulation of protein localisation in endoplasmic reticulum obo:GO_1905552 up regulation of protein localization in ER obo:GO_1905552 up regulation of protein localization in endoplasmic reticulum obo:GO_1905552 up regulation of protein localization to endoplasmic reticulum obo:GO_1905552 up-regulation of protein localisation in endoplasmic reticulum obo:GO_1905552 up-regulation of protein localization in ER obo:GO_1905552 up-regulation of protein localization in endoplasmic reticulum obo:GO_1905552 up-regulation of protein localization to endoplasmic reticulum obo:GO_1905552 upregulation of protein localisation in endoplasmic reticulum obo:GO_1905552 upregulation of protein localization in ER obo:GO_1905552 upregulation of protein localization in endoplasmic reticulum obo:GO_1905552 upregulation of protein localization to endoplasmic reticulum obo:GO_1905552 activation of protein localisation in endoplasmic reticulum obo:GO_1905552 activation of protein localization in ER obo:GO_1905552 activation of protein localization in endoplasmic reticulum obo:GO_1905552 activation of protein localization to endoplasmic reticulum obo:GO_1905552 biological_process obo:GO_1905552 GO:1905552 obo:GO_1905552 positive regulation of protein localization to endoplasmic reticulum obo:GO_1905562 Any process that modulates the frequency, rate or extent of vascular endothelial cell proliferation. obo:GO_1905562 obo:go.owl obo:GO_1905562 nc obo:GO_1905562 2016-10-17T09:24:17Z obo:GO_1905562 biological_process obo:GO_1905562 GO:1905562 obo:GO_1905562 regulation of vascular endothelial cell proliferation obo:GO_1905563 Any process that stops, prevents or reduces the frequency, rate or extent of vascular endothelial cell proliferation. obo:GO_1905563 obo:go.owl obo:GO_1905563 nc obo:GO_1905563 2016-10-17T09:24:26Z obo:GO_1905563 down regulation of vascular endothelial cell proliferation obo:GO_1905563 down-regulation of vascular endothelial cell proliferation obo:GO_1905563 downregulation of vascular endothelial cell proliferation obo:GO_1905563 inhibition of vascular endothelial cell proliferation obo:GO_1905563 biological_process obo:GO_1905563 GO:1905563 obo:GO_1905563 negative regulation of vascular endothelial cell proliferation obo:GO_1905564 Any process that activates or increases the frequency, rate or extent of vascular endothelial cell proliferation. obo:GO_1905564 obo:go.owl obo:GO_1905564 nc obo:GO_1905564 2016-10-17T09:24:35Z obo:GO_1905564 up regulation of vascular endothelial cell proliferation obo:GO_1905564 up-regulation of vascular endothelial cell proliferation obo:GO_1905564 upregulation of vascular endothelial cell proliferation obo:GO_1905564 activation of vascular endothelial cell proliferation obo:GO_1905564 biological_process obo:GO_1905564 GO:1905564 obo:GO_1905564 positive regulation of vascular endothelial cell proliferation obo:GO_1905573 Interacting selectively and non-covalently with ganglioside GM1. obo:GO_1905573 obo:go.owl obo:GO_1905573 pga obo:GO_1905573 2016-10-19T10:57:28Z obo:GO_1905573 molecular_function obo:GO_1905573 GO:1905573 obo:GO_1905573 ganglioside GM1 binding obo:GO_1905574 Interacting selectively and non-covalently with ganglioside GM2. obo:GO_1905574 obo:go.owl obo:GO_1905574 pga obo:GO_1905574 2016-10-19T11:17:01Z obo:GO_1905574 molecular_function obo:GO_1905574 GO:1905574 obo:GO_1905574 ganglioside GM2 binding obo:GO_1905575 Interacting selectively and non-covalently with ganglioside GM3. obo:GO_1905575 obo:go.owl obo:GO_1905575 pga obo:GO_1905575 2016-10-19T11:17:10Z obo:GO_1905575 molecular_function obo:GO_1905575 GO:1905575 obo:GO_1905575 ganglioside GM3 binding obo:GO_1905576 Interacting selectively and non-covalently with ganglioside GT1b. obo:GO_1905576 obo:go.owl obo:GO_1905576 pga obo:GO_1905576 2016-10-19T11:17:17Z obo:GO_1905576 molecular_function obo:GO_1905576 GO:1905576 obo:GO_1905576 ganglioside GT1b binding obo:GO_1905577 Interacting selectively and non-covalently with ganglioside GP1c. obo:GO_1905577 obo:go.owl obo:GO_1905577 pga obo:GO_1905577 2016-10-19T11:17:25Z obo:GO_1905577 molecular_function obo:GO_1905577 GO:1905577 obo:GO_1905577 ganglioside GP1c binding obo:GO_1905594 Interacting selectively and non-covalently with resveratrol. obo:GO_1905594 obo:go.owl obo:GO_1905594 pga obo:GO_1905594 2016-10-25T15:23:37Z obo:GO_1905594 molecular_function obo:GO_1905594 GO:1905594 obo:GO_1905594 (5-(aziridin-1-yl)-2,4-dinitrobenzamide obo:GO_1905594 resveratrol binding obo:GO_1905634 Any process that modulates the frequency, rate or extent of protein localization to chromatin. obo:GO_1905634 obo:go.owl obo:GO_1905634 pga obo:GO_1905634 2016-11-01T16:33:52Z obo:GO_1905634 regulation of protein localisation to chromatin obo:GO_1905634 biological_process obo:GO_1905634 GO:1905634 obo:GO_1905634 regulation of protein localization to chromatin obo:GO_1905664 Any process that modulates the frequency, rate or extent of calcium ion import across plasma membrane. obo:GO_1905664 obo:go.owl obo:GO_1905664 bhm obo:GO_1905664 2016-11-11T09:26:06Z obo:GO_1905664 biological_process obo:GO_1905664 GO:1905664 obo:GO_1905664 An example of this is PPP3CA in human (Q08209) in 17640527 (inferred from direct assay). obo:GO_1905664 regulation of calcium ion import across plasma membrane obo:GO_1905665 Any process that activates or increases the frequency, rate or extent of calcium ion import across plasma membrane. obo:GO_1905665 obo:go.owl obo:GO_1905665 bhm obo:GO_1905665 2016-11-11T09:26:23Z obo:GO_1905665 up regulation of calcium ion import across plasma membrane obo:GO_1905665 up-regulation of calcium ion import across plasma membrane obo:GO_1905665 upregulation of calcium ion import across plasma membrane obo:GO_1905665 activation of calcium ion import across plasma membrane obo:GO_1905665 biological_process obo:GO_1905665 GO:1905665 obo:GO_1905665 An example of this is PPP3CA in human (Q08209) in 17640527 (inferred from direct assay). obo:GO_1905665 positive regulation of calcium ion import across plasma membrane obo:GO_1905666 Any process that modulates the frequency, rate or extent of protein localization to endosome. obo:GO_1905666 obo:go.owl obo:GO_1905666 bc obo:GO_1905666 2016-11-11T11:19:01Z obo:GO_1905666 regulation of protein localisation in endosome obo:GO_1905666 regulation of protein localization in endosome obo:GO_1905666 biological_process obo:GO_1905666 GO:1905666 obo:GO_1905666 regulation of protein localization to endosome obo:GO_1905667 Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to endosome. obo:GO_1905667 obo:go.owl obo:GO_1905667 bc obo:GO_1905667 2016-11-11T11:19:09Z obo:GO_1905667 down regulation of protein localisation in endosome obo:GO_1905667 down regulation of protein localization in endosome obo:GO_1905667 down regulation of protein localization to endosome obo:GO_1905667 down-regulation of protein localisation in endosome obo:GO_1905667 down-regulation of protein localization in endosome obo:GO_1905667 down-regulation of protein localization to endosome obo:GO_1905667 downregulation of protein localisation in endosome obo:GO_1905667 downregulation of protein localization in endosome obo:GO_1905667 downregulation of protein localization to endosome obo:GO_1905667 negative regulation of protein localisation in endosome obo:GO_1905667 negative regulation of protein localization in endosome obo:GO_1905667 inhibition of protein localisation in endosome obo:GO_1905667 inhibition of protein localization in endosome obo:GO_1905667 inhibition of protein localization to endosome obo:GO_1905667 biological_process obo:GO_1905667 GO:1905667 obo:GO_1905667 negative regulation of protein localization to endosome obo:GO_1905668 Any process that activates or increases the frequency, rate or extent of protein localization to endosome. obo:GO_1905668 obo:go.owl obo:GO_1905668 bc obo:GO_1905668 2016-11-11T11:19:17Z obo:GO_1905668 positive regulation of protein localisation in endosome obo:GO_1905668 positive regulation of protein localization in endosome obo:GO_1905668 up regulation of protein localisation in endosome obo:GO_1905668 up regulation of protein localization in endosome obo:GO_1905668 up regulation of protein localization to endosome obo:GO_1905668 up-regulation of protein localisation in endosome obo:GO_1905668 up-regulation of protein localization in endosome obo:GO_1905668 up-regulation of protein localization to endosome obo:GO_1905668 upregulation of protein localisation in endosome obo:GO_1905668 upregulation of protein localization in endosome obo:GO_1905668 upregulation of protein localization to endosome obo:GO_1905668 activation of protein localisation in endosome obo:GO_1905668 activation of protein localization in endosome obo:GO_1905668 activation of protein localization to endosome obo:GO_1905668 biological_process obo:GO_1905668 GO:1905668 obo:GO_1905668 positive regulation of protein localization to endosome obo:GO_1905743 Any mitochondrial calcium uptake that is involved in negative regulation of presynaptic cytosolic calcium concentration. obo:GO_1905743 obo:go.owl obo:GO_1905743 dosumis obo:GO_1905743 2016-12-06T10:53:17Z obo:GO_1905743 calcium ion transmembrane import into mitochondrion involved in negative regulation of presynaptic cytosolic calcium concentration obo:GO_1905743 mitochondrial calcium uptake involved in negative regulation of presynaptic cytosolic calcium concentration obo:GO_1905743 biological_process obo:GO_1905743 GO:1905743 obo:GO_1905743 http://purl.oboInOwllibrary.org/oboInOwl/go#goslim_synapse obo:GO_1905743 calcium import into the mitochondrion involved in negative regulation of presynaptic cytosolic calcium concentration obo:GO_1905761 Interacting selectively and non-covalently with a SCF ubiquitin ligase complex. obo:GO_1905761 obo:go.owl obo:GO_1905761 ukemi obo:GO_1905761 2016-12-14T15:08:12Z obo:GO_1905761 CDL1 complex binding obo:GO_1905761 CRL1 complex binding obo:GO_1905761 Cul1-RING ubiquitin ligase complex binding obo:GO_1905761 SCF complex binding obo:GO_1905761 Skp1/Cul1/F-box protein complex binding obo:GO_1905761 cullin-RING ligase 1 binding obo:GO_1905761 SCF complex substrate recognition subunit binding obo:GO_1905761 molecular_function obo:GO_1905761 GO:1905761 obo:GO_1905761 SCF ubiquitin ligase complex binding obo:GO_1905762 Interacting selectively and non-covalently with a CCR4-NOT complex. obo:GO_1905762 obo:go.owl obo:GO_1905762 mah11 obo:GO_1905762 2016-12-15T15:48:53Z obo:GO_1905762 molecular_function obo:GO_1905762 GO:1905762 obo:GO_1905762 CCR4-NOT complex binding obo:GO_1905763 Interacting selectively and non-covalently with a MTREC complex. obo:GO_1905763 obo:go.owl obo:GO_1905763 mah11 obo:GO_1905763 2016-12-15T15:49:02Z obo:GO_1905763 Mtl1-Red1 core complex binding obo:GO_1905763 molecular_function obo:GO_1905763 GO:1905763 obo:GO_1905763 MTREC complex binding obo:GO_1905773 Interacting selectively and non-covalently with 8-hydroxy-2'-deoxyguanosine an oxidized purine residue found in damaged DNA. obo:GO_1905773 obo:go.owl obo:GO_1905773 NancyCampbell obo:GO_1905773 2016-12-21T15:57:27Z obo:GO_1905773 molecular_function obo:GO_1905773 GO:1905773 obo:GO_1905773 8-hydroxy-2'-deoxyguanosine DNA binding obo:GO_1905802 Any process that modulates the frequency, rate or extent of cellular response to manganese ion. obo:GO_1905802 obo:go.owl obo:GO_1905802 pgarmiri obo:GO_1905802 2017-01-11T14:59:39Z obo:GO_1905802 regulation of cellular response to manganese obo:GO_1905802 biological_process obo:GO_1905802 GO:1905802 obo:GO_1905802 regulation of cellular response to manganese ion obo:GO_1905803 Any process that stops, prevents or reduces the frequency, rate or extent of cellular response to manganese ion. obo:GO_1905803 obo:go.owl obo:GO_1905803 pgarmiri obo:GO_1905803 2017-01-11T14:59:48Z obo:GO_1905803 down regulation of cellular response to manganese obo:GO_1905803 down regulation of cellular response to manganese ion obo:GO_1905803 down-regulation of cellular response to manganese obo:GO_1905803 down-regulation of cellular response to manganese ion obo:GO_1905803 downregulation of cellular response to manganese obo:GO_1905803 downregulation of cellular response to manganese ion obo:GO_1905803 negative regulation of cellular response to manganese obo:GO_1905803 inhibition of cellular response to manganese obo:GO_1905803 inhibition of cellular response to manganese ion obo:GO_1905803 biological_process obo:GO_1905803 GO:1905803 obo:GO_1905803 negative regulation of cellular response to manganese ion obo:GO_1905804 Any process that activates or increases the frequency, rate or extent of cellular response to manganese ion. obo:GO_1905804 obo:go.owl obo:GO_1905804 pgarmiri obo:GO_1905804 2017-01-11T14:59:57Z obo:GO_1905804 positive regulation of cellular response to manganese obo:GO_1905804 up regulation of cellular response to manganese obo:GO_1905804 up regulation of cellular response to manganese ion obo:GO_1905804 up-regulation of cellular response to manganese obo:GO_1905804 up-regulation of cellular response to manganese ion obo:GO_1905804 upregulation of cellular response to manganese obo:GO_1905804 upregulation of cellular response to manganese ion obo:GO_1905804 activation of cellular response to manganese obo:GO_1905804 activation of cellular response to manganese ion obo:GO_1905804 biological_process obo:GO_1905804 GO:1905804 obo:GO_1905804 positive regulation of cellular response to manganese ion obo:GO_1905871 Any process that modulates the frequency, rate or extent of protein localization to cell leading edge. obo:GO_1905871 obo:go.owl obo:GO_1905871 slaulederkind obo:GO_1905871 2017-01-27T19:34:55Z obo:GO_1905871 regulation of protein localisation in cell leading edge obo:GO_1905871 regulation of protein localisation to cell leading edge obo:GO_1905871 regulation of protein localization in cell leading edge obo:GO_1905871 biological_process obo:GO_1905871 GO:1905871 obo:GO_1905871 regulation of protein localization to cell leading edge obo:GO_1905872 Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to cell leading edge. obo:GO_1905872 obo:go.owl obo:GO_1905872 slaulederkind obo:GO_1905872 2017-01-27T19:35:04Z obo:GO_1905872 down regulation of protein localisation in cell leading edge obo:GO_1905872 down regulation of protein localisation to cell leading edge obo:GO_1905872 down regulation of protein localization in cell leading edge obo:GO_1905872 down regulation of protein localization to cell leading edge obo:GO_1905872 down-regulation of protein localisation in cell leading edge obo:GO_1905872 down-regulation of protein localisation to cell leading edge obo:GO_1905872 down-regulation of protein localization in cell leading edge obo:GO_1905872 down-regulation of protein localization to cell leading edge obo:GO_1905872 downregulation of protein localisation in cell leading edge obo:GO_1905872 downregulation of protein localisation to cell leading edge obo:GO_1905872 downregulation of protein localization in cell leading edge obo:GO_1905872 downregulation of protein localization to cell leading edge obo:GO_1905872 negative regulation of protein localisation in cell leading edge obo:GO_1905872 negative regulation of protein localisation to cell leading edge obo:GO_1905872 negative regulation of protein localization in cell leading edge obo:GO_1905872 inhibition of protein localisation in cell leading edge obo:GO_1905872 inhibition of protein localisation to cell leading edge obo:GO_1905872 inhibition of protein localization in cell leading edge obo:GO_1905872 inhibition of protein localization to cell leading edge obo:GO_1905872 biological_process obo:GO_1905872 GO:1905872 obo:GO_1905872 negative regulation of protein localization to cell leading edge obo:GO_1905873 Any process that activates or increases the frequency, rate or extent of protein localization to cell leading edge. obo:GO_1905873 obo:go.owl obo:GO_1905873 slaulederkind obo:GO_1905873 2017-01-27T19:35:13Z obo:GO_1905873 positive regulation of protein localisation in cell leading edge obo:GO_1905873 positive regulation of protein localisation to cell leading edge obo:GO_1905873 positive regulation of protein localization in cell leading edge obo:GO_1905873 up regulation of protein localisation in cell leading edge obo:GO_1905873 up regulation of protein localisation to cell leading edge obo:GO_1905873 up regulation of protein localization in cell leading edge obo:GO_1905873 up regulation of protein localization to cell leading edge obo:GO_1905873 up-regulation of protein localisation in cell leading edge obo:GO_1905873 up-regulation of protein localisation to cell leading edge obo:GO_1905873 up-regulation of protein localization in cell leading edge obo:GO_1905873 up-regulation of protein localization to cell leading edge obo:GO_1905873 upregulation of protein localisation in cell leading edge obo:GO_1905873 upregulation of protein localisation to cell leading edge obo:GO_1905873 upregulation of protein localization in cell leading edge obo:GO_1905873 upregulation of protein localization to cell leading edge obo:GO_1905873 activation of protein localisation in cell leading edge obo:GO_1905873 activation of protein localisation to cell leading edge obo:GO_1905873 activation of protein localization in cell leading edge obo:GO_1905873 activation of protein localization to cell leading edge obo:GO_1905873 biological_process obo:GO_1905873 GO:1905873 obo:GO_1905873 positive regulation of protein localization to cell leading edge obo:GO_1905912 Any process that modulates the frequency, rate or extent of calcium ion export across the plasma membrane. obo:GO_1905912 obo:go.owl obo:GO_1905912 rachhuntley obo:GO_1905912 2017-02-07T13:20:39Z obo:GO_1905912 regulation of calcium ion efflux from cell obo:GO_1905912 regulation of calcium ion export from cell obo:GO_1905912 biological_process obo:GO_1905912 GO:1905912 obo:GO_1905912 regulation of calcium ion export across plasma membrane obo:GO_1905913 Any process that stops, prevents or reduces the frequency, rate or extent of calcium ion export across the plasma membrane. obo:GO_1905913 obo:go.owl obo:GO_1905913 rachhuntley obo:GO_1905913 2017-02-07T13:20:48Z obo:GO_1905913 down regulation of calcium ion efflux from cell obo:GO_1905913 down regulation of calcium ion export from cell obo:GO_1905913 down-regulation of calcium ion efflux from cell obo:GO_1905913 down-regulation of calcium ion export from cell obo:GO_1905913 downregulation of calcium ion efflux from cell obo:GO_1905913 downregulation of calcium ion export from cell obo:GO_1905913 negative regulation of calcium ion efflux from cell obo:GO_1905913 negative regulation of calcium ion export from cell obo:GO_1905913 inhibition of calcium ion efflux from cell obo:GO_1905913 inhibition of calcium ion export from cell obo:GO_1905913 biological_process obo:GO_1905913 GO:1905913 obo:GO_1905913 negative regulation of calcium ion export across plasma membrane obo:GO_1905914 Any process that activates or increases the frequency, rate or extent of calcium ion export across the plasma membrane. obo:GO_1905914 obo:go.owl obo:GO_1905914 rachhuntley obo:GO_1905914 2017-02-07T13:20:56Z obo:GO_1905914 positive regulation of calcium ion efflux from cell obo:GO_1905914 positive regulation of calcium ion export from cell obo:GO_1905914 up regulation of calcium ion efflux from cell obo:GO_1905914 up regulation of calcium ion export from cell obo:GO_1905914 up-regulation of calcium ion efflux from cell obo:GO_1905914 up-regulation of calcium ion export from cell obo:GO_1905914 upregulation of calcium ion efflux from cell obo:GO_1905914 upregulation of calcium ion export from cell obo:GO_1905914 activation of calcium ion efflux from cell obo:GO_1905914 activation of calcium ion export from cell obo:GO_1905914 biological_process obo:GO_1905914 GO:1905914 obo:GO_1905914 positive regulation of calcium ion export across plasma membrane obo:GO_1905945 Any process that modulates the frequency, rate or extent of response to calcium ion. obo:GO_1905945 obo:go.owl obo:GO_1905945 BarbaraCzub obo:GO_1905945 2017-02-13T10:56:34Z obo:GO_1905945 regulation of response to Ca2+ ion obo:GO_1905945 biological_process obo:GO_1905945 GO:1905945 obo:GO_1905945 regulation of response to calcium ion obo:GO_1905946 Any process that stops, prevents or reduces the frequency, rate or extent of response to calcium ion. obo:GO_1905946 obo:go.owl obo:GO_1905946 BarbaraCzub obo:GO_1905946 2017-02-13T10:56:41Z obo:GO_1905946 down regulation of response to Ca2+ ion obo:GO_1905946 down regulation of response to calcium ion obo:GO_1905946 down-regulation of response to Ca2+ ion obo:GO_1905946 down-regulation of response to calcium ion obo:GO_1905946 downregulation of response to Ca2+ ion obo:GO_1905946 downregulation of response to calcium ion obo:GO_1905946 negative regulation of response to Ca2+ ion obo:GO_1905946 inhibition of response to Ca2+ ion obo:GO_1905946 inhibition of response to calcium ion obo:GO_1905946 biological_process obo:GO_1905946 GO:1905946 obo:GO_1905946 negative regulation of response to calcium ion obo:GO_1905947 Any process that activates or increases the frequency, rate or extent of response to calcium ion. obo:GO_1905947 obo:go.owl obo:GO_1905947 BarbaraCzub obo:GO_1905947 2017-02-13T10:56:49Z obo:GO_1905947 positive regulation of response to Ca2+ ion obo:GO_1905947 up regulation of response to Ca2+ ion obo:GO_1905947 up regulation of response to calcium ion obo:GO_1905947 up-regulation of response to Ca2+ ion obo:GO_1905947 up-regulation of response to calcium ion obo:GO_1905947 upregulation of response to Ca2+ ion obo:GO_1905947 upregulation of response to calcium ion obo:GO_1905947 activation of response to Ca2+ ion obo:GO_1905947 activation of response to calcium ion obo:GO_1905947 biological_process obo:GO_1905947 GO:1905947 obo:GO_1905947 positive regulation of response to calcium ion obo:GO_1905949 Any process that stops, prevents or reduces the frequency, rate or extent of calcium ion import across plasma membrane. obo:GO_1905949 obo:go.owl obo:GO_1905949 bmeldal obo:GO_1905949 2017-02-17T09:42:30Z obo:GO_1905949 down regulation of calcium ion import across plasma membrane obo:GO_1905949 down-regulation of calcium ion import across plasma membrane obo:GO_1905949 downregulation of calcium ion import across plasma membrane obo:GO_1905949 inhibition of calcium ion import across plasma membrane obo:GO_1905949 biological_process obo:GO_1905949 GO:1905949 obo:GO_1905949 An example of this is PPP3CA in human (Q08209) in PMID:17640527 (inferred from direct assay). obo:GO_1905949 negative regulation of calcium ion import across plasma membrane obo:GO_1905952 Any process that modulates the frequency, rate or extent of lipid localization. obo:GO_1905952 obo:go.owl obo:GO_1905952 rozaru obo:GO_1905952 2017-02-21T12:12:22Z obo:GO_1905952 regulation of lipid localisation obo:GO_1905952 biological_process obo:GO_1905952 GO:1905952 obo:GO_1905952 regulation of lipid localization obo:GO_1905953 Any process that stops, prevents or reduces the frequency, rate or extent of lipid localization. obo:GO_1905953 obo:go.owl obo:GO_1905953 rozaru obo:GO_1905953 2017-02-21T12:12:41Z obo:GO_1905953 down regulation of lipid localisation obo:GO_1905953 down regulation of lipid localization obo:GO_1905953 down-regulation of lipid localisation obo:GO_1905953 down-regulation of lipid localization obo:GO_1905953 downregulation of lipid localisation obo:GO_1905953 downregulation of lipid localization obo:GO_1905953 negative regulation of lipid localisation obo:GO_1905953 inhibition of lipid localisation obo:GO_1905953 inhibition of lipid localization obo:GO_1905953 biological_process obo:GO_1905953 GO:1905953 obo:GO_1905953 negative regulation of lipid localization obo:GO_1905954 Any process that activates or increases the frequency, rate or extent of lipid localization. obo:GO_1905954 obo:go.owl obo:GO_1905954 rozaru obo:GO_1905954 2017-02-21T12:12:49Z obo:GO_1905954 positive regulation of lipid localisation obo:GO_1905954 up regulation of lipid localisation obo:GO_1905954 up regulation of lipid localization obo:GO_1905954 up-regulation of lipid localisation obo:GO_1905954 up-regulation of lipid localization obo:GO_1905954 upregulation of lipid localisation obo:GO_1905954 upregulation of lipid localization obo:GO_1905954 activation of lipid localisation obo:GO_1905954 activation of lipid localization obo:GO_1905954 biological_process obo:GO_1905954 GO:1905954 obo:GO_1905954 positive regulation of lipid localization obo:GO_1990034 The directed movement of calcium ions from inside of a cell, across the plasma membrane and into the extracellular region. obo:GO_1990034 obo:go.owl obo:GO_1990034 mah obo:GO_1990034 2013-02-07T13:01:29Z obo:GO_1990034 calcium ion efflux from cell obo:GO_1990034 calcium ion export from cell obo:GO_1990034 biological_process obo:GO_1990034 GO:1990034 obo:GO_1990034 calcium ion export across plasma membrane obo:GO_1990036 The directed movement of calcium ions into a sarcoplasmic reticulum. obo:GO_1990036 obo:go.owl obo:GO_1990036 tb obo:GO_1990036 2013-02-07T23:22:27Z obo:GO_1990036 biological_process obo:GO_1990036 GO:1990036 obo:GO_1990036 calcium ion import into sarcoplasmic reticulum obo:GO_1990066 The process by which excess light energy absorbed by chlorophyll and not used to drive photosynthesis is emitted by nonphotochemical quenching or chlorophyll fluorescence. obo:GO_1990066 obo:go.owl obo:GO_1990066 tb obo:GO_1990066 2013-03-27T21:02:00Z obo:GO_1990066 biological_process obo:GO_1990066 GO:1990066 obo:GO_1990066 energy quenching obo:GO_1990147 Interacting selectively and non-covalently with a talin, a family of related cytoskeletal proteins that play a role in assembly of actin filaments and migration of various cell types. obo:GO_1990147 obo:go.owl obo:GO_1990147 hjd obo:GO_1990147 2013-07-25T19:49:53Z obo:GO_1990147 molecular_function obo:GO_1990147 GO:1990147 obo:GO_1990147 talin binding obo:GO_1990165 Interacting selectively and non-covalently with damaged DNA containing single-strand breaks (SSBs). obo:GO_1990165 obo:go.owl obo:GO_1990165 pr obo:GO_1990165 2013-08-08T11:16:04Z obo:GO_1990165 SSB-containing DNA binding obo:GO_1990165 single-strand break-containing damaged DNA binding obo:GO_1990165 molecular_function obo:GO_1990165 GO:1990165 obo:GO_1990165 single-strand break-containing DNA binding obo:GO_1990175 Interacting selectively and non-covalently with an EH domain of a protein. The EH stand for Eps15 homology. This was originally identified as a motif present in three copies at the NH2-termini of Eps15 and of the related molecule Eps15R. obo:GO_1990175 obo:go.owl obo:GO_1990175 hjd obo:GO_1990175 2013-08-27T20:14:56Z obo:GO_1990175 molecular_function obo:GO_1990175 GO:1990175 obo:GO_1990175 EH domain binding obo:GO_1990226 Interacting selectively and non-covalently with a histone methyltransferase enzyme. obo:GO_1990226 obo:go.owl obo:GO_1990226 pr obo:GO_1990226 2013-11-07T11:59:58Z obo:GO_1990226 molecular_function obo:GO_1990226 GO:1990226 obo:GO_1990226 histone methyltransferase binding obo:GO_1990239 Interacting selectively and non-covalently with a steroid hormone. obo:GO_1990239 obo:go.owl obo:GO_1990239 pr obo:GO_1990239 2013-11-15T09:26:18Z obo:GO_1990239 molecular_function obo:GO_1990239 GO:1990239 obo:GO_1990239 steroid hormone binding obo:GO_1990244 Catalysis of the transfer of a phosphate group to the threonine-120 residue of histone H2A. obo:GO_1990244 obo:go.owl obo:GO_1990244 sp obo:GO_1990244 2013-12-04T06:38:32Z obo:GO_1990244 histone threonine kinase activity (H2A-T120 specific) obo:GO_1990244 molecular_function obo:GO_1990244 GO:1990244 obo:GO_1990244 histone kinase activity (H2A-T120 specific) obo:GO_1990247 Interacting selectively and non-covalently with an RNA molecule modified by N6-methyladenosine (m6A), a modification present at internal sites of mRNAs and some non-coding RNAs. obo:GO_1990247 obo:go.owl obo:GO_1990247 sp obo:GO_1990247 2013-12-04T06:55:29Z obo:GO_1990247 molecular_function obo:GO_1990247 GO:1990247 obo:GO_1990247 N6-methyladenosine-containing RNA binding obo:GO_1990253 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of leucine. obo:GO_1990253 obo:go.owl obo:GO_1990253 al obo:GO_1990253 2013-12-10T11:55:10Z obo:GO_1990253 CHEBI:25017 obo:GO_1990253 biological_process obo:GO_1990253 GO:1990253 obo:GO_1990253 cellular response to leucine starvation obo:GO_1990254 Interacting selectively and non-covalently with a keratin filament, an intermediate filament composed of acidic and basic keratins (types I and II), typically expressed in epithelial cells. obo:GO_1990254 obo:go.owl obo:GO_1990254 tb obo:GO_1990254 2013-12-13T22:05:25Z obo:GO_1990254 molecular_function obo:GO_1990254 GO:1990254 obo:GO_1990254 keratin filament binding obo:GO_1990267 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a transition metal nanoparticle. obo:GO_1990267 obo:go.owl obo:GO_1990267 sl obo:GO_1990267 2014-01-10T17:16:41Z obo:GO_1990267 biological_process obo:GO_1990267 response to colloidal metal obo:GO_1990267 response to neutral metal atoms obo:GO_1990267 GO:1990267 obo:GO_1990267 response to transition metal nanoparticle obo:GO_1990268 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a gold nanoparticle stimulus. obo:GO_1990268 obo:go.owl obo:GO_1990268 sl obo:GO_1990268 2014-01-10T17:37:34Z obo:GO_1990268 biological_process obo:GO_1990268 GO:1990268 obo:GO_1990268 response to gold nanoparticle obo:GO_1990269 Interacting selectively and non-covalently with phosphorylated serine residues in the C-terminal domain of RNA polymerase II. obo:GO_1990269 obo:go.owl obo:GO_1990269 tb obo:GO_1990269 2014-01-11T00:34:59Z obo:GO_1990269 RNA Pol II C-terminal domain phosphoserine binding obo:GO_1990269 RNAP II C-terminal domain phosphoserine binding obo:GO_1990269 molecular_function obo:GO_1990269 GO:1990269 obo:GO_1990269 RNA polymerase II C-terminal domain phosphoserine binding obo:GO_1990275 Interacting selectively and non-covalently with any part of a preribosome. obo:GO_1990275 obo:go.owl obo:GO_1990275 tb obo:GO_1990275 2014-01-16T19:14:50Z obo:GO_1990275 molecular_function obo:GO_1990275 GO:1990275 obo:GO_1990275 preribosome binding obo:GO_1990294 The phosphorylation of a peptidyl-threonine to form peptidyl-O-phospho-L-threonine on an identical protein. For example, phosphorylation by the other kinase within a homodimer. obo:GO_1990294 obo:go.owl obo:GO_1990294 al obo:GO_1990294 2014-02-05T12:42:46Z obo:GO_1990294 biological_process obo:GO_1990294 GO:1990294 obo:GO_1990294 peptidyl-threonine trans-autophosphorylation obo:GO_1990308 Interacting selectively and non-covalently with a type-I dockerin domain of a protein. Type-I dockerin domain is the binding partner of type-1 cohesin domain. obo:GO_1990308 obo:go.owl obo:GO_1990308 tt obo:GO_1990308 2014-03-07T03:10:37Z obo:GO_1990308 molecular_function obo:GO_1990308 GO:1990308 obo:GO_1990308 type-I dockerin domain binding obo:GO_1990309 Interacting selectively and non-covalently with a type-II dockerin domain of a protein. Type-II dockerin domain is the binding partner of type-II cohesin domain. obo:GO_1990309 obo:go.owl obo:GO_1990309 tt obo:GO_1990309 2014-03-07T03:16:49Z obo:GO_1990309 molecular_function obo:GO_1990309 GO:1990309 obo:GO_1990309 type-II dockerin domain binding obo:GO_1990310 Interacting selectively and non-covalently with a type-III dockerin domain of a protein. Type-III dockerin domain is the binding partner of type-III cohesin domain. obo:GO_1990310 obo:go.owl obo:GO_1990310 tt obo:GO_1990310 2014-03-07T03:22:36Z obo:GO_1990310 molecular_function obo:GO_1990310 GO:1990310 obo:GO_1990310 type-III dockerin domain binding obo:GO_1990311 Interacting selectively and non-covalently with a type-I cohesin domain of a protein. Type-I cohesin domain is the binding partner of type-I dockerin domain. obo:GO_1990311 