OTCS is a biological ontology of Two Component Systems.
Hsin-Hui Huang
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
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Tigecycline is an glycylcycline antibiotic. It works by inhibiting action of the prokaryotic 30S ribosome.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Tetracycline is a broad-spectrum polyketide antibiotic produced by many Streptomyces. It works by inhibiting action of the prokaryotic 30S ribosome.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Ertapenem is a carbapenem antibiotic and is highly resistant to beta-lactamases like other carbapenems. It inhibits bacterial cell wall synthesis.
Levofloxacin is a synthetic chemotherapeutic antibiotic of the fluoroquinolone drug class. Its main target is topoisomerase IV, inhibiting its function and disrupting DNA replication.
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.
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.
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.
Mutational alteration or enzymatic modification of antibiotic target which results in antibiotic resistance.
Protection of antibiotic action target from antibiotic binding, which process will result in antibiotic resistance.
Enzymatic inactivation of antibiotic to confer drug resistance.
Antibiotic resistance via the transport of antibiotics out of the cell.
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.
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.
Ristocetin is a glycopeptide antibiotic similar to vancomycin but positively charged. It is not used clinically because it induces platelet agglutination.
These antibiotics are derived from tetracycline, a polyketide antibiotic that inhibits the 30S subunit of bacterial ribosomes.
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.
A47934 is an 'aglycone' glycopeptide antibiotic produced by Streptomyces toyocaensis. It is a teicoplanin-like glycopeptide.
Balhimycin is a vancomycin-like glycopeptide antibiotic produced by Amycolatopsis balhimycina. It binds to the terminal Lys-D-Ala-D-Ala of peptidoglycan precursors.
Tylosin is a 16-membered macrolide, naturally produced by Streptomyces fradiae. It interacts with the bacterial ribosome 50S subunit to inhibit protein synthesis.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Reduction in permeability to antibiotic, generally through reduced production of porins, can provide resistance.
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.
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.
Tetroxoprim is a trimethoprim derivative that inhibits bacterial dihydrofolate reductase.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
A40926 is a glycopeptide antibiotic produced by Nonomuraea sp. ATCC 39727. It is precusor of the second-generation glycopeptide antibiotic dalbavancin.
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.
Rifabutin is a semisynthetic rifamycin used in tuberculosis therapy. It inhibits DNA-dependent RNA synthesis.
Rifapentine is a semisynthetic rifamycin that inhibits DNA-dependent RNA synthesis. It is often used in the treatment of tuberculosis and leprosy.
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.
Colistin A, or polymyxin E1, has a 6-octanoic acid lipid tail. Polymyxins disrupt the cell membrane of Gram-negative bacteria.
Colistin B, or polymyxin E2, has a 6-heptanoic acid lipid tail. Polymyxins disrupt the cell membrane of Gram-negative bacteria.
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.
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.
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.
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.
Benzylpenicillin, commonly referred to as penicillin G, is effective against both Gram-positive and Gram-negative bacteria. It is unstable in acid.
Phenoxymethylpenicillin, or penicillin V, is a penicillin derivative that is acid stable but less active than benzylpenicillin (penicillin G).
Propicillin is an orally taken penicillin derivative that has high absorption but poor activity.
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.
Flucloxacillin is similar to cloxacillin, with an extra additional fluorine atom.
Ampicillin is a penicillin derivative that is highly acid stable, with its activity similar to benzylpenicillin.
Azlocillin is a semisynthetic derivative of penicillin that is notably active against Ps. aeruginosa and other Gram-negative bacteria.
Mezlocillin is a penicillin derivative taken parenterally.
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.
Cefalexin is a cephalosporin antibiotic that causes filamentation. It is resistant to staphylococcal beta-lactamase, but degraded by enterobacterial beta-lactamases.
Cefadroxil, or p-hydroxycephalexin, is an cephalosporin antibiotic similar to cefalexin.
Cefotiam is a cephalosporin antibiotic with similar activity to cefuroxime but more active against enterobacteria. It is consumed orally as the prodrug cefotiam hexetil.
Cefaclor is a semisynthetic cephalosporin derived from cephalexin. It has broad-spectrum antibiotic activity.
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.
Cefixime is a cephalosporin resistant to most beta-lactamases. It is active against many enterobacteria, but activity against staphylococci is poor.
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.
Ceftibuten is a semisynthetic cephalosporin active against Gram-negative bacilli. It is resistant against many plasmid-mediated beta-lactamases.
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.
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.
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.
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.
A gentamicin class aminoglycoside antibiotic often used in mammalian cell culture work as a selectable marker for the neo cassette (APH3').
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.
Gentamicin B is a semisynthetic aminoglycoside antibacterial.
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.
Lividomycins are aminoglycosidic antibiotics produced by Streptomyces lividus. They contain 2-amino-2,3-dideoxy-D-glucose.
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.
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.
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.
Norfloxacin is a 6-fluoro, 7-piperazinyl quinolone with a wide range of activity against Gram-negative bacteria. It is inactive against most anaerobes.
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.
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.
Grepafloxacin is a broad-spectrum antibacterial quinoline. It is no longer taken due to its high toxicity.
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.
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.
Oxytetracycline is a derivative of tetracycline with a 5-hydroxyl group. Its activity is similar to other tetracyclines.
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.
Mafenide is a sulfonamide used topically for treating burns.
Bleomycinic acid is a glycopeptide antibiotic produced by Streptomyces verticillus taken as a mixture of bleomycins. It induces stand breaks in bacterial nucleic acids.
Bleomycin A2 is a glycopeptide antibiotic produced by Streptomyces verticillus taken as a mixture of bleomycins. It induces stand breaks in bacterial nucleic acids.
Bleomycin B2 is a glycopeptide antibiotic produced by Streptomyces verticillus taken as a mixture of bleomycins. It induces stand breaks in bacterial nucleic acids.
Sulfasalazine is a derivative of the early sulfonamide sulfapyridine (salicylazosulfapyridine). It was developed to increase water solubility and is taken orally for ulcerative colitis.
Sulfamethizole is a short-acting sulfonamide that inhibits dihydropteroate synthetase.
Lividomycin A is a pentasaccharide antibiotic which interferes with bacterial protein synthesis.
Lividomycin B is a derivative of lividomycin A with a removed mannose group (demannosyllividomycin A). Livodomycins interfere with bacterial protein synthesis.
Cefalotin is a semisynthetic cephalosporin antibiotic activate against staphylococci. It is resistant to staphylococci beta-lactamases but hydrolyzed by enterobacterial beta-lactamases.
Isopenicillin N is a natural penicillin derivative produced by Penicillium chrysogenum with activity similar to penicillin N.
Penicillin N is a penicillin derivative produced by Cephalosporium acremonium.
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).
Pefloxacin is structurally and functionally similar to norfloxacin. It is poorly active against mycobacteria, while anaerobes are resistant.
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.
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.
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.
A macrolide antibiotic from Streptomyces narbonensis subsp. josamyceticus. The drug has antimicrobial activity against a wide spectrum of pathogens.
Produced by Micromonospora griseorubida.
Kitasamycin is a macrolide antibiotic and is produced by Streptoverticillium kitasatoense. The drug has antimicrobial activity against a wide spectrum of pathogens.
Produced by Streptomyces halstedii and Streptomyces thermotolerans.
Produced by Streptomyces venezuelae ATCC 15439.
A gentamicin-group aminoglycoside isolated from Micromonospora.
A semisynthetic genamicin-group aminoglycoside, derived from verdamicin.
An unusual aminoglycoside because the cyclitol ring is not amino substituted; it was discovered as a fermentation product of Streptomyces kasugaensis.
CTX-M-15 is a beta-lactamase found in the Enterobacteriaceae family
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.
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.
Rokitamycin is a macrolide antibiotic. Synthesized from strains of Streptomyces kitasatoensis.
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.
Faropenem is an orally active beta-lactam antibiotic belonging to the penem group.
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.
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.
Temocillin is a beta-lactamase resistant carboxypenicillin. It is primarily used for the treatment of multiple drug resistant, Gram-negative bacteria, specifically Enterobacteriaceae.
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.
a 5th generation cephalosporin antibiotic
a aminomethylcycline antibiotic that targets 16s rRNA in gram positive and gram negative bacteria
A clinically developed Macrolide antibiotic targeting gram positive and gram negative bacteria.
A fluorocycline that acts to inhibit the bacterial ribosome.
Capreomycin is an aminoglycoside antibiotic, capable of treating a large number of infections but in particular used for killing bacteria causing tuberculosis.
Cefamandole is a second-generation cephalosporin-class beta-lactam antibiotic.
Cefetamet is a third-generation semi-synthetic beta-lactam antibiotic that inactivates inner cell wall PBPs through targeting binding, resulting in cell lysis.
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.
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.
Cefoperazone is a semi-synthetic cephalosporin containing a tetrazolyl moiety that is resistant to beta-lactamases. Particularly used for treatment of Pseudomonas spp. infections.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Flomoxef is a second-generation cephamycin (oxacephem) and beta-lactam antibiotic.
Gentamicin A is part of a complex of broad spectrum aminoglycoside antibiotics. Gentamicin inhibits protein synthesis, resulting in bacterial cell death.
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.
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.
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.
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).
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.
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.
1-cyclopropyl-6-fluoro-1,4-dihydro-8-methoxy-7-(3-methylaminopiperidine-1-yl)-4-oxoquinoline-3-carboxylic acid
EBR beta-lactamases are Class B beta-lactamases first isolated from Empedobacter brevis and are able to hydrolyze penicillins, cephalosporins, and carbapenems.
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.
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.
EBR-2 is a novel EBR-like class B beta-lactamase isolated from an extensively drug-resistant strain of Empedobacter falsenii
A carbapenem antibiotic, administered as the oral drug tebipenem-pivoxil, shown to be effective at treating bacterial infections.
A siderophore cephalosporin with antibiotic activity against Gram-negative pathogens including and specifically Pseudomonas aeruginosa.
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.
Tosufloxacin is a fluoroquinolone antibiotic with an extended spectrum of activity.
Rifalazil is a rifamycin derivative antibiotic, sometimes used for treating Clostridioides difficile infections.
Julius Caesar
Verdi’s Requiem
the Second World War
your body mass index
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
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
An entity is anything that exists or has existed or will exist. (axiom label in BFO2 Reference: [001-001])
entity
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
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
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])
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])
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])
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])
(forall (x y) (if (and (Continuant x) (exists (t) (continuantPartOfAt y x t))) (Continuant y))) // axiom label in BFO2 CLIF: [009-002]
(forall (x y) (if (and (Continuant x) (exists (t) (hasContinuantPartOfAt y x t))) (Continuant y))) // axiom label in BFO2 CLIF: [126-001]
(forall (x) (if (Continuant x) (Entity x))) // axiom label in BFO2 CLIF: [008-002]
(forall (x) (if (Material Entity x) (exists (t) (and (TemporalRegion t) (existsAt x t))))) // axiom label in BFO2 CLIF: [011-002]
continuant
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
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.
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.
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.
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])
Every occurrent occupies_spatiotemporal_region some spatiotemporal region. (axiom label in BFO2 Reference: [108-001])
b is an occurrent entity iff b is an entity that has temporal parts. (axiom label in BFO2 Reference: [079-001])
(forall (x) (if (Occurrent x) (exists (r) (and (SpatioTemporalRegion r) (occupiesSpatioTemporalRegion x r))))) // axiom label in BFO2 CLIF: [108-001]
(forall (x) (iff (Occurrent x) (and (Entity x) (exists (y) (temporalPartOf y x))))) // axiom label in BFO2 CLIF: [079-001]
occurrent
a chair
a heart
a leg
a molecule
a spatial region
an atom
an orchestra.
an organism
the bottom right portion of a human torso
the interior of your mouth
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])
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])
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])
(forall (x t) (if (IndependentContinuant x) (exists (r) (and (SpatialRegion r) (locatedInAt x r t))))) // axiom label in BFO2 CLIF: [134-001]
(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]
(iff (IndependentContinuant a) (and (Continuant a) (not (exists (b t) (specificallyDependsOnAt a b t))))) // axiom label in BFO2 CLIF: [017-002]
independent continuant
BFO 2 Reference: Spatial regions do not participate in processes.
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.
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])
All continuant parts of spatial regions are spatial regions. (axiom label in BFO2 Reference: [036-001])
(forall (x y t) (if (and (SpatialRegion x) (continuantPartOfAt y x t)) (SpatialRegion y))) // axiom label in BFO2 CLIF: [036-001]
(forall (x) (if (SpatialRegion x) (Continuant x))) // axiom label in BFO2 CLIF: [035-001]
spatial region
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
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])
All parts of temporal regions are temporal regions. (axiom label in BFO2 Reference: [101-001])
Every temporal region t is such that t occupies_temporal_region t. (axiom label in BFO2 Reference: [119-002])
(forall (r) (if (TemporalRegion r) (occupiesTemporalRegion r r))) // axiom label in BFO2 CLIF: [119-002]
(forall (x y) (if (and (TemporalRegion x) (occurrentPartOf y x)) (TemporalRegion y))) // axiom label in BFO2 CLIF: [101-001]
(forall (x) (if (TemporalRegion x) (Occurrent x))) // axiom label in BFO2 CLIF: [100-001]
temporal region
an infinitely thin plane in space.
the surface of a sphere-shaped part of space
A two-dimensional spatial region is a spatial region that is of two dimensions. (axiom label in BFO2 Reference: [039-001])
(forall (x) (if (TwoDimensionalSpatialRegion x) (SpatialRegion x))) // axiom label in BFO2 CLIF: [039-001]
two-dimensional spatial region
the spatiotemporal region occupied by a human life
the spatiotemporal region occupied by a process of cellular meiosis.
the spatiotemporal region occupied by the development of a cancer tumor
A spatiotemporal region is an occurrent entity that is part of spacetime. (axiom label in BFO2 Reference: [095-001])
All parts of spatiotemporal regions are spatiotemporal regions. (axiom label in BFO2 Reference: [096-001])
Each spatiotemporal region at any time t projects_onto some spatial region at t. (axiom label in BFO2 Reference: [099-001])
Each spatiotemporal region projects_onto some temporal region. (axiom label in BFO2 Reference: [098-001])
Every spatiotemporal region occupies_spatiotemporal_region itself.
Every spatiotemporal region s is such that s occupies_spatiotemporal_region s. (axiom label in BFO2 Reference: [107-002])
(forall (r) (if (SpatioTemporalRegion r) (occupiesSpatioTemporalRegion r r))) // axiom label in BFO2 CLIF: [107-002]
(forall (x t) (if (SpatioTemporalRegion x) (exists (y) (and (SpatialRegion y) (spatiallyProjectsOntoAt x y t))))) // axiom label in BFO2 CLIF: [099-001]
(forall (x y) (if (and (SpatioTemporalRegion x) (occurrentPartOf y x)) (SpatioTemporalRegion y))) // axiom label in BFO2 CLIF: [096-001]
(forall (x) (if (SpatioTemporalRegion x) (Occurrent x))) // axiom label in BFO2 CLIF: [095-001]
(forall (x) (if (SpatioTemporalRegion x) (exists (y) (and (TemporalRegion y) (temporallyProjectsOnto x y))))) // axiom label in BFO2 CLIF: [098-001]
spatiotemporal region
a process of cell-division, \ a beating of the heart
a process of meiosis
a process of sleeping
the course of a disease
the flight of a bird
the life of an organism
your process of aging.
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])
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)
(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]
process
an atom of element X has the disposition to decay to an atom of element Y
certain people have a predisposition to colon cancer
children are innately disposed to categorize objects in certain ways.
the cell wall is disposed to filter chemicals in endocitosis and exocitosis
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
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])
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])
(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]
(forall (x) (if (Disposition x) (and (RealizableEntity x) (exists (y) (and (MaterialEntity y) (bearerOfAt x y t)))))) // axiom label in BFO2 CLIF: [062-002]
disposition
the disposition of this piece of metal to conduct electricity.
the disposition of your blood to coagulate
the function of your reproductive organs
the role of being a doctor
the role of this boundary to delineate where Utah and Colorado meet
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])
All realizable dependent continuants have independent continuants that are not spatial regions as their bearers. (axiom label in BFO2 Reference: [060-002])
(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]
(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]
realizable entity
A zero-dimensional spatial region is a point in space. (axiom label in BFO2 Reference: [037-001])
(forall (x) (if (ZeroDimensionalSpatialRegion x) (SpatialRegion x))) // axiom label in BFO2 CLIF: [037-001]
zero-dimensional spatial region
the ambient temperature of this portion of air
the color of a tomato
the length of the circumference of your waist
the mass of this piece of gold.
the shape of your nose
the shape of your nostril
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])
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])
(forall (x) (if (Quality x) (SpecificallyDependentContinuant x))) // axiom label in BFO2 CLIF: [055-001]
(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]
quality
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
of one-sided specifically dependent continuants: the mass of this tomato
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.
the disposition of this fish to decay
the function of this heart: to pump blood
the mutual dependence of proton donors and acceptors in chemical reactions [79
the mutual dependence of the role predator and the role prey as played by two organisms in a given interaction
the pink color of a medium rare piece of grilled filet mignon at its center
the shape of this hole.
the smell of this portion of mozzarella
b is a relational specifically dependent continuant = Def. b is a specifically dependent continuant and there are n > 1 independent continuants c1, … cn which are not spatial regions are such that for all 1 i < 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])
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])
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.
(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]
(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]
specifically dependent continuant
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.
the priest role
the role of a boundary to demarcate two neighboring administrative territories
the role of a building in serving as a military target
the role of a stone in marking a property boundary
the role of subject in a clinical trial
the student role
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.
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])
(forall (x) (if (Role x) (RealizableEntity x))) // axiom label in BFO2 CLIF: [061-001]
role
an edge of a cube-shaped portion of space.
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])
(forall (x) (if (OneDimensionalSpatialRegion x) (SpatialRegion x))) // axiom label in BFO2 CLIF: [038-001]
one-dimensional spatial region
a cube-shaped region of space
a sphere-shaped region of space,
A three-dimensional spatial region is a spatial region that is of three dimensions. (axiom label in BFO2 Reference: [040-001])
(forall (x) (if (ThreeDimensionalSpatialRegion x) (SpatialRegion x))) // axiom label in BFO2 CLIF: [040-001]
three-dimensional spatial region
Manhattan Canyon)
a hole in the interior of a portion of cheese
a rabbit hole
an air traffic control region defined in the airspace above an airport
the Grand Canyon
the Piazza San Marco
the cockpit of an aircraft
the hold of a ship
the interior of a kangaroo pouch
the interior of the trunk of your car
the interior of your bedroom
the interior of your office
the interior of your refrigerator
the lumen of your gut
your left nostril (a fiat part – the opening – of your left nasal cavity)
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])
(forall (x) (if (Site x) (ImmaterialEntity x))) // axiom label in BFO2 CLIF: [034-002]
site
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.
the pdf file on your laptop, the pdf file that is a copy thereof on my laptop
the sequence of this protein molecule; the sequence that is a copy thereof in that protein molecule.
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])
(iff (GenericallyDependentContinuant a) (and (Continuant a) (exists (b t) (genericallyDependsOnAt a b t)))) // axiom label in BFO2 CLIF: [074-001]
generically dependent continuant
the function of a hammer to drive in nails
the function of a heart pacemaker to regulate the beating of a heart through electricity
the function of amylase in saliva to break down starch into sugar
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.
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])
(forall (x) (if (Function x) (Disposition x))) // axiom label in BFO2 CLIF: [064-001]
function
the boundary between the 2nd and 3rd year of your life.
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])
Every process boundary occupies_temporal_region a zero-dimensional temporal region. (axiom label in BFO2 Reference: [085-002])
(forall (x) (if (ProcessBoundary x) (exists (y) (and (ZeroDimensionalTemporalRegion y) (occupiesTemporalRegion x y))))) // axiom label in BFO2 CLIF: [085-002]
(iff (ProcessBoundary a) (exists (p) (and (Process p) (temporalPartOf a p) (not (exists (b) (properTemporalPartOf b a)))))) // axiom label in BFO2 CLIF: [084-001]
process boundary
the temporal region during which a process occurs.
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).
A one-dimensional temporal region is a temporal region that is extended. (axiom label in BFO2 Reference: [103-001])
(forall (x) (if (OneDimensionalTemporalRegion x) (TemporalRegion x))) // axiom label in BFO2 CLIF: [103-001]
one-dimensional temporal region
a flame
a forest fire
a human being
a hurricane
a photon
a puff of smoke
a sea wave
a tornado
an aggregate of human beings.
an energy wave
an epidemic
the undetached arm of a human being
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
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.
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.
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])
Every entity which has a material entity as continuant part is a material entity. (axiom label in BFO2 Reference: [020-002])
every entity of which a material entity is continuant part is also a material entity. (axiom label in BFO2 Reference: [021-002])
(forall (x) (if (MaterialEntity x) (IndependentContinuant x))) // axiom label in BFO2 CLIF: [019-002]
(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]
(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]
material entity
part of
has part
has_part
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])
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)'.
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.)
BFO2 Reference: independent continuant that is not a spatial region
BFO2 Reference: specifically dependent continuant
(iff (inheresInAt a b t) (and (DependentContinuant a) (IndependentContinuant b) (not (SpatialRegion b)) (specificallyDependsOnAt a b t))) // axiom label in BFO2 CLIF: [051-002]
inheres in at all times
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])
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)
(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]
bearer of at some time
[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])
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])
(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]
realized in
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])
(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]
realizes
[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)
[copied from inverse property 'has participant at some time'] BFO 2 Reference: Spatial regions do not participate in processes.
[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
[copied from inverse property 'has participant at some time'] BFO2 Reference: process
[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])
participates 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 'has participant at some time@en' is: exists t, exists_at(x,t) & exists_at(y,t) & 'has participant@en'(x,y,t)
BFO2 Reference: independent continuant that is not a spatial region, specifically dependent continuant, generically dependent continuant
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])
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])
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])
if b has_participant c at t then b is an occurrent. (axiom label in BFO2 Reference: [087-001])
if b has_participant c at t then c exists at t. (axiom label in BFO2 Reference: [089-001])
if b has_participant c at t then c is a continuant. (axiom label in BFO2 Reference: [088-001])
(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]
(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]
(forall (x y t) (if (hasParticipantAt x y t) (Continuant y))) // axiom label in BFO2 CLIF: [088-001]
(forall (x y t) (if (hasParticipantAt x y t) (Occurrent x))) // axiom label in BFO2 CLIF: [087-001]
(forall (x y t) (if (hasParticipantAt x y t) (existsAt y t))) // axiom label in BFO2 CLIF: [089-001]
has participant at some time
[copied from inverse property 'concretizes at some time'] You may concretize a piece of software by installing it in your computer
[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.
[copied from inverse property 'concretizes at some time'] you may concretize a poem as a pattern of memory traces in your head
[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)
[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])
concretized by at some time
You may concretize a piece of software by installing it in your computer
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.
you may concretize a poem as a pattern of memory traces in your head
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)
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])
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])
(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]
(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]
concretizes at some time
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
occurs in
[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
contains process
A pain s-depends_on the organism that is experiencing the pain
a gait s-depends_on the walking object. (All at some specific time.)
a shape s-depends_on the shaped object
one-sided s-dependence of a dependent continuant on an independent continuant: an instance of headache s-depends_on some head
one-sided s-dependence of a dependent continuant on an independent continuant: an instance of temperature s-depends_on some organism
one-sided s-dependence of a process on something: a process of cell death s-depends_on a cell
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
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
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
one-sided s-dependence of one occurrent on multiple independent continuants: a relational process of hitting a ball with a cricket bat
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
reciprocal s-dependence between occurrents: a process of buying and the associated process of selling
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
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
the one-sided dependence of an occurrent on an independent continuant: football match on the players, the ground, the ball
the one-sided dependence of an occurrent on an independent continuant: handwave on a hand
the three-sided reciprocal s-dependence of the hue, saturation and brightness of a color [45
the three-sided reciprocal s-dependence of the pitch, timbre and volume of a tone [45
the two-sided reciprocal s-dependence of the roles of husband and wife [20
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)'.
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
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
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.
BFO2 Reference: specifically dependent continuant\; process; process boundary
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
If b is s-depends_on something at some time, then b is not a material entity. (axiom label in BFO2 Reference: [052-001])
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])
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])
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])
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])
(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]
(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]
(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]
(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]
(forall (x) (if (exists (y t) (specificallyDependsOnAt x y t)) (not (MaterialEntity x)))) // axiom label in BFO2 CLIF: [052-001]
specifically depends on at all times
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])
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)'.
(iff (functionOf a b t) (and (Function a) (inheresInAt a b t))) // axiom label in BFO2 CLIF: [067-001]
function of at all times
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])
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)'.
(iff (qualityOfAt a b t) (and (Quality a) (IndependentContinuant b) (not (SpatialRegion b)) (specificallyDependsOnAt a b t))) // axiom label in BFO2 CLIF: [056-002]
quality of at all times
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])
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)'.
(iff (roleOfAt a b t) (and (Role a) (inheresInAt a b t))) // axiom label in BFO2 CLIF: [065-001]
role of at all times
Mary located_in Salzburg
the Empire State Building located_in New York.
this portion of cocaine located_in this portion of blood
this stem cell located_in this portion of bone marrow
your arm located_in your body
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])
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)'.
Located_in is transitive. (axiom label in BFO2 Reference: [046-001])
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])
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])
(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]
(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]
(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]
(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]
located in 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 '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)
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])
every region r is occupies_spatial_region r at all times. (axiom label in BFO2 Reference: [042-002])
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])
(forall (r t) (if (Region r) (occupiesSpatialRegionAt r r t))) // axiom label in BFO2 CLIF: [042-002]
(forall (x r t) (if (occupiesSpatialRegionAt x r t) (and (SpatialRegion r) (IndependentContinuant x)))) // axiom label in BFO2 CLIF: [041-002]
(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]
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 '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)
BFO2 Reference: generically dependent continuant
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])
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])
(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]
generically depends on at some time
a has_function b at t =Def. b function_of a at t. (axiom label in BFO2 Reference: [070-001])
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)
(iff (hasFunctionAt a b t) (functionOf b a t)) // axiom label in BFO2 CLIF: [070-001]
has function at some time
has quality at some time
a has_role b at t =Def. b role_of a at t. (axiom label in BFO2 Reference: [068-001])
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)
(iff (hasRoleAt a b t) (roleOfAt b a t)) // axiom label in BFO2 CLIF: [068-001]
has role at some time
[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)
[copied from inverse property 'generically depends on at some time'] BFO2 Reference: generically dependent continuant
[copied from inverse property 'generically depends on at some time'] BFO2 Reference: independent continuant
[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])
has generic dependent at some time
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])
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)'.
(iff (dispositionOf a b t) (and (Disposition a) (inheresInAt a b t))) // axiom label in BFO2 CLIF: [066-001]
disposition of at all times
b exists_at t means: b is an entity which exists at some temporal region t. (axiom label in BFO2 Reference: [118-002])
exists at
[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)
b has_continuant_part c at t = Def. c continuant_part_of b at t. (axiom label in BFO2 Reference: [006-001])
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)'.
[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'
(iff (hasContinuantPartAt a b t) (continuantPartOfAt b a t)) // axiom label in BFO2 CLIF: [006-001]
has continuant part at all times
b has_proper_continuant_part c at t = Def. c proper_continuant_part_of b at t. [XXX-001
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)'.
has proper continuant part at all times
a has_disposition b at t =Def. b disposition_of a at t. (axiom label in BFO2 Reference: [069-001])
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)
(iff (hasDispositionAt a b t) (dispositionOf b a t)) // axiom label in BFO2 CLIF: [069-001]
has disposition at some time
the material basis of John’s disposition to cough is the viral infection in John’s upper respiratory tract
the material basis of the disposition to wear unevenly of John’s tires is the worn suspension of his car.
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)'.
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])
(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]
has material basis at all times
[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.
[copied from inverse property 'member part of at some time'] each tree in a forest is a member_part of the forest
[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 > 1) with b = xi for some 1 ? i ? n. (axiom label in BFO2 Reference: [026-004])
[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)
[copied from inverse property 'member part of at some time'] BFO2 Reference: object
[copied from inverse property 'member part of at some time'] BFO2 Reference: object aggregate
has member part at some time
[copied from inverse property 'part of occurrent'] Mary’s 5th birthday occurrent_part_of Mary’s life
[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.
[copied from inverse property 'part of occurrent'] the first set of the tennis match occurrent_part_of the tennis match.
b has_occurrent_part c = Def. c occurrent_part_of b. (axiom label in BFO2 Reference: [007-001])
[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.
[copied from inverse property 'part of occurrent'] BFO2 Reference: occurrent
[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])
(iff (hasOccurrentPart a b) (occurrentPartOf b a)) // axiom label in BFO2 CLIF: [007-001]
has occurrent part
[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])
b has_proper_occurrent_part c = Def. c proper_occurrent_part_of b. [XXX-001
has proper occurrent part
has profile
[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
[copied from inverse property 'temporal part of'] the process boundary which separates the 3rd and 4th years of your life.
[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
[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])
[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])
has temporal part
[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)
[copied from inverse property 'occupies spatial region at some time'] BFO2 Reference: independent continuant
[copied from inverse property 'occupies spatial region at some time'] BFO2 Reference: spatial region
[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])
has spatial occupant at some time
[copied from inverse property 'located in at some time'] Mary located_in Salzburg
[copied from inverse property 'located in at some time'] the Empire State Building located_in New York.
[copied from inverse property 'located in at some time'] this portion of cocaine located_in this portion of blood
[copied from inverse property 'located in at some time'] this stem cell located_in this portion of bone marrow
[copied from inverse property 'located in at some time'] your arm located_in your body
[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])
[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)
[copied from inverse property 'located in at some time'] BFO2 Reference: independent continuant
has location at some time
[copied from inverse property 'specifically depends on at some time'] A pain s-depends_on the organism that is experiencing the pain
[copied from inverse property 'specifically depends on at some time'] a gait s-depends_on the walking object. (All at some specific time.)
[copied from inverse property 'specifically depends on at some time'] a shape s-depends_on the shaped object
[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
[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
[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
[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
[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
[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
[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
[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
[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
[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
[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
[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
[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
[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
[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
[copied from inverse property 'specifically depends on at some time'] the two-sided reciprocal s-dependence of the roles of husband and wife [20
[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)
[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
[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
[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.
[copied from inverse property 'specifically depends on at some time'] BFO2 Reference: specifically dependent continuant\; process; process boundary
[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
has specific dependent at some time
[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.
[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])
has spatiotemporal occupant
material basis 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.
each tree in a forest is a member_part of the forest
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 > 1) with b = xi for some 1 ? i ? n. (axiom label in BFO2 Reference: [026-004])
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)
if b member_part_of c at t then b continuant_part_of c at t. (axiom label in BFO2 Reference: [104-001])
(forall (x y t) (if (memberPartOfAt x y t) (continuantPartOfAt x y t))) // axiom label in BFO2 CLIF: [104-001]
member part of at some time
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.
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])
occupies spatiotemporal region
Mary’s 5th birthday occurrent_part_of Mary’s life
The process of a footballer’s heart beating once is an occurrent part but not a temporal_part of a game of football.
the first set of the tennis match occurrent_part_of the tennis match.
[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])
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.
b occurrent_part_of c =Def. b is a part of c & b and c are occurrents. (axiom label in BFO2 Reference: [003-002])
occurrent_part_of is antisymmetric. (axiom label in BFO2 Reference: [123-001])
occurrent_part_of is reflexive (every occurrent entity is an occurrent_part_of itself). (axiom label in BFO2 Reference: [113-002])
occurrent_part_of is transitive. (axiom label in BFO2 Reference: [112-001])
occurrent_part_of satisfies unique product. (axiom label in BFO2 Reference: [125-001])
occurrent_part_of satisfies weak supplementation. (axiom label in BFO2 Reference: [124-001])
(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]
(forall (x y t) (if (and (occurrentPartOf x y t) (occurrentPartOf y x t)) (= x y))) // axiom label in BFO2 CLIF: [123-001]
(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]
(forall (x y z) (if (and (occurrentPartOf x y) (occurrentPartOf y z)) (occurrentPartOf x z))) // axiom label in BFO2 CLIF: [112-001]
(forall (x) (if (Occurrent x) (occurrentPartOf x x))) // axiom label in BFO2 CLIF: [113-002]
part of occurrent
process profile of
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])
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])
proper temporal part of
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])
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)'.
(iff (properContinuantPartOfAt a b t) (and (continuantPartOfAt a b t) (not (= a b)))) // axiom label in BFO2 CLIF: [004-001]
proper part of continuant at all times
[copied from inverse property 'has proper occurrent part'] b has_proper_occurrent_part c = Def. c proper_occurrent_part_of b. [XXX-001
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])
(iff (properOccurrentPartOf a b) (and (occurrentPartOf a b) (not (= a b)))) // axiom label in BFO2 CLIF: [005-001]
proper part of occurrent
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
the process boundary which separates the 3rd and 4th years of your life.
your heart beating from 4pm to 5pm today is a temporal part of the process of your heart beating
b proper_temporal_part_of c =Def. b temporal_part_of c & not (b = c). (axiom label in BFO2 Reference: [116-001])
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])
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])
(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]
(iff (properTemporalPartOf a b) (and (temporalPartOf a b) (not (= a b)))) // axiom label in BFO2 CLIF: [116-001]
(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]
temporal part of
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])
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.
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
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.
Every continuant fiat boundary is located at some spatial region at every time at which it exists
(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]
continuant fiat boundary
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
immaterial entity
The Equator
all geopolitical boundaries
all lines of latitude and longitude
the line separating the outer surface of the mucosa of the lower lip from the outer surface of the skin of the chin.
the median sulcus of your tongue
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])
(iff (OneDimensionalContinuantFiatBoundary a) (and (ContinuantFiatBoundary a) (exists (b) (and (OneDimensionalSpatialRegion b) (forall (t) (locatedInAt a b t)))))) // axiom label in BFO2 CLIF: [032-001]
one-dimensional continuant fiat boundary
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
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.
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.
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])
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])
(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]
(iff (ProcessProfile a) (exists (b) (and (Process b) (processProfileOf a b)))) // axiom label in BFO2 CLIF: [093-002]
process profile
a marriage bond, an instance of love, an obligation between one person and another.
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])
(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]
relational quality
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])
(iff (TwoDimensionalContinuantFiatBoundary a) (and (ContinuantFiatBoundary a) (exists (b) (and (TwoDimensionalSpatialRegion b) (forall (t) (locatedInAt a b t)))))) // axiom label in BFO2 CLIF: [033-001]
two-dimensional continuant fiat boundary
the geographic North Pole
the point of origin of some spatial coordinate system.
the quadripoint where the boundaries of Colorado, Utah, New Mexico, and Arizona meet
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.
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])
(iff (ZeroDimensionalContinuantFiatBoundary a) (and (ContinuantFiatBoundary a) (exists (b) (and (ZeroDimensionalSpatialRegion b) (forall (t) (locatedInAt a b t)))))) // axiom label in BFO2 CLIF: [031-001]
zero-dimensional continuant fiat boundary
a temporal region that is occupied by a process boundary
right now
the moment at which a child is born
the moment at which a finger is detached in an industrial accident
the moment of death.
temporal instant.
A zero-dimensional temporal region is a temporal region that is without extent. (axiom label in BFO2 Reference: [102-001])
(forall (x) (if (ZeroDimensionalTemporalRegion x) (TemporalRegion x))) // axiom label in BFO2 CLIF: [102-001]
zero-dimensional temporal region
projects onto spatial region at some time
spatial projection of spatiotemporal at some time
projects onto temporal region
temporal projection of spatiotemporal
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])
occupies temporal region
[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])
has temporal occupant
[copied from inverse property 'exists at'] BFO2 Reference: entity
[copied from inverse property 'exists at'] BFO2 Reference: temporal region
[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])
during which exists
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)'.
bearer of at all times
has quality 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 function at all times@en' is: forall(t) exists_at(x,t) -> exists_at(y,t) and 'has function@en(x,y,t)'.
has function 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 role at all times@en' is: forall(t) exists_at(x,t) -> exists_at(y,t) and 'has role@en(x,y,t)'.
has role 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 disposition at all times@en' is: forall(t) exists_at(x,t) -> exists_at(y,t) and 'has disposition@en(x,y,t)'.
has disposition at all times
material basis of 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 'concretizes at all times@en' is: forall(t) exists_at(x,t) -> exists_at(y,t) and 'concretizes@en(x,y,t)'.
concretizes at all times
concretized by at all times
participates in 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 participant at all times@en' is: forall(t) exists_at(x,t) -> exists_at(y,t) and 'has participant@en(x,y,t)'.
has participant at all times
has specific dependent 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 '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)
specifically depends on at some time
has location 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 'located in at some time@en' is: exists t, exists_at(x,t) & exists_at(y,t) & 'located in@en'(x,y,t)
located in at some time
has member 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 '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)'.
member part of at all times
[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])
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)
[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)
has proper continuant part at some time
[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
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)
[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)
proper part of continuant at some time
Mary’s arm continuant_part_of Mary in the time of her life prior to her operation
the Northern hemisphere of the planet Earth is a part of the planet Earth at all times at which the planet Earth exists.
[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])
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)
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])
BFO2 Reference: continuantThe range for ‘t’ (as in all cases throughout this document unless otherwise specified) is: temporal region.
[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)
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])
continuant_part_of is antisymmetric. (axiom label in BFO2 Reference: [120-001])
continuant_part_of is reflexive (every continuant entity is a continuant_part_of itself). (axiom label in BFO2 Reference: [111-002])
continuant_part_of is transitive. (axiom label in BFO2 Reference: [110-001])
continuant_part_of satisfies unique product. (axiom label in BFO2 Reference: [122-001])
continuant_part_of satisfies weak supplementation. (axiom label in BFO2 Reference: [121-001])
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])
(forall (x t) (if (Continuant x) (continuantPartOfAt x x t))) // axiom label in BFO2 CLIF: [111-002]
(forall (x y t) (if (and (continuantPartOfAt x y t) (IndependentContinuant x)) (locatedInAt x y t))) // axiom label in BFO2 CLIF: [047-002]
(forall (x y t) (if (and (continuantPartOfAt x y t) (continuantPartOfAt y x t)) (= x y))) // axiom label in BFO2 CLIF: [120-001]
(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]
(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]
(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]
(iff (ImmaterialEntity a) (and (IndependentContinuant a) (not (exists (b t) (and (MaterialEntity b) (continuantPartOfAt b a t)))))) // axiom label in BFO2 CLIF: [028-001]
part of continuant at some time
[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)
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)'.
[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'
part of continuant at all times
[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
[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.
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)
[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)
[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])
[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.
[copied from inverse property 'part of continuant at some time'] BFO2 Reference: continuant
[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.
[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])
has continuant part at some time
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.
Really of interest to developers only
BFO OWL specification label
Relates an entity in the ontology to the term that is used to represent it in the the CLIF specification of BFO2
BFO CLIF specification label
has proper temporal part
[copied from inverse property 'has history'] b has_history c iff c history_of b [XXX-001
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
history of
b has_history c iff c history_of b [XXX-001
[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
has history
[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])
forall(t) exists_at(y,t) -> exists_at(x,t) and 'part of continuant'(x,y,t)
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'
[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)'.
part of continuant at all times that whole exists
[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
[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.
forall(t) exists_at(y,t) -> exists_at(x,t) and 'has continuant part'(x,y,t)
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'
[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)'.
[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])
[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.
[copied from inverse property 'part of continuant at all times'] BFO2 Reference: continuant
[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.
[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])
has continuant part at all times that part exists
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.
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.
Interacting selectively and non-covalently with transfer RNA.
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.
Interacting selectively and non-covalently with a SNARE (soluble N-ethylmaleimide-sensitive factor attached protein receptor) protein.
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.
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.
Interacting selectively and non-covalently with DNA sequences encoding ribosomal RNA.
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.
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.
Interacting selectively and non-covalently with magnesium (Mg) ions.
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.
response to reactive oxygen intermediate
Provision of the template used by reverse transcriptase to synthesize the G-rich strand of telomeric DNA.
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.
template for synthesis of G-rich strand of telomere DNA activity
Interacting selectively and non-covalently with a 7-methylguanosine (m7G) group or derivative located at the 5' end of an RNA molecule.
Interacting selectively and non-covalently with the 7-methylguanosine group added cotranscriptionally to the 5' end of RNA molecules transcribed by polymerase II.
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.
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.
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.
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.
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.
crossed form four-way junction DNA binding
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.
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.
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.
Interacting selectively and non-covalently with a region of DNA that contains double-stranded DNA flanked by a region of single-stranded DNA.
double-strand/single-strand DNA junction binding
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.
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.
The repair of UV-induced T-T, C-T and C-C dimers by directly reversing the damage to restore the original pyrimidines.
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.
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'.
pyrimidine dimer repair by nucleotide-excision repair
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.
double-strand break repair via homologous recombination
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.
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.
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.
double-strand break repair via break-induced replication
Synthesis of DNA that proceeds from the broken 3' single-strand DNA end and uses the homologous intact duplex as the template.
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.
Stimulates the hydrolysis and exchange of adenyl nucleotides by other proteins.
adenyl-nucleotide exchange factor activity
Interacting selectively and non-covalently with inositol hexakisphosphate.
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.
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".
transcription regulatory region sequence-specific DNA binding
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.
RNA polymerase II regulatory region sequence-specific DNA binding
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.
RNA polymerase II core promoter proximal region sequence-specific DNA binding
RNA polymerase II promoter proximal region sequence-specific DNA binding
RNA polymerase II upstream activating sequence (UAS) sequence-specific DNA binding
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".
RNA polymerase II proximal promoter sequence-specific DNA binding
Interacting selectively and non-covalently with a DNA sequence that is part of the core promoter of a RNA polymerase II-transcribed gene.
RNA polymerase II core promoter sequence-specific DNA binding
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.
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.
RNA polymerase II distal enhancer sequence-specific DNA binding
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.
eubacterial-type RNA polymerase regulatory region sequence-specific DNA binding
bacterial-type RNA polymerase regulatory region sequence-specific DNA binding
Interacting selectively and non-covalently with a DNA sequence that is part of the core promoter of a bacterial gene.
eubacterial-type RNA polymerase core promoter sequence-specific DNA binding
bacterial-type RNA polymerase core promoter sequence-specific DNA binding
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.
bacterial-type RNA polymerase core promoter proximal region sequence-specific DNA binding
eubacterial-type RNA polymerase regulatory transcription factor sequence-specific DNA binding
bacterial-type proximal promoter sequence-specific DNA binding
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.
core promoter proximal region sequence-specific DNA binding
promoter proximal region sequence-specific DNA binding
core promoter proximal region DNA binding
proximal promoter sequence-specific DNA binding
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.
polymerase III regulatory region sequence-specific DNA binding
Interacting selectively and non-covalently with RNA polymerase II core enzyme, a multisubunit eukaryotic nuclear RNA polymerase typically composed of twelve subunits.
Interacting selectively and non-covalently with RNA polymerase III core enzyme, a multisubunit eukaryotic nuclear RNA polymerase typically composed of seventeen subunits.
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.
eubacterial-type RNA polymerase core enzyme binding
bacterial-type RNA polymerase core enzyme binding
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.
mitochondrial single-subunit type RNA polymerase binding
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.
RNA polymerase III type 1 promoter sequence-specific DNA binding
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.
RNA polymerase III type 2 promoter sequence-specific DNA binding
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.
RNA polymerase III transcription factor recruiting activity
transcription factor activity, RNA polymerase III promoter sequence-specific binding, TFIIIB recruiting
RNA polymerase III hybrid type promoter TFIIIB recruiting transcription factor activity
RNA polymerase III promoter sequence-specific DNA binding TFIIIB recruiting transcription factor activity
RNA polymerase III type 1 promoter sequence-specific DNA binding TFIIIB recruiting transcription factor activity
RNA polymerase III type 2 promoter sequence-specific DNA binding TFIIIB recruiting transcription factor activity
RNA polymerase III type 3 promoter TFIIIB recruiting transcription factor activity
transcription factor activity, RNA polymerase III type 1 promoter sequence-specific binding, TFIIIB recruiting
transcription factor activity, RNA polymerase III type 2 promoter sequence-specific binding, TFIIIB recruiting
transcription factor activity, RNA polymerase III type 3 promoter TFIIIB recruiting
type 2 RNA polymerase III promoter recognition
type 3 RNA polymerase III promoter recognition
RNA polymerase III assembly factor activity
RNA polymerase III assembly factor activity, TFIIIB recruiting
transcription factor activity, RNA polymerase III type 1 promoter TFIIIB
Merged terms as in https://github.com/geneontology/go-ontology/issues/14852
RNA polymerase III transcription regulator recruiting activity
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.
RNA polymerase III type 3 promoter sequence-specific DNA binding
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.
sequence-specific DNA binding transcription factor recruiting transcription factor activity
transcription factor activity, sequence-specific DNA binding transcription factor recruiting
transcription factor activity, sequence-specific DNA-binding transcription factor recruiting
RNA polymerase II sequence-specific DNA-binding transcription factor recruiting activity
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.
RNA polymerase II regulatory region DNA binding
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.
RNA polymerase I regulatory region DNA binding
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.
RNA polymerase III regulatory region DNA binding
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.
eubacterial-type RNA polymerase regulatory region DNA binding
bacterial-type RNA polymerase regulatory region DNA binding
Interacting selectively and non-covalently with a DNA region that controls the transcription of the mitochondrial DNA.
mitochondrial heavy strand promoter anti-sense binding
mitochondrial heavy strand promoter sense binding
mitochondrial light strand promoter anti-sense binding
mitochondrial light strand promoter sense binding
mitochondrial RNA polymerase core promoter proximal region sequence-specific DNA binding
mitochondrial RNA polymerase core promoter sequence-specific DNA binding
mitochondrial RNA polymerase regulatory region DNA binding
mitochondrial RNA polymerase regulatory region sequence-specific DNA binding
mitochondrial proximal promoter sequence-specific DNA binding
mitochondrial promoter sequence-specific DNA binding
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.
plastid RNA polymerase regulatory region DNA binding
Interacting selectively and non-covalently with an RNA polymerase III transcription factor, any protein required to initiate or regulate transcription by RNA polymerase III.
RNA polymerase III transcription factor binding
RNA polymerase III general transcription initiation factor binding
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.
RNA polymerase III type 1 promoter DNA binding
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.
RNA polymerase III type 2 promoter DNA binding
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.
RNA polymerase III type 3 promoter DNA binding
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.
RNA polymerase III hybrid type promoter DNA binding
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.
RNA polymerase III hybrid type promoter sequence-specific DNA binding
Interacting selectively and non-covalently with RNA polymerase I core enzyme, a multisubunit eukaryotic nuclear RNA polymerase typically composed of seventeen subunits.
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.
core promoter sequence-specific DNA binding
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.
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.
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.
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.
single-subunit type RNA polymerase binding
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.
plastid single-subunit type RNA polymerase binding
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.
plastid PEP RNA polymerase core enzyme binding
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.
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.
transcription regulatory region RNA binding
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.
Interacting selectively and non-covalently with an RNA polymerase II transcription factor, any protein required to initiate or regulate transcription by RNA polymerase II.
RNA polymerase II transcription factor binding
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.
RNA polymerase II basal transcription factor binding
RNA polymerase II general transcription initiation factor binding
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.
TFIIA-class transcription factor binding
TFIIA-class transcription factor complex binding
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.
TFIIB-class transcription factor binding
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.
TFIID-class transcription factor binding
TFIID-class transcription factor complex binding
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.
TFIIE-class transcription factor binding
TFIIE-class transcription factor complex binding
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.
TFIIF-class transcription factor binding
TFIIF-class transcription factor complex binding
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.
TFIIH-class transcription factor binding
TFIIH-class transcription factor complex binding
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.
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.
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.
basal RNAP II transcription machinery binding
basal RNA polymerase II transcription machinery binding
Interacting selectively and non-covalently with an RNA polymerase II transcription activating factor, a protein involved in positive regulation of transcription.
RNA polymerase II activating transcription factor binding
Interacting selectively and non-covalently with an RNA polymerase II transcription repressing factor, a protein involved in negative regulation of transcription.
RNA polymerase II repressing transcription factor binding
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.
basal bacterial-type RNA polymerase transcription machinery binding
bacterial-type RNA polymerase holo enzyme binding
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.
transcription factor recruiting activity
transcription factor recruiting transcription factor activity
transcription factor activity, transcription factor recruiting
Changed subclasses https://github.com/geneontology/go-ontology/issues/15577
transcription regulator recruiting activity
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.
RNA polymerase II transcription factor recruiting activity
RNA polymerase II transcription factor recruiting transcription factor activity
TFIIE-class transcription factor recruiting transcription factor activity
TFIIF-class transcription factor recruiting transcription factor activity
TFIIH-class transcription factor recruiting transcription factor activity
transcription factor activity, TFIIE-class transcription factor recruiting
transcription factor activity, TFIIF-class transcription factor recruiting
transcription factor activity, TFIIH-class transcription factor recruiting
transcription factor activity, RNA polymerase II transcription factor recruiting
Merged terms see https://github.com/geneontology/go-ontology/issues/15795
RNA polymerase II transcription regulator recruiting activity
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.
core RNA polymerase II recruiting transcription factor activity
transcription factor activity, core RNA polymerase II recruiting
RNA polymerase II complex recruiting activity
Interacting selectively and non-covalently with a DNA sequence that controls mitochondrial transcription termination.
mitochondrial RNA polymerase terminator site sequence-specific DNA binding transcription factor activity
transcription factor activity, mitochondrial RNA polymerase terminator site sequence-specific binding
mitochondrial RNA polymerase termination site sequence-specific DNA binding
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.
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.
transcription termination site sequence-specific DNA binding
Interacting selectively and non-covalently with a sequence of DNA that is a terminator for bacterial-type RNA polymerase.
bacterial-type RNA polymerase termination site sequence-specific DNA binding
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.
bacterial-type RNA polymerase upstream activating sequence (UAS) sequence-specific DNA binding
bacterial-type RNA polymerase enhancer sequence-specific DNA binding
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.
TFIIIB-class transcription factor binding
TFIIIB-class transcription factor complex binding
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.
TFIIIA-class transcription factor binding
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.
TFIIIC-class transcription factor binding
TFIIIC-class transcription factor complex binding
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.
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.
transcription termination site DNA binding
Interacting selectively and non-covalently with an intronic DNA sequence that regulates the transcription of the transcript it is contained within.
intronic transcription regulatory region sequence-specific DNA binding
Interacting selectively and non-covalently with an RNA polymerase II intronic DNA sequence that regulates the transcription of the transcript it is contained within.
RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding
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.
RNA polymerase I regulatory region sequence-specific DNA binding
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.
RNA polymerase I core element sequence-specific DNA binding
RNA polymerase I core promoter sequence-specific DNA binding
RNA polymerase I CORE element sequence-specific DNA binding transcription factor recruiting transcription factor activity
transcription factor activity, RNA polymerase I CORE element binding transcription factor recruiting
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.
RNA polymerase I upstream element sequence-specific DNA binding
RNA polymerase I upstream control element sequence-specific DNA binding
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.
RNA polymerase I enhancer sequence-specific DNA binding
Interacting selectively and non-covalently with an RNA polymerase I transcription factor, any protein required to initiate or regulate transcription by RNA polymerase I.
RNA polymerase I transcription factor binding
RNA polymerase I general transcription initiation factor binding
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.
RNA polymerase I transcription factor recruiting activity
RNA polymerase I transcription factor recruiting transcription factor activity
transcription factor activity, RNA polymerase I transcription factor recruiting
RNA polymerase I transcription regulator recruiting activity
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.
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.
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.
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.
RNA polymerase II transcription cofactor binding
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.
RNA polymerase II transcription coactivator binding
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.
RNA polymerase II transcription corepressor binding
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.
Interacting selectively and non-covalently with lipopolysaccharide.
Interacting selectively and non-covalently with the interleukin-21 receptor.
Interacting selectively and non-covalently with amyloid-beta peptide/protein and/or its precursor.
The series of events required for a bitter taste stimulus to be received and converted to a molecular signal.
perception of bitter taste, detection of chemical stimulus
perception of bitter taste, sensory transduction of chemical stimulus
sensory detection of chemical stimulus during perception of bitter taste
sensory transduction of chemical stimulus during perception of bitter taste
detection of chemical stimulus involved in sensory perception of bitter taste
The series of events required for a sour taste stimulus to be received and converted to a molecular signal.
perception of sour taste, detection of chemical stimulus
perception of sour taste, sensory transduction of chemical stimulus
sensory detection of chemical stimulus during perception of sour taste
sensory transduction of chemical stimulus during perception of sour taste
detection of chemical stimulus involved in sensory perception of sour taste
The series of events required for a sweet taste stimulus to be received and converted to a molecular signal.
perception of sweet taste, detection of chemical stimulus
perception of sweet taste, sensory transduction of chemical stimulus
sensory detection of chemical stimulus during perception of sweet taste
sensory transduction of chemical stimulus during perception of sweet taste
detection of chemical stimulus involved in sensory perception of sweet taste
The series of events required for a salty taste stimulus to be received and converted to a molecular signal.
perception of salty taste, detection of chemical stimulus
perception of salty taste, sensory transduction of chemical stimulus
sensory detection of chemical stimulus during perception of salty taste
sensory transduction of chemical stimulus during perception of salty taste
detection of chemical stimulus involved in sensory perception of salty taste
Interacting selectively and non-covalently with a G protein-coupled receptor.
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.
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%.
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.
Interacting selectively and non-covalently with a phosphorylated tyrosine residue within a protein.
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.
Interacting selectively and non-covalently with a J-chain-containing polymeric immunoglobulin of the IgA or IgM isotypes.
Interacting selectively and non-covalently with an immunoglobulin of the IgM isotype.
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.
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.
Interacting selectively and non-covalently with any component or product of the complement cascade.
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.
Interacting selectively and non-covalently with the C1q component of the classical complement cascade.
Interacting selectively and non-covalently with the C3a product of the complement cascade.
Interacting selectively and non-covalently with the C3b product of the complement cascade.
Interacting selectively and non-covalently with the iC3b product of the complement cascade.
Interacting selectively and non-covalently with the C3dg product of the complement cascade.
Interacting selectively and non-covalently with the C3d product of the complement cascade.
Interacting selectively and non-covalently with the C4b product of the classical complement cascade.
Interacting selectively and non-covalently with the C5a product of the complement cascade.
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.
Note that collectins include such proteins as mannose-binding lectins (MBL) and surfactant proteins A and D (SP-A and SP-D).
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.
Note that pentraxins include such proteins as serum amyloid P component (SAP) and C-reactive protein (CRP).
Interacting selectively and non-covalently with (1->3)-beta-D-glucans.
Interacting selectively and non-covalently with lipoarabinomannan.
Interacting selectively and non-covalently with a nucleoside, a compound consisting of a purine or pyrimidine nitrogenous base linked either to ribose or deoxyribose.
Interacting selectively and non-covalently with a purine nucleoside, a compound consisting of a purine base linked either to ribose or deoxyribose.
Interacting selectively and non-covalently with a pyrimidine nucleoside, a compound consisting of a pyrimidine base linked either to ribose or deoxyribose.
Interacting selectively and non-covalently with a farnesylated protein.
Any process that modulates the frequency, rate, or extent of endothelial cell proliferation.
regulation of endothelial cell proliferation
Any process that stops, prevents, or reduces the rate or extent of endothelial cell proliferation.
down regulation of endothelial cell proliferation
down-regulation of endothelial cell proliferation
downregulation of endothelial cell proliferation
inhibition of endothelial cell proliferation
negative regulation of endothelial cell proliferation
Any process that activates or increases the rate or extent of endothelial cell proliferation.
up regulation of endothelial cell proliferation
up-regulation of endothelial cell proliferation
upregulation of endothelial cell proliferation
activation of endothelial cell proliferation
stimulation of endothelial cell proliferation
positive regulation of endothelial cell proliferation
Interacting selectively and non-covalently with a G-protein alpha subunit. The alpha subunit binds a guanine nucleotide.
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.
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.
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.
detection of hypoxic conditions in blood by chemoreceptor signalling
detection of hypoxic conditions in blood by chemoreceptor signaling
The process by a carbon dioxide stimulus is received and converted to a molecular signal by the vasomotor center of the central nervous system.
detection of carbon dioxide by vasomotor center
Interacting selectively and non-covalently with any protease or peptidase.
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.
Interacting selectively and non-covalently with one of the p53 family of proteins.
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.
The process of activating or increasing the rate or extent of mesenchymal cell proliferation. Mesenchymal cells are loosely organized embryonic cells.
up regulation of mesenchymal cell proliferation
up-regulation of mesenchymal cell proliferation
upregulation of mesenchymal cell proliferation
activation of mesenchymal cell proliferation
stimulation of mesenchymal cell proliferation
positive regulation of mesenchymal cell proliferation
Interacting selectively and non-covalently with a nucleobase, any of a class of pyrmidines or purines, organic nitrogenous bases.
Interacting selectively and non-covalently with adenine, a purine base.
Interacting selectively and non-covalently with cytosine.
Interacting selectively and non-covalently with guanine.
Interacting selectively and non-covalently with uracil.
Interacting selectively and non-covalently with thymine.
Interacting selectively and non-covalently with a purine nucleobase, an organic nitrogenous base with a purine skeleton.
Interacting selectively and non-covalently with a pyrimidine nucleobase, an organic nitrogenous base with a pyrimidine skeleton.
Interacting selectively and non-covalently with the interleukin-33 receptor.
Interacting selectively and non-covalently with interleukin-33.
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.
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.
Interacting selectively and non-covalently with UTP, uridine 5'-triphosphate.
Interacting selectively and non-covalently with CTP, cytidine 5'-triphosphate.
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.
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.
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.
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).
steroid receptor RNA activator RNA binding
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).
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.
response to bacteria associated molecule
response to bacterial associated molecule
response to bacterium associated molecule
response to molecule of bacterial origin
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.
Any process that modulates the frequency, rate, or extent of a response to biotic stimulus.
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.
regulation of response to biotic stimulus
Any process that stops, prevents, or reduces the frequency, rate, or extent of a response to biotic stimulus.
down regulation of response to biotic stimulus
down-regulation of response to biotic stimulus
downregulation of response to biotic stimulus
inhibition of response to biotic stimulus
negative regulation of response to biotic stimulus
Any process that activates or increases the frequency, rate, or extent of a response to biotic stimulus.
up regulation of response to biotic stimulus
up-regulation of response to biotic stimulus
upregulation of response to biotic stimulus
activation of response to biotic stimulus
stimulation of response to biotic stimulus
positive regulation of response to biotic stimulus
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.
detection of reduced oxygen by chemoreceptor signalling
detection of reduced oxygen by chemoreceptor signaling
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.
detection of increased carbon dioxide by chemoreceptor signalling
detection of increased carbon dioxide by chemoreceptor signaling
The process in which information about the levels of hydrogen ions are received and are converted to a molecular signal by chemoreceptors.
detection of pH by chemoreceptor signalling
detection of pH by chemoreceptor signaling
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.
detection of hypoxic conditions in blood by carotid body chemoreceptor signalling
detection of hypoxic conditions in blood by carotid body chemoreceptor signaling
The series of events in which a hydrogen ion stimulus is received by a cell and converted into a molecular signal.
The series of events in which a carbon dioxide stimulus is received by a cell and converted into a molecular signal.
The series of events in which an oxygen stimulus is received by a cell and converted into a molecular signal.
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.
detection of hypoxic conditions in blood by aortic body chemoreceptor signalling
detection of hypoxic conditions in blood by aortic body chemoreceptor signaling
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.
detection of increased carbon dioxide by aortic body chemoreceptor signalling
detection of increased carbon dioxide by aortic body chemoreceptor signaling
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.
detection of increased carbon dioxide by carotid body chemoreceptor signalling
detection of increased carbon dioxide by carotid body chemoreceptor signaling
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.
detection of pH by aortic body chemoreceptor signalling
detection of pH by aortic body chemoreceptor signaling
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.
detection of pH by carotid body chemoreceptor signalling
detection of pH by carotid body chemoreceptor signaling
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.
detection of reduced oxygen by aortic body chemoreceptor signalling
detection of reduced oxygen by aortic body chemoreceptor signaling
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.
detection of reduced oxygen by carotid body chemoreceptor signalling
detection of reduced oxygen by carotid body chemoreceptor signaling
The directed movement of sodium ions (Na+) by the kidney.
The delamination process that results in the shedding of a corneocyte from the surface of the epidermis.
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.
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.
Interacting selectively and non-covalently with any nucleic acid.
Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
Interacting selectively and non-covalently with oligo(A) and oligo(T) tracts of DNA (AT DNA).
Interacting selectively and non-covalently with DNA in a bent conformation.
Interacting selectively and non-covalently with damaged DNA.
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.
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.
Interacting selectively and non-covalently with double-stranded DNA.
Interacting selectively and non-covalently with double-stranded telomere-associated DNA.
Interacting selectively and non-covalently with DNA in the Z form, i.e. a left-handed helix in which the phosphate backbone zigzags.
Interacting selectively and non-covalently with any P-element, a class of Drosophila transposon responsible for hybrid dysgenesis.
Interacting selectively and non-covalently with DNA in a random coil configuration.
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.
Interacting selectively and non-covalently with single-stranded DNA.
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.
Interacting selectively and non-covalently with an RNA molecule or a portion thereof.
Interacting selectively and non-covalently with double-stranded RNA.
Interacting selectively and non-covalently with single-stranded RNA.
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.
Interacting selectively and non-covalently with the 3' untranslated region of an mRNA molecule.
Interacting selectively and non-covalently with monomeric or multimeric forms of actin, including actin filaments.
Interacting selectively and non-covalently with monomeric actin, also known as G-actin.
Interacting selectively and non-covalently with an actin filament along its length.
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.
Catalysis of the reaction: L-arginine + ATP = N(omega)-phospho-L-arginine + ADP + 2 H(+).
ATP:L-arginine N-phosphotransferase activity
adenosine 5'-triphosphate-arginine phosphotransferase activity
Catalysis of the hydrolysis of any O-glycosyl bond.
hydrolase activity, hydrolyzing O-glycosyl compounds
Catalysis of the transfer of a prenyl group from one compound (donor) to another (acceptor).
Catalysis of the phosphorylation of an amino acid residue in a protein, usually according to the reaction: a protein + ATP = a phosphoprotein + ADP.
Note that triphosphate is used as a phosphate donor by at least one kinase.
Catalysis of the reaction: ATP + protein L-histidine = ADP + protein phospho-L-histidine.
ATP:protein-L-histidine N-phosphotransferase activity
Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate.
protein serine-threonine kinase activity
serine(threonine) protein kinase activity
serine/threonine protein kinase activity
protein kinase (phosphorylating) activity
threonine-specific protein kinase activity
protein serine/threonine kinase activity
Catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein. This reaction requires the presence of a phosphatidylinositol-3-phosphate.
phosphatidylinositol-3-phosphate protein kinase activity
3-phosphoinositide-dependent protein kinase activity
Catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein. This reaction requires the presence of DNA.
