13:06:2021 12:12 PSI-MOD 1.2 Joshua Klein Annotation note 01 - "[PSI-MOD:ref]" has been replaced by PubMed:18688235. Annotation note 02 - When an entry in the RESID Database is annotated with different sources because the same modification can arise from different encoded amino acids, then the PSI-MOD definition for each different source instance carries the RESID cross-reference followed by a hash symbol "#" and a 3 or 4 character label. When an entry in the RESID Database is annotated as a general modification with the same enzymatic activity producing different chemical structures depending on natural variation in the nonproteinaceous substrate, on secondary modifications that do not change the nature of the primary modification, or on a combination of a primary and one or more secondary modifications on the same residue, then the PSI-MOD definition for each different instance carries the RESID cross-reference followed by the special tag "#var". Annotation note 03 - When an entry in the Unimod database is annotated as a general modification, and one or more instance sites are listed, then the PSI-MOD definition for each different site instance carries the Unimod cross-reference followed by a hash symbol and an amino acid code, "N-term" or "C-term". Annotation note 04 - The elemental formulas are in strict alphabetical order, not in CAS ("C" and "H" first) order. Isotope numbers are in parentheses before the element symbol, and an element should not occur in a formula both with and without an isotope number. In difference formulas, counts can be zero or negative. Annotation note 05 - In entries with an isotope indicator in the formula, average masses are meaningless and are assigned the value equal to the monoisotopic mass, but rounded to a lower precision; monoisotopic masses are calculated by using the masses for the indicated isotopes and the most common isotopes for other elements without isotope indicators in the formulas. Annotation note 06 - For cross-link modifications, the number following "Cross-link" in the comment record indicates the number of amino acid residues that appear in the origin record, used to check the difference formula and masses. This usage differs from RESID, where the cross-link number indicates the maximum number of peptide chains that can be cross-linked. Annotation note 07 - The synonym cross-reference "MOD:old name" has been replaced by "MOD:alternate name". Annotation note 08 - The DeltaMass listings for free amino acids have been removed. Most Unimod entries that have not been "approved" have by general agreement not been incorporated unless there has been a request for a specific term by a PRIDE submitter. Annotation note 09 - The Open Mass Spectrometry Search Algorithm, OMSSA, enumerated list of modifications are being incorporated. The string values are synonyms with the synonymtypedef "OMSSA-label", and their integer values (which are supposed to be stable) are definition cross-references. Annotation note 10 - GNOme is the Glycan Naming and Subsumption Ontology (https://gnome.glyomics.org/), an ontology for the support of glycomics. PSI-MOD does not have all possible glycans in its entries, just the ones that are noted to be on proteins and have been requested for addition. GNOme uses GlyTouCan (http://glytoucan.org/) to provide stable accessions for glycans described at varyious degrees of characterization, including compositions (no linkage) and topologies (no carbon bond positions or anomeric configurations). ISO-8601 date: 2022-06-13 12:12Z PSI-MOD