obo:go.owl obo:GO_1990311 tt obo:GO_1990311 2014-03-07T04:47:31Z obo:GO_1990311 molecular_function obo:GO_1990311 GO:1990311 obo:GO_1990311 type-I cohesin domain binding obo:GO_1990312 Interacting selectively and non-covalently with a type-II cohesin domain of a protein. Type-II cohesin domain is the binding partner of type-II dockerin domain. obo:GO_1990312 obo:go.owl obo:GO_1990312 tt obo:GO_1990312 2014-03-07T04:51:07Z obo:GO_1990312 molecular_function obo:GO_1990312 GO:1990312 obo:GO_1990312 type-II cohesin domain binding obo:GO_1990313 Interacting selectively and non-covalently with a type-III cohesin domain of a protein. Type-III cohesin domain is the binding partner of type-III dockerin domain. obo:GO_1990313 obo:go.owl obo:GO_1990313 tt obo:GO_1990313 2014-03-07T04:58:07Z obo:GO_1990313 molecular_function obo:GO_1990313 GO:1990313 obo:GO_1990313 type-III cohesin domain binding obo:GO_1990381 Interacting selectively and non-covalently with a ubiquitin-specific protease. obo:GO_1990381 obo:go.owl obo:GO_1990381 bf obo:GO_1990381 2014-05-19T10:01:53Z obo:GO_1990381 deubiquitinase binding obo:GO_1990381 deubiquitinating enzyme binding obo:GO_1990381 molecular_function obo:GO_1990381 GO:1990381 obo:GO_1990381 ubiquitin-specific protease binding obo:GO_1990383 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of biotin. obo:GO_1990383 obo:go.owl obo:GO_1990383 al obo:GO_1990383 2014-05-21T10:06:58Z obo:GO_1990383 biological_process obo:GO_1990383 GO:1990383 obo:GO_1990383 cellular response to biotin starvation obo:GO_1990388 The directed movement of iron ions into the phloem from the xylem. obo:GO_1990388 obo:go.owl obo:GO_1990388 tb obo:GO_1990388 2014-05-30T21:06:50Z obo:GO_1990388 biological_process obo:GO_1990388 GO:1990388 obo:GO_1990388 xylem-to-phloem iron transport obo:GO_1990394 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of cell wall damage. The process begins with detection of the damage and ends with a change in state or activity of the cell. obo:GO_1990394 obo:go.owl obo:GO_1990394 al obo:GO_1990394 2014-06-05T16:45:33Z obo:GO_1990394 biological_process obo:GO_1990394 GO:1990394 obo:GO_1990394 cellular response to cell wall damage obo:GO_1990396 The error-free repair of a single-strand break in DNA in which the broken DNA molecule is repaired using homologous sequences. A strand in the broken DNA searches for a homologous region in an intact chromosome to serve as the template for DNA synthesis. The restoration of two intact DNA molecules results in the exchange, reciprocal or nonreciprocal, of genetic material between the intact DNA molecule and the broken DNA molecule. obo:GO_1990396 obo:go.owl obo:GO_1990396 bhm obo:GO_1990396 2014-06-09T10:47:04Z obo:GO_1990396 biological_process obo:GO_1990396 GO:1990396 obo:GO_1990396 single-strand break repair via homologous recombination obo:GO_1990400 Interacting selectively and non-covalently with the mitochondrial large ribosomal subunit RNA (LSU rRNA), a constituent of the mitochondrial large ribosomal subunit. obo:GO_1990400 obo:go.owl obo:GO_1990400 mcc obo:GO_1990400 2014-06-23T16:47:09Z obo:GO_1990400 mitochondrial LSU rRNA binding obo:GO_1990400 21S rRNA binding obo:GO_1990400 molecular_function obo:GO_1990400 GO:1990400 obo:GO_1990400 In S. cerevisiae, this is the mitochondrial 21S rRNA obo:GO_1990400 mitochondrial ribosomal large subunit rRNA binding obo:GO_1990407 Interacting selectively and non-covalently with calcitonin gene-related peptide (CGRP). obo:GO_1990407 obo:go.owl obo:GO_1990407 bhm obo:GO_1990407 2014-07-02T14:22:06Z obo:GO_1990407 CGRP polypeptide binding obo:GO_1990407 calcitonin-gene-related peptide binding obo:GO_1990407 calcitonin-gene-related polypeptide binding obo:GO_1990407 molecular_function obo:GO_1990407 GO:1990407 obo:GO_1990407 An example of this is CALCRL in human (Q16602) in PMID:10882736 (inferred from direct assay/mutant phenotype/etc.). obo:GO_1990407 calcitonin gene-related peptide binding obo:GO_1990409 Interacting selectively and non-covalently with adrenomedullin (AM). obo:GO_1990409 obo:go.owl obo:GO_1990409 bhm obo:GO_1990409 2014-07-02T14:37:19Z obo:GO_1990409 AM binding obo:GO_1990409 molecular_function obo:GO_1990409 GO:1990409 obo:GO_1990409 An example of a protein that could be annotated to this term is CALCRL in human (Q16602) in PMID:10882736. obo:GO_1990409 adrenomedullin binding obo:GO_1990414 The repair of a replication-born double-strand DNA break in which the DNA molecule is repaired using the homologous sequence of the sister chromatid which serves as a template to repair the breaks. obo:GO_1990414 obo:go.owl obo:GO_1990414 rb obo:GO_1990414 2014-07-10T21:20:34Z obo:GO_1990414 replication-born DSB repair by SCE obo:GO_1990414 biological_process obo:GO_1990414 GO:1990414 obo:GO_1990414 replication-born double-strand break repair via sister chromatid exchange obo:GO_1990424 Catalysis of the reaction: ATP + a protein arginine = ADP + protein arginine phosphate. obo:GO_1990424 obo:go.owl obo:GO_1990424 jl obo:GO_1990424 2014-07-23T13:35:56Z obo:GO_1990424 molecular_function obo:GO_1990424 GO:1990424 obo:GO_1990424 This reaction occurs in bacterial species e.g. Bacillus subtilis. obo:GO_1990424 protein arginine kinase activity obo:GO_1990430 Interacting selectively and non-covalently with a protein that is part of an extracellular matrix. obo:GO_1990430 obo:go.owl obo:GO_1990430 jl obo:GO_1990430 2014-07-29T14:57:07Z obo:GO_1990430 molecular_function obo:GO_1990430 GO:1990430 obo:GO_1990430 extracellular matrix protein binding obo:GO_1990439 Catalysis of the reaction: MAP kinase threonine phosphate + H2O = MAP kinase threonine + phosphate and MAP kinase serine phosphate + H2O = MAP kinase serine + phosphate. obo:GO_1990439 obo:go.owl obo:GO_1990439 al obo:GO_1990439 2014-07-31T12:21:04Z obo:GO_1990439 molecular_function obo:GO_1990439 GO:1990439 obo:GO_1990439 MAP kinase serine/threonine phosphatase activity obo:GO_1990443 The phosphorylation by a protein of one or more of its own threonine amino acid residues, or a threonine residue on an identical protein. obo:GO_1990443 obo:go.owl obo:GO_1990443 al obo:GO_1990443 2014-08-02T15:08:41Z obo:GO_1990443 biological_process obo:GO_1990443 GO:1990443 obo:GO_1990443 peptidyl-threonine autophosphorylation obo:GO_1990444 Interacting selectively and non-covalently with an F-box domain of a protein. obo:GO_1990444 obo:go.owl obo:GO_1990444 bf obo:GO_1990444 2014-08-05T13:45:14Z obo:GO_1990444 molecular_function obo:GO_1990444 GO:1990444 obo:GO_1990444 F-box domain binding obo:GO_1990446 Interacting selectively and non-covalently with any part of a U1 small nuclear ribonucleoprotein particle. obo:GO_1990446 obo:go.owl obo:GO_1990446 mah obo:GO_1990446 2014-08-06T09:29:44Z obo:GO_1990446 molecular_function obo:GO_1990446 GO:1990446 obo:GO_1990446 U1 snRNP binding obo:GO_1990447 Interacting selectively and non-covalently with any part of a U2 small nuclear ribonucleoprotein particle. obo:GO_1990447 obo:go.owl obo:GO_1990447 mah obo:GO_1990447 2014-08-06T09:33:38Z obo:GO_1990447 molecular_function obo:GO_1990447 GO:1990447 obo:GO_1990447 U2 snRNP binding obo:GO_1990448 Interacting selectively and non-covalently with an exon-exon junction complex, a protein complex deposited by the spliceosome upstream of messenger RNA exon-exon junctions. The exon-exon junction complex provides a binding platform for factors involved in mRNA export and nonsense-mediated mRNA decay. obo:GO_1990448 obo:go.owl obo:GO_1990448 sart obo:GO_1990448 2014-08-06T10:02:46Z obo:GO_1990448 EJC binding obo:GO_1990448 molecular_function obo:GO_1990448 GO:1990448 obo:GO_1990448 exon-exon junction complex binding obo:GO_1990450 Interacting selectively and non-covalently with a linear polymer of ubiquitin. Linear ubiquitin polymers are formed by linking the amino-terminal methionine (M1) of one ubiquitin molecule to the carboxy-terminal glycine (G76) of the next. obo:GO_1990450 obo:go.owl obo:GO_1990450 bf obo:GO_1990450 2014-08-06T11:10:26Z obo:GO_1990450 M1-linked ubiquitin chain binding obo:GO_1990450 molecular_function obo:GO_1990450 GO:1990450 obo:GO_1990450 linear polyubiquitin binding obo:GO_1990451 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a disturbance in the homeostasis of organismal or cellular pH (with pH < 7). pH is a measure of the acidity or basicity of an aqueous solution. obo:GO_1990451 obo:go.owl obo:GO_1990451 jl obo:GO_1990451 2014-08-06T14:06:58Z obo:GO_1990451 cellular stress response to acidity obo:GO_1990451 biological_process obo:GO_1990451 GO:1990451 obo:GO_1990451 An example of this is NOX1 in human (Q9Y5S8) in PMID:10615049. obo:GO_1990451 cellular stress response to acidic pH obo:GO_1990458 Interacting selectively and non-covalently with lipooligosaccharide. Lipooligosaccharides (LOSs) are the major glycolipids expressed on mucosal Gram-negative bacteria. obo:GO_1990458 obo:go.owl obo:GO_1990458 hjd obo:GO_1990458 2014-08-15T19:58:08Z obo:GO_1990458 molecular_function obo:GO_1990458 LOS binding obo:GO_1990458 endotoxin binding obo:GO_1990458 GO:1990458 obo:GO_1990458 ChEBI distinguishes an oligosaccharide from a polysaccharide as the latter being anything of length 10 or greater. obo:GO_1990458 lipooligosaccharide binding obo:GO_1990459 Interacting selectively and non-covalently with the transferrin receptor. obo:GO_1990459 obo:go.owl obo:GO_1990459 tb obo:GO_1990459 2014-08-18T20:14:24Z obo:GO_1990459 molecular_function obo:GO_1990459 GO:1990459 obo:GO_1990459 transferrin receptor binding obo:GO_1990460 Interacting selectively and non-covalently with the leptin receptor. obo:GO_1990460 obo:go.owl obo:GO_1990460 tb obo:GO_1990460 2014-08-18T20:17:43Z obo:GO_1990460 molecular_function obo:GO_1990460 GO:1990460 obo:GO_1990460 leptin receptor binding obo:GO_1990470 Interacting selectively and non-covalently with piRNA clusters, double-stranded DNA regions that give rise to PIWI-interacting RNAs (piRNAs). obo:GO_1990470 obo:go.owl obo:GO_1990470 bhm obo:GO_1990470 2014-08-29T14:23:38Z obo:GO_1990470 molecular_function obo:GO_1990470 GO:1990470 obo:GO_1990470 An example of this is rhi in Drosophila melanogaster (Q7JXA8) in PMID:24906153 (inferred from direct assay). obo:GO_1990470 piRNA cluster binding obo:GO_1990471 Interacting selectively and non-covalently with uni-strand piRNA clusters, double-stranded DNA regions that give rise to PIWI-interacting RNAs (piRNAs) that map predominantly to only one strand and exhibit hallmarks of canonical Pol II transcription. Uni-strand piRNA clusters are found in many taxa. obo:GO_1990471 obo:go.owl obo:GO_1990471 bhm obo:GO_1990471 2014-08-29T14:37:35Z obo:GO_1990471 molecular_function obo:GO_1990471 GO:1990471 obo:GO_1990471 piRNA uni-strand cluster binding obo:GO_1990472 Interacting selectively and non-covalently with dual-strand piRNA clusters, double-stranded DNA regions that give rise to PIWI-interacting RNAs (piRNAs) where piRNAs originate from both DNA strands via noncanonical transcription. obo:GO_1990472 obo:go.owl obo:GO_1990472 bhm obo:GO_1990472 2014-08-29T14:50:54Z obo:GO_1990472 molecular_function obo:GO_1990472 GO:1990472 obo:GO_1990472 An example of this is rhi in Drosophila melanogaster (Q7JXA8) in PMID:24906153 (inferred from direct assay). obo:GO_1990472 piRNA dual-strand cluster binding obo:GO_1990473 Interacting selectively and non-covalently with a ciliary targeting sequence, a specific peptide sequence that acts as a signal to localize a membrane protein to the ciliary membrane. obo:GO_1990473 obo:go.owl obo:GO_1990473 pr obo:GO_1990473 2014-09-02T08:22:03Z obo:GO_1990473 CTS binding obo:GO_1990473 molecular_function obo:GO_1990473 GO:1990473 obo:GO_1990473 ciliary targeting signal binding obo:GO_1990516 The pathway by which a ribonucleotide is removed from DNA and replaced by a deoxyribonucleotide. The ribonucleotide is incised by RNase H2, and further excised by an endonuclease. The resulting 1 nt gap is then repaired by DNA polymerase and DNA ligase. obo:GO_1990516 obo:go.owl obo:GO_1990516 al obo:GO_1990516 2014-10-14T12:24:37Z obo:GO_1990516 biological_process obo:GO_1990516 GO:1990516 obo:GO_1990516 ribonucleotide excision repair obo:GO_1990525 Interacting selectively and non-covalently with a Baculovirus Inhibitor of apoptosis protein Repeat (BIR) domain. obo:GO_1990525 obo:go.owl obo:GO_1990525 jl obo:GO_1990525 2014-11-04T12:36:56Z obo:GO_1990525 Baculovirus Inhibitor of apoptosis protein Repeat domain binding obo:GO_1990525 molecular_function obo:GO_1990525 GO:1990525 obo:GO_1990525 An example of this is the Drosophila reaper gene in PMID:21886178. obo:GO_1990525 BIR domain binding obo:GO_1990540 The process in which a manganese ion is transported across a mitochondrial membrane, into or out of the mitochondrion. obo:GO_1990540 obo:go.owl obo:GO_1990540 vw obo:GO_1990540 2014-11-19T11:03:09Z obo:GO_1990540 biological_process obo:GO_1990540 GO:1990540 obo:GO_1990540 mitochondrial manganese ion transmembrane transport obo:GO_1990573 The directed movement of potassium ions from outside of a cell, across the plasma membrane and into the cytosol. obo:GO_1990573 obo:go.owl obo:GO_1990573 vw obo:GO_1990573 2014-12-04T09:48:12Z obo:GO_1990573 GO:0010107 obo:GO_1990573 potassium import obo:GO_1990573 potassium ion import obo:GO_1990573 potassium ion uptake obo:GO_1990573 biological_process obo:GO_1990573 GO:1990573 obo:GO_1990573 potassium ion import across plasma membrane obo:GO_1990579 The phosphorylation of a peptidyl-serine to form peptidyl-O-phospho-L-serine on an identical protein. For example, phosphorylation by the other kinase within a homodimer. obo:GO_1990579 obo:go.owl obo:GO_1990579 bf obo:GO_1990579 2014-12-09T09:20:08Z obo:GO_1990579 serine autophosphorylation in trans obo:GO_1990579 serine transautophosphorylation obo:GO_1990579 biological_process obo:GO_1990579 GO:1990579 obo:GO_1990579 peptidyl-serine trans-autophosphorylation obo:GO_1990593 Interacting selectively and non-covalently with the nascent polypeptide-associated complex, which is a heterodimeric protein complex that can reversibly bind to ribosomes and is located in direct proximity to newly synthesized polypeptide chains as they emerge from the ribosome. obo:GO_1990593 obo:go.owl obo:GO_1990593 mcc obo:GO_1990593 2014-12-15T22:20:45Z obo:GO_1990593 NAC binding obo:GO_1990593 NACA binding obo:GO_1990593 molecular_function obo:GO_1990593 GO:1990593 obo:GO_1990593 nascent polypeptide-associated complex binding obo:GO_1990603 The process by which the rods of the retina gradually become fully responsive to dim light when no longer exposed to bright light. obo:GO_1990603 obo:go.owl obo:GO_1990603 hjd obo:GO_1990603 2015-01-09T20:35:46Z obo:GO_1990603 biological_process obo:GO_1990603 GO:1990603 obo:GO_1990603 The proteins RGS9-1 and Gb5L localize to the rod inner segment during dark adaptation, but to the rod outer segment during light adaptation. PMID:23555598 obo:GO_1990603 dark adaptation obo:GO_1990605 Interacting selectively and non-covalently with an RNA molecule containing GU repeats. obo:GO_1990605 obo:go.owl obo:GO_1990605 al obo:GO_1990605 2015-01-13T18:18:01Z obo:GO_1990605 molecular_function obo:GO_1990605 GO:1990605 obo:GO_1990605 GU repeat RNA binding obo:GO_1990616 The directed movement of magnesium ions out of mitochondrial matrix into the cytosol by means of some agent such as a transporter or pore. obo:GO_1990616 obo:go.owl obo:GO_1990616 mcc obo:GO_1990616 2015-01-21T22:06:42Z obo:GO_1990616 magnesium ion efflux from mitochondrion obo:GO_1990616 biological_process obo:GO_1990616 GO:1990616 obo:GO_1990616 magnesium ion export from mitochondrion obo:GO_1990631 Interacting selectively and non-covalently with the protein-tyrosine kinase receptor ErbB-4/HER4. obo:GO_1990631 obo:go.owl obo:GO_1990631 sl obo:GO_1990631 2015-02-06T23:28:49Z obo:GO_1990631 HER4 receptor binding obo:GO_1990631 molecular_function obo:GO_1990631 GO:1990631 obo:GO_1990631 ErbB-4 class receptor binding obo:GO_1990634 Interacting selectively and non-covalently with the enzyme protein phosphatase 5. obo:GO_1990634 obo:go.owl obo:GO_1990634 sl obo:GO_1990634 2015-02-10T21:30:41Z obo:GO_1990634 protein phosphatase T binding obo:GO_1990634 molecular_function obo:GO_1990634 GO:1990634 obo:GO_1990634 protein phosphatase 5 binding obo:GO_1990641 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a starvation stimulus, deprivation of iron ion. obo:GO_1990641 obo:go.owl obo:GO_1990641 sl obo:GO_1990641 2015-02-11T18:43:28Z obo:GO_1990641 biological_process obo:GO_1990641 GO:1990641 obo:GO_1990641 response to iron ion starvation obo:GO_1990655 Interacting selectively and non-covalently with a 4 iron, 3 sulfur (4Fe-3S) cluster, an uncommon iron-sulfur cluster with unique properties found in oxygen-tolerant Ni-Fe hydrogenases of various bacteria. obo:GO_1990655 obo:go.owl obo:GO_1990655 pr obo:GO_1990655 2015-02-24T17:07:23Z obo:GO_1990655 molecular_function obo:GO_1990655 4Fe-3S cluster binding obo:GO_1990655 GO:1990655 obo:GO_1990655 4 iron, 3 sulfur cluster binding obo:GO_1990715 Interacting selectively and non-covalently with the coding sequence (CDS) of an mRNA molecule. obo:GO_1990715 obo:go.owl obo:GO_1990715 kmv obo:GO_1990715 2015-03-27T20:59:49Z obo:GO_1990715 mRNA coding region binding obo:GO_1990715 mRNA coding sequence binding obo:GO_1990715 molecular_function obo:GO_1990715 GO:1990715 obo:GO_1990715 mRNA CDS binding obo:GO_1990763 Interacting selectively and non-covalently with any member of the arrestin family, proteins involved in agonist-mediated desensitization of G protein-coupled receptors. obo:GO_1990763 obo:go.owl obo:GO_1990763 sl obo:GO_1990763 2015-06-09T23:29:42Z obo:GO_1990763 molecular_function obo:GO_1990763 GO:1990763 obo:GO_1990763 arrestin family protein binding obo:GO_1990782 Interacting selectively and non-covalently with protein tyrosine kinase. obo:GO_1990782 obo:go.owl obo:GO_1990782 sl obo:GO_1990782 2015-06-23T20:50:58Z obo:GO_1990782 tyrosine kinase binding obo:GO_1990782 molecular_function obo:GO_1990782 GO:1990782 obo:GO_1990782 protein tyrosine kinase binding obo:GO_1990808 Interacting selectively and non-covalently with an F-BAR domain of a protein, a domain of about 60 residues that occurs in a wide range of cytoskeletal proteins. obo:GO_1990808 obo:go.owl obo:GO_1990808 vw obo:GO_1990808 2015-07-21T18:43:00Z obo:GO_1990808 molecular_function obo:GO_1990808 GO:1990808 obo:GO_1990808 F-bar domain binding obo:GO_1990814 A nucleic acid binding activity that brings together complementary sequences of ssDNA so that they pair by hydrogen bonds to form a double-stranded DNA. obo:GO_1990814 obo:go.owl obo:GO_1990814 vw obo:GO_1990814 2015-07-29T12:35:03Z obo:GO_1990814 DNA reannealing activity obo:GO_1990814 molecular_function obo:GO_1990814 GO:1990814 obo:GO_1990814 DNA/DNA annealing activity obo:GO_1990825 Interacting selectively and non-covalently with messenger RNA (mRNA) of a specific nucleotide composition or a specific sequence motif. obo:GO_1990825 obo:go.owl obo:GO_1990825 sl obo:GO_1990825 2015-08-19T17:42:50Z obo:GO_1990825 molecular_function obo:GO_1990825 GO:1990825 obo:GO_1990825 sequence-specific mRNA binding obo:GO_1990827 Interacting selectively and non-covalently with an enzyme that catalyzes the removal of an amino group from a substrate, producing ammonia (NH3). obo:GO_1990827 obo:go.owl obo:GO_1990827 sl obo:GO_1990827 2015-08-19T23:48:32Z obo:GO_1990827 molecular_function obo:GO_1990827 GO:1990827 obo:GO_1990827 deaminase binding obo:GO_1990829 Interacting selectively and non-covalently with C-rich, single-stranded DNA. obo:GO_1990829 obo:go.owl obo:GO_1990829 sl obo:GO_1990829 2015-08-20T16:05:12Z obo:GO_1990829 C-rich ssDNA binding obo:GO_1990829 molecular_function obo:GO_1990829 GO:1990829 obo:GO_1990829 C-rich single-stranded DNA binding obo:GO_1990837 Interacting selectively and non-covalently with double-stranded DNA of a specific nucleotide composition, e.g. GC-rich DNA binding, or with a specific sequence motif or type of DNA, e.g. promotor binding or rDNA binding. obo:GO_1990837 obo:go.owl obo:GO_1990837 sl obo:GO_1990837 2015-08-25T17:30:06Z obo:GO_1990837 sequence-specific dsDNA binding obo:GO_1990837 molecular_function obo:GO_1990837 GO:1990837 obo:GO_1990837 sequence-specific double-stranded DNA binding obo:GO_1990856 Interacting selectively and non-covalently with methionine-initator methionine tRNA. obo:GO_1990856 obo:go.owl obo:GO_1990856 hjd obo:GO_1990856 2015-09-18T16:56:59Z obo:GO_1990856 molecular_function obo:GO_1990856 GO:1990856 obo:GO_1990856 An example of this is eukaryotic initiation factor 2 complex, which binds the methionyl-initiator methionine tRNA during ternary complex formation. The non-acylated tRNA is not bound. obo:GO_1990856 methionyl-initiator methionine tRNA binding obo:GO_1990889 Interacting selectively and non-covalently with a histone H4 in which the lysine residue at position 20 has been modified by trimethylation. obo:GO_1990889 obo:go.owl obo:GO_1990889 al obo:GO_1990889 2015-10-30T15:43:09Z obo:GO_1990889 molecular_function obo:GO_1990889 GO:1990889 obo:GO_1990889 H4K20me3 modified histone binding obo:GO_1990890 Interacting selectively and non-covalently with a netrin receptor. obo:GO_1990890 obo:go.owl obo:GO_1990890 kmv obo:GO_1990890 2015-11-02T22:56:07Z obo:GO_1990890 molecular_function obo:GO_1990890 GO:1990890 obo:GO_1990890 netrin receptor binding obo:GO_1990895 Any process that modulates the frequency, rate or extent of protein localization to cell cortex of cell tip. obo:GO_1990895 obo:go.owl obo:GO_1990895 vw obo:GO_1990895 2015-11-04T21:53:15Z obo:GO_1990895 biological_process obo:GO_1990895 GO:1990895 obo:GO_1990895 regulation of protein localization to cell cortex of cell tip obo:GO_1990910 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating lowered oxygen tension combined with low atmospheric pressure. Hypoxia is defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95% and hypobaric is defined as atmospheric pressure below 0.74 atm (greater than 2,500 m above sea level). obo:GO_1990910 obo:go.owl obo:GO_1990910 sl obo:GO_1990910 2015-12-07T19:34:14Z obo:GO_1990910 biological_process obo:GO_1990910 GO:1990910 obo:GO_1990910 response to hypobaric hypoxia obo:GO_1990928 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of amino acids. obo:GO_1990928 obo:go.owl obo:GO_1990928 sl obo:GO_1990928 2016-02-18T00:18:23Z obo:GO_1990928 biological_process obo:GO_1990928 GO:1990928 obo:GO_1990928 response to amino acid starvation obo:GO_1990932 Interacting selectively and non-covalently with 5.8S ribosomal RNA, a eukaryotic ribosomal RNA which forms a complex with 28S RNA. obo:GO_1990932 obo:go.owl obo:GO_1990932 sl obo:GO_1990932 2016-03-14T20:25:41Z obo:GO_1990932 molecular_function obo:GO_1990932 GO:1990932 obo:GO_1990932 5.8S rRNA binding obo:GO_1990935 Interacting selectively and non-covalently with any protein involved in the process of removing sections of the primary RNA transcript to form the mature form of the RNA. obo:GO_1990935 obo:go.owl obo:GO_1990935 sl obo:GO_1990935 2016-03-21T21:57:20Z obo:GO_1990935 molecular_function obo:GO_1990935 GO:1990935 obo:GO_1990935 splicing factor binding obo:GO_1990938 The phosphorylation by a protein of one or more of its own aspartate amino acid residues, or an aspartate residue on an identical protein. obo:GO_1990938 obo:go.owl obo:GO_1990938 bf obo:GO_1990938 2016-04-04T10:49:53Z obo:GO_1990938 aspartyl autophosphorylation obo:GO_1990938 peptidyl-aspartate autophosphorylation obo:GO_1990938 biological_process obo:GO_1990938 GO:1990938 obo:GO_1990938 peptidyl-aspartic acid autophosphorylation obo:GO_1990943 Interacting selectively and non-covalently with the replication fork barrier found in the mating type region of fission yeast. obo:GO_1990943 obo:go.owl obo:GO_1990943 mah obo:GO_1990943 2016-04-06T16:08:43Z obo:GO_1990943 RTS1 barrier binding obo:GO_1990943 RTS1 element binding obo:GO_1990943 molecular_function obo:GO_1990943 GO:1990943 obo:GO_1990943 mating type region replication fork barrier binding obo:GO_1990955 Interacting selectively and non-covalently with G-rich, single-stranded DNA. obo:GO_1990955 obo:go.owl obo:GO_1990955 hjd obo:GO_1990955 2016-05-13T17:44:28Z obo:GO_1990955 molecular_function obo:GO_1990955 GO:1990955 obo:GO_1990955 G-rich single-stranded DNA binding obo:GO_1990970 Interacting selectively and non-covalently with a trans-activation response (TAR) element, a hairpin RNA structure located at the 5' end of all HIV-1 transcripts, and which is required for trans-activation of a viral promoter. obo:GO_1990970 obo:go.owl obo:GO_1990970 bf obo:GO_1990970 2016-06-21T12:23:00Z obo:GO_1990970 TAR binding obo:GO_1990970 molecular_function obo:GO_1990970 GO:1990970 obo:GO_1990970 trans-activation response element binding obo:GO_2000008 Any process that modulates the frequency, rate or extent of protein localization to the cell surface. obo:GO_2000008 obo:go.owl obo:GO_2000008 jane obo:GO_2000008 2010-08-04T01:43:48Z obo:GO_2000008 regulation of protein localisation at cell surface obo:GO_2000008 regulation of protein localization at cell surface obo:GO_2000008 biological_process obo:GO_2000008 GO:2000008 obo:GO_2000008 regulation of protein localization to cell surface obo:GO_2000009 Any process that stops, prevents, or reduces the frequency, rate or extent of protein localization to the cell surface. obo:GO_2000009 obo:go.owl obo:GO_2000009 jane obo:GO_2000009 2010-08-04T01:43:52Z obo:GO_2000009 negative regulation of protein localisation at cell surface obo:GO_2000009 negative regulation of protein localization at cell surface obo:GO_2000009 biological_process obo:GO_2000009 GO:2000009 obo:GO_2000009 negative regulation of protein localization to cell surface obo:GO_2000010 Any process that activates or increases the frequency, rate or extent of protein localization to the cell surface. obo:GO_2000010 obo:go.owl obo:GO_2000010 jane obo:GO_2000010 2010-08-04T01:43:56Z obo:GO_2000010 positive regulation of protein localisation at cell surface obo:GO_2000010 positive regulation of protein localization at cell surface obo:GO_2000010 biological_process obo:GO_2000010 GO:2000010 obo:GO_2000010 positive regulation of protein localization to cell surface obo:GO_2000047 Any process that modulates the frequency, rate or extent of cell-cell adhesion mediated by cadherin. obo:GO_2000047 obo:go.owl obo:GO_2000047 jane obo:GO_2000047 2010-08-20T12:56:44Z obo:GO_2000047 biological_process obo:GO_2000047 GO:2000047 obo:GO_2000047 regulation of cell-cell adhesion mediated by cadherin obo:GO_2000048 Any process that stops, prevents, or reduces the frequency, rate or extent of cell-cell adhesion mediated by cadherin. obo:GO_2000048 obo:go.owl obo:GO_2000048 jane obo:GO_2000048 2010-08-20T12:56:51Z obo:GO_2000048 biological_process obo:GO_2000048 GO:2000048 obo:GO_2000048 negative regulation of cell-cell adhesion mediated by cadherin obo:GO_2000049 Any process that activates or increases the frequency, rate or extent of cell-cell adhesion mediated by cadherin. obo:GO_2000049 obo:go.owl obo:GO_2000049 jane obo:GO_2000049 2010-08-20T12:56:57Z obo:GO_2000049 biological_process obo:GO_2000049 GO:2000049 obo:GO_2000049 positive regulation of cell-cell adhesion mediated by cadherin obo:GO_2000118 Any process that modulates the frequency, rate or extent of sodium-dependent phosphate transport. obo:GO_2000118 obo:go.owl obo:GO_2000118 jane obo:GO_2000118 2010-09-23T01:34:59Z obo:GO_2000118 biological_process obo:GO_2000118 GO:2000118 obo:GO_2000118 regulation of sodium-dependent phosphate transport obo:GO_2000119 Any process that stops, prevents, or reduces the frequency, rate or extent of sodium-dependent phosphate transport. obo:GO_2000119 obo:go.owl obo:GO_2000119 jane obo:GO_2000119 2010-09-23T01:35:03Z obo:GO_2000119 biological_process obo:GO_2000119 GO:2000119 obo:GO_2000119 negative regulation of sodium-dependent phosphate transport obo:GO_2000120 Any process that activates or increases the frequency, rate or extent of sodium-dependent phosphate transport. obo:GO_2000120 obo:go.owl obo:GO_2000120 jane obo:GO_2000120 2010-09-23T01:35:06Z obo:GO_2000120 biological_process obo:GO_2000120 GO:2000120 obo:GO_2000120 positive regulation of sodium-dependent phosphate transport obo:GO_2000177 Any process that modulates the frequency, rate or extent of neural precursor cell proliferation. obo:GO_2000177 obo:go.owl obo:GO_2000177 dph obo:GO_2000177 2010-10-13T12:40:41Z obo:GO_2000177 biological_process obo:GO_2000177 GO:2000177 obo:GO_2000177 regulation of neural precursor cell proliferation obo:GO_2000178 Any process that stops, prevents, or reduces the frequency, rate or extent of neural precursor cell proliferation. obo:GO_2000178 obo:go.owl obo:GO_2000178 dph obo:GO_2000178 2010-10-13T12:40:43Z obo:GO_2000178 biological_process obo:GO_2000178 GO:2000178 obo:GO_2000178 negative regulation of neural precursor cell proliferation obo:GO_2000179 Any process that activates or increases the frequency, rate or extent of neural precursor cell proliferation. obo:GO_2000179 obo:go.owl obo:GO_2000179 dph obo:GO_2000179 2010-10-13T12:40:45Z obo:GO_2000179 biological_process obo:GO_2000179 GO:2000179 obo:GO_2000179 positive regulation of neural precursor cell proliferation obo:GO_2000185 Any process that modulates the frequency, rate or extent of phosphate transmembrane transport. obo:GO_2000185 obo:go.owl obo:GO_2000185 vw obo:GO_2000185 2010-10-15T11:33:04Z obo:GO_2000185 regulation of phosphate membrane transport obo:GO_2000185 biological_process obo:GO_2000185 GO:2000185 obo:GO_2000185 regulation of phosphate transmembrane transport obo:GO_2000186 Any process that stops, prevents, or reduces the frequency, rate or extent of phosphate transmembrane transport. obo:GO_2000186 obo:go.owl obo:GO_2000186 vw obo:GO_2000186 2010-10-15T11:33:08Z obo:GO_2000186 negative regulation of phosphate membrane transport obo:GO_2000186 biological_process obo:GO_2000186 GO:2000186 obo:GO_2000186 negative regulation of phosphate transmembrane transport obo:GO_2000187 Any process that activates or increases the frequency, rate or extent of phosphate transmembrane transport. obo:GO_2000187 obo:go.owl obo:GO_2000187 vw obo:GO_2000187 2010-10-15T11:33:10Z obo:GO_2000187 positive regulation of phosphate membrane transport obo:GO_2000187 biological_process obo:GO_2000187 GO:2000187 obo:GO_2000187 positive regulation of phosphate transmembrane transport obo:GO_2000197 Any process that modulates the frequency, rate or extent of ribonucleoprotein complex localization. obo:GO_2000197 obo:go.owl obo:GO_2000197 midori obo:GO_2000197 2010-10-26T10:35:48Z obo:GO_2000197 regulation of RNP localization obo:GO_2000197 regulation of cellular ribonucleoprotein complex localization obo:GO_2000197 regulation of establishment and maintenance of ribonucleoprotein complex localization obo:GO_2000197 regulation of ribonucleoprotein complex localisation obo:GO_2000197 biological_process obo:GO_2000197 GO:2000197 obo:GO_2000197 regulation of ribonucleoprotein complex localization obo:GO_2000198 Any process that stops, prevents, or reduces the frequency, rate or extent of ribonucleoprotein complex localization. obo:GO_2000198 obo:go.owl obo:GO_2000198 midori obo:GO_2000198 2010-10-26T10:35:52Z obo:GO_2000198 negative regulation of RNP localization obo:GO_2000198 negative regulation of cellular ribonucleoprotein complex localization obo:GO_2000198 negative regulation of establishment and maintenance of ribonucleoprotein complex localization obo:GO_2000198 negative regulation of ribonucleoprotein complex localisation obo:GO_2000198 biological_process obo:GO_2000198 GO:2000198 obo:GO_2000198 negative regulation of ribonucleoprotein complex localization obo:GO_2000199 Any process that activates or increases the frequency, rate or extent of ribonucleoprotein complex localization. obo:GO_2000199 obo:go.owl obo:GO_2000199 