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.
ATP:protein phosphotransferase (Ca2+/calmodulin-dependent) activity
Ca2+/calmodulin-dependent protein kinase activity
CaM-regulated serine/threonine kinase activity
calcium- and calmodulin-dependent protein kinase activity
calcium/calmodulin-dependent protein kinase activity
calmodulin regulated protein kinase activity
ATP:caldesmon O-phosphotransferase activity
Ca2+/calmodulin-dependent microtubule-associated protein 2 kinase activity
Ca2+/calmodulin-dependent protein kinase 1 activity
Ca2+/calmodulin-dependent protein kinase II activity
Ca2+/calmodulin-dependent protein kinase IV activity
Ca2+/calmodulin-dependent protein kinase kinase activity
Ca2+/calmodulin-dependent protein kinase kinase beta activity
calcium/calmodulin-dependent protein kinase type II activity
caldesmon kinase (phosphorylating) activity
calmodulin-dependent protein kinase I activity
microtubule-associated protein 2 kinase activity
multifunctional calcium- and calmodulin-regulated protein kinase activity
multifunctional calcium/calmodulin regulated protein kinase activity
calmodulin-dependent protein kinase activity
Catalysis of the reaction: ATP + [elongation factor 2] = ADP + [elongation factor 2] phosphate.
ATP:elongation factor 2 phosphotransferase activity
calmodulin-dependent protein kinase III activity
eukaryotic elongation factor 2 kinase activity
Catalysis of the reaction: ATP + myosin-light-chain = ADP + myosin-light-chain phosphate.
ATP:myosin-light-chain O-phosphotransferase
ATP:myosin-light-chain O-phosphotransferase activity
calcium/calmodulin-dependent myosin light chain kinase activity
myosin light chain protein kinase activity
myosin light-chain kinase (phosphorylating)
myosin light-chain kinase (phosphorylating) activity
smooth-muscle-myosin-light-chain kinase activity
Catalysis of the reaction: 4 ATP + 2 phosphorylase b = 4 ADP + phosphorylase a.
ATP:phosphorylase-b phosphotransferase activity
phosphorylase kinase (phosphorylating) activity
phosphorylase kinase, intrinsic catalyst activity
Catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein. This reaction requires diacylglycerol.
ATP:protein phosphotransferase (diacylglycerol-dependent) activity
diacylglycerol-activated phospholipid-dependent PKC activity
diacylglycerol-activated phospholipid-dependent protein kinase C activity
Catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein. This reaction requires diacylglycerol and calcium.
calcium-dependent protein kinase C activity
Catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein. This reaction requires diacylglycerol but not calcium.
calcium-independent protein kinase C activity
Catalysis of the reaction: ATP + G protein-coupled receptor = ADP + G protein-coupled receptor phosphate.
ATP:G-protein-coupled receptor phosphotransferase activity
G protein coupled receptor phosphorylating protein kinase activity
G protein-coupled receptor kinase activity
G-protein coupled receptor kinase activity
G-protein-coupled receptor phosphorylating protein kinase activity
GPCR phosphorylating protein kinase activity
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.
Catalysis of the reaction: JNKK + ATP = JNKK phosphate + ADP. This reaction is the phosphorylation and activation of JUN kinase kinases (JNKKs).
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.
ATP:protein phosphotransferase (MAPKK-activated) activity
mitogen-activated protein kinase activity
extracellular signal-regulated kinase activity
p42 mitogen-activated protein kinase activity
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.
ATP:protein phosphotransferase (MAPKKK-activated) activity
mitogen-activated protein kinase kinase activity
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.
ATP:protein phosphotransferase (MAPKKKK-activated) activity
mitogen-activated protein kinase kinase kinase activity
MLK-like mitogen-activated protein triple kinase activity
Catalysis of the reaction: ribosomal protein S6 + ATP = ribosomal protein S6 phosphate + ATP.
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.
ATP:protein phosphotransferase (Ser/Thr- and Tyr-phosphorylating) activity
Arabidopsis dual specificity kinase 1 activity
protein threonine/tyrosine kinase activity
protein serine/threonine/tyrosine kinase activity
Catalysis of the reaction: ATP + a protein tyrosine = ADP + protein tyrosine phosphate.
Catalysis of the reaction: ATP + protein L-tyrosine = ADP + protein L-tyrosine phosphate by a non-membrane spanning protein.
ATP:protein-tyrosine O-phosphotransferase activity
ATP:protein-L-tyrosine O-phosphotransferase (non-specific) activity
non-specific protein-tyrosine kinase activity
cytoplasmic protein tyrosine kinase activity
p60c-src protein tyrosine kinase activity
non-membrane spanning protein tyrosine kinase activity
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.
phosphoprotein phosphohydrolase activity
Catalysis of the reaction: protein serine phosphate + H2O = protein serine + phosphate, and protein threonine phosphate + H2O = protein threonine + phosphate.
serine/threonine specific protein phosphatase activity
3-hydroxy 3-methylglutaryl coenzymeA reductase phosphatase
Aspergillus awamori acid protein phosphatase
branched-chain alpha-keto acid dehydrogenase phosphatase
phosphopyruvate dehydrogenase phosphatase
protein phosphatase type 1, intrinsic catalyst activity
protein phosphatase type 2A, intrinsic catalyst activity
protein phosphatase type 2B, intrinsic catalyst activity
protein phosphatase type 4, intrinsic catalyst activity
protein serine/threonine phosphatase activity
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.
calcium-dependent protein serine/threonine phosphatase, intrinsic catalyst activity
calcium-dependent protein serine/threonine phosphatase activity
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.
magnesium-dependent protein serine/threonine phosphatase activity
Catalysis of the reaction: protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
[phosphotyrosine]protein phosphatase activity
phosphoprotein phosphatase (phosphotyrosine) activity
phosphotyrosine histone phosphatase activity
phosphotyrosine protein phosphatase activity
phosphotyrosylprotein phosphatase activity
protein phosphotyrosine phosphatase activity
protein-tyrosine-phosphate phosphohydrolase activity
tyrosine O-phosphate phosphatase activity
Catalysis of the reaction: non-membrane spanning protein tyrosine phosphate + H2O = non-membrane spanning protein tyrosine + phosphate.
non-membrane spanning protein tyrosine phosphatase activity
Catalysis of the reaction: prenylated-protein tyrosine phosphate + H2O = prenylated-protein tyrosine + phosphate.
prenylated protein tyrosine phosphatase activity
Catalysis of the reaction: ATP + pyruvate dehydrogenase (acetyl-transferring) = ADP + pyruvate dehydrogenase (acetyl-transferring) phosphate.
ATP:pyruvate dehydrogenase (acetyl-transferring) phosphotransferase activity
[pyruvate dehydrogenase (lipoamide)] kinase activity
pyruvate dehydrogenase (lipoamide) kinase activity
pyruvate dehydrogenase kinase (phosphorylating) activity
pyruvate dehydrogenase kinase activator protein activity
pyruvate dehydrogenase (acetyl-transferring) kinase activity
Catalysis of the reaction: [pyruvate dehydrogenase (lipoamide)] phosphate + H2O = [pyruvate dehydrogenase (lipoamide)] + phosphate.
[pyruvate dehydrogenase (lipoamide)] phosphatase, intrinsic catalyst activity
phosphopyruvate dehydrogenase phosphatase activity
pyruvate dehydrogenase (lipoamide) phosphatase activity
pyruvate dehydrogenase (lipoamide)-phosphatase activity
pyruvate dehydrogenase (lipoamide)-phosphate phosphohydrolase activity
pyruvate dehydrogenase phosphatase activity
[pyruvate dehydrogenase (lipoamide)] phosphatase activity
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.
Interacting selectively and non-covalently with the signal recognition particle.
See also the cellular component term 'signal recognition particle, endoplasmic reticulum targeting ; GO:0005786'.
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.
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.
peroxisomal targeting signal 1 (PTS1) binding
peroxisome matrix targeting signal-1 binding
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).
peroxisomal targeting signal 2 (PTS2) binding
peroxisome matrix targeting signal-2 binding
Combining with a laminin, a glycoprotein that constitutes the majority of proteins in the basement membrane, to initiate a change in cell activity.
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'.
Interacting selectively and non-covalently with protein kinase C.
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.
guanyl-nucleotide release factor activity
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.
guanyl-nucleotide exchange factor activity
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.
ARF guanyl-nucleotide exchange factor activity
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.
Ran guanyl-nucleotide exchange factor activity
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.
Ras guanyl-nucleotide exchange factor activity
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.
Rho guanyl-nucleotide exchange factor activity
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.
Note that the name Sar derives from 'secretion-associated, Ras-related'.
Sar guanyl-nucleotide exchange factor activity
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.
Where appropriate, also consider annotating to 'receptor agonist activity ; GO:0048018'.
Interacting selectively and non-covalently with the fibroblast growth factor receptor (FGFR).
fibroblast growth factor receptor ligand
Note that branchless is the Drosophila gene encoding fibroblast growth factor.
fibroblast growth factor receptor binding
Interacting selectively and non-covalently with the type 1 fibroblast growth factor receptor (FGFR1).
type 1 fibroblast growth factor receptor ligand
Note that breathless is the Drosophila gene encoding the type 1 fibroblast growth factor receptor (FGFR1).
type 1 fibroblast growth factor receptor binding
Interacting selectively and non-covalently with a frizzled (fz) receptor.
Interacting selectively and non-covalently with the type 2 fibroblast growth factor receptor (FGFR2).
type 2 fibroblast growth factor receptor ligand
Note that heartless is the Drosophila gene encoding the type 2 fibroblast growth factor receptor (FGFR2).
type 2 fibroblast growth factor receptor binding
Interacting selectively and non-covalently with the Notch (N) protein, a surface receptor.
Interacting selectively and non-covalently with the patched (ptc) protein, a receptor for hedgehog proteins.
Interacting selectively and non-covalently with a type II transforming growth factor beta receptor.
transforming growth factor beta receptor type II binding
transforming growth factor beta ligand binding to type II receptor
type II transforming growth factor beta receptor binding
Interacting selectively and non-covalently with the receptor tyrosine kinase-like orphan receptor (Ror).
receptor tyrosine kinase-like orphan receptor ligand
receptor tyrosine kinase-like orphan receptor binding
Interacting selectively and non-covalently with wishful thinking (Wit), a type II bone morphogenic protein receptor.
Interacting selectively and non-covalently with the sevenless (sev) protein, a receptor tyrosine kinase.
Interacting selectively and non-covalently with the smoothened (smo) protein, which interacts with patched to transmit hedgehog signals.
Interacting selectively and non-covalently with the Toll protein, a transmembrane receptor.
Interacting selectively and non-covalently with the torso (tor) protein, a receptor tyrosine kinase.
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).
death receptor interacting protein activity
death receptor-associated factor activity
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.
Functions to control the survival, growth, differentiation and effector function of tissues and cells.
Also consider annotating to 'receptor agonist activity ; GO:0048018'.
Interacting selectively and non-covalently with a cytokine receptor.
hematopoietin/interferon-class (D200-domain) cytokine receptor binding
hematopoietin/interferon-class (D200-domain) cytokine receptor ligand
Interacting selectively and non-covalently with the ciliary neurotrophic factor receptor.
ciliary neurotrophic factor receptor ligand
ciliary neurotrophic factor receptor binding
Interacting selectively and non-covalently with the erythropoietin receptor.
Interacting selectively and non-covalently with the granulocyte macrophage colony-stimulating factor receptor.
granulocyte macrophage colony stimulating factor receptor binding
granulocyte macrophage colony-stimulating factor
granulocyte macrophage colony-stimulating factor receptor ligand
granulocyte macrophage colony-stimulating factor receptor binding
Interacting selectively and non-covalently with the granulocyte colony-stimulating factor receptor.
granulocyte colony stimulating factor receptor binding
granulocyte colony-stimulating factor receptor ligand
granulocyte colony-stimulating factor receptor binding
Interacting selectively and non-covalently with the growth hormone receptor.
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).
Interacting selectively and non-covalently with the interferon-gamma receptor.
Interacting selectively and non-covalently with the interleukin-2 receptor.
Interacting selectively and non-covalently with the interleukin-3 receptor.
Interacting selectively and non-covalently with the interleukin-4 receptor.
Interacting selectively and non-covalently with the interleukin-5 receptor.
Interacting selectively and non-covalently with the interleukin-6 receptor.
Interacting selectively and non-covalently with the interleukin-7 receptor.
Interacting selectively and non-covalently with the interleukin-9 receptor.
Interacting selectively and non-covalently with the interleukin-10 receptor.
Interacting selectively and non-covalently with the interleukin-11 receptor.
Interacting selectively and non-covalently with the interleukin-12 receptor.
Interacting selectively and non-covalently with the interleukin-13 receptor.
Interacting selectively and non-covalently with the interleukin-14 receptor.
Interacting selectively and non-covalently with the leukemia inhibitory factor receptor.
leukemia inhibitory factor receptor ligand
leukemia inhibitory factor receptor binding
Interacting selectively and non-covalently with the oncostatin-M receptor.
Interacting selectively and non-covalently with the prolactin receptor.
Interacting selectively and non-covalently with the interleukin-1 receptor.
Interacting selectively and non-covalently with a Type I interleukin-1 receptor.
Interacting selectively and non-covalently with a Type II interleukin-1 receptor.
Blocks the binding of interleukin-1 to the interleukin-1 receptor complex.
interleukin-1 receptor antagonist activity
Interacting selectively and non-covalently with the interleukin-8 receptor.
Interacting selectively and non-covalently with the epidermal growth factor receptor.
transforming growth factor alpha receptor binding
transforming growth factor alpha receptor ligand
epidermal growth factor receptor binding
Interacting selectively and non-covalently with the macrophage colony-stimulating factor receptor.
macrophage colony stimulating factor receptor binding
macrophage colony-stimulating factor receptor ligand
macrophage colony-stimulating factor receptor binding
Interacting selectively and non-covalently with the insulin receptor.
Interacting selectively and non-covalently with the insulin-like growth factor receptor.
insulin-like growth factor receptor ligand
insulin-like growth factor receptor binding
Interacting selectively and non-covalently with the transforming growth factor beta receptor.
transforming growth factor beta receptor ligand
transforming growth factor beta ligand binding to type I receptor
transforming growth factor beta receptor anchoring activity
transforming growth factor beta receptor binding
Interacting selectively and non-covalently with the platelet-derived growth factor receptor.
platelet-derived growth factor receptor ligand
platelet-derived growth factor receptor binding
Interacting selectively and non-covalently with the nerve growth factor receptor.
Interacting selectively and non-covalently with the tumor necrosis factor receptor.
Interacting selectively and non-covalently with a neurotrophin receptor.
Interacting selectively and non-covalently with the neurotrophin p75 receptor.
Interacting selectively and non-covalently with a neurotrophin TRK receptor.
Interacting selectively and non-covalently with the neurotrophin TRKA receptor.
Interacting selectively and non-covalently with the neurotrophin TRKB receptor.
Interacting selectively and non-covalently with the neurotrophin TRKC receptor.
Interacting selectively and non-covalently with the hepatocyte growth factor receptor.
hepatocyte growth factor receptor ligand
hepatocyte growth factor receptor binding
Interacting selectively and non-covalently with any vascular endothelial growth factor receptor.
vascular endothelial growth factor receptor ligand
vascular endothelial growth factor receptor binding
Interacting selectively and non-covalently with the stem cell factor receptor (SCFR), a type III transmembrane kinase receptor.
Interacting selectively and non-covalently with CD40, a receptor found on the surface of all B-lymphocytes.
Interacting selectively and non-covalently with a CD27, a receptor found on the surface of T cells and some B cells and NK cells.
Interacting selectively and non-covalently with the protein-tyrosine kinase receptor Neu/ErbB-2/HER2.
Interacting selectively and non-covalently with an integrin.
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.
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.
gonadotrophin hormone-releasing hormone activity
luteinizing hormone-releasing factor activity
luteinizing hormone-releasing hormone activity
luteinizing hormone/follicle-stimulating hormone releasing factor activity
gonadotropin hormone-releasing hormone activity
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.
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.
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.
Acting as a marker to identify a membrane and interacting selectively with one or more SNAREs on another membrane to mediate membrane fusion.
The selective, non-covalent, often stoichiometric, interaction of a molecule with one or more specific sites on another molecule.
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.
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.
Interacting selectively and non-covalently with any androgen, male sex hormones.
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).
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.
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.
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.
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.
Interacting selectively and non-covalently with fatty acids, aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis.
Interacting selectively and non-covalently with iron (Fe) ions.
Interacting selectively and non-covalently with copper (Cu) ions.
Interacting selectively and non-covalently with calcium ions (Ca2+).
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
Interacting selectively and non-covalently with calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.
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%).
Interacting selectively and non-covalently with any protein involved in modulating the reorganization of the cytoskeleton.
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.
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.
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.
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.
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
Interacting selectively and non-covalently with GTP, guanosine triphosphate.
Interacting selectively and non-covalently with a macrolide, any of a large group of structurally related antibiotics produced by Streptomyces species.
Interacting selectively and non-covalently with the 23-membered macrolide lactone FK506.
FK506-sensitive peptidyl-prolyl cis-trans isomerase
Interacting selectively and non-covalently with the aldohexose galactose (galacto-hexose), a common constituent of many oligo- and polysaccharides.
Interacting selectively and non-covalently with the D- or L-enantiomer of glucose.
Interacting selectively and non-covalently with mannose, a monosaccharide hexose, stereoisomeric with glucose, that occurs naturally only in polymerized forms called mannans.
Interacting selectively and non-covalently with any glycan (polysaccharide) containing a substantial proportion of aminomonosaccharide residues.
Interacting selectively and non-covalently with hyaluronic acid, a polymer composed of repeating dimeric units of glucuronic acid and N-acetyl glucosamine.
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.
Interacting selectively and non-covalently with phospholipids, a class of lipids containing phosphoric acid as a mono- or diester.
Interacting selectively and non-covalently with phospholipids, a class of lipids containing phosphoric acid as a mono- or diester, in the presence of calcium.
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.
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.
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate binding
phosphatidylinositol 4,5-bisphosphate binding
phosphatidylinositol-4,5-bisphosphate binding
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.
phosphatidylinositol-3,4,5-trisphosphate binding
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.
multicellular organismal carbohydrate metabolic process
single-organism carbohydrate metabolic process
The chemical reactions and pathways involving any disaccharide, sugars composed of two monosaccharide units.
Any cellular metabolic process involving nucleobases, nucleosides, nucleotides and nucleic acids.
cellular nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
cellular nucleobase, nucleoside, nucleotide and nucleic acid metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
nucleobase, nucleoside and nucleotide metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleobase-containing compound metabolic process
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.
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.
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.
transcription-coupled nucleotide-excision repair
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.
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).
pyrimidine-dimer repair, DNA damage excision
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.
The repair of UV-induced T-T, C-T and C-C dimers.
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.
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.
The repair of double-strand breaks in DNA via homologous and nonhomologous mechanisms to reform a continuous DNA helix.
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'.
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.
double-strand break repair via nonhomologous end joining
The covalent alteration of one or more nucleotide sites in DNA, resulting in a change in its properties.
Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
regulation of cellular transcription, DNA-dependent
regulation of transcription, DNA-dependent
regulation of gene-specific transcription
regulation of transcription, DNA-templated
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).
process resulting in protein modification
The process of introducing a phosphate group on to a protein.
The process of removing one or more phosphoric residues from a protein.
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.
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.
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.
cellular aromatic compound metabolic process
Any process that modulates the frequency, rate or extent of phosphorus utilization.
The chemical reactions and pathways involving the phosphate group, the anion or salt of any phosphoric acid.
phosphate-containing compound metabolic process
The chemical reactions and pathways involving organic or inorganic compounds that contain nitrogen.
Any process that modulates the frequency, rate or extent of nitrogen utilization.
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.
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.
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.
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.
di-, tri-valent inorganic cation transport
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.
low voltage-dependent potassium channel auxiliary protein activity
low voltage-gated potassium channel auxiliary protein activity
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.
mitochondrial sodium/calcium ion exchange
sodium channel auxiliary protein activity
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.
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.
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.
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.
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.
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.
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.
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.
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.
The process in which a calcium ion (Ca2+) is transported across a mitochondrial membrane, into or out of the mitochondrion.
mitochondrial calcium ion transmembrane transport
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.
substrate-bound cell migration, cell release from substrate
negative regulation of cell adhesion involved in substrate-bound cell migration
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).
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).
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.
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.
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.
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.
cellular response to DNA damage stimulus
The widespread phosphorylation of various molecules, triggering many downstream processes, that occurs in response to the detection of DNA damage.
DNA damage induced protein phosphorylation
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.
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.
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.
cellular response to nitrogen starvation
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.
Any process that stops, prevents, or reduces the frequency, rate or extent of cell adhesion.
cell adhesion receptor inhibitor activity
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.
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.
The series of molecular signals initiated in response to osmotic change.
signal transduction during osmotic stress
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.
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.
See also the molecular function terms 'cytokine activity ; GO:0005125' and 'receptor agonist activity ; GO:0048018'.
Interacting selectively and non-covalently with the beta subunit of the catenin complex.
Interacting selectively and non-covalently with microtubules, filaments composed of tubulin monomers.
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.
The action characteristic of eclosion hormone, a peptide hormone that, upon receptor binding, triggers the death of certain muscles and neurons during insect metamorphosis.
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.
high-density lipoprotein particle binding
Binds to and increases the activity of an enzyme.
Interacting selectively and non-covalently with chitin, a linear polysaccharide consisting of beta-(1->4)-linked N-acetyl-D-glucosamine residues.
Catalysis of the hydrolysis of a phosphodiester to give a phosphomonoester and a free hydroxyl group.
The function that stimulates a cell to grow or proliferate. Most growth factors have other actions besides the induction of cell growth or proliferation.
Interacting selectively and non-covalently with an imaginal disc growth factor receptor.
imaginal disc growth factor receptor binding
Interacting selectively and non-covalently with any protein component of any cytoskeleton (actin, microtubule, or intermediate filament cytoskeleton).
Interacting selectively and non-covalently with 5S ribosomal RNA, the smallest RNA constituent of a ribosome.
Interacting selectively and non-covalently with the unprocessed 5S ribosomal RNA transcript.
Interacting selectively and non-covalently with a transcription factor, a protein required to initiate or regulate transcription.
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.
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
protein tyrosine/serine/threonine phosphatase activity
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.
Interacting selectively and non-covalently with a cAMP response element binding protein (a CREB protein).
3',5' cAMP response element binding protein binding
3',5'-cAMP response element binding protein binding
adenosine 3',5'-cyclophosphate response element binding protein binding
cyclic AMP response element binding protein binding
cAMP response element binding protein binding
Interacting selectively and non-covalently with oxysterol, an oxidized form of cholesterol.
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.
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.
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.
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.
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.
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.
metabolic process resulting in cell growth
multicellular organism metabolic process
Note that metabolic processes do not include single functions or processes such as protein-protein interactions, protein-nucleic acids, nor receptor-ligand interactions.
Interacting selectively and non-covalently with the enzyme protein phosphatase 1.
Catalysis of the transfer of a methyl group to an acceptor molecule.
Catalysis of the transfer of a methyl group to the carbon atom of an acceptor molecule.
Catalysis of the transfer of a methyl group to the nitrogen atom of an acceptor molecule.
Catalysis of the transfer of a methyl group to the oxygen atom of an acceptor molecule.
Interacting selectively and non-covalently with the enzyme adenylate cyclase.
Interacting selectively and non-covalently with any stretch of pyrimidines (cytosine or uracil) in an RNA molecule.
Interacting selectively and non-covalently with eukaryotic initiation factor 4E, a polypeptide factor involved in the initiation of ribosome-mediated translation.
Catalysis of the transfer of a glycosyl group from a UDP-sugar to a small hydrophobic molecule.
Interacting selectively and non-covalently with ferrous iron, Fe(II).
Interacting selectively and non-covalently with ferric iron, Fe(III).
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.
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).
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.
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.
Catalysis of the reaction: ATP + protein L-histidine = ADP + protein N(pi)-phospho-L-histidine.
ATP:protein-L-histidine N-pros-phosphotransferase activity
ATP:protein-L-histidine Npi-phosphotransferase activity
Catalysis of the reaction: ATP + protein L-histidine = ADP + protein N(tau)-phospho-L-histidine.
ATP:protein-L-histidine N-tele-phosphotransferase activity
ATP:protein-L-histidine Ntau-phosphotransferase activity
Interacting selectively and non-covalently with a sequence of uracil residues in an RNA molecule.
Interacting selectively and non-covalently with a polyglutamine tract, i.e. a series of consecutive glutamine residues, in a protein.
Interacting selectively and non-covalently with zinc (Zn) ions.
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.
Any process that activates or increases the rate or extent of cell proliferation.
positive regulation of cell proliferation
positive regulation of cell population proliferation
Any process that stops, prevents or reduces the rate or extent of cell proliferation.
negative regulation of cell proliferation
negative regulation of cell population proliferation
Interacting selectively and non-covalently with a lipid.
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.
Interacting selectively and non-covalently with 7S RNA, the RNA component of the signal recognition particle (SRP).
Interacting selectively and non-covalently with the gurken growth factor receptor.
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.
Ral GDP-dissociation stimulator activity
Ral guanyl-nucleotide exchange factor activity
Interacting selectively and non-covalently with a methylated cytosine/guanine dinucleotide.
Catalysis of the reactions: protein threonine phosphate + H2O = protein threonine + phosphate; and protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
protein tyrosine/threonine phosphatase activity
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.
MAP kinase kinase kinase kinase activity
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.
ATP:DNA-directed RNA polymerase phosphotransferase activity
[RNA-polymerase]-subunit kinase activity
RNA polymerase II carboxy-terminal domain kinase activity
RNA polymerase II CTD heptapeptide repeat kinase activity
Catalysis of the transfer of an acyl group to an oxygen atom on the acceptor molecule.
Catalysis of the transfer of an N-acetylglucosaminyl residue from UDP-N-acetyl-glucosamine to a sugar.
Catalysis of the transfer of an N-acetylgalactosaminyl residue from UDP-N-acetyl-galactosamine to an oligosaccharide.
acetylgalactosaminyltransferase activity
Catalysis of the transfer of a galactosyl group to an acceptor molecule, typically another carbohydrate or a lipid.
Catalysis of the reaction: ATP + IkappaB protein = ADP + IkappaB phosphoprotein.
ATP:IkappaB protein phosphotransferase activity
Note that phosphorylation of IkappaB targets it for proteasomal degradation and allows the nuclear translocation of kB.
Catalysis of the transfer of a fucosyl group to an acceptor molecule, typically another carbohydrate or a lipid.
Catalysis of the reaction: phospho-(DNA-directed RNA polymerase II) + H2O = (DNA-directed RNA polymerase II) + phosphate.
RNA polymerase II carboxy-terminal domain phosphatase activity
RNA polymerase II CTD heptapeptide repeat phosphatase activity
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.
Interacting selectively and non-covalently with selenium (Se).
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.
Interacting selectively and non-covalently with JUN kinase, an enzyme that catalyzes the phosphorylation and activation of members of the JUN family.
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.
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.
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.
Catalysis of the reaction: JUN kinase serine/threonine/tyrosine phosphate + H2O = JUN kinase serine/threonine/tyrosine + phosphate.
The action characteristic of a diuretic hormone, any peptide hormone that, upon receptor binding, regulates water balance and fluid secretion.
Interacting selectively and non-covalently with penicillin, any antibiotic that contains the condensed beta-lactamthiazolidine ring system.
Catalysis of the transfer of a methyl group from S-adenosyl-L-methionine to a substrate.
S-adenosyl methionine-dependent methyltransferase activity
SAM-dependent methyltransferase activity
S-adenosylmethionine-dependent methyltransferase activity
Catalysis of the reaction: ATP + (isocitrate dehydrogenase (NADP)) = ADP + (isocitrate dehydrogenase (NADP)) phosphate.
isocitrate dehydrogenase kinase/phosphatase activity
ATP:isocitrate dehydrogenase (NADP+) phosphotransferase activity
isocitrate dehydrogenase (NADP) kinase activity
isocitrate dehydrogenase (NADP+) kinase activity
isocitrate dehydrogenase kinase (phosphorylating) activity
isocitrate dehydrogenase kinase activity
[isocitrate dehydrogenase (NADP+)] kinase activity
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.
multicellular organismal catabolic process
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.
multicellular organismal macromolecule catabolic process
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.
multicellular organismal biosynthetic process
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.
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.
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.
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.
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.
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.
response to electromagnetic radiation stimulus
Note that 'radiation' refers to electromagnetic radiation of any wavelength.
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.
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.
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.
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.
response to ultraviolet radiation stimulus
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.
An error-prone process for repairing damaged microbial DNA.
The series of events in which an external stimulus is received by a cell and converted into a molecular signal.
The series of events in which an (non-living) abiotic stimulus is received by a cell and converted into a molecular signal.
The series of events in which a light stimulus (in the form of photons) is received and converted into a molecular signal.
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.
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.
detection of ultraviolet radiation stimulus
The series of events in which a chemical stimulus is received by a cell and converted into a molecular signal.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
A response to light intensity in which exposure to medium-intensity light results in increased tolerance to high-intensity light.
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.
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.
response to low light intensity stimulus
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.
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.
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.
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.
The greening response of plants grown in the dark (etiolated) as a result of chloroplast biogenesis and the accumulation of chlorophyll.
The series of events in which a carbohydrate stimulus is received by a cell and converted into a molecular signal.
The series of events in which a sucrose stimulus is received by a cell and converted into a molecular signal.
The series of events in which a stimulus from a hexose is received and converted into a molecular signal.
A series of molecular signals mediated by the detection of sucrose.
A series of molecular signals mediated by hexose and dependent on the detection of hexokinase.
A series of molecular signals mediated by hexose and independent of hexokinase.
A series of molecular signals mediated by the detection of carbohydrate.
A series of molecular signals mediated by the detection of hexose.
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways within a cell or an organism.
negative regulation of organismal metabolism
inhibition of organismal metabolic process
negative regulation of multicellular organismal metabolic process
negative regulation of metabolic process
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways within a cell or an organism.
positive regulation of multicellular organismal metabolic process
positive regulation of organismal metabolism
stimulation of organismal metabolic process
up-regulation of organismal metabolic process
positive regulation of metabolic process
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.
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.
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.
calcium-dependent protein serine/threonine kinase activity
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.
amino-terminal vacuolar sorting propeptide binding
Any process that modulates the frequency, rate or extent of signal transduction.
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.
cellular response to sulphate starvation
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.
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.
The recognition of soluble molecules in the environment.
Interacting selectively and non-covalently with auxin, plant hormones that regulate aspects of plant growth.
Interacting selectively and non-covalently with N-1-naphthylphthalamic acid, an auxin transport inhibitor.
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.
cellular response to iron ion starvation
The series of events in which a glutamine stimulus is received by a cell and converted into a molecular signal.
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.
Protection mechanism used by plants under conditions of excess energy absorption as a consequence of the light reactions of photosynthesis.
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.
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).
Interacting selectively and non-covalently with the enzyme thioglucosidase.
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.
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.
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.
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.
response to continuous far red light stimulus by the high-irradiance response system
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.
response to low fluence red light stimulus
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.
response to very low fluence red light stimulus
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.
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.
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.
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.
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.
response to medium wave ultraviolet light stimulus
response to medium wave ultraviolet radiation stimulus
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.
response to germicidal ultraviolet light stimulus
response to germicidal ultraviolet radiation stimulus
response to shortwave ultraviolet light stimulus
response to shortwave ultraviolet radiation stimulus
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.
response to low fluence blue light by blf system
response to low fluence blue light stimulus by blue low-fluence system
The series of events in which a phosphate ion stimulus is received by a cell and converted into a molecular signal.
The process in which a change in the level of mono- and disaccharide glucose trigger the expression of genes controlling metabolic and developmental processes.
Interacting selectively and non-covalently with heteropolysaccharides. A heteropolysaccharide is a glycan composed of more than one type of monosaccharide residue.
Interacting selectively and non-covalently with phytochrome.
Interacting selectively and non-covalently with phosphatidylinositol-5-phosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 5' position.
phosphatidylinositol-5-phosphate binding
Interacting selectively and non-covalently with gibberellins, plant hormones that regulate aspects of plant growth.
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.
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.
Catalysis of the transfer of a methyl group to the carboxyl group of an acceptor molecule to form a methyl ester.
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.
cellular response to magnesium starvation
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.
The directed movement of lithium ion out of a cell or organelle.
lithium ion export across the plasma membrane
Any process that modulates the frequency, rate or extent of anion channel activity.
Any process that stops, prevents, or reduces the frequency, rate, or extent of the anion channel activity.
negative regulation of anion channel activity
Any process in which blue light modulates the frequency, rate or extent of anion channel activity.
regulation by blue light of anion channel activity
regulation of anion channel activity by blue light
Any process in which blue light stops, prevents, or reduces the frequency, rate, or extent of the anion channel activity.
negative regulation by blue light of anion channel activity
inhibition by blue light of anion channel activity
negative regulation of anion channel activity by blue light
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.
Interacting selectively and non-covalently with abscisic acid, plant hormones that regulate aspects of plant growth.
Interacting selectively and non-covalently with a methylated cytosine/unspecified/guanine trinucleotide.
Interacting selectively and non-covalently with a methylated cytosine/unspecified/unspecified trinucleotide.
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.
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.
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.
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'.
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.
regulation of mesenchymal cell proliferation
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.
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.
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.
proteasome-mediated protein catabolic process
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.
regulation of calcium ion transport into cytosol
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.
negative regulation of calcium ion transport into cytosol
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.
positive regulation of calcium ion transport into cytosol
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.
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.
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.
positive regulation of sodium ion transport
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.
negative regulation of sodium ion transport
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.
regulation of glucose transmembrane transport
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.
positive regulation of glucose transport
positive regulation of glucose transmembrane transport
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.
negative regulation of glucose transport
negative regulation of glucose transmembrane transport
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.
regulation of keratinocyte proliferation
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.
positive regulation of keratinocyte proliferation
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.
negative regulation of keratinocyte proliferation
Interacting selectively and non-covalently with a region in a genome which promotes recombination.
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.
regulation of hydrogen ion transporting ATPase activity, rotational mechanism
regulation of proton-transporting ATPase activity, rotational mechanism
Catalysis of the reaction: a protein + ATP = a phosphoprotein + ADP. This reaction requires the presence of calcium.
calcium-dependent protein kinase activity
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.
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.
positive regulation of lipid sequestration
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.
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.
positive regulation of cholesterol sequestration
positive regulation of cholesterol storage
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.
negative regulation of cholesterol sequestration
negative regulation of cholesterol storage
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.
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.
regulation of sequestering of triacylglycerol
regulation of triacylglycerol sequestration
regulation of sequestering of triglyceride
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.
positive regulation of sequestering of triacylglycerol
positive regulation of triglyceride sequestration
positive regulation of sequestering of triglyceride
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.
negative regulation of sequestering of triacylglycerol
negative regulation of triglyceride sequestration
negative regulation of sequestering of triglyceride
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.
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.
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.
Any process that modulates the frequency, rate or extent of skeletal muscle satellite cell proliferation.
regulation of skeletal muscle satellite cell proliferation
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.
growth factor dependent regulation of skeletal muscle satellite cell proliferation
Any process that modulates the frequency, rate or extent of skeletal muscle cell proliferation.
regulation of skeletal muscle cell proliferation
Any process that activates or increases the frequency, rate or extent of skeletal muscle cell proliferation.
positive regulation of skeletal muscle cell proliferation
Any process that stops, prevents, or reduces the frequency, rate or extent of skeletal muscle cell proliferation.
negative regulation of skeletal muscle cell proliferation
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.
Interacting selectively and non-covalently with monomeric or multimeric forms of tubulin, including microtubules.
Interacting selectively and non-covalently with a toxic substance, a poisonous substance that causes damage to biological systems.
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.
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.
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.
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.
The directed movement of copper ions into a cell or organelle.
The directed movement of copper ions across the plasma membrane.
A process in which ferric-enterobactin, the iron-bound form of the siderophore enterobactin, is transported into the cell by specific cell surface receptors.
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.
ferric triacetylfusarinine C import into cell
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Catalysis of the hydrolysis of glucosyl compounds, substances containing a group derived from a cyclic form of glucose or a glucose derivative.
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.
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.
energy coupled proton transport, down electrochemical gradient
The transport of protons across a membrane to generate an electrochemical gradient (proton-motive force) that powers ATP synthesis.
The transport of protons across a membrane to generate an electrochemical gradient (proton-motive force) that powers GTP synthesis.
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.
energy coupled proton transmembrane transport, against electrochemical gradient
The transport of protons against an electrochemical gradient, using energy from light.
The transport of protons against an electrochemical gradient, using energy from electron transport.
electron transport coupled proton transport
Acts as a trigger for a pattern specification process when present at a specific concentration within a gradient.
Interacting selectively and non-covalently with cyclosporin A, a cyclic undecapeptide that contains several N-methylated and unusual amino acids.
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.
cellular response to phosphate starvation
A process that results in the assembly, arrangement of constituent parts, or disassembly of a cellular component.
cellular component organisation at cellular level
cellular component organisation in other organism
cellular component organization at cellular level
cellular component organization in other organism
The series of events in which a temperature stimulus (hot or cold) is received and converted into a molecular signal.
The process in which a cell irreversibly increases in size over time by accretion and biosynthetic production of matter similar to that already present.
non-developmental growth of a unicellular organism
Any process that modulates the frequency, rate or extent of light-activated channel activity.
regulation of light-activated channel activity
The action characteristic of myostimulatory hormone, a peptide hormone that stimulates muscle contraction.
The action characteristic of myostimulatory hormone, a peptide hormone that inhibits muscle contraction.
The action characteristic of ecdysiostatic hormone, a peptide hormone that inhibits ecdysone secretion.
Interacting selectively and non-covalently with nickel (Ni) cations.
Interacting selectively and non-covalently with chlorophyll; any compound of magnesium complexed in a porphyrin (tetrapyrrole) ring and which functions as a photosynthetic pigment.
Interacting selectively and non-covalently with bacteriochlorophyll c, a chlorophyll of photosynthetic bacteria, for example green sulfur bacteria.
Interacting selectively and non-covalently with the interleukin-15 receptor.
Interacting selectively and non-covalently with AMP, adenosine monophosphate.
Enables the transfer of a methyl group from S-adenosyl-L-methionine to an amino group of an arginine residue.
Catalysis of the transfer of a methyl group from S-adenosyl-L-methionine to the epsilon-amino group of a lysine residue.
Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.
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.
Catalysis of the transfer of an acetyl group to an acceptor molecule.
Catalysis of the transfer of a palmitoyl (CH3-[CH2]14-CO-) group to an acceptor molecule.
Catalysis of the transfer of an acyl group to a nitrogen atom on the acceptor molecule.
Catalysis of the transfer of a palmitoyl group to an oxygen atom on the acceptor molecule.
Catalysis of the transfer of an acyl group to a sulfur atom on the acceptor molecule.
Catalysis of the transfer of an acetyl group to a sulfur atom on the acceptor molecule.
Catalysis of the hydrolysis of a pyrophosphate bond between two phosphate groups, leaving one phosphate on each of the two fragments.
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.
pituitary adenylyl cyclase activating polypeptide activity
pituitary adenylate cyclase activating polypeptide activity
Interacting selectively and non-covalently with glutamate, the anion of 2-aminopentanedioic acid.
Interacting selectively and non-covalently with thienylcyclohexylpiperidine.
Interacting selectively and non-covalently with an amino acid, organic acids containing one or more amino substituents.
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.
growth hormone-releasing hormone activity
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.
Catalysis of the transfer of a one-carbon group from one compound (donor) to another (acceptor).
transferase activity, transferring one-carbon groups
Catalysis of the transfer of an acyl group from one compound (donor) to another (acceptor).
transferase activity, transferring acyl groups
Catalysis of the transfer of an acyl group, other than amino-acyl, from one compound (donor) to another (acceptor).
transferase activity, transferring groups other than amino-acyl groups
transferase activity, transferring acyl groups other than amino-acyl groups
Catalysis of the transfer of a succinyl (3-carboxypropanoyl) group to an acceptor molecule.
Catalysis of the transfer of a succinyl group to a sulfur atom on the acceptor molecule.
Catalysis of the transfer of a glycosyl group from one compound (donor) to another (acceptor).
transferase activity, transferring other glycosyl groups
Note that enzymes of class EC:2.4.99.- should also be annotated to this term.
transferase activity, transferring glycosyl groups
Catalysis of the transfer of a hexosyl group from one compound (donor) to another (acceptor).
transferase activity, transferring hexosyl groups
Catalysis of the transfer of a pentosyl group from one compound (donor) to another (acceptor).
transferase activity, transferring pentosyl groups
Catalysis of the transfer of an alkyl or aryl (but not methyl) group from one compound (donor) to another (acceptor).
transferase activity, transferring alkyl or aryl groups, other than methyl groups
transferase activity, transferring alkyl or aryl (other than methyl) groups
Catalysis of the transfer of a nitrogenous group from one compound (donor) to another (acceptor).
transferase activity, transferring other nitrogenous groups
Note that enzymes of class EC:2.6.99.- should also be annotated to this term.
transferase activity, transferring nitrogenous groups
Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to another (acceptor).
Note that this term encompasses all kinase activities, as well as activities that transfer other phosphorus-containing groups such as diphosphate or nucleotides.
transferase activity, transferring phosphorus-containing groups
Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to an alcohol group (acceptor).
phosphotransferase activity, alcohol group as acceptor
Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to a nitrogenous group (acceptor).
phosphotransferase activity, nitrogenous group as acceptor
Catalysis of the transfer of a nucleotidyl group to a reactant.
Catalysis of the transfer of a sulfur-containing group from one compound (donor) to another (acceptor).
transferase activity, transferring sulphur-containing groups
transferase activity, transferring sulfur-containing groups
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.
Catalysis of the hydrolysis of any ester bond.
hydrolase activity, acting on ester bonds
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.
Catalysis of the hydrolysis of phosphoric monoesters, releasing inorganic phosphate.
4-nitrophenylphosphate phosphohydrolase activity
p-nitrophenylphosphate phosphohydrolase activity
Catalysis of the hydrolysis of any glycosyl bond.
hydrolase activity, acting on glycosyl bonds
Catalysis of the hydrolysis of any carbon-nitrogen bond, C-N, with the exception of peptide bonds.
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in other compounds
Note that enzymes of class EC:3.5.99.- should also be annotated to this term.
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
Catalysis of the hydrolysis of any non-peptide carbon-nitrogen bond in a linear amide.
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
Catalysis of the hydrolysis of any acid anhydride.
hydrolase activity, acting on acid anhydrides, involved in cellular and subcellular movement
hydrolase activity, acting on acid anhydrides
Catalysis of the hydrolysis of any acid anhydride which contains phosphorus.
hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
Catalysis of the hydrolysis of any acid phosphorus-nitrogen bond.
hydrolase activity, acting on acid phosphorus-nitrogen bonds
Catalysis of the reaction: ATP + myosin-heavy-chain = ADP + myosin-heavy-chain phosphate.
ATP:myosin heavy-chain O-phosphotransferase activity
ATP:myosin-heavy-chain O-phosphotransferase activity
calmodulin-dependent myosin heavy chain kinase activity
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.
stress-activated protein kinase activity
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.
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.
Interacting selectively and non-covalently, in a ligand dependent manner, with a nuclear receptor protein.
ligand-dependent nuclear receptor binding
ligand-dependent nuclear receptor interactor activity
Interacting selectively and non-covalently with any glycoside in which the sugar group is galactose.
Interacting selectively and non-covalently with any member of the Ras superfamily of monomeric GTPases.
Catalysis of the reaction: MAP kinase serine/threonine/tyrosine phosphate + H2O = MAP kinase serine/threonine/tyrosine + phosphate.
dual-specificity MAP kinase phosphatase activity
MAP kinase tyrosine/serine/threonine phosphatase activity
Catalysis of the reaction: phosphomyosin + H2O = myosin + phosphate.
myosin phosphatase, intrinsic catalyst activity
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.
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.
Interacting selectively and non-covalently with a member of the class of TATA-binding proteins (TBP), including any of the TBP-related factors (TRFs).
TBP-related factor (TRF) protein binding
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.
Rap guanyl-nucleotide exchange factor activity
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.
alpha-melanocyte stimulating hormone activity
alpha-melanophore stimulating hormone activity
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.
corticotropin-releasing hormone activity
Interacting selectively and non-covalently with any peptide with hormonal activity in animals.
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.
Interacting selectively and non-covalently with the GTP-bound form of the Rho protein.
Interacting selectively and non-covalently with a FH1 domain of a protein, a proline-rich domain, usually located in front of a FH2 domain.
Interacting selectively and non-covalently with a small nuclear RNA (snRNA).
Interacting selectively and non-covalently with the U6 small nuclear RNA (U6 snRNA).
Note that this term may be useful for annotating small nuclear RNAs (snRNAs).
Interacting selectively and non-covalently with the SNAP receptor syntaxin-1.
Interacting selectively and non-covalently with purine nucleotides, any compound consisting of a purine nucleoside esterified with (ortho)phosphate.
Interacting selectively and non-covalently with a region of RNA containing frequent adenine and uridine bases.
Adenylate/uridylate-rich element binding
Interacting selectively and non-covalently with the sulfonylurea receptor, a regulatory subunit of the ATP-sensitive potassium ion channel.
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.
Rab guanyl-nucleotide exchange factor activity
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.
Interacting selectively and non-covalently with any triester of glycerol.
Interacting selectively and non-covalently with a sequence of cytosine residues in an RNA molecule.
Interacting selectively and non-covalently with U-rich sequence in the 3'-end of nuclear-transcribed mRNAs; required for cytoplasmic polyadenylylation.
uridine-rich cytoplasmic polyadenylation element binding
uridine-rich cytoplasmic polyadenylylation element binding
Interacting selectively and non-covalently with a fibroblast growth factor.
Interacting selectively and non-covalently with Rab protein, any member of the Rab subfamily of the Ras superfamily of monomeric GTPases.
Interacting selectively and non-covalently with Wnt-protein, a secreted growth factor involved in signaling.
Interacting selectively and non-covalently with the enzyme DEAD/H-box RNA helicase.
Interacting selectively and non-covalently with Ral protein, any member of the Ral subfamily of the Ras superfamily of monomeric GTPases.
Interacting selectively and non-covalently with an aryl hydrocarbon receptor.
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.
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).
Catalysis of the reaction: histone L-arginine + ATP = histone N(omega)-phospho-L-arginine + ADP + 2 H(+).
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).
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.
The chemical reactions and pathways involving a phenol, any compound containing one or more hydroxyl groups directly attached to an aromatic carbon ring.
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.
phenol-containing compound metabolic process
Interacting selectively and non-covalently with guanyl nucleotides, any compound consisting of guanosine esterified with (ortho)phosphate.
Interacting selectively and non-covalently with GMP, guanosine monophosphate.
Interacting selectively and non-covalently with GDP, guanosine 5'-diphosphate.
Interacting selectively and non-covalently with pyrimidine nucleotide, any compound consisting of a pyrimidine nucleoside esterified with (ortho)phosphate.
Catalysis of the transfer of a palmitoyl group to a nitrogen atom on the acceptor molecule.
Catalysis of the transfer of a myristoyl (CH3-[CH2]12-CO-) group to an acceptor molecule.
Catalysis of the transfer of a phosphate group, usually from ATP, to an amino acid substrate.
Modulates the activity of a kinase, an enzyme which catalyzes of the transfer of a phosphate group, usually from ATP, to a substrate molecule.
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.
Catalysis of the hydrolysis of an acetyl group or groups from a substrate molecule.
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.
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways within a cell or an organism.
regulation of multicellular organismal metabolic process
regulation of organismal metabolic process
Interacting selectively and non-covalently with a centromere, a region of chromosome where the spindle fibers attach during mitosis and meiosis.
The chemical reactions and pathways resulting in the formation of aromatic compounds, any substance containing an aromatic carbon ring.
aromatic hydrocarbon biosynthetic process
The chemical reactions and pathways involving a protein. Includes protein modification.
protein metabolic process and modification
multicellular organismal protein metabolic process
Any process involved in the maintenance of an internal steady state at the level of the cell.
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.
Interacting selectively and non-covalently with oxygen (O2).
Interacting selectively and non-covalently with and responding, e.g. by conformational change, to changes in the cellular level of oxygen (O2).
Interacting selectively and non-covalently with any growth factor, proteins or polypeptides that stimulate a cell or organism to grow or proliferate.
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.
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.
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.
Interacting selectively and non-covalently with ribosomal RNA.
Interacting selectively and non-covalently with an immunoglobulin of an IgA isotype.
Interacting selectively and non-covalently with an immunoglobulin of the IgE isotype.
Interacting selectively and non-covalently with an immunoglobulin of an IgG isotype.
Interacting selectively and non-covalently with an immunoglobulin.
Modulates the activity of a protein kinase, an enzyme which phosphorylates a protein.
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.
Interacting selectively and non-covalently with any enzyme.
Interacting selectively and non-covalently with a kinase, any enzyme that catalyzes the transfer of a phosphate group.
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.
Interacting selectively and non-covalently with any phosphatase.
Interacting selectively and non-covalently with any protein phosphatase.
Interacting selectively and non-covalently with a specific domain of a protein.
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.
Catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein; increases the activity of a cyclin-dependent protein kinase (CDK).
cyclin-dependent protein kinase activating kinase, intrinsic catalyst activity
cyclin-dependent protein kinase activating kinase activity
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.
modification-dependent protein breakdown
modification-dependent protein catabolism
modification-dependent protein degradation
modification-initiated protein catabolic process
modification-initiated protein catabolism
protein-ligand-dependent protein catabolic process
protein-ligand-dependent protein catabolism
modification-dependent protein catabolic process
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.
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.
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.
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.
Interacting selectively and non-covalently with interleukin-8.
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.
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.
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.
Interacting selectively and non-covalently with interferon-gamma. Interferon gamma is the only member of the type II interferon found so far.
Interacting selectively and non-covalently with interleukin-1.
Interacting selectively and non-covalently with interleukin-10.
Interacting selectively and non-covalently with interleukin-11.
Interacting selectively and non-covalently with interleukin-12.
Interacting selectively and non-covalently with interleukin-13.
Interacting selectively and non-covalently with interleukin-14.
Interacting selectively and non-covalently with any member of the interleukin-17 family of cytokines.
Interacting selectively and non-covalently with interleukin-2.
Interacting selectively and non-covalently with interleukin-21.
Interacting selectively and non-covalently with interleukin-3.
Interacting selectively and non-covalently with interleukin-4.
Interacting selectively and non-covalently with interleukin-5.
Interacting selectively and non-covalently with interleukin-6.
Interacting selectively and non-covalently with interleukin-7.
Interacting selectively and non-covalently with interleukin-9.
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.
Interacting selectively and non-covalently with diacylglycerol, a diester of glycerol and two fatty acids.
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.
Please note that this term does not refer to the in vitro assay called erythrocyte rosetting.
modulation by symbiont of host erythrocyte aggregation
The directed movement into a tissue or a cell or organelle of externally available hemoglobin by receptor-mediated endocytosis.
Interacting selectively and non-covalently with heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring.
The process that results in the loss of attachments of a cell in the ventricular zone.
down regulation of cell adhesion in ventricular zone
down-regulation of cell adhesion in ventricular zone
downregulation of cell adhesion in ventricular zone
inhibition of cell adhesion in ventricular zone
negative regulation of cell adhesion in ventricular zone
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.
down regulation of cell-glial cell adhesion involved in cerebral cortex lamination
down-regulation of cell-glial cell adhesion involved in cerebral cortex lamination
downregulation of cell-glial cell adhesion involved in cerebral cortex lamination
inhibition of cell-glial cell adhesion involved in cerebral cortex lamination
negative regulation of cell-glial cell adhesion involved in cerebral cortex lamination
The process that modulates the frequency, rate or extent of cell proliferation in the dorsal spinal cord.
regulation of cell proliferation in dorsal spinal cord
Any process that modulates the frequency, rate or extent of attachment of a cell to another cell.
Any process that stops, prevents or reduces the rate or extent of cell adhesion to another cell.
negative regulation of cell-cell adhesion
Any process that activates or increases the rate or extent of cell adhesion to another cell.
positive regulation of cell-cell adhesion
Any process that modulates the frequency, rate or extent of transmembrane transporter activity.
regulation of transmembrane transporter activity
A process in which the transfer of one or more phosphate groups to a substrate transmits a signal to the phosphorylated substrate.
signal transduction via phosphorylation event
signal transmission via phosphorylation event
signal transduction by protein phosphorylation
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.
signal transduction via a cis-phosphorylation event
signal transmission via a cis-phosphorylation event
signal transmission via auto-phosphorylation
signal transduction by cis-phosphorylation
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.
signal transduction via a trans-phosphorylation event
signal transmission via a trans-phosphorylation event
signal transduction by trans-phosphorylation
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.
regulation of gene expression as a consequence of signal transmission
signal transduction involved in regulation of gene expression
Interacting selectively and non-covalently with the major histocompatibility complex.
Interacting selectively and non-covalently with the class I major histocompatibility complex.
Interacting selectively and non-covalently with the class Ib major histocompatibility complex.
Interacting selectively and non-covalently with the class II major histocompatibility complex.
Interacting selectively and non-covalently with major histocompatibility complex class I molecules via the antigen binding groove.
MHC class I protein binding, via antigen binding groove
Interacting selectively and non-covalently with major histocompatibility complex class I molecules via the lateral surface.
MHC class I protein binding, via lateral surface
Interacting selectively and non-covalently with major histocompatibility complex class Ib molecules.
Interacting selectively and non-covalently with major histocompatibility complex class Ib molecules via the antigen binding groove.
MHC class Ib protein binding, via antigen binding groove
Interacting selectively and non-covalently with major histocompatibility complex class Ib molecules via the lateral surface.
MHC class Ib protein binding, via lateral surface
Any process that modulates the frequency, rate or extent of a signaling process.
Any process that activates, maintains or increases the frequency, rate or extent of a signaling process.
positive regulation of signalling process
positive regulation of signaling process
Any process that stops, prevents, or reduces the frequency, rate or extent of a signaling process.
negative regulation of signaling process
negative regulation of signalling process
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.
A growth factor that binds selectively and non-covalently to glial cell-derived neurotrophic factor receptors.
glial cell line-derived neurotrophic factor receptor ligand
glial cell line-derived neurotrophic factor receptor binding
glial cell-derived neurotrophic factor receptor binding
Interacting selectively and non-covalently with manganese (Mn) ions.
Interacting selectively and non-covalently with molybdenum (Mo) ions.
Any process that modulates the frequency, rate or extent of attachment of a cell to another cell or to the extracellular matrix.
cell adhesion receptor regulator activity
Interacting selectively and non-covalently with the peripheral benzodiazepine receptor (PBR).
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.
multicellular organismal protein catabolic process
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.
Interacting selectively and non-covalently with a PDZ domain of a protein, a domain found in diverse signaling proteins.
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.
low-density lipoprotein particle binding
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.
Interacting selectively and non-covalently with troponin C, the calcium-binding subunit of the troponin complex.
Interacting selectively and non-covalently with semaphorin receptors.
Binds to and modulates the activity of an enzyme.
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'.
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.
Interacting selectively and non-covalently with any polysaccharide, a polymer of many (typically more than 10) monosaccharide residues linked glycosidically.
Interacting selectively and non-covalently with cellulose.
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.
Interacting selectively and non-covalently with a LRR domain (leucine rich repeats) of a protein.
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.
Binds to and increases the activity of a protein kinase, an enzyme which phosphorylates a protein.
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.
The directed movement of chloride ions from one side of an epithelium to the other.
Interacting selectively and non-covalently with an estrogen receptor.
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.
Interacting selectively and non-covalently with the enzyme protein phosphatase 2B.
Interacting selectively and non-covalently with the SNAP receptor syntaxin-3.
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.
Interacts with the fibroblast growth factor receptor to reduce the action of another ligand, the agonist.
fibroblast growth factor receptor antagonist activity
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.
Interacting selectively and non-covalently with the interleukin-17 receptor.
Interacting selectively and non-covalently with receptors for intercellular adhesion molecule-3 (ICAM-3), such as DC-SIGN and LFA-1.
intercellular adhesion molecule-3 receptor ligand
intercellular adhesion molecule-3 receptor binding
Interacting selectively and non-covalently with the high molecular weight B cell growth factor receptor.
high molecular weight B lymphocyte growth factor receptor binding
high molecular weight B-cell growth factor receptor binding
high molecular weight B-lymphocyte growth factor receptor binding
high molecular weight B cell growth factor receptor ligand
high molecular weight B cell growth factor receptor binding
Interacting selectively and non-covalently with the interleukin-17E receptor.
Interacting selectively and non-covalently with lactose, a disaccharide of glucose and galactose, the carbohydrate of milk.
A small peptide excreted by a naturally transformable bacterium (e.g. Bacillus subtilis) that transmits a signal required for the establishment of competence.
Interacting selectively and non-covalently with hemoglobin, an oxygen carrying, conjugated protein containing four heme groups and globin.
Interacting selectively and non-covalently with ankyrin, a 200 kDa cytoskeletal protein that attaches other cytoskeletal proteins to integral membrane proteins.
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.
Interacting selectively and non-covalently with small nucleolar RNA.
Interacting selectively and non-covalently with any part of a small nucleolar ribonucleoprotein particle.
Catalysis of the reaction: acyl-CoA + dihydrolipoamide = CoA + S-acyldihydrolipoamide.
dihydrolipoamide S-acyltransferase activity
Interacting selectively and non-covalently with Hsp70 proteins, any of a group of heat shock proteins around 70kDa in size.
The function of interacting (directly or indirectly) with receptors such that the proportion of receptors in the active form is changed.
The function of interacting (directly or indirectly) with receptors such that the proportion of receptors in the active form is decreased.
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.
Interacting selectively and non-covalently with cAMP, the nucleotide cyclic AMP (adenosine 3',5'-cyclophosphate).
Interacting selectively and non-covalently with cGMP, the nucleotide cyclic GMP (guanosine 3',5'-cyclophosphate).
Interacting selectively and non-covalently with adenyl nucleotides, any compound consisting of adenosine esterified with (ortho)phosphate.
Specifies the site of a posttranscriptional modification in an RNA molecule by base pairing with a short sequence around the target residue.
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.
Specifies the site of a posttranscriptional modification in an rRNA molecule by base pairing with a short sequence around the target residue.
Specifies the site of a posttranscriptional modification in a tRNA molecule by base pairing with a short sequence around the target residue.
Specifies the site of pseudouridylation in an RNA molecule by base pairing with a short sequence around the target residue.
Specifies the site of pseudouridylation in an rRNA molecule by base pairing with a short sequence around the target residue.
Specifies the site of pseudouridylation in a tRNA molecule by base pairing with a short sequence around the target residue.
Specifies the site of 2'-O-ribose methylation in an RNA molecule by base pairing with a short sequence around the target residue.
RNA 2'-O-ribose methylation guide activity
Specifies the site of 2'-O-ribose methylation in an rRNA molecule by base pairing with a short sequence around the target residue.
rRNA 2'-O-ribose methylation guide activity
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.
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.
snRNA 2'-O-ribose methylation guide activity
Specifies the site of 2'-O-ribose methylation in a tRNA molecule by base pairing with a short sequence around the target residue.
tRNA 2'-O-ribose methylation guide activity
Activity that provides specificity to a pseudouridine synthetase by using base complementarity to guide site-specific pseudouridylations to a small nuclear RNA molecule.
Specifies the site of a posttranscriptional modification in an snRNA molecule by base pairing with a short sequence around the target residue.
Interacting selectively and non-covalently with the U1 small nuclear RNA (U1 snRNA).
Note that this term may be useful for annotating other small nuclear RNAs (snRNAs).
Interacting selectively and non-covalently with the U2 small nuclear RNA (U2 snRNA).
Interacting selectively and non-covalently with the U4 small nuclear RNA (U4 snRNA).
Interacting selectively and non-covalently with the U4atac small nuclear RNA (U4atac snRNA).
Interacting selectively and non-covalently with the U5 small nuclear RNA (U5 snRNA).
Interacting selectively and non-covalently with the U6atac small nuclear RNA (U6atac snRNA).
Interacting selectively and non-covalently with the U11 small nuclear RNA (U11 snRNA).
Interacting selectively and non-covalently with the U12 small nuclear RNA (U12 snRNA).
Interacting selectively and non-covalently with the pre-mRNA 5' splice site sequence.
Interacting selectively and non-covalently with the pre-mRNA 3' splice site sequence.
Interacting selectively and non-covalently with the 3' end of the U6 small nuclear RNA (U6 snRNA).
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.
Rac guanyl-nucleotide exchange factor activity
Modulates the rate of GTP hydrolysis by a GTPase.
small GTPase regulatory/interacting protein activity
The delamination process that results in the splitting off of border cells from the anterior epithelium, prior to border cell migration.
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.
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.
Interacting selectively and non-covalently with beta-2-microglobulin.
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.
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.
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.
endoplasmic reticulum signal peptide binding
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.
mitochondrial targeting sequence binding
mitochondrion targeting sequence binding
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.
The catalysis of phosphate removal from a phosphotyrosine using cysteine as a nucleophile and proceed by means of a thiol-phosphate intermediate.
protein tyrosine phosphatase activity, via thiol-phosphate intermediate
Catalysis of the reaction: protein tyrosine phosphate + H2O = protein tyrosine + phosphate. This reaction requires metal ions.
protein tyrosine phosphatase activity, metal-dependent
Interacting selectively and non-covalently with potassium (K+) ions.
Interacting selectively and non-covalently with Tat, a viral transactivating regulatory protein from the human immunodeficiency virus, or the equivalent protein from another virus.
Interacting selectively and non-covalently with a receptor that possesses protein tyrosine kinase activity.
transmembrane receptor protein tyrosine kinase ligand binding
Interacting selectively and non-covalently with molybdate (MoO4 2-) ions.
Interacting selectively and non-covalently with thiamine (vitamin B1), a water soluble vitamin present in fresh vegetables and meats, especially liver.
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.
Interacting selectively and non-covalently with taurine.
Interacting selectively and non-covalently with double-stranded DNA containing one or more mismatches.
Interacting selectively and non-covalently with a kininogen, any of a group of plasma proteins that are kinin precursors.
Interacting selectively and non-covalently with a kininogen of high molecular mass.
Interacting selectively and non-covalently with a kininogen of low molecular mass.
Interacting selectively and non-covalently with a high molecular weight kininogen receptor.
high molecular weight kininogen receptor binding
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.
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.
Interacting selectively and non-covalently with troponin I, the inhibitory subunit of the troponin complex.
Interacting selectively and non-covalently with troponin T, the tropomyosin-binding subunit of the troponin complex.
Interacting selectively and non-covalently with a heat shock protein, any protein synthesized or activated in response to heat shock.
Interacting selectively and non-covalently with phosphopantetheine, the vitamin pantetheine 4'-(dihydrogen phosphate).