version: 1.031.6 RESID release: 75.00 definition term replaced by Label from MS DeltaMass Short label from OMSSA Alternate name curated by PSI-MOD Short label curated by PSI-MOD subset of protein modifications Agreed label from MS community Alternate name from RESID Misnomer tagged alternate name from RESID Name from RESID Systematic name from RESID Protein feature description from UniProtKB Alternate name from Unimod Description (full_name) from Unimod Interim label from Unimod subset_property synonym_type_property database_cross_reference has_exact_synonym has_obo_format_version has_obo_namespace has_related_synonym has_scope has_synonym_type in_subset 'Entity A' contains 'Entity B' implies that 'Entity B' is a part of the structure of 'Entity A'. PSI-MOD contains The inverse relationship to "part of". contains 'Entity A' contains 'Entity B' implies that 'Entity B' is a part of the structure of 'Entity A'. PubMed:18688235 'Entity A' derives_from 'Entity B' implies that 'Entity A' is chemically derived from 'Entity B'. PSI-MOD derives_from derives from 'Entity A' derives_from 'Entity B' implies that 'Entity A' is chemically derived from 'Entity B'. PubMed:18688235 'Entity A' has_functional_parent 'Entity B' implies that 'Entity B' has at least one chacteristic group from which 'Entity A' can be derived by functional modification. PSI-MOD has_functional_parent This relationship indicates that the formula and mass of the child are not inherited from the mass of the parent. has functional parent 'Entity A' has_functional_parent 'Entity B' implies that 'Entity B' has at least one chacteristic group from which 'Entity A' can be derived by functional modification. PubMed:18688235 'Entity A' part_of 'Entity B' implies that 'Entity A' is a part of the structure of 'Entity B'. PSI-MOD part_of part of 'Entity A' part_of 'Entity B' implies that 'Entity A' is a part of the structure of 'Entity B'. PubMed:18688235 Covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid residue. ModRes PSI-MOD MOD:00000 protein modification Covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid residue. PubMed:18688235 ModRes A protein modification that effectively replaces a hydrogen atom with an alkyl group. AlkylRes PSI-MOD MOD:00001 alkylated residue A protein modification that effectively replaces a hydrogen atom with an alkyl group. PubMed:18688235 AlkylRes A protein modification that effectively converts an L-serine residue to O3-glycosylserine. S natural OGlycoSer PSI-MOD MOD:00002 O-glycosyl-L-serine OGlycoSer A protein modification that effectively converts an L-serine residue to O3-glycosylserine. PubMed:18688235 Entry from Unimod. PSI-MOD MOD:00003 This term is for organizational use only and should not be assigned. [JSG] Unimod Entry from Unimod. PubMed:18688235 Artifact entry from Unimod - OBSOLETE because organizational use is no longer required. PSI-MOD MOD:00004 artifact true Artifact entry from Unimod - OBSOLETE because organizational use is no longer required. PubMed:18688235 A protein modification that effectively converts an L-threonine residue to O3-glycosylthreonine. T natural OGlycoThr PSI-MOD MOD:00005 O-glycosyl-L-threonine A protein modification that effectively converts an L-threonine residue to O3-glycosylthreonine. PubMed:18688235 OGlycoThr A protein modification that effectively replaces a residue hydrogen atom on a nitrogen with a carbohydrate-like group through a glycosidic bond. NGlycoRes PSI-MOD MOD:00006 N-glycosylated residue A protein modification that effectively replaces a residue