midori obo:GO_2000199 2010-10-26T10:35:55Z obo:GO_2000199 positive regulation of RNP localization obo:GO_2000199 positive regulation of cellular ribonucleoprotein complex localization obo:GO_2000199 positive regulation of establishment and maintenance of ribonucleoprotein complex localization obo:GO_2000199 positive regulation of ribonucleoprotein complex localisation obo:GO_2000199 biological_process obo:GO_2000199 GO:2000199 obo:GO_2000199 positive regulation of ribonucleoprotein complex localization obo:GO_2000229 Any process that modulates the frequency, rate or extent of pancreatic stellate cell proliferation. obo:GO_2000229 obo:go.owl obo:GO_2000229 midori obo:GO_2000229 2010-11-09T03:45:18Z obo:GO_2000229 biological_process obo:GO_2000229 GO:2000229 obo:GO_2000229 regulation of pancreatic stellate cell proliferation obo:GO_2000230 Any process that stops, prevents, or reduces the frequency, rate or extent of pancreatic stellate cell proliferation. obo:GO_2000230 obo:go.owl obo:GO_2000230 midori obo:GO_2000230 2010-11-09T03:45:21Z obo:GO_2000230 biological_process obo:GO_2000230 GO:2000230 obo:GO_2000230 negative regulation of pancreatic stellate cell proliferation obo:GO_2000231 Any process that activates or increases the frequency, rate or extent of pancreatic stellate cell proliferation. obo:GO_2000231 obo:go.owl obo:GO_2000231 midori obo:GO_2000231 2010-11-09T03:45:23Z obo:GO_2000231 biological_process obo:GO_2000231 GO:2000231 obo:GO_2000231 positive regulation of pancreatic stellate cell proliferation obo:GO_2000275 Any process that modulates the frequency, rate or extent of oxidative phosphorylation uncoupler activity. obo:GO_2000275 obo:go.owl obo:GO_2000275 midori obo:GO_2000275 2010-12-07T12:14:54Z obo:GO_2000275 biological_process obo:GO_2000275 regulation of mitochondrial uncoupling protein activity obo:GO_2000275 regulation of uncoupling protein activity obo:GO_2000275 GO:2000275 obo:GO_2000275 regulation of oxidative phosphorylation uncoupler activity obo:GO_2000276 Any process that stops, prevents or reduces the frequency, rate or extent of oxidative phosphorylation uncoupler activity. obo:GO_2000276 obo:go.owl obo:GO_2000276 midori obo:GO_2000276 2010-12-07T12:14:59Z obo:GO_2000276 biological_process obo:GO_2000276 negative regulation of mitochondrial uncoupling protein activity obo:GO_2000276 negative regulation of uncoupling protein activity obo:GO_2000276 GO:2000276 obo:GO_2000276 negative regulation of oxidative phosphorylation uncoupler activity obo:GO_2000277 Any process that activates or increases the frequency, rate or extent of oxidative phosphorylation uncoupler activity. obo:GO_2000277 obo:go.owl obo:GO_2000277 midori obo:GO_2000277 2010-12-07T12:15:02Z obo:GO_2000277 biological_process obo:GO_2000277 positive regulation of mitochondrial uncoupling protein activity obo:GO_2000277 positive regulation of uncoupling protein activity obo:GO_2000277 GO:2000277 obo:GO_2000277 positive regulation of oxidative phosphorylation uncoupler activity obo:GO_2000288 Any process that activates or increases the frequency, rate or extent of myoblast proliferation. obo:GO_2000288 obo:go.owl obo:GO_2000288 rl obo:GO_2000288 2010-12-16T05:20:52Z obo:GO_2000288 biological_process obo:GO_2000288 GO:2000288 obo:GO_2000288 positive regulation of myoblast proliferation obo:GO_2000291 Any process that modulates the frequency, rate or extent of myoblast proliferation. obo:GO_2000291 obo:go.owl obo:GO_2000291 midori obo:GO_2000291 2010-12-20T10:34:26Z obo:GO_2000291 biological_process obo:GO_2000291 GO:2000291 obo:GO_2000291 regulation of myoblast proliferation obo:GO_2000398 Any process that modulates the frequency, rate or extent of thymocyte aggregation. obo:GO_2000398 obo:go.owl obo:GO_2000398 midori obo:GO_2000398 2011-02-22T02:49:19Z obo:GO_2000398 regulation of T cell precursor aggregation obo:GO_2000398 regulation of immature T-lymphocyte aggregation obo:GO_2000398 regulation of thymic lymphocyte aggregation obo:GO_2000398 biological_process obo:GO_2000398 regulation of immature T cell aggregation obo:GO_2000398 regulation of immature T-cell aggregation obo:GO_2000398 GO:2000398 obo:GO_2000398 regulation of thymocyte aggregation obo:GO_2000399 Any process that stops, prevents or reduces the frequency, rate or extent of thymocyte aggregation. obo:GO_2000399 obo:go.owl obo:GO_2000399 midori obo:GO_2000399 2011-02-22T02:49:44Z obo:GO_2000399 negative regulation of T cell precursor aggregation obo:GO_2000399 negative regulation of immature T-lymphocyte aggregation obo:GO_2000399 negative regulation of thymic lymphocyte aggregation obo:GO_2000399 biological_process obo:GO_2000399 negative regulation of immature T cell aggregation obo:GO_2000399 negative regulation of immature T-cell aggregation obo:GO_2000399 GO:2000399 obo:GO_2000399 negative regulation of thymocyte aggregation obo:GO_2000400 Any process that activates or increases the frequency, rate or extent of thymocyte aggregation. obo:GO_2000400 obo:go.owl obo:GO_2000400 midori obo:GO_2000400 2011-02-22T02:50:01Z obo:GO_2000400 positive regulation of T cell precursor aggregation obo:GO_2000400 positive regulation of immature T-lymphocyte aggregation obo:GO_2000400 positive regulation of thymic lymphocyte aggregation obo:GO_2000400 biological_process obo:GO_2000400 positive regulation of immature T cell aggregation obo:GO_2000400 positive regulation of immature T-cell aggregation obo:GO_2000400 GO:2000400 obo:GO_2000400 positive regulation of thymocyte aggregation obo:GO_2000428 Any process that modulates the frequency, rate or extent of neutrophil aggregation. obo:GO_2000428 obo:go.owl obo:GO_2000428 ebc obo:GO_2000428 2011-02-28T05:18:54Z obo:GO_2000428 regulation of neutrocyte aggregation obo:GO_2000428 regulation of neutrophil leucocyte aggregation obo:GO_2000428 regulation of neutrophilic leukocyte aggregation obo:GO_2000428 biological_process obo:GO_2000428 GO:2000428 obo:GO_2000428 regulation of neutrophil aggregation obo:GO_2000429 Any process that stops, prevents or reduces the frequency, rate or extent of neutrophil aggregation. obo:GO_2000429 obo:go.owl obo:GO_2000429 ebc obo:GO_2000429 2011-02-28T05:19:28Z obo:GO_2000429 negative regulation of neutrocyte aggregation obo:GO_2000429 negative regulation of neutrophil leucocyte aggregation obo:GO_2000429 negative regulation of neutrophilic leukocyte aggregation obo:GO_2000429 biological_process obo:GO_2000429 GO:2000429 obo:GO_2000429 negative regulation of neutrophil aggregation obo:GO_2000430 Any process that activates or increases the frequency, rate or extent of neutrophil aggregation. obo:GO_2000430 obo:go.owl obo:GO_2000430 ebc obo:GO_2000430 2011-02-28T05:19:51Z obo:GO_2000430 positive regulation of neutrocyte aggregation obo:GO_2000430 positive regulation of neutrophil leucocyte aggregation obo:GO_2000430 positive regulation of neutrophilic leukocyte aggregation obo:GO_2000430 biological_process obo:GO_2000430 GO:2000430 obo:GO_2000430 positive regulation of neutrophil aggregation obo:GO_2000603 Any process that modulates the frequency, rate or extent of secondary growth. obo:GO_2000603 obo:go.owl obo:GO_2000603 tanyaberardini obo:GO_2000603 2011-04-15T10:30:44Z obo:GO_2000603 biological_process obo:GO_2000603 GO:2000603 obo:GO_2000603 regulation of secondary growth obo:GO_2000604 Any process that stops, prevents or reduces the frequency, rate or extent of secondary growth. obo:GO_2000604 obo:go.owl obo:GO_2000604 tanyaberardini obo:GO_2000604 2011-04-15T10:30:47Z obo:GO_2000604 biological_process obo:GO_2000604 GO:2000604 obo:GO_2000604 negative regulation of secondary growth obo:GO_2000605 Any process that activates or increases the frequency, rate or extent of secondary growth. obo:GO_2000605 obo:go.owl obo:GO_2000605 tanyaberardini obo:GO_2000605 2011-04-15T10:30:49Z obo:GO_2000605 biological_process obo:GO_2000605 GO:2000605 obo:GO_2000605 positive regulation of secondary growth obo:GO_2000647 Any process that stops, prevents or reduces the frequency, rate or extent of stem cell proliferation. obo:GO_2000647 obo:go.owl obo:GO_2000647 dph obo:GO_2000647 2011-04-27T01:04:22Z obo:GO_2000647 biological_process obo:GO_2000647 GO:2000647 obo:GO_2000647 negative regulation of stem cell proliferation obo:GO_2000648 Any process that activates or increases the frequency, rate or extent of stem cell proliferation. obo:GO_2000648 obo:go.owl obo:GO_2000648 dph obo:GO_2000648 2011-04-27T01:04:25Z obo:GO_2000648 biological_process obo:GO_2000648 GO:2000648 obo:GO_2000648 positive regulation of stem cell proliferation obo:GO_2000649 Any process that modulates the frequency, rate or extent of sodium ion transmembrane transporter activity. obo:GO_2000649 obo:go.owl obo:GO_2000649 yaf obo:GO_2000649 2011-04-28T08:42:53Z obo:GO_2000649 regulation of sodium transporter activity obo:GO_2000649 biological_process obo:GO_2000649 GO:2000649 obo:GO_2000649 regulation of sodium ion transmembrane transporter activity obo:GO_2000650 Any process that stops, prevents or reduces the frequency, rate or extent of sodium ion transmembrane transporter activity. obo:GO_2000650 obo:go.owl obo:GO_2000650 yaf obo:GO_2000650 2011-04-28T08:42:57Z obo:GO_2000650 negative regulation of sodium transporter activity obo:GO_2000650 biological_process obo:GO_2000650 GO:2000650 obo:GO_2000650 negative regulation of sodium ion transmembrane transporter activity obo:GO_2000651 Any process that activates or increases the frequency, rate or extent of sodium ion transmembrane transporter activity. obo:GO_2000651 obo:go.owl obo:GO_2000651 yaf obo:GO_2000651 2011-04-28T08:43:00Z obo:GO_2000651 positive regulation of sodium transporter activity obo:GO_2000651 biological_process obo:GO_2000651 GO:2000651 obo:GO_2000651 positive regulation of sodium ion transmembrane transporter activity obo:GO_2000818 Any process that stops, prevents or reduces the frequency, rate or extent of myoblast proliferation. obo:GO_2000818 obo:go.owl obo:GO_2000818 pr obo:GO_2000818 2011-07-12T03:06:04Z obo:GO_2000818 biological_process obo:GO_2000818 GO:2000818 obo:GO_2000818 negative regulation of myoblast proliferation obo:GO_2000970 Any process that modulates the frequency, rate or extent of detection of glucose. obo:GO_2000970 obo:go.owl obo:GO_2000970 vk obo:GO_2000970 2011-08-02T10:18:52Z obo:GO_2000970 regulation of glucose detection obo:GO_2000970 biological_process obo:GO_2000970 regulation of glucose perception obo:GO_2000970 regulation of glucose sensing obo:GO_2000970 GO:2000970 obo:GO_2000970 regulation of detection of glucose obo:GO_2000971 Any process that stops, prevents or reduces the frequency, rate or extent of detection of glucose. obo:GO_2000971 obo:go.owl obo:GO_2000971 vk obo:GO_2000971 2011-08-02T10:18:54Z obo:GO_2000971 negative regulation of glucose detection obo:GO_2000971 biological_process obo:GO_2000971 negative regulation of glucose perception obo:GO_2000971 negative regulation of glucose sensing obo:GO_2000971 GO:2000971 obo:GO_2000971 negative regulation of detection of glucose obo:GO_2000972 Any process that activates or increases the frequency, rate or extent of detection of glucose. obo:GO_2000972 obo:go.owl obo:GO_2000972 vk obo:GO_2000972 2011-08-02T10:18:56Z obo:GO_2000972 positive regulation of glucose detection obo:GO_2000972 biological_process obo:GO_2000972 positive regulation of glucose perception obo:GO_2000972 positive regulation of glucose sensing obo:GO_2000972 GO:2000972 obo:GO_2000972 positive regulation of detection of glucose obo:GO_2001023 Any process that modulates the frequency, rate or extent of response to drug. obo:GO_2001023 obo:go.owl obo:GO_2001023 yaf obo:GO_2001023 2011-08-19T01:47:20Z obo:GO_2001023 biological_process obo:GO_2001023 regulation of drug resistance obo:GO_2001023 regulation of drug susceptibility/resistance obo:GO_2001023 GO:2001023 obo:GO_2001023 regulation of response to drug obo:GO_2001062 Interacting selectively and non-covalently with xylan. obo:GO_2001062 obo:go.owl obo:GO_2001062 jane obo:GO_2001062 2011-09-14T10:10:04Z obo:GO_2001062 molecular_function obo:GO_2001062 GO:2001062 obo:GO_2001062 xylan binding obo:GO_2001063 Interacting selectively and non-covalently with glucomannan. obo:GO_2001063 obo:go.owl obo:GO_2001063 jane obo:GO_2001063 2011-09-14T10:29:45Z obo:GO_2001063 molecular_function obo:GO_2001063 GO:2001063 obo:GO_2001063 glucomannan binding obo:GO_2001064 Interacting selectively and non-covalently with cellooligosaccharide. obo:GO_2001064 obo:go.owl obo:GO_2001064 jane obo:GO_2001064 2011-09-14T10:32:19Z obo:GO_2001064 molecular_function obo:GO_2001064 GO:2001064 obo:GO_2001064 cellooligosaccharide binding obo:GO_2001065 Interacting selectively and non-covalently with mannan. obo:GO_2001065 obo:go.owl obo:GO_2001065 jane obo:GO_2001065 2011-09-14T10:49:45Z obo:GO_2001065 molecular_function obo:GO_2001065 mannoglycan binding obo:GO_2001065 GO:2001065 obo:GO_2001065 mannan binding obo:GO_2001066 Interacting selectively and non-covalently with amylopectin. obo:GO_2001066 obo:go.owl obo:GO_2001066 jane obo:GO_2001066 2011-09-14T11:46:37Z obo:GO_2001066 molecular_function obo:GO_2001066 GO:2001066 obo:GO_2001066 amylopectin binding obo:GO_2001067 Interacting selectively and non-covalently with pullulan. obo:GO_2001067 obo:go.owl obo:GO_2001067 jane obo:GO_2001067 2011-09-14T11:50:06Z obo:GO_2001067 molecular_function obo:GO_2001067 GO:2001067 obo:GO_2001067 pullulan binding obo:GO_2001068 Interacting selectively and non-covalently with arabinoxylan. obo:GO_2001068 obo:go.owl obo:GO_2001068 jane obo:GO_2001068 2011-09-14T11:58:38Z obo:GO_2001068 molecular_function obo:GO_2001068 GO:2001068 obo:GO_2001068 arabinoxylan binding obo:GO_2001069 Interacting selectively and non-covalently with glycogen. obo:GO_2001069 obo:go.owl obo:GO_2001069 jane obo:GO_2001069 2011-09-14T12:01:06Z obo:GO_2001069 molecular_function obo:GO_2001069 animal starch binding obo:GO_2001069 liver starch binding obo:GO_2001069 GO:2001069 obo:GO_2001069 glycogen binding obo:GO_2001070 Interacting selectively and non-covalently with starch. obo:GO_2001070 obo:go.owl obo:GO_2001070 jane obo:GO_2001070 2011-09-14T12:02:50Z obo:GO_2001070 molecular_function obo:GO_2001070 amidon binding obo:GO_2001070 amylum binding obo:GO_2001070 GO:2001070 obo:GO_2001070 starch binding obo:GO_2001071 Interacting selectively and non-covalently with maltoheptaose. obo:GO_2001071 obo:go.owl obo:GO_2001071 jane obo:GO_2001071 2011-09-14T12:04:30Z obo:GO_2001071 molecular_function obo:GO_2001071 GO:2001071 obo:GO_2001071 maltoheptaose binding obo:GO_2001072 Interacting selectively and non-covalently with galactomannan. obo:GO_2001072 obo:go.owl obo:GO_2001072 jane obo:GO_2001072 2011-09-14T12:12:02Z obo:GO_2001072 molecular_function obo:GO_2001072 GO:2001072 obo:GO_2001072 galactomannan binding obo:GO_2001073 Interacting selectively and non-covalently with cyclodextrin. obo:GO_2001073 obo:go.owl obo:GO_2001073 jane obo:GO_2001073 2011-09-14T12:24:30Z obo:GO_2001073 molecular_function obo:GO_2001073 GO:2001073 obo:GO_2001073 cyclodextrin binding obo:GO_2001077 Interacting selectively and non-covalently with (1->3),(1->4)-beta-glucan. obo:GO_2001077 obo:go.owl obo:GO_2001077 jane obo:GO_2001077 2011-09-15T09:07:33Z obo:GO_2001077 (1,3),(1,4)-beta-glucan binding obo:GO_2001077 1->3,1->4-beta-glucan binding obo:GO_2001077 beta-(1,3),(1,4)-glucan binding obo:GO_2001077 beta-(1->3),(1->4)-glucan binding obo:GO_2001077 beta-1,3-1,4-glucan binding obo:GO_2001077 beta-1->3,1->4-glucan binding obo:GO_2001077 molecular_function obo:GO_2001077 GO:2001077 obo:GO_2001077 (1->3),(1->4)-beta-glucan binding obo:GO_2001078 Interacting selectively and non-covalently with (1->6)-beta-D-glucan. obo:GO_2001078 obo:go.owl obo:GO_2001078 jane obo:GO_2001078 2011-09-15T01:12:50Z obo:GO_2001078 (1,6)-beta-D-glucan binding obo:GO_2001078 1,6-beta-D-glucan binding obo:GO_2001078 1->6-beta-D-glucan binding obo:GO_2001078 beta-(1,6)-D-glucan binding obo:GO_2001078 beta-(1->6)-D-glucan binding obo:GO_2001078 beta-1,6-D-glucan binding obo:GO_2001078 beta-1->6-D-glucan binding obo:GO_2001078 molecular_function obo:GO_2001078 GO:2001078 obo:GO_2001078 (1->6)-beta-D-glucan binding obo:GO_2001079 Interacting selectively and non-covalently with beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc. obo:GO_2001079 obo:go.owl obo:GO_2001079 jane obo:GO_2001079 2011-09-15T01:15:19Z obo:GO_2001079 molecular_function obo:GO_2001079 GO:2001079 obo:GO_2001079 beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc binding obo:GO_2001080 Interacting selectively and non-covalently with chitosan. obo:GO_2001080 obo:go.owl obo:GO_2001080 jane obo:GO_2001080 2011-09-15T01:17:32Z obo:GO_2001080 molecular_function obo:GO_2001080 GO:2001080 obo:GO_2001080 chitosan binding obo:GO_2001081 Interacting selectively and non-covalently with (1->4)-beta-D-galactan. obo:GO_2001081 obo:go.owl obo:GO_2001081 jane obo:GO_2001081 2011-09-15T01:21:50Z obo:GO_2001081 (1,4)-beta-D-galactan binding obo:GO_2001081 molecular_function obo:GO_2001081 GO:2001081 obo:GO_2001081 (1->4)-beta-D-galactan binding obo:GO_2001082 Interacting selectively and non-covalently with inulin. obo:GO_2001082 obo:go.owl obo:GO_2001082 jane obo:GO_2001082 2011-09-15T01:23:59Z obo:GO_2001082 molecular_function obo:GO_2001082 GO:2001082 obo:GO_2001082 inulin binding obo:GO_2001083 Interacting selectively and non-covalently with alpha-D-glucan. obo:GO_2001083 obo:go.owl obo:GO_2001083 jane obo:GO_2001083 2011-09-15T01:26:14Z obo:GO_2001083 molecular_function obo:GO_2001083 GO:2001083 obo:GO_2001083 alpha-D-glucan binding obo:GO_2001084 Interacting selectively and non-covalently with L-arabinofuranose. obo:GO_2001084 obo:go.owl obo:GO_2001084 jane obo:GO_2001084 2011-09-15T01:33:53Z obo:GO_2001084 molecular_function obo:GO_2001084 GO:2001084 obo:GO_2001084 L-arabinofuranose binding obo:GO_2001085 Interacting selectively and non-covalently with arabinogalactan. obo:GO_2001085 obo:go.owl obo:GO_2001085 jane obo:GO_2001085 2011-09-15T01:35:51Z obo:GO_2001085 molecular_function obo:GO_2001085 GO:2001085 obo:GO_2001085 arabinogalactan binding obo:GO_2001147 Interacting selectively and non-covalently with camalexin. obo:GO_2001147 obo:go.owl obo:GO_2001147 tanyaberardini obo:GO_2001147 2011-10-19T10:54:19Z obo:GO_2001147 3-(1,3-thiazol-2-yl)-1H-indole binding obo:GO_2001147 molecular_function obo:GO_2001147 GO:2001147 obo:GO_2001147 camalexin binding obo:GO_2001225 Any process that modulates the frequency, rate or extent of chloride transport. obo:GO_2001225 obo:go.owl obo:GO_2001225 dph obo:GO_2001225 2011-11-18T05:45:56Z obo:GO_2001225 biological_process obo:GO_2001225 GO:2001225 obo:GO_2001225 regulation of chloride transport obo:GO_2001226 Any process that stops, prevents or reduces the frequency, rate or extent of chloride transport. obo:GO_2001226 obo:go.owl obo:GO_2001226 dph obo:GO_2001226 2011-11-18T05:46:03Z obo:GO_2001226 biological_process obo:GO_2001226 GO:2001226 obo:GO_2001226 negative regulation of chloride transport obo:GO_2001227 Interacting selectively and non-covalently with quercitrin. obo:GO_2001227 obo:go.owl obo:GO_2001227 tanyaberardini obo:GO_2001227 2011-11-18T09:58:37Z obo:GO_2001227 molecular_function obo:GO_2001227 GO:2001227 obo:GO_2001227 quercitrin binding obo:GO_2001231 Any process that modulates the frequency, rate or extent of protein localization to prospore membrane. obo:GO_2001231 obo:go.owl obo:GO_2001231 midori obo:GO_2001231 2011-11-21T04:13:30Z obo:GO_2001231 regulation of protein localisation to prospore membrane obo:GO_2001231 biological_process obo:GO_2001231 regulation of protein targeting to FSM obo:GO_2001231 regulation of protein targeting to ascospore-type prospore membrane obo:GO_2001231 regulation of protein targeting to forespore membrane obo:GO_2001231 regulation of protein targeting to prospore membrane obo:GO_2001231 regulation of protein-prospore membrane targeting obo:GO_2001231 GO:2001231 obo:GO_2001231 regulation of protein localization to prospore membrane obo:GO_2001232 Any process that activates or increases the frequency, rate or extent of protein localization to prospore membrane. obo:GO_2001232 obo:go.owl obo:GO_2001232 midori obo:GO_2001232 2011-11-21T04:13:36Z obo:GO_2001232 positive regulation of protein localisation to prospore membrane obo:GO_2001232 biological_process obo:GO_2001232 positive regulation of protein targeting to FSM obo:GO_2001232 positive regulation of protein targeting to ascospore-type prospore membrane obo:GO_2001232 positive regulation of protein targeting to forespore membrane obo:GO_2001232 positive regulation of protein targeting to prospore membrane obo:GO_2001232 positive regulation of protein-prospore membrane targeting obo:GO_2001232 GO:2001232 obo:GO_2001232 positive regulation of protein localization to prospore membrane obo:GO_2001256 Any process that modulates the frequency, rate or extent of store-operated calcium entry. obo:GO_2001256 obo:go.owl obo:GO_2001256 vk obo:GO_2001256 2011-12-07T07:08:38Z obo:GO_2001256 regulation of SOCE obo:GO_2001256 regulation of capacitative calcium entry obo:GO_2001256 regulation of store-operated calcium import obo:GO_2001256 biological_process obo:GO_2001256 regulation of calcium ion import obo:GO_2001256 GO:2001256 obo:GO_2001256 regulation of store-operated calcium entry obo:GO_2001257 Any process that modulates the frequency, rate or extent of cation channel activity. obo:GO_2001257 obo:go.owl obo:GO_2001257 vk obo:GO_2001257 2011-12-07T07:14:43Z obo:GO_2001257 regulation of cation diffusion facilitator activity obo:GO_2001257 regulation of nonselective cation channel activity obo:GO_2001257 biological_process obo:GO_2001257 GO:2001257 obo:GO_2001257 regulation of cation channel activity obo:GO_2001258 Any process that stops, prevents or reduces the frequency, rate or extent of cation channel activity. obo:GO_2001258 obo:go.owl obo:GO_2001258 vk obo:GO_2001258 2011-12-07T07:14:51Z obo:GO_2001258 negative regulation of cation diffusion facilitator activity obo:GO_2001258 negative regulation of nonselective cation channel activity obo:GO_2001258 biological_process obo:GO_2001258 GO:2001258 obo:GO_2001258 negative regulation of cation channel activity obo:GO_2001259 Any process that activates or increases the frequency, rate or extent of cation channel activity. obo:GO_2001259 obo:go.owl obo:GO_2001259 vk obo:GO_2001259 2011-12-07T07:14:57Z obo:GO_2001259 positive regulation of cation diffusion facilitator activity obo:GO_2001259 positive regulation of nonselective cation channel activity obo:GO_2001259 biological_process obo:GO_2001259 GO:2001259 obo:GO_2001259 positive regulation of cation channel activity obo:IAO_0000111 editor preferred term obo:IAO_0000111 obo:IAO_0000122 obo:IAO_0000111 The concise, meaningful, and human-friendly name for a class or property preferred by the ontology developers. (US-English) obo:IAO_0000111 PERSON:Daniel Schober obo:IAO_0000111 GROUP:OBI:<http://purl.obolibrary.org/obo/obi> obo:IAO_0000111 obo:iao.owl obo:IAO_0000111 editor preferred term obo:IAO_0000112 example obo:IAO_0000112 obo:IAO_0000122 obo:IAO_0000112 A phrase describing how a class name should be used. May also include other kinds of examples that facilitate immediate understanding of a class semantics, such as widely known prototypical subclasses or instances of the class. Although essential for high level terms, examples for low level terms (e.g., Affymetrix HU133 array) are not obo:IAO_0000112 PERSON:Daniel Schober obo:IAO_0000112 GROUP:OBI:<http://purl.obolibrary.org/obo/obi> obo:IAO_0000112 obo:iao.owl obo:IAO_0000112 example of usage obo:IAO_0000114 has curation status obo:IAO_0000114 PERSON:Alan Ruttenberg obo:IAO_0000114 PERSON:Bill Bug obo:IAO_0000114 PERSON:Melanie Courtot obo:IAO_0000114 OBI_0000281 obo:IAO_0000114 has curation status obo:IAO_0000115 definition obo:IAO_0000115 obo:IAO_0000122 obo:IAO_0000115 A property representing the English language definitions of what NCI means by the concept. They may also include information about the definition's source and attribution in a form that can easily be interpreted by software. obo:IAO_0000115 The official definition, explaining the meaning of a class or property. Shall be Aristotelian, formalized and normalized. Can be augmented with colloquial definitions. obo:IAO_0000115 PERSON:Daniel Schober obo:IAO_0000115 GROUP:OBI:<http://purl.obolibrary.org/obo/obi> obo:IAO_0000115 DEFINITION obo:IAO_0000115 obo:iao.owl obo:IAO_0000115 definition obo:IAO_0000115 definition obo:IAO_0000116 editor note obo:IAO_0000116 obo:IAO_0000122 obo:IAO_0000116 An administrative note intended for its editor. It may not be included in the publication version of the ontology, so it should contain nothing necessary for end users to understand the ontology. obo:IAO_0000116 PERSON:Daniel Schober obo:IAO_0000116 GROUP:OBI:<http://purl.obfoundry.org/obo/obi> obo:IAO_0000116 obo:iao.owl obo:IAO_0000116 editor note obo:IAO_0000117 term editor obo:IAO_0000117 obo:IAO_0000122 obo:IAO_0000117 Name of editor entering the term in the file. The term editor is a point of contact for information regarding the term. The term editor may be, but is not always, the author of the definition, which may have been worked upon by several people obo:IAO_0000117 20110707, MC: label update to term editor and definition modified accordingly. See http://code.google.com/p/information-artifact-ontology/issues/detail?id=115. obo:IAO_0000117 PERSON:Daniel Schober obo:IAO_0000117 GROUP:OBI:<http://purl.obolibrary.org/obo/obi> obo:IAO_0000117 obo:iao.owl obo:IAO_0000117 term editor obo:IAO_0000118 obo:IAO_0000125 obo:IAO_0000118 obo:iao.owl obo:IAO_0000118 alternative term obo:IAO_0000119 definition source obo:IAO_0000119 obo:IAO_0000122 obo:IAO_0000119 formal citation, e.g. identifier in external database to indicate / attribute source(s) for the definition. Free text indicate / attribute source(s) for the definition. EXAMPLE: Author Name, URI, MeSH Term C04, PUBMED ID, Wiki uri on 31.01.2007 obo:IAO_0000119 PERSON:Daniel Schober obo:IAO_0000119 Discussion on obo-discuss mailing-list, see http://bit.ly/hgm99w obo:IAO_0000119 GROUP:OBI:<http://purl.obolibrary.org/obo/obi> obo:IAO_0000119 obo:iao.owl obo:IAO_0000119 definition source obo:IAO_0000122 ready for release obo:IAO_0000125 pending final vetting obo:IAO_0000232 obo:IAO_0000122 obo:IAO_0000232 obo:iao.owl obo:IAO_0000232 curator note obo:IAO_0000412 obo:iao.owl obo:IAO_0000412 imported from obo:IAO_0000600 obo:iao.owl obo:IAO_0000600 elucidation obo:IAO_0000601 obo:iao.owl obo:IAO_0000601 has associated axiom(nl) obo:IAO_0000602 obo:iao.owl obo:IAO_0000602 has associated axiom(fol) obo:IAO_0010000 obo:iao.owl obo:IAO_0010000 has axiom label obo:NCBITaxon_10090 obo:ncbitaxon.owl obo:NCBITaxon_10090 obo:NCBITaxon_species obo:NCBITaxon_10090 NCBITaxon:85055 obo:NCBITaxon_10090 GC_ID:1 obo:NCBITaxon_10090 house mouse obo:NCBITaxon_10090 mouse obo:NCBITaxon_10090 ncbi_taxonomy obo:NCBITaxon_10090 Mus muscaris obo:NCBITaxon_10090 mice C57BL/6xCBA/CaJ hybrid obo:NCBITaxon_10090 Mus musculus obo:NCBITaxon_10239 obo:ncbitaxon.owl obo:NCBITaxon_10239 obo:NCBITaxon_superkingdom obo:NCBITaxon_10239 GC_ID:1 obo:NCBITaxon_10239 ncbi_taxonomy obo:NCBITaxon_10239 Vira obo:NCBITaxon_10239 Viridae obo:NCBITaxon_10239 viruses obo:NCBITaxon_10239 Viruses obo:NCBITaxon_11676 obo:ncbitaxon.owl obo:NCBITaxon_11676 obo:NCBITaxon_species obo:NCBITaxon_11676 HIV obo:NCBITaxon_11676 HIV-1 obo:NCBITaxon_11676 HIV1 obo:NCBITaxon_11676 LAV-1 obo:NCBITaxon_11676 GC_ID:1 obo:NCBITaxon_11676 ncbi_taxonomy obo:NCBITaxon_11676 AIDS virus obo:NCBITaxon_11676 Human immundeficiency virus type 1 obo:NCBITaxon_11676 Human immunodeficiencey virus type 1 obo:NCBITaxon_11676 Human immunodeficiency virus type 1 obo:NCBITaxon_11676 human immunodeficiency virus 1 HIV-1 obo:NCBITaxon_11676 human immunodeficiency virus HIV-1 obo:NCBITaxon_11676 human immunodeficiency virus type 1 ,HIV-1 obo:NCBITaxon_11676 human immunodeficiency virus type 1 HIV 1 obo:NCBITaxon_11676 human immunodeficiency virus type 1 HIV-1 obo:NCBITaxon_11676 human immunodeficiency virus type 1 HIV1 obo:NCBITaxon_11676 human immunodeficiency virus type 1, HIV-1 obo:NCBITaxon_11676 human immunodeficiency virus type I HIV-1 obo:NCBITaxon_11676 human immunodeficiency virus type-1 HIV-1 obo:NCBITaxon_11676 human immunodeficiency virus-1 HIV-1 obo:NCBITaxon_11676 Human immunodeficiency virus 1 obo:NCBITaxon_117571 obo:ncbitaxon.owl obo:NCBITaxon_117571 NCBITaxon:40673 obo:NCBITaxon_117571 GC_ID:1 obo:NCBITaxon_117571 bony vertebrates obo:NCBITaxon_117571 ncbi_taxonomy obo:NCBITaxon_117571 Euteleostomi obo:NCBITaxon_1206794 obo:ncbitaxon.owl obo:NCBITaxon_1206794 GC_ID:1 obo:NCBITaxon_1206794 ncbi_taxonomy obo:NCBITaxon_1206794 Ecdysozoa obo:NCBITaxon_1224 obo:ncbitaxon.owl obo:NCBITaxon_1224 obo:NCBITaxon_phylum obo:NCBITaxon_1224 GC_ID:11 obo:NCBITaxon_1224 PMID:11321122 obo:NCBITaxon_1224 PMID:11542017 obo:NCBITaxon_1224 PMID:11837318 obo:NCBITaxon_1224 PMID:16280474 obo:NCBITaxon_1224 purple bacteria obo:NCBITaxon_1224 purple bacteria and relatives obo:NCBITaxon_1224 purple non-sulfur bacteria obo:NCBITaxon_1224 purple photosynthetic bacteria obo:NCBITaxon_1224 purple photosynthetic bacteria and relatives obo:NCBITaxon_1224 ncbi_taxonomy obo:NCBITaxon_1224 proteobacteria obo:NCBITaxon_1224 Proteobacteria obo:NCBITaxon_1236 obo:ncbitaxon.owl obo:NCBITaxon_1236 obo:NCBITaxon_class obo:NCBITaxon_1236 GC_ID:11 obo:NCBITaxon_1236 PMID:16280474 obo:NCBITaxon_1236 ncbi_taxonomy obo:NCBITaxon_1236 Gammaproteobacteria Garrity et al. 2005 obo:NCBITaxon_1236 Proteobacteria gamma subdivision obo:NCBITaxon_1236 Purple bacteria, gamma subdivision obo:NCBITaxon_1236 g-proteobacteria obo:NCBITaxon_1236 gamma proteobacteria obo:NCBITaxon_1236 gamma subdivision obo:NCBITaxon_1236 gamma subgroup obo:NCBITaxon_1236 Gammaproteobacteria obo:NCBITaxon_2 obo:ncbitaxon.owl obo:NCBITaxon_2 obo:ogg.owl obo:NCBITaxon_2 obo:NCBITaxon_superkingdom obo:NCBITaxon_2 GC_ID:11 obo:NCBITaxon_2 PMID:10425795 obo:NCBITaxon_2 PMID:10425796 obo:NCBITaxon_2 PMID:10425797 obo:NCBITaxon_2 PMID:10490293 obo:NCBITaxon_2 PMID:10843050 obo:NCBITaxon_2 PMID:10939651 obo:NCBITaxon_2 PMID:10939673 obo:NCBITaxon_2 PMID:10939677 obo:NCBITaxon_2 PMID:11211268 obo:NCBITaxon_2 PMID:11321083 obo:NCBITaxon_2 PMID:11321113 obo:NCBITaxon_2 PMID:11411719 obo:NCBITaxon_2 PMID:11540071 obo:NCBITaxon_2 PMID:11542017 obo:NCBITaxon_2 PMID:11542087 obo:NCBITaxon_2 PMID:11760965 obo:NCBITaxon_2 PMID:12054223 obo:NCBITaxon_2 PMID:2112744 obo:NCBITaxon_2 PMID:270744 obo:NCBITaxon_2 PMID:8123559 obo:NCBITaxon_2 PMID:8590690 obo:NCBITaxon_2 PMID:9103655 obo:NCBITaxon_2 PMID:9336922 obo:NCBITaxon_2 eubacteria obo:NCBITaxon_2 ncbi_taxonomy obo:NCBITaxon_2 Monera obo:NCBITaxon_2 Procaryotae obo:NCBITaxon_2 Prokaryota obo:NCBITaxon_2 Prokaryotae obo:NCBITaxon_2 bacteria obo:NCBITaxon_2 not Bacteria Haeckel 1894 obo:NCBITaxon_2 prokaryote obo:NCBITaxon_2 prokaryotes obo:NCBITaxon_2 Bacteria obo:NCBITaxon_208964 obo:ncbitaxon.owl obo:NCBITaxon_208964 GC_ID:11 obo:NCBITaxon_208964 PMID:10984043 obo:NCBITaxon_208964 ncbi_taxonomy obo:NCBITaxon_208964 Pseudomonas aeruginosa PA01 obo:NCBITaxon_208964 Pseudomonas aeruginosa str. PA01 obo:NCBITaxon_208964 Pseudomonas aeruginosa str. PAO1 obo:NCBITaxon_208964 Pseudomonas aeruginosa PAO1 obo:NCBITaxon_2157 obo:ncbitaxon.owl obo:NCBITaxon_2157 obo:NCBITaxon_superkingdom obo:NCBITaxon_2157 GC_ID:11 obo:NCBITaxon_2157 PMID:10425795 obo:NCBITaxon_2157 PMID:10425796 obo:NCBITaxon_2157 PMID:10425797 obo:NCBITaxon_2157 PMID:10490293 obo:NCBITaxon_2157 PMID:10843050 obo:NCBITaxon_2157 PMID:10939651 obo:NCBITaxon_2157 PMID:10939673 obo:NCBITaxon_2157 PMID:10939677 obo:NCBITaxon_2157 PMID:11211268 obo:NCBITaxon_2157 PMID:11321083 obo:NCBITaxon_2157 PMID:11321113 obo:NCBITaxon_2157 PMID:11411719 obo:NCBITaxon_2157 