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.
broad-complex, tramtrack, and bric-a-brac domain binding
Interacting selectively and non-covalently with denatured proteins.
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.
Interacting selectively and non-covalently with a small monomeric GTPase.
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.
Any process that stops, prevents, or reduces the frequency, rate or extent of cell killing.
Any process that activates or increases the frequency, rate or extent of cell killing.
Interacting selectively and non-covalently with a translation initiation factor, any polypeptide factor involved in the initiation of ribosome-mediated translation.
Interacting selectively and non-covalently with eukaryotic initiation factor 4G, a polypeptide factor involved in the initiation of ribosome-mediated translation.
Interacting selectively and non-covalently with sodium ions (Na+).
Interacting selectively and non-covalently with lithium ions (Li+).
Interacting selectively and non-covalently with chloride ions (Cl-).
Interacting selectively and non-covalently with lipoic acid, 1,2-dithiolane-3-pentanoic acid.
Interacting selectively and non-covalently with a carboxylic acid, any organic acid containing one or more carboxyl (COOH) groups or anions (COO-).
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.
Interacting selectively and non-covalently with cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom.
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.
Interacting selectively and non-covalently with a hexon, the major protein component of the icosahedral capsid of an adenovirus.
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.
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.
Interacting selectively and non-covalently with a mitogen-activated protein kinase kinase, any protein that can phosphorylate a MAP kinase.
mitogen-activated protein kinase kinase binding
Interacting selectively and non-covalently with a mitogen-activated protein kinase kinase kinase, any protein that can phosphorylate a MAP kinase kinase.
mitogen-activated protein kinase kinase kinase binding
Interacting selectively and non-covalently with a class III myosin; myosin III is monomeric and has an N terminal kinase domain.
Interacting selectively and non-covalently with a class V myosin; myosin V is a dimeric molecule involved in intracellular transport.
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.
gonadotrophin-releasing hormone receptor binding
gonadotropin-releasing hormone receptor binding
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.
thyrotropin releasing hormone receptor binding
thyrotropin-releasing hormone receptor ligand
thyrotropin-releasing hormone receptor binding
Interacting selectively and non-covalently with the brain-derived neurotrophic factor receptor.
brain-derived neurotrophic factor ligand
brain-derived neurotrophic factor receptor binding
Interacting selectively and non-covalently with a protein upon poly-ubiquitination of the target protein.
polyubiquitin modification-dependent protein binding
Interacting selectively and non-covalently with a ubiquitin conjugating enzyme, any of the E2 proteins.
Interacting selectively and non-covalently with a ubiquitin protein ligase enzyme, any of the E3 proteins.
Interacting selectively and non-covalently with an opioid receptor.
Interacting selectively and non-covalently with replication fork barriers, sites that inhibit the progress of replication forks.
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.
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.
cellular response to extracellular stimulus
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.
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.
Interacting selectively and non-covalently with a G-protein beta subunit.
Interacting selectively and non-covalently with a G-protein gamma subunit.
Interacting selectively and non-covalently with a complex of G-protein beta/gamma subunits.
G-protein beta/gamma-subunit complex binding
Interacting selectively and non-covalently with an adenosine receptor.
Interacting selectively and non-covalently with an A1 adenosine receptor.
Interacting selectively and non-covalently with an A2A adenosine receptor.
Interacting selectively and non-covalently with an A2B adenosine receptor.
Interacting selectively and non-covalently with an A3 adenosine receptor.
Interacting selectively and non-covalently with an adrenergic receptor.
Interacting selectively and non-covalently with an alpha-1A adrenergic receptor.
Interacting selectively and non-covalently with an alpha-1B adrenergic receptor.
Interacting selectively and non-covalently with an alpha-1D adrenergic receptor.
Interacting selectively and non-covalently with an alpha-2A adrenergic receptor.
Interacting selectively and non-covalently with an alpha-2B adrenergic receptor.
Interacting selectively and non-covalently with an alpha-2C adrenergic receptor.
Interacting selectively and non-covalently with a beta-1 adrenergic receptor.
Interacting selectively and non-covalently with a beta-2 adrenergic receptor.
Interacting selectively and non-covalently with a beta-3 adrenergic receptor.
Interacting selectively and non-covalently with an adrenomedullin receptor.
Interacting selectively and non-covalently with an angiotensin receptor.
Interacting selectively and non-covalently with a type 1 angiotensin receptor.
Interacting selectively and non-covalently with a type 2 angiotensin receptor.
Interacting selectively and non-covalently with an apelin receptor.
Interacting selectively and non-covalently with a bombesin receptor.
Interacting selectively and non-covalently with a subtype 3 bombesin receptor.
Interacting selectively and non-covalently with an endothelin A receptor.
Interacting selectively and non-covalently with an endothelin B receptor.
Interacting selectively and non-covalently with a gastrin-releasing peptide receptor.
gastrin-releasing peptide receptor ligand
gastrin-releasing peptide receptor binding
Interacting selectively and non-covalently with a neuromedin B receptor.
Interacting selectively and non-covalently with a bradykinin receptor.
Interacting selectively and non-covalently with a B1 bradykinin receptor.
Interacting selectively and non-covalently with a B2 bradykinin receptor.
Interacting selectively and non-covalently with a C5a anaphylatoxin chemotactic receptor.
C5a anaphylatoxin chemotactic receptor ligand
C5a anaphylatoxin chemotactic receptor binding
Interacting selectively and non-covalently with a C5L2 anaphylatoxin chemotactic receptor.
C5L2 anaphylatoxin chemotactic receptor ligand
C5L2 anaphylatoxin chemotactic receptor binding
Interacting selectively and non-covalently with a calcitonin receptor.
Interacting selectively and non-covalently with a cannabinoid receptor.
Interacting selectively and non-covalently with a type 1 cannabinoid receptor.
Interacting selectively and non-covalently with a type 2 cannabinoid receptor.
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.
Interacting selectively and non-covalently with a hemoglobin alpha chain.
Interacting selectively and non-covalently with a hemoglobin beta chain.
Interacting selectively and non-covalently with a CXCR4 chemokine receptor.
stromal cell-derived factor 1 receptor binding
Interacting selectively and non-covalently with a CXCR5 chemokine receptor.
type 1 Burkitt's lymphoma receptor binding
Interacting selectively and non-covalently with a CXCR6 chemokine receptor.
Interacting selectively and non-covalently with a CCR1 chemokine receptor.
macrophage inflammatory protein-1 alpha receptor binding
Interacting selectively and non-covalently with a CCR2 chemokine receptor.
monocyte chemoattractant protein 1 receptor binding
Interacting selectively and non-covalently with a CCR3 chemokine receptor.
Interacting selectively and non-covalently with a CCR4 chemokine receptor.
Interacting selectively and non-covalently with a CCR5 chemokine receptor.
Interacting selectively and non-covalently with a CCR6 chemokine receptor.
Interacting selectively and non-covalently with a CCR7 chemokine receptor.
type 1 EBV-induced G-protein coupled receptor binding
Interacting selectively and non-covalently with a CCR8 chemokine receptor.
Interacting selectively and non-covalently with a CCR9 chemokine receptor.
Interacting selectively and non-covalently with a CCR10 chemokine receptor.
Interacting selectively and non-covalently with a CCR11 chemokine receptor.
Interacting selectively and non-covalently with a CX3C chemokine receptor.
Interacting selectively and non-covalently with a XCR1 chemokine receptor.
Interacting selectively and non-covalently with a cholecystokinin receptor.
Interacting selectively and non-covalently with a type A cholecystokinin receptor.
Interacting selectively and non-covalently with a type B gastrin/cholecystokinin receptor.
type B gastrin/cholecystokinin receptor ligand
type B gastrin/cholecystokinin receptor binding
Interacting selectively and non-covalently with a cysteinyl leukotriene receptor.
Interacting selectively and non-covalently with a type 1 cysteinyl leukotriene receptor.
type 1 cysteinyl leukotriene receptor ligand
type 1 cysteinyl leukotriene receptor binding
Interacting selectively and non-covalently with a type 2 cysteinyl leukotriene receptor.
type 2 cysteinyl leukotriene receptor ligand
type 2 cysteinyl leukotriene receptor binding
Interacting selectively and non-covalently with a D1 dopamine receptor.
Interacting selectively and non-covalently with a D2 dopamine receptor.
Interacting selectively and non-covalently with a D3 dopamine receptor.
Interacting selectively and non-covalently with a D4 dopamine receptor.
Interacting selectively and non-covalently with a D5 dopamine receptor.
Interacting selectively and non-covalently with an endothelial differentiation G protein-coupled receptor.
endothelial differentiation G-protein coupled receptor binding
endothelial differentiation G-protein coupled receptor ligand
endothelial differentiation G protein-coupled receptor binding
Interacting selectively and non-covalently with an Edg-1 sphingosine 1-phosphate receptor.
Edg-1 sphingosine 1-phosphate receptor ligand
Edg-1 sphingosine 1-phosphate receptor binding
Interacting selectively and non-covalently with an Edg-2 lysophosphatidic acid receptor.
Edg-2 lysophosphatidic acid receptor ligand
Edg-2 lysophosphatidic acid receptor binding
Interacting selectively and non-covalently with an Edg-3 sphingosine 1-phosphate receptor.
Edg-3 sphingosine 1-phosphate receptor ligand
Edg-3 sphingosine 1-phosphate receptor binding
Interacting selectively and non-covalently with an Edg-4 lysophosphatidic acid receptor.
Edg-4 lysophosphatidic acid receptor ligand
Edg-4 lysophosphatidic acid receptor binding
Interacting selectively and non-covalently with an Edg-5 sphingosine 1-phosphate receptor.
Edg-5 sphingosine 1-phosphate receptor ligand
Edg-5 sphingosine 1-phosphate receptor binding
Interacting selectively and non-covalently with an Edg-6 sphingosine 1-phosphate receptor.
Edg-6 sphingosine 1-phosphate receptor ligand
Edg-6 sphingosine 1-phosphate receptor binding
Interacting selectively and non-covalently with an Edg-7 lysophosphatidic acid receptor.
Edg-7 lysophosphatidic acid receptor ligand
Edg-7 lysophosphatidic acid receptor binding
Interacting selectively and non-covalently with a fMet-Leu-Phe receptor.
Interacting selectively and non-covalently with a follicle-stimulating hormone receptor.
follicle stimulating hormone receptor binding
follicle stimulating hormone receptor ligand
follicle-stimulating hormone receptor binding
Interacting selectively and non-covalently with a galanin receptor.
Interacting selectively and non-covalently with a type 1 galanin receptor.
Interacting selectively and non-covalently with a type 2 galanin receptor.
Interacting selectively and non-covalently with a type 3 galanin receptor.
Interacting selectively and non-covalently with a gastric inhibitory polypeptide receptor.
gastric inhibitory polypeptide receptor ligand
gastric inhibitory polypeptide receptor binding
Interacting selectively and non-covalently with a ghrelin receptor.
type 1 growth hormone secretagogue GH-releasing peptide receptor binding
Interacting selectively and non-covalently with a glucagon receptor.
Interacting selectively and non-covalently with a growth hormone-releasing hormone receptor.
growth hormone-releasing hormone receptor ligand
growth hormone-releasing hormone receptor binding
Interacting selectively and non-covalently with a type 1 hypocretin receptor.
Interacting selectively and non-covalently with a type 2 hypocretin receptor.
Interacting selectively and non-covalently with a kisspeptin receptor.
Interacting selectively and non-covalently with a leukotriene receptor.
Interacting selectively and non-covalently with a lutropin-choriogonadotropic hormone receptor.
lutropin-choriogonadotropic hormone receptor ligand
lutropin-choriogonadotropic hormone receptor binding
Interacting selectively and non-covalently with a melanin-concentrating hormone receptor.
melanin-concentrating hormone receptor ligand
melanin-concentrating hormone receptor binding
Interacting selectively and non-covalently with a type 1 melanin-concentrating hormone receptor.
type 1 melanin-concentrating hormone receptor ligand
type 1 melanin-concentrating hormone receptor binding
Interacting selectively and non-covalently with a type 2 melanin-concentrating hormone receptor.
type 2 melanin-concentrating hormone receptor ligand
type 2 melanin-concentrating hormone receptor binding
Interacting selectively and non-covalently with a melanocortin receptor.
Interacting selectively and non-covalently with a corticotropin hormone receptor.
adrenocorticotropin hormone receptor binding
adrenocorticotropic hormone receptor ligand
Interacting selectively and non-covalently with a type 3 melanocortin receptor.
Interacting selectively and non-covalently with a type 4 melanocortin receptor.
Interacting selectively and non-covalently with a type 5 melanocortin receptor.
Interacting selectively and non-covalently with a melatonin receptor.
Interacting selectively and non-covalently with a type 1A melatonin receptor.
Interacting selectively and non-covalently with a type 1B melatonin receptor.
Interacting selectively and non-covalently with a H9 melatonin receptor.
Interacting selectively and non-covalently with a motilin receptor.
Interacting selectively and non-covalently with a G protein-coupled acetylcholine receptor.
G-protein coupled acetylcholine receptor binding
muscarinic acetylcholine receptor binding
M1 muscarinic acetylcholine receptor binding
M1 muscarinic acetylcholine receptor ligand
M2 muscarinic acetylcholine receptor binding
M2 muscarinic acetylcholine receptor ligand
M3 muscarinic acetylcholine receptor binding
M3 muscarinic acetylcholine receptor ligand
M4 muscarinic acetylcholine receptor binding
M4 muscarinic acetylcholine receptor ligand
M5 muscarinic acetylcholine receptor binding
M5 muscarinic acetylcholine receptor ligand
muscarinic acetylcholine receptor ligand
G protein-coupled acetylcholine receptor binding
Interacting selectively and non-covalently with a G protein-coupled (metabotropic) GABA receptor.
Interacting selectively and non-covalently with a type 1 metabotropic GABA receptor.
type 1 metabotropic GABA receptor ligand
type 1 metabotropic GABA receptor binding
Interacting selectively and non-covalently with a type 2 metabotropic GABA receptor.
type 2 metabotropic GABA receptor ligand
type 2 metabotropic GABA receptor binding
Interacting selectively and non-covalently with a type 1 metabotropic glutamate receptor.
type 1 metabotropic glutamate receptor ligand
type 1 metabotropic glutamate receptor binding
Interacting selectively and non-covalently with a type 2 metabotropic glutamate receptor.
type 2 metabotropic glutamate receptor ligand
type 2 metabotropic glutamate receptor binding
Interacting selectively and non-covalently with a type 3 metabotropic glutamate receptor.
type 3 metabotropic glutamate receptor ligand
type 3 metabotropic glutamate receptor binding
Interacting selectively and non-covalently with a type 4 metabotropic glutamate receptor.
type 4 metabotropic glutamate receptor ligand
type 4 metabotropic glutamate receptor binding
Interacting selectively and non-covalently with a type 5 metabotropic glutamate receptor.
type 5 metabotropic glutamate receptor ligand
type 5 metabotropic glutamate receptor binding
Interacting selectively and non-covalently with a type 6 metabotropic glutamate receptor.
type 6 metabotropic glutamate receptor ligand
type 6 metabotropic glutamate receptor binding
Interacting selectively and non-covalently with a type 7 metabotropic glutamate receptor.
type 7 metabotropic glutamate receptor ligand
type 7 metabotropic glutamate receptor binding
Interacting selectively and non-covalently with a type 8 metabotropic glutamate receptor.
type 8 metabotropic glutamate receptor ligand
type 8 metabotropic glutamate receptor binding
Interacting selectively and non-covalently with a G protein-coupled (metabotropic) histamine receptor.
G-protein coupled histamine receptor binding
G protein-coupled histamine receptor binding
Interacting selectively and non-covalently with a H1 histamine receptor.
Interacting selectively and non-covalently with a H2 histamine receptor.
Interacting selectively and non-covalently with a H3 histamine receptor.
Interacting selectively and non-covalently with a H4 histamine receptor.
Interacting selectively and non-covalently with a G protein-coupled (metabotropic) nucleotide receptor.
G-protein coupled nucleotide receptor binding
metabotropic nucleotide receptor binding
G protein-coupled nucleotide receptor binding
Interacting selectively and non-covalently with a P2Y1 nucleotide receptor.
Interacting selectively and non-covalently with a P2Y2 nucleotide receptor.
Interacting selectively and non-covalently with a P2Y4 nucleotide receptor.
Interacting selectively and non-covalently with a P2Y5 nucleotide receptor.
Interacting selectively and non-covalently with a P2Y6 nucleotide receptor.
Interacting selectively and non-covalently with a P2Y8 nucleotide receptor.
Interacting selectively and non-covalently with a P2Y9 nucleotide receptor.
Interacting selectively and non-covalently with a P2Y10 nucleotide receptor.
Interacting selectively and non-covalently with a P2Y11 nucleotide receptor.
Interacting selectively and non-covalently with a metabotropic serotonin receptor.
G-protein coupled serotonin receptor binding
metabotropic 5-hydroxytryptamine receptor binding
G protein-coupled serotonin receptor binding
Interacting selectively and non-covalently with a type 1B serotonin receptor.
Interacting selectively and non-covalently with a type 1D serotonin receptor.
Interacting selectively and non-covalently with a type 1E serotonin receptor.
Interacting selectively and non-covalently with a type 1F serotonin receptor.
Interacting selectively and non-covalently with a type 2A serotonin receptor.
Interacting selectively and non-covalently with a type 2B serotonin receptor.
Interacting selectively and non-covalently with a type 2C serotonin receptor.
Interacting selectively and non-covalently with a type 4 serotonin receptor.
Interacting selectively and non-covalently with a type 5A serotonin receptor.
Interacting selectively and non-covalently with a type 5B serotonin receptor.
Interacting selectively and non-covalently with a type 6 serotonin receptor.
Interacting selectively and non-covalently with a type 7 serotonin receptor.
Interacting selectively and non-covalently with a neurokinin receptor.
Interacting selectively and non-covalently with a substance P receptor.
Interacting selectively and non-covalently with a neuromedin K receptor.
Interacting selectively and non-covalently with a substance K receptor.
Interacting selectively and non-covalently with a type 1 neuromedin U receptor.
Interacting selectively and non-covalently with a type 2 neuromedin U receptor.
Interacting selectively and non-covalently with a neuropeptide Y receptor.
Interacting selectively and non-covalently with a type 1 neuropeptide Y receptor.
Interacting selectively and non-covalently with a type 2 neuropeptide Y receptor.
Interacting selectively and non-covalently with a type 4 neuropeptide Y receptor.
Interacting selectively and non-covalently with a type 5 neuropeptide Y receptor.
Interacting selectively and non-covalently with a neurotensin receptor.
Interacting selectively and non-covalently with a type 1 neurotensin receptor.
Interacting selectively and non-covalently with an olfactory receptor.
Interacting selectively and non-covalently with a delta-type opioid receptor.
Interacting selectively and non-covalently with a kappa-type opioid receptor.
Interacting selectively and non-covalently with a mu-type opioid receptor.
Interacting selectively and non-covalently with a nociceptin receptor.
Interacting selectively and non-covalently with an orexigenic neuropeptide QRFP receptor.
orexigenic neuropeptide QRFP receptor ligand
orexigenic neuropeptide QRFP receptor binding
Interacting selectively and non-covalently with an oxytocin receptor.
Interacting selectively and non-covalently with a parathyroid hormone receptor.
Interacting selectively and non-covalently with a type 1 parathyroid hormone receptor.
type 1 parathyroid hormone receptor ligand
type 1 parathyroid hormone receptor binding
Interacting selectively and non-covalently with a pituitary adenylate cyclase-activating polypeptide receptor.
pituitary adenylate cyclase activating peptide receptor binding
pituitary adenylate cyclase-activating peptide receptor ligand
pituitary adenylate cyclase-activating polypeptide receptor binding
Interacting selectively and non-covalently with a platelet activating factor receptor.
platelet activating factor receptor ligand
platelet activating factor receptor binding
Interacting selectively and non-covalently with a prolactin-releasing peptide receptor.
prolactin-releasing peptide receptor ligand
prolactin-releasing peptide receptor binding
Interacting selectively and non-covalently with a prostanoid receptor.
Interacting selectively and non-covalently with a prostaglandin D2 receptor.
Interacting selectively and non-covalently with an EP1 subtype prostaglandin E2 receptor.
EP1 subtype prostaglandin E2 receptor ligand
EP1 subtype prostaglandin E2 receptor binding
Interacting selectively and non-covalently with an EP2 subtype prostaglandin E2 receptor.
EP2 subtype prostaglandin E2 receptor ligand
EP2 subtype prostaglandin E2 receptor binding
Interacting selectively and non-covalently with an EP3 subtype prostaglandin E2 receptor.
EP3 subtype prostaglandin E2 receptor ligand
EP3 subtype prostaglandin E2 receptor binding
Interacting selectively and non-covalently with an EP4 subtype prostaglandin E2 receptor.
EP4 subtype prostaglandin E2 receptor ligand
EP4 subtype prostaglandin E2 receptor binding
Interacting selectively and non-covalently with a prostaglandin F2-alpha receptor.
Interacting selectively and non-covalently with a prostacyclin receptor.
Interacting selectively and non-covalently with a thromboxane A2 receptor.
Interacting selectively and non-covalently with a proteinase activated receptor.
Interacting selectively and non-covalently with a type 1 proteinase activated receptor.
type 1 proteinase activated receptor ligand
type 1 proteinase activated receptor binding
Interacting selectively and non-covalently with a type 2 proteinase activated receptor.
type 2 proteinase activated receptor ligand
type 2 proteinase activated receptor binding
Interacting selectively and non-covalently with a type 3 proteinase activated receptor.
type 3 proteinase activated receptor ligand
type 3 proteinase activated receptor binding
Interacting selectively and non-covalently with a type 4 proteinase activated receptor.
type 4 proteinase activated receptor ligand
type 4 proteinase activated receptor binding
Interacting selectively and non-covalently with a secretin receptor.
Interacting selectively and non-covalently with a somatostatin receptor.
Interacting selectively and non-covalently with a type 1 somatostatin receptor.
Interacting selectively and non-covalently with a type 2 somatostatin receptor.
Interacting selectively and non-covalently with a type 3 somatostatin receptor.
Interacting selectively and non-covalently with a type 4 somatostatin receptor.
Interacting selectively and non-covalently with a type 5 somatostatin receptor.
Interacting selectively and non-covalently with a taste receptor.
Interacting selectively and non-covalently with a type 1 member 1 taste receptor.
Interacting selectively and non-covalently with a type 1 member 2 taste receptor.
Interacting selectively and non-covalently with a type 1 member 3 taste receptor.
Interacting selectively and non-covalently with a urotensin receptor.
Interacting selectively and non-covalently with a vasoactive intestinal polypeptide receptor.
vasoactive intestinal polypeptide receptor ligand
vasoactive intestinal polypeptide receptor binding
Interacting selectively and non-covalently with a type 1 vasoactive intestinal polypeptide receptor.
type 1 vasoactive intestinal polypeptide receptor ligand
type 1 vasoactive intestinal polypeptide receptor binding
Interacting selectively and non-covalently with a type 2 vasoactive intestinal polypeptide receptor.
type 2 vasoactive intestinal polypeptide receptor ligand
type 2 vasoactive intestinal polypeptide receptor binding
Interacting selectively and non-covalently with a vasopressin receptor.
Interacting selectively and non-covalently with a V1A vasopressin receptor.
Interacting selectively and non-covalently with a V1B vasopressin receptor.
Interacting selectively and non-covalently with a V2 vasopressin receptor.
Interacting selectively and non-covalently with a cortisol receptor.
Interacting selectively and non-covalently with a mineralocorticoid receptor.
Interacting selectively and non-covalently with insulin-like growth factor I.
Interacting selectively and non-covalently with insulin-like growth factor II.
Interacting selectively and non-covalently with any thioesterase enzyme.
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.
N-terminal myristoylation domain binding
Interacting selectively and non-covalently with the interleukin-28 receptor.
Interacting selectively and non-covalently with a light chain of a myosin complex.
Interacting selectively and non-covalently with the head/neck region of a myosin heavy chain.
Interacting selectively and non-covalently with the tail region of a myosin heavy chain.
Interacting selectively and non-covalently with a light chain of a myosin I complex.
Interacting selectively and non-covalently with the head/neck region of a myosin I heavy chain.
Interacting selectively and non-covalently with the tail region of a myosin I heavy chain.
Interacting selectively and non-covalently with a light chain of a myosin II complex.
Interacting selectively and non-covalently with the head/neck region of a myosin II heavy chain.
Interacting selectively and non-covalently with the tail region of a myosin II heavy chain.
Interacting selectively and non-covalently with a heavy chain of a myosin complex.
Interacting selectively and non-covalently with a heavy chain of a myosin I complex.
Interacting selectively and non-covalently with a heavy chain of a myosin II complex.
The chemical reactions and pathways involving mitochondrial DNA.
Interacting selectively and non-covalently with a clathrin heavy chain.
Interacting selectively and non-covalently with a clathrin light chain.
Interacting selectively and non-covalently with bile acids, any of a group of steroid carboxylic acids occurring in bile.
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.
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.
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.
Any process that modulates the frequency, rate or extent of a response to an external stimulus.
regulation of response to external stimulus
Any process that stops, prevents, or reduces the frequency, rate or extent of a response to an external stimulus.
down regulation of response to external stimulus
down-regulation of response to external stimulus
downregulation of response to external stimulus
inhibition of response to external stimulus
negative regulation of response to external stimulus
Any process that activates, maintains or increases the rate of a response to an external stimulus.
up regulation of response to external stimulus
up-regulation of response to external stimulus
upregulation of response to external stimulus
activation of response to external stimulus
stimulation of response to external stimulus
positive regulation of response to external stimulus
Interacting selectively and non-covalently with alkylated residues in DNA.
Interacting selectively and non-covalently with O6-alkylguanine adducts in DNA.
Interacting selectively and non-covalently with double-stranded DNA containing insertions or deletions.
Interacting selectively and non-covalently with double-stranded DNA containing an A/C mispair.
Interacting selectively and non-covalently with double-stranded DNA containing a G/T mispair.
Interacting selectively and non-covalently with double-stranded DNA containing a single base insertion or deletion.
single base insertion or deletion binding
Interacting selectively and non-covalently with double-stranded DNA containing a dinucleotide insertion or deletion.
dinucleotide insertion or deletion binding
Interacting selectively and non-covalently with double-stranded DNA containing a single adenine insertion or a deletion that results in an unpaired adenine.
Interacting selectively and non-covalently with double-stranded DNA containing a single cytosine insertion or a deletion that results in an unpaired cytosine.
Interacting selectively and non-covalently with double-stranded DNA containing a single guanine insertion or a deletion that results in an unpaired guanine.
Interacting selectively and non-covalently with double-stranded DNA containing a single thymine insertion or a deletion that results in an unpaired thymine.
Interacting selectively and non-covalently with succinate-semialdehyde dehydrogenase.
succinic semialdehyde dehydrogenase binding
succinate-semialdehyde dehydrogenase binding
Interacting selectively and non-covalently with double-stranded DNA containing a dinucleotide repeat insertion or a deletion resulting in unpaired dinucleotide repeats.
Interacting selectively and non-covalently with a small conjugating protein such as ubiquitin or a ubiquitin-like protein.
Interacting selectively and non-covalently with the small ubiquitin-like protein SUMO.
Interacting selectively and non-covalently with a polymer of the small ubiquitin-like protein SUMO.
Interacting selectively and non-covalently with acrosin, a protein that is found in the acrosomes of sperm and possesses protease and carbohydrate binding activities.
A process that initiates the activity of an inactive store-operated calcium channel.
activation of store-operated calcium channel activity
Interacting selectively and non-covalently with phosphatidylinositol-3-phosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3' position.
phosphatidylinositol 3-phosphate binding
phosphatidylinositol-3-phosphate binding
Interacting selectively and non-covalently with oxidized residues in DNA.
Interacting selectively and non-covalently with oxidized purine residues in DNA.
Interacting selectively and non-covalently with oxidized pyrimidine residues in DNA.
oxidized pyrimidine nucleobase DNA binding
Any process that modulates the frequency, rate or extent of the directed movement of substances within cells.
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of substances within cells.
down regulation of intracellular transport
down-regulation of intracellular transport
downregulation of intracellular transport
negative regulation of intracellular transport
Any process that activates or increases the frequency, rate or extent of the directed movement of substances within cells.
up regulation of intracellular transport
up-regulation of intracellular transport
positive regulation of intracellular transport
Interacting selectively and non-covalently with a HECT, 'Homologous to the E6-AP Carboxy-Terminus', domain of a protein.
Interacting selectively and non-covalently with a mismatch repair complex.
Interacting selectively and non-covalently with the mismatch repair complex MutLalpha.
Interacting selectively and non-covalently with the mismatch repair complex MutLbeta.
Interacting selectively and non-covalently with the mismatch repair complex MutSalpha.
Interacting selectively and non-covalently with the mismatch repair complex MutSbeta.
Any process that stops or reduces the activity of a transporter.
negative regulation of transporter activity
Any process that activates or increases the activity of a transporter.
positive regulation of transporter activity
Any process that modulates the activity of an ion transporter.
regulation of ion transmembrane transporter activity
Any process that stops or reduces the activity of an ion transporter.
down regulation of ion transporter activity
down-regulation of ion transporter activity
downregulation of ion transporter activity
negative regulation of ion transporter activity
negative regulation of ion transmembrane transporter activity
Any process that activates or increases the activity of an ion transporter.
positive regulation of ion transporter activity
up regulation of ion transporter activity
up-regulation of ion transporter activity
upregulation of ion transporter activity
positive regulation of ion transmembrane transporter activity
Any process that modulates the activity of a sodium:hydrogen antiporter, which catalyzes the reaction: Na+(out) + H+(in) = Na+(in) + H+(out).
regulation of sodium:hydrogen antiporter activity
regulation of sodium:proton antiporter activity
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).
down regulation of sodium:hydrogen antiporter activity
down-regulation of sodium:hydrogen antiporter activity
downregulation of sodium:hydrogen antiporter activity
negative regulation of sodium:hydrogen antiporter activity
inhibition of sodium:hydrogen antiporter activity
negative regulation of sodium:proton antiporter activity
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).
positive regulation of sodium:hydrogen antiporter activity
up regulation of sodium:hydrogen antiporter activity
up-regulation of sodium:hydrogen antiporter activity
upregulation of sodium:hydrogen antiporter activity
activation of sodium:hydrogen antiporter activity
stimulation of sodium:hydrogen antiporter activity
positive regulation of sodium:proton antiporter activity
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.
purine-rich negative regulatory element binding
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.
Cdc42/Rac interactive binding motif binding
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.
The directed movement of calcium ions (Ca2+) into, out of or within the Golgi apparatus.
The series of events in which a stimulus from a molecule of bacterial origin is received and converted into a molecular signal.
detection of bacteria associated molecule
detection of bacterial associated molecule
detection of bacterium associated molecule
detection of molecule of bacterial origin
The series of events in which a stimulus from a molecule of fungal origin is received and converted into a molecular signal.
The series of events in which a stimulus from a molecule of oomycetes origin is received and converted into a molecular signal.
detection of oomycetes associated molecule
detection of molecule of oomycetes origin
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.
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.
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.
Interacting selectively and non-covalently, in a non-covalent manner, with muramyl dipeptide; muramyl dipeptide is derived from peptidoglycan.
A process that modulates the size of a cellular component.
Interacting selectively and non-covalently with a deoxyribonucleoside, a compound consisting of a purine or pyrimidine nitrogenous base linked to deoxyribose.
Interacting selectively and non-covalently with a purine deoxyribonucleoside, a compound consisting of a purine base linked to deoxyribose.
Interacting selectively and non-covalently with a pyrimidine deoxyribonucleoside, a compound consisting of a pyrimidine base linked to deoxyribose.
Interacting selectively and non-covalently with a ribonucleoside, a compound consisting of a purine or pyrimidine nitrogenous base linked to ribose.
Interacting selectively and non-covalently with a purine ribonucleoside, a compound consisting of a purine base linked to ribose.
Interacting selectively and non-covalently with a pyrimidine ribonucleoside, a compound consisting of a pyrimidine base linked to ribose.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Interacting selectively and non-covalently with dAMP, deoxyadenosine monophosphate.
Interacting selectively and non-covalently with dADP, deoxyadenosine diphosphate.
Interacting selectively and non-covalently with dATP, deoxyadenosine triphosphate.
Interacting selectively and non-covalently with dGMP, deoxyguanosine monophosphate.
Interacting selectively and non-covalently with dGDP, deoxyguanosine diphosphate.
Interacting selectively and non-covalently with dGTP, deoxyguanosine triphosphate.
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.
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.
Interacting selectively and non-covalently with lead (Pb) ions.
Interacting selectively and non-covalently with a GTPase activating protein.
Interacting selectively and non-covalently with a heterotrimeric G-protein.
Interacting selectively and non-covalently with the sterol response element (SRE), a nonpalindromic sequence found in the promoters of genes involved in lipid metabolism.
Interacting selectively and non-covalently with any member of the tumor necrosis factor receptor superfamily.
tumor necrosis factor receptor superfamily binding
Interacting selectively and non-covalently with a proline-rich region within the same polypeptide.
intramolecular proline-rich region binding
intramolecular proline-rich ligand binding
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.
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.
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.
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.
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.
down regulation of organic acid transport
down-regulation of organic acid transport
downregulation of organic acid transport
negative regulation of organic acid transport
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.
positive regulation of organic acid transport
Interacting selectively and non-covalently with a sterol, any steroid containing a hydroxy group in the 3 position, closely related to cholestan-3-ol.
Interacting selectively and non-covalently with and responding, e.g. by conformational change, to changes in the cellular level of a sterol.
Any process that modulates the frequency, rate or extent of mononuclear cell proliferation.
regulation of peripheral blood mononuclear cell proliferation
regulation of mononuclear cell proliferation
Any process that stops, prevents, or reduces the frequency, rate or extent of mononuclear cell proliferation.
negative regulation of PBMC proliferation
negative regulation of peripheral blood mononuclear cell proliferation
negative regulation of mononuclear cell proliferation
Any process that activates or increases the frequency, rate or extent of mononuclear cell proliferation.
up regulation of mononuclear cell proliferation
up-regulation of mononuclear cell proliferation
upregulation of mononuclear cell proliferation
activation of mononuclear cell proliferation
positive regulation of PBMC proliferation
positive regulation of peripheral blood mononuclear cell proliferation
stimulation of mononuclear cell proliferation
positive regulation of mononuclear cell proliferation
Interacting selectively and non-covalently with an acetylcholine receptor.
Interacting selectively and non-covalently with a ubiquitin activating enzyme, any of the E1 proteins.
Interacting selectively and non-covalently with a progesterone receptor.
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.
Interacting selectively and non-covalently with a mitogen-activated protein kinase kinase kinase kinase, any protein that can phosphorylate a MAP kinase kinase kinase.
mitogen-activated protein kinase kinase kinase kinase binding
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.
Catalysis of the reaction: protein serine/threonine phosphate + H2O = protein serine/threonine + phosphate, dependent on the presence of calcium-bound calmodulin.
calcium- and calmodulin-dependent protein phosphatase activity
calcium/calmodulin-dependent protein phosphatase activity
Ca2+/CaM-dependent protein phosphatase activity
calmodulin-dependent protein phosphatase activity
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.
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.
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.
Interacting selectively and non-covalently with the RNA subunit of ribonuclease P.
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.
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.
iron assimilation by chelation and transport
iron assimilation by capture and transport
siderophore-dependent iron import into cell
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.
iron assimilation by reduction and transport
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.
Interacting selectively and non-covalently with urea, a water-soluble carboxamide with the structure H2N-CO-NH2.
Interacting selectively and non-covalently with the D- or L-enantiomer of xylose.
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.
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.
Interacting selectively and non-covalently with a monocarboxylic acid, any organic acid containing one carboxyl (COOH) group or anion (COO-).
Interacting selectively and non-covalently with ectoine, 1,4,5,6-tetrahydro-2-methyl-4-pyrimidinecarboxylic acid.
Interacting selectively and non-covalently with hydroxyectoine.
Interacting selectively and non-covalently with the D- or L-enantiomer of rhamnose.
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.
peroxisomal membrane protein (PMP) targeting signal (mPTS) binding
peroxisome membrane targeting sequence binding
Catalysis of the reaction: a phosphorylated MAP kinase + H2O = a MAP kinase + phosphate.
Catalysis of the reaction: MAP kinase tyrosine phosphate + H2O = MAP kinase tyrosine + phosphate.
tyrosine-specific MAP kinase phosphatase activity
MAP kinase tyrosine phosphatase activity
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.
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).
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.
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.
Facilitates the base-pairing of complementary single-stranded RNA.
Interacting selectively and non-covalently with a receptor that possesses protein serine/threonine kinase activity.
transmembrane receptor protein serine/threonine kinase ligand binding
receptor serine/threonine kinase binding
Interacting selectively and non-covalently with an activating transcription factor, any protein whose activity is required to initiate or upregulate transcription.
Any process that modulates the frequency, rate or extent of osteoblast proliferation.
Any process that stops, prevents or reduces the rate or extent of osteoblast proliferation.
down regulation of osteoblast proliferation
down-regulation of osteoblast proliferation
downregulation of osteoblast proliferation
negative regulation of osteoblast proliferation
Any process that activates or increases the rate or extent of osteoblast proliferation.
up regulation of osteoblast proliferation
up-regulation of osteoblast proliferation
upregulation of osteoblast proliferation
positive regulation of osteoblast proliferation
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.
Catalysis of the reaction: ATP + Fas-activated serine/threonine protein = ADP + Fas-activated serine/threonine phosphoprotein.
ATP:Fas-activated serine/threonine protein phosphotransferase activity
Fas-activated serine/threonine kinase activity
Interacting selectively and non-covalently with a sequence of guanine residues in an RNA molecule.
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.
Facilitates the displacement of one strand of an RNA-RNA duplex and its replacement with a different strand of higher complementarity.
Any process that modulates the frequency, rate, or extent of homotypic cell-cell adhesion.
regulation of homotypic cell-cell adhesion
Any process that stops, prevents, or reduces the frequency, rate, or extent of homotypic cell-cell adhesion.
negative regulation of homotypic cell-cell adhesion
Any process that activates or increases the frequency, rate, or extent of homotypic cell-cell adhesion.
positive regulation of homotypic cell-cell adhesion
Any process that modulates the frequency, rate, or extent of heterotypic cell-cell adhesion.
regulation of heterotypic cell-cell adhesion
Any process that activates or increases the frequency, rate, or extent of heterotypic cell-cell adhesion.
positive regulation of heterotypic cell-cell adhesion
Any process that modulates the frequency, rate, or extent of erythrocyte aggregation.
regulation of red blood cell aggregation
Any process that stops, prevents, or reduces the frequency, rate, or extent of erythrocyte aggregation.
negative regulation of red blood cell aggregation
negative regulation of erythrocyte aggregation
Any process that activates or increases the frequency, rate, or extent of erythrocyte aggregation.
positive regulation of red blood cell aggregation
positive regulation of erythrocyte aggregation
Interacting selectively and non-covalently with an apolipoprotein, the protein component of a lipoprotein complex.
Interacting selectively and non-covalently with apolipoprotein A-I.
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.
very-low-density lipoprotein particle binding
Interacting selectively and non-covalently with an apolipoprotein receptor.
Interacting selectively and non-covalently with an apolipoprotein A-I receptor.
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.
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.
cellular response to amino acid starvation
Catalysis of the reaction: ATP + a protein serine/threonine = ADP + protein serine/threonine phosphate, dependent on the presence of GTP.
A process in which an ion is transported across a membrane.
ATP hydrolysis coupled ion transmembrane transport
Note that this term is not intended for use in annotating lateral movement within membranes.
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.
cellular response to zinc ion limitation
cellular response to zinc ion starvation
Interacting selectively and non-covalently with any glycosylphosphatidylinositol anchor. GPI anchors serve to attach membrane proteins to the lipid bilayer of cell membranes.
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.
Interacting selectively and non-covalently with one or both of the catalytic subunits of protein kinase A.
protein kinase A catalytic subunit binding
Interacting selectively and non-covalently with one or both of the regulatory subunits of protein kinase A.
protein kinase A regulatory subunit binding
Any process that stops or reduces the rate of GTP hydrolysis by a GTPase.
negative regulation of guanosinetriphosphatase activity
down regulation of regulation of Ran GTPase activity
down-regulation of regulation of Ran GTPase activity
downregulation of regulation of Ran GTPase activity
inhibition of regulation of Ran GTPase activity
negative regulation of Rab GTPase activity
negative regulation of Ran GTPase activity
negative regulation of Ras GTPase activity
negative regulation of Rho GTPase activity
An example of this is P2xA in Dictyostelium (UniProt symbol Q86JM7) in PMID:24335649.
The series of events in which a stimulus from a monosaccharide is received and converted into a molecular signal.
The series of events in which a stimulus from a disaccharide is received and converted into a molecular signal.
The series of events in which a maltose stimulus is received by a cell and converted into a molecular signal.
Interacting selectively and non-covalently with an RNA molecule that has assumed an incorrect conformation.
Interacting selectively and non-covalently with a type III interferon. Interferon lambda is the only member of the type III interferon found so far.
Note that IL-28A, IL-28B, and IL-29 are types of interferon-lambda.
Interacting selectively and non-covalently with any part of a dynactin complex; dynactin is a large protein complex that activates dynein-based motor activity.
Interacting selectively and non-covalently with U3 small nucleolar RNA.
Interacting selectively and non-covalently with box C/D small nucleolar RNA.
Interacting selectively and non-covalently with box H/ACA small nucleolar RNA.
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.
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.
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.
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.
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.
cellular response to active oxygen species
cellular response to reactive oxidative species
cellular response to reactive oxygen intermediate
cellular response to reactive oxygen species
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.
Interacting selectively and non-covalently with 2-amino-5-(carbamimidamido)pentanoic acid.
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.
The chemical reactions and pathways involving various organic and inorganic nitrogenous compounds, as carried out by individual cells.
cellular nitrogen compound metabolic process
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.
cellular response to UV radiation stimulus
cellular response to ultraviolet light stimulus
cellular response to ultraviolet radiation stimulus
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.
cellular biopolymer biosynthetic process
cellular macromolecule biosynthetic process
The chemical reactions and pathways resulting in the formation of nucleobases, nucleosides, nucleotides and nucleic acids.
nucleobase, nucleoside, nucleotide and nucleic acid anabolism
nucleobase, nucleoside, nucleotide and nucleic acid biosynthesis
nucleobase, nucleoside, nucleotide and nucleic acid formation
nucleobase, nucleoside, nucleotide and nucleic acid synthesis
nucleobase-containing compound biosynthetic process
Interacting selectively and non-covalently with an inhibin complex, a dimer of one inhibin-alpha subunit and one inhibin-beta subunit.
Interacting selectively and non-covalently with an inhibin monomer, any of the polypeptides that combine to form activin and inhibin dimers.
Interacting selectively and non-covalently with a type I transforming growth factor beta receptor.
transforming growth factor beta receptor type I binding
type I transforming growth factor beta receptor binding
Interacting selectively and non-covalently with a type III transforming growth factor beta receptor.
transforming growth factor beta receptor type III binding
transforming growth factor beta ligand binding to type III receptor
type III transforming growth factor beta receptor binding
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.
high affinity ferrous ion transmembrane transport
high-affinity ferrous ion transmembrane transport
high-affinity iron ion transmembrane transport
low-affinity iron ion transmembrane transport
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.
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.
negative regulation of iron ion transport
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.
positive regulation of iron ion transport
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.
regulation of iron ion membrane transport
regulation of transmembrane Fe transport
regulation of transmembrane iron ion transport
regulation of transmembrane iron transport
regulation of iron ion transmembrane transport
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.
down regulation of transmembrane iron ion transport
down-regulation of transmembrane iron ion transport
downregulation of transmembrane iron ion transport
negative regulation of iron ion membrane transport
negative regulation of transmembrane iron ion transport
negative regulation of transmembrane iron transport
inhibition of transmembrane iron ion transport
negative regulation of iron ion transmembrane transport
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.
positive regulation of iron ion membrane transport
positive regulation of transmembrane iron ion transport
positive regulation of transmembrane iron transport
up regulation of transmembrane iron ion transport
up-regulation of transmembrane iron ion transport
upregulation of transmembrane iron ion transport
activation of transmembrane iron ion transport
stimulation of transmembrane iron ion transport
positive regulation of iron ion transmembrane transport
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.
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.
down regulation of transmembrane transport
down-regulation of transmembrane transport
downregulation of transmembrane transport
negative regulation of membrane transport
negative regulation of transmembrane transport
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.
positive regulation of membrane transport
up regulation of transmembrane transport
up-regulation of transmembrane transport
positive regulation of transmembrane transport
Any process that modulates the frequency, rate or extent of the directed movement of ions from one side of a membrane to the other.
regulation of transmembrane ion transport
regulation of ion transmembrane transport
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.
down regulation of transmembrane ion transport
down-regulation of transmembrane ion transport
downregulation of transmembrane ion transport
negative regulation of ion membrane transport
negative regulation of transmembrane ion transport
inhibition of transmembrane ion transport
negative regulation of ion transmembrane transport
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.
positive regulation of ion membrane transport
positive regulation of transmembrane ion transport
up regulation of transmembrane ion transport
up-regulation of transmembrane ion transport
upregulation of transmembrane ion transport
activation of transmembrane ion transport
stimulation of transmembrane ion transport
positive regulation of ion transmembrane transport
Interacting selectively and non-covalently with one or more specific sites on an immunoglobulin receptor molecule.
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.
Interacting selectively and non-covalently with the enzyme histone acetyltransferase.
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.
Interacting selectively and non-covalently with any inositol-containing glycerophospholipid, i.e. phosphatidylinositol (PtdIns) and its phosphorylated derivatives.
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.
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.
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.
Catalysis of the transfer of a phosphate group to the serine-10 residue of the N-terminal tail of histone H3.
histone kinase activity (H3-S3 specific)
histone serine kinase activity (H3-S10 specific)
histone-serine kinase activity (H3-S10 specific)
histone kinase activity (H3-S10 specific)
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.
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.
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.
Interacting selectively and non-covalently with the catalytic subunit of glutamate-cysteine ligase.
glutamate-cysteine ligase catalytic subunit binding
Interacting selectively and non-covalently with dopamine, a catecholamine neurotransmitter formed by aromatic-L-amino-acid decarboxylase from 3,4-dihydroxy-L-phenylalanine.
Catalysis of the transfer of a galactose group from UDP-galactose to an acceptor molecule.
Catalysis of the transfer of a xylosyl group from UDP-xylose to an acceptor molecule.
Interacting selectively and non-covalently with a glutamate receptor.
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.
Interacting selectively and non-covalently with a G protein-coupled glutamate receptor (a metabotropic glutamate receptor).
G-protein coupled glutamate receptor binding
G protein-coupled glutamate receptor binding
Interacting selectively and non-covalently with a nuclear hormone receptor, a ligand-dependent receptor found in the nucleus of the cell.
Interacting selectively and non-covalently with a steroid hormone receptor.
Interacting selectively and non-covalently with a glucocorticoid receptor.
Interacting selectively and non-covalently with a phthalate, any ester or salt of phthalic acid.
Interacting selectively and non-covalently with diphenyl phthalate, C(20)H(14)O(4).
Interacting selectively and non-covalently with dibutyl phthalate, C(16)H(22)O(4).
Interacting selectively and non-covalently with ethanol, CH(3)-CH(2)-OH.
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.
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.
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.
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.
selenocysteine insertion sequence binding
Interacting selectively and non-covalently with a chondroitin sulfate proteoglycan, any proteoglycan containing chondroitin sulfate as the glycosaminoglycan carbohydrate unit.
chondroitin sulfate proteoglycan binding
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).
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.
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.
Catalysis of the transfer of a phosphate group to the tyrosine-41 residue of histone H3.
histone tyrosine kinase activity (H3-Y41 specific)
histone-tyrosine kinase activity (H3-Y41 specific)
histone kinase activity (H3-Y41 specific)
Catalysis of the transfer of a phosphate group to the threonine-11 residue of the N-terminal tail of histone H3.
histone threonine kinase activity (H3-T11 specific)
histone-threonine kinase activity (H3-T11 specific)
histone kinase activity (H3-T11 specific)
Catalysis of the transfer of a phosphate group to the threonine-6 residue of the N-terminal tail of histone H3.
histone threonine kinase activity (H3-T6 specific)
histone-threonine kinase activity (H3-T6 specific)
histone kinase activity (H3-T6 specific)
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.
regulation of gluconate membrane transport
regulation of gluconate transmembrane transport
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.
negative regulation of gluconate membrane transport
negative regulation of gluconate transport
negative regulation of gluconate transmembrane transport
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.
positive regulation of gluconate membrane transport
positive regulation of gluconate transport
positive regulation of gluconate transmembrane transport
The directed movement of copper cation across a membrane.
Interacting selectively and non-covalently with cyclic-di-GMP, cyclic dimeric guanosine monophosphate.
The directed movement of nickel (Ni) cations across a membrane by means of some agent such as a transporter or pore.
Interacting selectively and non-covalently with any lipase.
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.
Interacting selectively and non-covalently with double-stranded DNA containing an A/A mispair.
Interacting selectively and non-covalently with double-stranded DNA containing an A/G mispair.
Interacting selectively and non-covalently with double-stranded DNA containing a C/C mispair.
Interacting selectively and non-covalently with double-stranded DNA containing a T/T mispair.
Interacting selectively and non-covalently with double-stranded DNA containing a C/T mispair.
Interacting selectively and non-covalently with double-stranded DNA containing a G/G mispair.
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.
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.
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.
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.
Interacting selectively and non-covalently with a ganglioside, a ceramide oligosaccharide carrying in addition to other sugar residues, one or more sialic acid residues.
Catalysis of the addition of a methylthioether group (-SCH3) to a nucleic acid or protein acceptor.
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).
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.
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.
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.
purine ribonucleoside triphosphate binding
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).
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).
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.
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.
Interacting selectively and non-covalently with chemokine (C-C motif) ligand 2.
Interacting selectively and non-covalently with chemokine (C-C motif) ligand 12.
Interacting selectively and non-covalently with chemokine (C-C motif) ligand 7.
Interacting selectively and non-covalently with the cytokine, macrophage migration inhibitory factor.
macrophage migration inhibitory factor binding
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.
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.
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.
Interacting selectively and non-covalently with chemokine (C-C motif) ligand 19.
Interacting selectively and non-covalently with chemokine (C-C motif) ligand 21.
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.
renal sodium ion absorption involved in negative regulation of renal sodium excretion
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.
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.
cellular response to copper ion starvation
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).
For binding to the death domain, consider instead the term 'death domain binding ; GO:0070513'.
Interacting selectively and non-covalently with flurbiprofen.
2-(2-fluoro-[1,1'-biphenyl-4-yl])propanoic acid binding
Interacting selectively and non-covalently with a region containing frequent adenine and uridine bases within the 3' untranslated region of a mRNA molecule.
mRNA 3'-UTR adenylate/uridylate-rich element binding
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.
Catalysis of the transfer of a phosphate group to the serine-139 residue of the C-terminal tail of histone H2A.
histone kinase activity (H2A.x-S139 specific)
Residue 1 of histone H2A is taken as the first residue following removal of the initiating Methionine (Met).
histone kinase activity (H2A-S139 specific)
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.
protein-coding primary transcript binding
Interacting selectively and non-covalently with the GAF domain of a protein.
The negative regulation of cell adhesion process in which a neural crest cell physically separates from the rest of the neural tube.
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.
The negative regulation of cell adhesion process in which a cardiac neural crest cell physically separates from the rest of the neural tube.
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.
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.
Interacting selectively and non-covalently with a small molecule, any low molecular weight, monomeric, non-encoded molecule.
Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.
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.
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.
peroxisome membrane class-1 targeting sequence binding
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.
peroxisome membrane class-2 targeting sequence binding
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.
cellular response to inositol starvation
Interacting selectively and non-covalently with a member of the bone morphogenetic protein (BMP) family.
Interacting selectively and non-covalently with 3-sulfino-L-alanine (cysteine sulfinate).
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.
Interacting selectively and non-covalently with the inorganic anion thiosulfate, a sulfur oxide that has formula O3S2.
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.
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).
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.
cellular response to adenine deprivation
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).
cellular response to vitamin B1 deprivation
cellular response to vitamin B1 starvation
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.
The directed movement of cadmium ions into the vacuole.
The phosphorylation by a protein of one or more of its own serine amino acid residues, or a serine residue on an identical protein.
The phosphorylation by a protein of a residue on an identical protein. For example, phosphorylation by the other kinase within a homodimer.
The phosphorylation by a protein of one or more of its own amino acid residues.
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.
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'.
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.
cellular response to lowered oxygen levels
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'.
cellular response to decreased oxygen levels
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.
cellular response to raised oxygen levels
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'.
cellular response to increased oxygen levels
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.
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.
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.
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.
recombination-dependent interstrand cross-link repair
recombinational interstrand cross-link repair
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.
recombination-independent interstrand cross-link repair
non-recombinational interstrand cross-link repair
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.
phosphatidylinositol 3-kinase regulatory subunit binding
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.
phosphatidylinositol 3-kinase catalytic subunit binding
The ability of a photoreceptor to adjust to varying levels of light.
Light adaptation is usually a combination of cell desensitization and response acceleration.
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.
The directed movement of sodium ions from inside of a cell, across the plasma membrane and into the extracellular region.
sodium ion export across plasma membrane
Interacting selectively and non-covalently with a protein upon poly-ubiquitination formed by linkages between lysine residues at position 48 in the target protein.
K48-linked polyubiquitin modification-dependent protein binding
A process in which a calcium ion (Ca2+) is transported from the cytosol, into the mitochondrial matrix.
calcium ion transmembrane import into mitochondrion
Interacting selectively and non-covalently with a hepatocyte growth factor.
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.
cellular response to cell envelope stress
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.
A series of molecular signals initiated by the absence of a ligand or the withdrawal of a ligand from a receptor.
signal transduction in absence of agonist
signal transduction in absence of ligand
Interacting selectively and non-covalently with tumor necrosis factor ligand superfamily member 11 (TNFSF11), a member of the tumor necrosis factor (TNF) cytokine family.
TNF-related activation-induced cytokine binding
osteoclast differentiation factor binding
receptor activator of nuclear factor kappa-B ligand binding
tumor necrosis factor (ligand) superfamily member 11 binding
tumor necrosis factor ligand superfamily member 11 binding
tumor necrosis factor superfamily member 11 binding
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.
MAPK activity involved in innate immune response
MAP kinase activity involved in innate immune response
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.
MAPK phosphatase activity involved in regulation of innate immune response
MAP kinase phosphatase activity involved in regulation of innate immune response
The phosphorylation by a protein of one or more of its own tyrosine amino acid residues, or a tyrosine residue on an identical protein.
receptor tyrosine kinase autophosphorylation
Interacting selectively and non-covalently with a vascular endothelial growth factor.
vascular endothelial growth factor binding
Interacting selectively and non-covalently with a nodal protein, a member of the transforming growth factor-beta superfamily.
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.
This term refers to inhibition of a member of the activin receptor family; activin receptors bind to multiple ligands including activin and nodal.
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.
activin receptor antagonist activity involved in negative regulation of nodal signalling pathway
activin receptor antagonist activity involved in negative regulation of nodal signaling pathway
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.
Interacting selectively and non-covalently with a neuregulin, a member of the EGF family of growth factors.
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.
Interacting selectively and non-covalently with a member of the neuropilin family.
Interacting selectively and non-covalently with RIG-I, a cytosolic pattern recognition receptor that initiates an antiviral signaling pathway upon binding to viral RNA.
Interacting selectively and non-covalently with MDA-5, a cytosolic pattern recognition receptor that initiates an antiviral signaling pathway upon binding to viral dsRNA.
Interacting selectively and non-covalently with a coreceptor. A coreceptor acts in cooperation with a primary receptor to transmit a signal within the cell.
The increase in size or mass of an entire organism, a part of an organism or a cell.
See also the biological process term 'cell growth ; GO:0016049'.
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.
Any process that modulates the rate of growth of all or part of an organism.
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.
Any process that increases the rate of growth of all or part of an organism.
Any process that modulates the frequency, rate or extent of locomotion of a cell or organism.
Any process that stops, prevents, or reduces the frequency, rate or extent of locomotion of a cell or organism.
Any process that activates or increases the frequency, rate or extent of locomotion of a cell or organism.
Interacting selectively and non-covalently with interleukin-18.
Interacting selectively and non-covalently with interleukin-15.
Interacting selectively and non-covalently with interleukin-16.
Interacting selectively and non-covalently with interleukin-19.
Interacting selectively and non-covalently with interleukin-20.
Interacting selectively and non-covalently with interleukin-22.
Interacting selectively and non-covalently with interleukin-23.
Interacting selectively and non-covalently with the granulocyte macrophage colony-stimulating factor complex.
granulocyte macrophage colony stimulating factor complex binding
granulocyte macrophage colony-stimulating factor complex binding
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.
Providing the environmental signal that initiates the directed movement of a motile cell or organism towards a higher concentration of that signal.
Any process that modulates the frequency, rate or extent of cell proliferation.
regulation of cell population proliferation
Interacting selectively and non-covalently with an unprocessed ribosomal RNA transcript.
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.
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.
Interacting selectively and non-covalently with the beta subunit of interleukin-12.
Interacting selectively and non-covalently with the alpha subunit of interleukin-12.
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.
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.
Any process in which DNA is protected from damage by, for example, oxidative stress.
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.
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.
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.
Interacting selectively and non-covalently with peptides, any of a group of organic compounds comprising two or more amino acids linked by peptide bonds.
Catalysis of the transfer of a xylosyl group to an acceptor molecule, typically another carbohydrate or a lipid.
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.
major histocompatibility complex binding
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.
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.
major histocompatibility complex class I binding
major histocompatibility complex class I ligand
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.
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.
major histocompatibility complex class II binding
major histocompatibility complex class II ligand
Interacting selectively and non-covalently with phosphate.
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.
Interacting selectively and non-covalently with the hypocretin receptor.
The directed movement of a motile cell or organism in response to an external stimulus.
directed movement in response to stimulus
Interacting selectively and non-covalently with any chemokine receptor.
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.
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).
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.
detection of triacylated bacterial lipoprotein
perception of triacylated bacterial lipopeptide
perception of triacylated bacterial lipoprotein
Note that bacterial lipopeptides are derived from bacterial lipoproteins, but the two terms are sometimes used interchangeably in the literature.
detection of triacyl bacterial lipopeptide
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.
detection of diacylated bacterial lipoprotein
perception of diacylated bacterial lipopeptide
perception of diacylated bacterial lipoprotein
detection of diacyl bacterial lipopeptide
Interacting selectively and non-covalently with a lipopeptide containing a nonprotein moiety consisting of three acyl groups.
Interacting selectively and non-covalently with a lipopeptide containing a nonprotein moiety consisting of two acyl groups.
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.
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.
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.
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.
Any biological process involved in the maintenance of an internal steady state.
negative regulation of homeostatic process
positive regulation of homeostatic process
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.
Any process that results in a change in the behavior of an organism as a result of deprivation of nourishment.
Interacting selectively and non-covalently with a T cell receptor, the antigen-recognizing receptor on the surface of T cells.
Interacting selectively and non-covalently with a CD4, a receptor found on the surface of T cells, monocytes and macrophages.
Interacting selectively and non-covalently with a CD8, a receptor found on the surface of thymocytes and cytotoxic and suppressor T-lymphocytes.
Interacting selectively and non-covalently with a CD70, a receptor found on the surface of most activated B cells and some activated T cells.
Interacting selectively and non-covalently with CD154, a receptor found on the surface of some activated lymphocytes.
Catalysis of the phosphorylation and activation of JUN kinase kinase kinases (JNKKKs).
JUN kinase kinase kinase kinase activity
Interacting selectively and non-covalently with the lateral surface of major histocompatibility complex class II molecules.
major histocompatibility complex class II protein binding, via lateral surface
MHC class II protein binding, via lateral surface
Interacting selectively and non-covalently with the antigen binding groove of major histocompatibility complex class II molecules.
major histocompatibility complex class II protein binding, via antigen binding groove
MHC class II protein binding, via antigen binding groove
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.
The series of events required to receive a stimulus indicating DNA damage has occurred and convert it to a molecular signal.
detection of DNA damage during DNA damage response
DNA damage response, perception of DNA damage
DNA damage response, detection of DNA damage
The transport of protons across a mitochondrial membrane to generate an electrochemical gradient (proton-motive force) that powers ATP synthesis.
mitochondrial ATP synthesis coupled proton transport
The transport of protons across the plasma membrane to generate an electrochemical gradient (proton-motive force) that powers ATP synthesis.
plasma membrane ATP synthesis coupled proton transport
Interacting selectively and non-covalently with an identical protein or proteins.
Interacting selectively and non-covalently with an identical protein to form a homodimer.
Interacting selectively and non-covalently with actinin, any member of a family of proteins that crosslink F-actin.
Interacting selectively and non-covalently with fucose, the pentose 6-deoxygalactose.
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.
Interacting selectively and non-covalently with the enzyme histone deacetylase.
Interacting selectively and non-covalently, in a non-covalent manner, with peptidoglycan, any of a class of glycoconjugates found in bacterial cell walls.
Interacting selectively and non-covalently with the RNA element BRE (Bruno response element).
Interacting selectively and non-covalently with one or more specific sites on a neuromedin U receptor.
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).
Interacting selectively and non-covalently and stoichiometrically with neuromedin U, a hypothalamic peptide involved in energy homeostasis and stress responses.
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.
Interacting selectively and non-covalently with the retinoic acid receptor, a ligand-regulated transcription factor belonging to the nuclear receptor superfamily.
Interacting selectively and non-covalently with any of the peroxisome proliferator activated receptors, alpha, beta or gamma.
peroxisome proliferator activated receptor binding
Interacting selectively and non-covalently with X11-like protein, a neuron-specific adaptor protein.
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.
Interacting selectively and non-covalently with the microtubule constituent protein alpha-tubulin.
Interacting selectively and non-covalently with the microtubule constituent protein gamma-tubulin.
Interacting selectively and non-covalently with any complex of RNA and protein.
Interacting selectively and non-covalently with any part of a ribosome.
Interacting selectively and non-covalently with any part of the larger ribosomal subunit.
Interacting selectively and non-covalently with any part of the small ribosomal subunit.
Interacting selectively and non-covalently with single-stranded telomere-associated DNA.
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.
rDNA spacer replication fork barrier binding
Interacting selectively and non-covalently with tumor necrosis factor, a proinflammatory cytokine produced by monocytes and macrophages.
Interacting selectively and non-covalently with a neurotrophin, any of a family of growth factors that prevent apoptosis in neurons and promote nerve growth.
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].
Interacting selectively and non-covalently with the protein-tyrosine kinase receptor ErbB-3/HER3.
Interacting selectively and non-covalently with ubiquitin, a protein that when covalently bound to other cellular proteins marks them for proteolytic degradation.