hydrogen atom on a nitrogen with a carbohydrate-like group through a glycosidic bond. PubMed:18688235 NGlycoRes A protein modification that effectively substitutes a selenium atom for a sulfur atom. 46.91 C 0 H 0 N 0 O 0 S -1 Se 1 47.94445 X natural Unimod:162 Se(S)Res PSI-MOD Delta:S(-1)Se(1) Selenium replaces sulphur MOD:00007 selenium substitution for sulfur A protein modification that effectively substitutes a selenium atom for a sulfur atom. PubMed:12148805 Unimod:162 Se(S)Res Delta:S(-1)Se(1) Selenium replaces sulphur Entry from Unimod representing one or more entries in RESID. OBSOLETE because organizational use is no longer required. PSI-MOD MOD:00008 common true Entry from Unimod representing one or more entries in RESID. OBSOLETE because organizational use is no longer required. PubMed:18688235 A protein modification that removes a residue, or inserts or replaces a residue with a natural, standard or nonstandard, encoded residue. X natural Res alpha-amino acid PSI-MOD MOD:00009 natural residue A protein modification that removes a residue, or inserts or replaces a residue with a natural, standard or nonstandard, encoded residue. PubMed:6692818 RESID:AA0000 Res alpha-amino acid A protein modification that effectively converts a source amino acid residue to an L-alanine. 0.0 C 0 H 0 N 0 O 0 0.0 C 3 H 5 N 1 O 1 71.08 71.03712 A natural (2S)-2-aminopropanoic acid 2-aminopropionic acid 2-azanylpropanoic acid Ala L-alanine alpha-alanine alpha-aminopropionic acid PSI-MOD MOD:00010 L-alanine residue A protein modification that effectively converts a source amino acid residue to an L-alanine. ChEBI:29948 DeltaMass:0 PubMed:6692818 RESID:AA0001 (2S)-2-aminopropanoic acid 2-aminopropionic acid 2-azanylpropanoic acid Ala L-alanine alpha-alanine alpha-aminopropionic acid A protein modification that effectively converts a source amino acid residue to an L-arginine. 0.0 C 0 H 0 N 0 O 0 0.0 C 6 H 12 N 4 O 1 156.19 156.1011 R natural (2S)-2-amino-5-[(diaminomethylidene)amino]pentanoic acid 2-amino-5-(carbamimidamido)pentanoic acid [tautomer] 2-amino-5-[(aminoiminomethyl)amino]pentanoic acid [tautomer] 2-amino-5-guanidinopentanoic acid 2-amino-5-guanidinovaleric acid 2-azanyl-5-[bis(azanyl)methylideneazanyl]pentanoic acid Arg L-arginine alpha-amino-delta-guanidinovaleric acid PSI-MOD MOD:00011 L-arginine residue A protein modification that effectively converts a source amino acid residue to an L-arginine. ChEBI:29952 DeltaMass:0 PubMed:518876 PubMed:6692818 RESID:AA0002 (2S)-2-amino-5-[(diaminomethylidene)amino]pentanoic acid 2-amino-5-(carbamimidamido)pentanoic acid [tautomer] 2-amino-5-[(aminoiminomethyl)amino]pentanoic acid [tautomer] 2-amino-5-guanidinopentanoic acid 2-amino-5-guanidinovaleric acid 2-azanyl-5-[bis(azanyl)methylideneazanyl]pentanoic acid Arg L-arginine alpha-amino-delta-guanidinovaleric acid A protein modification that effectively converts a source amino acid residue to an L-asparagine. 0.0 C 0 H 0 N 0 O 0 0.0 C 4 H 6 N 2 O 2 114.1 114.04293 N natural (2S)-2-amino-4-butanediamic acid 2,4-bis(azanyl)-4-oxobutanoic acid 2,4-diamino-4-oxobutanoic acid 2-amino-3-carbamoylpropanoic acid 2-amino-4-butanediamic acid 2-aminosuccinamic acid 2-aminosuccinic acid 4-amide Asn L-asparagine alpha-amino-beta-carbamylpropionic acid alpha-aminosuccinamic acid aspartic acid 4-amide aspartic acid beta-amide beta-asparagine PSI-MOD MOD:00012 L-asparagine residue A protein modification that effectively converts a source amino acid residue to an L-asparagine. ChEBI:29956 DeltaMass:0 PubMed:15736973 