PMID:11540071 obo:NCBITaxon_2157 PMID:11541975 obo:NCBITaxon_2157 PMID:11542064 obo:NCBITaxon_2157 PMID:11542149 obo:NCBITaxon_2157 PMID:11760965 obo:NCBITaxon_2157 PMID:12054223 obo:NCBITaxon_2157 PMID:2112744 obo:NCBITaxon_2157 PMID:270744 obo:NCBITaxon_2157 PMID:8123559 obo:NCBITaxon_2157 PMID:8590690 obo:NCBITaxon_2157 PMID:9103655 obo:NCBITaxon_2157 PMID:9336922 obo:NCBITaxon_2157 ncbi_taxonomy obo:NCBITaxon_2157 Archaebacteria obo:NCBITaxon_2157 Mendosicutes obo:NCBITaxon_2157 Metabacteria obo:NCBITaxon_2157 Monera obo:NCBITaxon_2157 Procaryotae obo:NCBITaxon_2157 Prokaryota obo:NCBITaxon_2157 Prokaryotae obo:NCBITaxon_2157 archaea obo:NCBITaxon_2157 prokaryote obo:NCBITaxon_2157 prokaryotes obo:NCBITaxon_2157 Archaea obo:NCBITaxon_224914 obo:ncbitaxon.owl obo:NCBITaxon_224914 GC_ID:11 obo:NCBITaxon_224914 PMID:11756688 obo:NCBITaxon_224914 ncbi_taxonomy obo:NCBITaxon_224914 Brucella melitensis 16M obo:NCBITaxon_224914 Brucella melitensis ATCC 23456 obo:NCBITaxon_224914 Brucella melitensis str. 16M obo:NCBITaxon_224914 Brucella melitensis str. ATCC 23456 obo:NCBITaxon_224914 Brucella melitensis bv. 1 str. 16M obo:NCBITaxon_2759 obo:ncbitaxon.owl obo:NCBITaxon_2759 obo:NCBITaxon_superkingdom obo:NCBITaxon_2759 GC_ID:1 obo:NCBITaxon_2759 PMID:23020233 obo:NCBITaxon_2759 eucaryotes obo:NCBITaxon_2759 eukaryotes obo:NCBITaxon_2759 ncbi_taxonomy obo:NCBITaxon_2759 Eucarya obo:NCBITaxon_2759 Eucaryotae obo:NCBITaxon_2759 Eukarya obo:NCBITaxon_2759 Eukaryotae obo:NCBITaxon_2759 eukaryotes obo:NCBITaxon_2759 Eukaryota obo:NCBITaxon_314146 obo:ncbitaxon.owl obo:NCBITaxon_314146 obo:NCBITaxon_superorder obo:NCBITaxon_314146 GC_ID:1 obo:NCBITaxon_314146 PMID:11214319 obo:NCBITaxon_314146 PMID:12082125 obo:NCBITaxon_314146 PMID:12878460 obo:NCBITaxon_314146 PMID:15522813 obo:NCBITaxon_314146 ncbi_taxonomy obo:NCBITaxon_314146 Euarchontoglires obo:NCBITaxon_33154 obo:ncbitaxon.owl obo:NCBITaxon_33154 GC_ID:1 obo:NCBITaxon_33154 ncbi_taxonomy obo:NCBITaxon_33154 Fungi/Metazoa group obo:NCBITaxon_33154 opisthokonts obo:NCBITaxon_33154 Opisthokonta obo:NCBITaxon_33213 obo:ncbitaxon.owl obo:NCBITaxon_33213 GC_ID:1 obo:NCBITaxon_33213 ncbi_taxonomy obo:NCBITaxon_33213 Bilateria obo:NCBITaxon_335341 obo:ncbitaxon.owl obo:NCBITaxon_335341 GC_ID:1 obo:NCBITaxon_335341 ncbi_taxonomy obo:NCBITaxon_335341 Influenza A virus (A/New York/392/2004(H3N2)) obo:NCBITaxon_36329 obo:ncbitaxon.owl obo:NCBITaxon_36329 GC_ID:1 obo:NCBITaxon_36329 ncbi_taxonomy obo:NCBITaxon_36329 PLASMODIUM FALCIPARUM (ISOLATE 3D7). obo:NCBITaxon_36329 Plasmodium falciparum (isolate 3D7) obo:NCBITaxon_36329 Plasmodium falciparum 3D7 obo:NCBITaxon_3702 obo:ncbitaxon.owl obo:NCBITaxon_3702 obo:NCBITaxon_species obo:NCBITaxon_3702 GC_ID:1 obo:NCBITaxon_3702 mouse-ear cress obo:NCBITaxon_3702 thale cress obo:NCBITaxon_3702 thale-cress obo:NCBITaxon_3702 ncbi_taxonomy obo:NCBITaxon_3702 Arabidopsis thaliana (thale cress) obo:NCBITaxon_3702 Arbisopsis thaliana obo:NCBITaxon_3702 Arabidopsis thaliana obo:NCBITaxon_511145 obo:ncbitaxon.owl obo:NCBITaxon_511145 GC_ID:11 obo:NCBITaxon_511145 Escherichia coli str. K12 substr. MG1655 obo:NCBITaxon_511145 Escherichia coli str. MG1655 obo:NCBITaxon_511145 Escherichia coli strain MG1655 obo:NCBITaxon_511145 ncbi_taxonomy obo:NCBITaxon_511145 Escherichia coli MG1655 obo:NCBITaxon_511145 Escherichia coli str. K-12 substr. MG1655 obo:NCBITaxon_559292 obo:ncbitaxon.owl obo:NCBITaxon_559292 GC_ID:1 obo:NCBITaxon_559292 ncbi_taxonomy obo:NCBITaxon_559292 Saccharomyces cerevisiae S288c obo:NCBITaxon_6239 obo:ncbitaxon.owl obo:NCBITaxon_6239 obo:NCBITaxon_species obo:NCBITaxon_6239 GC_ID:1 obo:NCBITaxon_6239 nematode obo:NCBITaxon_6239 ncbi_taxonomy obo:NCBITaxon_6239 Rhabditis elegans obo:NCBITaxon_6239 Caenorhabditis elegans obo:NCBITaxon_7227 obo:ncbitaxon.owl obo:NCBITaxon_7227 obo:NCBITaxon_species obo:NCBITaxon_7227 GC_ID:1 obo:NCBITaxon_7227 fruit fly obo:NCBITaxon_7227 ncbi_taxonomy obo:NCBITaxon_7227 Drosophila melangaster obo:NCBITaxon_7227 Drosophila melanogaster obo:NCBITaxon_7955 obo:ncbitaxon.owl obo:NCBITaxon_7955 obo:NCBITaxon_species obo:NCBITaxon_7955 NCBITaxon:27702 obo:NCBITaxon_7955 NCBITaxon:37966 obo:NCBITaxon_7955 GC_ID:1 obo:NCBITaxon_7955 leopard danio obo:NCBITaxon_7955 zebra danio obo:NCBITaxon_7955 zebra fish obo:NCBITaxon_7955 zebrafish obo:NCBITaxon_7955 ncbi_taxonomy obo:NCBITaxon_7955 Brachidanio rerio obo:NCBITaxon_7955 Brachydanio rerio obo:NCBITaxon_7955 Brachydanio rerio frankei obo:NCBITaxon_7955 Cyprinus rerio obo:NCBITaxon_7955 Cyprinus rerio Hamilton, 1822 obo:NCBITaxon_7955 Danio frankei obo:NCBITaxon_7955 Danio rerio (Hamilton, 1822) obo:NCBITaxon_7955 Danio rerio frankei obo:NCBITaxon_7955 Danio rerio obo:NCBITaxon_83332 obo:ncbitaxon.owl obo:NCBITaxon_83332 GC_ID:11 obo:NCBITaxon_83332 PMID:12218036 obo:NCBITaxon_83332 PMID:12368430 obo:NCBITaxon_83332 PMID:9634230 obo:NCBITaxon_83332 Mycobacterium tuberculosis str. H37Rv obo:NCBITaxon_83332 Mycobacterium tuberculosis strain H37Rv obo:NCBITaxon_83332 ncbi_taxonomy obo:NCBITaxon_83332 Mycobacterium tuberculosis H37Rv obo:NCBITaxon_83333 Escherichia coli K-12 obo:NCBITaxon_9606 obo:ncbitaxon.owl obo:NCBITaxon_9606 obo:NCBITaxon_species obo:NCBITaxon_9606 GC_ID:1 obo:NCBITaxon_9606 human obo:NCBITaxon_9606 man obo:NCBITaxon_9606 ncbi_taxonomy obo:NCBITaxon_9606 Homo sapiens obo:NCIT_A11 An association created to allow the source NICHD to assign a parent to each concept with the intent of creating a hierarchy that includes only terms in which they are a contributing source. obo:NCIT_A11 A11 obo:NCIT_A11 Conceptual Entity obo:NCIT_A11 Has_NICHD_Parent obo:NCIT_A11 Has_NICHD_Parent obo:NCIT_A11 Has_NICHD_Parent obo:NCIT_C258 Substances naturally produced by microorganisms or their derivatives that selectively target microorganisms not humans. Antibiotics kill or inhibit the growth of microorganisms by targeting components of the microbial cell absent from human cells, including bacterial cell walls, cell membrane, and 30S or 50S ribosomal subunits. These substances are used in the treatment of bacterial and other microbial infections. obo:NCIT_C258 obo:ncit.owl obo:NCIT_C258 obo:NCIT_C1909 obo:NCIT_C258 C258 obo:NCIT_C258 Chemical Viewed Functionally obo:NCIT_C258 Antibiotic obo:NCIT_C258 Antibiotic obo:NCIT_C258 C0003232 obo:NCIT_C258 CTRP obo:NCIT_C258 NICHD obo:NCIT_C258 A substance that kills microorganisms such as bacteria or mold, or stops them from growing and causing disease. obo:NCIT_C258 Substances that kill or inhibit the growth or other functions of microorganisms. These substances are used in the treatment of bacterial and other microbial infections, though this term is most often used to describe antibacterial agents. obo:NCIT_C258 Antibiotic obo:NCIT_C258 CHEBI:22582 obo:NCIT_C258 Antibiotic obo:NCIT_C258 Antibiotic obo:NCIT_C258 Antibiotic Agents obo:NCIT_C258 Antibiotic Drugs obo:NCIT_C258 Antibiotic Therapy obo:NCIT_C258 Antibiotics obo:NCIT_C258 Antimicrobial obo:NCIT_C258 Antimicrobial Agent obo:NCIT_C258 antibiotic obo:NCIT_C258 antimicrobial obo:NCIT_C258 http://purl.oboInOwllibrary.org/oboInOwl/NCIT_C116977 obo:NCIT_C258 http://purl.oboInOwllibrary.org/oboInOwl/NCIT_C116978 obo:NCIT_C258 http://purl.oboInOwllibrary.org/oboInOwl/NCIT_C128453 obo:NCIT_C258 http://purl.oboInOwllibrary.org/oboInOwl/NCIT_C90259 obo:NCIT_C258 antibiotic obo:NCIT_C41210 An environmental event, agent, act, or influence that can be detected by a receptor in the body and will invariably produce a reaction in a living organism, e.g. change in the behavior, functional or trophic reaction. obo:NCIT_C41210 obo:ncit.owl obo:NCIT_C41210 C41210 obo:NCIT_C41210 Functional Concept obo:NCIT_C41210 Stimulus obo:NCIT_C41210 C0234402 obo:NCIT_C41210 Stimulus obo:NCIT_C41210 Stimuli obo:NCIT_C41210 Stimulus obo:NCIT_C41210 stimulus obo:NCIT_NHC0 true obo:NCIT_NHC0 A property representing a concept unique identifier within the NCI Enterprise Vocabulary Service's NCI Thesaurus. obo:NCIT_NHC0 NHC0 obo:NCIT_NHC0 code obo:NCIT_NHC0 code obo:NCIT_NHC0 code obo:NCIT_P106 A property that represents a description of the sort of thing or category to which a concept belongs in the context of the UMLS semantic network. obo:NCIT_P106 P106 obo:NCIT_P106 Conceptual Entity obo:NCIT_P106 Semantic Type obo:NCIT_P106 Semantic_Type obo:NCIT_P106 In general, applying semantic types aids in allowing users (or computer programs) to draw conclusions about concepts by virtue of the categories to which they have been assigned. We use a set of semantic types developed for the UMLS Metathesaurus. There are currently 134 semantic types in the UMLS. obo:NCIT_P106 Semantic_Type obo:NCIT_P106 Semantic_Type obo:NCIT_P107 A property representing an alternative Preferred Name for use in some NCI systems. obo:NCIT_P107 P107 obo:NCIT_P107 Conceptual Entity obo:NCIT_P107 Display Name obo:NCIT_P107 Display_Name obo:NCIT_P107 Display Name obo:NCIT_P107 Display_Name obo:NCIT_P107 Display_Name obo:NCIT_P108 A property representing the word or phrase that NCI uses by preference to refer to the concept. obo:NCIT_P108 P108 obo:NCIT_P108 Conceptual Entity obo:NCIT_P108 Preferred Name obo:NCIT_P108 Preferred_Name obo:NCIT_P108 Preferred Name obo:NCIT_P108 Preferred Term obo:NCIT_P108 Preferred_Name obo:NCIT_P108 Preferred_Name obo:NCIT_P207 A property representing the concept unique identifier (CUI) assigned by the National Library of Medicine (NLM). If a concept in any NCI-maintained knowledgebase exists in the NLM Unified Medical Language System (UMLS), NCI includes the NLM CUI among the information we provide about the concept. obo:NCIT_P207 P207 obo:NCIT_P207 Conceptual Entity obo:NCIT_P207 UMLS CUI obo:NCIT_P207 UMLS_CUI obo:NCIT_P207 UMLS_CUI obo:NCIT_P207 UMLS_CUI obo:NCIT_P322 A property is used to indicate when a non-EVS entity has contributed to, and has a stake in, a concept. This is used where such entities, within or outside NCI, have indicated the need to be able to track their own concepts. A single concept can have multiple instances of this property if multiple entities have such a defined stake. obo:NCIT_P322 P322 obo:NCIT_P322 Conceptual Entity obo:NCIT_P322 Contributing Source obo:NCIT_P322 Contributing_Source obo:NCIT_P322 Contributing_Source obo:NCIT_P322 Contributing_Source obo:NCIT_P325 A property representing the English language definition of a concept from a source other than NCI. obo:NCIT_P325 P325 obo:NCIT_P325 Conceptual Entity obo:NCIT_P325 [source] Definition obo:NCIT_P325 ALT_DEFINITION obo:NCIT_P325 ALT_DEFINITION obo:NCIT_P325 ALT_DEFINITION obo:NCIT_P366 true obo:NCIT_P366 A property representing a retired unique concept identifier created and stored as Concept Name by legacy EVS software. Use of these values was long discouraged, but continued as late as 2009 when creation of new values ceased and Concept Name was retired. Legacy values are intended solely to help resolve and update earlier coding. obo:NCIT_P366 P366 obo:NCIT_P366 Conceptual Entity obo:NCIT_P366 Legacy Concept Name obo:NCIT_P366 Legacy Concept Name obo:NCIT_P366 Legacy_Concept_Name obo:NCIT_P368 A property representing that a concept in the 'Drug, Food, Chemical or Biomedical Material' branch of the NCI thesaurus maps to a specific concept in the EBI Chemical Entities of Biological Interest (CHEBI) database. obo:NCIT_P368 P368 obo:NCIT_P368 Conceptual Entity obo:NCIT_P368 CHEBI_ID obo:NCIT_P368 CHEBI_ID obo:NCIT_P368 CHEBI_ID obo:NCIT_P371 A property representing a term chosen by NICHD to be used in the representation of the NICHD hierarchy. obo:NCIT_P371 P371 obo:NCIT_P371 Conceptual Entity obo:NCIT_P371 NICHD_Hierarchy_Term obo:NCIT_P371 NICHD obo:NCIT_P371 NICHD_Hierarchy_Term obo:NCIT_P371 NICHD_Hierarchy_Term obo:NCIT_P98 A property representing notations made by NCI vocabulary curators. They are intended to provide supplemental, unstructured information to the user or additional insight about the concept. obo:NCIT_P98 P98 obo:NCIT_P98 Conceptual Entity obo:NCIT_P98 DesignNote obo:NCIT_P98 DesignNote obo:NCIT_P98 DesignNote obo:NCIT_P98 DesignNote obo:OBA_0000121 pH is a scale used to specify how acidic or basic a water-based solution is. obo:OBA_0000121 WEB: https://en.wikipedia.org/wiki/PH obo:OBA_0000121 obo:oba.owl obo:OBA_0000121 oba obo:OBA_0000121 OBA:0000121 obo:OBA_0000121 pH obo:OBI_0100026 organism obo:OBI_0100026 animal obo:OBI_0100026 fungus obo:OBI_0100026 plant obo:OBI_0100026 virus obo:OBI_0100026 obo:IAO_0000121 obo:OBI_0100026 A material entity that is an individual living system, such as animal, plant, bacteria or virus, that is capable of replicating or reproducing, growth and maintenance in the right environment. An organism may be unicellular or made up, like humans, of many billions of cells divided into specialized tissues and organs. obo:OBI_0100026 10/21/09: This is a placeholder term, that should ideally be imported from the NCBI taxonomy, but the high level hierarchy there does not suit our needs (includes plasmids and 'other organisms') obo:OBI_0100026 GROUP: OBI Biomaterial Branch obo:OBI_0100026 WEB: http://en.wikipedia.org/wiki/Organism obo:OBI_0100026 obo:obi.owl obo:OBI_0100026 obo:ogg.owl obo:OBI_0100026 organism obo:OGG_0000000001 A genome is a material entity that represents the entirety of an organism's hereditary information. The genome includes both the genes and the non-coding sequences of the DNA and RNA. obo:OGG_0000000001 Oliver He obo:OGG_0000000001 Book: Eugene Nester, Denise Anderson, C. Evans Roberts, Jr., Microbiology (Companion Site): A Human Perspective, 7th Edition. Mcgraw Hill, October 18, 2011. ISBN-13: 978-0073375311 obo:OGG_0000000001 WEB: http://en.wikipedia.org/wiki/Genome obo:OGG_0000000001 obo:ogg.owl obo:OGG_0000000001 genome obo:OGG_0000000002 A gene is a material entity that represents the entire DNA sequence required for synthesis of a functional protein or RNA molecule. obo:OGG_0000000002 Oliver He obo:OGG_0000000002 WEB: http://www.ncbi.nlm.nih.gov/books/NBK21640/ obo:OGG_0000000002 obo:ogg.owl obo:OGG_0000000002 In addition to the coding regions (exons), a gene includes transcription-control regions and sometimes introns. Although the majority of genes encode proteins, some encode tRNAs, rRNAs, and other types of RNA. obo:OGG_0000000002 gene obo:OGG_0000000003 a disposition that a gene can be used as a blueprint for generating a new form of product such as protein. obo:OGG_0000000003 Yongqun He obo:OGG_0000000003 WEB: http://www.ncbi.nlm.nih.gov/IEB/ToolBox/CPP_DOC/lxr/source/src/objects/entrezgene/entrezgene.asn obo:OGG_0000000003 obo:ogg.owl obo:OGG_0000000003 YH: According to NCBI Gene project, there are two gene types: unknown (0) , tRNA (1) , rRNA (2) , snRNA (3) , scRNA (4) , snoRNA (5) , protein-coding (6) , pseudo (7) , transposon (8) , miscRNA (9) , ncRNA (10) , other (255). Therefore, we have generated corresponding gene dispositions. Note that we don't use the term "gene type" here to differentiate the meanings of "type" and "disposition". obo:OGG_0000000003 gene disposition obo:OGG_0000000004 the symbol assigned by the nomenclature authority obo:OGG_0000000004 Oliver He, Yue Liu obo:OGG_0000000004 symbol from nomenclature authority obo:OGG_0000000005 the full name assigned by the nomenclature authority obo:OGG_0000000005 Oliver He, Yue Liu obo:OGG_0000000005 full name from nomenclature authority obo:OGG_0000000006 A GeneID in the NCBI Gene database obo:OGG_0000000006 Oliver He, Yue Liu obo:OGG_0000000006 NCBI GeneID obo:OGG_0000000007 the NCBI LocusTag name of a gene obo:OGG_0000000007 Oliver He, Yue Liu obo:OGG_0000000007 NCBI LocusTag obo:OGG_0000000008 the map location of a gene obo:OGG_0000000008 Oliver He, Yue Liu obo:OGG_0000000008 gene map location obo:OGG_0000000009 a date of content modification obo:OGG_0000000009 Oliver He, Yue Liu obo:OGG_0000000009 modification date obo:OGG_0000000010 a gene disposition that a gene can be used as a blueprint for generating a protein (i.e., a gene encodes for a protein). obo:OGG_0000000010 Yongqun He obo:OGG_0000000010 WEB: http://www.ncbi.nlm.nih.gov/IEB/ToolBox/CPP_DOC/lxr/source/src/objects/entrezgene/entrezgene.asn obo:OGG_0000000010 protein-coding gene disposition obo:OGG_0000000011 a gene disposition that is the disposition of a gene that encodes for a tRNA. obo:OGG_0000000011 Yongqun He, Bin Zhao obo:OGG_0000000011 WEB: http://www.ncbi.nlm.nih.gov/IEB/ToolBox/CPP_DOC/lxr/source/src/objects/entrezgene/entrezgene.asn obo:OGG_0000000011 RNA gene disposition obo:OGG_0000000012 a RNA gene disposition that is for a gene that encodes for a rRNA. obo:OGG_0000000012 Yongqun He obo:OGG_0000000012 WEB: http://www.ncbi.nlm.nih.gov/IEB/ToolBox/CPP_DOC/lxr/source/src/objects/entrezgene/entrezgene.asn obo:OGG_0000000012 rRNA gene disposition obo:OGG_0000000013 a RNA gene disposition that is for a gene that encodes for a snRNA. obo:OGG_0000000013 Yongqun He obo:OGG_0000000013 WEB: http://www.ncbi.nlm.nih.gov/IEB/ToolBox/CPP_DOC/lxr/source/src/objects/entrezgene/entrezgene.asn obo:OGG_0000000013 snRNA gene disposition obo:OGG_0000000014 a 'part of continuant at some time' relation that incides a genome belongs to a organism. obo:OGG_0000000014 Yongqun He, Bin Zhao obo:OGG_0000000014 obo:ogg.owl obo:OGG_0000000014 is genome of organism obo:OGG_0000000015 The NCBITaxon ontology ID of an organism. obo:OGG_0000000015 Oliver He, Yue Liu obo:OGG_0000000015 organism NCBITaxon ID obo:OGG_0000000016 a relation between a gene and the organism where this gene belongs to the organism in nature. It does not include a foreign gene that is transferred to an organism by a genetic engineering method. obo:OGG_0000000016 Oliver He, Yue Liu obo:OGG_0000000016 obo:ogg.owl obo:OGG_0000000016 is gene of organism obo:OGG_0000000017 A chromosome ID where a gene is located. obo:OGG_0000000017 Oliver He obo:OGG_0000000017 chromosome ID of gene obo:OGG_0000000018 an annotation property that specifies the type of a gene obo:OGG_0000000018 Oliver He obo:OGG_0000000018 type of gene obo:OGG_0000000019 an annotation property that specifies a nomenclature status obo:OGG_0000000019 Oliver He obo:OGG_0000000019 nomenclature status obo:OGG_0000000020 a RNA gene disposition that is for a gene that encodes for a tRNA. obo:OGG_0000000020 Yongqun He obo:OGG_0000000020 WEB: http://www.ncbi.nlm.nih.gov/IEB/ToolBox/CPP_DOC/lxr/source/src/objects/entrezgene/entrezgene.asn obo:OGG_0000000020 tRNA gene disposition obo:OGG_0000000021 a RNA gene disposition that is for a gene that encodes for a scRNA. obo:OGG_0000000021 Yongqun He obo:OGG_0000000021 WEB: http://www.ncbi.nlm.nih.gov/IEB/ToolBox/CPP_DOC/lxr/source/src/objects/entrezgene/entrezgene.asn obo:OGG_0000000021 scRNA gene disposition obo:OGG_0000000022 a RNA gene disposition that is for a gene that encodes for a snoRNA. obo:OGG_0000000022 Yongqun He obo:OGG_0000000022 WEB: http://www.ncbi.nlm.nih.gov/IEB/ToolBox/CPP_DOC/lxr/source/src/objects/entrezgene/entrezgene.asn obo:OGG_0000000022 snoRNA gene disposition obo:OGG_0000000023 a RNA gene disposition that is for a gene that encodes for a miscRNA. obo:OGG_0000000023 Yongqun He obo:OGG_0000000023 WEB: http://www.ncbi.nlm.nih.gov/IEB/ToolBox/CPP_DOC/lxr/source/src/objects/entrezgene/entrezgene.asn obo:OGG_0000000023 miscRNA gene disposition obo:OGG_0000000024 a RNA gene disposition that is for a gene that encodes for a ncRNA. obo:OGG_0000000024 Yongqun He obo:OGG_0000000024 WEB: http://www.ncbi.nlm.nih.gov/IEB/ToolBox/CPP_DOC/lxr/source/src/objects/entrezgene/entrezgene.asn obo:OGG_0000000024 ncRNA gene disposition obo:OGG_0000000025 a gene disposition that represents the disposition of gene being "pseudo", i.e., the gene is a pseudogene. obo:OGG_0000000025 Yongqun He obo:OGG_0000000025 WEB: http://www.ncbi.nlm.nih.gov/IEB/ToolBox/CPP_DOC/lxr/source/src/objects/entrezgene/entrezgene.asn obo:OGG_0000000025 pseudo gene disposition obo:OGG_0000000026 a gene disposition that represents the disposition of a gene that encodes for a transposon. obo:OGG_0000000026 Yongqun He obo:OGG_0000000026 WEB: http://www.ncbi.nlm.nih.gov/IEB/ToolBox/CPP_DOC/lxr/source/src/objects/entrezgene/entrezgene.asn obo:OGG_0000000026 transposon gene disposition obo:OGG_0000000027 a gene disposition that is "other", i.e., the gene is for a gene product that is not listed for another other gene type. obo:OGG_0000000027 Note: The other gene disposition originates from automated generation using terms imported from the NCBI Gene resource (http://www.ncbi.nlm.nih.gov/books/NBK3841/ ). However the use of such an information-related term is not fully compliant with the Foundry Principles. Before we can find a better solution, we will for now keep them in the OGG. obo:OGG_0000000027 Yongqun He obo:OGG_0000000027 WEB: http://www.ncbi.nlm.nih.gov/IEB/ToolBox/CPP_DOC/lxr/source/src/objects/entrezgene/entrezgene.asn obo:OGG_0000000027 other gene disposition obo:OGG_0000000028 a gene disposition that represents the disposition of gene where the gene product is unknown. obo:OGG_0000000028 Note: The unknown gene disposition originates from automated generation using terms imported from the NCBI Gene resource (http://www.ncbi.nlm.nih.gov/books/NBK3841/ ). However the use of such an information-related term is not fully compliant with the Foundry Principles. Before we can find a better solution, we will for now keep them in the OGG. obo:OGG_0000000028 Yongqun He obo:OGG_0000000028 WEB: http://www.ncbi.nlm.nih.gov/IEB/ToolBox/CPP_DOC/lxr/source/src/objects/entrezgene/entrezgene.asn obo:OGG_0000000028 unknown gene disposition obo:OGG_0000000029 an annotation property that shows the GO information associated with a specific gene. obo:OGG_0000000029 Yongqun He obo:OGG_0000000029 YH: use the convention: GO_ID (EC: xx; Qualifier: xx; PMID: xxxxx;) where GO_ID is a GO ID, EC is the Evidence Code, Qualifier is a specific association type, and PMID is a PubMed ID of a paper that supports the gene-GO association. obo:OGG_0000000029 has GO association obo:OGG_0000000030 An annotation property that represents a gene's association with PubMed publication(s). obo:OGG_0000000030 Yongqun He obo:OGG_0000000030 YH: use the format: PMID: pmid1, pmid2, ... where pmid1 and pmid2 are specfic PubMed IDs (PMIDs). obo:OGG_0000000030 has PubMed association obo:OGG_0000000031 a gene that encodes for a RNA obo:OGG_0000000031 Oliver He obo:OGG_0000000031 RNA gene obo:OGG_0000000032 a RNA gene that encodes for a miscRNA obo:OGG_0000000032 Oliver He obo:OGG_0000000032 miscRNA gene obo:OGG_0000000033 a RNA gene that encodes for a ncRNA obo:OGG_0000000033 Oliver He obo:OGG_0000000033 ncRNA gene obo:OGG_0000000034 a RNA gene that encodes for a rRNA obo:OGG_0000000034 Oliver He obo:OGG_0000000034 rRNA gene obo:OGG_0000000035 a RNA gene that encodes for a scRNA obo:OGG_0000000035 Oliver He obo:OGG_0000000035 scRNA gene obo:OGG_0000000036 a RNA gene that encodes for a snoRNA obo:OGG_0000000036 Oliver He obo:OGG_0000000036 snoRNA gene obo:OGG_0000000037 a RNA gene that encodes for a snRNA obo:OGG_0000000037 Oliver He obo:OGG_0000000037 snRNA gene obo:OGG_0000000038 a RNA gene that encodes for a tRNA obo:OGG_0000000038 Oliver He obo:OGG_0000000038 tRNA gene obo:OGG_0000000039 a gene that encodes for a protein obo:OGG_0000000039 Oliver He obo:OGG_0000000039 protein-coding gene obo:OGG_0000000040 a gene that has lost its protein-coding ability or is otherwise no longer expressed in the cell. obo:OGG_0000000040 Oliver He obo:OGG_0000000040 WEB: http://en.wikipedia.org/wiki/Pseudogene obo:OGG_0000000040 pseudo gene obo:OGG_0000000041 a gene that encodes for a transposable genetic element that can change its position within the genome. obo:OGG_0000000041 Oliver He obo:OGG_0000000041 WEB: http://en.wikipedia.org/wiki/Transposable_element obo:OGG_0000000041 transposon gene obo:OGG_0000000042 a gene that has an unknown gene disposition obo:OGG_0000000042 Note: The unknown gene disposition originates from automated generation using terms imported from the NCBI Gene resource (http://www.ncbi.nlm.nih.gov/books/NBK3841/ ). However the use of such an information-related term is not fully compliant with the Foundry Principles. Before we can find a better solution, we will for now keep them in the OGG. obo:OGG_0000000042 Oliver He obo:OGG_0000000042 WEB: http://www.ncbi.nlm.nih.gov/IEB/ToolBox/CPP_DOC/lxr/source/src/objects/entrezgene/entrezgene.asn obo:OGG_0000000042 WEB: http://www.ncbi.nlm.nih.gov/books/NBK3841/ obo:OGG_0000000042 gene with unknown gene disposition obo:OGG_0000000043 a gene that has an other gene disposition obo:OGG_0000000043 Note: The other gene disposition originates from automated generation using terms imported from the NCBI Gene resource (http://www.ncbi.nlm.nih.gov/books/NBK3841/ ). However the use of such an information-related term is not fully compliant with the Foundry Principles. Before we can find a better solution, we will for now keep them in the OGG. obo:OGG_0000000043 Oliver He obo:OGG_0000000043 WEB: http://www.ncbi.nlm.nih.gov/IEB/ToolBox/CPP_DOC/lxr/source/src/objects/entrezgene/entrezgene.asn obo:OGG_0000000043 WEB: http://www.ncbi.nlm.nih.gov/books/NBK3841/ obo:OGG_0000000043 gene with other gene disposition obo:OGG_1000000002 The genome of an organism of Bacteria obo:OGG_1000000002 Yue Liu, Bin Zhao, Oliver He obo:OGG_1000000002 obo:ogg.owl obo:OGG_1000000002 2 obo:OGG_1000000002 genome of Bacteria obo:OGG_2000000002 A gene of an organism of Bacteria obo:OGG_2000000002 Yue Liu, Bin Zhao, Oliver He obo:OGG_2000000002 obo:ogg.owl obo:OGG_2000000002 2 obo:OGG_2000000002 gene of Bacteria obo:OGG_2060511145 A gene of Escherichia coli str. K-12 that has a protein-coding gene disposition obo:OGG_2060511145 Bin Zhao, Oliver He obo:OGG_2060511145 obo:ogg.owl obo:OGG_2060511145 511145 obo:OGG_2060511145 protein-coding gene of Escherichia coli K-12 obo:OGG_3000945003 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000945003 ECK0563 obo:OGG_3000945003 JW0560 obo:OGG_3000945003 silR obo:OGG_3000945003 ylcA obo:OGG_3000945003 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000945003 obo:ogg.owl obo:OGG_3000945003 945003 obo:OGG_3000945003 b0571 obo:OGG_3000945003 20140406 obo:OGG_3000945003 511145 obo:OGG_3000945003 protein-coding obo:OGG_3000945003 NCBI-supplied obo:OGG_3000945003 PMID: 9278503; 11004187; 11283292; 11399769; 12368244; 12618449; 12627170; 12829268; 12829274; 12897016; 15522865; 15773991; 16397293; 17122336; 18631241 obo:OGG_3000945003 DNA-binding response regulator in two-component regulatory system with CusS obo:OGG_3000945003 EcoGene:EG13851 obo:OGG_3000945003 cusR obo:OGG_3000945044 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000945044 ECK0394 obo:OGG_3000945044 JW0390 obo:OGG_3000945044 R1pho obo:OGG_3000945044 nmpB obo:OGG_3000945044 phoR1 obo:OGG_3000945044 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000945044 obo:ogg.owl obo:OGG_3000945044 945044 obo:OGG_3000945044 b0400 obo:OGG_3000945044 20140406 obo:OGG_3000945044 511145 obo:OGG_3000945044 protein-coding obo:OGG_3000945044 NCBI-supplied obo:OGG_3000945044 GO_0006464; GO_0006793; GO_0009274; GO_0019866 obo:OGG_3000945044 PMID: 2187152; 2411941; 2693738; 2824439; 2896188; 3550103; 4570598; 4903904; 6310121; 6995425; 7021308; 7050395; 8391104; 8432742; 9278503; 9495769; 11466297; 11782500; 12533489; 12897016; 14526009; 15919996; 16120447; 16397293; 16606699; 17187058; 18031348; 18051755; 22812494; 23333741 obo:OGG_3000945044 sensory histidine kinase in two-component regulatory system with PhoB obo:OGG_3000945044 EcoGene:EG10733 obo:OGG_3000945044 phoR obo:OGG_3000945046 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000945046 ECK0393 obo:OGG_3000945046 JW0389 obo:OGG_3000945046 phoRc obo:OGG_3000945046 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000945046 obo:ogg.owl obo:OGG_3000945046 945046 obo:OGG_3000945046 b0399 obo:OGG_3000945046 20140406 obo:OGG_3000945046 511145 obo:OGG_3000945046 protein-coding obo:OGG_3000945046 NCBI-supplied obo:OGG_3000945046 GO_0005737; GO_0006793; GO_0016563 obo:OGG_3000945046 PMID: 324866; 1478454; 1482126; 1551836; 2157156; 2228961; 2411941; 2651888; 2693738; 2824439; 3054125; 3537313; 6260750; 6285149; 6307829; 6310121; 6343798; 7009567; 7016839; 7021308; 7050395; 7651320; 7699720; 7855419; 8098993; 8422984; 8432742; 8648643; 8691745; 8755861; 9016718; 9199401; 9278503; 9495769; 9555903; 9878437; 10089538; 10589831; 10653699; 10986267; 11073900; 11244058; 11466297; 11782500; 12015142; 12015152; 12351839; 12618449; 12897016; 14526009; 16154079; 16154092; 16397293; 16606699; 16818608; 16929106; 17020555; 17182055; 17543954; 18031348; 18631241; 19199332; 19371748; 19536200; 21829166; 23760278; 24199636 obo:OGG_3000945046 DNA-binding response regulator in two-component regulatory system with PhoR (or CreC) obo:OGG_3000945046 EcoGene:EG10728 obo:OGG_3000945046 phoB obo:OGG_3000945130 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000945130 ECK2253 obo:OGG_3000945130 JW2254 obo:OGG_3000945130 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000945130 obo:ogg.owl obo:OGG_3000945130 945130 obo:OGG_3000945130 b2259 obo:OGG_3000945130 20140406 obo:OGG_3000945130 511145 obo:OGG_3000945130 protein-coding obo:OGG_3000945130 NCBI-supplied obo:OGG_3000945130 GO_0042493 obo:OGG_3000945130 PMID: 8206837; 8524935; 8626063; 9278503; 10373459; 10775270; 12676988; 15371344; 15569938; 15691651; 16397293; 17615238; 17686460; 19428472; 19932119; 21811415 obo:OGG_3000945130 inactive two-component system connector protein obo:OGG_3000945130 EcoGene:EG12671 obo:OGG_3000945130 pmrD obo:OGG_3000945233 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000945233 ECK0612 obo:OGG_3000945233 JW0611 obo:OGG_3000945233 citA obo:OGG_3000945233 mpdB obo:OGG_3000945233 ybeP obo:OGG_3000945233 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000945233 obo:ogg.owl obo:OGG_3000945233 945233 obo:OGG_3000945233 b0619 obo:OGG_3000945233 20140406 obo:OGG_3000945233 511145 obo:OGG_3000945233 protein-coding obo:OGG_3000945233 NCBI-supplied obo:OGG_3000945233 GO_0006464; GO_0009274; GO_0019866 obo:OGG_3000945233 PMID: 6997437; 7045076; 8626281; 8655536; 9079897; 9095416; 9278503; 9701802; 11889485; 12618449; 12853150; 12897016; 12951338; 15308764; 15361616; 15919996; 16120447; 16397293; 16559027; 16606699; 16934473; 17222132; 18667579; 18997424; 19202292; 19426207; 22101843 obo:OGG_3000945233 sensory histidine kinase in two-component regulatory system with citB obo:OGG_3000945233 EcoGene:EG13646 obo:OGG_3000945233 dpiB obo:OGG_3000945302 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000945302 ECK0682 obo:OGG_3000945302 JW5096 obo:OGG_3000945302 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000945302 obo:ogg.owl obo:OGG_3000945302 945302 obo:OGG_3000945302 b0694 obo:OGG_3000945302 20140406 obo:OGG_3000945302 511145 obo:OGG_3000945302 protein-coding obo:OGG_3000945302 NCBI-supplied obo:OGG_3000945302 GO_0005737; GO_0016563 obo:OGG_3000945302 PMID: 1482126; 1532387; 1532388; 1630316; 1630317; 1970651; 2157156; 2995318; 3318698; 3536861; 6787588; 7699720; 7855422; 8098993; 8223625; 8276778; 8331081; 8437514; 8905232; 9099740; 9139930; 9278503; 9651326; 9748442; 10712703; 11016946; 11114904; 11123681; 11371546; 11931551; 12115059; 12618449; 12897016; 14534307; 15555756; 16322582; 16397293; 16887611; 17536175; 18631241; 19101563; 19400808; 20146748; 22291906; 23073764 obo:OGG_3000945302 DNA-binding response regulator in two-component regulatory system with KdpD obo:OGG_3000945302 EcoGene:EG10517 obo:OGG_3000945302 kdpE obo:OGG_3000945369 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000945369 ECK3016 obo:OGG_3000945369 JW2993 obo:OGG_3000945369 preA obo:OGG_3000945369 ygiX obo:OGG_3000945369 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000945369 obo:ogg.owl obo:OGG_3000945369 945369 obo:OGG_3000945369 b3025 obo:OGG_3000945369 20140406 obo:OGG_3000945369 511145 obo:OGG_3000945369 protein-coding obo:OGG_3000945369 NCBI-supplied obo:OGG_3000945369 