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.
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.
proteasomal ubiquitin-dependent protein breakdown
proteasomal ubiquitin-dependent protein catabolic process
proteasomal ubiquitin-dependent protein catabolism
proteasomal ubiquitin-dependent protein degradation
proteasome-mediated ubiquitin-dependent protein catabolic process
Interacting selectively and non-covalently with ions, charged atoms or groups of atoms.
Interacting selectively and non-covalently with anions, charged atoms or groups of atoms with a net negative charge.
Interacting selectively and non-covalently with cations, charged atoms or groups of atoms with a net positive charge.
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.
multicellular organismal macromolecule metabolic process
Interacting selectively and non-covalently with an RNA polymerase core enzyme, containing a specific subunit composition defined as the core enzyme.
Interacting selectively and non-covalently with an organic acid, any acidic compound containing carbon in covalent linkage.
Interacting selectively and non-covalently with an alcohol, any of a class of alkyl compounds containing a hydroxyl group.
Interacting selectively and non-covalently with vascular endothelial growth factor receptor 1.
vascular endothelial growth factor receptor 1 binding
Interacting selectively and non-covalently with vascular endothelial growth factor receptor 2.
vascular endothelial growth factor receptor 2 binding
Interacting selectively and non-covalently with vascular endothelial growth factor receptor 3.
fms-like-tyrosine kinase (Flt)-4 binding
vascular endothelial growth factor receptor 3 binding
Interacting selectively and non-covalently with sulfate, SO4(2-), a negatively charged small molecule.
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.
Interacting selectively and non-covalently with glycosphingolipid, a compound with residues of sphingoid and at least one monosaccharide.
Interacting selectively and non-covalently with alkanesulfonates, the anion of alkanesulfonic acids, sulfonic acid derivatives containing an aliphatic hydrocarbon group.
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.
structural maintenance of chromosomes family protein binding
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.
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.
down regulation of potassium ion transport
down-regulation of potassium ion transport
downregulation of potassium ion transport
negative regulation of potassium transport
negative regulation of potassium ion conductance
transmembrane conductance regulator activity
negative regulation of potassium ion transport
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.
positive regulation of potassium transport
up regulation of potassium ion transport
up-regulation of potassium ion transport
positive regulation of potassium conductance
positive regulation of potassium ion conductance
positive regulation of potassium ion transport
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.
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.
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.
Interacting selectively and non-covalently with any phospholipase, enzymes that catalyze of the hydrolysis of a glycerophospholipid.
Interacting selectively and non-covalently with glutathione; a tripeptide composed of the three amino acids cysteine, glutamic acid and glycine.
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.
phosphatidylinositol-3,4-bisphosphate binding
Interacting selectively and non-covalently with a proteoglycan, any glycoprotein in which the carbohydrate units are glycosaminoglycans.
Interacting selectively and non-covalently with a heparan sulfate proteoglycan, any proteoglycan containing heparan sulfate as the glycosaminoglycan carbohydrate unit.
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.
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.
Interacting selectively and non-covalently with protein kinase B, an intracellular kinase that is important in regulating glucose metabolism.
Interacting selectively and non-covalently with a 3-phosphoinositide-dependent protein kinase.
phosphatidylinositol-3-phosphate-dependent protein kinase binding
3-phosphoinositide-dependent protein kinase binding
Interacting selectively and non-covalently with protein histidine kinase.
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.
Interacting selectively and non-covalently with Myogenic Regulatory Factor (MRF), a member of the basic Helix-Loop-Helix (bHLH) superfamily of transcription factors.
Interacting selectively and non-covalently with an immunoglobulin of a D isotype.
The process of restoring mitochondrial DNA after damage.
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.
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.
Interacting selectively and non-covalently with ADP, adenosine 5'-diphosphate.
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.
Interacting selectively and non-covalently with inositol 1,3,4,5 tetrakisphosphate.
inositol 1,3,4,5 tetrakisphosphate binding
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.
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.
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.
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.
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.
insulin receptor substrate [protein] binding
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.
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.
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.
Any process that modulates the frequency, rate, or extent of carbon utilization.
Any process that modulates the frequency, rate or extent of carbohydrate utilization.
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.
Interacting selectively and non-covalently with a domain within the same polypeptide.
The series of events in which a pheromone stimulus is received by a cell and converted into a molecular signal.
Interacting selectively and non-covalently with suramin, a naphthalenesulfonic acid compound which is used in the treatment of diseases caused by trypanosomes and worms.
Catalysis of the transfer of a phosphate group to the serine-28 residue of the N-terminal tail of histone H3.
histone serine kinase activity (H3-S28 specific)
histone-serine kinase activity (H3-S28 specific)
histone kinase activity (H3-S28 specific)
Catalysis of the transfer of a phosphate group to the serine-1 residue of the N-terminal tail of histone H4.
histone serine kinase activity (H4-S1 specific)
histone-serine kinase activity (H4-S1 specific)
histone kinase activity (H4-S1 specific)
Catalysis of the transfer of a phosphate group to the serine-1 residue of the N-terminal tail of histone H2A.
histone serine kinase activity (H2A-S1 specific)
histone-serine kinase activity (H2A-S1 specific)
histone kinase activity (H2A-S1 specific)
Catalysis of the transfer of a phosphate group to the serine-14 or an equivalent residue of the N-terminal tail of histone H2B.
histone serine kinase activity (H2B-S14 specific)
histone-serine kinase activity (H2B-S14 specific)
histone kinase activity (H2B-S14 specific)
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.
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.
regulation of cellular component biogenesis
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.
positive regulation of cellular component biogenesis
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.
negative regulation of molecular function
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.
positive regulation of molecular function
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.
Interacting selectively and non-covalently with a TRAF-type zinc finger domain of a protein.
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.
transcription regulatory region DNA binding
Interacting selectively and non-covalently with an intronic DNA region that regulates the transcription of the transcript it is contained within.
intronic transcription regulatory region DNA binding
The chemical reactions and pathways by which individual cells transform chemical substances.
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.
The chemical reactions and pathways resulting in the breakdown of substances, carried out by individual cells.
The chemical reactions and pathways resulting in the formation of substances, carried out by individual cells.
The slowing of metabolic processes to very low levels in order to conserve energy as a part of hibernation.
inhibition of metabolic activity during hibernation
down regulation of metabolic activity during hibernation
down-regulation of metabolic activity during hibernation
downregulation of metabolic activity during hibernation
negative regulation of metabolic activity during hibernation
negative regulation of metabolic activity involved in hibernation
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.
cellular macromolecule metabolic process
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.
main pathways of carbohydrate metabolic process
main pathways of carbohydrate metabolism
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.
cellular macromolecule catabolic process
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.
The chemical reactions and pathways resulting in the formation of organic and inorganic nitrogenous compounds.
cellular nitrogen compound biosynthetic process
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.
retinoic acid-responsive element binding
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.
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.
Interacting selectively and non-covalently with a cytokinin, any of a class of adenine-derived compounds that can function in plants as growth regulators.
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.
DNA bending involving sequence-specific DNA binding
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.
RNA polymerase II core promoter proximal region sequence-specific DNA binding, bending
RNA polymerase II promoter proximal region sequence-specific DNA binding, bending
RNA polymerase II proximal promoter region sequence-specific DNA binding, bending
RNA polymerase II proximal promoter sequence-specific DNA binding, bending
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.
DNA bending involving non-sequence-specific DNA binding
non-sequence-specific DNA binding, bending
Interacting selectively and non-covalently with a small protein activating enzyme, such as ubiquitin-activating enzyme.
Interacting selectively and non-covalently with a ubiquitin-like protein ligase, such as ubiquitin-ligase.
small conjugating protein ligase binding
Interacting selectively and non-covalently with a ubiquitin-like protein conjugating enzyme such as ubiquitin conjugating enzyme.
small protein conjugating enzyme binding
ubiquitin-like protein conjugating enzyme binding
Interacting selectively and non-covalently with a DNA topoisomerase.
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.
Interacting selectively and non-covalently with a GTP cyclohydrolase.
Interacting selectively and non-covalently with cellotriose.
Interacting selectively and non-covalently with cellodextrin, a glucose polymer of 2 or more glucose monomers.
Interacting selectively and non-covalently with cellobiose, a disaccharide that represents the basic repeating unit of cellulose.
Interacting selectively and non-covalently with cellotetraose, an oligosaccharide consisting of four glucose residues resulting from hydrolysis of cellulose.
Interacting selectively and non-covalently with cellopentaose, an oligosaccharide consisting of four glucose residues resulting from hydrolysis of cellulose.
Interacting selectively and non-covalently with laminaribiose, a disaccharide.
Interacting selectively and non-covalently with pectin.
Interacting selectively and non-covalently with iron molybdenum cofactor, the cofactor located at the active site of the molybdenum nitrogenase.
Interacting selectively and non-covalently with the attachment site of the phosphopantetheine prosthetic group of an acyl carrier protein (ACP).
ACP phosphopantetheine attachment site binding
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.
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.
double-stranded hemi-methylated DNA binding
Interacting selectively and non-covalently with a macromolecular complex.
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.
double-strand break repair via single-strand annealing
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.
double-strand break repair via synthesis-dependent strand annealing
Correction of replication errors by DNA polymerase using a 3'-5' exonuclease activity.
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.
maintenance of fidelity involved in DNA-dependent DNA replication
maintenance of fidelity during DNA-dependent DNA replication
DNA-dependent DNA replication maintenance of fidelity
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.
The process in which a magnesium ion (Mg2+) is transported across a mitochondrial membrane, into or out of the mitochondrion.
mitochondrial magnesium ion transmembrane transport
Interacting selectively and non-covalently with the ends of DNA that are exposed by the creation of double-strand breaks (DSBs).
Interacting selectively and non-covalently with a pre-mRNA branch point sequence, located upstream of the 3' splice site.
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.
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.
Interacting selectively and non-covalently with a class II myosin, any member of the class of 'conventional' double-headed myosins that includes muscle myosin.
Interacting selectively and non-covalently with a chemokine receptor in the CXCR family.
Interacting selectively and non-covalently with the CXCR1 chemokine receptor.
Interacting selectively and non-covalently with the CXCR2 chemokine receptor.
Interacting selectively and non-covalently with the alpha subunit of the catenin complex.
Interacting selectively and non-covalently with the gamma subunit of the catenin complex.
Interacting selectively and non-covalently with cadherin, a type I membrane protein involved in cell adhesion.
Interacting selectively and non-covalently with a phosphorylated amino acid residue within a protein.
protein phosphorylated amino acid binding
Interacting selectively and non-covalently with unmethylated CpG motifs. Unmethylated CpG dinucleotides are often associated with gene promoters.
Interacting selectively and non-covalently with mercury (Hg) ions.
Blocks the binding of interleukin-1 to interleukin-1 type I receptors.
interleukin-1 type I receptor antagonist activity
Blocks the binding of interleukin-1 to interleukin-1 type II receptors.
interleukin-1 type II receptor antagonist activity
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.
Providing the environmental signal that initiates the directed movement of a motile cell or organism towards a lower concentration of that signal.
Interacting selectively and non-covalently with a light chain of the dynein complex.
Interacting selectively and non-covalently with a heavy chain of the dynein complex.
Interacting selectively and non-covalently with an intermediate chain of the dynein complex.
Interacting selectively and non-covalently with interleukin-24.
Interacting selectively and non-covalently with interleukin-25.
Interacting selectively and non-covalently with interleukin-26.
Interacting selectively and non-covalently with interleukin-27.
Interacting selectively and non-covalently with the interleukin-16 receptor.
Interacting selectively and non-covalently with the interleukin-18 receptor.
Interacting selectively and non-covalently with the interleukin-19 receptor.
Interacting selectively and non-covalently with the interleukin-20 receptor.
Interacting selectively and non-covalently with the interleukin-22 receptor.
Interacting selectively and non-covalently with the interleukin-23 receptor.
Interacting selectively and non-covalently with the interleukin-24 receptor.
Interacting selectively and non-covalently with the interleukin-25 receptor.
Interacting selectively and non-covalently with the interleukin-26 receptor.
Interacting selectively and non-covalently with the interleukin-27 receptor.
Interacting selectively and non-covalently with syndecan, an integral membrane proteoglycan (250-300 kDa) associated largely with epithelial cells.
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.
Any process that activates or increases the frequency, rate or extent of cell adhesion.
Any process that stops, prevents, or reduces the frequency, rate or extent of light-activated channel activity.
down regulation of light-activated channel activity
down-regulation of light-activated channel activity
downregulation of light-activated channel activity
inhibition of light-activated channel activity
negative regulation of light-activated channel activity
Any process that activates or increases the frequency, rate or extent of light-activated channel activity.
up regulation of light-activated channel activity
up-regulation of light-activated channel activity
upregulation of light-activated channel activity
activation of light-activated channel activity
stimulation of light-activated channel activity
positive regulation of light-activated channel activity
Any process that stops, prevents, or reduces the frequency, rate or extent of nitrogen utilization.
negative regulation of nitrogen utilization
Any process that activates or increases the frequency, rate or extent of nitrogen utilization.
positive regulation of nitrogen utilization
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.
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.
Any process that stops, prevents, or reduces the frequency, rate or extent of phosphorus utilization.
down regulation of phosphorus utilization
down-regulation of phosphorus utilization
downregulation of phosphorus utilization
negative regulation of phosphorus utilization
Any process that activates or increases the frequency, rate or extent of phosphorus utilization.
positive regulation of phosphorus utilization
Any process that reduces the rate of growth of all or part of an organism.
Any process that modulates the frequency, rate or extent of the import of the hexose monosaccharide glucose into a cell or organelle.
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.
Any process that activates or increases the frequency, rate or extent of the import of the hexose monosaccharide glucose into a cell or organelle.
Interacting selectively and non-covalently with a SMAD signaling protein.
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).
Catalysis of the transfer of a glucosyl group to an acceptor molecule, typically another carbohydrate or a lipid.
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.
perception of umami taste, detection of chemical stimulus
perception of umami taste, sensory transduction of chemical stimulus
sensory detection of chemical stimulus during perception of umami taste
sensory transduction of chemical stimulus during perception of umami taste
detection of chemical stimulus involved in sensory perception of umami taste
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.
regulation of calcium-dependent cell-cell adhesion
Any process that activates or increases the frequency, rate or extent of calcium-dependent cell-cell adhesion.
up regulation of calcium-dependent cell-cell adhesion
up-regulation of calcium-dependent cell-cell adhesion
upregulation of calcium-dependent cell-cell adhesion
activation of calcium-dependent cell-cell adhesion
stimulation of calcium-dependent cell-cell adhesion
positive regulation of calcium-dependent cell-cell adhesion
Any process that stops, prevents, or reduces the frequency, rate or extent of calcium-dependent cell-cell adhesion.
down regulation of calcium-dependent cell-cell adhesion
down-regulation of calcium-dependent cell-cell adhesion
downregulation of calcium-dependent cell-cell adhesion
inhibition of calcium-dependent cell-cell adhesion
negative regulation of calcium-dependent cell-cell adhesion
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).
The action characteristic of a hormone that takes part in the digestion process.
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.
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.
Interacting selectively and non-covalently with a lectin-like natural killer cell receptor.
natural killer cell lectin-like receptor binding
Interacting selectively and non-covalently with borate, the anion (BO3)3-.
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).
The process of restoring viral DNA after damage or errors in replication.
Interacts with chemokine receptors to reduce the action of a chemokine.
Any process that modulates the frequency, rate or extent of the directed movement of substances between the nucleus and the cytoplasm.
regulation of nucleocytoplasmic transport
Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of substances between the cytoplasm and the nucleus.
down regulation of nucleocytoplasmic transport
down-regulation of nucleocytoplasmic transport
downregulation of nucleocytoplasmic transport
inhibition of nucleocytoplasmic transport
negative regulation of nucleocytoplasmic transport
Any process that activates or increases the frequency, rate or extent of the directed movement of substances between the nucleus and the cytoplasm.
up regulation of nucleocytoplasmic transport
up-regulation of nucleocytoplasmic transport
upregulation of nucleocytoplasmic transport
activation of nucleocytoplasmic transport
stimulation of nucleocytoplasmic transport
positive regulation of nucleocytoplasmic transport
Interacting selectively and non-covalently with cadmium (Cd) ions.
Interacting selectively and non-covalently with N-acetylgalactosamine, 2-acetamido-2-deoxygalactopyranose, the n-acetyl derivative of galactosamine.
Interacting selectively and non-covalently with any metal ion.
Interacting selectively and non-covalently with an ephrin receptor.
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).
The controlled release of a substance by a cell or a tissue.
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.
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.
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.
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.
alpha-(1->3)-fucosyltransferase activity
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.
alpha-(1->6)-fucosyltransferase activity
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.
endoplasmic reticulum retention sequence binding
Interacting selectively and non-covalently with a retinoid X receptor.
Interacting selectively and non-covalently with a thyroid hormone receptor.
ligand-dependent thyroid hormone receptor interactor activity
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.
Interacting selectively and non-covalently with the TAP1 subunit of TAP (transporter associated with antigen processing) protein.
Interacting selectively and non-covalently with the TAP2 subunit of TAP (transporter associated with antigen processing) protein.
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.
Interacting selectively and non-covalently with a nonidentical protein to form a heterodimer.
The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits.
Catalysis of the reaction: [3-hydroxy-3-methylglutaryl-CoA reductase (NADPH)] + ATP = [3-hydroxy-3-methylglutaryl-CoA reductase (NADPH)] phosphate + ADP.
3-hydroxy-3-methylglutaryl coenzyme A reductase kinase activity
3-hydroxy-3-methylglutaryl-CoA reductase kinase activity
ATP:hydroxymethylglutaryl-CoA reductase (NADPH) phosphotransferase activity
beta-hydroxy-beta-methylglutaryl-CoA reductase kinase activity
hydroxymethylglutaryl coenzyme A reductase kinase (phosphorylating) activity
hydroxymethylglutaryl coenzyme A reductase kinase activity
hydroxymethylglutaryl-CoA reductase (NADPH) kinase activity
hydroxymethylglutaryl-CoA reductase (NADPH2) kinase activity
hydroxymethylglutaryl-CoA reductase kinase activity
[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase activity
Catalysis of the reaction: ATP + 3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) = ADP + 3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) phosphate.
3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase activity
ATP:3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) phosphotransferase activity
[3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] kinase activity
branched-chain 2-oxo acid dehydrogenase kinase activity
branched-chain alpha-ketoacid dehydrogenase kinase activity
branched-chain keto acid dehydrogenase kinase activity
branched-chain oxo acid dehydrogenase kinase (phosphorylating) activity
[3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase activity
Catalysis of the reaction: H2O + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate = phosphate + [hydroxymethylglutaryl-CoA reductase (NADPH)].
hydroxymethylglutaryl-CoA reductase (NADPH)-phosphatase activity
hydroxymethylglutaryl-CoA reductase (NADPH)-phosphate phosphohydrolase activity
[hydroxymethylglutaryl-CoA reductase (NADPH)]-phosphatase activity
Catalysis of the reaction: H2O + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate = phosphate + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)].
3-methyl-2-oxobutanoate dehydrogenase (lipoamide)-phosphatase activity
3-methyl-2-oxobutanoate dehydrogenase (lipoamide)-phosphate phosphohydrolase activity
branched-chain 2-keto acid dehydrogenase phosphatase activity
branched-chain oxo-acid dehydrogenase phosphatase activity
[3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]-phosphatase activity
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.
Catalysis of the reaction: ATP + beta-adrenergic receptor = ADP + phospho-beta-adrenergic receptor.
ATP:beta-adrenergic-receptor phosphotransferase activity
beta-adrenergic receptor-specific kinase activity
beta-adrenergic-receptor kinase (phosphorylating) activity
beta-adrenergic-receptor kinase activity
beta-adrenergic receptor kinase activity
Catalysis of the reaction: ATP + dephospho-[[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase] = ADP + [[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase].
AMP-activated protein kinase kinase activity
ATP:dephospho-{hydroxymethylglutaryl-CoA reductase (NADPH)kinase} phosphotransferase activity
dephospho-reductase kinase kinase activity
hydroxymethylglutaryl coenzyme A reductase kinase kinase (phosphorylating) activity
hydroxymethylglutaryl coenzyme A reductase kinase kinase activity
dephospho-[reductase kinase] kinase activity
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).
Definition discussed in https://github.com/geneontology/go-ontology/issues/14220
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.
Interacting selectively and non-covalently with a CCR chemokine receptor.
Interacting selectively and non-covalently with the 5' untranslated region of an mRNA molecule.
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.
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.
Interacting selectively and non-covalently with any disaccharide. Disaccharides are sugars composed of two monosaccharide units.
Interacting selectively and non-covalently with any trisaccharide. Trisaccharides are sugars composed of three monosaccharide units.
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.
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.
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.
Interacting selectively and non-covalently with ubiquinone, a quinone derivative with a tail of isoprene units.
Any process that modulates the frequency, rate or extent of multiplication or reproduction of fibroblast cells.
Any process that activates or increases the frequency, rate or extent of multiplication or reproduction of fibroblast cells.
up regulation of fibroblast proliferation
up-regulation of fibroblast proliferation
upregulation of fibroblast proliferation
positive regulation of fibroblast proliferation
Any process that stops, prevents, or reduces the frequency, rate or extent of multiplication or reproduction of fibroblast cells.
down regulation of fibroblast proliferation
down-regulation of fibroblast proliferation
downregulation of fibroblast proliferation
negative regulation of fibroblast proliferation
Interacting selectively and non-covalently with tau protein. tau is a microtubule-associated protein, implicated in Alzheimer's disease, Down Syndrome and ALS.
Interacting selectively and non-covalently with activin, a dimer of inhibin-beta subunits.
Interacting selectively and non-covalently with a the CXCR3 chemokine receptor.
The process in which iron is transported from the cytosol, into the mitochondrial matrix.
mitochondrial iron cation transmembrane transport
mitochondrial iron ion transmembrane transport
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.
mitogen-activated protein kinase p38 binding
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.
Interacting selectively and non-covalently with Rac protein, any member of the Rac subfamily of the Ras superfamily of monomeric GTPases.
Interacting selectively and non-covalently with brain-derived neurotrophic factor.
brain-derived neurotrophic factor binding
Interacting selectively and non-covalently with nerve growth factor (NGF).
Interacting selectively and non-covalently with platelet-derived growth factor.
Interacting selectively and non-covalently with epidermal growth factor.
Interacting selectively and non-covalently with the microtubule constituent protein beta-tubulin.
Interacting selectively and non-covalently with the Roundabout (ROBO) receptor, a transmembrane receptor.
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.
positive regulation of physiological process
positive regulation of biological process
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.
negative regulation of physiological process
negative regulation of biological process
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.
positive regulation of cellular physiological process
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.
negative regulation of cellular physiological process
Catalysis of the transfer of a galactose residue from a donor molecule to an oligosaccharide, forming a beta-1,3-linkage.
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.
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.
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.
photoperiodic control of inflorescence development
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.
long-day photoperiodic control of flowering
long-day photoperiodic control of flowering time
long-day photoperiodic control of inflorescence development
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.
short-day photoperiodic control of flowering
short-day photoperiodic control of flowering time
short-day photoperiodic control of inflorescence development
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.
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.
positive regulation of response to stimulus
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.
negative regulation of response to stimulus
Any process that modulates the frequency, rate or extent of smooth muscle cell proliferation.
regulation of smooth muscle cell proliferation
Any process that activates or increases the rate or extent of smooth muscle cell proliferation.
positive regulation of SMC proliferation
up regulation of smooth muscle cell proliferation
up-regulation of smooth muscle cell proliferation
upregulation of smooth muscle cell proliferation
activation of smooth muscle cell proliferation
stimulation of smooth muscle cell proliferation
positive regulation of smooth muscle cell proliferation
Any process that stops, prevents or reduces the rate or extent of smooth muscle cell proliferation.
down regulation of smooth muscle cell proliferation
down-regulation of smooth muscle cell proliferation
downregulation of smooth muscle cell proliferation
negative regulation of SMC proliferation
inhibition of smooth muscle cell proliferation
negative regulation of smooth muscle cell proliferation
Any biological process involved in the maintenance of an internal steady state of a chemical.
Catalysis of the reaction: myosin light-chain phosphate + H2O = myosin light chain + phosphate.
[Myosin light-chain]-phosphatase activity
myosin light chain kinase phosphatase activity
myosin-light-chain-phosphate phosphohydrolase activity
myosin light-chain kinase phosphatase activity
Catalysis of the reaction: [phosphorylase a] + 4 H2O = 2 [phosphorylase b] + 4 phosphate.
glycogen phosphorylase phosphatase activity
phosphorylase a phosphohydrolase activity
Catalysis of the reaction: ATP + rhodopsin = ADP + phosphorhodopsin.
ATP:rhodopsin phosphotransferase activity
rhodopsin kinase (phosphorylating) activity
G-protein-coupled receptor kinase 1 activity
Catalysis of the reaction: ATP + tau-protein = ADP + O-phospho-tau-protein.
ATP:tau-protein O-phosphotransferase activity
Catalysis of the reaction: ATP + tropomyosin = ADP + O-phosphotropomyosin.
ATP:tropomyosin O-phosphotransferase activity
tropomyosin kinase (phosphorylating) activity
Catalysis of the reaction: ATP + [tyrosine-3-monooxygenase] = ADP + phospho-[tyrosine-3-monooxygenase].
ATP:tyrosine-3-monoxygenase phosphotransferase activity
pheochromocytoma tyrosine hydroxylase-associated kinase activity
tyrosine 3-monooxygenase kinase (phosphorylating) activity
tyrosine 3-monooxygenase kinase activity
[tyrosine 3-monooxygenase] kinase activity
Catalysis of the reaction: ATP + [acetyl-CoA carboxylase] = ADP + [acetyl-CoA carboxylase] phosphate.
ATP:acetyl-CoA carboxylase phosphotransferase activity
acetyl coenzyme A carboxylase kinase (phosphorylating) activity
acetyl-CoA carboxylase kinase (AMP-activated) activity
acetyl-CoA carboxylase kinase (cAMP-independent) activity
acetyl-coenzyme A carboxylase kinase activity
acetyl-CoA carboxylase bound kinase activity
acetyl-CoA carboxylase kinase 2 activity
acetyl-CoA carboxylase kinase-2 activity
acetyl-CoA carboxylase kinase-3 (AMP-activated) activity
[acetyl-CoA carboxylase] kinase activity
Catalysis of the reaction: [acetyl-CoA carboxylase]-phosphate + H2O = [acetyl-CoA carboxylase] + phosphate.
acetyl-CoA carboxylase-phosphatase activity
acetyl-CoA:carbon-dioxide ligase (ADP-forming)-phosphate phosphohydrolase activity
[acetyl-CoA carboxylase]-phosphatase activity
Catalysis of the reaction: [glycogen-synthase D] + H2O = [glycogen-synthase I] + phosphate.
Mg2+ dependent glycogen synthase phosphatase activity
UDP-glucose:glycogen 4-alpha-D-glucosyltransferase-D phosphohydrolase activity
UDP-glycogen glucosyltransferase phosphatase activity
UDPglucose-glycogen glucosyltransferase phosphatase activity
UDPglucose:glycogen 4-alpha-D-glucosyltransferase-D phosphohydrolase activity
glycogen glucosyltransferase phosphatase activity
glycogen synthase D phosphatase activity
glycogen synthetase phosphatase activity
glycogen-synthase-D phosphatase activity
uridine diphosphoglucose-glycogen glucosyltransferase phosphatase activity
[glycogen-synthase-D] phosphatase activity
Catalysis of the reaction: [pyruvate kinase] phosphate + H2O = [pyruvate kinase] + phosphate.
ATP:pyruvate 2-O-phosphotransferase-phosphate phosphohydrolase activity
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.
Catalysis of the transfer of an alkylthio group from one compound (donor) to another (acceptor).
transferase activity, transferring alkylthio groups
Interacting selectively and non-covalently with icosanoids, any C20 polyunsaturated fatty acids or their derivatives, including the leukotrienes and the prostanoids.
Interacting selectively and non-covalently with icosatetraenoic acid, any straight-chain fatty acid with twenty carbon atoms and four double bonds per molecule.
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.
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.
5-oxo-6E,8Z,11Z,14Z-eicosatetraenoic acid binding
5-oxo-6E,8Z,11Z,14Z-icosatetraenoic acid binding
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.
5-hydroxy-6E,8Z,11Z,14Z-eicosatetraenoic acid binding
5-hydroxy-6E,8Z,11Z,14Z-icosatetraenoic acid binding
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.
5(S)-hydroxyperoxy-6E,8Z,11Z,14Z-eicosatetraenoic acid binding
5(S)-hydroxyperoxy-6E,8Z,11Z,14Z-icosatetraenoic acid binding
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.
3'-phosphoadenosine 5'-phosphosulphate binding
adenosine 3'-phosphate 5'-phosphosulfate binding
3'-phosphoadenosine 5'-phosphosulfate binding
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.
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.
nicotinamide adenine dinucleotide phosphate binding
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.
Any process that modulates the frequency, rate or extent of urothelial cell proliferation.
regulation of urothelial cell proliferation
Any process that stops, prevents or reduces the rate or extent of urothelial cell proliferation.
down regulation of urothelial cell proliferation
down-regulation of urothelial cell proliferation
downregulation of urothelial cell proliferation
inhibition of urothelial cell proliferation
negative regulation of urothelial cell proliferation
Any process that activates or increases the rate or extent of urothelial cell proliferation.
up regulation of urothelial cell proliferation
up-regulation of urothelial cell proliferation
upregulation of urothelial cell proliferation
activation of urothelial cell proliferation
stimulation of urothelial cell proliferation
positive regulation of urothelial cell proliferation
Any process that modulates the frequency, rate or extent of epithelial cell proliferation.
regulation of epithelial cell proliferation
Any process that activates or increases the rate or extent of epithelial cell proliferation.
up regulation of epithelial cell proliferation
up-regulation of epithelial cell proliferation
upregulation of epithelial cell proliferation
activation of epithelial cell proliferation
stimulation of epithelial cell proliferation
positive regulation of epithelial cell proliferation
Any process that stops, prevents or reduces the rate or extent of epithelial cell proliferation.
down regulation of epithelial cell proliferation
down-regulation of epithelial cell proliferation
downregulation of epithelial cell proliferation
inhibition of epithelial cell proliferation
negative regulation of epithelial cell proliferation
Interacting selectively and non-covalently with an androgen receptor.
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.
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.
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.
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.
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.
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.
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.
Interacting selectively and non-covalently with a low-density lipoprotein receptor.
low-density lipoprotein receptor binding
low-density lipoprotein particle receptor binding
Interacting selectively and non-covalently with a dopamine receptor.
Interacting selectively and non-covalently with the RAGE receptor, the receptor for advanced glycation end-products.
advanced glycation end-product receptor binding
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.
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.
regulation of cellular physiological process
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.
Interacting selectively and non-covalently with the gamma-aminobutyric acid (GABA, 4-aminobutyrate) receptor.
gamma-aminobutyric acid receptor binding
Interacting selectively and non-covalently with a phosphorylated serine residue within a protein.
Interacting selectively and non-covalently with a phosphorylated threonine residue within a protein.
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.
Interacting selectively and non-covalently with a cell adhesion molecule.
adhesive extracellular matrix constituent
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.
Interacting selectively and non-covalently with a cobalt (Co) ion.
The series of events involved in sensory perception in which a sensory stimulus is received and converted into a molecular signal.
sensory perception, sensory transduction of stimulus
detection of stimulus involved in sensory perception
The series of events in which a chemical stimulus is received and converted into a molecular signal as part of sensory perception.
sensory detection of chemical stimulus during sensory perception
sensory perception, sensory detection of chemical stimulus
sensory perception, sensory transduction of chemical stimulus
sensory transduction of chemical stimulus
sensory transduction of chemical stimulus during sensory perception
detection of chemical stimulus involved in sensory perception
The series of events involved in visual perception in which a light stimulus is received and converted into a molecular signal.
sensory detection of light during visual perception
sensory detection of light stimulus during visual perception
sensory transduction of light during visual perception
sensory transduction of light stimulus during visual perception
visual perception, detection of light stimulus
visual perception, sensory transduction during perception of light
visual perception, sensory transduction of light stimulus
detection of light stimulus involved in visual perception
The series of events involved in the perception of smell in which an olfactory chemical stimulus is received and converted into a molecular signal.
perception of smell, detection of chemical stimulus
perception of smell, sensory detection of chemical stimulus
perception of smell, sensory transduction of chemical stimulus
sensory detection of chemical stimulus during perception of smell
sensory transduction of chemical stimulus during perception of smell
detection of chemical stimulus involved in sensory perception of smell
The series of events involved in the perception of taste in which a gustatory chemical stimulus is received and converted into a molecular signal.
perception of taste, detection of chemical stimulus
perception of taste, sensory detection of chemical stimulus
perception of taste, sensory transduction of chemical stimulus
sensory detection of chemical stimulus during perception of taste
sensory transduction of chemical stimulus during perception of taste
detection of chemical stimulus involved in sensory perception of taste
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.
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.
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.
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.
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.
positive regulation of negative chemotaxis
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.
negative regulation of negative chemotaxis
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.
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.
positive regulation of positive chemotaxis
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.
negative regulation of positive chemotaxis
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.
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.
The series of events in which a temperature stimulus is received and converted into a molecular signal as part of thermoception.
sensory detection of temperature stimulus during thermoception
sensory detection of thermal stimulus during thermoception
sensory transduction of temperature stimulus during thermoception
sensory transduction of thermal stimulus during thermoception
thermoception, sensory detection of temperature stimulus
thermoception, sensory detection of thermal stimulus
thermoception, sensory transduction of temperature stimulus
thermoception, sensory transduction of thermal stimulus
detection of temperature stimulus involved in thermoception
The series of events in which a temperature stimulus is received and converted into a molecular signal as part of sensory perception.
sensory detection of temperature stimulus
sensory detection of temperature stimulus during sensory perception
sensory detection of thermal stimulus during sensory perception
sensory perception, sensory detection of temperature stimulus
sensory perception, sensory detection of thermal stimulus
sensory perception, sensory transduction of temperature stimulus
sensory perception, sensory transduction of thermal stimulus
sensory transduction of temperature stimulus
sensory transduction of temperature stimulus during sensory perception
sensory transduction of thermal stimulus during sensory perception
sensory detection of heat stimulus during sensory perception
sensory perception, sensory detection of heat stimulus
sensory perception, sensory transduction of heat stimulus
sensory transduction of heat stimulus during sensory perception
detection of temperature stimulus involved in sensory perception
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.
sensory detection of light stimulus during sensory perception
sensory perception, sensory detection of light stimulus
sensory perception, sensory transduction of light stimulus
sensory transduction of light stimulus during sensory perception
detection of light stimulus involved in sensory perception
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.
sensory detection of electrical stimulus
sensory detection of electrical stimulus during sensory perception
sensory perception, sensory detection of electrical stimulus
sensory perception, sensory transduction of electrical stimulus
sensory transduction of electrical stimulus
sensory transduction of electrical stimulus during sensory perception
detection of electrical stimulus involved in sensory perception
The series of events that contribute to electroception in which an electrical stimulus is received and converted into a molecular signal.
electroception, detection of electrical stimulus
electroception, sensory detection of electrical stimulus
electroception, sensory transduction of electrical stimulus
detection of electrical stimulus during electroreception
sensory detection of electrical stimulus during electroception
sensory transduction of electrical stimulus during electroception
detection of electrical stimulus involved in electroception
The series of events involved in the perception of pain in which a temperature stimulus is received and converted into a molecular signal.
perception of pain, detection of temperature stimulus
perception of pain, sensory detection of temperature stimulus
perception of pain, sensory transduction of temperature stimulus
sensory detection of temperature stimulus during perception of pain
sensory detection of thermal stimulus during sensory perception of pain
sensory perception of pain, sensory detection of thermal stimulus
sensory perception of pain, sensory transduction of thermal stimulus
sensory transduction of temperature stimulus during perception of pain
sensory transduction of thermal stimulus during sensory perception of pain
detection of temperature stimulus involved in sensory perception of pain
The series of events that contribute to the perception of pain in which an electrical stimulus is received and converted into a molecular signal.
perception of pain, detection of electrical stimulus
perception of pain, sensory detection of electrical stimulus
perception of pain, sensory transduction of electrical stimulus
detection of electrical stimulus during sensory perception of pain
sensory detection of electrical stimulus during perception of pain
sensory transduction of electrical stimulus during perception of pain
detection of electrical stimulus involved in sensory perception of pain
The series of events involved in the perception of pain in which a chemical stimulus is received and converted into a molecular signal.
perception of pain, detection of chemical stimulus
perception of pain, sensory detection of chemical stimulus
perception of pain, sensory transduction of chemical stimulus
sensory detection of chemical stimulus during perception of pain
sensory transduction of chemical stimulus during perception of pain
detection of chemical stimulus involved in sensory perception of pain
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.
magnetoception, sensory transduction of chemical stimulus
magnetoreception, detection of chemical stimulus
magnetoreception, sensory detection of chemical stimulus
magnetoreception, sensory transduction of chemical stimulus
sensory detection of chemical stimulus during magnetoreception
sensory transduction of chemical stimulus during magnetoreception
detection of chemical stimulus involved in magnetoreception
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.
magnetoception, sensory transduction of electrical stimulus
magnetoreception, detection of electrical stimulus
magnetoreception, sensory detection of electrical stimulus
magnetoreception, sensory transduction of electrical stimulus
detection of electrical stimulus during magnetoreception
sensory detection of electrical stimulus during magnetoreception
sensory transduction of electrical stimulus during magnetoreception
detection of electrical stimulus involved in magnetoreception
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.
magnetoreception, detection of light stimulus
magnetoreception, sensory detection of light stimulus
magnetoreception, sensory transduction of light stimulus
sensory detection of light stimulus during magnetoreception
sensory transduction of light stimulus during magnetoreception
detection of light stimulus involved in magnetoreception
The series of events by which an electrical stimulus is received and converted into a molecular signal.
Interacting selectively and non-covalently with the enzyme nitric-oxide synthase.
Interacting selectively and non-covalently with Hsp27 proteins, a lightweight heat shock protein.
Interacting selectively and non-covalently with the plus end of a microtubule.
Interacting selectively and non-covalently with the minus end of a microtubule.
Interacting selectively and non-covalently with an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits.
Interacting selectively and non-covalently with any subunit of protein kinase A.
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.
Interacting selectively and non-covalently with a mitogen-activated protein kinase.
mitogen-activated protein kinase binding
Interacting selectively and non-covalently with a GTPase, any enzyme that catalyzes the hydrolysis of GTP.
Interacting selectively and non-covalently with a GDP-dissociation inhibitor protein.
Interacting selectively and non-covalently with a Rho GDP-dissociation inhibitor protein.
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.
regulation of calcium-independent cell-cell adhesion
Any process that activates or increases the frequency, rate or extent of calcium-independent cell-cell adhesion.
up regulation of calcium-independent cell-cell adhesion
up-regulation of calcium-independent cell-cell adhesion
upregulation of calcium-independent cell-cell adhesion
activation of calcium-independent cell-cell adhesion
stimulation of calcium-independent cell-cell adhesion
positive regulation of calcium-independent cell-cell adhesion
Any process that stops, prevents, or reduces the frequency, rate or extent of calcium-independent cell-cell adhesion.
down regulation of calcium-independent cell-cell adhesion
down-regulation of calcium-independent cell-cell adhesion
downregulation of calcium-independent cell-cell adhesion
inhibition of calcium-independent cell-cell adhesion
negative regulation of calcium-independent cell-cell adhesion
Any process that modulates the frequency, rate or extent of the controlled release of a substance from a cell or a tissue.
Any process that activates or increases the frequency, rate or extent of the controlled release of a substance from a cell or a tissue.
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.
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.
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.
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.
Interacting selectively and non-covalently with NF-kappaB, a transcription factor for eukaryotic RNA polymerase II promoters.
Interacting selectively and non-covalently with an unfolded protein.
glycoprotein-specific chaperone activity
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.
Interacting selectively and non-covalently with an ATPase, any enzyme that catalyzes the hydrolysis of ATP.
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.
establishment and maintenance of localization
establishment and maintenance of position
establishment and maintenance of cellular component location
establishment and maintenance of substance location
establishment and maintenance of substrate location
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.
Interacting selectively and non-covalently with vanadium (V) ions.
Interacting selectively and non-covalently with a phosphorylated protein.
Any process that localizes a substance or cellular component. This may occur via movement, tethering or selective degradation.
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.
nicotinamide adenine dinucleotide binding
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.
cellular response to potassium ion deprivation
cellular response to potassium starvation
cellular response to potassium ion starvation
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.
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.
filamin-, actinin- and telethonin-binding protein of the Z-disc of striated muscle
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.
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.
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.
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.
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.
Interacting selectively and non-covalently with a phosphotyrosine-binding (PTB) domain of a protein.
phosphotyrosine-interacting domain binding
Interacting selectively and non-covalently with a receptor for hormones.
Interacting selectively and non-covalently with a receptor for peptide hormones.
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.
corticotropin releasing factor receptor binding
corticotropin-releasing factor receptor binding
corticotropin releasing factor receptor ligand
corticotropin-releasing hormone receptor binding
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.
type 1 corticotropin releasing factor receptor binding
type 1 corticotropin-releasing factor receptor binding
type 1 corticotropin releasing factor receptor ligand
corticotropin-releasing hormone receptor 1 binding
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.
type 2 corticotropin releasing factor receptor binding
type 2 corticotropin-releasing factor receptor binding
type 2 corticotropin releasing factor receptor ligand
corticotropin-releasing hormone receptor 2 binding
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.
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.
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.
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.
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.
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.
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.
nuclear factor of activated T cell protein binding
non-calcium-regulated NFAT protein binding
Interacting selectively and non-covalently with an iron-sulfur cluster, a combination of iron and sulfur atoms.
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.
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.
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.
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.
The series of events in which a glucose stimulus is received by a cell and converted into a molecular signal.
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.
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.
peptidolysis involved in cellular protein catabolic process
peptidolysis involved in cellular protein catabolism
peptidolysis during cellular protein catabolic process
peptidolysis during cellular protein catabolism
proteolysis during cellular protein catabolic process
proteolysis during cellular protein catabolism
proteolysis involved in cellular protein catabolic process
The series of events in which a stimulus is received by a cell or organism and converted into a molecular signal.
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.
Interacting selectively and non-covalently with the enzyme protein phosphatase 2A.
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.
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.
Interacting selectively and non-covalently with a misfolded protein.
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.
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.
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.
Interacting selectively and non-covalently with Hsp90 proteins, any of a group of heat shock proteins around 90kDa in size.
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.
Interacting selectively and non-covalently with granulocyte colony-stimulating factor, G-CSF.
granulocyte colony stimulating factor binding
granulocyte colony-stimulating factor binding
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.
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.
down regulation of calcium ion transport
down-regulation of calcium ion transport
negative regulation of calcium transport
negative regulation of calcium ion transport
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.
positive regulation of calcium transport
positive regulation of calcium ion transport
Interacting selectively and non-covalently with a light intermediate chain of the dynein complex.
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.
modulation of intracellular trafficking in other organism
modulation of intracellular transport in other organism during symbiotic interaction
modulation of intracellular transport in other organism involved in symbiotic interaction
A type of cell wall modification in which the cell wall is reinforced and made thicker.
Catalysis of the hydrolysis of a carboxylic ester bond.
Any biological process involved in the maintenance of an internal steady state of a chemical at the level of the cell.
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.
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.
The splitting or migration of one epithelial sheet into two involved in the process of deuterostomic gastrulation.
delamination involved in gastrulation with mouth forming second
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.
response to high fluence blue light by bhf system
response to high fluence blue light stimulus by blue high-fluence system
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.
response to very low light intensity stimulus
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.
The directed movement of copper ions out of a cell or organelle.
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.
positive regulation of epithelial cell proliferation involved in wound healing
The process in which a startle magnitude is reduced when the startling stimulus is preceded by a low-intensity prepulse.
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.
The process of negative regulation of cell adhesion that results in a cell or sheet of cells splitting off from an existing epithelial sheet.
The negative regulation of cell adhesion process in which an oenocyte splits off of an existing epithelial sheet.
The negative regulation of cell adhesion process in which a neuroblast splits off of a neurectodermal sheet.
Any process that stops, prevents or reduces the rate or extent of cell proliferation in response to cell density.
negative regulation of cell proliferation involved in contact inhibition
The series of events in which information about the density of cells in a population is received and converted into a molecular signal.
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.
detection of cell density by contact stimulus
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.
detection of cell density by secreted molecule
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.
detection of cell density by contact stimulus involved in contact inhibition
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.
Any process that modulates the establishment or extent of a membrane potential in the polarizing direction towards the resting potential in a ventricular cardiomyocyte.
regulation of ventricular cardiac muscle cell repolarization
regulation of ventricular cardiomyocyte membrane repolarization
regulation of ventricular cardiac muscle repolarization
regulation of ventricular cardiac muscle cell membrane repolarization
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.
Any process that modulates the establishment or extent of a membrane potential in the polarizing direction towards the resting potential in an atrial cardiomyocyte.
regulation of atrial cardiac muscle cell repolarization
regulation of atrial cardiomyocyte membrane repolarization
regulation of atrial cardiac muscle cell membrane repolarization
The directed movement of calcium ions (Ca2+) into, out of or within the cytosol.
The directed movement of calcium ions (Ca2+) into the cytosol.
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.
regulation of actin cortical patch localisation
regulation of actin cortical patch localization
Modulates the rate of NTP hydrolysis by a NTPase.
nucleoside-triphosphatase regulator activity
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.
regulation of cell proliferation involved in tissue homeostasis
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).
regulation of protein folding in endoplasmic reticulum
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.
Any process that modulates the frequency, rate or extent of cell proliferation that contributes to the shaping of the kidney.
regulation of cell proliferation involved in kidney morphogenesis
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.
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.
negative regulation of protein refolding
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.
regulation of positive chemotaxis to cAMP
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.
regulation of positive chemotaxis to cAMP by chlorinated alkylphenone
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.
regulation of positive chemotaxis to cAMP by DIF-1
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.
regulation of positive chemotaxis to cAMP by DIF-2
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.
positive regulation of positive chemotaxis to cAMP
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.
negative regulation of positive chemotaxis to cAMP
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.
positive regulation of positive chemotaxis to cAMP by chlorinated alkylphenone
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.
negative regulation of positive chemotaxis to cAMP by chlorinated alkylphenone
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.
positive regulation of positive chemotaxis to cAMP by DIF-1
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.
negative regulation of positive chemotaxis to cAMP by DIF-1
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.
positive regulation of chemotaxis to cAMP by DIF-2
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.
negative regulation of positive chemotaxis to cAMP by DIF-2
Any process that modulates the frequency, rate or extent of type B pancreatic cell proliferation.
regulation of type B pancreatic cell proliferation
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.
response to reverse transcriptase inhibitor
Interacting selectively and non-covalently with cyclic-GMP-AMP (cGAMP) cyclic nucleotide.
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.
calcium ion transmembrane transport via high voltage-gated calcium channel
Interacting selectively and non-covalently with a histone H3 in which the lysine residue at position 27 has been modified by trimethylation.
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.
RNA polymerase II sequence-specific DNA binding transcription factor binding
RNA polymerase II sequence-specific DNA-binding transcription factor binding
RNA polymerase II-specific DNA-binding transcription factor binding
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.
ubiquitin modification-dependent histone binding
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.
rhamnose-binding lectin family protein binding
Interacting selectively and non-covalently with any member of the importin-alpha family.
Interacting selectively and non-covalently with C-rich, single-stranded, telomere-associated DNA.
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.
Interacting selectively and non-covalently with an alpha-latrotoxin receptor.
Interacting selectively and non-covalently with a translation elongation factor, any polypeptide factor involved in the peptide elongation in ribosome-mediated translation.
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.
Interacting selectively and non-covalently with Epidermal Growth Factor (EGF) repeats.
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.
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.
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.
Golgi calcium ion transmembrane transport
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.
Interacting selectively and non-covalently with and responding, e.g. by conformational change, to changes in the cellular level of calcium ions (Ca2+).
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.
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.
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.
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.
Interacting selectively and non-covalently with a transcription factor TFIIH holo complex.
transcription factor TFIIH holo complex binding
Interacting selectively and non-covalently with a FACT complex.
Interacting selectively and non-covalently with a NuA4 histone acetyltransferase complex.
NuA4 histone acetyltransferase complex binding
Interacting selectively and non-covalently with a TAP complex.
Interacting selectively and non-covalently with an oligosaccharyltransferase complex.
oligosaccharyltransferase complex binding
Interacting selectively and non-covalently with a BBSome complex.
Interacting selectively and non-covalently with a box C/D snoRNP complex.
Interacting selectively and non-covalently with a box H/ACA snoRNP complex.
Interacting selectively and non-covalently with a PSII associated light-harvesting complex II.
PSII associated light-harvesting complex II binding
Interacting selectively and non-covalently with a chloroplast photosystem I.
Interacting selectively and non-covalently with a chloroplast photosystem II.
Interacting selectively and non-covalently with a GARP complex.
Interacting selectively and non-covalently with a SAGA complex.
Interacting selectively and non-covalently with a histone H3 in which the lysine residue at position 9 has been modified by trimethylation.
Interacting selectively and non-covalently with a TSC1-TSC2 complex.
Interacting selectively and non-covalently with a region of RNA containing a Pumilio-response element element. The consensus sequence for the element is UGUAAAUA.
Any process that modulates the frequency, rate or extent of protein localization to a non-growing cell tip.
regulation of protein localization to non-growing cell tip
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to a non-growing cell tip.
negative regulation of protein localization to non-growing cell tip
The directed import of zinc(2+) from the cytosol, across an organelle membrane, into the organelle.
Any process that modulates a measurable attribute of any biological process, quality or function.
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.
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.
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.
Interacting selectively and non-covalently with nitric oxide (NO).
Interacting selectively and non-covalently with the telomerase RNA template.
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.
Interacting selectively and non-covalently with a type V collagen trimer.
Interacting selectively and non-covalently with the D- or L-enantiomer of fructose, the ketohexose arabino-hex-2-ulose.
Interacting selectively and non-covalently with an RNA polymerase molecule or complex.
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.
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.
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.
Interacting selectively and non-covalently with fructose 6-phosphate.
Interacting selectively and non-covalently with the delta subunit of the catenin complex.
Interacting selectively and non-covalently with the cytokine ciliary neurotrophic factor.
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.
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.
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.
Interacting selectively and non-covalently with a DNA polymerase.
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.
Any process that modulates the frequency, rate or extent of the directed movement of a protein to a specific location.
regulation of establishment of protein localisation
regulation of establishment of protein localization
Any process that modulates the frequency, rate or extent of the directed movement of a protein to a specific location on a chromosome.
regulation of establishment of protein localisation to chromosome
regulation of establishment of protein localization to chromosome
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.
regulation of establishment of protein localisation to telomere
regulation of establishment of protein localization to telomere
Interacting selectively and non-covalently with phosphatidylinositol-4-phosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 4' position.
phosphatidylinositol-4-phosphate binding
Interacting selectively and non-covalently with any of the vitamin B6 compounds: pyridoxal, pyridoxamine and pyridoxine and the active form, pyridoxal phosphate.
Interacting selectively and non-covalently with pyridoxal, 3-hydroxy-5-(hydroxymethyl)-2-methylpyridine-4-carbaldehyde, a form of vitamin B6.
Interacting selectively and non-covalently with pyridoxamine, 4-(aminomethyl)-5-(hydroxymethyl)-2-methylpyridin-3-ol, a form of vitamin B6.
Interacting selectively and non-covalently with pyridoxine, 4,5-bis(hydroxymethyl)-2-methylpyridin-3-ol, a form of vitamin B6.
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.
The directed movement of calcium ions (Ca2+) into, out of or within the sarcoplasmic reticulum.
sarcoplasmic reticulum calcium ion transport
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.
Interacting selectively and non-covalently with thyroxine (T4) or triiodothyronine (T3), tyrosine-based hormones produced by the thyroid gland.
Interacting selectively and non-covalently with a lipoprotein particle receptor.
Interacting selectively and non-covalently with a very-low-density lipoprotein receptor.
very-low-density lipoprotein receptor binding
very-low-density lipoprotein particle receptor binding
Interacting selectively and non-covalently with aspartate, the alpha-amino-acid anion of 2-aminobutanedioic acid that has formula C4H5NO4.
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.
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.
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.
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.
The series of events in which a bacterial lipopeptide stimulus is received by a cell and converted into a molecular signal.
Any process that modulates the frequency, rate or extent of fat cell proliferation.
regulation of adipose cell proliferation
Any process that stops or decreases the rate or extent of fat cell proliferation.
down regulation of fat cell proliferation
down-regulation of fat cell proliferation
downregulation of fat cell proliferation
negative regulation of adipocyte proliferation
negative regulation of adipose cell proliferation
negative regulation of fat cell proliferation
Any process that activates or increases the rate or extent of fat cell proliferation.
positive regulation of adipocyte proliferation
positive regulation of adipose cell proliferation
positive regulation of fat cell proliferation
Any process that modulates the frequency, rate or extent of brown fat cell proliferation.
regulation of brown adipocyte proliferation
regulation of brown adipose cell proliferation
regulation of brown fat cell proliferation
Any process that stops or decreases the rate or extent of brown fat cell proliferation.
down regulation of brown fat cell proliferation
down-regulation of brown fat cell proliferation
downregulation of brown fat cell proliferation
negative regulation of brown adipocyte proliferation
negative regulation of brown adipose cell proliferation
inhibition of brown fat cell proliferation
negative regulation of brown fat cell proliferation
Any process that activates or increases the rate or extent of brown fat cell proliferation.
positive regulation of brown adipocyte proliferation
positive regulation of brown adipose cell proliferation
up regulation of brown fat cell proliferation
up-regulation of brown fat cell proliferation
upregulation of brown fat cell proliferation
activation of brown fat cell proliferation
stimulation of brown fat cell proliferation
positive regulation of brown fat cell proliferation
Any process that modulates the frequency, rate or extent of white fat cell proliferation.
regulation of white adipocyte proliferation
regulation of white adipose cell proliferation
regulation of white fat cell proliferation
Any process that stops or decreases the rate or extent of white fat cell proliferation.
down regulation of white fat cell proliferation
down-regulation of white fat cell proliferation
downregulation of white fat cell proliferation
negative regulation of white adipocyte proliferation
negative regulation of white adipose cell proliferation
inhibition of white fat cell proliferation
negative regulation of white fat cell proliferation
Any process that activates or increases the rate or extent of white fat cell proliferation.
positive regulation of white adipocyte proliferation
positive regulation of white adipose cell proliferation
up regulation of white fat cell proliferation
up-regulation of white fat cell proliferation
upregulation of white fat cell proliferation
activation of white fat cell proliferation
stimulation of white fat cell proliferation
positive regulation of white fat cell proliferation
Interacting selectively and non-covalently with high mobility group box 1 (HMBGB1).
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.
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.
Interacting selectively and non-covalently with the oxidized form, NADP+, of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions.
oxidized nicotinamide adenine dinucleotide phosphate binding
Interacting selectively and non-covalently with the reduced form, NADPH, of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions.
reduced nicotinamide adenine dinucleotide phosphate binding
Interacting selectively and non-covalently with the oxidized form, NAD, of nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions.
oxidized nicotinamide adenine dinucleotide binding
Interacting selectively and non-covalently with the reduced form, NADH, of nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions.
reduced nicotinamide adenine dinucleotide binding
Interacting selectively and non-covalently with ammonium ions (NH4+).
Interacting selectively and non-covalently with glutamine, 2,5-diamino-5-oxopentanoic acid.
Interacting selectively and non-covalently with a common mediator SMAD signaling protein.
Interacting selectively and non-covalently with an inhibitory SMAD signaling protein.
Interacting selectively and non-covalently with a receptor-regulated SMAD signaling protein.
The chemical reactions and pathways involving trehalose that occur as a result of a stimulus indicating the organism is under stress.
trehalose metabolic process involved in response to stress
trehalose metabolism in response to stress
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.
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.
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.
Interacting selectively and non-covalently with a transcription repressor, any protein whose activity is required to prevent or downregulate transcription.
Interacting selectively and non-covalently with any oligosaccharide, a molecule with between two and (about) 20 monosaccharide residues connected by glycosidic linkages.
The directed movement of calcium ions into a cell or organelle.
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.
For binding to the death effector domain, consider instead the term 'death effector domain binding ; GO:0035877'.
Interacting selectively and non-covalently with a protein upon poly-ubiquitination formed by linkages between lysine residues at position 63 in the target protein.
K63-linked polyubiquitin modification-dependent protein binding
Interacting selectively and non-covalently with oleic acid, the 18-carbon monounsaturated fatty acid (9Z)-octadec-9-enoic acid.
Interacting selectively and non-covalently with linoleic acid, the 18-carbon unsaturated fatty acid (9Z,12Z)-octadeca-9,12-dienoic acid.
Interacting selectively and non-covalently with stearic acid, the 18-carbon saturated fatty acid octadecanoic acid.
Catalysis of the transfer of an uridylyl group to an acceptor.
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.
Interacting selectively and non-covalently with a histone in which a lysine residue has been modified by acetylation.
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.
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.
juvenile hormone response element binding
Interacting selectively and non-covalently with a proteasome, a large multisubunit protein complex that catalyzes protein degradation.
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.
Interacting selectively and non-covalently with a high-density lipoprotein receptor.
high-density lipoprotein receptor binding
high-density lipoprotein particle receptor binding
Any process that modulates the frequency, rate or extent of leukocyte proliferation.
Any process that stops, prevents, or reduces the frequency, rate or extent of leukocyte proliferation.
down regulation of leukocyte proliferation
down-regulation of leukocyte proliferation
downregulation of leukocyte proliferation
negative regulation of leukocyte proliferation
Any process that activates or increases the frequency, rate or extent of leukocyte proliferation.
up regulation of leukocyte proliferation
up-regulation of leukocyte proliferation
positive regulation of leukocyte proliferation
Any process that modulates the frequency, rate or extent of mast cell proliferation.
Any process that stops, prevents or reduces the rate or extent of mast cell proliferation.
down regulation of mast cell proliferation
down-regulation of mast cell proliferation
downregulation of mast cell proliferation
negative regulation of mast cell proliferation
Any process that activates or increases the rate or extent of mast cell proliferation.
up regulation of mast cell proliferation
up-regulation of mast cell proliferation
positive regulation of mast cell proliferation
Interacting selectively and non-covalently with a preprotein, the unprocessed form of a protein destined to undergo co- or post-translational processing.
Interacting selectively and non-covalently with inositol 1,4,5 trisphosphate.
Interacting selectively and non-covalently with a receptor that spans a cell membrane and possesses protein serine/threonine kinase activity.
transmembrane receptor protein serine/threonine kinase binding
Interacting selectively and non-covalently with an activin receptor.
Interacting selectively and non-covalently with a type I activin receptor.
Interacting selectively and non-covalently with a type II activin receptor.
Interacting selectively and non-covalently with a BMP receptor.
bone morphogenetic protein receptor binding
A mismatch repair process that corrects errors introduced that ensures the accuracy of DNA replication.
mismatch repair involved in maintenance of fidelity during DNA-dependent DNA replication
mismatch repair involved in maintenance of fidelity involved in DNA-dependent DNA replication
Interacting selectively and non-covalently with any stretch of purines (adenine or guanine) in an RNA molecule.
Interacting selectively and non-covalently with 2-amino-4-methylpentanoic acid.
The directed movement of cyclic AMP (cAMP), into, out of or within a cell.
The directed movement of cyclic GMP (cGMP), into, out of or within a cell.
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.
Interacting selectively and non-covalently with interleukin-35.
Interacting selectively and non-covalently with the interleukin-35 receptor.
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.
The directed movement of divalent metal cations, any metal ion with a +2 electric charge, out of a cell or organelle.
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.
Interacting selectively and non-covalently with a growth factor receptor.
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.
Interacting selectively and non-covalently with a heavy chain of a myosin VI complex.
Interacting selectively and non-covalently with the head/neck region of a myosin VI heavy chain.
Interacting selectively and non-covalently with a light chain of a myosin VI complex.
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.
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.
Interacting selectively and non-covalently with a precursor microRNA (pre-miRNA) transcript, a stem-loop-containing precursor of microRNA.
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.
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.
Interacting selectively and non-covalently with lipoteichoic acid.
Interacting selectively and non-covalently with 2-amino-3-hydroxypropanoic acid.
The nucleotide-excision repair process in which DNA lesions are removed from nontranscribed strands and from transcriptionally silent regions over the entire genome.
global genomic nucleotide-excision repair
global genome nucleotide-excision repair
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).
UV-damaged DNA endonuclease-dependent excision repair
Interacting selectively and non-covalently with F420, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
Interacting selectively and non-covalently with pyrroloquinoline quinone, PQQ, the coenzyme or the prosthetic group of certain alcohol dehydrogenases and glucose dehydrogenases.
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.
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.
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.
Toll-Interleukin receptor domain binding
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.
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.
Interacting selectively and non-covalently with any part of a small nuclear ribonucleoprotein particle.
The series of events in which a stimulus indicating oxidative stress is received and converted into a molecular signal.
Interacting selectively and non-covalently with a type 1 melanocortin receptor.
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.
Interacting selectively and non-covalently with eukaryotic initiation factor eIF2, a protein complex involved in the initiation of ribosome-mediated translation.
eukaryotic initiation factor eIF2 binding
Interacting selectively and non-covalently with a conserved stem-loop structure found in histone pre-mRNAs.
Interacting selectively and non-covalently with the downstream cleavage product (DCP) generated by histone pre-mRNA 3'-end processing.
Interacting selectively and non-covalently with the U7 small nuclear RNA (U7 snRNA).
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.
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.
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.
cellular response to external biotic stimulus
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.
cellular response to bacteria associated molecule
cellular response to bacterial associated molecule
cellular response to bacterium associated molecule
cellular response to molecule of bacterial origin
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.
cellular response to bacterial lipoprotein
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.
cellular response to bacterial lipopeptide
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.
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.
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.
cellular response to fungus associated molecule
cellular response to molecule of fungal origin
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.
cellular response to oomycetes associated molecule
cellular response to molecule of oomycetes origin
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.
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.
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.
Interacting selectively and non-covalently with a connexin, any of a group of related proteins that assemble to form gap junctions.
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.
cellular response to electrical stimulus
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.
cellular response to gravitational stimulus
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.
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.
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.
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.
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.
cellular response to DL-alpha-tocopherol acetate
cellular response to DL-alpha-tocopheryl acetate
cellular response to O-Acetyl-alpha-tocopherol
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.
Any process that modulates the frequency, rate or extent of hair follicle cell proliferation.
regulation of hair follicle cell proliferation
Any process that stops, prevents or reduces the rate or extent of hair follicle cell proliferation.
down regulation of hair follicle cell proliferation
down-regulation of hair follicle cell proliferation
downregulation of hair follicle cell proliferation
inhibition of hair follicle cell proliferation
negative regulation of hair follicle cell proliferation
Any process that activates or increases the rate or extent of hair follicle cell proliferation.
up regulation of hair follicle cell proliferation
up-regulation of hair follicle cell proliferation
upregulation of hair follicle cell proliferation
activation of hair follicle cell proliferation
stimulation of hair follicle cell proliferation
positive regulation of hair follicle cell proliferation
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.