PubMed:5681232 PubMed:6692818 PubMed:9789001 RESID:AA0003 (2S)-2-amino-4-butanediamic acid 2,4-bis(azanyl)-4-oxobutanoic acid 2,4-diamino-4-oxobutanoic acid 2-amino-3-carbamoylpropanoic acid 2-amino-4-butanediamic acid 2-aminosuccinamic acid 2-aminosuccinic acid 4-amide Asn L-asparagine alpha-amino-beta-carbamylpropionic acid alpha-aminosuccinamic acid aspartic acid 4-amide aspartic acid beta-amide beta-asparagine A protein modification that effectively converts a source amino acid residue to an L-aspartic acid. 0.0 C 0 H 0 N 0 O 0 0.0 C 4 H 5 N 1 O 3 115.09 115.02694 D natural (2S)-2-aminobutanedioic acid 2-azanylbutanedioic acid Asp L-aspartic acid aminosuccinic acid PSI-MOD MOD:00013 L-aspartic acid residue A protein modification that effectively converts a source amino acid residue to an L-aspartic acid. ChEBI:29958 DeltaMass:0 PubMed:1097438 PubMed:339692 PubMed:4399050 PubMed:5764436 PubMed:6692818 PubMed:8089117 PubMed:9521123 PubMed:9582379 RESID:AA0004 (2S)-2-aminobutanedioic acid 2-azanylbutanedioic acid Asp L-aspartic acid aminosuccinic acid A protein modification that effectively converts a source amino acid residue to an L-cysteine. 0.0 C 0 H 0 N 0 O 0 S 0 0.0 C 3 H 5 N 1 O 1 S 1 103.14 103.009186 C natural (2R)-2-amino-3-sulfanylpropanoic acid (R)-cysteine 2-amino-3-mercaptopropanoic acid 2-amino-3-mercaptopropionic acid 2-azanyl-3-sulfanylpropanoic acid 3-mercapto-L-alanine Cys Cysteine (C, Cys) L-(+)-cysteine L-cysteine alpha-amino-beta-mercaptopropanoic acid alpha-amino-beta-mercaptopropionic acid alpha-amino-beta-thiolpropionic acid beta-mercaptoalanine half-cystine thioserine PSI-MOD MOD:00014 From DeltaMass: Average Mass: 121. L-cysteine residue A protein modification that effectively converts a source amino acid residue to an L-cysteine. ChEBI:29950 DeltaMass:0 PubMed:1310545 PubMed:15790858 PubMed:3447159 PubMed:6692818 PubMed:7338899 RESID:AA0005 (2R)-2-amino-3-sulfanylpropanoic acid (R)-cysteine 2-amino-3-mercaptopropanoic acid 2-amino-3-mercaptopropionic acid 2-azanyl-3-sulfanylpropanoic acid 3-mercapto-L-alanine Cys Cysteine (C, Cys) L-(+)-cysteine L-cysteine alpha-amino-beta-mercaptopropanoic acid alpha-amino-beta-mercaptopropionic acid alpha-amino-beta-thiolpropionic acid beta-mercaptoalanine half-cystine thioserine A protein modification that effectively converts a source amino acid residue to an L-glutamic acid. 0.0 C 0 H 0 N 0 O 0 0.0 C 5 H 7 N 1 O 3 129.12 129.04259 E natural (2S)-2-aminopentanedioic acid 1-aminopropane-1,3-dicarboxylic acid 2-aminoglutaric acid 2-azanylpentanedioic acid Glu L-glutamic acid alpha-aminoglutaric acid glutaminic acid PSI-MOD MOD:00015 L-glutamic acid residue A protein modification that effectively converts a source amino acid residue to an L-glutamic acid. ChEBI:29972 DeltaMass:0 PubMed:1881881 PubMed:4565668 PubMed:4922541 PubMed:6692818 PubMed:9326660 PubMed:957425 RESID:AA0006 (2S)-2-aminopentanedioic acid 1-aminopropane-1,3-dicarboxylic acid 2-aminoglutaric acid 2-azanylpentanedioic acid Glu L-glutamic acid alpha-aminoglutaric acid glutaminic acid A protein modification that effectively converts a source amino acid residue to an L-glutamine. 