GO_0006355 obo:OGG_3000945369 PMID: 9278503; 11929534; 12618449; 12897016; 16194231; 16397293; 16397770; 18631241; 19703104 obo:OGG_3000945369 quorum sensing DNA-binding response regulator in two-component regulatory system with QseC obo:OGG_3000945369 EcoGene:EG13026 obo:OGG_3000945369 qseB obo:OGG_3000945595 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000945595 ECK0984 obo:OGG_3000945595 JW5135 obo:OGG_3000945595 yccI obo:OGG_3000945595 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000945595 obo:ogg.owl obo:OGG_3000945595 945595 obo:OGG_3000945595 b0993 obo:OGG_3000945595 20140406 obo:OGG_3000945595 511145 obo:OGG_3000945595 protein-coding obo:OGG_3000945595 NCBI-supplied obo:OGG_3000945595 GO_0006464; GO_0009061; GO_0009274; GO_0019866 obo:OGG_3000945595 PMID: 8083154; 8809780; 9135110; 9278503; 10411745; 10648521; 11274133; 11562502; 12897016; 15919996; 16397293; 19748340 obo:OGG_3000945595 hybrid sensory histidine kinase in two-component regulatory system with TorR obo:OGG_3000945595 EcoGene:EG12617 obo:OGG_3000945595 torS obo:OGG_3000945697 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000945697 ECK1116 obo:OGG_3000945697 JW1116 obo:OGG_3000945697 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000945697 obo:ogg.owl obo:OGG_3000945697 945697 obo:OGG_3000945697 b1130 obo:OGG_3000945697 20140406 obo:OGG_3000945697 511145 obo:OGG_3000945697 protein-coding obo:OGG_3000945697 NCBI-supplied obo:OGG_3000945697 GO_0005737; GO_0016563 obo:OGG_3000945697 PMID: 1465423; 1482126; 1530848; 1729205; 1729240; 2157156; 7699720; 8098993; 8900137; 8905232; 9278503; 9603873; 10464230; 10775270; 10807931; 11435407; 12123454; 12139620; 12218035; 12429059; 12618449; 12670981; 12702718; 12813061; 12897016; 13129944; 14523115; 15126461; 15703297; 15883881; 16041131; 16397293; 16818608; 17543954; 17545283; 17628149; 17909183; 17998538; 18631241; 18792678; 18987315; 19426448; 19702577; 19772633; 19889087; 20345657; 22267510; 23300478 obo:OGG_3000945697 DNA-binding response regulator in two-component regulatory system with PhoQ obo:OGG_3000945697 EcoGene:EG10731 obo:OGG_3000945697 phoP obo:OGG_3000945788 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000945788 ECK1216 obo:OGG_3000945788 JW1213 obo:OGG_3000945788 frdR obo:OGG_3000945788 narR obo:OGG_3000945788 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000945788 obo:ogg.owl obo:OGG_3000945788 945788 obo:OGG_3000945788 b1222 obo:OGG_3000945788 20140406 obo:OGG_3000945788 511145 obo:OGG_3000945788 protein-coding obo:OGG_3000945788 NCBI-supplied obo:OGG_3000945788 GO_0006464; GO_0009061; GO_0009274; GO_0019866 obo:OGG_3000945788 PMID: 1528845; 1812811; 1999382; 2144276; 2544557; 2649492; 2657652; 2668029; 2832370; 3276662; 7601854; 7855431; 8051011; 8473280; 8501030; 8905232; 9006026; 9220011; 9278503; 9426129; 10464202; 11994152; 12486044; 12546643; 12581159; 12644479; 12897007; 12897016; 15919996; 15995204; 16377617; 16397293; 18375557; 19217390; 19966007; 19968795; 23517441 obo:OGG_3000945788 sensory histidine kinase in two-component regulatory system with NarL obo:OGG_3000945788 EcoGene:EG10646 obo:OGG_3000945788 narX obo:OGG_3000945795 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000945795 ECK1215 obo:OGG_3000945795 JW1212 obo:OGG_3000945795 frdR obo:OGG_3000945795 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000945795 obo:ogg.owl obo:OGG_3000945795 945795 obo:OGG_3000945795 b1221 obo:OGG_3000945795 20140406 obo:OGG_3000945795 511145 obo:OGG_3000945795 protein-coding obo:OGG_3000945795 NCBI-supplied obo:OGG_3000945795 GO_0005737; GO_0009061; GO_0016563; GO_0016564 obo:OGG_3000945795 PMID: 1482126; 1629213; 1812811; 1999382; 2066339; 2157156; 2173895; 2544557; 2648330; 2649492; 2657652; 2832370; 3035558; 3054467; 3276662; 3308846; 6261088; 7050087; 7601827; 7601854; 7643383; 7699720; 7854119; 8057356; 8098993; 8501030; 8780507; 8905232; 9278503; 9521685; 11115116; 12079504; 12581159; 12618449; 12644479; 12818201; 12897016; 12923080; 12951338; 15225315; 15978080; 15995204; 16199562; 16262254; 16377617; 16397293; 16417496; 16606699; 16936015; 17366475; 17449618; 17720788; 17965164; 18227264; 18631241; 19245365; 19251855; 19968795; 20634237 obo:OGG_3000945795 DNA-binding response regulator in two-component regulatory system with NarX (or NarQ) obo:OGG_3000945795 EcoGene:EG10643 obo:OGG_3000945795 narL obo:OGG_3000945855 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000945855 ECK1230 obo:OGG_3000945855 JW1223 obo:OGG_3000945855 hnr obo:OGG_3000945855 mviA obo:OGG_3000945855 sprE obo:OGG_3000945855 verA obo:OGG_3000945855 ychL obo:OGG_3000945855 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000945855 obo:ogg.owl obo:OGG_3000945855 945855 obo:OGG_3000945855 b1235 obo:OGG_3000945855 20140406 obo:OGG_3000945855 511145 obo:OGG_3000945855 protein-coding obo:OGG_3000945855 NCBI-supplied obo:OGG_3000945855 GO_0005737 obo:OGG_3000945855 PMID: 7997161; 8282700; 8635466; 8637901; 8885260; 8905232; 9278503; 9495753; 9515704; 9882671; 10339606; 10572304; 10672187; 10869095; 11442836; 11566997; 12354235; 12618449; 12897016; 12912910; 14536077; 14671322; 15489452; 15530384; 15629914; 16267278; 16291649; 16397293; 16556229; 16600914; 16606699; 17067847; 17122336; 17332743; 17403784; 18036141; 18239914; 18383615; 18519731; 18616600; 18792681; 19124769; 19125225; 19767441; 19781640 obo:OGG_3000945855 response regulator binding RpoS to initiate proteolysis by ClpXP; required for the PcnB-degradosome interaction during stationary phase obo:OGG_3000945855 EcoGene:EG12121 obo:OGG_3000945855 rssB obo:OGG_3000945978 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000945978 ECK0562 obo:OGG_3000945978 JW5082 obo:OGG_3000945978 silS obo:OGG_3000945978 ybcZ obo:OGG_3000945978 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000945978 obo:ogg.owl obo:OGG_3000945978 945978 obo:OGG_3000945978 b0570 obo:OGG_3000945978 20140406 obo:OGG_3000945978 511145 obo:OGG_3000945978 protein-coding obo:OGG_3000945978 NCBI-supplied obo:OGG_3000945978 GO_0006464; GO_0019866 obo:OGG_3000945978 PMID: 9278503; 11004187; 11283292; 11399769; 12829268; 12829274; 12897016; 15522865; 15919996; 16120447; 16397293; 22348296 obo:OGG_3000945978 sensory histidine kinase in two-component regulatory system with CusR, senses copper ions obo:OGG_3000945978 EcoGene:EG13642 obo:OGG_3000945978 cusS obo:OGG_3000946182 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000946182 ECK0986 obo:OGG_3000946182 JW0980 obo:OGG_3000946182 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000946182 obo:ogg.owl obo:OGG_3000946182 946182 obo:OGG_3000946182 b0995 obo:OGG_3000946182 20140406 obo:OGG_3000946182 511145 obo:OGG_3000946182 protein-coding obo:OGG_3000946182 NCBI-supplied obo:OGG_3000946182 GO_0005737; GO_0009061; GO_0016563 obo:OGG_3000946182 PMID: 1482126; 2157156; 7699720; 7798146; 8083154; 8098993; 8596446; 8905232; 9278503; 10648521; 11274133; 12618449; 12897016; 16322582; 16397293; 16606699; 18631241 obo:OGG_3000946182 DNA-binding response regulator in two-component regulatory system with TorS obo:OGG_3000946182 EcoGene:EG12615 obo:OGG_3000946182 torR obo:OGG_3000946199 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000946199 ECK1603 obo:OGG_3000946199 JW1600 obo:OGG_3000946199 urpT obo:OGG_3000946199 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000946199 obo:ogg.owl obo:OGG_3000946199 946199 obo:OGG_3000946199 b1608 obo:OGG_3000946199 20140406 obo:OGG_3000946199 511145 obo:OGG_3000946199 protein-coding obo:OGG_3000946199 NCBI-supplied obo:OGG_3000946199 GO_0005737; GO_0016563 obo:OGG_3000946199 PMID: 1495392; 9097039; 9278503; 12399493; 12618449; 12813061; 12897016; 12951338; 15126461; 15522865; 15748988; 15883881; 16397293; 16849790; 17293428; 17468243; 18631241; 19376873; 19465656 obo:OGG_3000946199 multicopy supressor of yjeE, yeaZ or ygjD deletion lethality, predicted response regulator of two-component regulatory system with sensor protein RstB obo:OGG_3000946199 EcoGene:EG13190 obo:OGG_3000946199 rstA obo:OGG_3000946326 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000946326 ECK1115 obo:OGG_3000946326 JW1115 obo:OGG_3000946326 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000946326 obo:ogg.owl obo:OGG_3000946326 946326 obo:OGG_3000946326 b1129 obo:OGG_3000946326 20140406 obo:OGG_3000946326 511145 obo:OGG_3000946326 protein-coding obo:OGG_3000946326 NCBI-supplied obo:OGG_3000946326 GO_0006464; GO_0009274; GO_0019866 obo:OGG_3000946326 PMID: 1465423; 1729240; 8548821; 8900137; 8905232; 9278503; 9603873; 10464230; 10775270; 12218035; 12429059; 12670981; 12702718; 12813061; 12897016; 13129944; 14523115; 15126461; 15522865; 15703297; 15883881; 15919996; 16041131; 16120447; 16397293; 17543954; 17628149; 17909183; 17985211; 17998538; 18348979; 18468622; 18792678; 18987315; 19702577; 19889087; 20345657; 20404199; 22267510; 22651704; 23300478 obo:OGG_3000946326 sensory histidine kinase in two-component regulatory system with PhoP obo:OGG_3000946326 EcoGene:EG10732 obo:OGG_3000946326 phoQ obo:OGG_3000946351 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000946351 ECK1824 obo:OGG_3000946351 JW1815 obo:OGG_3000946351 yobG obo:OGG_3000946351 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000946351 obo:ogg.owl obo:OGG_3000946351 946351 obo:OGG_3000946351 b1826 obo:OGG_3000946351 20140406 obo:OGG_3000946351 511145 obo:OGG_3000946351 protein-coding obo:OGG_3000946351 NCBI-supplied obo:OGG_3000946351 PMID: 9278503; 10464230; 12399493; 12813061; 12876315; 15126461; 15174130; 16041131; 16397293; 17543954; 17909183; 19121005; 19734312; 19854892 obo:OGG_3000946351 regulatory peptide for PhoPQ, feedback inhibition obo:OGG_3000946351 EcoGene:EG14383 obo:OGG_3000946351 mgrB obo:OGG_3000946393 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000946393 ECK1883 obo:OGG_3000946393 JW1871 obo:OGG_3000946393 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000946393 obo:ogg.owl obo:OGG_3000946393 946393 obo:OGG_3000946393 b1882 obo:OGG_3000946393 20140406 obo:OGG_3000946393 511145 obo:OGG_3000946393 protein-coding obo:OGG_3000946393 NCBI-supplied obo:OGG_3000946393 GO_0005737; GO_0042330 obo:OGG_3000946393 PMID: 353036; 1390767; 1482126; 1869568; 2157156; 2201404; 2644646; 2646634; 2689446; 3076076; 3185734; 3280143; 3510184; 6089173; 6090423; 6307970; 7034961; 7045071; 7592359; 7592655; 7615544; 7623663; 7699720; 7723026; 7855419; 8098993; 8176739; 8251514; 8354264; 8524808; 8631757; 8632450; 8763950; 8809743; 8820640; 9010924; 9030562; 9030763; 9097040; 9115243; 9188789; 9209042; 9278503; 9437425; 9473056; 9560203; 9636149; 9657998; 9748445; 9761838; 9761905; 10029518; 10096080; 10594818; 10731410; 10748173; 10748215; 10819997; 10894745; 10972797; 11023787; 11134926; 11135671; 11243808; 11279165; 11359578; 11410584; 12080332; 12145642; 12232047; 12511501; 12591864; 12591865; 12618449; 12736245; 12897016; 12951338; 14563873; 14741223; 15042093; 15175281; 15189900; 15236585; 15289606; 15327941; 15327942; 15351654; 15375146; 15539117; 15569922; 15601687; 15741343; 15909991; 16208378; 16306993; 16369945; 16397293; 16452309; 16630631; 16683020; 16707688; 17050923; 17122336; 17172298; 17339063; 17609139; 17609141; 17609145; 17628132; 17708539; 17998207; 18234227; 18427119; 18476921; 18557815; 18619461; 18644380; 18687900; 18711126; 18801331; 19096502; 19246239; 19467245; 19494578; 19540260; 19547746; 19646451; 20345663; 20398208; 20439729; 20498085; 21422514; 21642453; 21764922; 23454041; 23648838 obo:OGG_3000946393 chemotaxis regulator transmitting signal to flagellar motor component obo:OGG_3000946393 EcoGene:EG10150 obo:OGG_3000946393 cheY obo:OGG_3000946394 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000946394 ECK1884 obo:OGG_3000946394 JW1872 obo:OGG_3000946394 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000946394 obo:ogg.owl obo:OGG_3000946394 946394 obo:OGG_3000946394 b1883 obo:OGG_3000946394 20140406 obo:OGG_3000946394 511145 obo:OGG_3000946394 protein-coding obo:OGG_3000946394 NCBI-supplied obo:OGG_3000946394 GO_0005737; GO_0006464; GO_0042330 obo:OGG_3000946394 PMID: 353036; 1547277; 2644646; 2646634; 2661528; 2677005; 3007436; 3056911; 3076082; 3280143; 3510184; 3539934; 6307970; 7034961; 7045071; 8420965; 9097040; 9209042; 9278503; 10231491; 10464232; 10850799; 10894745; 11243808; 11435446; 11669626; 11742065; 12618449; 15111386; 15175281; 15175286; 15306010; 15375146; 15539117; 15916610; 16030204; 16306993; 16397293; 16446460; 16565056; 16855257; 16924119; 17122336; 17208180; 17609145; 18179279; 18427119; 19156130; 20972792; 21978288 obo:OGG_3000946394 fused chemotaxis regulator: protein-glutamate methylesterase in two-component regulatory system with CheA obo:OGG_3000946394 EcoGene:EG10147 obo:OGG_3000946394 cheB obo:OGG_3000946401 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000946401 ECK1889 obo:OGG_3000946401 JW1877 obo:OGG_3000946401 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000946401 obo:ogg.owl obo:OGG_3000946401 946401 obo:OGG_3000946401 b1888 obo:OGG_3000946401 20140406 obo:OGG_3000946401 511145 obo:OGG_3000946401 protein-coding obo:OGG_3000946401 NCBI-supplied obo:OGG_3000946401 GO_0006464; GO_0042330 obo:OGG_3000946401 PMID: 324984; 370826; 392505; 1326408; 1495964; 1537797; 1624413; 1737035; 1991711; 1992467; 2002011; 2033064; 2068106; 2254280; 2403544; 2558046; 2646634; 2832069; 2847160; 3032955; 3313398; 3510184; 3520334; 4567134; 6213619; 6305515; 6307970; 6374654; 6449010; 6784119; 7577981; 7589525; 7592359; 7592655; 7724572; 7751280; 7929006; 7961989; 8021207; 8415608; 8486661; 8491182; 8524808; 8555213; 8639521; 8663384; 8755897; 8820640; 8820644; 8943256; 9020767; 9097040; 9106209; 9153237; 9278503; 9305977; 9315712; 9437425; 9442881; 9495737; 9636149; 9791174; 9822812; 10029518; 10464232; 10648522; 10676817; 10859356; 10894745; 10972797; 11056533; 11056546; 11092844; 11134926; 11243808; 11923283; 11964403; 12119290; 12644507; 14621982; 14726213; 14741223; 14769919; 15042093; 15090507; 15111386; 15170328; 15175281; 15236585; 15289606; 15306010; 15327941; 15375146; 15451661; 15539117; 15569922; 15572451; 15766267; 15853891; 16030204; 16245946; 16293695; 16306993; 16369945; 16397293; 16621823; 16630631; 16679313; 16707688; 16740938; 16846213; 16856941; 16973743; 17122336; 17360429; 17609125; 17609145; 17628132; 17694049; 17708539; 18711126; 19053273; 19096502; 19256549; 19502407; 19542283; 19580745; 19581362; 19705835; 19768197; 19783813; 21606342; 21636905; 21642453; 21978288; 22355139; 23802570; 24163342 obo:OGG_3000946401 fused chemotactic sensory histidine kinase in two-component regulatory system with CheB and CheY: sensory histidine kinase/signal sensing protein obo:OGG_3000946401 EcoGene:EG10146 obo:OGG_3000946401 cheA obo:OGG_3000946424 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000946424 ECK1913 obo:OGG_3000946424 JW1899 obo:OGG_3000946424 gacA obo:OGG_3000946424 sirA obo:OGG_3000946424 yecB obo:OGG_3000946424 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000946424 obo:ogg.owl obo:OGG_3000946424 946424 obo:OGG_3000946424 b1914 obo:OGG_3000946424 20140406 obo:OGG_3000946424 511145 obo:OGG_3000946424 protein-coding obo:OGG_3000946424 NCBI-supplied obo:OGG_3000946424 GO_0016563 obo:OGG_3000946424 PMID: 3295776; 3515318; 8951818; 9097040; 9278503; 10048039; 11022030; 11244064; 11768529; 12193630; 12533459; 12618449; 12897016; 15130116; 16237014; 16397293; 16529647; 16980446; 17366475; 18792681 obo:OGG_3000946424 DNA-binding response regulator in two-component regulatory system with BarA obo:OGG_3000946424 EcoGene:EG11140 obo:OGG_3000946424 uvrY obo:OGG_3000946486 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000946486 ECK1965 obo:OGG_3000946486 JW5322 obo:OGG_3000946486 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000946486 obo:ogg.owl obo:OGG_3000946486 946486 obo:OGG_3000946486 b1969 obo:OGG_3000946486 20140406 obo:OGG_3000946486 511145 obo:OGG_3000946486 protein-coding obo:OGG_3000946486 NCBI-supplied obo:OGG_3000946486 GO_0016563 obo:OGG_3000946486 PMID: 9097040; 9278503; 10734204; 12618449; 12897016; 12951338; 15522865; 15556475; 15690043; 15773991; 16397293; 18631241 obo:OGG_3000946486 predicted DNA-binding response regulator in two-component system with YedV obo:OGG_3000946486 EcoGene:EG14045 obo:OGG_3000946486 yedW obo:OGG_3000946487 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000946487 ECK1964 obo:OGG_3000946487 JW1951 obo:OGG_3000946487 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000946487 obo:ogg.owl obo:OGG_3000946487 946487 obo:OGG_3000946487 b1968 obo:OGG_3000946487 20140406 obo:OGG_3000946487 511145 obo:OGG_3000946487 protein-coding obo:OGG_3000946487 NCBI-supplied obo:OGG_3000946487 GO_0006464 obo:OGG_3000946487 PMID: 9097040; 9278503; 12897016; 15522865; 15773991; 15919996; 16120447; 16397293 obo:OGG_3000946487 predicted sensory kinase in two-component regulatory system with YedW obo:OGG_3000946487 EcoGene:EG14044 obo:OGG_3000946487 yedV obo:OGG_3000946605 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000946605 ECK2075 obo:OGG_3000946605 JW2064 obo:OGG_3000946605 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000946605 obo:ogg.owl obo:OGG_3000946605 946605 obo:OGG_3000946605 b2079 obo:OGG_3000946605 20140406 obo:OGG_3000946605 511145 obo:OGG_3000946605 protein-coding obo:OGG_3000946605 NCBI-supplied obo:OGG_3000946605 GO_0005737; GO_0016563 obo:OGG_3000946605 PMID: 1482126; 2157156; 7699720; 8098993; 8282725; 9097040; 9278503; 12107133; 12107134; 12354228; 12456787; 12618449; 12897016; 12951338; 15522865; 15686558; 15716448; 16397293; 17884222; 18039828; 18631241; 19091747; 19763168; 21515766 obo:OGG_3000946605 DNA-binding response regulator in two-component regulatory system with BaeS obo:OGG_3000946605 EcoGene:EG11618 obo:OGG_3000946605 baeR obo:OGG_3000946611 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000946611 ECK2074 obo:OGG_3000946611 JW2063 obo:OGG_3000946611 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000946611 obo:ogg.owl obo:OGG_3000946611 946611 obo:OGG_3000946611 b2078 obo:OGG_3000946611 20140406 obo:OGG_3000946611 511145 obo:OGG_3000946611 protein-coding obo:OGG_3000946611 NCBI-supplied obo:OGG_3000946611 GO_0006464; GO_0009274; GO_0019866 obo:OGG_3000946611 PMID: 8282725; 9097040; 9278503; 12107133; 12107134; 12354228; 12456787; 12618449; 12897016; 12951338; 15686558; 15716448; 15919996; 16120447; 16397293; 17884222; 18039828; 19763168; 21515766 obo:OGG_3000946611 sensory histidine kinase in two-component regulatory system with BaeR obo:OGG_3000946611 EcoGene:EG11617 obo:OGG_3000946611 baeS obo:OGG_3000946717 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000946717 ECK2209 obo:OGG_3000946717 JW2204 obo:OGG_3000946717 yojN obo:OGG_3000946717 yojP obo:OGG_3000946717 yojQ obo:OGG_3000946717 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000946717 obo:ogg.owl obo:OGG_3000946717 946717 obo:OGG_3000946717 b2216 obo:OGG_3000946717 20140406 obo:OGG_3000946717 511145 obo:OGG_3000946717 protein-coding obo:OGG_3000946717 NCBI-supplied obo:OGG_3000946717 GO_0006464 obo:OGG_3000946717 PMID: 2404948; 7984428; 9097040; 9278503; 11309126; 11758943; 12410838; 12581159; 12864862; 12897016; 13129944; 14514676; 15375134; 15452440; 15476819; 15901715; 16153174; 16166540; 16397293; 16427772; 16606699; 16607041; 16621809; 17005198; 17185552; 17575454; 17941710; 18192383; 21481780 obo:OGG_3000946717 phosphotransfer intermediate protein in two-component regulatory system with RcsBC obo:OGG_3000946717 EcoGene:EG12385 obo:OGG_3000946717 rcsD obo:OGG_3000946723 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000946723 ECK2376 obo:OGG_3000946723 JW5388 obo:OGG_3000946723 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000946723 obo:ogg.owl obo:OGG_3000946723 946723 obo:OGG_3000946723 b2380 obo:OGG_3000946723 20140406 obo:OGG_3000946723 511145 obo:OGG_3000946723 protein-coding obo:OGG_3000946723 NCBI-supplied obo:OGG_3000946723 PMID: 7966317; 9205837; 9278503; 12897016; 12914674; 15919996; 16120447; 16397293 obo:OGG_3000946723 sensor kinase regulating yhjX; pyruvate-responsive YpdAB two-component system obo:OGG_3000946723 EcoGene:EG14148 obo:OGG_3000946723 ypdA obo:OGG_3000946744 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000946744 ECK0683 obo:OGG_3000946744 JW0683 obo:OGG_3000946744 kac obo:OGG_3000946744 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000946744 obo:ogg.owl obo:OGG_3000946744 946744 obo:OGG_3000946744 b0695 obo:OGG_3000946744 20140406 obo:OGG_3000946744 511145 obo:OGG_3000946744 protein-coding obo:OGG_3000946744 NCBI-supplied obo:OGG_3000946744 GO_0006464; GO_0009274; GO_0019866 obo:OGG_3000946744 PMID: 355227; 1532387; 1532388; 1630316; 1630317; 2995318; 3318698; 3536861; 4908783; 6787588; 7499326; 7715454; 7855422; 8223625; 8276778; 8331081; 8437514; 8798785; 8905232; 9099740; 9139930; 9278503; 9651326; 9675324; 9748442; 9756874; 9858704; 10550471; 10712703; 10747873; 11016946; 11114904; 11123681; 11371546; 11931551; 12115059; 12420175; 12535080; 12694185; 12897016; 14534307; 15555756; 15919996; 16120447; 16397293; 16484207; 16559072; 16887611; 17704218; 17710642; 17985211; 18245296; 18433452; 19101563; 19400808; 19589130; 19850005; 20146748; 20498088; 23651428 obo:OGG_3000946744 fused sensory histidine kinase in two-component regulatory system with KdpE: signal sensing protein obo:OGG_3000946744 EcoGene:EG10516 obo:OGG_3000946744 kdpD obo:OGG_3000946841 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000946841 ECK2365 obo:OGG_3000946841 JW2366 obo:OGG_3000946841 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000946841 obo:ogg.owl obo:OGG_3000946841 946841 obo:OGG_3000946841 b2369 obo:OGG_3000946841 20140406 obo:OGG_3000946841 511145 obo:OGG_3000946841 protein-coding obo:OGG_3000946841 NCBI-supplied obo:OGG_3000946841 GO_0005737; GO_0016563 obo:OGG_3000946841 PMID: 1289796; 8125343; 9278503; 9535079; 10825546; 10923791; 11157960; 11914367; 12135487; 12399493; 12456787; 12618449; 12670992; 12694615; 12897016; 12951338; 14523115; 15126461; 15489450; 16397293; 16428726; 17998538; 18792678; 19352034 obo:OGG_3000946841 DNA-binding response regulator in two-component regulatory system with EvgS obo:OGG_3000946841 EcoGene:EG11609 obo:OGG_3000946841 evgA obo:OGG_3000946844 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000946844 ECK2366 obo:OGG_3000946844 JW2367 obo:OGG_3000946844 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000946844 obo:ogg.owl obo:OGG_3000946844 946844 obo:OGG_3000946844 b2370 obo:OGG_3000946844 20140406 obo:OGG_3000946844 511145 obo:OGG_3000946844 protein-coding obo:OGG_3000946844 NCBI-supplied obo:OGG_3000946844 GO_0006464; GO_0009274; GO_0019866 obo:OGG_3000946844 PMID: 1289796; 8125343; 9278503; 9501520; 9532784; 9535079; 10825546; 10923791; 11157960; 11914367; 12135487; 12399493; 12456787; 12581159; 12618449; 12670992; 12694615; 12897016; 12900028; 14523115; 15126461; 15489450; 16397293; 16606699; 17122336; 17985211; 17998538; 18792678; 19352034 obo:OGG_3000946844 hybrid sensory histidine kinase in two-component regulatory system with EvgA obo:OGG_3000946844 EcoGene:EG11610 obo:OGG_3000946844 evgS obo:OGG_3000946948 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000946948 ECK2464 obo:OGG_3000946948 JW2453 obo:OGG_3000946948 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000946948 obo:ogg.owl obo:OGG_3000946948 946948 obo:OGG_3000946948 b2469 obo:OGG_3000946948 20140406 obo:OGG_3000946948 511145 obo:OGG_3000946948 protein-coding obo:OGG_3000946948 NCBI-supplied obo:OGG_3000946948 GO_0006464; GO_0009061; GO_0009274; GO_0019866 obo:OGG_3000946948 PMID: 1447165; 1508040; 1528845; 8051011; 8501030; 9220011; 9278503; 12546643; 12581159; 12644479; 12897007; 12897016; 14622424; 15919996; 15947133; 16377617; 16397293; 16417496; 18375557; 19968795 obo:OGG_3000946948 sensory histidine kinase in two-component regulatory system with NarP (NarL) obo:OGG_3000946948 EcoGene:EG11460 obo:OGG_3000946948 narQ obo:OGG_3000947008 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000947008 ECK0613 obo:OGG_3000947008 JW0612 obo:OGG_3000947008 citB obo:OGG_3000947008 criR obo:OGG_3000947008 mpdA obo:OGG_3000947008 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000947008 obo:ogg.owl obo:OGG_3000947008 947008 obo:OGG_3000947008 b0620 obo:OGG_3000947008 20140406 obo:OGG_3000947008 511145 obo:OGG_3000947008 protein-coding obo:OGG_3000947008 NCBI-supplied obo:OGG_3000947008 GO_0005737; GO_0016563 obo:OGG_3000947008 PMID: 6997437; 8626281; 8655536; 9079897; 9095416; 9223636; 9278503; 9701802; 11889485; 12167547; 12618449; 12897016; 12951338; 14526013; 15308764; 15361616; 16397293; 16559027; 16934473; 18997424; 19202292; 19426207; 22101843 obo:OGG_3000947008 DNA-binding response regulator in two-component regulatory system with citA obo:OGG_3000947008 EcoGene:EG13544 obo:OGG_3000947008 dpiA obo:OGG_3000947013 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000947013 ECK2553 obo:OGG_3000947013 JW5407 obo:OGG_3000947013 qseE obo:OGG_3000947013 yfhK obo:OGG_3000947013 yfhZ obo:OGG_3000947013 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000947013 obo:ogg.owl obo:OGG_3000947013 947013 obo:OGG_3000947013 b2556 obo:OGG_3000947013 20140406 obo:OGG_3000947013 511145 obo:OGG_3000947013 protein-coding obo:OGG_3000947013 NCBI-supplied obo:OGG_3000947013 GO_0006464 obo:OGG_3000947013 PMID: 9205844; 9278503; 12897016; 15522865; 15919996; 16120447; 16397293; 17220220; 17854828; 19289831; 19843219 obo:OGG_3000947013 sensor protein kinase regulating glmY sRNA in two-component system with response regulator GlrR obo:OGG_3000947013 EcoGene:EG13461 obo:OGG_3000947013 glrK obo:OGG_3000947042 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000947042 ECK2551 obo:OGG_3000947042 JW2538 obo:OGG_3000947042 qseF obo:OGG_3000947042 yfhA obo:OGG_3000947042 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000947042 obo:ogg.owl obo:OGG_3000947042 947042 obo:OGG_3000947042 b2554 obo:OGG_3000947042 20140406 obo:OGG_3000947042 511145 obo:OGG_3000947042 protein-coding obo:OGG_3000947042 NCBI-supplied obo:OGG_3000947042 GO_0006464 obo:OGG_3000947042 PMID: 2034230; 2885322; 8226691; 8412694; 9278503; 10734204; 12618449; 12897016; 15522865; 15556475; 16397293; 17220220; 19289831; 19843219 obo:OGG_3000947042 response regulator regulating glmY sRNA in two-component system with sensor protein GlrK obo:OGG_3000947042 EcoGene:EG11285 obo:OGG_3000947042 glrR obo:OGG_3000947079 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000947079 ECK0528 obo:OGG_3000947079 JW5073 obo:OGG_3000947079 ybcA obo:OGG_3000947079 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000947079 obo:ogg.owl obo:OGG_3000947079 947079 obo:OGG_3000947079 b0535 obo:OGG_3000947079 20140406 obo:OGG_3000947079 511145 obo:OGG_3000947079 protein-coding obo:OGG_3000947079 NCBI-supplied obo:OGG_3000947079 GO_0009289; GO_0016563 obo:OGG_3000947079 PMID: 2183007; 7592479; 9278503; 12618449; 12897016; 12951338; 16397293 obo:OGG_3000947079 predicted DNA-binding transcriptional regulator obo:OGG_3000947079 EcoGene:EG11103 obo:OGG_3000947079 fimZ obo:OGG_3000947174 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000947174 ECK3017 obo:OGG_3000947174 JW2994 obo:OGG_3000947174 preB obo:OGG_3000947174 ygiY obo:OGG_3000947174 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000947174 obo:ogg.owl obo:OGG_3000947174 947174 obo:OGG_3000947174 b3026 obo:OGG_3000947174 20140406 obo:OGG_3000947174 511145 obo:OGG_3000947174 protein-coding obo:OGG_3000947174 NCBI-supplied obo:OGG_3000947174 GO_0006464 obo:OGG_3000947174 PMID: 9278503; 11929534; 12076823; 12847292; 12897016; 15919996; 16120447; 16194231; 16397293; 16803956; 17949301; 19289831; 19703104; 20498088; 20594156 obo:OGG_3000947174 quorum sensing sensory histidine kinase in two-component regulatory system with QseB obo:OGG_3000947174 EcoGene:EG13027 obo:OGG_3000947174 qseC obo:OGG_3000947255 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000947255 ECK2780 obo:OGG_3000947255 JW2757 obo:OGG_3000947255 airS obo:OGG_3000947255 gacC obo:OGG_3000947255 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000947255 obo:ogg.owl obo:OGG_3000947255 947255 obo:OGG_3000947255 b2786 obo:OGG_3000947255 20140406 obo:OGG_3000947255 511145 obo:OGG_3000947255 protein-coding obo:OGG_3000947255 NCBI-supplied obo:OGG_3000947255 GO_0006464; GO_0009274; GO_0019866 obo:OGG_3000947255 PMID: 1574005; 7957084; 9278503; 10931332; 11022030; 11768529; 12193624; 12193630; 12533459; 12581159; 12897016; 14619967; 15522865; 15919996; 16237014; 16397293; 16529647; 16980446; 17122336; 18792681; 20118252 obo:OGG_3000947255 hybrid sensory histidine kinase, in two-component regulatory system with UvrY obo:OGG_3000947255 EcoGene:EG11367 obo:OGG_3000947255 barA obo:OGG_3000947272 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000947272 ECK3391 obo:OGG_3000947272 JW3367 obo:OGG_3000947272 cpr obo:OGG_3000947272 ompB obo:OGG_3000947272 perA obo:OGG_3000947272 tpo obo:OGG_3000947272 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000947272 obo:ogg.owl obo:OGG_3000947272 947272 obo:OGG_3000947272 b3404 obo:OGG_3000947272 20140406 obo:OGG_3000947272 511145 obo:OGG_3000947272 protein-coding obo:OGG_3000947272 NCBI-supplied obo:OGG_3000947272 GO_0006464; GO_0009274; GO_0019866 obo:OGG_3000947272 PMID: 387722; 1311295; 1323560; 1662380; 1700256; 1741624; 1885551; 1901856; 2005134; 2552265; 2558046; 2668953; 2824492; 2845093; 2851704; 2997120; 3157679; 3294816; 3536870; 6292199; 6292200; 6311806; 6337119; 6452446; 6761552; 6799653; 6820310; 6997269; 7021856; 7042694; 7855421; 8106326; 8132603; 9070221; 9188462; 9209057; 9278503; 9409762; 9538242; 9817206; 10192921; 10426948; 10760160; 10884412; 10947842; 11533042; 11973328; 12139613; 12453214; 12453215; 12672798; 12691749; 12754242; 12767831; 12897016; 15175316; 15316026; 15357641; 15522091; 15571621; 15919996; 16077119; 16120447; 16164563; 16397293; 16553882; 16677301; 17426813; 17609131; 17609132; 17635923; 17941710; 18077424; 18193944; 18363324; 18363790; 18438992; 18761686; 19432797; 19445950; 20849081; 20889743; 21854787; 22392928; 22543870; 23333741 obo:OGG_3000947272 sensory histidine kinase in two-component regulatory system with OmpR obo:OGG_3000947272 EcoGene:EG10269 obo:OGG_3000947272 envZ obo:OGG_3000947395 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000947395 ECK2377 obo:OGG_3000947395 JW2378 obo:OGG_3000947395 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000947395 obo:ogg.owl obo:OGG_3000947395 947395 obo:OGG_3000947395 b2381 obo:OGG_3000947395 20140406 obo:OGG_3000947395 511145 obo:OGG_3000947395 protein-coding obo:OGG_3000947395 NCBI-supplied obo:OGG_3000947395 PMID: 9278503; 12618449; 12897016; 16397293; 16606699; 17187058 obo:OGG_3000947395 response regulator activating yhjX; pyruvate-responsive YpdAB two-component system obo:OGG_3000947395 EcoGene:EG14149 obo:OGG_3000947395 ypdB obo:OGG_3000947441 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000947441 ECK2210 obo:OGG_3000947441 JW2205 obo:OGG_3000947441 viaA obo:OGG_3000947441 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000947441 obo:ogg.owl obo:OGG_3000947441 947441 obo:OGG_3000947441 b2217 obo:OGG_3000947441 20140406 obo:OGG_3000947441 511145 obo:OGG_3000947441 protein-coding obo:OGG_3000947441 NCBI-supplied obo:OGG_3000947441 GO_0005737; GO_0009242; GO_0016563; GO_0016564; GO_0042280 obo:OGG_3000947441 PMID: 1482126; 1522067; 1597415; 1943696; 1999391; 2157156; 2404948; 2836365; 3029041; 3888955; 7534408; 7699720; 7855424; 8098993; 8366025; 8576059; 8759878; 8763957; 9097040; 9209051; 9278503; 9364917; 9882673; 10564486; 10702265; 11309126; 11566985; 11758943; 11976318; 12410838; 12581159; 12618449; 12670962; 12864862; 12867437; 12897016; 12951338; 13129944; 14514676; 14766922; 15004283; 15375134; 15476819; 15838058; 15901715; 16000739; 16153174; 16166540; 16397293; 16427772; 16606699; 16607041; 16621809; 16740933; 16776655; 16858726; 17185552; 17187058; 