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.
Interacting selectively and non-covalently with DNA sequences encoding transfer RNA.
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.
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.
cellular response to alkyl hydroperoxide
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.
cellular response to lipid hydroperoxide
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.
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.
cellular response to increased oxygen tension
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.
cellular response to lowered oxygen tension
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%.
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.
cellular response to cell-matrix adhesion
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.
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.
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.
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'.
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.
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.
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.
cellular response to non-ionic osmotic stress
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.
cellular response to ionic osmotic stress
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.
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.
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.
cellular response to hyperosmotic salt stress
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.
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.
cellular response to hypotonic salt stress
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.
cellular response to electromagnetic radiation stimulus
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.
cellular response to ionizing radiation stimulus
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.
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).
cellular response to X-ray radiation stimulus
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.
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.
cellular response to blue light stimulus
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.
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.
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.
cellular response to high light intensity
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.
cellular response to low light intensity stimulus
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.
cellular response to very low light intensity stimulus
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.
cellular response to red or far red light
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.
cellular response to far red light stimulus
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.
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.
cellular response to UV-A light stimulus
cellular response to UV-A radiation stimulus
cellular response to UVA radiation stimulus
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.
cellular response to UV-B light stimulus
cellular response to UV-B radiation stimulus
cellular response to UVB radiation stimulus
cellular response to medium wave ultraviolet light stimulus
cellular response to medium wave ultraviolet radiation stimulus
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.
cellular response to UV-C light stimulus
cellular response to UV-C radiation stimulus
cellular response to UVC radiation stimulus
cellular response to germicidal ultraviolet light stimulus
cellular response to germicidal ultraviolet radiation stimulus
cellular response to shortwave ultraviolet light stimulus
cellular response to shortwave ultraviolet radiation stimulus
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.
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.
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.
cellular response to temperature stimulus
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.
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.
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.
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.
cell wall organisation in other organism
cell wall organization at cellular level
cell wall organization in other organism
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.
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.
The directed movement of zinc(2+) ions from outside of a cell, across the plasma membrane and into the cytosol.
high-affinity zinc II ion transmembrane import
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.
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.
regulation of zinc ion membrane transport
regulation of zinc ion transmembrane transport
Any process that modulates the frequency, rate or extent of zinc ion import.
regulation of zinc ion transmembrane import
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.
negative regulation of zinc ion transport
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.
negative regulation of zinc ion membrane transport
negative regulation of zinc ion transmembrane transport
Any process that stops, prevents, or reduces the frequency, rate or extent of zinc ion import.
negative regulation of zinc ion transmembrane import
A series of molecular signals mediated by the detection of hydrogen peroxide (H2O2).
hydrogen peroxide mediated signalling pathway
hydrogen peroxide mediated signaling pathway
Interacting selectively and non-covalently with a RNA/DNA hybrid.
The series of events in which an organic substance stimulus is received by a cell and converted into a molecular signal.
The chemical reactions and pathways involving an organic substance, any molecular entity containing carbon.
organic molecular entity metabolic process
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.
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.
response to diacylated bacterial lipoprotein
response to diacyl bacterial lipopeptide
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.
response to triacylated bacterial lipoprotein
response to triacyl bacterial lipopeptide
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.
cellular response to diacylated bacterial lipoprotein
cellular response to diacyl bacterial lipopeptide
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.
cellular response to triacylated bacterial lipoprotein
cellular response to triacyl bacterial lipopeptide
Interacting selectively and non-covalently with chemokine (C-C motif) ligand 5.
Regulated upon Activation, Normal T-cell Expressed, and Secreted binding
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.
Interacting selectively and non-covalently with a protein upon poly-ubiquitination formed by linkages between lysine residues at position 11 in the target protein.
K11-linked polyubiquitin modification-dependent protein binding
Interacting selectively and non-covalently with a protein upon poly-ubiquitination formed by linkages between lysine residues at position 6 in the target protein.
K6-linked polyubiquitin modification-dependent protein binding
A process in which a potassium ion is transported from one side of a membrane to the other.
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.
Interacting selectively and non-covalently with a protein-lipid complex, any macromolecular complex that contains both protein and lipid molecules.
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.
intermediate-density lipoprotein binding
intermediate-density lipoprotein particle binding
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.
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.
Interacting selectively and non-covalently with a neuropeptide receptor.
Interacting selectively and non-covalently with a beta-endorphin receptor.
Interacting selectively and non-covalently with a corazonin receptor.
Interacting selectively and non-covalently with a neuropeptide F receptor.
Interacting selectively and non-covalently with a proctolin receptor.
Interacting selectively and non-covalently with a tachykinin receptor.
A process that modulates the frequency, rate or extent of cell proliferation in the bone marrow.
regulation of bone marrow cell proliferation
regulation of cell proliferation in bone marrow
A process that activates or increases the frequency, rate or extent of cell proliferation in the bone marrow.
positive regulation of bone marrow cell proliferation
up regulation of cell proliferation in bone marrow
up-regulation of cell proliferation in bone marrow
upregulation of cell proliferation in bone marrow
activation of cell proliferation in bone marrow
stimulation of cell proliferation in bone marrow
positive regulation of cell proliferation in bone marrow
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.
Interacting selectively and non-covalently with bicarbonate (CHO3-) ions.
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.
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.
context dependent regulatory domain binding
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).
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.
oxidized flavin adenine dinucleotide binding
oxidized flavine-adenine dinucleotide binding
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.
reduced flavin adenine dinucleotide binding
reduced flavine-adenine dinucleotide binding
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.
Any process that modulates the frequency, rate or extent of mesenchymal stem cell proliferation and contributes to the shaping of a nephron.
regulation of mesenchymal stem cell proliferation involved in nephron morphogenesis
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.
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.
negative regulation of mesenchymal cell proliferation
Interacting selectively and non-covalently with a modified amino acid.
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.
Catalysis of the transfer of a phosphate group to the threonine-3 residue of the N-terminal tail of histone H3.
histone threonine kinase activity (H3-T3 specific)
histone-threonine kinase activity (H3-T3 specific)
histone kinase activity (H3-T3 specific)
Catalysis of the transfer of a phosphate group to the serine-121 residue of the N-terminal tail of histone H2A.
histone serine kinase activity (H2A-S121 specific)
histone-serine kinase activity (H2A-S121 specific)
histone kinase activity (H2A-S121 specific)
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.
sensing involved in DNA damage checkpoint
detection of DNA damage stimulus involved in DNA damage checkpoint
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.
detection of DNA damage stimulus involved in G2/M transition DNA damage checkpoint
G2/M transition DNA damage checkpoint sensor mechanism
G2/M transition DNA damage checkpoint sensor process
sensing involved in G2/M transition DNA damage checkpoint
detection of DNA damage stimulus involved in G2 DNA damage checkpoint
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.
DNA replication checkpoint sensor mechanism
DNA replication checkpoint sensor process
sensing involved in DNA replication checkpoint
detection of stimulus involved in DNA replication checkpoint
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.
Catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein. This reaction requires binding of the GTPase Rho.
Rho-dependent protein serine/threonine kinase activity
Interacting selectively and non-covalently with L-DOPA, the modified amino acid (2S)-2-amino-3-(3,4-dihydroxyphenyl)propanoic acid.
Interacting selectively and non-covalently with2-amino-3-(4-hydroxyphenyl)propanoic acid.
Interacting selectively and non-covalently with ADP-D-ribose, an ADP-aldose having ribose as the aldose fragment.
Interacting selectively and non-covalently with monomeric ADP-D-ribose, an ADP-aldose having ribose as the aldose fragment.
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.
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.
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.
cellular response to sodium dodecyl sulfate
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.
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.
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.
cellular response to calcium ion starvation
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.
response to 2-methyl-prop-2-yl-hydroperoxide
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.
cellular response to 2-methyl-prop-2-yl-hydroperoxide
cellular response to tert-butyl hydroperoxide
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.
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.
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.
phosphatidylinositol-3,5-bisphosphate binding
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.
Interacting selectively and non-covalently with the tail region of a myosin XI heavy chain.
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.
regulation of plant-type cell wall organisation or biogenesis
regulation of plant-type cell wall organization or biogenesis
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.
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).
Interacting selectively and non-covalently with any protein or protein complex contributing to the adhesion of two different types of cells.
protein binding involved in heterotypic cell-cell adhesion
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.
cell adhesive protein binding involved in atrial cardiomyocyte-AV node cell communication
cell adhesive protein binding involved in atrial cardiomyocyte-atrioventricular node cell communication
cell adhesive protein binding involved in atrial cardiac muscle cell-AV node cell communication
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.
cell adhesive protein binding involved in atrioventricular node cell-bundle of His cell communication
cell adhesive protein binding involved in AV node cell-bundle of His cell communication
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.
cell adhesive protein binding involved in bundle of His cell-Purkinje myocyte communication
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.
cell adhesive protein binding involved in Purkinje myocyte-ventricular cardiac muscle cell communication
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.
cell adhesive protein binding involved in SA cardiomyocyte-atrial cardiomyocyte communication
cell adhesive protein binding involved in SA cardiac muscle cell-atrial cardiac muscle cell communication
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.
Interacting selectively and non-covalently with an RHG (reaper/hid/grimm) domain/motif (AKA iap binding motif).
inhibitor of apoptosis binding domain binding
Interacting selectively and non-covalently with a caspase family protein.
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.
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.
positive regulation of ribosome biogenesis
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.
negative regulation of ribosome biogenesis
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.
regulation of secretion by asymmetric Golgi ribbon formation
Any process that modulates the rate, frequency, or extent of the directed movement of calcium ions into a cell or organelle.
regulation of transmembrane calcium influx
Any process that increases the rate, frequency, or extent of the directed movement of calcium ions into a cell or organelle.
positive regulation of transmembrane calcium influx
positive regulation of calcium ion import
Any process that decreases the rate, frequency, or extent of the directed movement of calcium ions into a cell or organelle.
negative regulation of transmembrane calcium influx
negative regulation of calcium ion import
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.
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.
positive regulation of osteoclast proliferation
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.
negative regulation of osteoclast proliferation
Any cellular metabolic process involving nucleic acids.
The process of loading nitrate into the sieve tube or companion cell of the phloem for long distance transport from source to sink.
Interacting selectively and non-covalently with a brassinosteroid.
The directed movement of lithium ions across a membrane.
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.
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.
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.
The process by which excess light energy absorbed by chlorophyll and not used to drive photosynthesis is re-emitted as light.
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.
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.
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.
The phosphorylation by a protein of one or more of its own histidine residues, or a histidine residue on an identical protein.
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.
response to the introduction of novel objects
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.
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.
cellular response to oxygen-glucose deprivation
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.
double-stranded/single-stranded junction telomeric DNA binding
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.
calcium ion transmembrane transport via low voltage-gated calcium channel
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.
Interacting selectively and non-covalently with a meprin and TRAF homology (MATH) domain.
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.
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.
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.
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.
The directed movement of heme out of a cell or organelle.
Interacting selectively and non-covalently with and responding, e.g. by conformational change, to changes in the cellular level of cadmium (Cd++).
Interacting selectively and non-covalently with and responding, e.g. by conformational change, to changes in the cellular level of copper(I) (Cu+).
Facilitates the base-pairing of single-stranded RNA to double-stranded DNA resulting in the formation of R-loops.
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.
Interacting selectively and non-covalently with a member of the hedgehog protein family, signaling proteins involved in development.
Interacting selectively and non-covalently with a member of the neuroligin protein family, neuronal cell surface proteins that mediate synapse formation.
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.
Interacting selectively and non-covalently with an intronic sequence of a pre-messenger RNA (pre-mRNA).
Interacting selectively and non-covalently with a pyrimidine-rich (CU-rich) intronic sequence of a pre-messenger RNA (pre-mRNA).
pre-messenger RNA intronic pyrimidine-rich binding
pre-mRNA intronic pyrimidine-rich binding
Interacting selectively and non-covalently with an organic cyclic compound, any molecular entity that contains carbon arranged in a cyclic molecular structure.
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.
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.
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.
Interacting selectively and non-covalently with any part of a mitochondrial ribosome, a ribosome found in the mitochondrion of a eukaryotic cell.
Interacting selectively and non-covalently with guanosine tetraphosphate (5'-ppGpp-3'), a guanosine bisphosphate having diphosphate groups at both the 3' and 5'-positions.
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.
Interacting selectively and non-covalently with a flavonol, a flavonoid that contains a 3-hydroxy-2-phenylchromen-4-one backbone.
Interacting selectively and non-covalently with a flavanol.
Interacting selectively and non-covalently with a catechin, a polyphenolic antioxidant plant metabolite with a flavonoid or flavan-3-ol structure.
Interacting selectively and non-covalently with epigallocatechin 3-gallate, a compound that is a gallic acid ester of a catechin.
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.
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.
Interacting selectively and non-covalently with a 7SK small nuclear RNA (7SK snRNA).
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.
Interacting selectively and non-covalently with a carbohydrate derivative.
Interacting selectively and non-covalently with any isoform of the MDM2/MDM4 protein family, comprising negative regulators of p53.
The acidification of the synaptic vesicle lumen via transport of protons into the vesicle. The resulting electrochemical gradient powers neurotransmitter loading.
The directed movement of copper ions from outside of a cell, across an ascospore-type prospore membrane and into the cytosol.
copper ion import across prospore membrane
copper ion import into ascospore-type prospore
The process of negative regulation of cell adhesion that results in blood vessel endothelial cells splitting off from an existing endothelial sheet.
blood vessel endothelial cell delamination
The repair of double-strand breaks in mitochondrial DNA via homologous and nonhomologous mechanisms to reform a continuous DNA helix.
Note that the processes of nuclear double-strand break repair and mitochondrial double-strand break repair are genetically separable.
mitochondrial double-strand break repair
The repair of a double-strand break in mitochondrial DNA in which the broken DNA molecule is repaired using homologous sequences.
mtDSB repair via homologous recombination
mitochondrial double-strand break repair via homologous recombination
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.
calcium transmembrane import into cytosol
calcium ion transmembrane import into cytosol
Interacting selectively and non-covalently with any member of the cullin family, hydrophobic proteins that act as scaffolds for ubiquitin ligases (E3).
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.
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'.
The directed movement of potassium ions from inside of a cell, across the plasma membrane and into the extracellular region.
Merged as of ticket of related term https://github.com/geneontology/go-ontology/issues/14265
potassium ion export across plasma membrane
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)).
Interacting selectively and non-covalently with amylin.
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.
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.
signal transducers and activators of transcription family protein binding
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.
suppressor of cytokine signaling family protein binding
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).
double-strand break repair via classical nonhomologous end joining
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.
double-strand break repair via microhomology-mediated end joining
double-strand break repair via alternative nonhomologous end joining
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.
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.
The directed movement of copper (Cu) ions passing through the blood-brain barrier.
copper ion transport across blood-brain barrier
The directed movement of copper (Cu) ions passing through the blood-cerebrospinal fluid barrier.
copper ion transport across blood-CSF barrier
copper ion transport across blood-cerebrospinal fluid barrier
Interacting selectively and non-covalently with a disordered domain of a protein.
disordered protein domain specific binding
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).
lamina-associated polypeptide, emerin, MAN1 domain binding
Interacting selectively and non-covalently with G-rich, single-stranded, telomere-associated DNA.
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.
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.
detection of humidity stimulus involved in sensory perception
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.
detection of high humidity stimulus involved in sensory perception
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.
detection of low humidity stimulus involved in sensory perception
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.
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.
Catalysis of a hydrolase reaction that removes a palmitoyl moiety from some substrate.
Catalysis of the reaction: protein arginine phosphate + H2O = protein arginine + phosphate.
Made part of peptidyl-N-phospho-arginine phosphatase activity on the assumption that arginine phosphorylation in proteins occurs via an N link.
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.
protein binding involved in cell adhesion
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.
protein binding involved in cell-cell adhesion
Interacting selectively and non-covalently with a collagen fibril.
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.
protein binding involved in cell-matrix adhesion
Any collagen binding that occurs as part of cell-matrix adhesion.
collagen binding involved in cell-matrix adhesion
Any integrin binding that occurs as part of the process of cell-matrix adhesion.
integrin binding involved in cell-matrix adhesion
Any cadherin binding that occurs as part of the process of cell-cell adhesion.
cadherin binding involved in cell-cell adhesion
Interacting selectively and non-covalently with a peptidyl-proline 4-dioxygenase.
The process in which a cation is transported across a membrane.
ATP hydrolysis coupled cation transmembrane transport
The directed movement of inorganic cations from outside of a cell, across the plasma membrane and into the cytosol.
inorganic cation import across plasma membrane
The process in which an inorganic ion is transported across a membrane.
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.
transmembrane inorganic cation transport
inorganic cation transmembrane transport
Any process that modulates the frequency, rate or extent of neurotransmitter receptor localization to postsynaptic specialization membrane.
regulation of neurotransmitter receptor localization to postsynaptic specialization membrane
The directed movement of calcium ions from outside of a cell, across the plasma membrane and into the cytosol.
calcium ion import across plasma membrane
The directed movement of copper ions from outside of a cell, across the plasma membrane and into the cytosol.
copper ion import across plasma membrane
The directed movement of iron ions from outside of a cell, across the cell outer membrane and into the periplasmic space.
ferric iron import across cell outer membrane
high-affinity ferric iron transmembrane transport
iron ion import across cell outer membrane
The directed movement of iron ions from outside of a cell, across the plasma membrane and into the cytosol.
ferrous iron import across plasma membrane
The directed movement of nickel cations from outside of a cell, across the plasma membrane and into the cytosol.
nickel cation import across plasma membrane
The directed movement of sodium ions from outside of a cell, across the plasma membrane and into the cytosol.
sodium ion import across plasma membrane
Interacting selectively and non-covalently with a FXYD domain.
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
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.
A molecular function that modulates the activity of a gene product or complex. Examples include enzyme regulators and channel regulators.
Interacting selectively and non-covalently with a 7-methylguanosine (m7G) group or derivative located at the 5' end of an mRNA molecule.
Interacting selectively and non-covalently with single-stranded DNA of a specific nucleotide composition.
sequence-specific single stranded DNA binding
Interacting selectively and non-covalently with double-stranded miRNA. double-stranded miRNA is formed by processing of pre-miRNA stem-loop structures.
DNA-binding activity that is dependent on binding to a histone.
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.
RNA polymerase II C-terminal domain binding
Interacting selectively and non-covalently with any estrogen.
The directed movement of Zn2+ ions from the cytoplasm into the lumen of a cytoplasmic vesicle.
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.
regulation of cytosolic calcium ion concentration by calcium ion buffering
calcium ion binding involved in regulation of cytosolic calcium ion concentration
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.
calcium ion binding involved in regulation of presynaptic cytosolic calcium levels
regulation of presynaptic cytosolic calcium ion concentration by calcium ion buffering
calcium ion binding involved in regulation of presynaptic cytosolic calcium ion concentration
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.
calcium ion binding involved in regulation of postsynaptic cytosolic calcium levels
regulation of postsynaptic cytosolic calcium ion concentration by calcium ion buffering
calcium ion binding involved in regulation of postsynaptic cytosolic calcium ion concentration
The directed movement of inorganic ions from outside of a cell, across the plasma membrane and into the cytosol.
inorganic ion import across plasma membrane
Interacting selectively and non-covalently with the side of a microtubule.
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.
regulation of cardiac muscle cell repolarization
regulation of cardiomyocyte membrane repolarization
regulation of cardiac muscle cell membrane repolarization
Any transcription from RNA polymerase II promoter process that negatively_regulates single organismal cell-cell adhesion
negative regulation of cell-cell adhesion by transcription from RNA polymerase II promoter
Catalysis of the reaction: protein histidine phosphate + H2O = protein histidine + phosphate
Catalysis of the reaction: [isocitrate dehydrogenase] phosphate + H2O = [isocitrate dehydrogenase] + phosphate.
[isocitrate dehydrogenase (NADP+)] phosphatase activity
Interacting selectively and non-covalently with the FMN-binding domain of a protein.
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.
cellular response to environmental stimulus
Any process that regulates the localization of a protein to the medial cortex.
regulation of protein localization to medial cortex
Any process that activates or increases the frequency, rate or extent of protein localization to the medial cortex.
positive regulation of protein localization to medial cortex
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to the cell cortex of the cell tip.
negative regulation of protein localization to cell cortex of cell tip
Interacting selectively and non-covalently with the GATOR1 complex.
Any process that stops, prevents or reduces the frequency, rate or extent of store-operated calcium entry.
negative regulation of store-operated calcium entry
Any process that activates or increases the frequency, rate or extent of store-operated calcium entry.
positive regulation of store-operated calcium entry
Interacting selectively and non-covalently with the IkappaB kinase complex.
Interacting selectively and non-covalently with a Sec61 translocon complex.
Interacting selectively and non-covalently with the P-TEFb complex.
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.
It is unclear if the motif bound by CNBHD is a specific motif or just a beta sheet with the appropriate amino acids.
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.
Any process that modulates the frequency, rate or extent of cardiac muscle myoblast proliferation.
regulation of cardiac muscle myoblast proliferation
Any process that stops, prevents, or reduces the frequency, rate or extent of cardiac muscle myoblast proliferation.
negative regulation of cardiac muscle myoblast proliferation
Any process that activates or increases the frequency, rate or extent of cardiac muscle myoblast proliferation.
positive regulation of cardiac muscle myoblast proliferation
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.
rDNA spacer replication fork barrier binding, bending
Interacting selectively and non-covalently with the C2 domain of a protein, a protein structural domain involved in targeting proteins to cell membranes.
Any process that modulates the frequency, rate or extent of mitotic telomere clustering during interphase.
regulation of mitotic telomere clustering during interphase
regulation of interphase mitotic telomere clustering
Any process that stops, prevents, or reduces the frequency, rate or extent of mitotic telomere clustering during interphase.
negative regulation of mitotic telomere clustering during interphase
negative regulation of interphase mitotic telomere clustering
Any process that modulates the frequency, rate or extent of calcium import into the mitochondrion.
regulation of calcium import into the mitochondrion
Any process that activates or increases the frequency, rate or extent of calcium import into the mitochondrion.
positive regulation of calcium import into the mitochondrion
Any process that stops, prevents or reduces the frequency, rate or extent of calcium ion import into the mitochondrion.
negative regulation of calcium import into the mitochondrion
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.
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.
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.
The directed movement of hydrogen ions (protons) from inside a cell, across the plasma membrane and into the extracellular region.
hydrogen ion export across plasma membrane
Any process that modulates the frequency, rate or extent of macrophage proliferation.
Any process that activates or increases the frequency, rate or extent of macrophage proliferation.
positive regulation of macrophage proliferation
Any process that stops, prevents, or reduces the frequency, rate or extent of macrophage proliferation.
negative regulation of macrophage proliferation
Any process that modulates the frequency, rate or extent of protein localization to a medial cortical node.
regulation of protein localization to medial cortical node
Any process that activates or increases the frequency, rate or extent of protein localization to a medial cortical node.
positive regulation of protein localization to medial cortical node
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.
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.
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.
Interacting selectively and non-covalently with an outer dynein arm in the presence of calcium.
calcium-dependent outer dynein arm binding
Interacting selectively and non-covalently with any carbohydrate in the presence of calcium.
Interacting selectively and non-covalently with an intraciliary transport particle A (IFT A) complex.
intraciliary transport complex A binding
intraflagellar transport complex A binding
intraflagellar transport particle A binding
intraciliary transport particle A binding
The series of events in which a hot stimulus is received and converted into a molecular signal as part of thermoception.
sensory detection of heat stimulus during thermoception
sensory detection of hot stimulus during thermoception
sensory transduction of heat stimulus during thermoception
sensory transduction of hot stimulus during thermoception
thermoception, sensory detection of heat stimulus
thermoception, sensory detection of hot stimulus
thermoception, sensory transduction of heat stimulus
thermoception, sensory transduction of hot stimulus
detection of hot stimulus involved in thermoception
The series of events in which a cold stimulus is received and converted into a molecular signal as part of thermoception.
sensory detection of cold stimulus during thermoception
sensory transduction of cold stimulus during thermoception
thermoception, sensory detection of cold stimulus
thermoception, sensory transduction of cold stimulus
detection of cold stimulus involved in thermoception
Interacting selectively and non-covalently with an intraciliary transport particle B (IFT B) complex.
intraciliary transport complex B binding
intraflagellar transport complex B binding
intraflagellar transport particle B binding
intraciliary transport particle B binding
Any process that stops, prevents, or reduces the frequency, rate or extent of protein localization to chromatin.
negative regulation of protein localisation to chromatin
negative regulation of protein localization to chromatin
Any process that activates or increases the frequency, rate or extent of protein localization to chromatin.
positive regulation of protein localisation to chromatin
positive regulation of protein localization to chromatin
Any process that modulates the frequency, rate or extent of the controlled release of bile acid from a cell or a tissue.
Any process that activates or increases the frequency, rate or extent of the controlled release of bile acid from a cell or a tissue.
positive regulation of bile acid secretion
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.
negative regulation of bile acid secretion
Interacting selectively and non-covalently with a protein upon post-translation modification of the target protein.
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.
Interacting selectively and non-covalently with a protein upon phosphorylation of the target protein.
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.
phosphorylation-dependent protein binding
Interacting selectively and non-covalently with a protein upon glycosylation of the target protein.
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.
Interacting selectively and non-covalently with a protein upon acetylation of the target protein.
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.
Interacting selectively and non-covalently with a protein upon methylation of the target protein.
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.
Interacting selectively and non-covalently with a protein upon modification by a ubiquitin-like protein of the target protein.
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.
ubiquitination-like modification-dependent protein binding
Interacting selectively and non-covalently with a protein upon ubiquitination of the target protein.
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.
Interacting selectively and non-covalently with a protein upon sumoylation of the target protein.
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.
The directed movement of manganese ions from inside of a cell, across the plasma membrane and into the extracellular region.
manganese ion export across plasma membrane
Interacting selectively and non-covalently with a glycosylated region of a protein.
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.
Catalytic activity that acts to modify a protein.
Catalytic activity that acts to modify RNA.
Catalytic activity that acts to modify a tRNA.
The process in which a potassium ion is transported across a mitochondrial membrane, into or out of the mitochondrion.
mitochondrial potassium ion transmembrane transport
The directed movement of copper ions out of the vacuole across the vacuolar membrane.
The directed movement of calcium cations into the vacuole across the vacuolar membrane.
The directed movement of zinc ions from inside the vacuole across the vacuolar membrane and into the cytosol.
Interacting selectively and non-covalently with the Golgi transport complex, a multisubunit tethering complex of the CATCHR family.
The directed import of zinc(2+) from the cytosol, across the endoplasmic reticulum membrane, into the endoplasmic reticulum.
zinc ion import across endoplasmic reticulum
zinc(2+) import across endoplasmic reticulum
zinc(2+) import into endoplasmic reticulum
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.
zinc ion import into endoplasmic reticulum
Interacting selectively and non-covalently with a PRC1 complex.
Interacting selectively and non-covalently with a mitochondrial proton-transporting ATP synthase complex.
mitochondrial proton-transporting ATP synthase complex binding
Interacting selectively and non-covalently with a mRNA cap binding complex.
The activity of a pathogen-derived entity that interacts with a host receptor to activate effector-triggered immunity.
pathogen-derived receptor ligand activity
Interacting selectively and non-covalently with a general transcription initiation factor, a protein that contributes to transcription start site selection and transcription initiation.
general transcription initiation factor binding
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.
DNA-binding transcription factor binding
Uptake of iron into a cell via binding to an extracellular receptor, which is internalized by endocytosis.
Binding to a small molecule and eliciting a change in the protein's activity in response to the intracellular level of that small molecule.
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to the medial cortex.
negative regulation of protein localization to medial cortex
The directed movement of heme from inside the vacuole across the vacuolar membrane and into the cytosol.
Create new term see https://github.com/geneontology/go-ontology/issues/17407
Any process that modulates the frequency, rate or extent of protein localization to lysosome.
regulation of protein localization to lysosome
Any process that activates or increases the frequency, rate or extent of protein localization to lysosome.
positive regulation of protein localization to lysosome
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to lysosome.
negative regulation of protein localization to lysosome
Any process that modulates the frequency, rate or extent of postsynaptic neurotransmitter receptor diffusion trapping.
regulation of postsynaptic neurotransmitter receptor diffusion trapping
Any RNA binding that is involved in posttranscriptional gene silencing.
RNA binding involved in post-transcriptional gene silencing
RNA binding involved in posttranscriptional gene silencing
Any process that modulates the frequency, rate or extent of hemostasis.
Any process that stops, prevents or reduces the frequency, rate or extent of hemostasis.
Any process that activates or increases the frequency, rate or extent of hemostasis.
Any process that modulates the frequency, rate or extent of cellular response to alkalinity.
regulation of cellular response to alkalinity
regulation of cellular response to basic pH
regulation of cellular response to alkaline pH
Any process that modulates the frequency, rate or extent of sulfite transport.
Any process that activates or increases the frequency, rate or extent of sulfite transport.
positive regulation of sulphite transport
positive regulation of sulfite transport
Any process that modulates the frequency, rate or extent of G-protein activated inward rectifier potassium channel activity.
regulation of G protein activated inward rectifier potassium channel activity
regulation of G protein enhanced inward rectifier potassium channel activity
regulation of G-protein enhanced inward rectifier potassium channel activity
regulation of G-protein-activated inward rectifier potassium channel activity
regulation of G-protein-enhanced inward rectifier potassium channel activity
regulation of G-protein activated inward rectifier potassium channel activity
Any process that activates or increases the frequency, rate or extent of G-protein activated inward rectifier potassium channel activity.
positive regulation of G protein activated inward rectifier potassium channel activity
positive regulation of G protein enhanced inward rectifier potassium channel activity
positive regulation of G-protein enhanced inward rectifier potassium channel activity
positive regulation of G-protein-activated inward rectifier potassium channel activity
positive regulation of G-protein-enhanced inward rectifier potassium channel activity
up regulation of G protein activated inward rectifier potassium channel activity
up regulation of G protein enhanced inward rectifier potassium channel activity
up regulation of G-protein activated inward rectifier potassium channel activity
up regulation of G-protein enhanced inward rectifier potassium channel activity
up regulation of G-protein-activated inward rectifier potassium channel activity
up regulation of G-protein-enhanced inward rectifier potassium channel activity
up-regulation of G protein activated inward rectifier potassium channel activity
up-regulation of G protein enhanced inward rectifier potassium channel activity
up-regulation of G-protein activated inward rectifier potassium channel activity
up-regulation of G-protein enhanced inward rectifier potassium channel activity
up-regulation of G-protein-activated inward rectifier potassium channel activity
up-regulation of G-protein-enhanced inward rectifier potassium channel activity
upregulation of G protein activated inward rectifier potassium channel activity
upregulation of G protein enhanced inward rectifier potassium channel activity
upregulation of G-protein activated inward rectifier potassium channel activity
upregulation of G-protein enhanced inward rectifier potassium channel activity
upregulation of G-protein-activated inward rectifier potassium channel activity
upregulation of G-protein-enhanced inward rectifier potassium channel activity
activation of G protein activated inward rectifier potassium channel activity
activation of G protein enhanced inward rectifier potassium channel activity
activation of G-protein activated inward rectifier potassium channel activity
activation of G-protein enhanced inward rectifier potassium channel activity
activation of G-protein-activated inward rectifier potassium channel activity
activation of G-protein-enhanced inward rectifier potassium channel activity
positive regulation of G-protein activated inward rectifier potassium channel activity
Any process that modulates the frequency, rate or extent of protein localization to nucleus.
regulation of protein localisation to nucleus
regulation of protein localization in cell nucleus
regulation of protein localization in nucleus
regulation of protein localization to nucleus
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to nucleus.
down regulation of protein localisation to nucleus
down regulation of protein localization in cell nucleus
down regulation of protein localization in nucleus
down regulation of protein localization to nucleus
down-regulation of protein localisation to nucleus
down-regulation of protein localization in cell nucleus
down-regulation of protein localization in nucleus
down-regulation of protein localization to nucleus
downregulation of protein localisation to nucleus
downregulation of protein localization in cell nucleus
downregulation of protein localization in nucleus
downregulation of protein localization to nucleus
negative regulation of protein localisation to nucleus
negative regulation of protein localization in cell nucleus
negative regulation of protein localization in nucleus
inhibition of protein localisation to nucleus
inhibition of protein localization in cell nucleus
inhibition of protein localization in nucleus
inhibition of protein localization to nucleus
negative regulation of protein localization to nucleus
Any process that activates or increases the frequency, rate or extent of protein localization to nucleus.
activation of protein localization in nucleus
positive regulation of protein localisation to nucleus
positive regulation of protein localization in cell nucleus
positive regulation of protein localization in nucleus
up regulation of protein localisation to nucleus
up regulation of protein localization in cell nucleus
up regulation of protein localization in nucleus
up regulation of protein localization to nucleus
up-regulation of protein localisation to nucleus
up-regulation of protein localization in cell nucleus
up-regulation of protein localization in nucleus
up-regulation of protein localization to nucleus
upregulation of protein localisation to nucleus
upregulation of protein localization in cell nucleus
upregulation of protein localization in nucleus
upregulation of protein localization to nucleus
activation of protein localisation to nucleus
activation of protein localization in cell nucleus
activation of protein localization to nucleus
positive regulation of protein localization to nucleus
Any process that modulates the frequency, rate or extent of monocyte aggregation.
regulation of mononuclear phagocyte aggregation
Any process that stops, prevents or reduces the frequency, rate or extent of monocyte aggregation.
down regulation of mononuclear phagocyte aggregation
down-regulation of mononuclear phagocyte aggregation
downregulation of mononuclear phagocyte aggregation
inhibition of mononuclear phagocyte aggregation
negative regulation of mononuclear phagocyte aggregation
negative regulation of monocyte aggregation
Any process that activates or increases the frequency, rate or extent of monocyte aggregation.
activation of mononuclear phagocyte aggregation
positive regulation of mononuclear phagocyte aggregation
up regulation of mononuclear phagocyte aggregation
up-regulation of mononuclear phagocyte aggregation
upregulation of mononuclear phagocyte aggregation
positive regulation of monocyte aggregation
Any cardiac neural crest cell delamination that is involved in outflow tract morphogenesis.
cardiac neural crest cell delamination involved in outflow tract morphogenesis
Interacting selectively and non-covalently with an oligopeptide.
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.
Any process that modulates the frequency, rate or extent of potassium ion transmembrane transporter activity.
regulation of potassium transporter activity
regulation of potassium ion transmembrane transporter activity
Any process that stops, prevents or reduces the frequency, rate or extent of potassium ion transmembrane transporter activity.
down regulation of potassium ion transmembrane transporter activity
down regulation of potassium transporter activity
down-regulation of potassium ion transmembrane transporter activity
down-regulation of potassium transporter activity
downregulation of potassium ion transmembrane transporter activity
downregulation of potassium transporter activity
inhibition of potassium transporter activity
negative regulation of potassium transporter activity
inhibition of potassium ion transmembrane transporter activity
negative regulation of potassium ion transmembrane transporter activity
Any process that activates or increases the frequency, rate or extent of potassium ion transmembrane transporter activity.
activation of potassium transporter activity
positive regulation of potassium transporter activity
up regulation of potassium ion transmembrane transporter activity
up regulation of potassium transporter activity
up-regulation of potassium ion transmembrane transporter activity
up-regulation of potassium transporter activity
upregulation of potassium ion transmembrane transporter activity
upregulation of potassium transporter activity
activation of potassium ion transmembrane transporter activity
positive regulation of potassium ion transmembrane transporter activity
Any process that modulates the frequency, rate or extent of calcium ion transmembrane transporter activity.
regulation of calcium ion transmembrane transporter activity
Any process that stops, prevents or reduces the frequency, rate or extent of calcium ion transmembrane transporter activity.
down regulation of calcium ion transmembrane transporter activity
down-regulation of calcium ion transmembrane transporter activity
downregulation of calcium ion transmembrane transporter activity
inhibition of calcium ion transmembrane transporter activity
negative regulation of calcium ion transmembrane transporter activity
Any process that activates or increases the frequency, rate or extent of calcium ion transmembrane transporter activity.
up regulation of calcium ion transmembrane transporter activity
up-regulation of calcium ion transmembrane transporter activity
upregulation of calcium ion transmembrane transporter activity
activation of calcium ion transmembrane transporter activity
positive regulation of calcium ion transmembrane transporter activity
The chemical reactions and pathways involving carbohydrate derivative.
carbohydrate derivative metabolic process
The chemical reactions and pathways resulting in the breakdown of carbohydrate derivative.
carbohydrate derivative catabolic process
Interacting selectively and non-covalently with salicylic acid.
Any positive regulation of calcium ion transport into cytosol that is involved in cellular response to calcium ion.
positive regulation of calcium ion transport into cytosol involved in cellular response to Ca2+ ion
positive regulation of calcium ion transport into cytosol involved in cellular response to calcium ion
Any positive regulation of calcium ion transport into cytosol that is involved in cellular response to salt stress.
positive regulation of calcium ion transport into cytosol involved in cellular response to ionic osmotic stress
positive regulation of calcium ion transport into cytosol involved in cellular salinity response
positive regulation of calcium ion transport into cytosol involved in cellular response to salt stress
Any negative regulation of calcium ion transport into cytosol that is involved in cellular response to salt stress.
negative regulation of calcium ion transport into cytosol involved in cellular response to ionic osmotic stress
negative regulation of calcium ion transport into cytosol involved in cellular salinity response
negative regulation of calcium ion transport into cytosol involved in cellular response to salt stress
Any nucleotide-excision repair that is involved in interstrand cross-link repair.
NER involved in interstrand cross-link repair
nucleotide-excision repair involved in ICL repair
nucleotide-excision repair involved in interstrand cross-link repair
Interacting selectively and non-covalently with nucleoside phosphate.
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.
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.
Interacting selectively and non-covalently with catecholamine.
Any process that modulates the frequency, rate or extent of store-operated calcium channel activity.
regulation of store-operated calcium channel activity
Any process that stops, prevents or reduces the frequency, rate or extent of store-operated calcium channel activity.
down regulation of store-operated calcium channel activity
down-regulation of store-operated calcium channel activity
downregulation of store-operated calcium channel activity
inhibition of store-operated calcium channel activity
negative regulation of store-operated calcium channel activity
Any process that activates or increases the frequency, rate or extent of store-operated calcium channel activity.
up regulation of store-operated calcium channel activity
up-regulation of store-operated calcium channel activity
upregulation of store-operated calcium channel activity
positive regulation of store-operated calcium channel activity
Interacting selectively and non-covalently with tungstate.
The chemical reactions and pathways involving organic cyclic compound.
organic cyclic compound metabolic process
The chemical reactions and pathways resulting in the formation of organic cyclic compound.
organic cyclic compound biosynthetic process
Interacting selectively and non-covalently with heterocyclic compound.
Any process that modulates the frequency, rate or extent of potassium ion transmembrane transport.
regulation of potassium ion membrane transport
regulation of potassium ion transmembrane transport
Any process that stops, prevents or reduces the frequency, rate or extent of potassium ion transmembrane transport.
down regulation of potassium ion transmembrane transport
down-regulation of potassium ion transmembrane transport
downregulation of potassium ion transmembrane transport
negative regulation of potassium ion membrane transport
inhibition of potassium ion transmembrane transport
negative regulation of potassium ion transmembrane transport
Any process that activates or increases the frequency, rate or extent of potassium ion transmembrane transport.
positive regulation of potassium ion membrane transport
up regulation of potassium ion transmembrane transport
up-regulation of potassium ion transmembrane transport
upregulation of potassium ion transmembrane transport
activation of potassium ion transmembrane transport
positive regulation of potassium ion transmembrane transport
Any process that modulates the frequency, rate or extent of chorionic trophoblast cell proliferation.
regulation of chorionic trophoblast cell proliferation
Any process that stops, prevents or reduces the frequency, rate or extent of chorionic trophoblast cell proliferation.
down regulation of chorionic trophoblast cell proliferation
down-regulation of chorionic trophoblast cell proliferation
downregulation of chorionic trophoblast cell proliferation
inhibition of chorionic trophoblast cell proliferation
negative regulation of chorionic trophoblast cell proliferation
Any process that activates or increases the frequency, rate or extent of chorionic trophoblast cell proliferation.
up regulation of chorionic trophoblast cell proliferation
up-regulation of chorionic trophoblast cell proliferation
upregulation of chorionic trophoblast cell proliferation
activation of chorionic trophoblast cell proliferation
positive regulation of chorionic trophoblast cell proliferation
Any process that modulates the frequency, rate or extent of voltage-gated calcium channel activity.
regulation of depolarization-activated calcium channel
regulation of depolarization-activated voltage gated calcium channel activity
regulation of depolarization-activated voltage-gated calcium channel
regulation of depolarization-activated voltage-gated calcium channel activity
regulation of voltage gated calcium channel activity
regulation of voltage-dependent calcium channel activity
regulation of voltage-gated calcium ion channel activity
regulation of voltage-sensitive calcium channel
regulation of dihydropyridine-sensitive calcium channel activity
regulation of voltage-gated calcium channel activity
Any process that stops, prevents or reduces the frequency, rate or extent of voltage-gated calcium channel activity.
down regulation of depolarization-activated calcium channel
down-regulation of depolarization-activated calcium channel
downregulation of depolarization-activated calcium channel
inhibition of depolarization-activated calcium channel
negative regulation of depolarization-activated calcium channel
down regulation of depolarization-activated voltage gated calcium channel activity
down regulation of depolarization-activated voltage-gated calcium channel
down regulation of depolarization-activated voltage-gated calcium channel activity
down regulation of voltage gated calcium channel activity
down regulation of voltage-dependent calcium channel activity
down regulation of voltage-gated calcium channel activity
down regulation of voltage-gated calcium ion channel activity
down regulation of voltage-sensitive calcium channel
down-regulation of depolarization-activated voltage gated calcium channel activity
down-regulation of depolarization-activated voltage-gated calcium channel
down-regulation of depolarization-activated voltage-gated calcium channel activity
down-regulation of voltage gated calcium channel activity
down-regulation of voltage-dependent calcium channel activity
down-regulation of voltage-gated calcium channel activity
down-regulation of voltage-gated calcium ion channel activity
down-regulation of voltage-sensitive calcium channel
downregulation of depolarization-activated voltage gated calcium channel activity
downregulation of depolarization-activated voltage-gated calcium channel
downregulation of depolarization-activated voltage-gated calcium channel activity
downregulation of voltage gated calcium channel activity
downregulation of voltage-dependent calcium channel activity
downregulation of voltage-gated calcium channel activity
downregulation of voltage-gated calcium ion channel activity
downregulation of voltage-sensitive calcium channel
inhibition of depolarization-activated voltage gated calcium channel activity
inhibition of depolarization-activated voltage-gated calcium channel
inhibition of depolarization-activated voltage-gated calcium channel activity
inhibition of voltage gated calcium channel activity
inhibition of voltage-dependent calcium channel activity
inhibition of voltage-gated calcium ion channel activity
inhibition of voltage-sensitive calcium channel
negative regulation of depolarization-activated voltage gated calcium channel activity
negative regulation of depolarization-activated voltage-gated calcium channel
negative regulation of depolarization-activated voltage-gated calcium channel activity
negative regulation of voltage gated calcium channel activity
negative regulation of voltage-dependent calcium channel activity
negative regulation of voltage-gated calcium ion channel activity
negative regulation of voltage-sensitive calcium channel
down regulation of dihydropyridine-sensitive calcium channel activity
down-regulation of dihydropyridine-sensitive calcium channel activity
downregulation of dihydropyridine-sensitive calcium channel activity
inhibition of dihydropyridine-sensitive calcium channel activity
inhibition of voltage-gated calcium channel activity
negative regulation of dihydropyridine-sensitive calcium channel activity
negative regulation of voltage-gated calcium channel activity
Any process that activates or increases the frequency, rate or extent of voltage-gated calcium channel activity.
activation of depolarization-activated calcium channel
positive regulation of depolarization-activated calcium channel
up regulation of depolarization-activated calcium channel
up-regulation of depolarization-activated calcium channel
upregulation of depolarization-activated calcium channel
activation of depolarization-activated voltage gated calcium channel activity
activation of depolarization-activated voltage-gated calcium channel
activation of depolarization-activated voltage-gated calcium channel activity
activation of voltage gated calcium channel activity
activation of voltage-dependent calcium channel activity
activation of voltage-gated calcium ion channel activity
activation of voltage-sensitive calcium channel
positive regulation of depolarization-activated voltage gated calcium channel activity
positive regulation of depolarization-activated voltage-gated calcium channel
positive regulation of depolarization-activated voltage-gated calcium channel activity
positive regulation of voltage gated calcium channel activity
positive regulation of voltage-dependent calcium channel activity
positive regulation of voltage-gated calcium ion channel activity
positive regulation of voltage-sensitive calcium channel
up regulation of depolarization-activated voltage gated calcium channel activity
up regulation of depolarization-activated voltage-gated calcium channel
up regulation of depolarization-activated voltage-gated calcium channel activity
up regulation of voltage gated calcium channel activity
up regulation of voltage-dependent calcium channel activity
up regulation of voltage-gated calcium channel activity
up regulation of voltage-gated calcium ion channel activity
up regulation of voltage-sensitive calcium channel
up-regulation of depolarization-activated voltage gated calcium channel activity
up-regulation of depolarization-activated voltage-gated calcium channel
up-regulation of depolarization-activated voltage-gated calcium channel activity
up-regulation of voltage gated calcium channel activity
up-regulation of voltage-dependent calcium channel activity
up-regulation of voltage-gated calcium channel activity
up-regulation of voltage-gated calcium ion channel activity
up-regulation of voltage-sensitive calcium channel
upregulation of depolarization-activated voltage gated calcium channel activity
upregulation of depolarization-activated voltage-gated calcium channel
upregulation of depolarization-activated voltage-gated calcium channel activity
upregulation of voltage gated calcium channel activity
upregulation of voltage-dependent calcium channel activity
upregulation of voltage-gated calcium channel activity
upregulation of voltage-gated calcium ion channel activity
upregulation of voltage-sensitive calcium channel
activation of dihydropyridine-sensitive calcium channel activity
activation of voltage-gated calcium channel activity
positive regulation of dihydropyridine-sensitive calcium channel activity
up regulation of dihydropyridine-sensitive calcium channel activity
up-regulation of dihydropyridine-sensitive calcium channel activity
upregulation of dihydropyridine-sensitive calcium channel activity
positive regulation of voltage-gated calcium channel activity
Any hydrogen peroxide mediated signaling pathway that is involved in stomatal movement.
H2O2 mediated signaling pathway involved in stomatal movement
hydrogen peroxide mediated signalling pathway involved in stomatal movement
hydrogen peroxide mediated signaling pathway involved in stomatal movement
Any process that activates or increases the frequency, rate or extent of anion channel activity.
positive regulation of anion channel activity
Interacting selectively and non-covalently with hypochlorite.
The chemical reactions and pathways involving organonitrogen compound.
organonitrogen compound metabolic process
The chemical reactions and pathways resulting in the breakdown of organonitrogen compound.
organonitrogen compound catabolic process
Interacting selectively and non-covalently with fatty acid derivative.
The chemical reactions and pathways resulting in the breakdown of an organic substance, any molecular entity containing carbon.
organic molecular entity catabolic process
The chemical reactions and pathways resulting in the formation of an organic substance, any molecular entity containing carbon.
organic molecular entity biosynthetic process
Any process that modulates the frequency, rate or extent of acid-sensing ion channel activity.
regulation of acid-sensing ion channel activity
Any process that stops, prevents or reduces the frequency, rate or extent of acid-sensing ion channel activity.
down regulation of acid-sensing ion channel activity
down-regulation of acid-sensing ion channel activity
downregulation of acid-sensing ion channel activity
inhibition of acid-sensing ion channel activity
negative regulation of acid-sensing ion channel activity
Any process that activates or increases the frequency, rate or extent of acid-sensing ion channel activity.
up regulation of acid-sensing ion channel activity
up-regulation of acid-sensing ion channel activity
upregulation of acid-sensing ion channel activity
activation of acid-sensing ion channel activity
positive regulation of acid-sensing ion channel activity
Interacting selectively and non-covalently with dethiobiotin.
Interacting selectively and non-covalently with phosphatidylglycerol.
Interacting selectively and non-covalently with cardiolipin.
Interacting selectively and non-covalently with XTP.
Interacting selectively and non-covalently with ITP.
Any process that modulates the frequency, rate or extent of synoviocyte proliferation.
Any process that stops, prevents or reduces the frequency, rate or extent of synoviocyte proliferation.
down regulation of synoviocyte proliferation
down-regulation of synoviocyte proliferation
downregulation of synoviocyte proliferation
negative regulation of synoviocyte proliferation
Any process that activates or increases the frequency, rate or extent of synoviocyte proliferation.
up regulation of synoviocyte proliferation
up-regulation of synoviocyte proliferation
upregulation of synoviocyte proliferation
positive regulation of synoviocyte proliferation
The directed movement of calcium ion out of a cell or organelle.
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.
Interacting selectively and non-covalently with a sulfur compound.
Interacting selectively and non-covalently with proton.
Interacting selectively and non-covalently with leptomycin B.
Any process that modulates the frequency, rate or extent of high voltage-gated calcium channel activity.
regulation of high voltage gated calcium channel activity
regulation of high voltage-dependent calcium channel activity
regulation of high voltage-gated calcium channel activity
Any process that stops, prevents or reduces the frequency, rate or extent of high voltage-gated calcium channel activity.
down regulation of high voltage gated calcium channel activity
down regulation of high voltage-dependent calcium channel activity
down regulation of high voltage-gated calcium channel activity
down-regulation of high voltage gated calcium channel activity
down-regulation of high voltage-dependent calcium channel activity
down-regulation of high voltage-gated calcium channel activity
downregulation of high voltage gated calcium channel activity
downregulation of high voltage-dependent calcium channel activity
downregulation of high voltage-gated calcium channel activity
inhibition of high voltage gated calcium channel activity
inhibition of high voltage-dependent calcium channel activity
negative regulation of high voltage gated calcium channel activity
negative regulation of high voltage-dependent calcium channel activity
inhibition of high voltage-gated calcium channel activity
negative regulation of high voltage-gated calcium channel activity
Any process that activates or increases the frequency, rate or extent of high voltage-gated calcium channel activity.
activation of high voltage gated calcium channel activity
activation of high voltage-dependent calcium channel activity
positive regulation of high voltage gated calcium channel activity
positive regulation of high voltage-dependent calcium channel activity
up regulation of high voltage gated calcium channel activity
up regulation of high voltage-dependent calcium channel activity
up regulation of high voltage-gated calcium channel activity
up-regulation of high voltage gated calcium channel activity
up-regulation of high voltage-dependent calcium channel activity
up-regulation of high voltage-gated calcium channel activity
upregulation of high voltage gated calcium channel activity
upregulation of high voltage-dependent calcium channel activity
upregulation of high voltage-gated calcium channel activity
activation of high voltage-gated calcium channel activity
positive regulation of high voltage-gated calcium channel activity
Any process that modulates the frequency, rate or extent of an ATPase-coupled calcium transmembrane transporter activity.
regulation of ATP phosphohydrolase (Ca2+-transporting)
regulation of Ca(2+)-transporting ATPase activity
regulation of Ca2+-pumping ATPase activity
regulation of Ca2+-transporting ATPase activity
regulation of calcium transporting ATPase activity
regulation of calcium-transporting ATPase activity
regulation of calcium-translocating P-type ATPase activity
regulation of sarco(endo)plasmic reticulum Ca2+-ATPase
regulation of sarcoplasmic reticulum ATPase
regulation of ATPase-coupled calcium transmembrane transporter activity
Any process that stops, prevents or reduces the frequency, rate or extent of an ATPase-coupled calcium transmembrane transporter activity.
down regulation of ATP phosphohydrolase (Ca2+-transporting)
down regulation of Ca(2+)-transporting ATPase activity
down regulation of Ca2+-pumping ATPase activity
down regulation of Ca2+-transporting ATPase activity
down regulation of calcium transporting ATPase activity
down regulation of calcium-transporting ATPase activity
down-regulation of ATP phosphohydrolase (Ca2+-transporting)
down-regulation of Ca(2+)-transporting ATPase activity
down-regulation of Ca2+-pumping ATPase activity
down-regulation of Ca2+-transporting ATPase activity
down-regulation of calcium transporting ATPase activity
down-regulation of calcium-transporting ATPase activity
downregulation of ATP phosphohydrolase (Ca2+-transporting)
downregulation of Ca(2+)-transporting ATPase activity
downregulation of Ca2+-pumping ATPase activity
downregulation of Ca2+-transporting ATPase activity
downregulation of calcium transporting ATPase activity
downregulation of calcium-transporting ATPase activity
inhibition of ATP phosphohydrolase (Ca2+-transporting)
inhibition of Ca(2+)-transporting ATPase activity
inhibition of Ca2+-pumping ATPase activity
inhibition of Ca2+-transporting ATPase activity
inhibition of calcium transporting ATPase activity
negative regulation of ATP phosphohydrolase (Ca2+-transporting)
negative regulation of Ca(2+)-transporting ATPase activity
negative regulation of Ca2+-pumping ATPase activity
negative regulation of Ca2+-transporting ATPase activity
negative regulation of calcium transporting ATPase activity
negative regulation of calcium-transporting ATPase activity
down regulation of calcium ABC transporter
down regulation of calcium efflux ATPase
down regulation of calcium-translocating P-type ATPase activity
down regulation of plasma membrane Ca-ATPase
down regulation of sarco(endo)plasmic reticulum Ca2+-ATPase
down regulation of sarcoplasmic reticulum ATPase
down-regulation of calcium ABC transporter
down-regulation of calcium efflux ATPase
down-regulation of calcium-translocating P-type ATPase activity
down-regulation of plasma membrane Ca-ATPase
down-regulation of sarco(endo)plasmic reticulum Ca2+-ATPase
down-regulation of sarcoplasmic reticulum ATPase
downregulation of calcium ABC transporter
downregulation of calcium-translocating P-type ATPase activity
downregulation of plasma membrane Ca-ATPase
downregulation of sarco(endo)plasmic reticulum Ca2+-ATPase
downregulation of sarcoplasmic reticulum ATPase
inhibition of calcium-translocating P-type ATPase activity
inhibition of calcium-transporting ATPase activity
inhibition of sarco(endo)plasmic reticulum Ca2+-ATPase
inhibition of sarcoplasmic reticulum ATPase
negative regulation of calcium ABC transporter
negative regulation of calcium efflux ATPase
negative regulation of calcium-translocating P-type ATPase activity
negative regulation of plasma membrane Ca-ATPase
negative regulation of sarco(endo)plasmic reticulum Ca2+-ATPase
negative regulation of sarcoplasmic reticulum ATPase
negative regulation of ATPase-coupled calcium transmembrane transporter activity
Any process that activates or increases the frequency, rate or extent of an ATPase-coupled calcium transmembrane transporter activity.
activation of ATP phosphohydrolase (Ca2+-transporting)
activation of Ca(2+)-transporting ATPase activity
activation of Ca2+-pumping ATPase activity
activation of Ca2+-transporting ATPase activity
activation of calcium transporting ATPase activity
positive regulation of ATP phosphohydrolase (Ca2+-transporting)
positive regulation of Ca(2+)-transporting ATPase activity
positive regulation of Ca2+-pumping ATPase activity
positive regulation of Ca2+-transporting ATPase activity
positive regulation of calcium transporting ATPase activity
positive regulation of calcium-transporting ATPase activity
up regulation of ATP phosphohydrolase (Ca2+-transporting)
up regulation of Ca(2+)-transporting ATPase activity
up regulation of Ca2+-pumping ATPase activity
up regulation of Ca2+-transporting ATPase activity
up regulation of calcium transporting ATPase activity
up regulation of calcium-transporting ATPase activity
up-regulation of ATP phosphohydrolase (Ca2+-transporting)
up-regulation of Ca(2+)-transporting ATPase activity
up-regulation of Ca2+-pumping ATPase activity
up-regulation of Ca2+-transporting ATPase activity
up-regulation of calcium transporting ATPase activity
up-regulation of calcium-transporting ATPase activity
upregulation of ATP phosphohydrolase (Ca2+-transporting)
upregulation of Ca(2+)-transporting ATPase activity
upregulation of Ca2+-pumping ATPase activity
upregulation of Ca2+-transporting ATPase activity
upregulation of calcium transporting ATPase activity
upregulation of calcium-transporting ATPase activity
activation of calcium-translocating P-type ATPase activity
activation of calcium-transporting ATPase activity
activation of sarco(endo)plasmic reticulum Ca2+-ATPase
activation of sarcoplasmic reticulum ATPase
positive regulation of calcium ABC transporter
positive regulation of calcium efflux ATPase
positive regulation of calcium-translocating P-type ATPase activity
positive regulation of plasma membrane Ca-ATPase
positive regulation of sarco(endo)plasmic reticulum Ca2+-ATPase
positive regulation of sarcoplasmic reticulum ATPase
up regulation of calcium ABC transporter
up regulation of calcium-translocating P-type ATPase activity
up regulation of plasma membrane Ca-ATPase
up regulation of sarco(endo)plasmic reticulum Ca2+-ATPase
up regulation of sarcoplasmic reticulum ATPase
up-regulation of calcium ABC transporter
up-regulation of calcium-translocating P-type ATPase activity
up-regulation of plasma membrane Ca-ATPase
up-regulation of sarco(endo)plasmic reticulum Ca2+-ATPase
up-regulation of sarcoplasmic reticulum ATPase
upregulation of calcium-translocating P-type ATPase activity
upregulation of plasma membrane Ca-ATPase
upregulation of sarco(endo)plasmic reticulum Ca2+-ATPase
upregulation of sarcoplasmic reticulum ATPase
positive regulation of ATPase-coupled calcium transmembrane transporter activity
Any process that modulates the frequency, rate or extent of protein localization to cell division site.
regulation of protein localisation to cell division site
regulation of protein localization to cell division site
Any regulation of protein localization to cell division site that is involved in cytokinesis.
regulation of protein localisation to cell division site involved in cytokinesis
regulation of protein localization to cell division site involved in cytokinesis
Any protein kinase activity that is involved in regulation of protein localization to cell division site involved in cytokinesis.
protein kinase activity involved in regulation of protein localisation to cell division site involved in cytokinesis
protamine kinase activity involved in regulation of protein localisation to cell division site involved in cytokinesis
protamine kinase activity involved in regulation of protein localization to cell division site involved in cytokinesis
protein kinase activity involved in regulation of protein localization to cell division site involved in cytokinesis
Interacting selectively and non-covalently with proline.
Any process that modulates the frequency, rate or extent of inward rectifier potassium channel activity.
regulation of inward rectifier potassium channel activity
Any process that activates or increases the frequency, rate or extent of inward rectifier potassium channel activity.
positive regulation of Kir channel activity
up regulation of inward rectifier potassium channel activity
up-regulation of inward rectifier potassium channel activity
upregulation of inward rectifier potassium channel activity
activation of inward rectifier potassium channel activity
positive regulation of inward rectifier potassium channel activity
Interacting selectively and non-covalently with phosphatidylinositol phosphate.
Interacting selectively and non-covalently with maltose.
The directed movement of nitrate into a cell or organelle.
Interacting selectively and non-covalently with (25S)-Delta(4)-dafachronate.
Interacting selectively and non-covalently with (25S)-Delta(7)-dafachronate.
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.
Any process that modulates the frequency, rate or extent of calcium ion import into sarcoplasmic reticulum.
regulation of calcium ion import into sarcoplasmic reticulum
Any process that stops, prevents or reduces the frequency, rate or extent of calcium ion import into sarcoplasmic reticulum.
down regulation of calcium ion import into sarcoplasmic reticulum
down-regulation of calcium ion import into sarcoplasmic reticulum
downregulation of calcium ion import into sarcoplasmic reticulum
inhibition of calcium ion import into sarcoplasmic reticulum
negative regulation of calcium ion import into sarcoplasmic reticulum
Any process that activates or increases the frequency, rate or extent of calcium ion import into sarcoplasmic reticulum.
up regulation of calcium ion import into sarcoplasmic reticulum
up-regulation of calcium ion import into sarcoplasmic reticulum
upregulation of calcium ion import into sarcoplasmic reticulum
activation of calcium ion import into sarcoplasmic reticulum
positive regulation of calcium ion import into sarcoplasmic reticulum
Interacting selectively and non-covalently with calcitriol. Calcitriol (1,25-dihydroxycholecalciferol) is the hormonally active form of vitamin D3.
1alpha,25-dihydroxycholecalciferol binding
Interacting selectively and non-covalently with calcidiol.
Interacting selectively and non-covalently with lithocholic acid.
Interacting selectively and non-covalently with chenodeoxycholic acid.
Any process that modulates the frequency, rate or extent of cyclic nucleotide-gated ion channel activity.
regulation of cyclic nucleotide activated ion channel activity
regulation of cyclic nucleotide gated ion channel activity
regulation of cyclic nucleotide-activated ion channel activity
regulation of cyclic nucleotide-gated ion channel activity
Any process that stops, prevents or reduces the frequency, rate or extent of cyclic nucleotide-gated ion channel activity.
down regulation of cyclic nucleotide activated ion channel activity
down regulation of cyclic nucleotide gated ion channel activity
down regulation of cyclic nucleotide-activated ion channel activity
down regulation of cyclic nucleotide-gated ion channel activity
down-regulation of cyclic nucleotide activated ion channel activity
down-regulation of cyclic nucleotide gated ion channel activity
down-regulation of cyclic nucleotide-activated ion channel activity
down-regulation of cyclic nucleotide-gated ion channel activity
downregulation of cyclic nucleotide activated ion channel activity
downregulation of cyclic nucleotide gated ion channel activity
downregulation of cyclic nucleotide-activated ion channel activity
downregulation of cyclic nucleotide-gated ion channel activity
inhibition of cyclic nucleotide activated ion channel activity
inhibition of cyclic nucleotide gated ion channel activity
inhibition of cyclic nucleotide-activated ion channel activity
negative regulation of cyclic nucleotide activated ion channel activity
negative regulation of cyclic nucleotide gated ion channel activity
negative regulation of cyclic nucleotide-activated ion channel activity
inhibition of cyclic nucleotide-gated ion channel activity
negative regulation of cyclic nucleotide-gated ion channel activity
Any process that activates or increases the frequency, rate or extent of cyclic nucleotide-gated ion channel activity.
activation of cyclic nucleotide activated ion channel activity
activation of cyclic nucleotide gated ion channel activity
activation of cyclic nucleotide-activated ion channel activity
positive regulation of cyclic nucleotide activated ion channel activity
positive regulation of cyclic nucleotide gated ion channel activity
positive regulation of cyclic nucleotide-activated ion channel activity
up regulation of cyclic nucleotide activated ion channel activity
up regulation of cyclic nucleotide gated ion channel activity
up regulation of cyclic nucleotide-activated ion channel activity
up regulation of cyclic nucleotide-gated ion channel activity
up-regulation of cyclic nucleotide activated ion channel activity
up-regulation of cyclic nucleotide gated ion channel activity
up-regulation of cyclic nucleotide-activated ion channel activity
up-regulation of cyclic nucleotide-gated ion channel activity
upregulation of cyclic nucleotide activated ion channel activity
upregulation of cyclic nucleotide gated ion channel activity
upregulation of cyclic nucleotide-activated ion channel activity
upregulation of cyclic nucleotide-gated ion channel activity
activation of cyclic nucleotide-gated ion channel activity
positive regulation of cyclic nucleotide-gated ion channel activity
Interacting selectively and non-covalently with 5-O-phosphono-alpha-D-ribofuranosyl diphosphate.