0.0 C 0 H 0 N 0 O 0 0.0 C 5 H 8 N 2 O 2 128.13 128.05858 Q natural (2S)-2-amino-5-pentanediamic acid 2,5-bis(azanyl)-5-oxopentanoic acid 2,5-diamino-5-oxopentanoic acid 2-amino-4-carbamoylbutanoic acid 2-aminoglutaramic acid Gln L-glutamine alpha-amino-gamma-carbamylbutyric acid glutamic acid 5-amide glutamic acid gamma-amide glutamide PSI-MOD MOD:00016 L-glutamine residue glutamic acid gamma-amide glutamide A protein modification that effectively converts a source amino acid residue to an L-glutamine. ChEBI:30011 DeltaMass:0 PubMed:3340166 PubMed:6692818 PubMed:9342308 RESID:AA0007 (2S)-2-amino-5-pentanediamic acid 2,5-bis(azanyl)-5-oxopentanoic acid 2,5-diamino-5-oxopentanoic acid 2-amino-4-carbamoylbutanoic acid 2-aminoglutaramic acid Gln L-glutamine alpha-amino-gamma-carbamylbutyric acid glutamic acid 5-amide A protein modification that effectively converts a source amino acid residue to a glycine. 0.0 C 0 H 0 N 0 O 0 0.0 C 2 H 3 N 1 O 1 57.05 57.021465 G natural Gly aminoacetic acid aminoethanoic acid azanylethanoic acid glycine glycocoll PSI-MOD MOD:00017 glycine residue A protein modification that effectively converts a source amino acid residue to a glycine. ChEBI:29947 DeltaMass:0 PubMed:1310545 PubMed:6692818 RESID:AA0008 Gly aminoacetic acid aminoethanoic acid azanylethanoic acid glycine glycocoll A protein modification that effectively converts a source amino acid residue to an L-histidine. 0.0 C 0 H 0 N 0 O 0 0.0 C 6 H 7 N 3 O 1 137.14 137.05891 H natural (2S)-2-amino-3-(1H-imidazol-4-yl)propanoic acid (2S)-2-amino-3-(1H-imidazol-5-yl)propanoic acid [tautomer] 2-azanyl-3-(1H-imidazol-4-yl)propanoic acid 2-azanyl-3-(1H-imidazol-5-yl)propanoic acid [tautomer] 4-(2-amino-2-carboxyethyl)imidazole His L-histidine alpha-amino-beta-(4-imidazole)propionic acid glyoxaline-5-alanine PSI-MOD MOD:00018 L-histidine residue A protein modification that effectively converts a source amino acid residue to an L-histidine. ChEBI:29979 DeltaMass:0 PubMed:14342316 PubMed:2722967 PubMed:512 PubMed:5460889 PubMed:6129252 PubMed:6692818 PubMed:6876174 RESID:AA0009 (2S)-2-amino-3-(1H-imidazol-4-yl)propanoic acid (2S)-2-amino-3-(1H-imidazol-5-yl)propanoic acid [tautomer] 2-azanyl-3-(1H-imidazol-4-yl)propanoic acid 2-azanyl-3-(1H-imidazol-5-yl)propanoic acid [tautomer] 4-(2-amino-2-carboxyethyl)imidazole His L-histidine alpha-amino-beta-(4-imidazole)propionic acid glyoxaline-5-alanine A protein modification that effectively converts a source amino acid residue to an L-isoleucine. 0.0 C 0 H 0 N 0 O 0 0.0 C 6 H 11 N 1 O 1 113.16 113.08406 I natural (2S,3S)-2-amino-3-methylpentanoic acid 2-azanyl-3-methylpentanoic acid 3-methyl-norvaline Ile Isoleucyl L-erythro-isoleucine L-isoleucine alpha-amino-beta-methylvaleric acid PSI-MOD MOD:00019 L-isoleucine residue A protein modification that effectively converts a source amino acid residue to an L-isoleucine. ChEBI:30009 DeltaMass:0 PubMed:6692818 RESID:AA0010 (2S,3S)-2-amino-3-methylpentanoic acid 2-azanyl-3-methylpentanoic acid 3-methyl-norvaline Ile Isoleucyl L-erythro-isoleucine L-isoleucine alpha-amino-beta-methylvaleric acid A protein modification that effectively converts a source amino acid residue to an L-leucine. 0.0 C 0 H 0 N 0 O 0 0.0 C 6 H 11 N 1 O 1 113.16 113.08406 L natural (2S)-2-amino-4-methylpentanoic acid 2-azanyl-4-methylpentanoic acid 4-methyl-norvaline L-leucine Leu alpha-amino-gamma-methylvaleric acid alpha-aminoisocaproic acid PSI-MOD MOD:00020 L-leucine residue A protein modification that effectively converts a source amino acid residue to an L-leucine. ChEBI:30006 DeltaMass:0 PubMed:11478885 PubMed:6692818 RESID:AA0011 (2S)-2-amino-4-methylpentanoic acid 2-azanyl-4-methylpentanoic acid 4-methyl-norvaline L-leucine Leu alpha-amino-gamma-methylvaleric acid alpha-aminoisocaproic acid A protein modification that effectively converts a source amino acid residue to L-lysine. 