17366475; 17379715; 17468243; 17575454; 17644608; 18192383; 18792681; 19026860; 19136591; 19240136; 19552773; 19806199; 19943899; 20189963; 20435136; 21481780; 21571995; 22295907; 23392250; 23852870 obo:OGG_3000947441 DNA-binding response regulator in two-component regulatory system with RcsC and YojN obo:OGG_3000947441 EcoGene:EG10821 obo:OGG_3000947441 rcsB obo:OGG_3000947444 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000947444 Az obo:OGG_3000947444 ECK2213 obo:OGG_3000947444 JW2214 obo:OGG_3000947444 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000947444 obo:ogg.owl obo:OGG_3000947444 947444 obo:OGG_3000947444 b2220 obo:OGG_3000947444 20140406 obo:OGG_3000947444 511145 obo:OGG_3000947444 protein-coding obo:OGG_3000947444 NCBI-supplied obo:OGG_3000947444 GO_0005737; GO_0006596; GO_0016563; GO_0019395 obo:OGG_3000947444 PMID: 1482126; 2157156; 2883171; 3025185; 3116274; 4563344; 4942769; 7618860; 7699720; 8098993; 8346225; 9097040; 9278503; 9781887; 12618449; 12897016; 15200682; 16153782; 16397293; 16564134; 16819267; 17224065; 17475408; 17537579; 17616594; 18235991; 18855762; 19198978; 20563612; 21295116 obo:OGG_3000947444 fused response regulator of ato operon, in two-component system with AtoS: response regulator/sigma54 interaction protein obo:OGG_3000947444 EcoGene:EG11668 obo:OGG_3000947444 atoC obo:OGG_3000947887 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000947887 ECK3200 obo:OGG_3000947887 JW5536 obo:OGG_3000947887 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000947887 obo:ogg.owl obo:OGG_3000947887 947887 obo:OGG_3000947887 b3210 obo:OGG_3000947887 20140406 obo:OGG_3000947887 511145 obo:OGG_3000947887 protein-coding obo:OGG_3000947887 NCBI-supplied obo:OGG_3000947887 GO_0006464; GO_0009060; GO_0009274; GO_0019866 obo:OGG_3000947887 PMID: 1328158; 1512197; 1592804; 1597416; 1812811; 2070418; 2170337; 2201868; 2565334; 2644240; 2964639; 7855430; 7957084; 8022271; 8071220; 8132465; 8226939; 8412675; 8825099; 8892825; 9054511; 9188789; 9278503; 9286997; 9302022; 9489669; 9632255; 9683496; 9685739; 9761838; 9830034; 9972245; 10531481; 10585483; 10734219; 10770787; 10781568; 10788795; 10851007; 10940038; 10947842; 10998176; 11133990; 11148031; 11286551; 11423658; 11527965; 11782500; 12486057; 12562763; 12576590; 12581159; 12897016; 14711822; 15028693; 15326287; 15669087; 15670209; 15699038; 15838044; 15838055; 15919996; 16140472; 16291649; 16397293; 16709570; 16750836; 17213678; 18223071; 18792681; 18824089; 19593437; 19614590; 19682256; 19715602; 19851741; 19897650; 19933363; 20498088; 23064346; 23331412; 23645604 obo:OGG_3000947887 aerobic respiration control sensor histidine protein kinase, cognate to two-component response regulators ArcA and RssB obo:OGG_3000947887 EcoGene:EG10062 obo:OGG_3000947887 arcB obo:OGG_3000947913 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000947913 ECK3392 obo:OGG_3000947913 JW3368 obo:OGG_3000947913 kmt obo:OGG_3000947913 ompB obo:OGG_3000947913 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000947913 obo:ogg.owl obo:OGG_3000947913 947913 obo:OGG_3000947913 b3405 obo:OGG_3000947913 20140406 obo:OGG_3000947913 511145 obo:OGG_3000947913 protein-coding obo:OGG_3000947913 NCBI-supplied obo:OGG_3000947913 GO_0005737; GO_0009274; GO_0016563; GO_0016564 obo:OGG_3000947913 PMID: 1310090; 1311295; 1321117; 1482126; 1618729; 1657696; 1662380; 1695892; 1700256; 1741624; 1769957; 1885551; 2005134; 2157156; 2552265; 2558046; 2845093; 2997120; 3010044; 3157679; 3294816; 3536870; 6263866; 6281238; 6292199; 6292200; 6799653; 7021856; 7042694; 7565603; 7568033; 7642497; 7699720; 7855421; 8098993; 8876642; 8989318; 9016718; 9188462; 9278503; 9422609; 9484896; 9573197; 10192921; 10498711; 10653699; 10760160; 10802181; 10947842; 11717281; 11812125; 11952900; 11973328; 12077136; 12453214; 12453215; 12618449; 12818201; 12897016; 12951338; 15004283; 15175316; 15357641; 15571621; 15713883; 15743943; 15743952; 15979641; 16000739; 16385048; 16397293; 16553882; 16606699; 16618701; 16855227; 17122336; 17416652; 17426813; 17628138; 17941710; 18077424; 18193944; 18195018; 18223071; 18363790; 18438992; 18761686; 18953042; 19383700; 19432797; 19445950; 19502392; 19542330; 19552773; 20889743; 21131484; 21179024; 23175504 obo:OGG_3000947913 DNA-binding response regulator in two-component regulatory system with EnvZ obo:OGG_3000947913 EcoGene:EG10672 obo:OGG_3000947913 ompR obo:OGG_3000948178 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000948178 ECK3660 obo:OGG_3000948178 JW3644 obo:OGG_3000948178 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000948178 obo:ogg.owl obo:OGG_3000948178 948178 obo:OGG_3000948178 b3669 obo:OGG_3000948178 20140406 obo:OGG_3000948178 511145 obo:OGG_3000948178 protein-coding obo:OGG_3000948178 NCBI-supplied obo:OGG_3000948178 GO_0005737; GO_0016052; GO_0016563 obo:OGG_3000948178 PMID: 1482126; 1569007; 1569008; 2157156; 3038843; 3042748; 3301805; 6309737; 6350260; 7596290; 7686882; 7699720; 8098993; 8144492; 8999880; 9220010; 9278503; 10512697; 10572130; 10913075; 10966457; 11053370; 11325944; 11739766; 11782500; 11976297; 12107138; 12618449; 12897016; 12936984; 16397293; 16606699; 17463081 obo:OGG_3000948178 DNA-binding response regulator in two-component regulatory system wtih UhpB obo:OGG_3000948178 EcoGene:EG11051 obo:OGG_3000948178 uhpA obo:OGG_3000948195 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000948195 ECK3659 obo:OGG_3000948195 JW3643 obo:OGG_3000948195 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000948195 obo:ogg.owl obo:OGG_3000948195 948195 obo:OGG_3000948195 b3668 obo:OGG_3000948195 20140406 obo:OGG_3000948195 511145 obo:OGG_3000948195 protein-coding obo:OGG_3000948195 NCBI-supplied obo:OGG_3000948195 GO_0006464; GO_0009274; GO_0016052; GO_0019866 obo:OGG_3000948195 PMID: 1569007; 1569008; 3038843; 3042748; 3301805; 7596290; 7686882; 8144492; 8349544; 9278503; 11053370; 11325944; 11739766; 12107138; 12876315; 12897016; 12914674; 15174130; 15919996; 16397293; 17463081 obo:OGG_3000948195 sensory histidine kinase in two-component regulatory sytem with UhpA obo:OGG_3000948195 EcoGene:EG11052 obo:OGG_3000948195 uhpB obo:OGG_3000948360 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000948360 ECK3862 obo:OGG_3000948360 JW3840 obo:OGG_3000948360 glnR obo:OGG_3000948360 ntrB obo:OGG_3000948360 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000948360 obo:ogg.owl obo:OGG_3000948360 948360 obo:OGG_3000948360 b3869 obo:OGG_3000948360 20140406 obo:OGG_3000948360 511145 obo:OGG_3000948360 protein-coding obo:OGG_3000948360 NCBI-supplied obo:OGG_3000948360 GO_0006464; GO_0006542; GO_0009274; GO_0019866 obo:OGG_3000948360 PMID: 1352516; 2016302; 2574599; 2839825; 2858855; 2865194; 2874557; 2882477; 2904147; 3027504; 3536843; 6113591; 6115384; 6120929; 6120930; 6122676; 6130464; 6131062; 6148334; 7901195; 7961767; 8226644; 8346018; 9278503; 9737856; 9737857; 9892680; 10074086; 10231487; 10819971; 11063580; 11063581; 11782500; 11931552; 12057972; 12366843; 12368244; 12562801; 12627170; 12730324; 12838411; 12873150; 12897016; 15150219; 15157101; 15208307; 15289551; 15317778; 15357304; 16397293; 16945478; 17628156; 19877669; 19877670; 23088566 obo:OGG_3000948360 sensory histidine kinase in two-component regulatory system with GlnG obo:OGG_3000948360 EcoGene:EG10387 obo:OGG_3000948360 glnL obo:OGG_3000948361 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000948361 ECK3861 obo:OGG_3000948361 JW3839 obo:OGG_3000948361 glnT obo:OGG_3000948361 ntrC obo:OGG_3000948361 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000948361 obo:ogg.owl obo:OGG_3000948361 948361 obo:OGG_3000948361 b3868 obo:OGG_3000948361 20140406 obo:OGG_3000948361 511145 obo:OGG_3000948361 protein-coding obo:OGG_3000948361 NCBI-supplied obo:OGG_3000948361 GO_0005737; GO_0006542; GO_0016563; GO_0016564 obo:OGG_3000948361 PMID: 41243; 1321122; 1350679; 1356964; 2574599; 2848245; 2858855; 2871943; 2882477; 2904147; 6111550; 6113591; 6115384; 6120929; 6122676; 6130464; 6131062; 6148334; 7961766; 8094391; 8346018; 8407777; 9278503; 9696779; 9720863; 9737855; 9737857; 10074086; 10779705; 10891265; 10960104; 11063581; 11121068; 11528004; 11782500; 12180911; 12366843; 12617754; 12618449; 12730324; 12897016; 14561776; 14563853; 15208307; 15317778; 15327947; 15659685; 16397293; 16531068; 16553838; 16751184; 16945478; 17284458; 17628156; 18631241; 19576227; 19877669; 19877670 obo:OGG_3000948361 fused DNA-binding response regulator in two-component regulatory system with GlnL: response regulator/sigma54 interaction protein obo:OGG_3000948361 EcoGene:EG10385 obo:OGG_3000948361 glnG obo:OGG_3000948404 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000948404 ECK3905 obo:OGG_3000948404 JW3883 obo:OGG_3000948404 yiiA obo:OGG_3000948404 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000948404 obo:ogg.owl obo:OGG_3000948404 948404 obo:OGG_3000948404 b3912 obo:OGG_3000948404 20140406 obo:OGG_3000948404 511145 obo:OGG_3000948404 protein-coding obo:OGG_3000948404 NCBI-supplied obo:OGG_3000948404 GO_0005737; GO_0006805; GO_0016563 obo:OGG_3000948404 PMID: 1482126; 2157156; 3058985; 7699720; 7883164; 8098993; 8294007; 8346018; 8748033; 9159398; 9159399; 9278503; 9401031; 10464196; 10483736; 10542180; 10671468; 10708362; 10972835; 11514504; 11717281; 11830644; 12081643; 12354228; 12368244; 12618449; 12627170; 12670966; 12897016; 12951338; 15205435; 15576781; 15629938; 15686558; 15690043; 15743943; 15743952; 15773991; 15852340; 16077119; 16397293; 16436431; 16487683; 16861804; 17142356; 17259177; 17307737; 18069965; 18223085; 18227171; 18631241; 18761686; 19091747; 19103922; 19432797; 19445950; 19596441; 19601955; 19763168; 19893610; 24163343 obo:OGG_3000948404 DNA-binding response regulator in two-component regulatory system with CpxA obo:OGG_3000948404 EcoGene:EG10020 obo:OGG_3000948404 cpxR obo:OGG_3000948405 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000948405 ECK3904 obo:OGG_3000948405 JW3882 obo:OGG_3000948405 ecfB obo:OGG_3000948405 eup obo:OGG_3000948405 rssE obo:OGG_3000948405 ssd obo:OGG_3000948405 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000948405 obo:ogg.owl obo:OGG_3000948405 948405 obo:OGG_3000948405 b3911 obo:OGG_3000948405 20140406 obo:OGG_3000948405 511145 obo:OGG_3000948405 protein-coding obo:OGG_3000948405 NCBI-supplied obo:OGG_3000948405 GO_0006464; GO_0006805; GO_0009274; GO_0019866 obo:OGG_3000948405 PMID: 353502; 2185221; 2565334; 3007473; 3058985; 3539185; 3894006; 6097795; 6097796; 6102380; 6106014; 6802799; 6997275; 6998969; 7037752; 7883164; 8294007; 8346018; 8432716; 8748033; 9023180; 9159398; 9159399; 9278503; 9401031; 9642209; 10464196; 10483736; 10542180; 10671468; 10708362; 10966457; 10972835; 12081643; 12670966; 12897007; 12897016; 15205435; 15522865; 15576781; 15629938; 15773991; 15919996; 16077119; 16120447; 16397293; 16487683; 16861804; 17122336; 17142356; 17259177; 17985211; 18069965; 18223085; 18227171; 18761686; 18824089; 19013277; 19103922; 19432797; 19445950; 19596441; 19601955; 19763168; 21179024; 21349329; 24163343 obo:OGG_3000948405 sensory histidine kinase in two-component regulatory system with CpxR obo:OGG_3000948405 EcoGene:EG10163 obo:OGG_3000948405 cpxA obo:OGG_3000948505 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000948505 ECK3996 obo:OGG_3000948505 JW3968 obo:OGG_3000948505 hydG obo:OGG_3000948505 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000948505 obo:ogg.owl obo:OGG_3000948505 948505 obo:OGG_3000948505 b4004 obo:OGG_3000948505 20140406 obo:OGG_3000948505 511145 obo:OGG_3000948505 protein-coding obo:OGG_3000948505 NCBI-supplied obo:OGG_3000948505 GO_0005737; GO_0006113; GO_0016563 obo:OGG_3000948505 PMID: 1482126; 2045358; 2157156; 2666400; 7699720; 8098993; 8265357; 9278503; 11243806; 12618449; 12897016; 15522865; 15659689; 16397293; 16531068; 17372774; 23049878 obo:OGG_3000948505 fused DNA-binding response regulator in two-component regulatory system with ZraS: response regulator/sigma54 interaction protein obo:OGG_3000948505 EcoGene:EG10482 obo:OGG_3000948505 zraR obo:OGG_3000948506 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000948506 ECK3995 obo:OGG_3000948506 JW3967 obo:OGG_3000948506 hydH obo:OGG_3000948506 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000948506 obo:ogg.owl obo:OGG_3000948506 948506 obo:OGG_3000948506 b4003 obo:OGG_3000948506 20140406 obo:OGG_3000948506 511145 obo:OGG_3000948506 protein-coding obo:OGG_3000948506 NCBI-supplied obo:OGG_3000948506 GO_0006113; GO_0006464; GO_0009274; GO_0019866 obo:OGG_3000948506 PMID: 2666400; 8265357; 9278503; 11243806; 12897016; 15522865; 15919996; 16120447; 16397293; 17985211 obo:OGG_3000948506 sensory histidine kinase in two-component regulatory system with ZraR obo:OGG_3000948506 EcoGene:EG10008 obo:OGG_3000948506 zraS obo:OGG_3000948609 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000948609 ECK4391 obo:OGG_3000948609 JW4362 obo:OGG_3000948609 phoM obo:OGG_3000948609 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000948609 obo:ogg.owl obo:OGG_3000948609 948609 obo:OGG_3000948609 b4399 obo:OGG_3000948609 20140406 obo:OGG_3000948609 511145 obo:OGG_3000948609 protein-coding obo:OGG_3000948609 NCBI-supplied obo:OGG_3000948609 GO_0006464; GO_0009274; GO_0019866 obo:OGG_3000948609 PMID: 1551826; 2228961; 2411941; 2835585; 3275616; 3531171; 3542979; 6092847; 6277871; 6330029; 6381964; 7021308; 7610040; 8432742; 9278503; 11350954; 12429059; 12897016; 15522865; 15919996; 16120447; 16397293; 16818608; 18031348; 18223071; 18326580; 18375564 obo:OGG_3000948609 sensory histidine kinase in two-component regulatory system with CreB or PhoB, regulator of the CreBC regulon obo:OGG_3000948609 EcoGene:EG10730 obo:OGG_3000948609 creC obo:OGG_3000948631 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000948631 ECK4106 obo:OGG_3000948631 JW4074 obo:OGG_3000948631 pmrA obo:OGG_3000948631 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000948631 obo:ogg.owl obo:OGG_3000948631 948631 obo:OGG_3000948631 b4113 obo:OGG_3000948631 20140406 obo:OGG_3000948631 511145 obo:OGG_3000948631 protein-coding obo:OGG_3000948631 NCBI-supplied obo:OGG_3000948631 GO_0005737; GO_0016563 obo:OGG_3000948631 PMID: 1482126; 2157156; 7565089; 7610040; 7699720; 8098993; 8282725; 8391535; 8524935; 9278503; 9371451; 10373459; 10775270; 11222580; 11535605; 12139617; 12399493; 12618449; 12676988; 12897016; 15322361; 15522865; 15556475; 15569938; 15659161; 15659689; 16397293; 16428424; 17686460; 18631241; 20384697; 22442305; 24062463 obo:OGG_3000948631 DNA-binding response regulator in two-component regulatory system with BasS obo:OGG_3000948631 EcoGene:EG11615 obo:OGG_3000948631 basR obo:OGG_3000948632 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000948632 ECK4105 obo:OGG_3000948632 JW4073 obo:OGG_3000948632 pmrB obo:OGG_3000948632 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000948632 obo:ogg.owl obo:OGG_3000948632 948632 obo:OGG_3000948632 b4112 obo:OGG_3000948632 20140406 obo:OGG_3000948632 511145 obo:OGG_3000948632 protein-coding obo:OGG_3000948632 NCBI-supplied obo:OGG_3000948632 GO_0006464; GO_0009274; GO_0019866 obo:OGG_3000948632 PMID: 7610040; 8282725; 9278503; 10775270; 12676988; 12897016; 15322361; 15522865; 15659689; 15919996; 16120447; 16397293; 17985211; 22442305 obo:OGG_3000948632 sensory histidine kinase in two-component regulatory system with BasR obo:OGG_3000948632 EcoGene:EG11614 obo:OGG_3000948632 basS obo:OGG_3000948639 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000948639 ECK4118 obo:OGG_3000948639 JW4086 obo:OGG_3000948639 yjdH obo:OGG_3000948639 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000948639 obo:ogg.owl obo:OGG_3000948639 948639 obo:OGG_3000948639 b4125 obo:OGG_3000948639 20140406 obo:OGG_3000948639 511145 obo:OGG_3000948639 protein-coding obo:OGG_3000948639 NCBI-supplied obo:OGG_3000948639 GO_0006464; GO_0009061; GO_0009274 obo:OGG_3000948639 PMID: 7610040; 9278503; 9765574; 9973351; 11803016; 12167640; 12754220; 12897016; 12907689; 14996819; 15781452; 15862241; 15919996; 15995204; 16120447; 16397293; 16606699; 17416661; 17618229; 18667579; 18701447; 18820688; 18957436; 19661178; 19789137; 20453099; 22101843; 22780562 obo:OGG_3000948639 sensory histidine kinase in two-component regulatory system with DcuR, regulator of anaerobic fumarate respiration obo:OGG_3000948639 EcoGene:EG12465 obo:OGG_3000948639 dcuS obo:OGG_3000948640 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000948640 ECK4117 obo:OGG_3000948640 JW4085 obo:OGG_3000948640 yjdG obo:OGG_3000948640 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000948640 obo:ogg.owl obo:OGG_3000948640 948640 obo:OGG_3000948640 b4124 obo:OGG_3000948640 20140406 obo:OGG_3000948640 511145 obo:OGG_3000948640 protein-coding obo:OGG_3000948640 NCBI-supplied obo:OGG_3000948640 GO_0005737; GO_0009061 obo:OGG_3000948640 PMID: 7610040; 9278503; 9624689; 9765574; 9973351; 12167640; 12618449; 12754220; 12897016; 12951338; 14996819; 15073297; 15995204; 16397293; 17618229; 22101843 obo:OGG_3000948640 DNA-binding response regulator in two-component regulatory system with DcuS obo:OGG_3000948640 EcoGene:EG12464 obo:OGG_3000948640 dcuR obo:OGG_3000948778 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000948778 ECK4237 obo:OGG_3000948778 JW4201 obo:OGG_3000948778 corB obo:OGG_3000948778 mgt obo:OGG_3000948778 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000948778 obo:ogg.owl obo:OGG_3000948778 948778 obo:OGG_3000948778 b4242 obo:OGG_3000948778 20140406 obo:OGG_3000948778 511145 obo:OGG_3000948778 protein-coding obo:OGG_3000948778 NCBI-supplied obo:OGG_3000948778 GO_0009274; GO_0015662; GO_0015986; GO_0019866 obo:OGG_3000948778 PMID: 780341; 2670893; 4992523; 7610040; 9278503; 9622348; 10464230; 12123454; 12813061; 15126461; 15748988; 15919996; 15947133; 16041131; 16397293; 16606699; 16615891; 16990279; 17381304; 17543954; 17909183; 18248433; 19702577; 19923713 obo:OGG_3000948778 magnesium transporter obo:OGG_3000948778 EcoGene:EG12525 obo:OGG_3000948778 mgtA obo:OGG_3000948870 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000948870 ECK1604 obo:OGG_3000948870 JW1601 obo:OGG_3000948870 uspT obo:OGG_3000948870 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000948870 obo:ogg.owl obo:OGG_3000948870 948870 obo:OGG_3000948870 b1609 obo:OGG_3000948870 20140406 obo:OGG_3000948870 511145 obo:OGG_3000948870 protein-coding obo:OGG_3000948870 NCBI-supplied obo:OGG_3000948870 GO_0006464; GO_0009274; GO_0019866 obo:OGG_3000948870 PMID: 1495392; 1925016; 2646639; 9097039; 9205844; 9278503; 12813061; 12897016; 15126461; 15322361; 15522865; 15919996; 16120447; 16397293; 17985211; 21854787 obo:OGG_3000948870 sensory histidine kinase in two-component regulatory system with RstA obo:OGG_3000948870 EcoGene:EG11233 obo:OGG_3000948870 rstB obo:OGG_3000948874 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000948874 ECK4393 obo:OGG_3000948874 JW4364 obo:OGG_3000948874 cpxC obo:OGG_3000948874 dye obo:OGG_3000948874 fexA obo:OGG_3000948874 msp obo:OGG_3000948874 seg obo:OGG_3000948874 sfrA obo:OGG_3000948874 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000948874 obo:ogg.owl obo:OGG_3000948874 948874 obo:OGG_3000948874 b4401 obo:OGG_3000948874 20140406 obo:OGG_3000948874 511145 obo:OGG_3000948874 protein-coding obo:OGG_3000948874 NCBI-supplied obo:OGG_3000948874 GO_0005737; GO_0016563; GO_0016564 obo:OGG_3000948874 PMID: 1315704; 1328158; 1482126; 1512197; 1565612; 1592804; 1812811; 1851949; 1885542; 2041478; 2157156; 2170337; 2565334; 2964639; 2984198; 6304010; 6328216; 7007352; 7565118; 7610040; 7699720; 7855430; 8022271; 8098993; 8132465; 8226939; 8412671; 8550494; 8825099; 8892825; 9278503; 9286997; 9298646; 9302022; 9632255; 9683496; 9830034; 9868788; 9880556; 10071223; 10216875; 10585483; 10794600; 10851007; 10940038; 10947842; 10998176; 11092847; 11123679; 11133990; 11527965; 11782500; 11932447; 12368244; 12486057; 12581159; 12596232; 12618449; 12627170; 12897016; 14711822; 15252051; 15326287; 15669087; 15699038; 15728117; 15838044; 15852340; 15876365; 16140031; 16140472; 16291649; 16397293; 16606699; 16630255; 16709570; 16750836; 16849788; 16849790; 16962353; 17013945; 17187058; 17213678; 17307737; 17313674; 17360572; 18223071; 18326580; 18349549; 18349550; 18402772; 18631241; 18824089; 19013277; 19091747; 19536200; 19561129; 19614590; 19682256; 19715602; 19851741; 19887109; 19897650; 19933363; 20622065; 21252224; 21464517; 21481254; 22009573; 23065979; 23331412; 24146625 obo:OGG_3000948874 DNA-binding response regulator in two-component regulatory system with ArcB or CpxA obo:OGG_3000948874 EcoGene:EG10061 obo:OGG_3000948874 arcA obo:OGG_3000948922 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000948922 ECK4390 obo:OGG_3000948922 JW4361 obo:OGG_3000948922 ORF2 obo:OGG_3000948922 yjjE obo:OGG_3000948922 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000948922 obo:ogg.owl obo:OGG_3000948922 948922 obo:OGG_3000948922 b4398 obo:OGG_3000948922 20140406 obo:OGG_3000948922 511145 obo:OGG_3000948922 protein-coding obo:OGG_3000948922 NCBI-supplied obo:OGG_3000948922 GO_0005737; GO_0016563 obo:OGG_3000948922 PMID: 1482126; 1551826; 2157156; 2228961; 3531171; 7610040; 7699720; 7855419; 8098993; 9278503; 12429059; 12618449; 12897016; 12951338; 15522865; 16397293; 16818608; 18223071; 18375564; 18631241; 19561129 obo:OGG_3000948922 DNA-binding response regulator in two-component regulatory system with CreC obo:OGG_3000948922 EcoGene:EG11218 obo:OGG_3000948922 creB obo:OGG_3000948993 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000948993 ECK2211 obo:OGG_3000948993 JW5917 obo:OGG_3000948993 JW5920 obo:OGG_3000948993 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000948993 obo:ogg.owl obo:OGG_3000948993 948993 obo:OGG_3000948993 b2218 obo:OGG_3000948993 20140406 obo:OGG_3000948993 511145 obo:OGG_3000948993 protein-coding obo:OGG_3000948993 NCBI-supplied obo:OGG_3000948993 GO_0006464; GO_0009242; GO_0009274; GO_0019866; GO_0042280 obo:OGG_3000948993 PMID: 1447156; 2404948; 2836365; 3029041; 3888955; 8366025; 8576059; 8990283; 9278503; 9352941; 9364917; 10564486; 11309126; 11566985; 11758943; 11807084; 11976318; 12410838; 12581159; 12864862; 12897016; 13129944; 14514676; 14651646; 15375134; 15476819; 15901715; 15919996; 16153174; 16166540; 16397293; 16427772; 16607041; 16621809; 16740933; 16776655; 16816180; 17005198; 17036162; 17122336; 17185552; 17575454; 17941710; 18192383; 18792681; 19026860; 19260968; 19552773; 19696107 obo:OGG_3000948993 hybrid sensory kinase in two-component regulatory system with RcsB and YojN obo:OGG_3000948993 EcoGene:EG10822 obo:OGG_3000948993 rcsC obo:OGG_3000949011 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000949011 ECK2212 obo:OGG_3000949011 JW2213 obo:OGG_3000949011 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000949011 obo:ogg.owl obo:OGG_3000949011 949011 obo:OGG_3000949011 b2219 obo:OGG_3000949011 20140406 obo:OGG_3000949011 511145 obo:OGG_3000949011 protein-coding obo:OGG_3000949011 NCBI-supplied obo:OGG_3000949011 GO_0006464; GO_0009274; GO_0019395; GO_0019866 obo:OGG_3000949011 PMID: 2883171; 8346225; 9097040; 9278503; 12897016; 14592990; 15200682; 15919996; 16120447; 16153782; 16397293; 16564134; 17122336; 17224065; 17475408; 17537579; 18235991; 18534200; 18855762; 19198978; 20563612; 21295116 obo:OGG_3000949011 sensory histidine kinase in two-component regulatory system with AtoC obo:OGG_3000949011 EcoGene:EG11667 obo:OGG_3000949011 atoS obo:OGG_3000949024 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000949024 ECK2117 obo:OGG_3000949024 JW5352 obo:OGG_3000949024 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000949024 obo:ogg.owl obo:OGG_3000949024 949024 obo:OGG_3000949024 b2125 obo:OGG_3000949024 20140406 obo:OGG_3000949024 511145 obo:OGG_3000949024 protein-coding obo:OGG_3000949024 NCBI-supplied obo:OGG_3000949024 PMID: 9278503; 12618449; 12897016; 12951338; 16397293; 22685278 obo:OGG_3000949024 predicted response regulator in two-component system withYehU obo:OGG_3000949024 EcoGene:EG12006 obo:OGG_3000949024 yehT obo:OGG_3000949027 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000949027 ECK2118 obo:OGG_3000949027 JW5353 obo:OGG_3000949027 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000949027 obo:ogg.owl obo:OGG_3000949027 949027 obo:OGG_3000949027 b2126 obo:OGG_3000949027 20140406 obo:OGG_3000949027 511145 obo:OGG_3000949027 protein-coding obo:OGG_3000949027 NCBI-supplied obo:OGG_3000949027 GO_0006464 obo:OGG_3000949027 PMID: 9278503; 12897016; 12914674; 15919996; 16120447; 16397293; 22685278 obo:OGG_3000949027 predicted sensory kinase in two-component system with YehT, inner membrane protein obo:OGG_3000949027 EcoGene:EG12007 obo:OGG_3000949027 yehU obo:OGG_3000949081 Bin Zhao, Yue Liu, Oliver He obo:OGG_3000949081 ECK2185 obo:OGG_3000949081 JW2181 obo:OGG_3000949081 WEB: http://www.ncbi.nlm.nih.gov/gene obo:OGG_3000949081 obo:ogg.owl obo:OGG_3000949081 949081 obo:OGG_3000949081 b2193 obo:OGG_3000949081 20140406 obo:OGG_3000949081 511145 obo:OGG_3000949081 protein-coding obo:OGG_3000949081 NCBI-supplied obo:OGG_3000949081 GO_0005737; GO_0009061; GO_0016563; GO_0016564 obo:OGG_3000949081 PMID: 1482126; 2157156; 7699720; 8098993; 8412692; 8501030; 9278503; 9302020; 12581159; 12618449; 12644479; 12897016; 12923080; 15728117; 15978080; 16199562; 16377617; 16397293; 16417496; 16818608; 16936015; 17313674; 17720788; 17965164; 18227264; 19968795; 20634237 obo:OGG_3000949081 DNA-binding response regulator in two-component regulatory system with NarQ or NarX obo:OGG_3000949081 EcoGene:EG11527 obo:OGG_3000949081 narP obo:OTCS_0000001 The two-component regulatory system (TCS) serves as a basic stimulus-response coupling mechanism to allow organisms to sense and respond to changes in many different environmental conditions. In addition, the prototypical TCS consists of a sensor kinase that responds to specific stimulus by modifying the phosphorylated state of a cognate response regulator. obo:OTCS_0000001 Oliver He, Ming Liu, Hsin-Hui Huang obo:OTCS_0000001 WEB: https://en.wikipedia.org/wiki/Two-component_regulatory_system WEB: https://www.ncbi.nih.gov/pmc/articles/PMC2751022/ obo:OTCS_0000001 two-component regulatory system obo:OTCS_0000002 The PhoRB TCS consists of PhoB classical type sensor kinase and PhoR response regulator. Phosphate homeostasis is controlled by the PhoBR TCS. The phosphorylated PhoR induce the pho regulon expression such as genes involved in phosphate uptake, phosphate storage, and phosphate-obtaining enzymes. obo:OTCS_0000002 Oliver He, Hsin-Hui Huang obo:OTCS_0000002 PhoRB two-component regulatory system of Escherichia coli K-12 obo:OTCS_0000002 WEB: https://www.ncbi.nlm.nih.gov/pubmed/23154290 obo:OTCS_0000002 PhoRB two-component regulatory system obo:OTCS_0000003 The cell envelope comprises the inner (cytoplasmic) membrane and the cell wall (peptidoglycan layer) of a bacterium. In Gram negative bacteria an outer membrane is also included. The antibiotics targeting on cell envelope may influence cell morphology and further cause cell lysis. The beta-lactams and glycopeptides are mainly affect the synthesis of peptidoglycan. On the other hand, the bactericidal mechanism of polymyxin is to disrupt the outer and inner membrane. obo:OTCS_0000003 Oliver He, Hsin-Hui Huang obo:OTCS_0000003 WEB: https://en.wikipedia.org/wiki/Cell_envelope WEB: https://en.wikiepdie.org/wiki/Polymyxin WEB: https://www.ncbi.nlm.nih.gov/pubmed/29109626 obo:OTCS_0000003 antibiotic targeting on cell envelope obo:OTCS_0000004 A two-component regulatory system of bacteria, including Gram positive and negative bacteria. obo:OTCS_0000004 Oliver He, Ming Liu, Hsin-Hui Huang obo:OTCS_0000004 bacterial two-component regulatory system obo:OTCS_0000005 A bacterial histidine phosphotransferase gene role means the gene is able to encode the histidine phosphotransferase protein obo:OTCS_0000005 Oliver He, Hsin-Hui Huang obo:OTCS_0000005 bacterial histidine phosphotransferase gene role obo:OTCS_0000006 a gene that encodes for a bacterial histidine phosphotransferase protein obo:OTCS_0000006 Oliver He, Ming Liu, Hsin-Hui Huang obo:OTCS_0000006 bacterial histidine phosphotransferase gene obo:OTCS_0000007 The CusSR TCS consist of CusS classical type sensor kinase and CusR response regulator. The CusSR which activated expression of the cusCFBA, encoding a tripartite transporter that functions in copper and silver extrusion, in response to elevated copper and silver concentrations. obo:OTCS_0000007 Oliver He, Hsin-Hui Huang obo:OTCS_0000007 CusSR two-component regulatory system of Escherichia coli K-12 obo:OTCS_0000007 WEB: https://www.ncbi.nlm.nih.gov/pubmed/11004187 WEB: https://www.ncbi.nlm.nih.gov/pubmed/11283292 obo:OTCS_0000007 CusSR two-component regulatory system obo:OTCS_0000008 In the classical form, the sensor kinase only contain a input domain and a transmitter domain (H1 domain). The input domain and transmitter domain usually located at the N-terminal and C-terminal of the sensor kinase, respectively. obo:OTCS_0000008 Oliver He, Ming Liu, Hsin-Hui Huang obo:OTCS_0000008 WEB: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6335343/ obo:OTCS_0000008 bacterial classical sensor kinase protein obo:OTCS_0000010 The chemical concentration is the abundance of a constituent divided by the total volume of a chemical substance. A chemical substance is a form of matter having constant chemical composition and characteristic properties. obo:OTCS_0000010 Oliver He, Hsin-Hui Huang obo:OTCS_0000010 WEB: https://en.wikipedia.org/wiki/Chemical_substance WEB: https://en.wikipedia.org/wiki/Concentration obo:OTCS_0000010 chemical concentration obo:OTCS_0000012 a gene that encodes for bacterial protein obo:OTCS_0000012 Oliver He, Ming Liu, Hsin-Hui Huang obo:OTCS_0000012 bacterial protein-encoding gene obo:OTCS_0000013 Oliver He, Ming Liu, Hsin-Hui Huang obo:OTCS_0000013 a gene that encodes for bacterial sensor kinase protein, including classical, hybrid , and unothodox type sensor kinase protein obo:OTCS_0000013 bacterial sensor kinase gene obo:OTCS_0000014 The PhoPQ TCS consists of PhoQ classical type sensor kinase and PhoP response regulator. In E. coli, the PhoPQ TCS play key role in response to magnesium limitation and antimicrobial peptides resistance. obo:OTCS_0000014 Oliver He, Hsin-Hui Huang obo:OTCS_0000014 PhoPQ two-component regulatory system of Escherichia coli K-12 obo:OTCS_0000014 WEB: https://www.ncbi.nlm.nih.gov/pubmed/11222580 WEB: https://www.ncbi.nlm.nih.gov/pubmed/10464230 obo:OTCS_0000014 PhoPQ two-component regulatory system obo:OTCS_0000015 A bacterial sensor kinase gene role means the gene is able to encode the bacterial sensor kinase protein. obo:OTCS_0000015 Oliver He, Hsin-Hui Huang obo:OTCS_0000015 bacterial sensor kinase gene role obo:OTCS_0000016 A bacterial response regulator gene role means the gene is able to encode bacterial response regulator protein. obo:OTCS_0000016 Oliver He, Hsin-Hui Huang obo:OTCS_0000016 bacterial response regulator gene role obo:OTCS_0000017 In the unorthodox form, the transmitter domain (H1 domain) is followed by an additional consered aspartic residue (D1) and a transmitter domain (H2 domain) in the C-terminal of sensor kinase. Besides, a conserved aspartic residue is referred to the receiver (D2) domain in the response regulator. The phosphoryl group can be transferred by H1-D1-H2-D2, which is a four step phosphorelay mechanism. obo:OTCS_0000017 Oliver He, Ming Liu, Hsin-Hui Huang obo:OTCS_0000017 WEB: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6335343/ obo:OTCS_0000017 bacterial unorthodox sensor kinase protein obo:OTCS_0000018 a relation between the two-component regulatory system and the organism where this two-component regulatory system belong to this organism in nature. It does not include a foreign two-component regulatory system that is transferred to an organism from by a genetic engineering