5-O-phosphono-alpha-D-ribofuranosyl diphosphate binding
Interacting selectively and non-covalently with IMP, inosine monophosphate.
Any process that modulates the frequency, rate or extent of delayed rectifier potassium channel activity.
regulation of delayed rectifier potassium channel activity
Any process that stops, prevents or reduces the frequency, rate or extent of delayed rectifier potassium channel activity.
down regulation of delayed rectifier potassium channel activity
down-regulation of delayed rectifier potassium channel activity
downregulation of delayed rectifier potassium channel activity
inhibition of delayed rectifier potassium channel activity
negative regulation of delayed rectifier potassium channel activity
Any process that activates or increases the frequency, rate or extent of delayed rectifier potassium channel activity.
up regulation of delayed rectifier potassium channel activity
up-regulation of delayed rectifier potassium channel activity
upregulation of delayed rectifier potassium channel activity
activation of delayed rectifier potassium channel activity
positive regulation of delayed rectifier potassium channel activity
Any process that modulates the frequency, rate or extent of polyamine transmembrane transport.
regulation of polyamine transmembrane transport
Any process that stops, prevents or reduces the frequency, rate or extent of polyamine transmembrane transport.
down regulation of polyamine transmembrane transport
down-regulation of polyamine transmembrane transport
downregulation of polyamine transmembrane transport
inhibition of polyamine transmembrane transport
negative regulation of polyamine transmembrane transport
Any process that activates or increases the frequency, rate or extent of polyamine transmembrane transport.
up regulation of polyamine transmembrane transport
up-regulation of polyamine transmembrane transport
upregulation of polyamine transmembrane transport
activation of polyamine transmembrane transport
positive regulation of polyamine transmembrane transport
Interacting selectively and non-covalently with D3 vitamins.
Any process that modulates the frequency, rate or extent of sodium ion transmembrane transport.
regulation of sodium ion membrane transport
regulation of sodium ion transmembrane transport
Any process that stops, prevents or reduces the frequency, rate or extent of sodium ion transmembrane transport.
down regulation of sodium ion membrane transport
down regulation of sodium ion transmembrane transport
down-regulation of sodium ion membrane transport
down-regulation of sodium ion transmembrane transport
downregulation of sodium ion membrane transport
downregulation of sodium ion transmembrane transport
negative regulation of sodium ion membrane transport
inhibition of sodium ion membrane transport
inhibition of sodium ion transmembrane transport
negative regulation of sodium ion transmembrane transport
Any process that activates or increases the frequency, rate or extent of sodium ion transmembrane transport.
positive regulation of sodium ion membrane transport
up regulation of sodium ion membrane transport
up regulation of sodium ion transmembrane transport
up-regulation of sodium ion membrane transport
up-regulation of sodium ion transmembrane transport
upregulation of sodium ion membrane transport
upregulation of sodium ion transmembrane transport
activation of sodium ion membrane transport
activation of sodium ion transmembrane transport
positive regulation of sodium ion transmembrane transport
Any process that modulates the frequency, rate or extent of copper ion transmembrane transport.
regulation of copper cation transmembrane transport
regulation of copper ion membrane transport
regulation of copper ion transmembrane transport
Any process that stops, prevents or reduces the frequency, rate or extent of copper ion transmembrane transport.
down regulation of copper cation transmembrane transport
down regulation of copper ion membrane transport
down regulation of copper ion transmembrane transport
down-regulation of copper cation transmembrane transport
down-regulation of copper ion membrane transport
down-regulation of copper ion transmembrane transport
downregulation of copper cation transmembrane transport
downregulation of copper ion membrane transport
downregulation of copper ion transmembrane transport
negative regulation of copper cation transmembrane transport
negative regulation of copper ion membrane transport
inhibition of copper cation transmembrane transport
inhibition of copper ion membrane transport
inhibition of copper ion transmembrane transport
negative regulation of copper ion transmembrane transport
Any process that activates or increases the frequency, rate or extent of copper ion transmembrane transport.
positive regulation of copper cation transmembrane transport
positive regulation of copper ion membrane transport
up regulation of copper cation transmembrane transport
up regulation of copper ion membrane transport
up regulation of copper ion transmembrane transport
up-regulation of copper cation transmembrane transport
up-regulation of copper ion membrane transport
up-regulation of copper ion transmembrane transport
upregulation of copper cation transmembrane transport
upregulation of copper ion membrane transport
upregulation of copper ion transmembrane transport
activation of copper cation transmembrane transport
activation of copper ion membrane transport
activation of copper ion transmembrane transport
positive regulation of copper ion transmembrane transport
Interacting selectively and non-covalently with hydroquinone.
Any blood vessel endothelial cell delamination that is involved in blood vessel lumen ensheathment.
blood vessel endothelial cell delamination involved in blood vessel lumen ensheathment
Any process that modulates the frequency, rate or extent of protein localization to spindle pole body.
regulation of protein localisation to spindle pole body
regulation of protein localization to spindle pole body
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to spindle pole body.
down regulation of protein localisation to spindle pole body
down regulation of protein localization to spindle pole body
down-regulation of protein localisation to spindle pole body
down-regulation of protein localization to spindle pole body
downregulation of protein localisation to spindle pole body
downregulation of protein localization to spindle pole body
negative regulation of protein localisation to spindle pole body
inhibition of protein localisation to spindle pole body
inhibition of protein localization to spindle pole body
negative regulation of protein localization to spindle pole body
Any process that activates or increases the frequency, rate or extent of protein localization to spindle pole body.
positive regulation of protein localisation to spindle pole body
up regulation of protein localisation to spindle pole body
up regulation of protein localization to spindle pole body
up-regulation of protein localisation to spindle pole body
up-regulation of protein localization to spindle pole body
upregulation of protein localisation to spindle pole body
upregulation of protein localization to spindle pole body
activation of protein localisation to spindle pole body
activation of protein localization to spindle pole body
positive regulation of protein localization to spindle pole body
Any chemoattractant activity that is involved in axon guidance.
chemoattractant activity involved in axon pathfinding
chemoattractant activity involved in axon growth cone guidance
chemoattractant activity involved in axon chemotaxis
chemoattractant activity involved in axon guidance
Interacting selectively and non-covalently with ceramide 1-phosphate.
Any detection of stimulus that is involved in meiotic spindle checkpoint.
stimulus detection involved in meiotic spindle checkpoint
perception of stimulus involved in meiotic spindle checkpoint
stimulus sensing involved in meiotic spindle checkpoint
detection of stimulus involved in meiotic spindle checkpoint
Any detection of stimulus that is involved in G1 DNA damage checkpoint.
detection of stimulus involved in G1/S DNA damage checkpoint
stimulus detection involved in G1 DNA damage checkpoint
stimulus detection involved in G1/S DNA damage checkpoint
perception of stimulus involved in G1 DNA damage checkpoint
perception of stimulus involved in G1/S DNA damage checkpoint
stimulus sensing involved in G1 DNA damage checkpoint
stimulus sensing involved in G1/S DNA damage checkpoint
detection of stimulus involved in G1 DNA damage checkpoint
Any process that modulates the frequency, rate or extent of water channel activity.
Any process that stops, prevents or reduces the frequency, rate or extent of water channel activity.
down regulation of water channel activity
down-regulation of water channel activity
downregulation of water channel activity
negative regulation of water channel activity
Any process that activates or increases the frequency, rate or extent of water channel activity.
positive regulation of water channel activity
Any positive regulation of water channel activity that is involved in maintenance of lens transparency.
positive regulation of water channel activity involved in maintenance of ocular lens transparency
positive regulation of water channel activity involved in preservation of lens transparency
up regulation of water channel activity involved in maintenance of lens transparency
up regulation of water channel activity involved in maintenance of ocular lens transparency
up regulation of water channel activity involved in preservation of lens transparency
up-regulation of water channel activity involved in maintenance of lens transparency
up-regulation of water channel activity involved in maintenance of ocular lens transparency
up-regulation of water channel activity involved in preservation of lens transparency
upregulation of water channel activity involved in maintenance of lens transparency
upregulation of water channel activity involved in maintenance of ocular lens transparency
upregulation of water channel activity involved in preservation of lens transparency
activation of aquaporin involved in maintenance of lens transparency
activation of aquaporin involved in maintenance of ocular lens transparency
activation of aquaporin involved in preservation of lens transparency
activation of water channel activity involved in maintenance of lens transparency
activation of water channel activity involved in maintenance of ocular lens transparency
activation of water channel activity involved in preservation of lens transparency
aquaporin activation involved in maintenance of lens transparency
aquaporin activation involved in maintenance of ocular lens transparency
aquaporin activation involved in preservation of lens transparency
positive regulation of aquaporin involved in maintenance of lens transparency
positive regulation of aquaporin involved in maintenance of ocular lens transparency
positive regulation of aquaporin involved in preservation of lens transparency
up regulation of aquaporin involved in maintenance of lens transparency
up regulation of aquaporin involved in maintenance of ocular lens transparency
up regulation of aquaporin involved in preservation of lens transparency
up-regulation of aquaporin involved in maintenance of lens transparency
up-regulation of aquaporin involved in maintenance of ocular lens transparency
up-regulation of aquaporin involved in preservation of lens transparency
upregulation of aquaporin involved in maintenance of lens transparency
upregulation of aquaporin involved in maintenance of ocular lens transparency
upregulation of aquaporin involved in preservation of lens transparency
positive regulation of water channel activity involved in maintenance of lens transparency
Interacting selectively and non-covalently with riboflavin.
Any process that modulates the frequency, rate or extent of mesenchymal stem cell proliferation.
regulation of mesenchymal stem cell proliferation
Any process that stops, prevents or reduces the frequency, rate or extent of mesenchymal stem cell proliferation.
down regulation of mesenchymal stem cell proliferation
down-regulation of mesenchymal stem cell proliferation
downregulation of mesenchymal stem cell proliferation
negative regulation of MSC proliferation
inhibition of mesenchymal stem cell proliferation
negative regulation of mesenchymal stem cell proliferation
Any process that activates or increases the frequency, rate or extent of mesenchymal stem cell proliferation.
positive regulation of MSC proliferation
up regulation of mesenchymal stem cell proliferation
up-regulation of mesenchymal stem cell proliferation
upregulation of mesenchymal stem cell proliferation
activation of mesenchymal stem cell proliferation
positive regulation of mesenchymal stem cell proliferation
Any process that modulates the frequency, rate or extent of protein localization to synapse.
regulation of protein localisation to synapse
regulation of protein localization to synapse
Any process that activates or increases the frequency, rate or extent of protein localization to synapse.
positive regulation of protein localisation to synapse
up regulation of protein localisation to synapse
up regulation of protein localization to synapse
up-regulation of protein localisation to synapse
up-regulation of protein localization to synapse
upregulation of protein localisation to synapse
upregulation of protein localization to synapse
activation of protein localisation to synapse
activation of protein localization to synapse
positive regulation of protein localization to synapse
Interacting selectively and non-covalently with L-cysteine.
Any protein binding that is involved in negative regulation of telomere maintenance via telomerase.
protein binding involved in down regulation of telomere maintenance via telomerase activity
protein binding involved in down-regulation of telomere maintenance via telomerase activity
protein binding involved in downregulation of telomere maintenance via telomerase activity
protein binding involved in inhibition of telomere maintenance via telomerase
protein binding involved in negative regulation of telomere maintenance via telomerase
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.
Any process that modulates the frequency, rate or extent of generation of calcium ion transmembrane transport via high voltage-gated calcium channel.
regulation of generation of L-type calcium current
regulation of calcium ion transmembrane transport via high voltage-gated calcium channel
Interacting selectively and non-covalently with sn-glycerol 3-phosphate.
An example of this is UgpB in E. coli [P0AG80] - see PMID:23013274.
Any process that modulates the frequency, rate or extent of intracellular signal transduction.
regulation of intracellular signaling cascade
regulation of intracellular signaling chain
regulation of intracellular protein kinase cascade
regulation of intracellular signal transduction pathway
regulation of signal transmission via intracellular cascade
regulation of intracellular signaling pathway
regulation of signal transduction via intracellular signaling cascade
regulation of intracellular signal transduction
Any process that modulates the frequency, rate or extent of protein localization to mitotic spindle pole body.
regulation of protein localisation to mitotic spindle pole body
regulation of protein localization to mitotic spindle pole body
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to mitotic spindle pole body.
down regulation of protein localisation to mitotic spindle pole body
down regulation of protein localization to mitotic spindle pole body
down-regulation of protein localisation in mitotic spindle pole body
down-regulation of protein localisation to mitotic spindle pole body
down-regulation of protein localization to mitotic spindle pole body
downregulation of protein localisation to mitotic spindle pole body
downregulation of protein localization to mitotic spindle pole body
negative regulation of protein localisation to mitotic spindle pole body
inhibition of protein localisation to mitotic spindle pole body
inhibition of protein localization to mitotic spindle pole body
negative regulation of protein localization to mitotic spindle pole body
The directed movement of a proton across a membrane.
passive proton transport, down the electrochemical gradient
The directed movement of silver ion across a membrane.
The process in which an aluminium ion is transported across a membrane.
Any process that modulates the frequency, rate or extent of large conductance calcium-activated potassium channel activity.
regulation of BK calcium-activated potassium channel activity
regulation of large conductance KCa channels
regulation of large conductance calcium-activated potassium channel activity
Any process that stops, prevents or reduces the frequency, rate or extent of large conductance calcium-activated potassium channel activity.
down regulation of BK calcium-activated potassium channel activity
down regulation of large conductance KCa channels
down regulation of large conductance calcium-activated potassium channel activity
down-regulation of BK calcium-activated potassium channel activity
down-regulation of large conductance KCa channels
down-regulation of large conductance calcium-activated potassium channel activity
downregulation of BK calcium-activated potassium channel activity
downregulation of large conductance KCa channels
downregulation of large conductance calcium-activated potassium channel activity
negative regulation of BK calcium-activated potassium channel activity
negative regulation of large conductance KCa channels
inhibition of BK calcium-activated potassium channel activity
inhibition of large conductance KCa channels
inhibition of large conductance calcium-activated potassium channel activity
negative regulation of BK channel activity
negative regulation of large conductance calcium-activated potassium channel activity
Any process that activates or increases the frequency, rate or extent of large conductance calcium-activated potassium channel activity.
positive regulation of BK calcium-activated potassium channel activity
positive regulation of large conductance KCa channels
up regulation of BK calcium-activated potassium channel activity
up regulation of large conductance KCa channels
up regulation of large conductance calcium-activated potassium channel activity
up-regulation of BK calcium-activated potassium channel activity
up-regulation of large conductance KCa channels
up-regulation of large conductance calcium-activated potassium channel activity
upregulation of BK calcium-activated potassium channel activity
upregulation of large conductance KCa channels
upregulation of large conductance calcium-activated potassium channel activity
activation of BK calcium-activated potassium channel activity
activation of large conductance KCa channels
activation of large conductance calcium-activated potassium channel activity
positive regulation of BK channel activity
positive regulation of large conductance calcium-activated potassium channel activity
The directed movement of calcium ion into a cytosol.
Interacting selectively and non-covalently with carbon dioxide.
Any process that modulates the frequency, rate or extent of receptor localization to synapse.
regulation of receptor localisation to synapse
regulation of receptor localization to synapse
Any process that stops, prevents or reduces the frequency, rate or extent of receptor localization to synapse.
down regulation of receptor localisation to synapse
down regulation of receptor localization to synapse
down-regulation of receptor localisation to synapse
down-regulation of receptor localization to synapse
downregulation of receptor localisation to synapse
downregulation of receptor localization to synapse
negative regulation of receptor localisation to synapse
inhibition of receptor localisation to synapse
inhibition of receptor localization to synapse
negative regulation of receptor localization to synapse
Any process that activates or increases the frequency, rate or extent of receptor localization to synapse.
positive regulation of receptor localisation to synapse
up regulation of receptor localisation to synapse
up regulation of receptor localization to synapse
up-regulation of receptor localisation to synapse
up-regulation of receptor localization to synapse
upregulation of receptor localisation to synapse
upregulation of receptor localization to synapse
activation of receptor localisation to synapse
activation of receptor localization to synapse
positive regulation of receptor localization to synapse
Any process that stops, prevents or reduces the frequency, rate or extent of satellite cell proliferation.
down regulation of satellite cell proliferation
down-regulation of satellite cell proliferation
downregulation of satellite cell proliferation
inhibition of satellite cell proliferation
negative regulation of skeletal muscle satellite cell proliferation
Any process that activates or increases the frequency, rate or extent of skeletal muscle satellite cell proliferation.
up regulation of satellite cell proliferation
up-regulation of satellite cell proliferation
upregulation of satellite cell proliferation
activation of satellite cell proliferation
positive regulation of skeletal muscle satellite cell proliferation
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.
negative regulation of growth factor dependent skeletal muscle satellite cell proliferation
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.
positive regulation of growth factor dependent skeletal muscle satellite cell proliferation
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.
down regulation of cartilage cell proliferation
down regulation of chondrocyte cell proliferation
down regulation of chondrocyte proliferation
down-regulation of cartilage cell proliferation
down-regulation of chondrocyte cell proliferation
down-regulation of chondrocyte proliferation
downregulation of cartilage cell proliferation
downregulation of chondrocyte cell proliferation
downregulation of chondrocyte proliferation
negative regulation of cartilage cell proliferation
negative regulation of chondrocyte cell proliferation
inhibition of cartilage cell proliferation
inhibition of chondrocyte cell proliferation
negative regulation of chondrocyte proliferation
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.
positive regulation of cartilage cell proliferation
positive regulation of chondrocyte cell proliferation
up regulation of cartilage cell proliferation
up regulation of chondrocyte cell proliferation
up regulation of chondrocyte proliferation
up-regulation of cartilage cell proliferation
up-regulation of chondrocyte cell proliferation
up-regulation of chondrocyte proliferation
upregulation of cartilage cell proliferation
upregulation of chondrocyte cell proliferation
upregulation of chondrocyte proliferation
activation of cartilage cell proliferation
activation of chondrocyte cell proliferation
positive regulation of chondrocyte proliferation
Any process that modulates the frequency, rate or extent of protein localization to microtubule.
regulation of protein localisation to microtubule
regulation of protein localization to microtubule
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to microtubule.
down regulation of protein localisation to microtubule
down regulation of protein localization to microtubule
down-regulation of protein localisation to microtubule
down-regulation of protein localization to microtubule
downregulation of protein localisation to microtubule
downregulation of protein localization to microtubule
negative regulation of protein localisation to microtubule
inhibition of protein localisation to microtubule
inhibition of protein localization to microtubule
negative regulation of protein localization to microtubule
Any process that stops, prevents or reduces the frequency, rate or extent of cell proliferation in dorsal spinal cord.
down regulation of cell proliferation in dorsal spinal cord
down-regulation of cell proliferation in dorsal spinal cord
downregulation of cell proliferation in dorsal spinal cord
inhibition of cell proliferation in dorsal spinal cord
negative regulation of cell proliferation in dorsal spinal cord
Any process that activates or increases the frequency, rate or extent of cell proliferation in dorsal spinal cord.
up regulation of cell proliferation in dorsal spinal cord
up-regulation of cell proliferation in dorsal spinal cord
upregulation of cell proliferation in dorsal spinal cord
activation of cell proliferation in dorsal spinal cord
positive regulation of cell proliferation in dorsal spinal cord
Interacting selectively and non-covalently with phosphatidylinositol bisphosphate.
An example of this is KCNJ2 in human (P63252) in PMID:18690034 (inferred from direct assay)
phosphatidylinositol bisphosphate binding
Any process that modulates the frequency, rate or extent of intracellular calcium activated chloride channel activity.
regulation of intracellular calcium activated chloride channel activity
Any process that stops, prevents or reduces the frequency, rate or extent of intracellular calcium activated chloride channel activity.
down regulation of intracellular calcium activated chloride channel activity
down-regulation of intracellular calcium activated chloride channel activity
downregulation of intracellular calcium activated chloride channel activity
inhibition of intracellular calcium activated chloride channel activity
negative regulation of intracellular calcium activated chloride channel activity
Any process that activates or increases the frequency, rate or extent of intracellular calcium activated chloride channel activity.
up regulation of intracellular calcium activated chloride channel activity
up-regulation of intracellular calcium activated chloride channel activity
upregulation of intracellular calcium activated chloride channel activity
activation of intracellular calcium activated chloride channel activity
positive regulation of intracellular calcium activated chloride channel activity
Any process that modulates the frequency, rate or extent of voltage-gated chloride channel activity.
regulation of voltage gated chloride channel activity
regulation of voltage-dependent chloride channel activity
regulation of voltage-gated chloride channel activity
Any process that stops, prevents or reduces the frequency, rate or extent of voltage-gated chloride channel activity.
down regulation of voltage gated chloride channel activity
down regulation of voltage-dependent chloride channel activity
down regulation of voltage-gated chloride channel activity
down-regulation of voltage gated chloride channel activity
down-regulation of voltage-dependent chloride channel activity
down-regulation of voltage-gated chloride channel activity
downregulation of voltage gated chloride channel activity
downregulation of voltage-dependent chloride channel activity
downregulation of voltage-gated chloride channel activity
negative regulation of voltage gated chloride channel activity
negative regulation of voltage-dependent chloride channel activity
inhibition of voltage gated chloride channel activity
inhibition of voltage-dependent chloride channel activity
inhibition of voltage-gated chloride channel activity
negative regulation of voltage-gated chloride channel activity
Any process that activates or increases the frequency, rate or extent of voltage-gated chloride channel activity.
positive regulation of voltage gated chloride channel activity
positive regulation of voltage-dependent chloride channel activity
up regulation of voltage gated chloride channel activity
up regulation of voltage-dependent chloride channel activity
up regulation of voltage-gated chloride channel activity
up-regulation of voltage gated chloride channel activity
up-regulation of voltage-dependent chloride channel activity
up-regulation of voltage-gated chloride channel activity
upregulation of voltage gated chloride channel activity
upregulation of voltage-dependent chloride channel activity
upregulation of voltage-gated chloride channel activity
activation of voltage gated chloride channel activity
activation of voltage-dependent chloride channel activity
activation of voltage-gated chloride channel activity
positive regulation of voltage-gated chloride channel activity
Any process that modulates the frequency, rate or extent of protein localization to early endosome.
regulation of protein localisation in early endosome
regulation of protein localisation to early endosome
regulation of protein localization in early endosome
regulation of protein localization to early endosome
Any process that activates or increases the frequency, rate or extent of protein localization to early endosome.
positive regulation of protein localisation in early endosome
positive regulation of protein localisation to early endosome
positive regulation of protein localization in early endosome
up regulation of protein localisation in early endosome
up regulation of protein localisation to early endosome
up regulation of protein localization in early endosome
up regulation of protein localization to early endosome
up-regulation of protein localisation in early endosome
up-regulation of protein localisation to early endosome
up-regulation of protein localization in early endosome
up-regulation of protein localization to early endosome
upregulation of protein localisation in early endosome
upregulation of protein localisation to early endosome
upregulation of protein localization in early endosome
upregulation of protein localization to early endosome
activation of protein localisation in early endosome
activation of protein localisation to early endosome
activation of protein localization in early endosome
activation of protein localization to early endosome
positive regulation of protein localization to early endosome
Any process that modulates the frequency, rate or extent of leukocyte cell-cell adhesion.
Exogenous expression of ASS1 or NOS3 in HUVECs enhances NO production and inhibits monocyte adhesion
regulation of leukocyte cell-cell adhesion
Any process that stops, prevents or reduces the frequency, rate or extent of leukocyte cell-cell adhesion.
down regulation of leukocyte cell adhesion
down regulation of leukocyte cell-cell adhesion
down-regulation of leukocyte cell adhesion
down-regulation of leukocyte cell-cell adhesion
downregulation of leukocyte cell adhesion
downregulation of leukocyte cell-cell adhesion
negative regulation of leukocyte adhesion
negative regulation of leukocyte cell adhesion
inhibition of leukocyte cell-cell adhesion
negative regulation of leukocyte cell-cell adhesion
Any process that activates or increases the frequency, rate or extent of leukocyte cell-cell adhesion.
positive regulation of leukocyte adhesion
positive regulation of leukocyte cell adhesion
up regulation of leukocyte cell adhesion
up regulation of leukocyte cell-cell adhesion
up-regulation of leukocyte cell adhesion
up-regulation of leukocyte cell-cell adhesion
upregulation of leukocyte cell-cell adhesion
activation of leukocyte cell-cell adhesion
positive regulation of leukocyte cell-cell adhesion
Any process that modulates the frequency, rate or extent of protein localization to cell tip.
regulation of protein localisation to cell tip
regulation of protein localization to cell tip
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to cell tip.
down regulation of protein localisation to cell tip
down regulation of protein localization to cell tip
down-regulation of protein localisation to cell tip
down-regulation of protein localization to cell tip
downregulation of protein localisation to cell tip
downregulation of protein localization to cell tip
negative regulation of protein localisation to cell tip
inhibition of protein localisation to cell tip
inhibition of protein localization to cell tip
negative regulation of protein localization to cell tip
Any process that activates or increases the frequency, rate or extent of protein localization to cell tip.
positive regulation of protein localisation to cell tip
up regulation of protein localisation to cell tip
up regulation of protein localization to cell tip
up-regulation of protein localisation to cell tip
up-regulation of protein localization to cell tip
upregulation of protein localisation to cell tip
upregulation of protein localization to cell tip
activation of protein localisation to cell tip
activation of protein localization to cell tip
positive regulation of protein localization to cell tip
Any process that modulates the frequency, rate or extent of protein localization to plasma membrane.
regulation of protein localization in plasma membrane
regulation of establishment of protein localisation in plasma membrane
regulation of establishment of protein localization in plasma membrane
regulation of establishment of protein localization to plasma membrane
regulation of protein localisation in plasma membrane
regulation of protein targeting to plasma membrane
regulation of protein-plasma membrane targeting
regulation of protein localization to plasma membrane
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to plasma membrane.
down regulation of protein localisation in plasma membrane
down regulation of protein localization in plasma membrane
down regulation of protein localization to plasma membrane
down-regulation of protein localisation in plasma membrane
down-regulation of protein localization in plasma membrane
down-regulation of protein localization to plasma membrane
downregulation of protein localisation in plasma membrane
downregulation of protein localization in plasma membrane
downregulation of protein localization to plasma membrane
negative regulation of protein localization in plasma membrane
inhibition of protein localisation in plasma membrane
inhibition of protein localization in plasma membrane
inhibition of protein localization to plasma membrane
inhibition of protein targeting to plasma membrane
inhibition of protein-plasma membrane targeting
down regulation of protein targeting to plasma membrane
down regulation of protein-plasma membrane targeting
down-regulation of protein targeting to plasma membrane
down-regulation of protein-plasma membrane targeting
downregulation of protein targeting to plasma membrane
downregulation of protein-plasma membrane targeting
negative regulation of establishment of protein localisation in plasma membrane
negative regulation of establishment of protein localization in plasma membrane
negative regulation of establishment of protein localization to plasma membrane
negative regulation of protein localisation in plasma membrane
negative regulation of protein targeting to plasma membrane
negative regulation of protein-plasma membrane targeting
negative regulation of protein localization to plasma membrane
Any process that activates or increases the frequency, rate or extent of protein localization to plasma membrane.
positive regulation of protein localisation in plasma membrane
positive regulation of protein localization in plasma membrane
up regulation of protein localisation in plasma membrane
up regulation of protein localization in plasma membrane
up regulation of protein localization to plasma membrane
up-regulation of protein localisation in plasma membrane
up-regulation of protein localization in plasma membrane
up-regulation of protein localization to plasma membrane
upregulation of protein localisation in plasma membrane
upregulation of protein localization in plasma membrane
upregulation of protein localization to plasma membrane
activation of protein localisation in plasma membrane
activation of protein localization in plasma membrane
activation of protein localization to plasma membrane
activation of protein targeting to plasma membrane
activation of protein-plasma membrane targeting
positive regulation of establishment of protein localisation in plasma membrane
positive regulation of establishment of protein localization to plasma membrane
positive regulation of protein targeting to plasma membrane
positive regulation of protein-plasma membrane targeting
up regulation of protein targeting to plasma membrane
up regulation of protein-plasma membrane targeting
up-regulation of protein targeting to plasma membrane
up-regulation of protein-plasma membrane targeting
upregulation of protein targeting to plasma membrane
upregulation of protein-plasma membrane targeting
positive regulation of protein localization to plasma membrane
Interacting selectively and non-covalently with cupric ion, copper(2+).
Interacting selectively and non-covalently with cuprous ion, copper(1+).
Any process that modulates the frequency, rate or extent of calcium ion transmembrane transport.
regulation of calcium ion membrane transport
regulation of transmembrane calcium transport
human HRC regulates RYR2 and thus regulates transmembrane transport of calcium from SR to cytosol
regulation of calcium ion transmembrane transport
Any process that stops, prevents or reduces the frequency, rate or extent of calcium ion transmembrane transport.
down regulation of calcium ion membrane transport
down regulation of calcium ion transmembrane transport
down regulation of transmembrane calcium transport
down-regulation of calcium ion membrane transport
down-regulation of calcium ion transmembrane transport
down-regulation of transmembrane calcium transport
downregulation of calcium ion membrane transport
downregulation of calcium ion transmembrane transport
downregulation of transmembrane calcium transport
negative regulation of calcium ion membrane transport
negative regulation of transmembrane calcium transport
inhibition of calcium ion membrane transport
inhibition of calcium ion transmembrane transport
inhibition of transmembrane calcium transport
negative regulation of calcium ion transmembrane transport
Any mRNA binding that is involved in posttranscriptional gene silencing.
mRNA binding involved in post-transcriptional gene silencing
mRNA binding involved in posttranscriptional gene silencing
Any process that modulates the frequency, rate or extent of calcium:sodium antiporter activity.
regulation of mitochondrial sodium/calcium ion exchange
regulation of calcium:sodium antiporter activity
Any process that stops, prevents or reduces the frequency, rate or extent of calcium:sodium antiporter activity.
down regulation of calcium:sodium antiporter activity
down regulation of sodium/calcium exchanger
down-regulation of calcium:sodium antiporter activity
down-regulation of sodium/calcium exchanger
downregulation of calcium:sodium antiporter activity
downregulation of sodium/calcium exchanger
negative regulation of sodium/calcium exchanger
inhibition of calcium:sodium antiporter activity
down regulation of mitochondrial sodium/calcium ion exchange
down regulation of sodium:calcium exchange
down-regulation of mitochondrial sodium/calcium ion exchange
down-regulation of sodium:calcium exchange
downregulation of mitochondrial sodium/calcium ion exchange
downregulation of sodium:calcium exchange
inhibition of mitochondrial sodium/calcium ion exchange
negative regulation of mitochondrial sodium/calcium ion exchange
negative regulation of sodium:calcium exchange
negative regulation of calcium:sodium antiporter activity
Any process that activates or increases the frequency, rate or extent of calcium:sodium antiporter activity.
positive regulation of sodium/calcium exchanger
up regulation of calcium:sodium antiporter activity
up regulation of sodium/calcium exchanger
up-regulation of calcium:sodium antiporter activity
up-regulation of sodium/calcium exchanger
upregulation of calcium:sodium antiporter activity
upregulation of sodium/calcium exchanger
activation of calcium:sodium antiporter activity
activation of mitochondrial sodium/calcium ion exchange
positive regulation of mitochondrial sodium/calcium ion exchange
positive regulation of sodium:calcium exchange
up regulation of mitochondrial sodium/calcium ion exchange
up regulation of sodium:calcium exchange
up-regulation of mitochondrial sodium/calcium ion exchange
up-regulation of sodium:calcium exchange
upregulation of mitochondrial sodium/calcium ion exchange
positive regulation of calcium:sodium antiporter activity
Any process that modulates the frequency, rate or extent of potassium ion import.
Any process that stops, prevents or reduces the frequency, rate or extent of potassium ion import across the plasma membrane.
negative regulation of potassium ion import
negative regulation of potassium ion uptake
negative regulation of potassium ion import across plasma membrane
Any process that activates or increases the frequency, rate or extent of potassium ion import across the plasma membrane.
positive regulation of potassium ion import
positive regulation of potassium ion uptake
positive regulation of potassium ion import across plasma membrane
Any process that modulates the frequency, rate or extent of protein folding.
regulation of chaperonin-mediated tubulin folding
regulation of chaperonin ATPase activity
regulation of glycoprotein-specific chaperone activity
regulation of non-chaperonin molecular chaperone ATPase activity
regulation of protein complex assembly, multichaperone pathway
Any process that stops, prevents or reduces the frequency, rate or extent of protein folding.
down regulation of alpha-tubulin folding
down regulation of chaperonin-mediated tubulin folding
down-regulation of alpha-tubulin folding
down-regulation of chaperonin-mediated tubulin folding
downregulation of chaperonin-mediated tubulin folding
inhibition of chaperonin-mediated tubulin folding
negative regulation of alpha-tubulin folding
negative regulation of beta-tubulin folding
negative regulation of chaperonin-mediated tubulin folding
down regulation of chaperonin ATPase activity
down regulation of co-chaperone activity
down regulation of co-chaperonin activity
down regulation of glycoprotein-specific chaperone activity
down regulation of non-chaperonin molecular chaperone ATPase activity
down regulation of protein complex assembly, multichaperone pathway
down-regulation of chaperonin ATPase activity
down-regulation of co-chaperone activity
down-regulation of co-chaperonin activity
down-regulation of glycoprotein-specific chaperone activity
down-regulation of non-chaperonin molecular chaperone ATPase activity
down-regulation of protein complex assembly, multichaperone pathway
downregulation of chaperonin ATPase activity
downregulation of co-chaperonin activity
downregulation of glycoprotein-specific chaperone activity
downregulation of non-chaperonin molecular chaperone ATPase activity
downregulation of protein complex assembly, multichaperone pathway
inhibition of chaperonin ATPase activity
inhibition of glycoprotein-specific chaperone activity
inhibition of non-chaperonin molecular chaperone ATPase activity
inhibition of protein complex assembly, multichaperone pathway
negative regulation of chaperone activity
negative regulation of chaperonin ATPase activity
negative regulation of co-chaperone activity
negative regulation of co-chaperonin activity
negative regulation of glycoprotein-specific chaperone activity
negative regulation of non-chaperonin molecular chaperone ATPase activity
negative regulation of protein complex assembly, multichaperone pathway
Any process that activates or increases the frequency, rate or extent of protein folding.
activation of chaperonin-mediated tubulin folding
positive regulation of alpha-tubulin folding
positive regulation of beta-tubulin folding
positive regulation of chaperonin-mediated tubulin folding
up regulation of chaperonin-mediated tubulin folding
up-regulation of chaperonin-mediated tubulin folding
upregulation of chaperonin-mediated tubulin folding
activation of chaperonin ATPase activity
activation of glycoprotein-specific chaperone activity
activation of non-chaperonin molecular chaperone ATPase activity
activation of protein complex assembly, multichaperone pathway
positive regulation of chaperone activity
positive regulation of chaperonin ATPase activity
positive regulation of co-chaperone activity
positive regulation of co-chaperonin activity
positive regulation of glycoprotein-specific chaperone activity
positive regulation of non-chaperonin molecular chaperone ATPase activity
positive regulation of protein complex assembly, multichaperone pathway
up regulation of chaperonin ATPase activity
up regulation of glycoprotein-specific chaperone activity
up regulation of non-chaperonin molecular chaperone ATPase activity
up regulation of protein complex assembly, multichaperone pathway
up-regulation of chaperonin ATPase activity
up-regulation of glycoprotein-specific chaperone activity
up-regulation of non-chaperonin molecular chaperone ATPase activity
up-regulation of protein complex assembly, multichaperone pathway
upregulation of chaperonin ATPase activity
upregulation of glycoprotein-specific chaperone activity
upregulation of non-chaperonin molecular chaperone ATPase activity
upregulation of protein complex assembly, multichaperone pathway
Any process that modulates the frequency, rate or extent of cell wall organization or biogenesis.
regulation of cell wall organisation or biogenesis
regulation of cell wall organization or biogenesis at cellular level
regulation of cellular cell wall organisation or biogenesis
regulation of cellular cell wall organization or biogenesis
regulation of cell wall organization or biogenesis
Any process that stops, prevents or reduces the frequency, rate or extent of cell wall organization or biogenesis.
down regulation of cell wall organisation or biogenesis
down regulation of cell wall organization or biogenesis
down regulation of cell wall organization or biogenesis at cellular level
down regulation of cellular cell wall organisation or biogenesis
down regulation of cellular cell wall organization or biogenesis
down-regulation of cell wall organisation or biogenesis
down-regulation of cell wall organization or biogenesis
down-regulation of cell wall organization or biogenesis at cellular level
down-regulation of cellular cell wall organisation or biogenesis
down-regulation of cellular cell wall organization or biogenesis
downregulation of cell wall organisation or biogenesis
downregulation of cell wall organization or biogenesis
downregulation of cell wall organization or biogenesis at cellular level
downregulation of cellular cell wall organisation or biogenesis
downregulation of cellular cell wall organization or biogenesis
negative regulation of cell wall organisation or biogenesis
negative regulation of cell wall organization or biogenesis at cellular level
negative regulation of cellular cell wall organisation or biogenesis
negative regulation of cellular cell wall organization or biogenesis
inhibition of cell wall organisation or biogenesis
inhibition of cell wall organization or biogenesis
inhibition of cell wall organization or biogenesis at cellular level
inhibition of cellular cell wall organisation or biogenesis
inhibition of cellular cell wall organization or biogenesis
negative regulation of cell wall organization or biogenesis
Any process that activates or increases the frequency, rate or extent of cell wall organization or biogenesis.
positive regulation of cell wall organisation or biogenesis
positive regulation of cell wall organization or biogenesis at cellular level
positive regulation of cellular cell wall organisation or biogenesis
positive regulation of cellular cell wall organization or biogenesis
up regulation of cell wall organisation or biogenesis
up regulation of cell wall organization or biogenesis
up regulation of cell wall organization or biogenesis at cellular level
up regulation of cellular cell wall organisation or biogenesis
up regulation of cellular cell wall organization or biogenesis
up-regulation of cell wall organisation or biogenesis
up-regulation of cell wall organization or biogenesis
up-regulation of cell wall organization or biogenesis at cellular level
up-regulation of cellular cell wall organisation or biogenesis
up-regulation of cellular cell wall organization or biogenesis
upregulation of cell wall organisation or biogenesis
upregulation of cell wall organization or biogenesis
upregulation of cell wall organization or biogenesis at cellular level
upregulation of cellular cell wall organisation or biogenesis
upregulation of cellular cell wall organization or biogenesis
activation of cell wall organisation or biogenesis
activation of cell wall organization or biogenesis
activation of cell wall organization or biogenesis at cellular level
activation of cellular cell wall organisation or biogenesis
activation of cellular cell wall organization or biogenesis
positive regulation of cell wall organization or biogenesis
Any process that modulates the frequency, rate or extent of homophilic cell adhesion.
Any process that stops, prevents or reduces the frequency, rate or extent of homophilic cell adhesion.
down regulation of homophilic cell adhesion
down-regulation of homophilic cell adhesion
downregulation of homophilic cell adhesion
negative regulation of homophilic cell adhesion
Any process that activates or increases the frequency, rate or extent of homophilic cell adhesion.
up regulation of homophilic cell adhesion
up-regulation of homophilic cell adhesion
upregulation of homophilic cell adhesion
positive regulation of homophilic cell adhesion
Any process that modulates the frequency, rate or extent of sodium:potassium-exchanging ATPase activity.
regulation of (Na+ + K+)-ATPase activity
regulation of (Na+ + K+)-activated ATPase activity
regulation of ATP phosphohydrolase (Na+/K+-exchanging)
regulation of Na(+)/K(+)-ATPase activity
regulation of Na(+)/K(+)-exchanging ATPase activity
regulation of Na+/K+-exchanging ATPase activity
regulation of Na,K-activated ATPase activity
regulation of sodium/potassium-exchanging ATPase activity
regulation of sodium/potassium-transporting ATPase activity
regulation of sodium:potassium exchanging ATPase activity
regulation of sodium:potassium-exchanging ATPase activity
Any process that stops, prevents or reduces the frequency, rate or extent of sodium:potassium-exchanging ATPase activity.
down regulation of (Na+ + K+)-ATPase activity
down regulation of (Na+ + K+)-activated ATPase activity
down regulation of ATP phosphohydrolase (Na+/K+-exchanging)
down regulation of Na(+)/K(+)-ATPase activity
down regulation of Na(+)/K(+)-exchanging ATPase activity
down regulation of Na+,K+-ATPase activity
down regulation of Na+/K+-ATPase activity
down regulation of Na+/K+-exchanging ATPase activity
down regulation of Na,K-activated ATPase activity
down regulation of sodium/potassium-exchanging ATPase activity
down regulation of sodium/potassium-transporting ATPase activity
down regulation of sodium:potassium exchanging ATPase activity
down regulation of sodium:potassium-exchanging ATPase activity
down-regulation of (Na+ + K+)-ATPase activity
down-regulation of (Na+ + K+)-activated ATPase activity
down-regulation of ATP phosphohydrolase (Na+/K+-exchanging)
down-regulation of Na(+)/K(+)-ATPase activity
down-regulation of Na(+)/K(+)-exchanging ATPase activity
down-regulation of Na+,K+-ATPase activity
down-regulation of Na+/K+-ATPase activity
down-regulation of Na+/K+-exchanging ATPase activity
down-regulation of Na,K-activated ATPase activity
down-regulation of sodium/potassium-exchanging ATPase activity
down-regulation of sodium/potassium-transporting ATPase activity
down-regulation of sodium:potassium exchanging ATPase activity
down-regulation of sodium:potassium-exchanging ATPase activity
downregulation of (Na+ + K+)-ATPase activity
downregulation of (Na+ + K+)-activated ATPase activity
downregulation of ATP phosphohydrolase (Na+/K+-exchanging)
downregulation of Na(+)/K(+)-ATPase activity
downregulation of Na(+)/K(+)-exchanging ATPase activity
downregulation of Na+,K+-ATPase activity
downregulation of Na+/K+-ATPase activity
downregulation of Na+/K+-exchanging ATPase activity
downregulation of Na,K-activated ATPase activity
downregulation of sodium/potassium-exchanging ATPase activity
downregulation of sodium/potassium-transporting ATPase activity
downregulation of sodium:potassium exchanging ATPase activity
downregulation of sodium:potassium-exchanging ATPase activity
negative regulation of (Na+ + K+)-ATPase activity
negative regulation of (Na+ + K+)-activated ATPase activity
negative regulation of ATP phosphohydrolase (Na+/K+-exchanging)
negative regulation of Na(+)/K(+)-ATPase activity
negative regulation of Na(+)/K(+)-exchanging ATPase activity
negative regulation of Na+,K+-ATPase activity
negative regulation of Na+/K+-ATPase activity
negative regulation of Na+/K+-exchanging ATPase activity
negative regulation of Na,K-activated ATPase activity
negative regulation of sodium/potassium-exchanging ATPase activity
negative regulation of sodium/potassium-transporting ATPase activity
negative regulation of sodium:potassium exchanging ATPase activity
inhibition of (Na+ + K+)-ATPase activity
inhibition of (Na+ + K+)-activated ATPase activity
inhibition of ATP phosphohydrolase (Na+/K+-exchanging)
inhibition of Na(+)/K(+)-ATPase activity
inhibition of Na(+)/K(+)-exchanging ATPase activity
inhibition of Na+/K+-exchanging ATPase activity
inhibition of Na,K-activated ATPase activity
inhibition of sodium/potassium-exchanging ATPase activity
inhibition of sodium/potassium-transporting ATPase activity
inhibition of sodium:potassium exchanging ATPase activity
inhibition of sodium:potassium-exchanging ATPase activity
negative regulation of sodium:potassium-exchanging ATPase activity
Any process that activates or increases the frequency, rate or extent of sodium:potassium-exchanging ATPase activity.
positive regulation of (Na+ + K+)-ATPase activity
positive regulation of (Na+ + K+)-activated ATPase activity
positive regulation of ATP phosphohydrolase (Na+/K+-exchanging)
positive regulation of Na(+)/K(+)-ATPase activity
positive regulation of Na(+)/K(+)-exchanging ATPase activity
positive regulation of Na+,K+-ATPase activity
positive regulation of Na+/K+-ATPase activity
positive regulation of Na+/K+-exchanging ATPase activity
positive regulation of Na,K-activated ATPase activity
positive regulation of sodium/potassium-exchanging ATPase activity
positive regulation of sodium/potassium-transporting ATPase activity
positive regulation of sodium:potassium exchanging ATPase activity
up regulation of (Na+ + K+)-ATPase activity
up regulation of (Na+ + K+)-activated ATPase activity
up regulation of ATP phosphohydrolase (Na+/K+-exchanging)
up regulation of Na(+)/K(+)-ATPase activity
up regulation of Na(+)/K(+)-exchanging ATPase activity
up regulation of Na+/K+-exchanging ATPase activity
up regulation of Na,K-activated ATPase activity
up regulation of sodium/potassium-exchanging ATPase activity
up regulation of sodium/potassium-transporting ATPase activity
up regulation of sodium:potassium exchanging ATPase activity
up regulation of sodium:potassium-exchanging ATPase activity
up-regulation of (Na+ + K+)-ATPase activity
up-regulation of (Na+ + K+)-activated ATPase activity
up-regulation of ATP phosphohydrolase (Na+/K+-exchanging)
up-regulation of Na(+)/K(+)-ATPase activity
up-regulation of Na(+)/K(+)-exchanging ATPase activity
up-regulation of Na+/K+-exchanging ATPase activity
up-regulation of Na,K-activated ATPase activity
up-regulation of sodium/potassium-exchanging ATPase activity
up-regulation of sodium/potassium-transporting ATPase activity
up-regulation of sodium:potassium exchanging ATPase activity
up-regulation of sodium:potassium-exchanging ATPase activity
upregulation of (Na+ + K+)-ATPase activity
upregulation of (Na+ + K+)-activated ATPase activity
upregulation of ATP phosphohydrolase (Na+/K+-exchanging)
upregulation of Na(+)/K(+)-ATPase activity
upregulation of Na(+)/K(+)-exchanging ATPase activity
upregulation of Na+/K+-exchanging ATPase activity
upregulation of Na,K-activated ATPase activity
upregulation of sodium/potassium-exchanging ATPase activity
upregulation of sodium/potassium-transporting ATPase activity
upregulation of sodium:potassium exchanging ATPase activity
upregulation of sodium:potassium-exchanging ATPase activity
activation of (Na+ + K+)-ATPase activity
activation of (Na+ + K+)-activated ATPase activity
activation of ATP phosphohydrolase (Na+/K+-exchanging)
activation of Na(+)/K(+)-ATPase activity
activation of Na(+)/K(+)-exchanging ATPase activity
activation of Na+/K+-exchanging ATPase activity
activation of Na,K-activated ATPase activity
activation of sodium/potassium-exchanging ATPase activity
activation of sodium/potassium-transporting ATPase activity
activation of sodium:potassium exchanging ATPase activity
activation of sodium:potassium-exchanging ATPase activity
positive regulation of sodium:potassium-exchanging ATPase activity
The directed movement of calcium ion from cytosol to endoplasmic reticulum.
calcium ion transport from cytosol to endoplasmic reticulum
Any process that modulates the frequency, rate or extent of protein localization to cilium.
regulation of protein localization to cilium
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to cilium.
down regulation of protein localization to cilium
down-regulation of protein localization to cilium
downregulation of protein localization to cilium
inhibition of protein localization to cilium
negative regulation of protein localization to cilium
Any process that activates or increases the frequency, rate or extent of protein localization to cilium.
up regulation of protein localization to cilium
up-regulation of protein localization to cilium
upregulation of protein localization to cilium
activation of protein localization to cilium
positive regulation of protein localization to cilium
Any process that modulates the frequency, rate or extent of protein localization to ciliary membrane.
regulation of protein localisation in ciliary membrane
regulation of protein localisation to ciliary membrane
regulation of protein localization in ciliary membrane
regulation of protein localization to ciliary membrane
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to ciliary membrane.
down regulation of protein localisation in ciliary membrane
down regulation of protein localisation to ciliary membrane
down regulation of protein localization in ciliary membrane
down regulation of protein localization to ciliary membrane
down-regulation of protein localisation in ciliary membrane
down-regulation of protein localisation to ciliary membrane
down-regulation of protein localization in ciliary membrane
down-regulation of protein localization to ciliary membrane
downregulation of protein localisation in ciliary membrane
downregulation of protein localisation to ciliary membrane
downregulation of protein localization in ciliary membrane
downregulation of protein localization to ciliary membrane
negative regulation of protein localisation in ciliary membrane
negative regulation of protein localisation to ciliary membrane
negative regulation of protein localization in ciliary membrane
inhibition of protein localisation in ciliary membrane
inhibition of protein localisation to ciliary membrane
inhibition of protein localization in ciliary membrane
inhibition of protein localization to ciliary membrane
negative regulation of protein localization to ciliary membrane
Any process that activates or increases the frequency, rate or extent of protein localization to ciliary membrane.
positive regulation of protein localisation in ciliary membrane
positive regulation of protein localisation to ciliary membrane
positive regulation of protein localization in ciliary membrane
up regulation of protein localisation in ciliary membrane
up regulation of protein localisation to ciliary membrane
up regulation of protein localization in ciliary membrane
up regulation of protein localization to ciliary membrane
up-regulation of protein localisation in ciliary membrane
up-regulation of protein localisation to ciliary membrane
up-regulation of protein localization in ciliary membrane
up-regulation of protein localization to ciliary membrane
upregulation of protein localisation in ciliary membrane
upregulation of protein localisation to ciliary membrane
upregulation of protein localization in ciliary membrane
upregulation of protein localization to ciliary membrane
activation of protein localisation in ciliary membrane
activation of protein localisation to ciliary membrane
activation of protein localization in ciliary membrane
activation of protein localization to ciliary membrane
positive regulation of protein localization to ciliary membrane
Any process that stops, prevents or reduces the frequency, rate or extent of inward rectifier potassium channel activity.
down regulation of inward rectifier potassium channel activity
down-regulation of inward rectifier potassium channel activity
downregulation of inward rectifier potassium channel activity
negative regulation of Kir channel activity
inhibition of inward rectifier potassium channel activity
negative regulation of inward rectifier potassium channel activity
Any process that modulates the frequency, rate or extent of chaperone-mediated protein folding.
regulation of chaperone-mediated protein folding
Any process that stops, prevents or reduces the frequency, rate or extent of chaperone-mediated protein folding.
down regulation of chaperone-mediated protein folding
down-regulation of chaperone-mediated protein folding
downregulation of chaperone-mediated protein folding
inhibition of chaperone-mediated protein folding
negative regulation of chaperone-mediated protein folding
Any process that activates or increases the frequency, rate or extent of chaperone-mediated protein folding.
up regulation of chaperone-mediated protein folding
up-regulation of chaperone-mediated protein folding
upregulation of chaperone-mediated protein folding
activation of chaperone-mediated protein folding
positive regulation of chaperone-mediated protein folding
Any process that modulates the frequency, rate or extent of cytoplasmic transport.
Any process that stops, prevents or reduces the frequency, rate or extent of cytoplasmic transport.
down regulation of cytoplasmic transport
down-regulation of cytoplasmic transport
down regulation of cytoplasmic streaming
down-regulation of cytoplasmic streaming
negative regulation of cytoplasmic streaming
negative regulation of cytoplasmic transport
Any process that activates or increases the frequency, rate or extent of cytoplasmic transport.
positive regulation of cytoplasmic streaming
positive regulation of cytoplasmic transport
Any process that modulates the frequency, rate or extent of establishment of protein localization to mitochondrion.
regulation of establishment of protein localisation to mitochondrion
regulation of establishment of protein localization in mitochondrion
regulation of establishment of protein localization to mitochondrion
Any process that stops, prevents or reduces the frequency, rate or extent of establishment of protein localization to mitochondrion.
down regulation of establishment of protein localisation to mitochondrion
down regulation of establishment of protein localization in mitochondrion
down regulation of establishment of protein localization to mitochondrion
down-regulation of establishment of protein localisation to mitochondrion
down-regulation of establishment of protein localization in mitochondrion
down-regulation of establishment of protein localization to mitochondrion
downregulation of establishment of protein localisation to mitochondrion
downregulation of establishment of protein localization in mitochondrion
downregulation of establishment of protein localization to mitochondrion
negative regulation of establishment of protein localisation to mitochondrion
negative regulation of establishment of protein localization in mitochondrion
inhibition of establishment of protein localisation to mitochondrion
inhibition of establishment of protein localization in mitochondrion
inhibition of establishment of protein localization to mitochondrion
negative regulation of establishment of protein localization to mitochondrion
Any process that activates or increases the frequency, rate or extent of establishment of protein localization to mitochondrion.
positive regulation of establishment of protein localisation to mitochondrion
positive regulation of establishment of protein localization in mitochondrion
up regulation of establishment of protein localisation to mitochondrion
up regulation of establishment of protein localization in mitochondrion
up regulation of establishment of protein localization to mitochondrion
up-regulation of establishment of protein localisation to mitochondrion
up-regulation of establishment of protein localization in mitochondrion
up-regulation of establishment of protein localization to mitochondrion
upregulation of establishment of protein localisation to mitochondrion
upregulation of establishment of protein localization in mitochondrion
upregulation of establishment of protein localization to mitochondrion
activation of establishment of protein localisation to mitochondrion
activation of establishment of protein localization in mitochondrion
activation of establishment of protein localization to mitochondrion
positive regulation of establishment of protein localization to mitochondrion
Any signal transduction that is involved in regulation of aerobic respiration.
signaling cascade involved in regulation of aerobic respiration
signalling cascade involved in regulation of aerobic respiration
signaling pathway involved in regulation of aerobic respiration
signalling pathway involved in regulation of aerobic respiration
signal transduction involved in regulation of aerobic respiration
Any process that stops, prevents or reduces the frequency, rate or extent of cell proliferation in bone marrow.
down regulation of bone marrow cell proliferation
down regulation of cell proliferation in bone marrow
down-regulation of bone marrow cell proliferation
down-regulation of cell proliferation in bone marrow
downregulation of bone marrow cell proliferation
downregulation of cell proliferation in bone marrow
negative regulation of bone marrow cell proliferation
inhibition of bone marrow cell proliferation
inhibition of cell proliferation in bone marrow
negative regulation of cell proliferation in bone marrow
Interacting selectively and non-covalently with melibiose.
Any process that modulates the frequency, rate or extent of sodium ion import across the plasma membrane.
regulation of sodium ion import across plasma membrane
Any process that stops, prevents or reduces the frequency, rate or extent of sodium ion import across the plasma membrane.
down regulation of sodium ion import across plasma membrane
down-regulation of sodium ion import across plasma membrane
downregulation of sodium ion import across plasma membrane
inhibition of sodium ion import across plasma membrane
negative regulation of sodium ion import across plasma membrane
Any process that activates or increases the frequency, rate or extent of sodium ion import across the plasma membrane.
up regulation of sodium ion import across plasma membrane
up-regulation of sodium ion import across plasma membrane
upregulation of sodium ion import across plasma membrane
activation of sodium ion import across plasma membrane
positive regulation of sodium ion import across plasma membrane
Any process that stops, prevents or reduces the frequency, rate or extent of anion transport.
Any process that activates or increases the frequency, rate or extent of anion transport.
Interacting selectively and non-covalently with cortisol.
Any process that modulates the frequency, rate or extent of inorganic anion transmembrane transport.
regulation of inorganic anion membrane transport
regulation of transmembrane inorganic anion transport
regulation of inorganic anion transmembrane transport
Any process that stops, prevents or reduces the frequency, rate or extent of inorganic anion transmembrane transport.
down regulation of inorganic anion membrane transport
down regulation of inorganic anion transmembrane transport
down regulation of transmembrane inorganic anion transport
down-regulation of inorganic anion membrane transport
down-regulation of inorganic anion transmembrane transport
down-regulation of transmembrane inorganic anion transport
downregulation of inorganic anion membrane transport
downregulation of inorganic anion transmembrane transport
downregulation of transmembrane inorganic anion transport
negative regulation of inorganic anion membrane transport
negative regulation of transmembrane inorganic anion transport
inhibition of inorganic anion membrane transport
inhibition of inorganic anion transmembrane transport
inhibition of transmembrane inorganic anion transport
negative regulation of inorganic anion transmembrane transport
Any process that activates or increases the frequency, rate or extent of inorganic anion transmembrane transport.
positive regulation of inorganic anion membrane transport
positive regulation of transmembrane inorganic anion transport
up regulation of inorganic anion membrane transport
up regulation of inorganic anion transmembrane transport
up regulation of transmembrane inorganic anion transport
up-regulation of inorganic anion membrane transport
up-regulation of inorganic anion transmembrane transport
up-regulation of transmembrane inorganic anion transport
upregulation of inorganic anion membrane transport
upregulation of inorganic anion transmembrane transport
upregulation of transmembrane inorganic anion transport
activation of inorganic anion membrane transport
activation of inorganic anion transmembrane transport
activation of transmembrane inorganic anion transport
positive regulation of inorganic anion transmembrane transport
Any process that stops, prevents or reduces the frequency, rate or extent of voltage-gated potassium channel activity.
down regulation of voltage gated potassium channel activity
down regulation of voltage-dependent potassium channel activity
down regulation of voltage-gated potassium channel activity
down regulation of voltage-gated potassium ion channel activity
down regulation of voltage-sensitive potassium channel
down-regulation of voltage gated potassium channel activity
down-regulation of voltage-dependent potassium channel activity
down-regulation of voltage-gated potassium channel activity
down-regulation of voltage-gated potassium ion channel activity
down-regulation of voltage-sensitive potassium channel
downregulation of voltage gated potassium channel activity
downregulation of voltage-dependent potassium channel activity
downregulation of voltage-gated potassium channel activity
downregulation of voltage-gated potassium ion channel activity
downregulation of voltage-sensitive potassium channel
negative regulation of voltage gated potassium channel activity
negative regulation of voltage-dependent potassium channel activity
negative regulation of voltage-gated potassium ion channel activity
negative regulation of voltage-sensitive potassium channel
inhibition of voltage gated potassium channel activity
inhibition of voltage-dependent potassium channel activity
inhibition of voltage-gated potassium channel activity
inhibition of voltage-gated potassium ion channel activity
inhibition of voltage-sensitive potassium channel
negative regulation of voltage-gated potassium channel activity
Any process that activates or increases the frequency, rate or extent of voltage-gated potassium channel activity.
positive regulation of voltage gated potassium channel activity
positive regulation of voltage-dependent potassium channel activity
positive regulation of voltage-gated potassium ion channel activity
positive regulation of voltage-sensitive potassium channel
up regulation of voltage gated potassium channel activity
up regulation of voltage-dependent potassium channel activity
up regulation of voltage-gated potassium channel activity
up regulation of voltage-gated potassium ion channel activity
up regulation of voltage-sensitive potassium channel
up-regulation of voltage gated potassium channel activity
up-regulation of voltage-dependent potassium channel activity
up-regulation of voltage-gated potassium channel activity
up-regulation of voltage-gated potassium ion channel activity
up-regulation of voltage-sensitive potassium channel
upregulation of voltage gated potassium channel activity
upregulation of voltage-dependent potassium channel activity
upregulation of voltage-gated potassium channel activity
upregulation of voltage-gated potassium ion channel activity
upregulation of voltage-sensitive potassium channel
activation of voltage gated potassium channel activity
activation of voltage-dependent potassium channel activity
activation of voltage-gated potassium channel activity
activation of voltage-gated potassium ion channel activity
activation of voltage-sensitive potassium channel
positive regulation of voltage-gated potassium channel activity
Single strand break repair that takes place in a telomere.
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.
regulation of cellular protein localisation
regulation of channel localizer activity
regulation of cellular protein localization
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.
down regulation of cellular protein localisation
down regulation of cellular protein localization
down-regulation of cellular protein localisation
down-regulation of cellular protein localization
downregulation of cellular protein localisation
downregulation of cellular protein localization
negative regulation of cellular protein localisation
down regulation of channel localizer activity
down-regulation of channel localizer activity
downregulation of channel localizer activity
inhibition of cellular protein localisation
inhibition of cellular protein localization
inhibition of channel localizer activity
negative regulation of channel localizer activity
negative regulation of cellular protein localization
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.
positive regulation of cellular protein localisation
up regulation of cellular protein localisation
up regulation of cellular protein localization
up-regulation of cellular protein localisation
up-regulation of cellular protein localization
upregulation of cellular protein localisation
upregulation of cellular protein localization
activation of cellular protein localisation
activation of cellular protein localization
activation of channel localizer activity
positive regulation of channel localizer activity
up regulation of channel localizer activity
up-regulation of channel localizer activity
upregulation of channel localizer activity
positive regulation of cellular protein localization
The directed movement of magnesium ion across a membrane.
Interacting selectively and non-covalently with corticosterone.
Interacting selectively and non-covalently with 11-deoxycortisol.
Interacting selectively and non-covalently with 21-deoxycortisol.
Interacting selectively and non-covalently with 11-deoxycorticosterone.
Interacting selectively and non-covalently with 11beta-hydroxyprogesterone.
Interacting selectively and non-covalently with 17alpha-hydroxyprogesterone.
Any process that modulates the frequency, rate or extent of receptor clustering.
Any process that stops, prevents or reduces the frequency, rate or extent of receptor clustering.
negative regulation of receptor clustering
Any process that activates or increases the frequency, rate or extent of receptor clustering.
positive regulation of receptor clustering
Interacting selectively and non-covalently with estradiol.
Any process that modulates the frequency, rate or extent of anion transmembrane transport.
regulation of anion transmembrane transport
Any process that stops, prevents or reduces the frequency, rate or extent of anion transmembrane transport.
down regulation of anion transmembrane transport
down-regulation of anion transmembrane transport
downregulation of anion transmembrane transport
inhibition of anion transmembrane transport
negative regulation of anion transmembrane transport
Any process that activates or increases the frequency, rate or extent of anion transmembrane transport.
up regulation of anion transmembrane transport
up-regulation of anion transmembrane transport
upregulation of anion transmembrane transport
activation of anion transmembrane transport
positive regulation of anion transmembrane transport
Interacting selectively and non-covalently with enterobactin.