method. obo:OTCS_0000018 Oliver He, Meng Liu, Hsin-Hui Huang obo:OTCS_0000018 is two-component regulatory system of organism obo:OTCS_0000019 The two-component regulatory system of Escherichia coli K-12. On the basis of E. coli K-12 genome sequence, a total of 28 TCSs have been reported. Among 28 TCSs, 23 TCSs are classical TCSs and the remaining 5 TCSs are unorthodox TCSs. obo:OTCS_0000019 Oliver He, Ming Liu, Hsin-Hui Huang obo:OTCS_0000019 TCS of Escherichia coli K-12 obo:OTCS_0000019 two-component regulatory system of Escherichia coli K-12 obo:OTCS_0000022 In the hybrid form, the sensor kinase contains a input domain, transmitter domain (H1), and followed by an additional conserved aspartic residue D1 domain. The difference between hybrid and unorthodox sensor kinase is that the H2 domain of the hybrid version is an external phosphotransfer module that acts as an individual protein. obo:OTCS_0000022 Oliver He, Ming Liu, Hsin-Hui Huang obo:OTCS_0000022 WEB: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6335343/ obo:OTCS_0000022 bacterial hybrid sensor kinase protein obo:OTCS_0000023 The bacterial classical sensor kinase role is the role of protein, consisting of a sensor and a transmitter domain, has ability to sense signal and trigger activation by autophosphorylation. Then, the phosphryl group can be transferred to cognate response regulator. obo:OTCS_0000023 Oliver He, Hsin-Hui Huang obo:OTCS_0000023 WEB: https://www.ncbi.nlm.nih.gov/pubmed/30687268 obo:OTCS_0000023 bacterial classical sensor kinase role obo:OTCS_0000024 A bacterial hybrid sensor kinase role is a role of protein, consisting of a sensor, a transmitter, and a receiver domain, also has ability to sense the signal and trigger activation by autophosphorylation. The difference between classical and hybrid sensor kinase is that the signal are transmitted through a His residue (located in transmitter domain), then Asp residue (located in receiver domain or hybrid SK), and then His residue (located in the histidine phosphotransferase proein), final is to the Asp reside (located in the cognate response regulator). obo:OTCS_0000024 Oliver He, Hsin-Hui Huang obo:OTCS_0000024 WEB: https://www.ncbi.nlm.nih.gov/pubmed/30687268 obo:OTCS_0000024 bacterial hybrid sensor kinase role obo:OTCS_0000025 A bacterial unorthodox sensor kinase role is the role of protein, consisting of a sensor, a transmitter, a receiver, and a histidine-containing phosphotransmitter domain, also has ability to sense signal and trigger activation by autophosphorylation. The phophoryl group can be transferred by H1-D1-H2-D2, which the H1, D1, and H2 are located in the unorthodox SK and the D2 is located in the cognate response regulator. The difference between hybrid and unorthodox type is that the histidine phosphotransmitter domain of the hybrid type is an external phosphotransfer module that acts as an individual protein. obo:OTCS_0000025 Oliver He, Hsin-Hui Huang obo:OTCS_0000025 WEB: https://www.ncbi.nlm.nih.gov/pubmed/30687268 obo:OTCS_0000025 bacterial unorthodox sensor kinase role obo:OTCS_0000026 The bacterial classifical two-component system composed of two proteins, sensor kinase and response regulator and this system is a one-step phosphotransfer occurs between the sensor kinase and response regulator. obo:OTCS_0000026 Oliver He, Ming Liu, Hsin-Hui Huang obo:OTCS_0000026 bacterial classical TCS obo:OTCS_0000026 WEB: http://www.ncbi.nlm.nih.gov/pubmed/10203840 obo:OTCS_0000026 bacterial classical two-component regulatory system obo:OTCS_0000027 Unorthodox two-component regulatory system are characterized by a "multi-step phosphorelay" that alternates between several histidine and aspartate residue (His-Asp-His-Asp) and involves additional receiver and HPt domains. obo:OTCS_0000027 Oliver He, Ming Liu, Hsin-Hui Huang obo:OTCS_0000027 bacterial phosphorelay obo:OTCS_0000027 bacterial unorthodox system obo:OTCS_0000027 WEB: https://www.ncbi.nlm.nih.gov/pubmed/10203840 obo:OTCS_0000027 bacterial unorthodox two component system obo:OTCS_0000028 For unothodox two-component regulatory system, the histidine phosphotransferase protein has a conserved histidine phosphorylation site. The histidine phosphotransferase protein can receive the phosphoryl group from the hybrid sensor kinase and further transfers the phosphoryl group to the conserved aspartic residue located at the N-terminal of cognate response regulator. obo:OTCS_0000028 Oliver He, Ming Liu, Hsin-Hui Huang obo:OTCS_0000028 WEB: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6335343 WEB: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5571105 obo:OTCS_0000028 bacterial histidine phosphotransferase protein obo:OTCS_0000029 The bacterial histidine phosphotransferase protein role is a role of protein harbors a phosphorylatable histidine residue which are responsible for transferring a phosphoryl group from an aspartate residue on the hybrid sensor kinase protein. obo:OTCS_0000029 Oliver He, Hsin-Hui Huang obo:OTCS_0000029 WEB: https://www.ncbi.nlm.nih.gov/pubmed/30687268 obo:OTCS_0000029 bacterial histidine phosphotransferase protein role obo:OTCS_0000030 The DpiBA TCS consists of DpiB classical type sensor kinase and DpiA response regulator. The DpiBA TCS activates genes involved in anaerobic citrate catabolism when E. coli survival under anaerobic conditions. obo:OTCS_0000030 Oliver He, Hsin-Hui Huang obo:OTCS_0000030 CitAB two-component regulatory system obo:OTCS_0000030 DpiBA two-component regulatory system of Escherichia coli K-12 obo:OTCS_0000030 WEB: https://www.ncbi.nlm.nih.gov/pubmed/18997424 WEB: https://www.ncbi.nlm.nih.gov/pubmed/19202292 obo:OTCS_0000030 DpiBA two-component regulatory system obo:OTCS_0000031 The KdpDE TCS consists of KdpD classical type sensor kinase and KdpE response regulator. The KdpDE TCS was controlled by intracellular and extracellular potassium concentration, intracellular ionic strength, and ATP levels. The activated KdpDE enhances the expression of kdpFABC encoding a high affinity potassium transporter which man maintain the potassium homeostasis. obo:OTCS_0000031 Oliver He, Hsin-Hui Huang obo:OTCS_0000031 KdpDE two-component regulatory system of Escherichia coli K-12 obo:OTCS_0000031 WEB: https://www.ncbi.nlm.nih.gov/pubmed/7855422 WEB: https://www.ncbi.nlm.nih.gov/pubmed/11016946 WEB: https://www.ncbi.nlm.nih.gov/pubmed/23651428 obo:OTCS_0000031 KdpDE two-component regulatory system obo:OTCS_0000032 The NarLX TCS consists of NarX classical type sensor kinase and NarL response regulator. The NarXL control anaerobic respiratory pathway by upregulating gene involved in anaerobic nitrate respiration in response to nitrate and nitrite. The NarX is mainly to detect nitrate limitation. obo:OTCS_0000032 Oliver He, Hsin-Hui Huang obo:OTCS_0000032 NarLX two-component regulatory system of Escherichia coli K-12 obo:OTCS_0000032 WEB: https://www.ncbi.nlm.nih.gov/pubmed/8412692 WEB: https://www.ncbi.nlm.nih.gov/pubmed/7855431 obo:OTCS_0000032 NarLX two-component regulatory system obo:OTCS_0000033 The RstBA TCS consists of RstB classical type sensor kinase and RstA response regulator. The rstBA expression is positively regulated by PhoPQ TCS. The RstBA TCS makes contribution to antibiotic, anti-inflammatory agents (ketoprofen), and muscle relaxant (pridinol) resistance. obo:OTCS_0000033 Oliver He, Hsin-Hui Huang obo:OTCS_0000033 RstBA two-component regulatory system of Escherichia coli K-12 obo:OTCS_0000033 WEB: https://www.ncbi.nlm.nih.gov/pubmed/12813061 obo:OTCS_0000033 RstBA two-component regulatory system obo:OTCS_0000034 The HprSR TCS consists of HprS classical type sensor kinase and HprR response regulator. The HprSR TCS is implicated in the stress response to hydrogen peroxide (H2O2) and regulates several target operon (cyoABCDE, cusCFBA, hiuH) implicated in the production of reactive oxygen species. obo:OTCS_0000034 Oliver He, Hsin-Hui Huang obo:OTCS_0000034 HprSR two-component regulatory system of Escherichia coli K-12 obo:OTCS_0000034 YedVW two-component regulatory system obo:OTCS_0000034 WEB: https://www.ncbi.nlm.nih.gov/pubmed/25568260 WEB: https://www.ncbi.nlm.nih.gov/pubmed/27983483 obo:OTCS_0000034 HprSR two-component regulatory system obo:OTCS_0000035 The BaeSR consists of BaeS classical sensor kinase and BaeR response regulator. The BaeSR TCS, one of the envelope stress response in E. coli that responds to envelope stress triggered by spheroblast formation, misfolded protein, and envelope-damaging agents, as a global regulator to influence mdtABCD, acrD, and spy gene expression, and though multiple antibiotics susceptibility. obo:OTCS_0000035 Oliver He, Hsin-Hui Huang obo:OTCS_0000035 BaeSR two-component regulatory system of Escherichia coli K-12 obo:OTCS_0000035 WEB://www.ncbi.nlm.nih.gov/pubmed/21515766 obo:OTCS_0000035 BaeSR two-component regulatory system obo:OTCS_0000036 The BtsSR TCS consists of BtsS classical type sensor kinase and BtsR response regulator. The BtsSR TCS that sense the presence of pyruvate (concentration higher than 50 uM) during nutrient limitation and induces expression of btsT encoding a high-affinity pyuvate:H+ symporter. obo:OTCS_0000036 Oliver He, Hsin-Hui Huang obo:OTCS_0000036 BtsSR two-component regulatory system of Escherichia coli K-12 obo:OTCS_0000036 YehUT two-component regulatory system obo:OTCS_0000036 WEB: https://www.ncbi.nlm.nih.gov/pubmed/29038258 obo:OTCS_0000036 BtsSR two-component regulatory system obo:OTCS_0000037 The Rcs phosphorelay consists of three proteins, including RcsC hybrid type sensor kinase, RcsD classical type sensor kinase, and RcsB response regulator. The Rcs phosphorelay responds to peptidoglycan damage caused by beta-lactams, polymyxins, or low temperatue and contributes to the intrinsic resistance of E. coli to beta-lactam antibiotics. obo:OTCS_0000037 Oliver He, Hsin-Hui Huang obo:OTCS_0000037 RcsBCD phosphorelay of Escherichia coli K-12 obo:OTCS_0000037 RcsBCD phosphorelay two-component regulatory system of Escherichia coli K-12 obo:OTCS_0000037 RcsBCD two-component regulatory system of Escherichia coli K-12 obo:OTCS_0000037 WEB: https://www.ncbi.nlm.nih.gov/pubmed/18192383 obo:OTCS_0000037 RcsBCD two-component regulatory system obo:OTCS_0000038 AtoSC TCS consists of AtoS classical sensor kinase and AtoC response regulator. The AtoSC TCS, activating in the presence of acetoacetate, participates in shory-chain fatty acid metabolism by regulating atoDAEB operon. obo:OTCS_0000038 Oliver He, Hsin-Hui Huang obo:OTCS_0000038 AtoSC two-component regulatory system of Escherichia coli K-12 obo:OTCS_0000038 WEB://www.ncbi.nlm.nih.gov/pubmed/21757361 obo:OTCS_0000038 AtoSC two-component regulatory system obo:OTCS_0000039 The YpdAB TCS consists of YpdA classical type sensor kinase and YpdB response regulator. The YpdA senses the presence of pyruvate (concentration higher than 600 uM) in the extracellular condition during nutrient limitation. The phosphorylated YpdB induces expression of yhjX encoding a oxalate/formate antiporter. obo:OTCS_0000039 Oliver He, Hsin-Hui Huang obo:OTCS_0000039 PyrSR two-component regulatory system obo:OTCS_0000039 YpdAB two-component regulatory system of Escherichia coli K-12 obo:OTCS_0000039 WEB: https://www.ncbi.nlm.nih.gov/pubmed/29038258 obo:OTCS_0000039 YpdAB two-component regulatory system obo:OTCS_0000040 The NarQP TCS consists of NarQ classical type sensor kinase and NarP response regulator. The NarQ modulate anaerobic respiratory gene expression in response to nitrate and nitrite. The NarQ is mainly to detect the nitrite limitation. obo:OTCS_0000040 Oliver He, Hsin-Hui Huang obo:OTCS_0000040 NarQP two-component regulatory system of Escherichia coli K-12 obo:OTCS_0000040 WEB: https://www.ncbi.nlm.nih.gov/pubmed/8412692 WEB: https://www.ncbi.nlm.nih.gov/pubmed/7855431 obo:OTCS_0000040 NarQP two-component regulatory system obo:OTCS_0000041 The GlrKR TCS consists of GlrK classical type sensor kinase and GlrR response regulator. The host stress hormones epinephrine (Epi) and norepinephrine are sense though the GlrK (QseC) and this pathway is dependent on the outer membrane lipoprotein QseG. The activated GlrKR may positively regulate the rpoE expreesion which permits rapid response to a veriety stress conditions. obo:OTCS_0000041 Oliver He, Hsin-Hui Huang obo:OTCS_0000041 GlrKR two-component regulatory system of Escherichia coli K-12 obo:OTCS_0000041 QseEF two-component regulatory system obo:OTCS_0000041 YfhKA two-component regulatory system obo:OTCS_0000041 WEB: https://www.ncbi.nlm.nih.gov/pubmed/30040820 WEB: https://www.ncbi.nlm.nih.gov/pubmed/27629414 obo:OTCS_0000041 GlrKR two-component regulatory system obo:OTCS_0000042 The QseBC TCS consists of QseC classical type sensor kinase and QseB response regulator. The QseBC TCS detect quorum sensing autoinducer (AI-2) and is dedicated to transducing this signal towards regulation of the flagella synthesis and biofilm formation. obo:OTCS_0000042 Oliver He, Hsin-Hui Huang obo:OTCS_0000042 QseBC two-component regulatory system of Escherichia coli K-12 obo:OTCS_0000042 WEB: https://www.ncbi.nlm.nih.gov/pubmed/11929534 WEB: https://www.ncbi.nlm.nih.gov/pubmed/16352847 obo:OTCS_0000042 QseBC two-component regulatory system obo:OTCS_0000043 The EnvZ-OmpR TCS consists of EnvZ classical type sensor kinase and OmpR response regulator. The EnvZ-OmpR TCS of E. coli is best definied by its modulation of the two outer membrane diffusion pores OmpF and OmpC in response to changes in medium osmolarity. obo:OTCS_0000043 Oliver He, Hsin-Hui Huang obo:OTCS_0000043 EnvZ-OmpR two-component regulatory system of Escherichia coli K-12 obo:OTCS_0000043 EnvZ/OmpR TCS of Escherichia coli str. K-12 substr. MG1655 obo:OTCS_0000043 WEB: https://www.ncbi.nlm.nih.gov/pubmed/2668953 obo:OTCS_0000043 EnvZ-OmpR two-component regulatory system obo:OTCS_0000044 The UhpAB TCS consists of UhpB classical type sensor kinase and UhpA response regulator. The UhpC phosphate sensor protein required to sense extracellular hexose phosphate and further trigger UhpB sensor kinase autophosphorylation. The phosphorylated UhpAB activates the transcription of uhpT encoding a hexose phosphate transport that exchanges intracellular phosphate for extracellular hexose phosphate. obo:OTCS_0000044 Oliver He, Hsin-Hui Huang obo:OTCS_0000044 UhpAB two-component regulatory system of Escherichia coli K-12 obo:OTCS_0000044 WEB: https://www.ncbi.nlm.nih.gov/pubmed/8349544 WEB: https://www.ncbi.nlm.nih.gov/pubmed/3042748 WEB: https://www.ncbi.nlm.nih.gov/pubmed/11739766 obo:OTCS_0000044 UhpAB two-component regulatory system obo:OTCS_0000045 The NtrBC TCS consists of NtrB classical type sensor kinase and NtrC response regulator. The NtrBC enhnace nitrogen uptake, assimilate ammonia, and scavenge nitrogen-containing compounds in reponse to nitrogen starvation. obo:OTCS_0000045 Oliver He, Hsin-Hui Huang obo:OTCS_0000045 GlnGL two-component regulatory system obo:OTCS_0000045 NtrBC two-component regulatory system of Escherichia coli K-12 obo:OTCS_0000045 WEB: https://www.ncbi.nlm.nih.gov/pubmed/24947454 obo:OTCS_0000045 NtrBC two-component regulatory system obo:OTCS_0000046 The CpxAR TCS consists of CpxA classical type sensor kinase and CpxR response regulator. The CpxAR TCS is one of the envelope stress response in E. coli which activates protease and chaperones in response to cell envelope damage. Besides, the phosphorylated CpxR also can modulate the expression of gene involved in drug resistance, DNA repair, bacterial adherence, and motility. Activation of CpxAR TCS is complex, many stimuli (e.g. alkaline pH, high salt concentration, metals, and surface adhesion) have been identified. In addition, the CpxA also directly sense misfolded proteins such as PapE protein. obo:OTCS_0000046 Oliver He, Hsin-Hui Huang obo:OTCS_0000046 CpxAR two-component regulatory system of Escherichia coli K-12 obo:OTCS_0000046 WEB: https://www.ncbi.nlm.nih.gov/pubmed/22092888 obo:OTCS_0000046 CpxAR two-component regulatory system obo:OTCS_0000047 The ZraSR TCS consists of ZraS classical type sensor kinase and ZraR response regulator. The ZraSR TCS participates in zine and lead balance and confers to antibiotic resistance. The zraP gene activated by phosphorylated ZraSR TCS which scavenges the zinc ions present in the periplasm. obo:OTCS_0000047 Oliver He, Hsin-Hui Huang obo:OTCS_0000047 ZraSR two-component regulatory system of Escherichia coli K-12 obo:OTCS_0000047 WEB: https://www.ncbi.nlm.nih.gov/pubmed/26438879 WEB: https://www.ncbi.nlm.nih.gov/pubmed/30389436 obo:OTCS_0000047 ZraSR two-component regulatory system obo:OTCS_0000048 The BasSR TCS consists of BasS classical type sensor kinase and BarR response regulator. The BasSR TCS is known as an iron- and zinc-sensing transcriptional regulator in E. coli and further can contols, directly or indirectly, a set of genes that are associated with metal-response membrane modification, and genes for response to acidic and/or anaerobic growth conditions. obo:OTCS_0000048 Oliver He, Hsin-Hui Huang obo:OTCS_0000048 BasSR two-component regulatory system of Escherichia coli K-12 obo:OTCS_0000048 PmrAB two-component regulatory system obo:OTCS_0000048 WEB: https://www.ncbi.nlm.nih.gov/pubmed/15322361 WEB: https://www.ncbi.nlm.nih.gov/pubmed/15659689 WEB: https://www.ncbi.nlm.nih.gov/pubmed/22442305 obo:OTCS_0000048 BasSR two-component regulatory system obo:OTCS_0000049 The DcuSR TCS consists of DcuS classical type sensor kinase and DcuR response regulator. The DcuSR TCS controls the expression of genes relating to the catabolism of exogenous C4 dicarboxylates such as fumarate, malate, maleate, succinate, L-tartrate and aspartate during aerobic and anaerobic growth. obo:OTCS_0000049 Oliver He, Hsin-Hui Huang obo:OTCS_0000049 DcuSR two-component regulatory system of Escherichia coli K-12 obo:OTCS_0000049 WEB: https://www.ncbi.nlm.nih.gov/pubmed/9973351 WEB: https://www.ncbi.nlm.nih.gov/pubmed/14996819 obo:OTCS_0000049 DcuSR two-component regulatory system obo:OTCS_0000050 The CreBC TCS consists of CreC classical type sensor kinase and CreB response regulator. The CreBC TCS of E. coli is responsive to carbon sources and oxygen availability, and its activation is beneficial, as it mediates growth adaptation to anaerobic environments. obo:OTCS_0000050 Oliver He, Hsin-Hui Huang obo:OTCS_0000050 CreBC two-component regulatory system of Escherichia coli K-12 obo:OTCS_0000050 WEB: https://www.ncbi.nlm.nih.gov/pubmed/11350954 obo:OTCS_0000050 CreBC two-component regulatory system obo:OTCS_0000051 The TorSR TCS consists of TorS unorthodox type sensor kinase and TorR response regulator. The catalytic respiration TorCAD pathway is induced in the presence of trimethylamine N-oxide (TMAO) by the TorSR TCS. The TMAO is one of the alternative terminal electron acceptors which can let E. coli growth under anaerobic condition. obo:OTCS_0000051 Oliver He, Hsin-Hui Huang obo:OTCS_0000051 TorSR two-component regulatory system of Escherichia coli K-12 obo:OTCS_0000051 WEB: https://www.ncbi.nlm.nih.gov/pubmed/17850256 obo:OTCS_0000051 TorSR two-component regulatory system obo:OTCS_0000052 The EvgSA TCS consists of EvgS unorthodox type sensor kinase and EvgA response regulator. The EvgSA TCS confers acid resistance to E. coli cell. The EvgS activated under E. coli sense acidic pH. obo:OTCS_0000052 Oliver He, Hsin-Hui Huang obo:OTCS_0000052 EvgSA two-component regulatory system of Escherichia coli K-12 obo:OTCS_0000052 WEB: https://www.ncbi.nlm.nih.gov/pubmed/24957621 obo:OTCS_0000052 EvgSA two-component regulatory system obo:OTCS_0000053 The BarA-UvrY consists of BarA unorthodox type sensor kinase and UvrY response regulator. The BarA senses and responds to the presence of formate and acetate but also to that of other short-chain acids. Phosphorylated BarA catalyzes the transphosphorylation of UvrY which in turn activates expression of the noncoding RNAs of the carbon storage regulation (Csr) system, CsrB and CsrC. obo:OTCS_0000053 Oliver He, Hsin-Hui Huang obo:OTCS_0000053 BarA-UvrY two-component regulatory system of Escherichia coli K-12 obo:OTCS_0000053 BarA/UvrY two-component regulatory system obo:OTCS_0000053 WEB: https://www.ncbi.nlm.nih.gov/pubmed/20118252 WEB: https://www.ncbi.nlm.nih.gov/pubmed/9211896 WEB: https://www.ncbi.nlm.nih.gov/pubmed/25535275 obo:OTCS_0000053 BarA-UvrY two-component regulatory system obo:OTCS_0000054 The ArcAB TCS consists of ArcB unorthodox sensor kinase and ArcA response regulator. The ArcAB TCS of E. coli inovlved in sensing oxygen availability and the concomitant transcriptional regulation of oxidative and germentative catabolism. obo:OTCS_0000054 Oliver He, Hsin-Hui Huang obo:OTCS_0000054 ArcAB two-component regulatory system of Escherichia coli str. K-12 obo:OTCS_0000054 WEB: http://www.ncbi.nlm.nih.gov/pubmed/19933363 obo:OTCS_0000054 ArcAB two-component regulatory system obo:OTCS_0000055 The concentration of ion. An ion is an atom or molecule that has a net electrical charge. obo:OTCS_0000055 Oliver He, Hsin-Hui Huang obo:OTCS_0000055 WEB: https://en.wikipedia.org/wiki/ion obo:OTCS_0000055 ion concentration obo:OTCS_0000056 The ion concentration outside the cytoplasm of a cell. obo:OTCS_0000056 Oliver He, Hsin-Hui Huang obo:OTCS_0000056 extracytoplasmic ion concentration obo:OTCS_0000057 The ion concentration within the cell. The cytoplasm, or protoplasm, of bacterial cells is where the functions for cell growth, metabolism, and replication are carried out, that enclosed by the cell membrane. obo:OTCS_0000057 Oliver He, Hsin-Hui Huang obo:OTCS_0000057 WEB: https://micro.magnet.fsu.edu/cells/bacteriacell.html obo:OTCS_0000057 cytoplasmic ion concentration obo:OTCS_0000058 The concentration of anion. An anion is negatively charged ion, with more electrons than protons. obo:OTCS_0000058 Oliver He, Hsin-Hui Huang obo:OTCS_0000058 WEB: https://en.wikipedia.org/wiki/ion obo:OTCS_0000058 anion concentraion obo:OTCS_0000059 The concentration of cation. A cation is a positively charged ion, with fewer electrons than protons. obo:OTCS_0000059 Oliver He, Hsin-Hui Huang obo:OTCS_0000059 WEB: https://en.wikipedia.org/wiki/ion obo:OTCS_0000059 cation concentration obo:OTCS_0000060 The bacterial response regulator role is the role of protein serves as the phosphoacceptor which can receive the phosphoryl group from sensor kinase. obo:OTCS_0000060 Oliver He, Hsin-Hui Huang obo:OTCS_0000060 WEB: https://www.ncbi.nlm.nih.gov/pubmed/30687268 obo:OTCS_0000060 bacterial response regulator role obo:OTCS_0000061 a bacterial protein that mediates a cell's response to changes in its environment as part of the two-component regulatory system obo:OTCS_0000061 Oliver He, Ming Liu, Hsin-Hui Huang obo:OTCS_0000061 bacterial RR protein obo:OTCS_0000061 http://en.wikipedia.org/wiki/Response_regulator obo:OTCS_0000061 bacterial response regulator protein obo:OTCS_0000062 a gene that encodes for a bacterial respose regulator protein obo:OTCS_0000062 Oliver He, Ming Liu, Hsin-Hui Huang obo:OTCS_0000062 bacterial response regulator gene obo:OTCS_0000063 The concentration of a magnesium(2+). obo:OTCS_0000063 Oliver He, Hsin-Hui Huang obo:OTCS_0000063 magnesium(2+) concentration obo:OTCS_0000064 magnesium(2+) concentration lower than 10 uM obo:OTCS_0000065 the verb detect means to discover or observe the existence of something obo:OTCS_0000065 senses obo:OTCS_0000065 detects obo:OTCS_0000066 regulation of two-component regulatory system obo:OTCS_0000067 negative regulation of two-component regulatory system obo:OTCS_0000068 positive regulation of two-component regulatory system obo:OTCS_0000069 negative regulation of Escherichia coli K-12 two-component regulatory system obo:OTCS_0000070 negative regulation of Escherichia coli K-12 PhoPQ two-component regulatory system obo:OTCS_0000071 response to antimicrobial peptide obo:OTCS_0000072 response to cationic antimicrobial peptide obo:OTCS_0000073 response to anionic antimicrobial peptide obo:OTCS_0000074 positive regulation of Escherichia coli K-12 two-component regulatory system obo:OTCS_0000075 positive regulation of Escherichia coli K-12 BasSR two-component regulatory system obo:OTCS_0000076 The protein synthesis is catalyzed by ribosomes and cytoplasmic factors. The bacterial 70S ribosome is composed of two ribonucleoprotein subunits, the 30S and 50S subunits. Antibiotics inhibit protein biosynthesis by targeting on the 30S and 50S subunit of the bacterial ribosome. obo:OTCS_0000076 Oliver He, Hsin-Hui Huang obo:OTCS_0000076 WEB: https://www.ncbi.nlm.nih.gov/pubmed/29109626 obo:OTCS_0000076 antibiotic targeting on protein synthesis obo:OTCS_0000077 Nucleic acid synthesis is the process that nucleic acids are synthesized from triphosphate nucleotide precursors by DNA or RNA polymerases using DNA as a template. obo:OTCS_0000077 Oliver He, Hsin-Hui Huang obo:OTCS_0000077 WEB: https://www.sciencedirect.com/topics/neuroscience/nucleic-acid-synthesis obo:OTCS_0000077 antibiotic targeting on nucleic acid synthesis obo:OTCS_0000081 The 30S subunit is an integral part of mRNA translation. It binds three prokaryotic initiation factors: IF-1, IF-2, and IF-3. obo:OTCS_0000081 Oliver He, Hsin-Hui Huang obo:OTCS_0000081 WEB: https://en.wikipedia.org/wiki/Prokaryotic_small_ribosomal_subunit obo:OTCS_0000081 antibiotic targeting on 30S subunit of bacterial ribosome obo:OTCS_0000082 50S is the larger subunit of the 70S ribosome of prokaryotes. The 50S subunit primary composed of proteins but also contains single-stranded RNA known as ribosomal RNA (rRNA). rRNA forms secondary and tertiary structures to maintain the structure and carry out the catalytic functions of the ribosome. obo:OTCS_0000082 Oliver He, Hsin-Hui Huang obo:OTCS_0000082 WEB: https://en.wikipedia.org/wiki/Prokaryotic_large_ribosome_subunit obo:OTCS_0000082 antibiotic targeting on 50S subunit of bacterial ribosome obo:OTCS_0000083 DNA replication is the biological process of producing two identical replicas of DNA from one original DNA molecules. DNA replication occurs in living organisms acting as the basis for biological inheritance. The cell possesses the distinctive property of division, which makes replication of DNA essential. obo:OTCS_0000083 Oliver He, Hsin-Hui Huang obo:OTCS_0000083 WEB: https://en.wikipedia.org/wiki/DNA_replication obo:OTCS_0000083 targeting on DNA replication obo:OTCS_0000084 RNA synthesis is a process which also called "transcription". Transcription is the first step of DNA based gene expression, in which a particular segment DNA is copied into RNA (especially mRNA) by the enzyme RNA polymerase. During transcription, a DNA sequence is read by an RNA polymerase, which produces a complementary, antiparallel RNA strand called a primary transcript. obo:OTCS_0000084 Oliver He, Hsin-Hui Huang obo:OTCS_0000084 WEB: https://en.wikipedia.org/wiki/Trancription_(biology) obo:OTCS_0000084 targeting on RNA synthesis obo:OTCS_0000085 Folate derivatives participate in the biosynthesis of both purines and pyrimidines. Formyl folate is required for two of the steps in the biosynthesis of inosine monophosphate, the precursor to GMP and AMP. Methylenetetrahydrofolate donates the C1 center required for the biosynthesis of dTMP from dUMP. The conversion is catalyzed by thymidylate synthase. obo:OTCS_0000085 Oliver He, Hsin-Hui Huang obo:OTCS_0000085 WEB: https://en.wikipedia.org/wiki/Folate obo:OTCS_0000085 targeting on folate synthesis obo:OTCS_0000086 Antibiotic resistance is the ability of microbe, especially bacteria, to resist or to become tolerant to antibiotics to which they were once sensitive. obo:OTCS_0000086 WEB: https://www.medicinenet.com/script/main/art.asp?articlekey=2276 obo:OTCS_0000086 antibiotic resistance obo:OTCS_0000088 Bacteria has ability to generate the enzymes caplable of introducing chemical changes to the antibiotic. obo:OTCS_0000088 WEB: https://www.ncbi.nlm.nih.gov/pubmed/27227291 obo:OTCS_0000088 chemical alteration of antibiotic obo:OTCS_0000089 The antibiotic was destroyed by some enzymes generating from bacteria and further lead to antibiotic become ineffective. obo:OTCS_0000089 WEB: https://www.ncbi.nlm.nih.gov/pubmed/27227291 obo:OTCS_0000089 destruction of antibiotic obo:OTCS_0000090 Many of antibiotics used in clinical practice have intracellular bacterial targets; therefore, the antibiotics must penetrate the outer and/or cytoplasmic membrane in order to exert its antimicrobial effect. Bacteria have developed mechanism to prevent the accumulation of antibiotic by decreasing permeability or increasing efflux of the antibiotics from the cell. obo:OTCS_0000090 WEB: https://www.ncbi.nlm.nih.gov/pubmed/27227291 WEB: https://www.ncbi.nlm.nih.gov/pubmed/29109626 obo:OTCS_0000090 reduction of accumulation of antibiotic obo:OTCS_0000093 Natural variations or acquired changes in the antibiotic target site can avoid the action of the antibiotics. obo:OTCS_0000093 WEB: https://www.ncbi.nlm.nih.gov/pubmed/27227291 WEB: https://www.ncbi.nlm.nih.gov/pubmed/29109626 obo:OTCS_0000093 alternation in antibiotic target site obo:PATO_0001655 Osmolarity, also known as osmotic concentration, is the measure of solute concentration. obo:PATO_0001655 WEB: https://en.wikipedia.org/wiki/Osmotic_concentration obo:PATO_0001655 obo:oba.owl obo:PATO_0001655 osmolarity obo:PR_000000001 An amino acid chain that is produced de novo by ribosome-mediated translation of a genetically-encoded mRNA. obo:PR_000000001 obo:pr.owl obo:PR_000000001 protein obo:PR_000000001 PR:000000001 obo:PR_000000001 Proteins descended from a common ancestor can be classified into families and superfamilies composed of products of evolutionarily-related genes. The domain architecture of a protein is described by the order of its constituent domains. Proteins with the same domains in the same order are defined as homeomorphic [PRO:WCB]. obo:PR_000000001 protein obo:PR_000023544 A protein that is a translation product of the Escherichia coli K-12 phoP gene or a 1:1 ortholog thereof. The phoP-phoQ two-component system regulates the transcription of numerous genes in response to changes in extracellular divalent cation concentration and pH. obo:PR_000023544 obo:pr.owl obo:PR_000023544 phoP obo:PR_000023544 protein obo:PR_000023544 PR:000023544 obo:PR_000023544 Category=gene. obo:PR_000023544 transcriptional regulatory protein PhoP obo:PR_000023545 A protein that is a translation product of the Escherichia coli K-12 phoQ gene or a 1:1 ortholog thereof. The phoP-phoQ two-component system regulates the transcription of numerous genes in response to changes in extracellular divalent cation concentration and pH. obo:PR_000023545 obo:pr.owl obo:PR_000023545 phoQ obo:PR_000023545 protein obo:PR_000023545 PR:000023545 obo:PR_000023545 Category=gene. obo:PR_000023545 sensor protein PhoQ obo:PR_000029062 A protein that is encoded in the genome of Escherichia coli K-12. obo:PR_000029062 obo:pr.owl obo:PR_000029062 Ecol protein obo:PR_000029062 protein obo:PR_000029062 PR:000029062 obo:PR_000029062 Escherichia coli K-12 protein obo:PR_000036195 A protein that is encoded in the genome of some Bacteria <prokaryote>. obo:PR_000036195 obo:pr.owl obo:PR_000036195 Bacteria <prokaryote> protein obo:PR_000036195 protein obo:PR_000036195 PR:000036195 obo:PR_000036195 bacterial protein obo:PR_P07330 protein-glutamate methylesterase/protein-glutamine glutaminase (Escherichia coli K-12) obo:PR_P07363 chemotaxis protein CheA (Escherichia coli K-12) obo:PR_P08368 A transcriptional regulatory protein CreB that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P08368] obo:PR_P08368 EcoCyc:CREB-MONOMER obo:PR_P08368 UniProtKB:P08368 obo:PR_P08368 Ec-creB obo:PR_P08368 protein obo:PR_P08368 yjjE, b4398 obo:PR_P08368 PR:P08368 obo:PR_P08368 Category=organism-gene. obo:PR_P08368 transcriptional regulatory protein CreB (Escherichia coli K-12) obo:PR_P08400 A phosphate regulon sensor protein PhoR that is encoded in the genome of