The directed movement of iron ions from inside of a cell, across the plasma membrane and into the extracellular region.
ferrous iron export across plasma membrane
An example of this is mouse ferroportin (symbol Slc40a1, UniProtKB identifier: Q9JHI9).
Any process that modulates the frequency, rate or extent of sebum secreting cell proliferation.
regulation of sebum secreting cell proliferation
Any process that stops, prevents or reduces the frequency, rate or extent of sebum secreting cell proliferation.
down regulation of sebum secreting cell proliferation
down-regulation of sebum secreting cell proliferation
downregulation of sebum secreting cell proliferation
inhibition of sebum secreting cell proliferation
down regulation of sebocyte proliferation
down-regulation of sebocyte proliferation
downregulation of sebocyte proliferation
negative regulation of sebocyte proliferation
negative regulation of sebum secreting cell proliferation
Any process that activates or increases the frequency, rate or extent of sebum secreting cell proliferation.
up regulation of sebum secreting cell proliferation
up-regulation of sebum secreting cell proliferation
upregulation of sebum secreting cell proliferation
activation of sebum secreting cell proliferation
positive regulation of sebocyte proliferation
positive regulation of sebum secreting cell proliferation
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.
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.
cellular response to monosodium glutamate
Any process that modulates the frequency, rate or extent of t-SNARE clustering.
Any process that stops, prevents or reduces the frequency, rate or extent of t-SNARE clustering.
negative regulation of t-SNARE clustering
Any process that activates or increases the frequency, rate or extent of t-SNARE clustering.
positive regulation of t-SNARE clustering
Interacting selectively and non-covalently with S-adenosyl-L-methionine.
Any process that modulates the frequency, rate or extent of cholangiocyte proliferation.
regulation of cholangiocyte proliferation
Any process that stops, prevents or reduces the frequency, rate or extent of cholangiocyte proliferation.
down regulation of cholangiocyte proliferation
down regulation of hepatoblast proliferation
down-regulation of cholangiocyte proliferation
down-regulation of hepatoblast proliferation
downregulation of cholangiocyte proliferation
downregulation of hepatoblast proliferation
negative regulation of hepatoblast proliferation
inhibition of cholangiocyte proliferation
negative regulation of cholangiocyte proliferation
Any process that activates or increases the frequency, rate or extent of cholangiocyte proliferation.
positive regulation of hepatoblast proliferation
up regulation of cholangiocyte proliferation
up regulation of hepatoblast proliferation
up-regulation of cholangiocyte proliferation
up-regulation of hepatoblast proliferation
upregulation of cholangiocyte proliferation
upregulation of hepatoblast proliferation
activation of cholangiocyte proliferation
positive regulation of cholangiocyte proliferation
Any process that modulates the frequency, rate or extent of cation transmembrane transport.
regulation of cation transmembrane transport
Any process that stops, prevents or reduces the frequency, rate or extent of cation transmembrane transport.
down regulation of cation transmembrane transport
down-regulation of cation transmembrane transport
downregulation of cation transmembrane transport
inhibition of cation transmembrane transport
negative regulation of cation transmembrane transport
Any process that activates or increases the frequency, rate or extent of cation transmembrane transport.
up regulation of cation transmembrane transport
up-regulation of cation transmembrane transport
upregulation of cation transmembrane transport
activation of cation transmembrane transport
positive regulation of cation transmembrane transport
Any process that modulates the frequency, rate or extent of granulosa cell proliferation.
regulation of granulosa cell proliferation
Any process that stops, prevents or reduces the frequency, rate or extent of granulosa cell proliferation.
down regulation of granulosa cell proliferation
down-regulation of granulosa cell proliferation
downregulation of granulosa cell proliferation
inhibition of granulosa cell proliferation
negative regulation of granulosa cell proliferation
Any process that activates or increases the frequency, rate or extent of granulosa cell proliferation.
up regulation of granulosa cell proliferation
up-regulation of granulosa cell proliferation
upregulation of granulosa cell proliferation
activation of granulosa cell proliferation
positive regulation of granulosa cell proliferation
Any process that modulates the frequency, rate or extent of iodide transport.
Any process that stops, prevents or reduces the frequency, rate or extent of iodide transport.
Any process that activates or increases the frequency, rate or extent of iodide transport.
Any process that modulates the frequency, rate or extent of iodide transmembrane transport.
regulation of iodide transmembrane transport
Any process that stops, prevents or reduces the frequency, rate or extent of iodide transmembrane transport.
down regulation of iodide transmembrane transport
down-regulation of iodide transmembrane transport
downregulation of iodide transmembrane transport
inhibition of iodide transmembrane transport
negative regulation of iodide transmembrane transport
Any process that activates or increases the frequency, rate or extent of iodide transmembrane transport.
up regulation of iodide transmembrane transport
up-regulation of iodide transmembrane transport
upregulation of iodide transmembrane transport
activation of iodide transmembrane transport
positive regulation of iodide transmembrane transport
Any process that modulates the frequency, rate or extent of an iron transmembrane transporter activity.
regulation of iron cation channel activity
regulation of iron-specific channel activity
regulation of iron ion transmembrane transporter activity
Any process that stops, prevents or reduces the frequency, rate or extent of an iron transmembrane transporter activity.
down regulation of iron cation channel activity
down regulation of iron channel activity
down regulation of iron-specific channel activity
down-regulation of iron cation channel activity
down-regulation of iron channel activity
down-regulation of iron-specific channel activity
downregulation of iron cation channel activity
downregulation of iron-specific channel activity
negative regulation of iron cation channel activity
negative regulation of iron channel activity
negative regulation of iron-specific channel activity
inhibition of iron cation channel activity
inhibition of iron-specific channel activity
negative regulation of iron ion transmembrane transporter activity
Any process that activates or increases the frequency, rate or extent of an iron transmembrane transporter activity.
positive regulation of iron cation channel activity
positive regulation of iron channel activity
positive regulation of iron transmembrane transporter activity
positive regulation of iron-specific channel activity
up regulation of iron cation channel activity
up regulation of iron-specific channel activity
up-regulation of iron cation channel activity
up-regulation of iron-specific channel activity
upregulation of iron cation channel activity
upregulation of iron-specific channel activity
activation of iron cation channel activity
activation of iron-specific channel activity
positive regulation of iron ion transmembrane transporter activity
The directed import of zinc(2+) from the cytosol across the Golgi membrane into the Golgi apparatus.
zinc II ion import across Golgi membrane
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.
Interacting selectively and non-covalently with a BAT3 complex.
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.
response to methamphetamine hydrochloride
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.
cellular response to methamphetamine HCL
cellular response to methamphetamine hydrochloride
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.
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.
The directed movement of heme from outside of a cell, across the plasma membrane and into the cytosol.
Any process that modulates the frequency, rate or extent of chemokinesis.
Any process that stops, prevents or reduces the frequency, rate or extent of chemokinesis.
Any process that activates or increases the frequency, rate or extent of chemokinesis.
Any process that modulates the frequency, rate or extent of protein localization to actin cortical patch.
regulation of protein localisation to actin cortical patch
regulation of protein localization to actin cortical patch
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to actin cortical patch.
down regulation of protein localisation to actin cortical patch
down regulation of protein localization to actin cortical patch
down-regulation of protein localisation to actin cortical patch
down-regulation of protein localization to actin cortical patch
downregulation of protein localisation to actin cortical patch
downregulation of protein localization to actin cortical patch
negative regulation of protein localisation to actin cortical patch
inhibition of protein localisation to actin cortical patch
inhibition of protein localization to actin cortical patch
negative regulation of protein localization to actin cortical patch
Any process that activates or increases the frequency, rate or extent of protein localization to actin cortical patch.
positive regulation of protein localisation to actin cortical patch
up regulation of protein localisation to actin cortical patch
up regulation of protein localization to actin cortical patch
up-regulation of protein localisation to actin cortical patch
up-regulation of protein localization to actin cortical patch
upregulation of protein localisation to actin cortical patch
upregulation of protein localization to actin cortical patch
activation of protein localisation to actin cortical patch
activation of protein localization to actin cortical patch
positive regulation of protein localization to actin cortical patch
Any process that modulates the frequency, rate or extent of protein localization to cell periphery.
regulation of protein localization to cell periphery
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to cell periphery.
down regulation of protein localization to cell periphery
down-regulation of protein localization to cell periphery
downregulation of protein localization to cell periphery
inhibition of protein localization to cell periphery
negative regulation of protein localization to cell periphery
Any process that activates or increases the frequency, rate or extent of protein localization to cell periphery.
up regulation of protein localization to cell periphery
up-regulation of protein localization to cell periphery
upregulation of protein localization to cell periphery
activation of protein localization to cell periphery
positive regulation of protein localization to cell periphery
Interacting selectively and non-covalently with heparan sulfate.
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.
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.
Interacting selectively and non-covalently with melatonin.
Any process that activates or increases the frequency, rate or extent of calcium ion transmembrane transport.
positive regulation of calcium ion membrane transport
positive regulation of transmembrane calcium transport
up regulation of calcium ion membrane transport
up regulation of calcium ion transmembrane transport
up regulation of transmembrane calcium transport
up-regulation of calcium ion membrane transport
up-regulation of calcium ion transmembrane transport
up-regulation of transmembrane calcium transport
upregulation of calcium ion membrane transport
upregulation of calcium ion transmembrane transport
upregulation of transmembrane calcium transport
activation of calcium ion membrane transport
activation of calcium ion transmembrane transport
activation of transmembrane calcium transport
positive regulation of calcium ion transmembrane transport
Any process that modulates the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
regulation of ATP phosphohydrolase (H+/K+-exchanging)
regulation of H(+)/K(+)-exchanging ATPase activity
regulation of H+/K+-exchanging ATPase activity
regulation of hydrogen/potassium-exchanging ATPase activity
regulation of hydrogen:potassium exchanging ATPase activity
regulation of hydrogen:potassium-exchanging ATPase activity
regulation of gastric H(+)/K(+) ATPase activity
regulation of potassium:proton exchanging ATPase activity
Any process that stops, prevents or reduces the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
down regulation of (K+ + H+)-ATPase activity
down regulation of ATP phosphohydrolase (H+/K+-exchanging)
down regulation of H(+)/K(+)-ATPase activity
down regulation of H(+)/K(+)-exchanging ATPase activity
down regulation of H+-K+-ATPase activity
down regulation of H+/K+-ATPase activity
down regulation of H+/K+-exchanging ATPase activity
down regulation of hydrogen/potassium-exchanging ATPase activity
down regulation of hydrogen:potassium exchanging ATPase activity
down regulation of hydrogen:potassium-exchanging ATPase activity
down-regulation of (K+ + H+)-ATPase activity
down-regulation of ATP phosphohydrolase (H+/K+-exchanging)
down-regulation of H(+)/K(+)-ATPase activity
down-regulation of H(+)/K(+)-exchanging ATPase activity
down-regulation of H+-K+-ATPase activity
down-regulation of H+/K+-ATPase activity
down-regulation of H+/K+-exchanging ATPase activity
down-regulation of hydrogen/potassium-exchanging ATPase activity
down-regulation of hydrogen:potassium exchanging ATPase activity
down-regulation of hydrogen:potassium-exchanging ATPase activity
downregulation of (K+ + H+)-ATPase activity
downregulation of ATP phosphohydrolase (H+/K+-exchanging)
downregulation of H(+)/K(+)-ATPase activity
downregulation of H(+)/K(+)-exchanging ATPase activity
downregulation of H+/K+-exchanging ATPase activity
downregulation of hydrogen/potassium-exchanging ATPase activity
downregulation of hydrogen:potassium exchanging ATPase activity
downregulation of hydrogen:potassium-exchanging ATPase activity
negative regulation of (K+ + H+)-ATPase activity
negative regulation of ATP phosphohydrolase (H+/K+-exchanging)
negative regulation of H(+)/K(+)-ATPase activity
negative regulation of H(+)/K(+)-exchanging ATPase activity
negative regulation of H+-K+-ATPase activity
negative regulation of H+/K+-ATPase activity
negative regulation of H+/K+-exchanging ATPase activity
negative regulation of H,K-ATPase activity
negative regulation of hydrogen/potassium-exchanging ATPase activity
negative regulation of hydrogen:potassium exchanging ATPase activity
negative regulation of hydrogen:potassium-exchanging ATPase activity
down regulation of gastric H(+)/K(+) ATPase activity
down-regulation of gastric H(+)/K(+) ATPase activity
downregulation of gastric H(+)/K(+) ATPase activity
inhibition of ATP phosphohydrolase (H+/K+-exchanging)
inhibition of H(+)/K(+)-exchanging ATPase activity
inhibition of H+/K+-exchanging ATPase activity
inhibition of gastric H(+)/K(+) ATPase activity
inhibition of hydrogen/potassium-exchanging ATPase activity
inhibition of hydrogen:potassium exchanging ATPase activity
inhibition of hydrogen:potassium-exchanging ATPase activity
negative regulation of gastric H(+)/K(+) ATPase activity
negative regulation of gastric H+/K+ ATPase
negative regulation of potassium:proton exchanging ATPase activity
Any process that activates or increases the frequency, rate or extent of hydrogen:potassium-exchanging ATPase activity.
positive regulation of (K+ + H+)-ATPase activity
positive regulation of ATP phosphohydrolase (H+/K+-exchanging)
positive regulation of H(+)/K(+)-ATPase activity
positive regulation of H(+)/K(+)-exchanging ATPase activity
positive regulation of H+-K+-ATPase activity
positive regulation of H+/K+-ATPase activity
positive regulation of H+/K+-exchanging ATPase activity
positive regulation of H,K-ATPase activity
positive regulation of hydrogen/potassium-exchanging ATPase activity
positive regulation of hydrogen:potassium exchanging ATPase activity
positive regulation of hydrogen:potassium-exchanging ATPase activity
up regulation of (K+ + H+)-ATPase activity
up regulation of ATP phosphohydrolase (H+/K+-exchanging)
up regulation of H(+)/K(+)-ATPase activity
up regulation of H(+)/K(+)-exchanging ATPase activity
up regulation of H+/K+-exchanging ATPase activity
up regulation of hydrogen/potassium-exchanging ATPase activity
up regulation of hydrogen:potassium exchanging ATPase activity
up regulation of hydrogen:potassium-exchanging ATPase activity
up-regulation of (K+ + H+)-ATPase activity
up-regulation of ATP phosphohydrolase (H+/K+-exchanging)
up-regulation of H(+)/K(+)-ATPase activity
up-regulation of H(+)/K(+)-exchanging ATPase activity
up-regulation of H+/K+-exchanging ATPase activity
up-regulation of hydrogen/potassium-exchanging ATPase activity
up-regulation of hydrogen:potassium exchanging ATPase activity
up-regulation of hydrogen:potassium-exchanging ATPase activity
upregulation of (K+ + H+)-ATPase activity
upregulation of ATP phosphohydrolase (H+/K+-exchanging)
upregulation of H(+)/K(+)-ATPase activity
upregulation of H(+)/K(+)-exchanging ATPase activity
upregulation of H+/K+-exchanging ATPase activity
upregulation of hydrogen/potassium-exchanging ATPase activity
upregulation of hydrogen:potassium exchanging ATPase activity
upregulation of hydrogen:potassium-exchanging ATPase activity
activation of ATP phosphohydrolase (H+/K+-exchanging)
activation of H(+)/K(+)-exchanging ATPase activity
activation of H+/K+-exchanging ATPase activity
activation of gastric H(+)/K(+) ATPase activity
activation of hydrogen/potassium-exchanging ATPase activity
activation of hydrogen:potassium exchanging ATPase activity
activation of hydrogen:potassium-exchanging ATPase activity
positive regulation of gastric H(+)/K(+) ATPase activity
positive regulation of gastric H+/K+ ATPase
up regulation of gastric H(+)/K(+) ATPase activity
up-regulation of gastric H(+)/K(+) ATPase activity
upregulation of gastric H(+)/K(+) ATPase activity
positive regulation of potassium:proton exchanging ATPase activity
Interacting selectively and non-covalently with Ac-Asp-Glu.
Any process that modulates the frequency, rate or extent of protein localization to basolateral plasma membrane.
regulation of protein localisation in basolateral plasma membrane
regulation of protein localisation to basolateral plasma membrane
regulation of protein localization in basolateral plasma membrane
regulation of protein localization to basolateral plasma membrane
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to basolateral plasma membrane.
down regulation of protein localisation in basolateral plasma membrane
down regulation of protein localisation to basolateral plasma membrane
down regulation of protein localization in basolateral plasma membrane
down regulation of protein localization to basolateral plasma membrane
down-regulation of protein localisation in basolateral plasma membrane
down-regulation of protein localisation to basolateral plasma membrane
down-regulation of protein localization in basolateral plasma membrane
down-regulation of protein localization to basolateral plasma membrane
downregulation of protein localisation in basolateral plasma membrane
downregulation of protein localisation to basolateral plasma membrane
downregulation of protein localization in basolateral plasma membrane
downregulation of protein localization to basolateral plasma membrane
negative regulation of protein localisation in basolateral plasma membrane
negative regulation of protein localisation to basolateral plasma membrane
negative regulation of protein localization in basolateral plasma membrane
inhibition of protein localisation in basolateral plasma membrane
inhibition of protein localisation to basolateral plasma membrane
inhibition of protein localization in basolateral plasma membrane
inhibition of protein localization to basolateral plasma membrane
negative regulation of protein localization to basolateral plasma membrane
Any process that activates or increases the frequency, rate or extent of protein localization to basolateral plasma membrane.
positive regulation of protein localisation in basolateral plasma membrane
positive regulation of protein localisation to basolateral plasma membrane
positive regulation of protein localization in basolateral plasma membrane
up regulation of protein localisation in basolateral plasma membrane
up regulation of protein localisation to basolateral plasma membrane
up regulation of protein localization in basolateral plasma membrane
up regulation of protein localization to basolateral plasma membrane
up-regulation of protein localisation in basolateral plasma membrane
up-regulation of protein localisation to basolateral plasma membrane
up-regulation of protein localization in basolateral plasma membrane
up-regulation of protein localization to basolateral plasma membrane
upregulation of protein localisation in basolateral plasma membrane
upregulation of protein localisation to basolateral plasma membrane
upregulation of protein localization in basolateral plasma membrane
upregulation of protein localization to basolateral plasma membrane
activation of protein localisation in basolateral plasma membrane
activation of protein localisation to basolateral plasma membrane
activation of protein localization in basolateral plasma membrane
activation of protein localization to basolateral plasma membrane
positive regulation of protein localization to basolateral plasma membrane
Any process that modulates the frequency, rate or extent of mitotic telomere tethering at nuclear periphery.
regulation of mitotic telomere tethering at nuclear periphery
Any process that stops, prevents or reduces the frequency, rate or extent of mitotic telomere tethering at nuclear periphery.
down regulation of mitotic telomere tethering at nuclear periphery
down-regulation of mitotic telomere tethering at nuclear periphery
downregulation of mitotic telomere tethering at nuclear periphery
inhibition of mitotic telomere tethering at nuclear periphery
negative regulation of mitotic telomere tethering at nuclear periphery
Any process that modulates the frequency, rate or extent of chemotaxis to arachidonic acid.
regulation of chemotaxis to arachidonic acid
Any process that stops, prevents or reduces the frequency, rate or extent of chemotaxis to arachidonic acid.
down regulation of chemotaxis to arachidonic acid
down-regulation of chemotaxis to arachidonic acid
downregulation of chemotaxis to arachidonic acid
inhibition of chemotaxis to arachidonic acid
negative regulation of chemotaxis to arachidonic acid
Any process that activates or increases the frequency, rate or extent of chemotaxis to arachidonic acid.
up regulation of chemotaxis to arachidonic acid
up-regulation of chemotaxis to arachidonic acid
upregulation of chemotaxis to arachidonic acid
activation of chemotaxis to arachidonic acid
positive regulation of chemotaxis to arachidonic acid
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.
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.
Any process that modulates the frequency, rate or extent of intracellular mRNA localization.
regulation of establishment and maintenance of intracellular RNA localization
regulation of intracellular mRNA localisation
regulation of mRNA localization, intracellular
regulation of intracellular mRNA positioning
regulation of mRNA positioning, intracellular
regulation of intracellular mRNA localization
Any process that stops, prevents or reduces the frequency, rate or extent of intracellular mRNA localization.
down regulation of establishment and maintenance of intracellular RNA localization
down regulation of intracellular mRNA localisation
down regulation of intracellular mRNA localization
down regulation of mRNA localization, intracellular
down-regulation of establishment and maintenance of intracellular RNA localization
down-regulation of intracellular mRNA localisation
down-regulation of intracellular mRNA localization
down-regulation of mRNA localization, intracellular
downregulation of establishment and maintenance of intracellular RNA localization
downregulation of intracellular mRNA localisation
downregulation of intracellular mRNA localization
downregulation of mRNA localization, intracellular
negative regulation of establishment and maintenance of intracellular RNA localization
negative regulation of intracellular mRNA localisation
negative regulation of mRNA localization, intracellular
down regulation of intracellular mRNA positioning
down regulation of mRNA positioning, intracellular
down-regulation of intracellular mRNA positioning
down-regulation of mRNA positioning, intracellular
downregulation of intracellular mRNA positioning
downregulation of mRNA positioning, intracellular
inhibition of establishment and maintenance of intracellular RNA localization
inhibition of intracellular mRNA localisation
inhibition of intracellular mRNA localization
inhibition of intracellular mRNA positioning
inhibition of mRNA localization, intracellular
inhibition of mRNA positioning, intracellular
negative regulation of intracellular mRNA positioning
negative regulation of mRNA positioning, intracellular
negative regulation of intracellular mRNA localization
Any process that activates or increases the frequency, rate or extent of intracellular mRNA localization.
positive regulation of establishment and maintenance of intracellular RNA localization
positive regulation of intracellular mRNA localisation
positive regulation of mRNA localization, intracellular
up regulation of establishment and maintenance of intracellular RNA localization
up regulation of intracellular mRNA localisation
up regulation of intracellular mRNA localization
up regulation of mRNA localization, intracellular
up-regulation of establishment and maintenance of intracellular RNA localization
up-regulation of intracellular mRNA localisation
up-regulation of intracellular mRNA localization
up-regulation of mRNA localization, intracellular
upregulation of establishment and maintenance of intracellular RNA localization
upregulation of intracellular mRNA localisation
upregulation of intracellular mRNA localization
upregulation of mRNA localization, intracellular
activation of establishment and maintenance of intracellular RNA localization
activation of intracellular mRNA localisation
activation of intracellular mRNA localization
activation of intracellular mRNA positioning
activation of mRNA localization, intracellular
activation of mRNA positioning, intracellular
positive regulation of intracellular mRNA positioning
positive regulation of mRNA positioning, intracellular
up regulation of intracellular mRNA positioning
up regulation of mRNA positioning, intracellular
up-regulation of intracellular mRNA positioning
up-regulation of mRNA positioning, intracellular
upregulation of intracellular mRNA positioning
upregulation of mRNA positioning, intracellular
positive regulation of intracellular mRNA localization
Any process that activates or increases the frequency, rate or extent of protein refolding.
activation of heat shock protein activity
positive regulation of heat shock protein activity
up regulation of heat shock protein activity
up-regulation of heat shock protein activity
upregulation of heat shock protein activity
positive regulation of protein refolding
Interacting selectively and non-covalently with prostaglandin.
Interacting selectively and non-covalently with advanced glycation end-product.
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.
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.
cellular response to monosodium L-glutamate
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.
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.
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.
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.
The directed movement of ATP out of a cell or organelle.
Interacting selectively and non-covalently with alpha-aminoacyl-tRNA.
Any process that stops, prevents or reduces the frequency, rate or extent of type B pancreatic cell proliferation.
down regulation of pancreatic B cell proliferation
down regulation of pancreatic beta cell proliferation
down regulation of type B pancreatic cell proliferation
down-regulation of pancreatic B cell proliferation
down-regulation of pancreatic beta cell proliferation
down-regulation of type B pancreatic cell proliferation
downregulation of pancreatic B cell proliferation
downregulation of pancreatic beta cell proliferation
downregulation of type B pancreatic cell proliferation
negative regulation of pancreatic B cell proliferation
negative regulation of pancreatic beta cell proliferation
inhibition of pancreatic B cell proliferation
inhibition of pancreatic beta cell proliferation
inhibition of type B pancreatic cell proliferation
negative regulation of type B pancreatic cell proliferation
Any process that activates or increases the frequency, rate or extent of type B pancreatic cell proliferation.
positive regulation of pancreatic B cell proliferation
positive regulation of pancreatic beta cell proliferation
up regulation of pancreatic B cell proliferation
up regulation of pancreatic beta cell proliferation
up regulation of type B pancreatic cell proliferation
up-regulation of pancreatic B cell proliferation
up-regulation of pancreatic beta cell proliferation
up-regulation of type B pancreatic cell proliferation
upregulation of pancreatic B cell proliferation
upregulation of pancreatic beta cell proliferation
upregulation of type B pancreatic cell proliferation
activation of pancreatic B cell proliferation
activation of pancreatic beta cell proliferation
activation of type B pancreatic cell proliferation
positive regulation of type B pancreatic cell proliferation
Any process that modulates the frequency, rate or extent of acinar cell proliferation.
regulation of acinous cell proliferation
Any process that stops, prevents or reduces the frequency, rate or extent of acinar cell proliferation.
down regulation of acinar cell proliferation
down regulation of acinic cell proliferation
down regulation of acinous cell proliferation
down-regulation of acinar cell proliferation
down-regulation of acinic cell proliferation
down-regulation of acinous cell proliferation
downregulation of acinar cell proliferation
downregulation of acinic cell proliferation
downregulation of acinous cell proliferation
negative regulation of acinic cell proliferation
negative regulation of acinous cell proliferation
inhibition of acinous cell proliferation
negative regulation of acinar cell proliferation
Any process that activates or increases the frequency, rate or extent of acinar cell proliferation.
positive regulation of acinic cell proliferation
positive regulation of acinous cell proliferation
up regulation of acinar cell proliferation
up regulation of acinic cell proliferation
up regulation of acinous cell proliferation
up-regulation of acinar cell proliferation
up-regulation of acinic cell proliferation
up-regulation of acinous cell proliferation
upregulation of acinar cell proliferation
upregulation of acinic cell proliferation
upregulation of acinous cell proliferation
activation of acinous cell proliferation
positive regulation of acinar cell proliferation
Any process that modulates the frequency, rate or extent of protein localization to cell-cell adherens junction.
regulation of protein localisation in cell-cell adherens junction
regulation of protein localisation to cell-cell adherens junction
regulation of protein localization in cell-cell adherens junction
regulation of protein localization to cell-cell adherens junction
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to cell-cell adherens junction.
down regulation of protein localisation in cell-cell adherens junction
down regulation of protein localisation to cell-cell adherens junction
down regulation of protein localization in cell-cell adherens junction
down regulation of protein localization to cell-cell adherens junction
down-regulation of protein localisation in cell-cell adherens junction
down-regulation of protein localisation to cell-cell adherens junction
down-regulation of protein localization in cell-cell adherens junction
down-regulation of protein localization to cell-cell adherens junction
downregulation of protein localisation in cell-cell adherens junction
downregulation of protein localisation to cell-cell adherens junction
downregulation of protein localization in cell-cell adherens junction
downregulation of protein localization to cell-cell adherens junction
negative regulation of protein localisation in cell-cell adherens junction
negative regulation of protein localisation to cell-cell adherens junction
negative regulation of protein localization in cell-cell adherens junction
inhibition of protein localisation in cell-cell adherens junction
inhibition of protein localisation to cell-cell adherens junction
inhibition of protein localization in cell-cell adherens junction
inhibition of protein localization to cell-cell adherens junction
negative regulation of protein localization to cell-cell adherens junction
Any process that activates or increases the frequency, rate or extent of protein localization to cell-cell adherens junction.
positive regulation of protein localisation in cell-cell adherens junction
positive regulation of protein localisation to cell-cell adherens junction
positive regulation of protein localization in cell-cell adherens junction
up regulation of protein localisation in cell-cell adherens junction
up regulation of protein localisation to cell-cell adherens junction
up regulation of protein localization in cell-cell adherens junction
up regulation of protein localization to cell-cell adherens junction
up-regulation of protein localisation in cell-cell adherens junction
up-regulation of protein localisation to cell-cell adherens junction
up-regulation of protein localization in cell-cell adherens junction
up-regulation of protein localization to cell-cell adherens junction
upregulation of protein localisation in cell-cell adherens junction
upregulation of protein localisation to cell-cell adherens junction
upregulation of protein localization in cell-cell adherens junction
upregulation of protein localization to cell-cell adherens junction
activation of protein localisation in cell-cell adherens junction
activation of protein localisation to cell-cell adherens junction
activation of protein localization in cell-cell adherens junction
activation of protein localization to cell-cell adherens junction
positive regulation of protein localization to cell-cell adherens junction
Any process that modulates the frequency, rate or extent of vascular smooth muscle cell proliferation.
regulation of vascular smooth muscle cell proliferation
Any process that stops, prevents or reduces the frequency, rate or extent of vascular smooth muscle cell proliferation.
down regulation of vascular smooth muscle cell proliferation
down-regulation of vascular smooth muscle cell proliferation
downregulation of vascular smooth muscle cell proliferation
negative regulation of VSMC proliferation
inhibition of vascular smooth muscle cell proliferation
negative regulation of vascular smooth muscle cell proliferation
Any process that activates or increases the frequency, rate or extent of vascular smooth muscle cell proliferation.
positive regulation of VSMC proliferation
up regulation of vascular smooth muscle cell proliferation
up-regulation of vascular smooth muscle cell proliferation
upregulation of vascular smooth muscle cell proliferation
activation of vascular smooth muscle cell proliferation
positive regulation of vascular smooth muscle cell proliferation
Interacting selectively and non-covalently with a beta-catenin destruction complex.
Axin-APC-beta-catenin-GSK3B complex binding
beta-catenin degradation complex binding
beta-catenin destruction complex binding
Any process that modulates the frequency, rate or extent of protein localization to nucleolus.
regulation of protein localisation in nucleolus
regulation of protein localisation to nucleolus
regulation of protein localization in nucleolus
regulation of protein localization to nucleolus
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to nucleolus.
down regulation of protein localisation in nucleolus
down regulation of protein localisation to nucleolus
down regulation of protein localization in nucleolus
down regulation of protein localization to nucleolus
down-regulation of protein localisation in nucleolus
down-regulation of protein localisation to nucleolus
down-regulation of protein localization in nucleolus
down-regulation of protein localization to nucleolus
downregulation of protein localisation in nucleolus
downregulation of protein localisation to nucleolus
downregulation of protein localization in nucleolus
downregulation of protein localization to nucleolus
negative regulation of protein localisation in nucleolus
negative regulation of protein localisation to nucleolus
negative regulation of protein localization in nucleolus
inhibition of protein localisation in nucleolus
inhibition of protein localisation to nucleolus
inhibition of protein localization in nucleolus
inhibition of protein localization to nucleolus
negative regulation of protein localization to nucleolus
Any process that activates or increases the frequency, rate or extent of protein localization to nucleolus.
positive regulation of protein localisation in nucleolus
positive regulation of protein localisation to nucleolus
positive regulation of protein localization in nucleolus
up regulation of protein localisation in nucleolus
up regulation of protein localisation to nucleolus
up regulation of protein localization in nucleolus
up regulation of protein localization to nucleolus
up-regulation of protein localisation in nucleolus
up-regulation of protein localisation to nucleolus
up-regulation of protein localization in nucleolus
up-regulation of protein localization to nucleolus
upregulation of protein localisation in nucleolus
upregulation of protein localisation to nucleolus
upregulation of protein localization in nucleolus
upregulation of protein localization to nucleolus
activation of protein localisation in nucleolus
activation of protein localisation to nucleolus
activation of protein localization in nucleolus
activation of protein localization to nucleolus
positive regulation of protein localization to nucleolus
Interacting selectively and non-covalently with octanoic acid.
Interacting selectively and non-covalently with all-trans-retinol.
Interacting selectively and non-covalently with isopentadecanoic acid.
Any process that modulates the frequency, rate or extent of protein localization to cell cortex.
regulation of protein localisation to cell cortex
An example is cye-1 in C. elegans, UniProt ID O01501 in PMID:17115027.
regulation of protein localization to cell cortex
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to cell cortex.
down regulation of protein localisation to cell cortex
down regulation of protein localization to cell cortex
down-regulation of protein localisation to cell cortex
down-regulation of protein localization to cell cortex
downregulation of protein localisation to cell cortex
downregulation of protein localization to cell cortex
negative regulation of protein localisation to cell cortex
inhibition of protein localisation to cell cortex
inhibition of protein localization to cell cortex
negative regulation of protein localization to cell cortex
Any process that activates or increases the frequency, rate or extent of protein localization to cell cortex.
positive regulation of protein localisation to cell cortex
up regulation of protein localisation to cell cortex
up regulation of protein localization to cell cortex
up-regulation of protein localisation to cell cortex
up-regulation of protein localization to cell cortex
upregulation of protein localisation to cell cortex
upregulation of protein localization to cell cortex
activation of protein localisation to cell cortex
activation of protein localization to cell cortex
positive regulation of protein localization to cell cortex
Any process that modulates the frequency, rate or extent of protein localization to centrosome.
regulation of protein localisation to centrosome
An example is cdk-2 in C. elegans (UniProt ID O61847) in PMID:17115027 (inferred from mutant phenotype).
regulation of protein localization to centrosome
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to centrosome.
down regulation of protein localisation to centrosome
down regulation of protein localization to centrosome
down-regulation of protein localisation to centrosome
down-regulation of protein localization to centrosome
downregulation of protein localisation to centrosome
downregulation of protein localization to centrosome
negative regulation of protein localisation to centrosome
inhibition of protein localisation to centrosome
inhibition of protein localization to centrosome
negative regulation of protein localization to centrosome
Any process that activates or increases the frequency, rate or extent of protein localization to centrosome.
positive regulation of protein localisation to centrosome
up regulation of protein localisation to centrosome
up regulation of protein localization to centrosome
up-regulation of protein localisation to centrosome
up-regulation of protein localization to centrosome
upregulation of protein localisation to centrosome
upregulation of protein localization to centrosome
activation of protein localisation to centrosome
activation of protein localization to centrosome
positive regulation of protein localization to centrosome
Any process that modulates the frequency, rate or extent of dense core granule transport.
regulation of dense core vesicle transport
cdk-5 in C.elegans (G5ECH7) in PMID:22699897 (inferred from mutant phenotype).
regulation of dense core granule transport
Any process that stops, prevents or reduces the frequency, rate or extent of dense core granule transport.
down regulation of dense core granule transport
down regulation of dense core vesicle transport
down-regulation of dense core granule transport
down-regulation of dense core vesicle transport
downregulation of dense core granule transport
downregulation of dense core vesicle transport
negative regulation of dense core vesicle transport
inhibition of dense core granule transport
inhibition of dense core vesicle transport
negative regulation of dense core granule transport
Any process that activates or increases the frequency, rate or extent of dense core granule transport.
positive regulation of dense core vesicle transport
up regulation of dense core granule transport
up regulation of dense core vesicle transport
up-regulation of dense core granule transport
up-regulation of dense core vesicle transport
upregulation of dense core granule transport
upregulation of dense core vesicle transport
activation of dense core granule transport
activation of dense core vesicle transport
positive regulation of dense core granule transport
Any process that modulates the frequency, rate or extent of protein localization to chromosome, telomeric region.
regulation of protein localisation to chromosome, telomeric region
regulation of protein localization to telomere
regulation of protein localization to chromosome, telomeric region
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to chromosome, telomeric region.
down regulation of protein localisation to chromosome, telomeric region
down regulation of protein localization to chromosome, telomeric region
down regulation of protein localization to telomere
down-regulation of protein localisation to chromosome, telomeric region
down-regulation of protein localization to chromosome, telomeric region
down-regulation of protein localization to telomere
downregulation of protein localisation to chromosome, telomeric region
downregulation of protein localization to chromosome, telomeric region
downregulation of protein localization to telomere
negative regulation of protein localisation to chromosome, telomeric region
negative regulation of protein localization to telomere
inhibition of protein localisation to chromosome, telomeric region
inhibition of protein localization to chromosome, telomeric region
inhibition of protein localization to telomere
negative regulation of protein localization to chromosome, telomeric region
Any process that activates or increases the frequency, rate or extent of protein localization to chromosome, telomeric region.
positive regulation of protein localisation to chromosome, telomeric region
positive regulation of protein localization to telomere
up regulation of protein localisation to chromosome, telomeric region
up regulation of protein localization to chromosome, telomeric region
up regulation of protein localization to telomere
up-regulation of protein localisation to chromosome, telomeric region
up-regulation of protein localization to chromosome, telomeric region
up-regulation of protein localization to telomere
upregulation of protein localisation to chromosome, telomeric region
upregulation of protein localization to chromosome, telomeric region
upregulation of protein localization to telomere
activation of protein localisation to chromosome, telomeric region
activation of protein localization to chromosome, telomeric region
activation of protein localization to telomere
positive regulation of protein localization to chromosome, telomeric region
Interacting selectively and non-covalently with a TORC2 complex.
rapamycin and nutrient-insensitive TOR complex binding
Interacting selectively and non-covalently with a TORC2 complex, a protein complex that mediates the phosphorylation of protein kinase B
Any process that stops, prevents or reduces the frequency, rate or extent of establishment of protein localization to telomere.
down regulation of establishment of protein localisation to telomere
down regulation of establishment of protein localization to chromosome, telomeric region
down regulation of establishment of protein localization to telomere
down-regulation of establishment of protein localisation to telomere
down-regulation of establishment of protein localization to chromosome, telomeric region
down-regulation of establishment of protein localization to telomere
downregulation of establishment of protein localisation to telomere
downregulation of establishment of protein localization to chromosome, telomeric region
downregulation of establishment of protein localization to telomere
negative regulation of establishment of protein localisation to telomere
negative regulation of establishment of protein localization to chromosome, telomeric region
inhibition of establishment of protein localisation to telomere
inhibition of establishment of protein localization to chromosome, telomeric region
inhibition of establishment of protein localization to telomere
negative regulation of establishment of protein localization to telomere
Any process that activates or increases the frequency, rate or extent of establishment of protein localization to telomere.
positive regulation of establishment of protein localisation to telomere
positive regulation of establishment of protein localization to chromosome, telomeric region
up regulation of establishment of protein localisation to telomere
up regulation of establishment of protein localization to chromosome, telomeric region
up regulation of establishment of protein localization to telomere
up-regulation of establishment of protein localisation to telomere
up-regulation of establishment of protein localization to chromosome, telomeric region
up-regulation of establishment of protein localization to telomere
upregulation of establishment of protein localisation to telomere
upregulation of establishment of protein localization to chromosome, telomeric region
upregulation of establishment of protein localization to telomere
activation of establishment of protein localisation to telomere
activation of establishment of protein localization to chromosome, telomeric region
activation of establishment of protein localization to telomere
positive regulation of establishment of protein localization to telomere
Interacting selectively and non-covalently with a proteasome core complex.
Interacting selectively and non-covalently with a proteasome regulatory particle.
PA700-dependent proteasome activator binding
Any process that modulates the frequency, rate or extent of protein localization to Cajal body.
regulation of protein localisation in Cajal body
regulation of protein localisation to Cajal body
regulation of protein localization in Cajal body
regulation of protein localization to Cajal body
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to Cajal body.
down regulation of protein localisation in Cajal body
down regulation of protein localisation to Cajal body
down regulation of protein localization in Cajal body
down regulation of protein localization to Cajal body
down-regulation of protein localisation in Cajal body
down-regulation of protein localisation to Cajal body
down-regulation of protein localization in Cajal body
down-regulation of protein localization to Cajal body
downregulation of protein localisation in Cajal body
downregulation of protein localisation to Cajal body
downregulation of protein localization in Cajal body
downregulation of protein localization to Cajal body
negative regulation of protein localisation in Cajal body
negative regulation of protein localisation to Cajal body
negative regulation of protein localization in Cajal body
inhibition of protein localisation in Cajal body
inhibition of protein localisation to Cajal body
inhibition of protein localization in Cajal body
inhibition of protein localization to Cajal body
negative regulation of protein localization to Cajal body
Any process that activates or increases the frequency, rate or extent of protein localization to Cajal body.
positive regulation of protein localisation in Cajal body
positive regulation of protein localisation to Cajal body
positive regulation of protein localization in Cajal body
up regulation of protein localisation in Cajal body
up regulation of protein localisation to Cajal body
up regulation of protein localization in Cajal body
up regulation of protein localization to Cajal body
up-regulation of protein localisation in Cajal body
up-regulation of protein localisation to Cajal body
up-regulation of protein localization in Cajal body
up-regulation of protein localization to Cajal body
upregulation of protein localisation in Cajal body
upregulation of protein localisation to Cajal body
upregulation of protein localization in Cajal body
upregulation of protein localization to Cajal body
activation of protein localisation in Cajal body
activation of protein localisation to Cajal body
activation of protein localization in Cajal body
activation of protein localization to Cajal body
positive regulation of protein localization to Cajal body
Any process that stops, prevents or reduces the frequency, rate or extent of calcium ion transmembrane transport via high voltage-gated calcium channel.
down regulation of generation of L-type calcium current
down-regulation of generation of L-type calcium current
downregulation of generation of L-type calcium current
inhibition of generation of L-type calcium current
negative regulation of generation of L-type calcium current
negative regulation of calcium ion transmembrane transport via high voltage-gated calcium channel
Any process that activates or increases the frequency, rate or extent of calcium ion transmembrane transport via high voltage-gated calcium channel.
up regulation of generation of L-type calcium current
up-regulation of generation of L-type calcium current
upregulation of generation of L-type calcium current
activation of generation of L-type calcium current
positive regulation of generation of L-type calcium current
positive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel
Any process that modulates the frequency, rate or extent of hepatic stellate cell proliferation.
regulation of hepatic perisinusoidal cell proliferation
regulation of perisinusoidal cell proliferation
regulation of hepatic stellate cell proliferation
Any process that stops, prevents or reduces the frequency, rate or extent of hepatic stellate cell proliferation.
down regulation of Ito cell proliferation
down regulation of hepatic perisinusoidal cell proliferation
down regulation of hepatic stellate cell proliferation
down regulation of perisinusoidal cell proliferation
down-regulation of Ito cell proliferation
down-regulation of hepatic perisinusoidal cell proliferation
down-regulation of hepatic stellate cell proliferation
down-regulation of perisinusoidal cell proliferation
downregulation of Ito cell proliferation
downregulation of hepatic perisinusoidal cell proliferation
downregulation of hepatic stellate cell proliferation
downregulation of perisinusoidal cell proliferation
negative regulation of Ito cell proliferation
negative regulation of hepatic perisinusoidal cell proliferation
negative regulation of perisinusoidal cell proliferation
inhibition of hepatic perisinusoidal cell proliferation
inhibition of hepatic stellate cell proliferation
inhibition of perisinusoidal cell proliferation
negative regulation of hepatic stellate cell proliferation
Any process that activates or increases the frequency, rate or extent of hepatic stellate cell proliferation.
positive regulation of Ito cell proliferation
positive regulation of hepatic perisinusoidal cell proliferation
positive regulation of perisinusoidal cell proliferation
up regulation of hepatic perisinusoidal cell proliferation
up regulation of hepatic stellate cell proliferation
up regulation of perisinusoidal cell proliferation
up-regulation of hepatic perisinusoidal cell proliferation
up-regulation of hepatic stellate cell proliferation
up-regulation of perisinusoidal cell proliferation
upregulation of hepatic perisinusoidal cell proliferation
upregulation of hepatic stellate cell proliferation
upregulation of perisinusoidal cell proliferation
activation of hepatic perisinusoidal cell proliferation
activation of hepatic stellate cell proliferation
activation of perisinusoidal cell proliferation
positive regulation of hepatic stellate cell proliferation
Any process that modulates the frequency, rate or extent of establishment of RNA localization to telomere.
regulation of establishment of RNA localisation to telomere
regulation of establishment of RNA localization to telomere
Any process that stops, prevents or reduces the frequency, rate or extent of establishment of RNA localization to telomere.
down regulation of establishment of RNA localisation to telomere
down regulation of establishment of RNA localization to telomere
down-regulation of establishment of RNA localisation to telomere
down-regulation of establishment of RNA localization to telomere
downregulation of establishment of RNA localisation to telomere
downregulation of establishment of RNA localization to telomere
negative regulation of establishment of RNA localisation to telomere
inhibition of establishment of RNA localisation to telomere
inhibition of establishment of RNA localization to telomere
negative regulation of establishment of RNA localization to telomere
Any process that activates or increases the frequency, rate or extent of establishment of RNA localization to telomere.
positive regulation of establishment of RNA localisation to telomere
up regulation of establishment of RNA localisation to telomere
up regulation of establishment of RNA localization to telomere
up-regulation of establishment of RNA localisation to telomere
up-regulation of establishment of RNA localization to telomere
upregulation of establishment of RNA localisation to telomere
upregulation of establishment of RNA localization to telomere
activation of establishment of RNA localisation to telomere
activation of establishment of RNA localization to telomere
positive regulation of establishment of RNA localization to telomere
Any process that modulates the frequency, rate or extent of establishment of the localization of a protein-containing macromolecular complex to a telomere.
regulation of establishment of macromolecular complex localisation to telomere
regulation of establishment of macromolecular complex localization to telomere
regulation of establishment of protein-containing complex localization to telomere
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.
down regulation of establishment of macromolecular complex localisation to telomere
down regulation of establishment of macromolecular complex localization to telomere
down-regulation of establishment of macromolecular complex localisation to telomere
down-regulation of establishment of macromolecular complex localization to telomere
downregulation of establishment of macromolecular complex localisation to telomere
downregulation of establishment of macromolecular complex localization to telomere
negative regulation of establishment of macromolecular complex localisation to telomere
inhibition of establishment of macromolecular complex localisation to telomere
inhibition of establishment of macromolecular complex localization to telomere
negative regulation of establishment of macromolecular complex localization to telomere
negative regulation of establishment of protein-containing complex localization to telomere
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.
positive regulation of establishment of macromolecular complex localisation to telomere
up regulation of establishment of macromolecular complex localisation to telomere
up regulation of establishment of macromolecular complex localization to telomere
up-regulation of establishment of macromolecular complex localisation to telomere
up-regulation of establishment of macromolecular complex localization to telomere
upregulation of establishment of macromolecular complex localisation to telomere
upregulation of establishment of macromolecular complex localization to telomere
activation of establishment of macromolecular complex localisation to telomere
activation of establishment of macromolecular complex localization to telomere
positive regulation of establishment of macromolecular complex localization to telomere
positive regulation of establishment of protein-containing complex localization to telomere
Interacting selectively and non-covalently with an MCM complex.
mini-chromosome maintenance complex binding
Any process that stops, prevents or reduces the frequency, rate or extent of establishment of protein localization.
down regulation of establishment of protein localisation
down regulation of establishment of protein localization
down-regulation of establishment of protein localisation
down-regulation of establishment of protein localization
downregulation of establishment of protein localisation
downregulation of establishment of protein localization
negative regulation of establishment of protein localisation
negative regulation of protein positioning
negative regulation of protein recruitment
inhibition of establishment of protein localisation
inhibition of establishment of protein localization
negative regulation of establishment of protein localization
Any process that activates or increases the frequency, rate or extent of establishment of protein localization.
positive regulation of establishment of protein localisation
positive regulation of protein positioning
positive regulation of protein recruitment
up regulation of establishment of protein localisation
up regulation of establishment of protein localization
up-regulation of establishment of protein localisation
up-regulation of establishment of protein localization
upregulation of establishment of protein localisation
upregulation of establishment of protein localization
activation of establishment of protein localisation
activation of establishment of protein localization
positive regulation of establishment of protein localization
Any process that modulates the frequency, rate or extent of leukocyte adhesion to vascular endothelial cell.
regulation of leukocyte adhesion to vascular endothelial cell
Any process that stops, prevents or reduces the frequency, rate or extent of leukocyte adhesion to vascular endothelial cell.
down regulation of leukocyte adhesion to vascular endothelial cell
down-regulation of leukocyte adhesion to vascular endothelial cell
downregulation of leukocyte adhesion to vascular endothelial cell
inhibition of leukocyte adhesion to vascular endothelial cell
negative regulation of leukocyte adhesion to vascular endothelial cell
Any process that activates or increases the frequency, rate or extent of leukocyte adhesion to vascular endothelial cell.
up regulation of leukocyte adhesion to vascular endothelial cell
up-regulation of leukocyte adhesion to vascular endothelial cell
upregulation of leukocyte adhesion to vascular endothelial cell
activation of leukocyte adhesion to vascular endothelial cell
positive regulation of leukocyte adhesion to vascular endothelial cell
Any process that modulates the frequency, rate or extent of leukocyte adhesion to arterial endothelial cell.
regulation of leukocyte adhesion to arterial endothelial cell
Any process that stops, prevents or reduces the frequency, rate or extent of leukocyte adhesion to arterial endothelial cell.
down regulation of leukocyte adhesion to arterial endothelial cell
down-regulation of leukocyte adhesion to arterial endothelial cell
downregulation of leukocyte adhesion to arterial endothelial cell
inhibition of leukocyte adhesion to arterial endothelial cell
negative regulation of leukocyte adhesion to arterial endothelial cell
Any process that activates or increases the frequency, rate or extent of leukocyte adhesion to arterial endothelial cell.
up regulation of leukocyte adhesion to arterial endothelial cell
up-regulation of leukocyte adhesion to arterial endothelial cell
upregulation of leukocyte adhesion to arterial endothelial cell
activation of leukocyte adhesion to arterial endothelial cell
positive regulation of leukocyte adhesion to arterial endothelial cell
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.
Interacting selectively and non-covalently with guanosine.
Any process that modulates the frequency, rate or extent of voltage-gated sodium channel activity.
regulation of voltage gated sodium channel activity
regulation of voltage-dependent sodium channel activity
regulation of voltage-gated sodium ion channel activity
regulation of voltage-sensitive sodium channel
regulation of voltage-gated sodium channel activity
Any process that stops, prevents or reduces the frequency, rate or extent of voltage-gated sodium channel activity.
down regulation of voltage gated sodium channel activity
down regulation of voltage-dependent sodium channel activity
down regulation of voltage-gated sodium channel activity
down regulation of voltage-gated sodium ion channel activity
down regulation of voltage-sensitive sodium channel
down-regulation of voltage gated sodium channel activity
down-regulation of voltage-dependent sodium channel activity
down-regulation of voltage-gated sodium channel activity
down-regulation of voltage-gated sodium ion channel activity
down-regulation of voltage-sensitive sodium channel
downregulation of voltage gated sodium channel activity
downregulation of voltage-dependent sodium channel activity
downregulation of voltage-gated sodium channel activity
downregulation of voltage-gated sodium ion channel activity
downregulation of voltage-sensitive sodium channel
negative regulation of voltage gated sodium channel activity
negative regulation of voltage-dependent sodium channel activity
negative regulation of voltage-gated sodium ion channel activity
negative regulation of voltage-sensitive sodium channel
inhibition of voltage gated sodium channel activity
inhibition of voltage-dependent sodium channel activity
inhibition of voltage-gated sodium channel activity
inhibition of voltage-gated sodium ion channel activity
inhibition of voltage-sensitive sodium channel
negative regulation of voltage-gated sodium channel activity
Any process that activates or increases the frequency, rate or extent of voltage-gated sodium channel activity.
positive regulation of voltage gated sodium channel activity
positive regulation of voltage-dependent sodium channel activity
positive regulation of voltage-gated sodium ion channel activity
positive regulation of voltage-sensitive sodium channel
up regulation of voltage gated sodium channel activity
up regulation of voltage-dependent sodium channel activity
up regulation of voltage-gated sodium channel activity
up regulation of voltage-gated sodium ion channel activity
up regulation of voltage-sensitive sodium channel
up-regulation of voltage gated sodium channel activity
up-regulation of voltage-dependent sodium channel activity
up-regulation of voltage-gated sodium channel activity
up-regulation of voltage-gated sodium ion channel activity
up-regulation of voltage-sensitive sodium channel
upregulation of voltage gated sodium channel activity
upregulation of voltage-dependent sodium channel activity
upregulation of voltage-gated sodium channel activity
upregulation of voltage-gated sodium ion channel activity
upregulation of voltage-sensitive sodium channel
activation of voltage gated sodium channel activity
activation of voltage-dependent sodium channel activity
activation of voltage-gated sodium channel activity
activation of voltage-gated sodium ion channel activity
activation of voltage-sensitive sodium channel
positive regulation of voltage-gated sodium channel activity
Any process that modulates the frequency, rate or extent of protein localization to phagocytic vesicle.
regulation of protein localisation in phagocytic vesicle
regulation of protein localisation to phagocytic vesicle
regulation of protein localisation to phagosome
regulation of protein localization in phagocytic vesicle
regulation of protein recruitment to phagosome
regulation of protein localization to phagocytic vesicle
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to phagocytic vesicle.
down regulation of protein localisation in phagocytic vesicle
down regulation of protein localisation to phagocytic vesicle
down regulation of protein localisation to phagosome
down regulation of protein localization in phagocytic vesicle
down regulation of protein localization to phagocytic vesicle
down regulation of protein recruitment to phagosome
down-regulation of protein localisation in phagocytic vesicle
down-regulation of protein localisation to phagocytic vesicle
down-regulation of protein localisation to phagosome
down-regulation of protein localization in phagocytic vesicle
down-regulation of protein localization to phagocytic vesicle
down-regulation of protein recruitment to phagosome
downregulation of protein localisation in phagocytic vesicle
downregulation of protein localisation to phagocytic vesicle
downregulation of protein localisation to phagosome
downregulation of protein localization in phagocytic vesicle
downregulation of protein localization to phagocytic vesicle
downregulation of protein recruitment to phagosome
negative regulation of protein localisation in phagocytic vesicle
negative regulation of protein localisation to phagocytic vesicle
negative regulation of protein localisation to phagosome
negative regulation of protein localization in phagocytic vesicle
negative regulation of protein recruitment to phagosome
inhibition of protein localisation in phagocytic vesicle
inhibition of protein localisation to phagocytic vesicle
inhibition of protein localisation to phagosome
inhibition of protein localization in phagocytic vesicle
inhibition of protein localization to phagocytic vesicle
inhibition of protein recruitment to phagosome
negative regulation of protein localization to phagocytic vesicle
Any process that activates or increases the frequency, rate or extent of protein localization to phagocytic vesicle.
positive regulation of protein localisation in phagocytic vesicle
positive regulation of protein localisation to phagocytic vesicle
positive regulation of protein localisation to phagosome
positive regulation of protein localization in phagocytic vesicle
positive regulation of protein recruitment to phagosome
up regulation of protein localisation in phagocytic vesicle
up regulation of protein localisation to phagocytic vesicle
up regulation of protein localisation to phagosome
up regulation of protein localization in phagocytic vesicle
up regulation of protein localization to phagocytic vesicle
up regulation of protein recruitment to phagosome
up-regulation of protein localisation in phagocytic vesicle
up-regulation of protein localisation to phagocytic vesicle
up-regulation of protein localisation to phagosome
up-regulation of protein localization in phagocytic vesicle
up-regulation of protein localization to phagocytic vesicle
up-regulation of protein recruitment to phagosome
upregulation of protein localisation in phagocytic vesicle
upregulation of protein localisation to phagocytic vesicle
upregulation of protein localisation to phagosome
upregulation of protein localization in phagocytic vesicle
upregulation of protein localization to phagocytic vesicle
upregulation of protein recruitment to phagosome
activation of protein localisation in phagocytic vesicle
activation of protein localisation to phagocytic vesicle
activation of protein localisation to phagosome
activation of protein localization in phagocytic vesicle
activation of protein localization to phagocytic vesicle
activation of protein recruitment to phagosome
positive regulation of protein localization to phagocytic vesicle
Interacting selectively and non-covalently with a RISC complex.
Any process that modulates the frequency, rate or extent of proton-transporting ATP synthase activity, rotational mechanism.
regulation of H+-transporting ATP synthase activity
regulation of hydrogen ion translocating F-type ATPase activity
regulation of hydrogen ion transporting ATP synthase activity, rotational mechanism
regulation of hydrogen ion transporting two-sector ATPase activity
regulation of proton-transporting ATP synthase activity, rotational mechanism
Any process that stops, prevents or reduces the frequency, rate or extent of proton-transporting ATP synthase activity, rotational mechanism.
down regulation of H+-transporting ATP synthase activity
down regulation of hydrogen ion translocating F-type ATPase activity
down regulation of hydrogen ion transporting ATP synthase activity, rotational mechanism
down regulation of hydrogen ion transporting two-sector ATPase activity
down regulation of proton-transporting ATP synthase activity, rotational mechanism
down-regulation of H+-transporting ATP synthase activity
down-regulation of hydrogen ion translocating F-type ATPase activity
down-regulation of hydrogen ion transporting ATP synthase activity, rotational mechanism
down-regulation of hydrogen ion transporting two-sector ATPase activity
down-regulation of proton-transporting ATP synthase activity, rotational mechanism
downregulation of H+-transporting ATP synthase activity
downregulation of hydrogen ion translocating F-type ATPase activity
downregulation of hydrogen ion transporting ATP synthase activity, rotational mechanism
downregulation of hydrogen ion transporting two-sector ATPase activity
downregulation of proton-transporting ATP synthase activity, rotational mechanism
negative regulation of H+-transporting ATP synthase activity
negative regulation of hydrogen ion translocating F-type ATPase activity
negative regulation of hydrogen ion transporting ATP synthase activity, rotational mechanism
negative regulation of hydrogen ion transporting two-sector ATPase activity
inhibition of H+-transporting ATP synthase activity
inhibition of hydrogen ion translocating F-type ATPase activity
inhibition of hydrogen ion transporting ATP synthase activity, rotational mechanism
inhibition of hydrogen ion transporting two-sector ATPase activity
inhibition of proton-transporting ATP synthase activity, rotational mechanism
negative regulation of proton-transporting ATP synthase activity, rotational mechanism
Any process that activates or increases the frequency, rate or extent of proton-transporting ATP synthase activity, rotational mechanism.
positive regulation of H+-transporting ATP synthase activity
positive regulation of hydrogen ion translocating F-type ATPase activity
positive regulation of hydrogen ion transporting ATP synthase activity, rotational mechanism
positive regulation of hydrogen ion transporting two-sector ATPase activity
up regulation of H+-transporting ATP synthase activity
up regulation of hydrogen ion translocating F-type ATPase activity
up regulation of hydrogen ion transporting ATP synthase activity, rotational mechanism
up regulation of hydrogen ion transporting two-sector ATPase activity
up regulation of proton-transporting ATP synthase activity, rotational mechanism
up-regulation of H+-transporting ATP synthase activity
up-regulation of hydrogen ion translocating F-type ATPase activity
up-regulation of hydrogen ion transporting ATP synthase activity, rotational mechanism
up-regulation of hydrogen ion transporting two-sector ATPase activity
up-regulation of proton-transporting ATP synthase activity, rotational mechanism
upregulation of H+-transporting ATP synthase activity
upregulation of hydrogen ion translocating F-type ATPase activity
upregulation of hydrogen ion transporting ATP synthase activity, rotational mechanism
upregulation of hydrogen ion transporting two-sector ATPase activity
upregulation of proton-transporting ATP synthase activity, rotational mechanism
activation of H+-transporting ATP synthase activity
activation of hydrogen ion translocating F-type ATPase activity
activation of hydrogen ion transporting ATP synthase activity, rotational mechanism
activation of hydrogen ion transporting two-sector ATPase activity
activation of proton-transporting ATP synthase activity, rotational mechanism
positive regulation of proton-transporting ATP synthase activity, rotational mechanism
Interacting selectively and non-covalently with a Swi5-Sfr1 complex.
Any process that modulates the frequency, rate or extent of protein localization to kinetochore.
regulation of protein localisation to kinetochore
regulation of condensin localization to kinetochore
regulation of protein localization to kinetochore
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to kinetochore.
down regulation of protein localisation to kinetochore
down regulation of protein localization to kinetochore
down-regulation of protein localisation to kinetochore
down-regulation of protein localization to kinetochore
downregulation of protein localisation to kinetochore
downregulation of protein localization to kinetochore
negative regulation of protein localisation to kinetochore
down regulation of condensin localization to kinetochore
down-regulation of condensin localization to kinetochore
downregulation of condensin localization to kinetochore
inhibition of condensin localization to kinetochore
inhibition of protein localisation to kinetochore
inhibition of protein localization to kinetochore
negative regulation of condensin localization to kinetochore
negative regulation of protein localization to kinetochore
Any process that activates or increases the frequency, rate or extent of protein localization to kinetochore.
positive regulation of protein localisation to kinetochore
up regulation of protein localisation to kinetochore
up regulation of protein localization to kinetochore
up-regulation of protein localisation to kinetochore
up-regulation of protein localization to kinetochore
upregulation of protein localisation to kinetochore
upregulation of protein localization to kinetochore
activation of condensin localization to kinetochore
activation of protein localisation to kinetochore
activation of protein localization to kinetochore
positive regulation of condensin localization to kinetochore
up regulation of condensin localization to kinetochore
up-regulation of condensin localization to kinetochore
upregulation of condensin localization to kinetochore
positive regulation of protein localization to kinetochore
Any process that modulates the frequency, rate or extent of protein localization to presynapse.
regulation of protein localisation in presynapse
regulation of protein localisation to presynapse
regulation of protein localization in presynapse
regulation of recruitment of presynaptic proteins
regulation of protein localization to presynapse
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to presynapse.
down regulation of protein localisation in presynapse
down regulation of protein localisation to presynapse
down regulation of protein localization in presynapse
down regulation of protein localization to presynapse
down regulation of recruitment of presynaptic proteins
down-regulation of protein localisation in presynapse
down-regulation of protein localisation to presynapse
down-regulation of protein localization in presynapse
down-regulation of protein localization to presynapse
down-regulation of recruitment of presynaptic proteins
downregulation of protein localisation in presynapse
downregulation of protein localisation to presynapse
downregulation of protein localization in presynapse
downregulation of protein localization to presynapse
downregulation of recruitment of presynaptic proteins
negative regulation of protein localisation in presynapse
negative regulation of protein localisation to presynapse
negative regulation of protein localization in presynapse
negative regulation of recruitment of presynaptic proteins
inhibition of protein localisation in presynapse
inhibition of protein localisation to presynapse
inhibition of protein localization in presynapse
inhibition of protein localization to presynapse
inhibition of recruitment of presynaptic proteins
negative regulation of protein localization to presynapse
Any process that activates or increases the frequency, rate or extent of protein localization to presynapse.
positive regulation of protein localisation in presynapse
positive regulation of protein localisation to presynapse
positive regulation of protein localization in presynapse
positive regulation of recruitment of presynaptic proteins
up regulation of protein localisation in presynapse
up regulation of protein localisation to presynapse
up regulation of protein localization in presynapse
up regulation of protein localization to presynapse
up regulation of recruitment of presynaptic proteins
up-regulation of protein localisation in presynapse
up-regulation of protein localisation to presynapse
up-regulation of protein localization in presynapse
up-regulation of protein localization to presynapse
up-regulation of recruitment of presynaptic proteins
upregulation of protein localisation in presynapse
upregulation of protein localisation to presynapse
upregulation of protein localization in presynapse
upregulation of protein localization to presynapse
upregulation of recruitment of presynaptic proteins
activation of protein localisation in presynapse
activation of protein localisation to presynapse
activation of protein localization in presynapse
activation of protein localization to presynapse
activation of recruitment of presynaptic proteins
positive regulation of protein localization to presynapse
Any regulation of protein localization to cell division site that is involved in cell separation after cytokinesis.
regulation of protein localisation to cell division site involved in cell separation after cytokinesis
regulation of protein localisation to cell division site involved in cell separation following cytokinesis
regulation of protein localisation to cell division site involved in mitotic cytokinetic cell separation
regulation of protein localisation to cell division site involved in cytokinetic cell separation
regulation of protein localization to cell division site involved in cell separation after cytokinesis
Interacting selectively and non-covalently with a retromer complex.
Any process that modulates the frequency, rate or extent of protein localization to membrane.
regulation of protein localisation in membrane
regulation of protein localization in membrane
regulation of protein localization to membrane
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to membrane.
down regulation of protein localisation in membrane
down regulation of protein localization in membrane
down regulation of protein localization to membrane
down-regulation of protein localisation in membrane
down-regulation of protein localization in membrane
down-regulation of protein localization to membrane
downregulation of protein localisation in membrane
downregulation of protein localization in membrane
downregulation of protein localization to membrane
negative regulation of protein localisation in membrane
negative regulation of protein localization in membrane
inhibition of protein localisation in membrane
inhibition of protein localization in membrane
inhibition of protein localization to membrane
negative regulation of protein localization to membrane
Any process that activates or increases the frequency, rate or extent of protein localization to membrane.
positive regulation of protein localisation in membrane
positive regulation of protein localization in membrane
up regulation of protein localisation in membrane
up regulation of protein localization in membrane
up regulation of protein localization to membrane
up-regulation of protein localisation in membrane
up-regulation of protein localization in membrane
up-regulation of protein localization to membrane
upregulation of protein localisation in membrane
upregulation of protein localization in membrane
upregulation of protein localization to membrane
activation of protein localisation in membrane
activation of protein localization in membrane
activation of protein localization to membrane
positive regulation of protein localization to membrane
Interacting selectively and non-covalently with acetyl-CoA.
Interacting selectively and non-covalently with a polysome.
Any process that modulates the frequency, rate or extent of protein localization to endoplasmic reticulum.
regulation of protein localisation in endoplasmic reticulum
regulation of protein localization in ER
regulation of protein localization in endoplasmic reticulum
regulation of protein localization to endoplasmic reticulum
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to endoplasmic reticulum.
down regulation of protein localisation in endoplasmic reticulum
down regulation of protein localization in ER
down regulation of protein localization in endoplasmic reticulum
down regulation of protein localization to endoplasmic reticulum
down-regulation of protein localisation in endoplasmic reticulum
down-regulation of protein localization in ER
down-regulation of protein localization in endoplasmic reticulum
down-regulation of protein localization to endoplasmic reticulum
downregulation of protein localisation in endoplasmic reticulum
downregulation of protein localization in ER
downregulation of protein localization in endoplasmic reticulum
downregulation of protein localization to endoplasmic reticulum
negative regulation of protein localisation in endoplasmic reticulum
negative regulation of protein localization in ER
negative regulation of protein localization in endoplasmic reticulum
inhibition of protein localisation in endoplasmic reticulum
inhibition of protein localization in ER
inhibition of protein localization in endoplasmic reticulum
inhibition of protein localization to endoplasmic reticulum
negative regulation of protein localization to endoplasmic reticulum
Any process that activates or increases the frequency, rate or extent of protein localization to endoplasmic reticulum.
positive regulation of protein localisation in endoplasmic reticulum
positive regulation of protein localization in ER
positive regulation of protein localization in endoplasmic reticulum
up regulation of protein localisation in endoplasmic reticulum
up regulation of protein localization in ER
up regulation of protein localization in endoplasmic reticulum
up regulation of protein localization to endoplasmic reticulum
up-regulation of protein localisation in endoplasmic reticulum
up-regulation of protein localization in ER
up-regulation of protein localization in endoplasmic reticulum
up-regulation of protein localization to endoplasmic reticulum
upregulation of protein localisation in endoplasmic reticulum
upregulation of protein localization in ER
upregulation of protein localization in endoplasmic reticulum
upregulation of protein localization to endoplasmic reticulum
activation of protein localisation in endoplasmic reticulum
activation of protein localization in ER
activation of protein localization in endoplasmic reticulum
activation of protein localization to endoplasmic reticulum
positive regulation of protein localization to endoplasmic reticulum
Any process that modulates the frequency, rate or extent of vascular endothelial cell proliferation.
regulation of vascular endothelial cell proliferation
Any process that stops, prevents or reduces the frequency, rate or extent of vascular endothelial cell proliferation.
down regulation of vascular endothelial cell proliferation
down-regulation of vascular endothelial cell proliferation
downregulation of vascular endothelial cell proliferation
inhibition of vascular endothelial cell proliferation
negative regulation of vascular endothelial cell proliferation
Any process that activates or increases the frequency, rate or extent of vascular endothelial cell proliferation.
up regulation of vascular endothelial cell proliferation
up-regulation of vascular endothelial cell proliferation
upregulation of vascular endothelial cell proliferation
activation of vascular endothelial cell proliferation
positive regulation of vascular endothelial cell proliferation
Interacting selectively and non-covalently with ganglioside GM1.
Interacting selectively and non-covalently with ganglioside GM2.
Interacting selectively and non-covalently with ganglioside GM3.
Interacting selectively and non-covalently with ganglioside GT1b.
Interacting selectively and non-covalently with ganglioside GP1c.
Interacting selectively and non-covalently with resveratrol.
Any process that modulates the frequency, rate or extent of protein localization to chromatin.
regulation of protein localisation to chromatin
regulation of protein localization to chromatin
Any process that modulates the frequency, rate or extent of calcium ion import across plasma membrane.
An example of this is PPP3CA in human (Q08209) in 17640527 (inferred from direct assay).
regulation of calcium ion import across plasma membrane
Any process that activates or increases the frequency, rate or extent of calcium ion import across plasma membrane.
up regulation of calcium ion import across plasma membrane
up-regulation of calcium ion import across plasma membrane
upregulation of calcium ion import across plasma membrane
activation of calcium ion import across plasma membrane
positive regulation of calcium ion import across plasma membrane
Any process that modulates the frequency, rate or extent of protein localization to endosome.
regulation of protein localisation in endosome
regulation of protein localization in endosome
regulation of protein localization to endosome
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to endosome.
down regulation of protein localisation in endosome
down regulation of protein localization in endosome
down regulation of protein localization to endosome
down-regulation of protein localisation in endosome
down-regulation of protein localization in endosome
down-regulation of protein localization to endosome
downregulation of protein localisation in endosome
downregulation of protein localization in endosome
downregulation of protein localization to endosome
negative regulation of protein localisation in endosome
negative regulation of protein localization in endosome
inhibition of protein localisation in endosome
inhibition of protein localization in endosome
inhibition of protein localization to endosome
negative regulation of protein localization to endosome
Any process that activates or increases the frequency, rate or extent of protein localization to endosome.
positive regulation of protein localisation in endosome
positive regulation of protein localization in endosome
up regulation of protein localisation in endosome
up regulation of protein localization in endosome
up regulation of protein localization to endosome
up-regulation of protein localisation in endosome
up-regulation of protein localization in endosome
up-regulation of protein localization to endosome
upregulation of protein localisation in endosome
upregulation of protein localization in endosome
upregulation of protein localization to endosome
activation of protein localisation in endosome
activation of protein localization in endosome
activation of protein localization to endosome
positive regulation of protein localization to endosome
Any mitochondrial calcium uptake that is involved in negative regulation of presynaptic cytosolic calcium concentration.
calcium ion transmembrane import into mitochondrion involved in negative regulation of presynaptic cytosolic calcium concentration
mitochondrial calcium uptake involved in negative regulation of presynaptic cytosolic calcium concentration
calcium import into the mitochondrion involved in negative regulation of presynaptic cytosolic calcium concentration
Interacting selectively and non-covalently with a SCF ubiquitin ligase complex.
Cul1-RING ubiquitin ligase complex binding
SCF complex substrate recognition subunit binding
Interacting selectively and non-covalently with a CCR4-NOT complex.
Interacting selectively and non-covalently with a MTREC complex.
Interacting selectively and non-covalently with 8-hydroxy-2'-deoxyguanosine an oxidized purine residue found in damaged DNA.
Any process that modulates the frequency, rate or extent of cellular response to manganese ion.
regulation of cellular response to manganese
regulation of cellular response to manganese ion
Any process that stops, prevents or reduces the frequency, rate or extent of cellular response to manganese ion.
down regulation of cellular response to manganese
down regulation of cellular response to manganese ion
down-regulation of cellular response to manganese
down-regulation of cellular response to manganese ion
downregulation of cellular response to manganese
downregulation of cellular response to manganese ion
negative regulation of cellular response to manganese
inhibition of cellular response to manganese
inhibition of cellular response to manganese ion
negative regulation of cellular response to manganese ion
Any process that activates or increases the frequency, rate or extent of cellular response to manganese ion.
positive regulation of cellular response to manganese
up regulation of cellular response to manganese
up regulation of cellular response to manganese ion
up-regulation of cellular response to manganese
up-regulation of cellular response to manganese ion
upregulation of cellular response to manganese
upregulation of cellular response to manganese ion
activation of cellular response to manganese
activation of cellular response to manganese ion
positive regulation of cellular response to manganese ion
Any process that modulates the frequency, rate or extent of protein localization to cell leading edge.
regulation of protein localisation in cell leading edge
regulation of protein localisation to cell leading edge
regulation of protein localization in cell leading edge
regulation of protein localization to cell leading edge
Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to cell leading edge.
down regulation of protein localisation in cell leading edge
down regulation of protein localisation to cell leading edge
down regulation of protein localization in cell leading edge
down regulation of protein localization to cell leading edge
down-regulation of protein localisation in cell leading edge
down-regulation of protein localisation to cell leading edge
down-regulation of protein localization in cell leading edge
down-regulation of protein localization to cell leading edge
downregulation of protein localisation in cell leading edge
downregulation of protein localisation to cell leading edge
downregulation of protein localization in cell leading edge
downregulation of protein localization to cell leading edge
negative regulation of protein localisation in cell leading edge
negative regulation of protein localisation to cell leading edge
negative regulation of protein localization in cell leading edge
inhibition of protein localisation in cell leading edge
inhibition of protein localisation to cell leading edge
inhibition of protein localization in cell leading edge
inhibition of protein localization to cell leading edge
negative regulation of protein localization to cell leading edge
Any process that activates or increases the frequency, rate or extent of protein localization to cell leading edge.
positive regulation of protein localisation in cell leading edge
positive regulation of protein localisation to cell leading edge
positive regulation of protein localization in cell leading edge
up regulation of protein localisation in cell leading edge
up regulation of protein localisation to cell leading edge
up regulation of protein localization in cell leading edge
up regulation of protein localization to cell leading edge
up-regulation of protein localisation in cell leading edge
up-regulation of protein localisation to cell leading edge
up-regulation of protein localization in cell leading edge
up-regulation of protein localization to cell leading edge
upregulation of protein localisation in cell leading edge
upregulation of protein localisation to cell leading edge
upregulation of protein localization in cell leading edge
upregulation of protein localization to cell leading edge
activation of protein localisation in cell leading edge
activation of protein localisation to cell leading edge
activation of protein localization in cell leading edge
activation of protein localization to cell leading edge
positive regulation of protein localization to cell leading edge
Any process that modulates the frequency, rate or extent of calcium ion export across the plasma membrane.
regulation of calcium ion efflux from cell
regulation of calcium ion export from cell
regulation of calcium ion export across plasma membrane
Any process that stops, prevents or reduces the frequency, rate or extent of calcium ion export across the plasma membrane.
down regulation of calcium ion efflux from cell
down regulation of calcium ion export from cell
down-regulation of calcium ion efflux from cell
down-regulation of calcium ion export from cell
downregulation of calcium ion efflux from cell
downregulation of calcium ion export from cell
negative regulation of calcium ion efflux from cell
negative regulation of calcium ion export from cell
inhibition of calcium ion efflux from cell
inhibition of calcium ion export from cell
negative regulation of calcium ion export across plasma membrane
Any process that activates or increases the frequency, rate or extent of calcium ion export across the plasma membrane.
positive regulation of calcium ion efflux from cell
positive regulation of calcium ion export from cell
up regulation of calcium ion efflux from cell
up regulation of calcium ion export from cell
up-regulation of calcium ion efflux from cell
up-regulation of calcium ion export from cell
upregulation of calcium ion efflux from cell
upregulation of calcium ion export from cell
activation of calcium ion efflux from cell
activation of calcium ion export from cell
positive regulation of calcium ion export across plasma membrane
Any process that modulates the frequency, rate or extent of response to calcium ion.
Any process that stops, prevents or reduces the frequency, rate or extent of response to calcium ion.
down regulation of response to calcium ion
down-regulation of response to calcium ion
downregulation of response to calcium ion
negative regulation of response to Ca2+ ion
negative regulation of response to calcium ion
Any process that activates or increases the frequency, rate or extent of response to calcium ion.
positive regulation of response to Ca2+ ion
up regulation of response to calcium ion
up-regulation of response to calcium ion
positive regulation of response to calcium ion
Any process that stops, prevents or reduces the frequency, rate or extent of calcium ion import across plasma membrane.
down regulation of calcium ion import across plasma membrane
down-regulation of calcium ion import across plasma membrane
downregulation of calcium ion import across plasma membrane
inhibition of calcium ion import across plasma membrane
An example of this is PPP3CA in human (Q08209) in PMID:17640527 (inferred from direct assay).
negative regulation of calcium ion import across plasma membrane
Any process that modulates the frequency, rate or extent of lipid localization.
Any process that stops, prevents or reduces the frequency, rate or extent of lipid localization.
negative regulation of lipid localisation
negative regulation of lipid localization
Any process that activates or increases the frequency, rate or extent of lipid localization.
positive regulation of lipid localisation
positive regulation of lipid localization
The directed movement of calcium ions from inside of a cell, across the plasma membrane and into the extracellular region.
calcium ion export across plasma membrane
The directed movement of calcium ions into a sarcoplasmic reticulum.
calcium ion import into sarcoplasmic reticulum
The process by which excess light energy absorbed by chlorophyll and not used to drive photosynthesis is emitted by nonphotochemical quenching or chlorophyll fluorescence.
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.
Interacting selectively and non-covalently with damaged DNA containing single-strand breaks (SSBs).
single-strand break-containing damaged DNA binding
single-strand break-containing DNA binding
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.
Interacting selectively and non-covalently with a histone methyltransferase enzyme.
Interacting selectively and non-covalently with a steroid hormone.
Catalysis of the transfer of a phosphate group to the threonine-120 residue of histone H2A.
histone threonine kinase activity (H2A-T120 specific)
histone kinase activity (H2A-T120 specific)
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.
N6-methyladenosine-containing RNA binding
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.
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.
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.
response to transition metal nanoparticle
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.
Interacting selectively and non-covalently with phosphorylated serine residues in the C-terminal domain of RNA polymerase II.
RNA Pol II C-terminal domain phosphoserine binding
RNAP II C-terminal domain phosphoserine binding
RNA polymerase II C-terminal domain phosphoserine binding
Interacting selectively and non-covalently with any part of a preribosome.
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.
peptidyl-threonine trans-autophosphorylation
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.
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.
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.
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.
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.
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.
Interacting selectively and non-covalently with a ubiquitin-specific protease.
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.
The directed movement of iron ions into the phloem from the xylem.
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.
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.
single-strand break repair via homologous recombination
Interacting selectively and non-covalently with the mitochondrial large ribosomal subunit RNA (LSU rRNA), a constituent of the mitochondrial large ribosomal subunit.
In S. cerevisiae, this is the mitochondrial 21S rRNA
mitochondrial ribosomal large subunit rRNA binding
Interacting selectively and non-covalently with calcitonin gene-related peptide (CGRP).
calcitonin-gene-related polypeptide binding
An example of this is CALCRL in human (Q16602) in PMID:10882736 (inferred from direct assay/mutant phenotype/etc.).
Interacting selectively and non-covalently with adrenomedullin (AM).
An example of a protein that could be annotated to this term is CALCRL in human (Q16602) in PMID:10882736.
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.
replication-born double-strand break repair via sister chromatid exchange
Catalysis of the reaction: ATP + a protein arginine = ADP + protein arginine phosphate.
This reaction occurs in bacterial species e.g. Bacillus subtilis.
Interacting selectively and non-covalently with a protein that is part of an extracellular matrix.
Catalysis of the reaction: MAP kinase threonine phosphate + H2O = MAP kinase threonine + phosphate and MAP kinase serine phosphate + H2O = MAP kinase serine + phosphate.
MAP kinase serine/threonine phosphatase activity
The phosphorylation by a protein of one or more of its own threonine amino acid residues, or a threonine residue on an identical protein.
Interacting selectively and non-covalently with an F-box domain of a protein.
Interacting selectively and non-covalently with any part of a U1 small nuclear ribonucleoprotein particle.
Interacting selectively and non-covalently with any part of a U2 small nuclear ribonucleoprotein particle.
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.
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.
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.
An example of this is NOX1 in human (Q9Y5S8) in PMID:10615049.
Interacting selectively and non-covalently with lipooligosaccharide. Lipooligosaccharides (LOSs) are the major glycolipids expressed on mucosal Gram-negative bacteria.
ChEBI distinguishes an oligosaccharide from a polysaccharide as the latter being anything of length 10 or greater.
Interacting selectively and non-covalently with the transferrin receptor.
Interacting selectively and non-covalently with the leptin receptor.
Interacting selectively and non-covalently with piRNA clusters, double-stranded DNA regions that give rise to PIWI-interacting RNAs (piRNAs).
An example of this is rhi in Drosophila melanogaster (Q7JXA8) in PMID:24906153 (inferred from direct assay).
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.
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.
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.
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.
Interacting selectively and non-covalently with a Baculovirus Inhibitor of apoptosis protein Repeat (BIR) domain.
Baculovirus Inhibitor of apoptosis protein Repeat domain binding
An example of this is the Drosophila reaper gene in PMID:21886178.
The process in which a manganese ion is transported across a mitochondrial membrane, into or out of the mitochondrion.
mitochondrial manganese ion transmembrane transport
The directed movement of potassium ions from outside of a cell, across the plasma membrane and into the cytosol.
potassium ion import across plasma membrane
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.
peptidyl-serine trans-autophosphorylation
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.
nascent polypeptide-associated complex binding
The process by which the rods of the retina gradually become fully responsive to dim light when no longer exposed to bright light.
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
Interacting selectively and non-covalently with an RNA molecule containing GU repeats.
The directed movement of magnesium ions out of mitochondrial matrix into the cytosol by means of some agent such as a transporter or pore.
Interacting selectively and non-covalently with the protein-tyrosine kinase receptor ErbB-4/HER4.
Interacting selectively and non-covalently with the enzyme protein phosphatase 5.
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.
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.
Interacting selectively and non-covalently with the coding sequence (CDS) of an mRNA molecule.
Interacting selectively and non-covalently with any member of the arrestin family, proteins involved in agonist-mediated desensitization of G protein-coupled receptors.
Interacting selectively and non-covalently with protein tyrosine kinase.
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.
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.
Interacting selectively and non-covalently with messenger RNA (mRNA) of a specific nucleotide composition or a specific sequence motif.
Interacting selectively and non-covalently with an enzyme that catalyzes the removal of an amino group from a substrate, producing ammonia (NH3).
Interacting selectively and non-covalently with C-rich, single-stranded DNA.
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.
sequence-specific double-stranded DNA binding
Interacting selectively and non-covalently with methionine-initator methionine tRNA.
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.
methionyl-initiator methionine tRNA binding
Interacting selectively and non-covalently with a histone H4 in which the lysine residue at position 20 has been modified by trimethylation.
Interacting selectively and non-covalently with a netrin receptor.
Any process that modulates the frequency, rate or extent of protein localization to cell cortex of cell tip.
regulation of protein localization to cell cortex of cell tip
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).
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.
Interacting selectively and non-covalently with 5.8S ribosomal RNA, a eukaryotic ribosomal RNA which forms a complex with 28S RNA.
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.
The phosphorylation by a protein of one or more of its own aspartate amino acid residues, or an aspartate residue on an identical protein.
peptidyl-aspartic acid autophosphorylation
Interacting selectively and non-covalently with the replication fork barrier found in the mating type region of fission yeast.
mating type region replication fork barrier binding
Interacting selectively and non-covalently with G-rich, single-stranded DNA.
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.
trans-activation response element binding
Any process that modulates the frequency, rate or extent of protein localization to the cell surface.
regulation of protein localisation at cell surface
regulation of protein localization at cell surface
regulation of protein localization to cell surface
Any process that stops, prevents, or reduces the frequency, rate or extent of protein localization to the cell surface.
negative regulation of protein localisation at cell surface
negative regulation of protein localization at cell surface
negative regulation of protein localization to cell surface
Any process that activates or increases the frequency, rate or extent of protein localization to the cell surface.
positive regulation of protein localisation at cell surface
positive regulation of protein localization at cell surface
positive regulation of protein localization to cell surface
Any process that modulates the frequency, rate or extent of cell-cell adhesion mediated by cadherin.
regulation of cell-cell adhesion mediated by cadherin
Any process that stops, prevents, or reduces the frequency, rate or extent of cell-cell adhesion mediated by cadherin.
negative regulation of cell-cell adhesion mediated by cadherin
Any process that activates or increases the frequency, rate or extent of cell-cell adhesion mediated by cadherin.
positive regulation of cell-cell adhesion mediated by cadherin
Any process that modulates the frequency, rate or extent of sodium-dependent phosphate transport.
regulation of sodium-dependent phosphate transport
Any process that stops, prevents, or reduces the frequency, rate or extent of sodium-dependent phosphate transport.
negative regulation of sodium-dependent phosphate transport
Any process that activates or increases the frequency, rate or extent of sodium-dependent phosphate transport.
positive regulation of sodium-dependent phosphate transport
Any process that modulates the frequency, rate or extent of neural precursor cell proliferation.
regulation of neural precursor cell proliferation
Any process that stops, prevents, or reduces the frequency, rate or extent of neural precursor cell proliferation.
negative regulation of neural precursor cell proliferation
Any process that activates or increases the frequency, rate or extent of neural precursor cell proliferation.
positive regulation of neural precursor cell proliferation
Any process that modulates the frequency, rate or extent of phosphate transmembrane transport.
regulation of phosphate membrane transport
regulation of phosphate transmembrane transport
Any process that stops, prevents, or reduces the frequency, rate or extent of phosphate transmembrane transport.
negative regulation of phosphate membrane transport
negative regulation of phosphate transmembrane transport
Any process that activates or increases the frequency, rate or extent of phosphate transmembrane transport.
positive regulation of phosphate membrane transport
positive regulation of phosphate transmembrane transport
Any process that modulates the frequency, rate or extent of ribonucleoprotein complex localization.
regulation of cellular ribonucleoprotein complex localization
regulation of establishment and maintenance of ribonucleoprotein complex localization
regulation of ribonucleoprotein complex localisation
regulation of ribonucleoprotein complex localization
Any process that stops, prevents, or reduces the frequency, rate or extent of ribonucleoprotein complex localization.
negative regulation of cellular ribonucleoprotein complex localization
negative regulation of establishment and maintenance of ribonucleoprotein complex localization
negative regulation of ribonucleoprotein complex localisation
negative regulation of ribonucleoprotein complex localization
Any process that activates or increases the frequency, rate or extent of ribonucleoprotein complex localization.
positive regulation of cellular ribonucleoprotein complex localization
positive regulation of establishment and maintenance of ribonucleoprotein complex localization
positive regulation of ribonucleoprotein complex localisation
positive regulation of ribonucleoprotein complex localization
Any process that modulates the frequency, rate or extent of pancreatic stellate cell proliferation.
regulation of pancreatic stellate cell proliferation
Any process that stops, prevents, or reduces the frequency, rate or extent of pancreatic stellate cell proliferation.
negative regulation of pancreatic stellate cell proliferation
Any process that activates or increases the frequency, rate or extent of pancreatic stellate cell proliferation.
positive regulation of pancreatic stellate cell proliferation
Any process that modulates the frequency, rate or extent of oxidative phosphorylation uncoupler activity.
regulation of mitochondrial uncoupling protein activity
regulation of uncoupling protein activity
regulation of oxidative phosphorylation uncoupler activity
Any process that stops, prevents or reduces the frequency, rate or extent of oxidative phosphorylation uncoupler activity.
negative regulation of mitochondrial uncoupling protein activity
negative regulation of uncoupling protein activity
negative regulation of oxidative phosphorylation uncoupler activity
Any process that activates or increases the frequency, rate or extent of oxidative phosphorylation uncoupler activity.
positive regulation of mitochondrial uncoupling protein activity
positive regulation of uncoupling protein activity
positive regulation of oxidative phosphorylation uncoupler activity
Any process that activates or increases the frequency, rate or extent of myoblast proliferation.
positive regulation of myoblast proliferation
Any process that modulates the frequency, rate or extent of myoblast proliferation.
Any process that modulates the frequency, rate or extent of thymocyte aggregation.
regulation of T cell precursor aggregation
regulation of immature T-lymphocyte aggregation
regulation of thymic lymphocyte aggregation
regulation of immature T cell aggregation
regulation of immature T-cell aggregation
Any process that stops, prevents or reduces the frequency, rate or extent of thymocyte aggregation.
negative regulation of T cell precursor aggregation
negative regulation of immature T-lymphocyte aggregation
negative regulation of thymic lymphocyte aggregation
negative regulation of immature T cell aggregation
negative regulation of immature T-cell aggregation
negative regulation of thymocyte aggregation
Any process that activates or increases the frequency, rate or extent of thymocyte aggregation.
positive regulation of T cell precursor aggregation
positive regulation of immature T-lymphocyte aggregation
positive regulation of thymic lymphocyte aggregation
positive regulation of immature T cell aggregation
positive regulation of immature T-cell aggregation
positive regulation of thymocyte aggregation
Any process that modulates the frequency, rate or extent of neutrophil aggregation.
regulation of neutrophil leucocyte aggregation
regulation of neutrophilic leukocyte aggregation
Any process that stops, prevents or reduces the frequency, rate or extent of neutrophil aggregation.
negative regulation of neutrocyte aggregation
negative regulation of neutrophil leucocyte aggregation
negative regulation of neutrophilic leukocyte aggregation
negative regulation of neutrophil aggregation
Any process that activates or increases the frequency, rate or extent of neutrophil aggregation.
positive regulation of neutrocyte aggregation
positive regulation of neutrophil leucocyte aggregation
positive regulation of neutrophilic leukocyte aggregation
positive regulation of neutrophil aggregation
Any process that modulates the frequency, rate or extent of secondary growth.
Any process that stops, prevents or reduces the frequency, rate or extent of secondary growth.
Any process that activates or increases the frequency, rate or extent of secondary growth.
Any process that stops, prevents or reduces the frequency, rate or extent of stem cell proliferation.
negative regulation of stem cell proliferation
Any process that activates or increases the frequency, rate or extent of stem cell proliferation.
positive regulation of stem cell proliferation
Any process that modulates the frequency, rate or extent of sodium ion transmembrane transporter activity.
regulation of sodium transporter activity
regulation of sodium ion transmembrane transporter activity
Any process that stops, prevents or reduces the frequency, rate or extent of sodium ion transmembrane transporter activity.
negative regulation of sodium transporter activity
negative regulation of sodium ion transmembrane transporter activity
Any process that activates or increases the frequency, rate or extent of sodium ion transmembrane transporter activity.
positive regulation of sodium transporter activity
positive regulation of sodium ion transmembrane transporter activity
Any process that stops, prevents or reduces the frequency, rate or extent of myoblast proliferation.
negative regulation of myoblast proliferation
Any process that modulates the frequency, rate or extent of detection of glucose.
Any process that stops, prevents or reduces the frequency, rate or extent of detection of glucose.
negative regulation of glucose detection
negative regulation of glucose perception
negative regulation of detection of glucose
Any process that activates or increases the frequency, rate or extent of detection of glucose.
positive regulation of glucose detection
positive regulation of glucose perception
positive regulation of detection of glucose
Any process that modulates the frequency, rate or extent of response to drug.
regulation of drug susceptibility/resistance
Interacting selectively and non-covalently with xylan.
Interacting selectively and non-covalently with glucomannan.
Interacting selectively and non-covalently with cellooligosaccharide.
Interacting selectively and non-covalently with mannan.
Interacting selectively and non-covalently with amylopectin.
Interacting selectively and non-covalently with pullulan.
Interacting selectively and non-covalently with arabinoxylan.
Interacting selectively and non-covalently with glycogen.
Interacting selectively and non-covalently with starch.
Interacting selectively and non-covalently with maltoheptaose.
Interacting selectively and non-covalently with galactomannan.
Interacting selectively and non-covalently with cyclodextrin.
Interacting selectively and non-covalently with (1->3),(1->4)-beta-glucan.
Interacting selectively and non-covalently with (1->6)-beta-D-glucan.
Interacting selectively and non-covalently with beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc.
beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc binding
Interacting selectively and non-covalently with chitosan.
Interacting selectively and non-covalently with (1->4)-beta-D-galactan.
Interacting selectively and non-covalently with inulin.
Interacting selectively and non-covalently with alpha-D-glucan.
Interacting selectively and non-covalently with L-arabinofuranose.
Interacting selectively and non-covalently with arabinogalactan.
Interacting selectively and non-covalently with camalexin.
Any process that modulates the frequency, rate or extent of chloride transport.
Any process that stops, prevents or reduces the frequency, rate or extent of chloride transport.
negative regulation of chloride transport
Interacting selectively and non-covalently with quercitrin.
Any process that modulates the frequency, rate or extent of protein localization to prospore membrane.
regulation of protein localisation to prospore membrane
regulation of protein targeting to ascospore-type prospore membrane
regulation of protein targeting to forespore membrane
regulation of protein targeting to prospore membrane
regulation of protein-prospore membrane targeting
regulation of protein localization to prospore membrane
Any process that activates or increases the frequency, rate or extent of protein localization to prospore membrane.
positive regulation of protein localisation to prospore membrane
positive regulation of protein targeting to FSM
positive regulation of protein targeting to ascospore-type prospore membrane
positive regulation of protein targeting to forespore membrane
positive regulation of protein targeting to prospore membrane
positive regulation of protein-prospore membrane targeting
positive regulation of protein localization to prospore membrane
Any process that modulates the frequency, rate or extent of store-operated calcium entry.
regulation of capacitative calcium entry
regulation of store-operated calcium import
regulation of store-operated calcium entry
Any process that modulates the frequency, rate or extent of cation channel activity.
regulation of cation diffusion facilitator activity
regulation of nonselective cation channel activity
Any process that stops, prevents or reduces the frequency, rate or extent of cation channel activity.
negative regulation of cation diffusion facilitator activity
negative regulation of nonselective cation channel activity
negative regulation of cation channel activity
Any process that activates or increases the frequency, rate or extent of cation channel activity.
positive regulation of cation diffusion facilitator activity
positive regulation of nonselective cation channel activity
positive regulation of cation channel activity
editor preferred term
The concise, meaningful, and human-friendly name for a class or property preferred by the ontology developers. (US-English)
PERSON:Daniel Schober
example
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
example of usage
has curation status
PERSON:Alan Ruttenberg
PERSON:Bill Bug
PERSON:Melanie Courtot
definition
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.
The official definition, explaining the meaning of a class or property. Shall be Aristotelian, formalized and normalized. Can be augmented with colloquial definitions.
editor note
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.
term editor
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
20110707, MC: label update to term editor and definition modified accordingly. See http://code.google.com/p/information-artifact-ontology/issues/detail?id=115.
alternative term
definition source
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
Discussion on obo-discuss mailing-list, see http://bit.ly/hgm99w
ready for release
pending final vetting
curator note
imported from
elucidation
has associated axiom(nl)
has associated axiom(fol)
has axiom label
human immunodeficiency virus type 1 ,HIV-1
human immunodeficiency virus type 1 HIV 1
human immunodeficiency virus type 1 HIV-1
human immunodeficiency virus type 1 HIV1
human immunodeficiency virus type 1, HIV-1
human immunodeficiency virus type I HIV-1
human immunodeficiency virus type-1 HIV-1
purple photosynthetic bacteria and relatives
Influenza A virus (A/New York/392/2004(H3N2))
Escherichia coli str. K12 substr. MG1655
Escherichia coli str. K-12 substr. MG1655
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.
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.
A substance that kills microorganisms such as bacteria or mold, or stops them from growing and causing disease.
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.
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.
A property representing a concept unique identifier within the NCI Enterprise Vocabulary Service's NCI Thesaurus.
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.
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.
A property representing an alternative Preferred Name for use in some NCI systems.
A property representing the word or phrase that NCI uses by preference to refer to the concept.
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.
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.
A property representing the English language definition of a concept from a source other than NCI.
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.
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.
A property representing a term chosen by NICHD to be used in the representation of the NICHD hierarchy.
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.
pH is a scale used to specify how acidic or basic a water-based solution is.
organism
animal
fungus
plant
virus
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.
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')
WEB: http://en.wikipedia.org/wiki/Organism
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.
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
WEB: http://en.wikipedia.org/wiki/Genome
genome
A gene is a material entity that represents the entire DNA sequence required for synthesis of a functional protein or RNA molecule.
WEB: http://www.ncbi.nlm.nih.gov/books/NBK21640/
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.
gene
a disposition that a gene can be used as a blueprint for generating a new form of product such as protein.
WEB: http://www.ncbi.nlm.nih.gov/IEB/ToolBox/CPP_DOC/lxr/source/src/objects/entrezgene/entrezgene.asn
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".
gene disposition
the symbol assigned by the nomenclature authority
symbol from nomenclature authority
the full name assigned by the nomenclature authority
full name from nomenclature authority
NCBI GeneID
NCBI LocusTag
gene map location
modification date
a gene disposition that a gene can be used as a blueprint for generating a protein (i.e., a gene encodes for a protein).
protein-coding gene disposition
a gene disposition that is the disposition of a gene that encodes for a tRNA.
RNA gene disposition
a RNA gene disposition that is for a gene that encodes for a rRNA.
rRNA gene disposition
a RNA gene disposition that is for a gene that encodes for a snRNA.
snRNA gene disposition
a 'part of continuant at some time' relation that incides a genome belongs to a organism.
is genome of organism
The NCBITaxon ontology ID of an organism.
organism NCBITaxon ID
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.
is gene of organism
A chromosome ID where a gene is located.
chromosome ID of gene
an annotation property that specifies the type of a gene
type of gene
an annotation property that specifies a nomenclature status
nomenclature status
a RNA gene disposition that is for a gene that encodes for a tRNA.
tRNA gene disposition
a RNA gene disposition that is for a gene that encodes for a scRNA.
scRNA gene disposition
a RNA gene disposition that is for a gene that encodes for a snoRNA.
snoRNA gene disposition
a RNA gene disposition that is for a gene that encodes for a miscRNA.
miscRNA gene disposition
a RNA gene disposition that is for a gene that encodes for a ncRNA.
ncRNA gene disposition
a gene disposition that represents the disposition of gene being "pseudo", i.e., the gene is a pseudogene.
pseudo gene disposition
a gene disposition that represents the disposition of a gene that encodes for a transposon.
transposon gene disposition
a gene disposition that is "other", i.e., the gene is for a gene product that is not listed for another other gene type.
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.
other gene disposition
a gene disposition that represents the disposition of gene where the gene product is unknown.
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.
unknown gene disposition
an annotation property that shows the GO information associated with a specific gene.
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.
has GO association
An annotation property that represents a gene's association with PubMed publication(s).
YH: use the format: PMID: pmid1, pmid2, ... where pmid1 and pmid2 are specfic PubMed IDs (PMIDs).
has PubMed association
RNA gene
miscRNA gene
ncRNA gene
rRNA gene
scRNA gene
snoRNA gene
snRNA gene
tRNA gene
protein-coding gene
a gene that has lost its protein-coding ability or is otherwise no longer expressed in the cell.
WEB: http://en.wikipedia.org/wiki/Pseudogene
pseudo gene
a gene that encodes for a transposable genetic element that can change its position within the genome.
WEB: http://en.wikipedia.org/wiki/Transposable_element
transposon gene
a gene that has an unknown gene disposition
WEB: http://www.ncbi.nlm.nih.gov/books/NBK3841/
gene with unknown gene disposition
a gene that has an other gene disposition
gene with other gene disposition
A gene of Escherichia coli str. K-12 that has a protein-coding gene disposition
protein-coding gene of Escherichia coli K-12
DNA-binding response regulator in two-component regulatory system with CusS
sensory histidine kinase in two-component regulatory system with PhoB
DNA-binding response regulator in two-component regulatory system with PhoR (or CreC)
inactive two-component system connector protein
sensory histidine kinase in two-component regulatory system with citB
DNA-binding response regulator in two-component regulatory system with KdpD
quorum sensing DNA-binding response regulator in two-component regulatory system with QseC
hybrid sensory histidine kinase in two-component regulatory system with TorR
DNA-binding response regulator in two-component regulatory system with PhoQ
sensory histidine kinase in two-component regulatory system with NarL
DNA-binding response regulator in two-component regulatory system with NarX (or NarQ)
response regulator binding RpoS to initiate proteolysis by ClpXP; required for the PcnB-degradosome interaction during stationary phase
sensory histidine kinase in two-component regulatory system with CusR, senses copper ions
DNA-binding response regulator in two-component regulatory system with TorS
multicopy supressor of yjeE, yeaZ or ygjD deletion lethality, predicted response regulator of two-component regulatory system with sensor protein RstB
sensory histidine kinase in two-component regulatory system with PhoP
regulatory peptide for PhoPQ, feedback inhibition
chemotaxis regulator transmitting signal to flagellar motor component
fused chemotaxis regulator: protein-glutamate methylesterase in two-component regulatory system with CheA
fused chemotactic sensory histidine kinase in two-component regulatory system with CheB and CheY: sensory histidine kinase/signal sensing protein
DNA-binding response regulator in two-component regulatory system with BarA
predicted DNA-binding response regulator in two-component system with YedV
predicted sensory kinase in two-component regulatory system with YedW
DNA-binding response regulator in two-component regulatory system with BaeS
sensory histidine kinase in two-component regulatory system with BaeR
phosphotransfer intermediate protein in two-component regulatory system with RcsBC
sensor kinase regulating yhjX; pyruvate-responsive YpdAB two-component system
fused sensory histidine kinase in two-component regulatory system with KdpE: signal sensing protein
DNA-binding response regulator in two-component regulatory system with EvgS
hybrid sensory histidine kinase in two-component regulatory system with EvgA
sensory histidine kinase in two-component regulatory system with NarP (NarL)
DNA-binding response regulator in two-component regulatory system with citA
sensor protein kinase regulating glmY sRNA in two-component system with response regulator GlrR
response regulator regulating glmY sRNA in two-component system with sensor protein GlrK
predicted DNA-binding transcriptional regulator
quorum sensing sensory histidine kinase in two-component regulatory system with QseB
hybrid sensory histidine kinase, in two-component regulatory system with UvrY
sensory histidine kinase in two-component regulatory system with OmpR
response regulator activating yhjX; pyruvate-responsive YpdAB two-component system
DNA-binding response regulator in two-component regulatory system with RcsC and YojN
fused response regulator of ato operon, in two-component system with AtoS: response regulator/sigma54 interaction protein
aerobic respiration control sensor histidine protein kinase, cognate to two-component response regulators ArcA and RssB
DNA-binding response regulator in two-component regulatory system with EnvZ
DNA-binding response regulator in two-component regulatory system wtih UhpB
sensory histidine kinase in two-component regulatory sytem with UhpA
sensory histidine kinase in two-component regulatory system with GlnG
fused DNA-binding response regulator in two-component regulatory system with GlnL: response regulator/sigma54 interaction protein
DNA-binding response regulator in two-component regulatory system with CpxA
sensory histidine kinase in two-component regulatory system with CpxR
fused DNA-binding response regulator in two-component regulatory system with ZraS: response regulator/sigma54 interaction protein
sensory histidine kinase in two-component regulatory system with ZraR
sensory histidine kinase in two-component regulatory system with CreB or PhoB, regulator of the CreBC regulon
DNA-binding response regulator in two-component regulatory system with BasS
sensory histidine kinase in two-component regulatory system with BasR
sensory histidine kinase in two-component regulatory system with DcuR, regulator of anaerobic fumarate respiration
DNA-binding response regulator in two-component regulatory system with DcuS
sensory histidine kinase in two-component regulatory system with RstA
DNA-binding response regulator in two-component regulatory system with ArcB or CpxA
DNA-binding response regulator in two-component regulatory system with CreC
hybrid sensory kinase in two-component regulatory system with RcsB and YojN
sensory histidine kinase in two-component regulatory system with AtoC
predicted response regulator in two-component system withYehU
predicted sensory kinase in two-component system with YehT, inner membrane protein
DNA-binding response regulator in two-component regulatory system with NarQ or NarX
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.
WEB: https://en.wikipedia.org/wiki/Two-component_regulatory_system WEB: https://www.ncbi.nih.gov/pmc/articles/PMC2751022/
two-component regulatory system
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.
PhoRB two-component regulatory system of Escherichia coli K-12
WEB: https://www.ncbi.nlm.nih.gov/pubmed/23154290
PhoRB two-component regulatory system
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.
WEB: https://en.wikipedia.org/wiki/Cell_envelope WEB: https://en.wikiepdie.org/wiki/Polymyxin WEB: https://www.ncbi.nlm.nih.gov/pubmed/29109626
antibiotic targeting on cell envelope
A two-component regulatory system of bacteria, including Gram positive and negative bacteria.
bacterial two-component regulatory system
A bacterial histidine phosphotransferase gene role means the gene is able to encode the histidine phosphotransferase protein
bacterial histidine phosphotransferase gene role
a gene that encodes for a bacterial histidine phosphotransferase protein
bacterial histidine phosphotransferase gene
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.
CusSR two-component regulatory system of Escherichia coli K-12
WEB: https://www.ncbi.nlm.nih.gov/pubmed/11004187 WEB: https://www.ncbi.nlm.nih.gov/pubmed/11283292
CusSR two-component regulatory system
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.
WEB: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6335343/
bacterial classical sensor kinase protein
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.
WEB: https://en.wikipedia.org/wiki/Chemical_substance WEB: https://en.wikipedia.org/wiki/Concentration
chemical concentration
a gene that encodes for bacterial protein
bacterial protein-encoding gene
a gene that encodes for bacterial sensor kinase protein, including classical, hybrid , and unothodox type sensor kinase protein
bacterial sensor kinase gene
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.
PhoPQ two-component regulatory system of Escherichia coli K-12
WEB: https://www.ncbi.nlm.nih.gov/pubmed/11222580 WEB: https://www.ncbi.nlm.nih.gov/pubmed/10464230
PhoPQ two-component regulatory system
A bacterial sensor kinase gene role means the gene is able to encode the bacterial sensor kinase protein.
bacterial sensor kinase gene role
A bacterial response regulator gene role means the gene is able to encode bacterial response regulator protein.
bacterial response regulator gene role
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.
bacterial unorthodox sensor kinase protein
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.
is two-component regulatory system of organism
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.
two-component regulatory system of Escherichia coli K-12
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.
bacterial hybrid sensor kinase protein
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.
WEB: https://www.ncbi.nlm.nih.gov/pubmed/30687268
bacterial classical sensor kinase role
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).
bacterial hybrid sensor kinase role
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.
bacterial unorthodox sensor kinase role
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.
WEB: http://www.ncbi.nlm.nih.gov/pubmed/10203840
bacterial classical two-component regulatory system
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.
WEB: https://www.ncbi.nlm.nih.gov/pubmed/10203840
bacterial unorthodox two component system
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.
WEB: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6335343 WEB: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5571105
bacterial histidine phosphotransferase protein
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.
bacterial histidine phosphotransferase protein role
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.
DpiBA two-component regulatory system of Escherichia coli K-12
WEB: https://www.ncbi.nlm.nih.gov/pubmed/18997424 WEB: https://www.ncbi.nlm.nih.gov/pubmed/19202292
DpiBA two-component regulatory system
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.
KdpDE two-component regulatory system of Escherichia coli K-12
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
KdpDE two-component regulatory system
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.
NarLX two-component regulatory system of Escherichia coli K-12
WEB: https://www.ncbi.nlm.nih.gov/pubmed/8412692 WEB: https://www.ncbi.nlm.nih.gov/pubmed/7855431
NarLX two-component regulatory system
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.
RstBA two-component regulatory system of Escherichia coli K-12
WEB: https://www.ncbi.nlm.nih.gov/pubmed/12813061
RstBA two-component regulatory system
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.
HprSR two-component regulatory system of Escherichia coli K-12
WEB: https://www.ncbi.nlm.nih.gov/pubmed/25568260 WEB: https://www.ncbi.nlm.nih.gov/pubmed/27983483
HprSR two-component regulatory system
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.
BaeSR two-component regulatory system of Escherichia coli K-12
BaeSR two-component regulatory system
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.
BtsSR two-component regulatory system of Escherichia coli K-12
WEB: https://www.ncbi.nlm.nih.gov/pubmed/29038258
BtsSR two-component regulatory system
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.
RcsBCD phosphorelay of Escherichia coli K-12
RcsBCD phosphorelay two-component regulatory system of Escherichia coli K-12
RcsBCD two-component regulatory system of Escherichia coli K-12
WEB: https://www.ncbi.nlm.nih.gov/pubmed/18192383
RcsBCD two-component regulatory system
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.
AtoSC two-component regulatory system of Escherichia coli K-12
AtoSC two-component regulatory system
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.
YpdAB two-component regulatory system of Escherichia coli K-12
YpdAB two-component regulatory system
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.
NarQP two-component regulatory system of Escherichia coli K-12
NarQP two-component regulatory system
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.
GlrKR two-component regulatory system of Escherichia coli K-12
WEB: https://www.ncbi.nlm.nih.gov/pubmed/30040820 WEB: https://www.ncbi.nlm.nih.gov/pubmed/27629414
GlrKR two-component regulatory system
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.
QseBC two-component regulatory system of Escherichia coli K-12
WEB: https://www.ncbi.nlm.nih.gov/pubmed/11929534 WEB: https://www.ncbi.nlm.nih.gov/pubmed/16352847
QseBC two-component regulatory system
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.
EnvZ-OmpR two-component regulatory system of Escherichia coli K-12
EnvZ/OmpR TCS of Escherichia coli str. K-12 substr. MG1655
WEB: https://www.ncbi.nlm.nih.gov/pubmed/2668953
EnvZ-OmpR two-component regulatory system
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.
UhpAB two-component regulatory system of Escherichia coli K-12
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
UhpAB two-component regulatory system
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.
NtrBC two-component regulatory system of Escherichia coli K-12
WEB: https://www.ncbi.nlm.nih.gov/pubmed/24947454
NtrBC two-component regulatory system
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.
CpxAR two-component regulatory system of Escherichia coli K-12
WEB: https://www.ncbi.nlm.nih.gov/pubmed/22092888
CpxAR two-component regulatory system
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.
ZraSR two-component regulatory system of Escherichia coli K-12
WEB: https://www.ncbi.nlm.nih.gov/pubmed/26438879 WEB: https://www.ncbi.nlm.nih.gov/pubmed/30389436
ZraSR two-component regulatory system
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.
BasSR two-component regulatory system of Escherichia coli K-12
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
BasSR two-component regulatory system
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.
DcuSR two-component regulatory system of Escherichia coli K-12
WEB: https://www.ncbi.nlm.nih.gov/pubmed/9973351 WEB: https://www.ncbi.nlm.nih.gov/pubmed/14996819
DcuSR two-component regulatory system
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.
CreBC two-component regulatory system of Escherichia coli K-12
WEB: https://www.ncbi.nlm.nih.gov/pubmed/11350954
CreBC two-component regulatory system
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.
TorSR two-component regulatory system of Escherichia coli K-12
WEB: https://www.ncbi.nlm.nih.gov/pubmed/17850256
TorSR two-component regulatory system
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.
EvgSA two-component regulatory system of Escherichia coli K-12
WEB: https://www.ncbi.nlm.nih.gov/pubmed/24957621
EvgSA two-component regulatory system
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.
BarA-UvrY two-component regulatory system of Escherichia coli K-12
BarA/UvrY two-component regulatory system
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
BarA-UvrY two-component regulatory system
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.
ArcAB two-component regulatory system of Escherichia coli str. K-12
WEB: http://www.ncbi.nlm.nih.gov/pubmed/19933363
ArcAB two-component regulatory system
The concentration of ion. An ion is an atom or molecule that has a net electrical charge.
ion concentration
The ion concentration outside the cytoplasm of a cell.
extracytoplasmic ion concentration
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.
WEB: https://micro.magnet.fsu.edu/cells/bacteriacell.html
cytoplasmic ion concentration
The concentration of anion. An anion is negatively charged ion, with more electrons than protons.
anion concentraion
The concentration of cation. A cation is a positively charged ion, with fewer electrons than protons.
cation concentration
The bacterial response regulator role is the role of protein serves as the phosphoacceptor which can receive the phosphoryl group from sensor kinase.
bacterial response regulator role
a bacterial protein that mediates a cell's response to changes in its environment as part of the two-component regulatory system
bacterial response regulator protein
a gene that encodes for a bacterial respose regulator protein
bacterial response regulator gene
magnesium(2+) concentration
magnesium(2+) concentration lower than 10 uM
the verb detect means to discover or observe the existence of something
detects
regulation of two-component regulatory system
negative regulation of two-component regulatory system
positive regulation of two-component regulatory system
negative regulation of Escherichia coli K-12 two-component regulatory system
negative regulation of Escherichia coli K-12 PhoPQ two-component regulatory system
response to antimicrobial peptide
response to cationic antimicrobial peptide
response to anionic antimicrobial peptide
positive regulation of Escherichia coli K-12 two-component regulatory system
positive regulation of Escherichia coli K-12 BasSR two-component regulatory system
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.
WEB: https://www.ncbi.nlm.nih.gov/pubmed/29109626
antibiotic targeting on protein synthesis
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.
WEB: https://www.sciencedirect.com/topics/neuroscience/nucleic-acid-synthesis
antibiotic targeting on nucleic acid synthesis
The 30S subunit is an integral part of mRNA translation. It binds three prokaryotic initiation factors: IF-1, IF-2, and IF-3.
WEB: https://en.wikipedia.org/wiki/Prokaryotic_small_ribosomal_subunit
antibiotic targeting on 30S subunit of bacterial ribosome
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.
WEB: https://en.wikipedia.org/wiki/Prokaryotic_large_ribosome_subunit
antibiotic targeting on 50S subunit of bacterial ribosome
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.
WEB: https://en.wikipedia.org/wiki/DNA_replication
targeting on DNA replication
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.
WEB: https://en.wikipedia.org/wiki/Trancription_(biology)
targeting on RNA synthesis
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.
WEB: https://en.wikipedia.org/wiki/Folate
targeting on folate synthesis
Antibiotic resistance is the ability of microbe, especially bacteria, to resist or to become tolerant to antibiotics to which they were once sensitive.
WEB: https://www.medicinenet.com/script/main/art.asp?articlekey=2276
antibiotic resistance
Bacteria has ability to generate the enzymes caplable of introducing chemical changes to the antibiotic.
WEB: https://www.ncbi.nlm.nih.gov/pubmed/27227291
chemical alteration of antibiotic
The antibiotic was destroyed by some enzymes generating from bacteria and further lead to antibiotic become ineffective.
destruction of antibiotic
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.
WEB: https://www.ncbi.nlm.nih.gov/pubmed/27227291 WEB: https://www.ncbi.nlm.nih.gov/pubmed/29109626
reduction of accumulation of antibiotic
Natural variations or acquired changes in the antibiotic target site can avoid the action of the antibiotics.
alternation in antibiotic target site
Osmolarity, also known as osmotic concentration, is the measure of solute concentration.
WEB: https://en.wikipedia.org/wiki/Osmotic_concentration
An amino acid chain that is produced de novo by ribosome-mediated translation of a genetically-encoded mRNA.
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].
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.
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.
A protein that is encoded in the genome of Escherichia coli K-12.
A protein that is encoded in the genome of some Bacteria <prokaryote>.
protein-glutamate methylesterase/protein-glutamine glutaminase (Escherichia coli K-12)
chemotaxis protein CheA (Escherichia coli K-12)
A transcriptional regulatory protein CreB that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P08368]
transcriptional regulatory protein CreB (Escherichia coli K-12)
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]
phosphate regulon sensor protein PhoR (Escherichia coli K-12)
A sensor protein CreC that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P08401]
sensor protein CreC (Escherichia coli K-12)
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]
sensor protein UhpB (Escherichia coli K-12)
signal transduction histidine-protein kinase/phosphatase UhpB (Escherichia coli K-12)
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]
Dye resistance protein (Escherichia coli K-12)
aerobic respiration control protein ArcA (Escherichia coli K-12)
A transcriptional regulatory protein OmpR that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AA16]
transcriptional regulatory protein OmpR (Escherichia coli K-12)
A sensor histidine kinase YpdA that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AA93]
sensor histidine kinase YpdA (Escherichia coli K-12)
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]
positive transcription regulator EvgA (Escherichia coli K-12)
DNA-binding transcriptional activator EvgA (Escherichia coli K-12)
A transcriptional regulatory protein CusR that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0ACZ8]
transcriptional regulatory protein CusR (Escherichia coli K-12)
A transcriptional regulatory protein DcuR that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AD01]
transcriptional regulatory protein DcuR (Escherichia coli K-12)
A sensor histidine kinase BtsS that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AD14]
Sensor histidine kinase YehU (Escherichia coli K-12)
sensor histidine kinase BtsS (Escherichia coli K-12)
A transcriptional regulatory protein YpdB that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AE39]
transcriptional regulatory protein YpdB (Escherichia coli K-12)
chemotaxis protein CheY (Escherichia coli K-12)
A sensor histidine kinase CpxA that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AE82]
sensor histidine kinase CpxA (Escherichia coli K-12)
A transcriptional regulatory protein CpxR that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AE88]
transcriptional regulatory protein CpxR (Escherichia coli K-12)
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]
aerobic respiration control sensor protein ArcB (Escherichia coli K-12)
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]
signal transduction histidine-protein kinase BarA (Escherichia coli K-12)
A sensor protein dcuS that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AEC8]
sensor histidine kinase DcuS (Escherichia coli K-12)
A response regulator UvrY that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AED5]
response regulator UvrY (Escherichia coli K-12)
A transcriptional regulatory protein DpiA that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AEF4]
destabilizer of plasmid inheritance (Escherichia coli K-12)
transcriptional regulatory protein DpiA (Escherichia coli K-12)
An osmolarity sensor protein EnvZ that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AEJ4]
osmolarity sensor protein EnvZ (Escherichia coli K-12)
A fimbriae Z protein that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AEL8]
fimbriae Z protein (Escherichia coli K-12)
A regulator of RpoS that is encoded in the genome of Escherichia coli K-12. [PRO:DNx: http://www.uniprot.org/uniprot/P0AEV1]
regulator of RpoS (Escherichia coli K-12)
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]
nitrate/nitrite response regulator protein NarL (Escherichia coli K-12)
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]
nitrate/nitrite sensor protein NarX (Escherichia coli K-12)
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]
Nitrogen regulation protein NR(II) (Escherichia coli K-12)
Nitrogen regulator II (Escherichia coli K-12)
sensory histidine kinase/phosphatase NtrB (Escherichia coli K-12)
A DNA-binding transcriptional regulator NtrC that is the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AFB8]
nitrogen regulation protein NR(I) (Escherichia coli K-12)
nitrogen regulator I (Escherichia coli K-12)
DNA-binding transcriptional regulator NtrC (Escherichia coli K-12)
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]
phosphate regulon transcriptional regulatory protein PhoB (Escherichia coli K-12)
A transcriptional regulatory protein BtsR that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AFT5]
transcriptional regulatory protein YehT (Escherichia coli K-12)
transcriptional regulatory protein BtsR (Escherichia coli K-12)
A transcriptional regulatory protein GlrR that is encoded in the genome of Escherichia coli K-12.
transcriptional regulatory protein GlrR (Escherichia coli K-12)
A transcriptional regulatory protein UhpA that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0AGA6]
transcriptional regulatory protein UhpA (Escherichia coli K-12)
A sensor histidine kinase RcsC that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/PODMC5]
capsular synthesis regulator component C (Escherichia coli K-12)
sensor histidine kinase RcsC (Escherichia coli K-12)
A transcriptional regulatory protein RcsB that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P0DMC7]
capsular synthesis regulator component B (Escherichia coli K-12)
transcriptional regulatory protein RcsB (Escherichia coli K-12)
A transcriptional regulatory protein ZraR that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P14375]
transcriptional regulatory protein ZraR (Escherichia coli K-12)
A sensor protein ZraS that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P14377]
sensor protein ZraS (Escherichia coli K-12)
A sensor protein RstB that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P18392]
sensor protein RstB (Escherichia coli K-12)
A sensor protein KdpD that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P21865]
sensor protein KdpD (Escherichia coli K-12)
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]
kdp operon transcriptional regulatory protein KdpE (Escherichia coli K-12)
A transcriptional regulatory protein PhoP that is encoded in the genome of Escherichia coli K-12.
transcriptional regulatory protein PhoP (Escherichia coli K-12)
A sensor protein PhoQ that is encoded in the genome of Escherichia coli K-12.
sensor histidine protein kinase/phosphatase PhoQ (Escherichia coli K-12)
sensor protein PhoQ (Escherichia coli K-12)
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]
nitrate/nitrite sensor protein NarQ (Escherichia coli K-12)
A transcriptional regulatory protein BasR that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P30843]
transcriptional regulatory protein BasR (Escherichia coli K-12)
A sensor protein BasS that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P30844]
sensor protein BasS (Escherichia coli K-12)
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]
signal transduction histidine-protein kinase BaeS (Escherichia coli K-12)
A sensor protein EvgS that is encoded in the genome of Escherichia coli K-12.
sensor protein EvgS (Escherichia coli K-12)
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]
nitrate/nitrite response regulator protein NarP (Escherichia coli K-12)
A torCAD operon transcriptional regulatory protein TorR that is encoded in the genome of Escherichia coli K-12.
torCAD operon transcriptional regulatory protein TorR (Escherichia coli K-12)
A sensor protein TorS that is encoded in the genome of Escherichia coli K-12.
sensor protein TorS (Escherichia coli K-12)
A phosphotransferase RcsD that is encoded in the genome of Escherichia coli K-12.
Sensor-like histidine kinase RcsD (Escherichia coli K-12)
phosphotransfer intermediate RcsD (Escherichia coli K-12)
phosphotransferase RcsD (Escherichia coli K-12)
A sensor protein QseC that is encoded in the genome of Escherichia coli K-12.
sensor protein QseC (Escherichia coli K-12)
A transcriptional regulatory protein QseB that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P52076]
transcriptional regulatory protein QseB (Escherichia coli K-12)
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]
sensor hidtidine kinase GlrK (Escherichia coli K-12)
A transcriptional regulatory protein RstA that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P52108]
transcriptional regulatory protein RstA (Escherichia coli K-12)
A transcriptional regulatory protein BaeR that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P69228]
transcriptional regulatory protein BaeR (Escherichia coli K-12)
A sensor-like histidine kinase yedV that is encoded in the genome of Escherichia coli K-12.
hydrogen peroxide response sensor (Escherichia coli K-12)
sensor histidine kinase HprS (Escherichia coli K-12)
A transcriptional regulatory protein yedW that is encoded in the genome of Escherichia coli K-12.
hydrogen peroxide response regulator (Escherichia coli K-12)
transcriptional regulatory protein HprR (Escherichia coli K-12)
A sensor histidine kinase CusS that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P77485]
sensor histidine kinase CusS (Escherichia coli K-12)
A sensor kinase dpiB that is encoded in the genome of Escherichia coli K-12. [PRO:DNx http://www.uniprot.org/uniprot/P77510]
Sensor histidine kinase CitA (Escherichia coli K-12)
sensor histidine kinase DpiB (Escherichia coli K-12)
A regulatory protein AtoC that is encoded in the genome of Escherichia coli K-12. [PRO:DNx: http://www.uniprot.org/uniprot/Q06065]
Acetoacetate metabolism regulatory protein (Escherichia coli K-12)
DNA-binding transcriptional regulator AtoC (Escherichia coli K-12)
Ornithine decarboxylase antizyme (Escherichia coli K-12)
acetoacetate metabolism regulatory protein AtoC (Escherichia colie K-12)
regulatory protein AtoC (Escherichia coli K-12)
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]
signal transduction histidine-protein kinase AtoS (Escherichia coli K-12)
participates in
this blood clot participates in this blood coagulation
this input material (or this output material) participates in this process
this investigator participates in this investigation
a relation between a continuant and a process, in which the continuant is somehow involved in the process
participates_in
has participant
this enzyme has function this catalysis function (more colloquially: this enzyme has this catalysis function)
a relation between an independent continuant (the bearer) and a function, in which the function specifically depends on the bearer for its existence
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.
has_function
has function
this person has role this investigator role (more colloquially: this person has this role of investigator)
a relation between an independent continuant (the bearer) and a role, in which the role specifically depends on the bearer for its existence
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.
has_role
has role
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.
temporal interpretation
every HOTAIR lncRNA is the gene product of some HOXC gene
every sonic hedgehog protein (PR:000014841) is the gene product of some sonic hedgehog gene
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
Chris Mungall
has gene product
a particular instances of akt-2 enables some instance of protein kinase activity
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.
This relation is currently used experimentally by the Gene Ontology Consortium. It may not be stable and may be obsoleted at some future time.
enables
c involved_in p if and only if c enables some process p', and p' is part of p
involved in
enabled by
A material entity consisting of multiple components that are causally integrated.
May be replaced by a BFO class, as discussed in http://www.jbiomedsem.com/content/4/1/43
Holds between protein a (a transcription factor) and DNA element b if and only if a diminishes the process of transcription of b.
Logical axioms to be added after the relevant branch of GO is MIREOTed in
Holds between protein a (a transcription factor) and DNA element b if and only if a activates the process of transcription of b.
Yue Liu
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.
A biological ontology in the area of genes and genomes.
OGG: Ontology of Genes and Genomes
Vision Release: 1.0.59
A metadata relation between a class and its taxonomic rank (eg species, family)
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.
An association that connects the concept defining a particular terminology subset with concepts that belong to this subset.