Escherichia coli K-12. [PRO:DNx: http://www.uniprot.org/uniprot/P08400] obo:PR_P08400 EcoCyc:PHOR-MONOMER obo:PR_P08400 UniProtKB:P08400 obo:PR_P08400 Ec-phoR obo:PR_P08400 protein obo:PR_P08400 nmpB, b0400 obo:PR_P08400 PR:P08400 obo:PR_P08400 Category=organism-gene. obo:PR_P08400 phosphate regulon sensor protein PhoR (Escherichia coli K-12) obo:PR_P08401 A sensor protein CreC that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P08401] obo:PR_P08401 EcoCyc:CREC-MONOMER obo:PR_P08401 UniProtKB:P08401 obo:PR_P08401 Ec-creC obo:PR_P08401 protein obo:PR_P08401 phoM, b4399 obo:PR_P08401 PR:P08401 obo:PR_P08401 Category:organism-gene. obo:PR_P08401 sensor protein CreC (Escherichia coli K-12) obo:PR_P09835 A signal transduction histidine-protein kinase/phosphatase UhpB that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P09835] obo:PR_P09835 Category=organism-gene. obo:PR_P09835 EcoCyc:UHPB-MONOMER obo:PR_P09835 UniProtKB:P09835 obo:PR_P09835 Ec-uhpB obo:PR_P09835 sensor protein UhpB (Escherichia coli K-12) obo:PR_P09835 protein obo:PR_P09835 b3668 obo:PR_P09835 PR:P09835 obo:PR_P09835 signal transduction histidine-protein kinase/phosphatase UhpB (Escherichia coli K-12) obo:PR_P0A9Q1 An aerobic respiration control protein ArcA that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0A9Q1] obo:PR_P0A9Q1 EcoCyc:ARCA-MONOMER obo:PR_P0A9Q1 UniProtKB:P0A9Q1 obo:PR_P0A9Q1 Dye resistance protein (Escherichia coli K-12) obo:PR_P0A9Q1 Ec-arcA obo:PR_P0A9Q1 protein obo:PR_P0A9Q1 dye, seg, cpxC, sfrA, fexA, msp, b4401 obo:PR_P0A9Q1 PR:P0A9Q1 obo:PR_P0A9Q1 Category=organism-gene. obo:PR_P0A9Q1 aerobic respiration control protein ArcA (Escherichia coli K-12) obo:PR_P0AA16 A transcriptional regulatory protein OmpR that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AA16] obo:PR_P0AA16 EcoCyc:OMPR-MONOMER obo:PR_P0AA16 UniProtKB:P0AA16 obo:PR_P0AA16 Ec-ompR obo:PR_P0AA16 protein obo:PR_P0AA16 kmt, ompB, b3405 obo:PR_P0AA16 PR:P0AA16 obo:PR_P0AA16 Category:organism-gene. obo:PR_P0AA16 transcriptional regulatory protein OmpR (Escherichia coli K-12) obo:PR_P0AA93 A sensor histidine kinase YpdA that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AA93] obo:PR_P0AA93 EcoCyc:G7243-MONOMER obo:PR_P0AA93 UniProtKB:P0AA93 obo:PR_P0AA93 Ec-ypdA obo:PR_P0AA93 protein obo:PR_P0AA93 b2380 obo:PR_P0AA93 PR:P0AA93 obo:PR_P0AA93 Category=organism-gene. obo:PR_P0AA93 sensor histidine kinase YpdA (Escherichia coli K-12) obo:PR_P0ACZ4 A DNA-binding transcriptional activator EvgA that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0ACZ4] obo:PR_P0ACZ4 EcoCyc:EVGA-MONOMER obo:PR_P0ACZ4 UniProtKB:P0ACZ4 obo:PR_P0ACZ4 Ec-evgA obo:PR_P0ACZ4 positive transcription regulator EvgA (Escherichia coli K-12) obo:PR_P0ACZ4 protein obo:PR_P0ACZ4 b2369 obo:PR_P0ACZ4 PR:P0ACZ4 obo:PR_P0ACZ4 Category=organism-gene. obo:PR_P0ACZ4 DNA-binding transcriptional activator EvgA (Escherichia coli K-12) obo:PR_P0ACZ8 A transcriptional regulatory protein CusR that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0ACZ8] obo:PR_P0ACZ8 EcoCyc:G6319-MONOMER obo:PR_P0ACZ8 UniProtKB:P0ACZ8 obo:PR_P0ACZ8 Ec-cusR obo:PR_P0ACZ8 protein obo:PR_P0ACZ8 ylcA, b0571 obo:PR_P0ACZ8 PR:P0ACZ8 obo:PR_P0ACZ8 Category=organism-gene. obo:PR_P0ACZ8 transcriptional regulatory protein CusR (Escherichia coli K-12) obo:PR_P0AD01 A transcriptional regulatory protein DcuR that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AD01] obo:PR_P0AD01 EcoCyc:DCUR-MONOMER obo:PR_P0AD01 UniProtKB:P0AD01 obo:PR_P0AD01 Ec-dcuR obo:PR_P0AD01 protein obo:PR_P0AD01 yjdG, b4124 obo:PR_P0AD01 PR:P0AD01 obo:PR_P0AD01 Category=organism-gene. obo:PR_P0AD01 transcriptional regulatory protein DcuR (Escherichia coli K-12) obo:PR_P0AD14 A sensor histidine kinase BtsS that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AD14] obo:PR_P0AD14 EcoCyc:EG12007-MONOMER obo:PR_P0AD14 UniProtKB:P0AD14 obo:PR_P0AD14 Ec-yehU obo:PR_P0AD14 Sensor histidine kinase YehU (Escherichia coli K-12) obo:PR_P0AD14 protein obo:PR_P0AD14 yehU, b2126 obo:PR_P0AD14 PR:P0AD14 obo:PR_P0AD14 Category=organism-gene. obo:PR_P0AD14 sensor histidine kinase BtsS (Escherichia coli K-12) obo:PR_P0AE39 A transcriptional regulatory protein YpdB that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AE39] obo:PR_P0AE39 EcoCyc:G7244-MONOMER obo:PR_P0AE39 UniProtKB:P0AE39 obo:PR_P0AE39 Ec-ypdB obo:PR_P0AE39 protein obo:PR_P0AE39 b2381 obo:PR_P0AE39 PR:P0AE39 obo:PR_P0AE39 Category=organism-gene. obo:PR_P0AE39 transcriptional regulatory protein YpdB (Escherichia coli K-12) obo:PR_P0AE67 chemotaxis protein CheY (Escherichia coli K-12) obo:PR_P0AE82 A sensor histidine kinase CpxA that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AE82] obo:PR_P0AE82 EcoCyc:CPXA-MONOMER obo:PR_P0AE82 UniProtKB:P0AE82 obo:PR_P0AE82 Ec-cpxA obo:PR_P0AE82 protein obo:PR_P0AE82 eup, ecfB, b3911, ssd obo:PR_P0AE82 PR:P0AE82 obo:PR_P0AE82 Category=organism-gene. obo:PR_P0AE82 sensor histidine kinase CpxA (Escherichia coli K-12) obo:PR_P0AE88 A transcriptional regulatory protein CpxR that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AE88] obo:PR_P0AE88 EcoCyc:CPXR-MONOMER obo:PR_P0AE88 UniProtKB:P0AE88 obo:PR_P0AE88 Ec-cpxR obo:PR_P0AE88 protein obo:PR_P0AE88 yiiA, b3912 obo:PR_P0AE88 PR:P0AE88 obo:PR_P0AE88 Category:organism-gene. obo:PR_P0AE88 transcriptional regulatory protein CpxR (Escherichia coli K-12) obo:PR_P0AEC3 An aerobic respiration control sensor protein ArcB that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AEC3] obo:PR_P0AEC3 EcoCyc:ARCB-MONOMER obo:PR_P0AEC3 UniProtKB:P0AEC3 obo:PR_P0AEC3 Ec-arcB obo:PR_P0AEC3 protein obo:PR_P0AEC3 b3210 obo:PR_P0AEC3 PR:P0AEC3 obo:PR_P0AEC3 Category=organism-gene. obo:PR_P0AEC3 aerobic respiration control sensor protein ArcB (Escherichia coli K-12) obo:PR_P0AEC5 A signal transduction histidine-protein kinase BarA that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AEC5] obo:PR_P0AEC5 Category=organism-gene. obo:PR_P0AEC5 EcoCyc:BARA-MONOMER obo:PR_P0AEC5 UniProtKB:P0AEC5 obo:PR_P0AEC5 Ec-barA obo:PR_P0AEC5 protein obo:PR_P0AEC5 b2786 obo:PR_P0AEC5 PR:P0AEC5 obo:PR_P0AEC5 signal transduction histidine-protein kinase BarA (Escherichia coli K-12) obo:PR_P0AEC8 A sensor protein dcuS that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AEC8] obo:PR_P0AEC8 EcoCyc:DCUS-MONOMER obo:PR_P0AEC8 UniProtKB:P0AEC8 obo:PR_P0AEC8 Ec-dcuS obo:PR_P0AEC8 Fumarate sensor (Escherichia coli K-12) obo:PR_P0AEC8 protein obo:PR_P0AEC8 yjdH, b4125 obo:PR_P0AEC8 PR:P0AEC8 obo:PR_P0AEC8 Category:organism-gene. obo:PR_P0AEC8 sensor histidine kinase DcuS (Escherichia coli K-12) obo:PR_P0AED5 A response regulator UvrY that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AED5] obo:PR_P0AED5 EcoCyc:EG11140-MONOMER obo:PR_P0AED5 UniProtKB:P0AED5 obo:PR_P0AED5 Ec-uvrY obo:PR_P0AED5 protein obo:PR_P0AED5 b1914, yecB obo:PR_P0AED5 PR:P0AED5 obo:PR_P0AED5 Category=organism-gene. obo:PR_P0AED5 response regulator UvrY (Escherichia coli K-12) obo:PR_P0AEF4 A transcriptional regulatory protein DpiA that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AEF4] obo:PR_P0AEF4 EcoCyc:G6346-MONOMER obo:PR_P0AEF4 UniProtKB:P0AEF4 obo:PR_P0AEF4 Ec-dpiA obo:PR_P0AEF4 destabilizer of plasmid inheritance (Escherichia coli K-12) obo:PR_P0AEF4 protein obo:PR_P0AEF4 mpdA, criR, citB, b0620 obo:PR_P0AEF4 PR:P0AEF4 obo:PR_P0AEF4 Category=organism-gene. obo:PR_P0AEF4 transcriptional regulatory protein DpiA (Escherichia coli K-12) obo:PR_P0AEJ4 An osmolarity sensor protein EnvZ that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AEJ4] obo:PR_P0AEJ4 EcoCyc:ENVZ-MONOMER obo:PR_P0AEJ4 UniProtKB:P0AEJ4 obo:PR_P0AEJ4 Ec-envZ obo:PR_P0AEJ4 protein obo:PR_P0AEJ4 perA, tpo, ompB, b3404 obo:PR_P0AEJ4 PR:P0AEJ4 obo:PR_P0AEJ4 Category=organism-gene. obo:PR_P0AEJ4 osmolarity sensor protein EnvZ (Escherichia coli K-12) obo:PR_P0AEL8 A fimbriae Z protein that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AEL8] obo:PR_P0AEL8 EcoCyc:EG11103-MONOMER obo:PR_P0AEL8 UniProtKB:P0AEL8 obo:PR_P0AEL8 Ec-fimZ obo:PR_P0AEL8 protein obo:PR_P0AEL8 b0535, ybcA obo:PR_P0AEL8 PR:P0AEL8 obo:PR_P0AEL8 Category=organism-gene. obo:PR_P0AEL8 fimbriae Z protein (Escherichia coli K-12) obo:PR_P0AEV1 A regulator of RpoS that is encoded in the genome of Escherichia coli K-12. [PRO:DNx: http://www.uniprot.org/uniprot/P0AEV1] obo:PR_P0AEV1 EcoCyc: EG12121-MONOMER obo:PR_P0AEV1 UniProtKB:P0AEV1 obo:PR_P0AEV1 Ec-hnr obo:PR_P0AEV1 protein obo:PR_P0AEV1 sprE, ychL, b1235, hnr obo:PR_P0AEV1 PR:P0AEV1 obo:PR_P0AEV1 Category=organism-gene. obo:PR_P0AEV1 regulator of RpoS (Escherichia coli K-12) obo:PR_P0AF28 A nitrate/nitrite response regulator protein NarL that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AF28] obo:PR_P0AF28 EcoCyc:NARL-MONOMER obo:PR_P0AF28 UniProtKB:P0AF28 obo:PR_P0AF28 Ec-narL obo:PR_P0AF28 protein obo:PR_P0AF28 frdR, b1221 obo:PR_P0AF28 PR:P0AF28 obo:PR_P0AF28 Category=organism-gene. obo:PR_P0AF28 nitrate/nitrite response regulator protein NarL (Escherichia coli K-12) obo:PR_P0AFA2 A nitrate/nitrite sensor protein NarX that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AFA2] obo:PR_P0AFA2 EcoCyc:NARX-MONOMER obo:PR_P0AFA2 UniProtKB:P0AFA2 obo:PR_P0AFA2 Ec-narX obo:PR_P0AFA2 protein obo:PR_P0AFA2 narR, b1222 obo:PR_P0AFA2 PR:P0AFA2 obo:PR_P0AFA2 Category=organism-gene. obo:PR_P0AFA2 nitrate/nitrite sensor protein NarX (Escherichia coli K-12) obo:PR_P0AFB5 A sensory histidine kinase/phosphatase NtrB that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot.P0AFB5] obo:PR_P0AFB5 Category=organism-gene. obo:PR_P0AFB5 EcoCyc:PROTEIN-NRII obo:PR_P0AFB5 UniProtKB:P0AFB5 obo:PR_P0AFB5 Ec-glnL obo:PR_P0AFB5 NRII (Escherichia coli K-12) obo:PR_P0AFB5 Nitrogen regulation protein NR(II) (Escherichia coli K-12) obo:PR_P0AFB5 Nitrogen regulator II (Escherichia coli K-12) obo:PR_P0AFB5 protein obo:PR_P0AFB5 ntrB, b3869, glnR obo:PR_P0AFB5 PR:P0AFB5 obo:PR_P0AFB5 sensory histidine kinase/phosphatase NtrB (Escherichia coli K-12) obo:PR_P0AFB8 A DNA-binding transcriptional regulator NtrC that is the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AFB8] obo:PR_P0AFB8 EcoCyc:PROTEIN-NRI obo:PR_P0AFB8 UniProtKB:P0AFB8 obo:PR_P0AFB8 Ec-glnG obo:PR_P0AFB8 NRI(Escherichia coli) obo:PR_P0AFB8 nitrogen regulation protein NR(I) (Escherichia coli K-12) obo:PR_P0AFB8 nitrogen regulator I (Escherichia coli K-12) obo:PR_P0AFB8 protein obo:PR_P0AFB8 b3868, ntrC, glnT obo:PR_P0AFB8 PR:P0AFB8 obo:PR_P0AFB8 Category=organism-gene. obo:PR_P0AFB8 DNA-binding transcriptional regulator NtrC (Escherichia coli K-12) obo:PR_P0AFJ5 A phosphate regulon transcriptional regulatory protein PhoB that is encoded in the genome of Escherichia coli K-12. [PRO:DNx: http://www.uniprot.org/uniprot/P0AFJ5] obo:PR_P0AFJ5 EcoCyc:PHOB-MONOMER obo:PR_P0AFJ5 UniProtKB:P0AFJ5 obo:PR_P0AFJ5 Ec-phoB obo:PR_P0AFJ5 protein obo:PR_P0AFJ5 b0399 obo:PR_P0AFJ5 PR:P0AFJ5 obo:PR_P0AFJ5 Category=organism-gene. obo:PR_P0AFJ5 phosphate regulon transcriptional regulatory protein PhoB (Escherichia coli K-12) obo:PR_P0AFT5 A transcriptional regulatory protein BtsR that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AFT5] obo:PR_P0AFT5 EcoCyc:EG12006-MONOMER obo:PR_P0AFT5 UniProtKB:P0AFT5 obo:PR_P0AFT5 Ec-yehT obo:PR_P0AFT5 transcriptional regulatory protein YehT (Escherichia coli K-12) obo:PR_P0AFT5 protein obo:PR_P0AFT5 yehT, b2125 obo:PR_P0AFT5 PR:P0AFT5 obo:PR_P0AFT5 Category=organism-gene. obo:PR_P0AFT5 transcriptional regulatory protein BtsR (Escherichia coli K-12) obo:PR_P0AFU4 A transcriptional regulatory protein GlrR that is encoded in the genome of Escherichia coli K-12. obo:PR_P0AFU4 EcoCyc:EG11285-MONOMER obo:PR_P0AFU4 UniProtKB:P0AFU4 obo:PR_P0AFU4 Ec-glrR obo:PR_P0AFU4 protein obo:PR_P0AFU4 b2554, yfhA obo:PR_P0AFU4 PR:P0AFU4 obo:PR_P0AFU4 Category=organism-gene. obo:PR_P0AFU4 transcriptional regulatory protein GlrR (Escherichia coli K-12) obo:PR_P0AGA6 A transcriptional regulatory protein UhpA that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AGA6] obo:PR_P0AGA6 EcoCyc:UHPA-MONOMER obo:PR_P0AGA6 UniProtKB:P0AGA6 obo:PR_P0AGA6 Ec-uhpA obo:PR_P0AGA6 protein obo:PR_P0AGA6 b3669 obo:PR_P0AGA6 PR:P0AGA6 obo:PR_P0AGA6 Category=organism-gene. obo:PR_P0AGA6 transcriptional regulatory protein UhpA (Escherichia coli K-12) obo:PR_P0DMC5 A sensor histidine kinase RcsC that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/PODMC5] obo:PR_P0DMC5 EcoCyc:RCSC-MONOMER obo:PR_P0DMC5 UniProtKB:P0DMC5 obo:PR_P0DMC5 Ec-rcsC obo:PR_P0DMC5 capsular synthesis regulator component C (Escherichia coli K-12) obo:PR_P0DMC5 protein obo:PR_P0DMC5 b2218 obo:PR_P0DMC5 PR:P0DMC5 obo:PR_P0DMC5 Category=organism-gene. obo:PR_P0DMC5 sensor histidine kinase RcsC (Escherichia coli K-12) obo:PR_P0DMC7 A transcriptional regulatory protein RcsB that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0DMC7] obo:PR_P0DMC7 PR:P69407 obo:PR_P0DMC7 EcoCyc:RCSB-MONOMER obo:PR_P0DMC7 UniProtKB:P0DMC7 obo:PR_P0DMC7 Ec-rcsB obo:PR_P0DMC7 capsular synthesis regulator component B (Escherichia coli K-12) obo:PR_P0DMC7 protein obo:PR_P0DMC7 b2217 obo:PR_P0DMC7 PR:P0DMC7 obo:PR_P0DMC7 Category:organism-gene. obo:PR_P0DMC7 transcriptional regulatory protein RcsB (Escherichia coli K-12) obo:PR_P14375 A transcriptional regulatory protein ZraR that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P14375] obo:PR_P14375 EcoCyc:HYDG-MONOMER obo:PR_P14375 UniProtKB:P14375 obo:PR_P14375 Ec-zraR obo:PR_P14375 protein obo:PR_P14375 hydG, b4004 obo:PR_P14375 PR:P14375 obo:PR_P14375 Category=organism-gene. obo:PR_P14375 transcriptional regulatory protein ZraR (Escherichia coli K-12) obo:PR_P14377 A sensor protein ZraS that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P14377] obo:PR_P14377 EcoCyc:HYDH-MONOMER obo:PR_P14377 UniProtKB:P14377 obo:PR_P14377 Ec-zraS obo:PR_P14377 protein obo:PR_P14377 hydH, b4003 obo:PR_P14377 PR:P14377 obo:PR_P14377 Category=organism-gene. obo:PR_P14377 sensor protein ZraS (Escherichia coli K-12) obo:PR_P18392 A sensor protein RstB that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P18392] obo:PR_P18392 EcoCyc:RSTB-MONOMER obo:PR_P18392 UniProtKB:P18392 obo:PR_P18392 Ec-rstB obo:PR_P18392 protein obo:PR_P18392 uspT, b1609 obo:PR_P18392 PR:P18392 obo:PR_P18392 Category:organism-gene. obo:PR_P18392 sensor protein RstB (Escherichia coli K-12) obo:PR_P21865 A sensor protein KdpD that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P21865] obo:PR_P21865 EcoCyc:KDPD-MONOMER obo:PR_P21865 UniProtKB:P21865 obo:PR_P21865 Ec-kdpD obo:PR_P21865 protein obo:PR_P21865 b0695 obo:PR_P21865 PR:P21865 obo:PR_P21865 Category=organism-gene. obo:PR_P21865 sensor protein KdpD (Escherichia coli K-12) obo:PR_P21866 A kdp operon transcriptional regulatory protein KdpE that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P21866] obo:PR_P21866 EcoCyc:KDPE-MONOMER obo:PR_P21866 UniProtKB:P21866 obo:PR_P21866 Ec-kdpE obo:PR_P21866 protein obo:PR_P21866 b0694 obo:PR_P21866 PR:P21866 obo:PR_P21866 Category=organism-gene. obo:PR_P21866 kdp operon transcriptional regulatory protein KdpE (Escherichia coli K-12) obo:PR_P23836 A transcriptional regulatory protein PhoP that is encoded in the genome of Escherichia coli K-12. obo:PR_P23836 obo:pr.owl obo:PR_P23836 EcoCyc:PHOP-MONOMER obo:PR_P23836 UniProtKB:P23836 obo:PR_P23836 Ec-phoP obo:PR_P23836 protein obo:PR_P23836 b1130 obo:PR_P23836 PR:P23836 obo:PR_P23836 Category=organism-gene. obo:PR_P23836 transcriptional regulatory protein PhoP (Escherichia coli K-12) obo:PR_P23837 A sensor protein PhoQ that is encoded in the genome of Escherichia coli K-12. obo:PR_P23837 obo:pr.owl obo:PR_P23837 EcoCyc:PHOQ-MONOMER obo:PR_P23837 UniProtKB:P23837 obo:PR_P23837 Ec-phoQ obo:PR_P23837 sensor histidine protein kinase/phosphatase PhoQ (Escherichia coli K-12) obo:PR_P23837 protein obo:PR_P23837 b1129 obo:PR_P23837 PR:P23837 obo:PR_P23837 Category=organism-gene. obo:PR_P23837 sensor protein PhoQ (Escherichia coli K-12) obo:PR_P27896 A nitrate/nitrite sensor protein NarQ that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P27896] obo:PR_P27896 EcoCyc:NARQ-MONOMER obo:PR_P27896 UniProtKB:P27896 obo:PR_P27896 Ec-narQ obo:PR_P27896 protein obo:PR_P27896 b2469 obo:PR_P27896 PR:P27896 obo:PR_P27896 Category=organism-gene. obo:PR_P27896 nitrate/nitrite sensor protein NarQ (Escherichia coli K-12) obo:PR_P30843 A transcriptional regulatory protein BasR that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P30843] obo:PR_P30843 EcoCyc:BASR-MONOMER obo:PR_P30843 UniProtKB:P30843 obo:PR_P30843 Ec-basR obo:PR_P30843 protein obo:PR_P30843 pmrA, b4113 obo:PR_P30843 PR:P30843 obo:PR_P30843 Category=organism-gene. obo:PR_P30843 transcriptional regulatory protein BasR (Escherichia coli K-12) obo:PR_P30844 A sensor protein BasS that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P30844] obo:PR_P30844 EcoCyc:BASS-MONOMER obo:PR_P30844 UniProtKB:P30844 obo:PR_P30844 Ec-basS obo:PR_P30844 protein obo:PR_P30844 pmrB, b4112 obo:PR_P30844 PR:P30844 obo:PR_P30844 Category=organism-gene. obo:PR_P30844 sensor protein BasS (Escherichia coli K-12) obo:PR_P30847 A signal transduction histidine-protein kinase BaeS that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P30847] obo:PR_P30847 EcoCyc:BAES-MONOMER obo:PR_P30847 UniProtKB:P30847 obo:PR_P30847 Ec-baeS obo:PR_P30847 protein obo:PR_P30847 b2078 obo:PR_P30847 PR:P30847 obo:PR_P30847 Category=organism-gene. obo:PR_P30847 signal transduction histidine-protein kinase BaeS (Escherichia coli K-12) obo:PR_P30855 A sensor protein EvgS that is encoded in the genome of Escherichia coli K-12. obo:PR_P30855 EcoCyc:EVGS-MONOMER obo:PR_P30855 UniProtKB:P30855 obo:PR_P30855 Ec-evgS obo:PR_P30855 protein obo:PR_P30855 b2370 obo:PR_P30855 PR:P30855 obo:PR_P30855 Category=organism-gene. obo:PR_P30855 sensor protein EvgS (Escherichia coli K-12) obo:PR_P31802 A nitrate/nitrite response regulator protein NarP that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P31802] obo:PR_P31802 EcoCyc:NARP-MONOMER obo:PR_P31802 UniProtKB:P31802 obo:PR_P31802 Ec-narP obo:PR_P31802 protein obo:PR_P31802 b2193 obo:PR_P31802 PR:P31802 obo:PR_P31802 Category=organism-gene. obo:PR_P31802 nitrate/nitrite response regulator protein NarP (Escherichia coli K-12) obo:PR_P38684 A torCAD operon transcriptional regulatory protein TorR that is encoded in the genome of Escherichia coli K-12. obo:PR_P38684 EcoCyc:TORR-MONOMER obo:PR_P38684 UniProtKB:P38684 obo:PR_P38684 Ec-torR obo:PR_P38684 protein obo:PR_P38684 b0995 obo:PR_P38684 PR:P38684 obo:PR_P38684 Category=organism-gene. obo:PR_P38684 torCAD operon transcriptional regulatory protein TorR (Escherichia coli K-12) obo:PR_P39453 A sensor protein TorS that is encoded in the genome of Escherichia coli K-12. obo:PR_P39453 EcoCyc:TORS-MONOMER obo:PR_P39453 UniProtKB:P39453 obo:PR_P39453 Ec-torS obo:PR_P39453 protein obo:PR_P39453 yccI, b0993 obo:PR_P39453 PR:P39453 obo:PR_P39453 Category=organism-gene. obo:PR_P39453 sensor protein TorS (Escherichia coli K-12) obo:PR_P39838 A phosphotransferase RcsD that is encoded in the genome of Escherichia coli K-12. obo:PR_P39838 EcoCyc:EG12385-MONOMER obo:PR_P39838 UniProtKB:P39838 obo:PR_P39838 Ec-rcsD obo:PR_P39838 Ec-yojN obo:PR_P39838 Sensor-like histidine kinase RcsD (Escherichia coli K-12) obo:PR_P39838 phosphotransfer intermediate RcsD (Escherichia coli K-12) obo:PR_P39838 protein obo:PR_P39838 yojN, yojP, yojQ, b2216 obo:PR_P39838 PR:P39838 obo:PR_P39838 Category=organism-gene. obo:PR_P39838 phosphotransferase RcsD (Escherichia coli K-12) obo:PR_P40719 A sensor protein QseC that is encoded in the genome of Escherichia coli K-12. obo:PR_P40719 EcoCyc:EG12658-MONOMER obo:PR_P40719 UniProtKB:P40719 obo:PR_P40719 Ec-qseC obo:PR_P40719 protein obo:PR_P40719 ygiY, b3026 obo:PR_P40719 PR:P40719 obo:PR_P40719 Category=organism-gene. obo:PR_P40719 sensor protein QseC (Escherichia coli K-12) obo:PR_P52076 A transcriptional regulatory protein QseB that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P52076] obo:PR_P52076 EcoCyc:G7575-MONOMER obo:PR_P52076 UniProtKB:P52076 obo:PR_P52076 Ec-qseB obo:PR_P52076 protein obo:PR_P52076 ygiX, b3025 obo:PR_P52076 PR:P52076 obo:PR_P52076 Category=organism-gene. obo:PR_P52076 transcriptional regulatory protein QseB (Escherichia coli K-12) obo:PR_P52101 A sensor-like histidine kinase GlrK that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P52101] obo:PR_P52101 EcoCyc:G7345-MONOMER obo:PR_P52101 UniProtKB:P52101 obo:PR_P52101 Ec-glrK obo:PR_P52101 protein obo:PR_P52101 yfhK, b2556 obo:PR_P52101 PR:P52101 obo:PR_P52101 Category:organism-gene. obo:PR_P52101 sensor hidtidine kinase GlrK (Escherichia coli K-12) obo:PR_P52108 A transcriptional regulatory protein RstA that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P52108] obo:PR_P52108 EcoCyc:RSTA-MONOMER obo:PR_P52108 UniProtKB:P52108 obo:PR_P52108 Ec-rstA obo:PR_P52108 protein obo:PR_P52108 b1608, urpT obo:PR_P52108 PR:P52108 obo:PR_P52108 Category=organism-gene. obo:PR_P52108 transcriptional regulatory protein RstA (Escherichia coli K-12) obo:PR_P69228 A transcriptional regulatory protein BaeR that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P69228] obo:PR_P69228 Category=organism-gene. obo:PR_P69228 EcoCyc:BAER-MONOMER obo:PR_P69228 UniProtKB:P69228 obo:PR_P69228 Ec-baeR obo:PR_P69228 protein obo:PR_P69228 b2079 obo:PR_P69228 PR:P69228 obo:PR_P69228 transcriptional regulatory protein BaeR (Escherichia coli K-12) obo:PR_P76339 A sensor-like histidine kinase yedV that is encoded in the genome of Escherichia coli K-12. obo:PR_P76339 EcoCyc:G7056-MONOMER obo:PR_P76339 UniProtKB:P76339 obo:PR_P76339 Ec-yedV obo:PR_P76339 hydrogen peroxide response sensor (Escherichia coli K-12) obo:PR_P76339 protein obo:PR_P76339 b1968, yedV obo:PR_P76339 PR:P76339 obo:PR_P76339 Category=organism-gene. obo:PR_P76339 sensor histidine kinase HprS (Escherichia coli K-12) obo:PR_P76340 A transcriptional regulatory protein yedW that is encoded in the genome of Escherichia coli K-12. obo:PR_P76340 EcoCyc:G7057-MONOMER obo:PR_P76340 UniProtKB:P76340 obo:PR_P76340 Ec-yedW obo:PR_P76340 hydrogen peroxide response regulator (Escherichia coli K-12) obo:PR_P76340 protein obo:PR_P76340 b1969, yedW obo:PR_P76340 PR:P76340 obo:PR_P76340 Category:organism-gene. obo:PR_P76340 transcriptional regulatory protein HprR (Escherichia coli K-12) obo:PR_P77485 A sensor histidine kinase CusS that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P77485] obo:PR_P77485 EcoCyc:G6318-MONOMER obo:PR_P77485 UniProtKB:P77485 obo:PR_P77485 Ec-cusS obo:PR_P77485 protein obo:PR_P77485 ybcZ, b0570 obo:PR_P77485 PR:P77485 obo:PR_P77485 Category=organism-gene. obo:PR_P77485 sensor histidine kinase CusS (Escherichia coli K-12) obo:PR_P77510 A sensor kinase dpiB that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P77510] obo:PR_P77510 EcoCyc:G6345-MONOMER obo:PR_P77510 UniProtKB:P77510 obo:PR_P77510 Ec-dpiB obo:PR_P77510 Sensor histidine kinase CitA (Escherichia coli K-12) obo:PR_P77510 protein obo:PR_P77510 mpdB, b0619, ybeP, citA obo:PR_P77510 PR:P77510 obo:PR_P77510 Category=organism-gene. obo:PR_P77510 sensor histidine kinase DpiB (Escherichia coli K-12) obo:PR_Q06065 A regulatory protein AtoC that is encoded in the genome of Escherichia coli K-12. [PRO:DNx: http://www.uniprot.org/uniprot/Q06065] obo:PR_Q06065 EcoCyc:ATOC-MONOMER obo:PR_Q06065 UniProtKB:Q06065 obo:PR_Q06065 Acetoacetate metabolism regulatory protein (Escherichia coli K-12) obo:PR_Q06065 DNA-binding transcriptional regulator AtoC (Escherichia coli K-12) obo:PR_Q06065 Ec-atoC obo:PR_Q06065 Ornithine decarboxylase antizyme (Escherichia coli K-12) obo:PR_Q06065 acetoacetate metabolism regulatory protein AtoC (Escherichia colie K-12) obo:PR_Q06065 protein obo:PR_Q06065 az, b2220 obo:PR_Q06065 PR:Q06065 obo:PR_Q06065 Category=organism-gene. obo:PR_Q06065 regulatory protein AtoC (Escherichia coli K-12) obo:PR_Q06067 A signal transduction histidine-protein kinase AtoS that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/Q06067] obo:PR_Q06067 EcoCyc:ATOS-MONOMER obo:PR_Q06067 UniProtKB:Q06067 obo:PR_Q06067 Ec-atoS obo:PR_Q06067 protein obo:PR_Q06067 b2219 obo:PR_Q06067 PR:Q06067 obo:PR_Q06067 Category:organism-gene. obo:PR_Q06067 signal transduction histidine-protein kinase AtoS (Escherichia coli K-12) obo:RO_0000056 participates in obo:RO_0000056 this blood clot participates in this blood coagulation obo:RO_0000056 this input material (or this output material) participates in this process obo:RO_0000056 this investigator participates in this investigation obo:RO_0000056 a relation between a continuant and a process, in which the continuant is somehow involved in the process obo:RO_0000056 participates_in obo:RO_0000056 obo:ro.owl obo:RO_0000056 participates in obo:RO_0000057 has participant obo:RO_0000085 this enzyme has function this catalysis function (more colloquially: this enzyme has this catalysis function) obo:RO_0000085 a relation between an independent continuant (the bearer) and a function, in which the function specifically depends on the bearer for its existence obo:RO_0000085 A bearer can have many functions, and its functions can exist for different periods of time, but none of its functions can exist when the bearer does not exist. A function need not be realized at all the times that the function exists. obo:RO_0000085 has_function obo:RO_0000085 obo:ro.owl obo:RO_0000085 has function obo:RO_0000087 this person has role this investigator role (more colloquially: this person has this role of investigator) obo:RO_0000087 a relation between an independent continuant (the bearer) and a role, in which the role specifically depends on the bearer for its existence obo:RO_0000087 A bearer can have many roles, and its roles can exist for different periods of time, but none of its roles can exist when the bearer does not exist. A role need not be realized at all the times that the role exists. obo:RO_0000087 has_role obo:RO_0000087 obo:ro.owl obo:RO_0000087 has role obo:RO_0001900 An assertion that holds between an OWL Object Property and a temporal interpretation that elucidates how OWL Class Axioms that use this property are to be interpreted in a temporal context. obo:RO_0001900 temporal interpretation obo:RO_0001900 https://code.google.com/p/obo-relations/wiki/ROAndTime obo:RO_0002017 has component activity obo:RO_0002160 only_in_taxon obo:RO_0002205 every HOTAIR lncRNA is the gene product of some HOXC gene obo:RO_0002205 every sonic hedgehog protein (PR:000014841) is the gene product of some sonic hedgehog gene obo:RO_0002205 obo:IAO_0000125 obo:RO_0002205 x has gene product y if and only if x is a gene (SO:0000704) that participates in some gene expression process (GO:0010467) where the output of that process is either y or something that is ribosomally translated from y obo:RO_0002205 Chris Mungall obo:RO_0002205 obo:ro.owl obo:RO_0002205 has gene product obo:RO_0002211 regulates obo:RO_0002212 negatively regulates obo:RO_0002213 positively regulates obo:RO_0002327 a particular instances of akt-2 enables some instance of protein kinase activity obo:RO_0002327 Chris Mungall obo:RO_0002327 catalyzes obo:RO_0002327 executes obo:RO_0002327 has obo:RO_0002327 is catalyzing obo:RO_0002327 is executing obo:RO_0002327 This relation differs from the parent relation 'capable of' in that the parent is weaker and only expresses a capability that may not be actually realized, whereas this relation is always realized. obo:RO_0002327 This relation is currently used experimentally by the Gene Ontology Consortium. It may not be stable and may be obsoleted at some future time. obo:RO_0002327 obo:ro.owl obo:RO_0002327 enables obo:RO_0002331 c involved_in p if and only if c enables some process p', and p' is part of p obo:RO_0002331 Chris Mungall obo:RO_0002331 actively involved in obo:RO_0002331 enables part of obo:RO_0002331 obo:ro.owl obo:RO_0002331 involved in obo:RO_0002331 http://wiki.geneontology.org/index.php/Involved_in obo:RO_0002333 enabled by obo:RO_0002511 transcribed to obo:RO_0002513 ribosomally translates to obo:RO_0002577 A material entity consisting of multiple components that are causally integrated. obo:RO_0002577 May be replaced by a BFO class, as discussed in http://www.jbiomedsem.com/content/4/1/43 obo:RO_0002577 Chris Mungall obo:RO_0002577 http://www.jbiomedsem.com/content/4/1/43 obo:RO_0002577 obo:ro.owl obo:RO_0002577 system obo:RO_0003002 Holds between protein a (a transcription factor) and DNA element b if and only if a diminishes the process of transcription of b. obo:RO_0003002 Logical axioms to be added after the relevant branch of GO is MIREOTed in obo:RO_0003002 obo:ro.owl obo:RO_0003002 represses expression of obo:RO_0003003 Holds between protein a (a transcription factor) and DNA element b if and only if a activates the process of transcription of b. obo:RO_0003003 Logical axioms to be added after the relevant branch of GO is MIREOTed in obo:RO_0003003 obo:ro.owl obo:RO_0003003 increases expression of obo:ogg.owl Bin Zhao obo:ogg.owl Yongqun "Oliver" He (YH) obo:ogg.owl Yue Liu obo:ogg.owl 12-01-2016 obo:ogg.owl OGG is a biological ontology in the area of genes and genomes. OGG uses the Basic Formal Ontology (BFO) as its upper level ontology. This OGG document contains the genes and genomes of a list of selected organisms, including human, two viruses (HIV and influenza virus), and bacteria (B. melitensis strain 16M, E. coli strain K-12 substrain MG1655, M. tuberculosis strain H37Rv, and P. aeruginosa strain PAO1). More OGG information for other organisms (e.g., mouse, zebrafish, fruit fly, yeast, etc.) may be found in other OGG subsets. obo:ogg.owl OWL-DL obo:ogg.owl http://creativecommons.org/licenses/by/3.0/ obo:ogg.owl A biological ontology in the area of genes and genomes. obo:ogg.owl OGG: Ontology of Genes and Genomes obo:ogg.owl Vision Release: 1.0.59 obo:ogg.owl mailto:yongqunh@med.umich.edu obo:ncbitaxon#has_rank A metadata relation between a class and its taxonomic rank (eg species, family) obo:ncbitaxon#has_rank ncbi_taxonomy obo:ncbitaxon#has_rank has_rank obo:pr#has_gene_template has_gene_template oboInOwl:hasAlternativeId has_alternative_id oboInOwl:hasBroadSynonym has_broad_synonym oboInOwl:hasDbXref database_cross_reference oboInOwl:hasExactSynonym A property representing a fully qualified synonym, contains the string, term type, source, and an optional source code if appropriate. Each subfield is deliniated to facilitate interpretation by software. oboInOwl:hasExactSynonym FULL_SYN oboInOwl:hasExactSynonym Synonym with Source Data oboInOwl:hasExactSynonym has exact synonym oboInOwl:hasExactSynonym has_exact_synonym oboInOwl:hasNarrowSynonym has_narrow_synonym oboInOwl:hasOBONamespace has_obo_namespace oboInOwl:hasRelatedSynonym has_related_synonym oboInOwl:inSubset An association that connects the concept defining a particular terminology subset with concepts that belong to this subset. oboInOwl:inSubset Concept_In_Subset oboInOwl:inSubset in subset oboInOwl:inSubset in_subset rdfs:label label obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:pr.owl obo:ogg.owl obo:ogg.owl obo:go.owl obo:ogg.owl obo:ogg.owl obo:ogg.owl obo:ogg.owl obo:ogg.owl obo:ogg.owl obo:ogg.owl obo:ogg.owl obo:ogg.owl obo:ogg.owl obo:go.owl obo:ogg.owl obo:ogg.owl obo:pr.owl obo:ogg.owl obo:ogg.owl obo:ogg.owl obo:ogg.owl obo:ogg.owl obo:pr.owl obo:ogg.owl obo:go.owl obo:ogg.owl obo:ogg.owl obo:ogg.owl obo:pr.owl obo:ogg.owl obo:ogg.owl obo:ogg.owl obo:ogg.owl obo:ogg.owl obo:ogg.owl obo:go.owl obo:ogg.owl obo:ogg.owl obo:ogg.owl obo:ogg.owl obo:ogg.owl obo:ogg.owl obo:ogg.owl obo:ogg.owl obo:ogg.owl obo:ogg.owl obo:go.owl obo:ogg.owl obo:ogg.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl 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obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl obo:go.owl xsd:boolean xsd:string obo:NCIT_Semantic_Type-enum xsd:string xsd:string xsd:string xsd:string xsd:string obo:OGG_0000000002