0.0 C 0 H 0 N 0 O 0 0.0 C 6 H 12 N 2 O 1 128.18 128.09496 K natural (2S)-2,6-diaminohexanoic acid 2,6-bis(azanyl)hexanoic acid 6-amino-L-norleucine ACT_SITE Schiff-base intermediate with substrate L-lysine Lys alpha,epsilon-diaminocaproic acid PSI-MOD MOD:00021 L-lysine residue A protein modification that effectively converts a source amino acid residue to L-lysine. ChEBI:29967 DeltaMass:0 PubMed:3106962 PubMed:6120171 PubMed:6692818 RESID:AA0012 (2S)-2,6-diaminohexanoic acid 2,6-bis(azanyl)hexanoic acid 6-amino-L-norleucine ACT_SITE Schiff-base intermediate with substrate L-lysine Lys alpha,epsilon-diaminocaproic acid A protein modification that effectively converts a source amino acid residue to L-methionine. 0.0 C 0 H 0 N 0 O 0 S 0 0.0 C 5 H 9 N 1 O 1 S 1 131.19 131.04048 M natural (2S)-2-amino-4-(methylsulfanyl)butanoic acid 2-amino-4-(methylthio)butanoic acid 2-amino-4-(methylthio)butyric acid 2-azanyl-4-(methylsulfanyl)butanoic acid L-(-)-methionine L-methionine Met S-methyl-L-homocysteine alpha-amino-gamma-methylmercaptobutyric acid alpha-amino-gamma-methylthiobutyric acid gamma-methylthio-alpha-aminobutyric acid PSI-MOD MOD:00022 From DeltaMass: Average Mass: 149 L-methionine residue A protein modification that effectively converts a source amino acid residue to L-methionine. ChEBI:29983 DeltaMass:0 PubMed:6411710 PubMed:6692818 RESID:AA0013 (2S)-2-amino-4-(methylsulfanyl)butanoic acid 2-amino-4-(methylthio)butanoic acid 2-amino-4-(methylthio)butyric acid 2-azanyl-4-(methylsulfanyl)butanoic acid L-(-)-methionine L-methionine Met S-methyl-L-homocysteine alpha-amino-gamma-methylmercaptobutyric acid alpha-amino-gamma-methylthiobutyric acid gamma-methylthio-alpha-aminobutyric acid A protein modification that effectively converts a source amino acid residue to L-phenylalanine. 0.0 C 0 H 0 N 0 O 0 0.0 C 9 H 9 N 1 O 1 147.18 147.06842 F natural (2S)-2-amino-3-phenylpropanoic acid 2-azanyl-3-phenylpropanoic acid L-phenylalanine Phe alpha-amino-beta-phenylpropionic acid PSI-MOD MOD:00023 L-phenylalanine residue A protein modification that effectively converts a source amino acid residue to L-phenylalanine. ChEBI:29997 DeltaMass:0 PubMed:6692818 RESID:AA0014 (2S)-2-amino-3-phenylpropanoic acid 2-azanyl-3-phenylpropanoic acid L-phenylalanine Phe alpha-amino-beta-phenylpropionic acid A protein modification that effectively converts a source amino acid residue to L-proline. 0.0 C 0 H 0 N 0 O 0 0.0 C 5 H 7 N 1 O 1 97.12 97.052765 P natural (2S)-2-pyrrolidinecarboxylic acid L-proline Pro pyrrolidine-2-carboxylic acid PSI-MOD MOD:00024 L-proline residue A protein modification that effectively converts a source amino acid residue to L-proline. ChEBI:30017 DeltaMass:0 PubMed:6692818 PubMed:8547259 RESID:AA0015 (2S)-2-pyrrolidinecarboxylic acid L-proline Pro pyrrolidine-2-carboxylic acid A protein modification that effectively converts a source amino acid residue to L-serine. 0.0 C 0 H 0 N 0 O 0 0.0 C 3 H 5 N 1 O 2 87.08 87.03203 S natural (2S)-2-amino-3-hydroxypropanoic acid 2-azanyl-3-hydroxypropanoic acid 3-hydroxy-L-alanine L-serine Ser alpha-amino-beta-hydroxypropionic acid beta-hydroxyalanine PSI-MOD MOD:00025 L-serine residue A protein modification that effectively converts a source amino acid residue to L-serine. ChEBI:29999 DeltaMass:0 PubMed:4399050 PubMed:6692818 RESID:AA0016 (2S)-2-amino-3-hydroxypropanoic acid 2-azanyl-3-hydroxypropanoic acid 3-hydroxy-L-alanine L-serine Ser alpha-amino-beta-hydroxypropionic acid beta-hydroxyalanine A protein modification that effectively converts a source amino acid residue to L-threonine. 0.0 C 0 H 0 N 0 O 0 0.0 C 4 H 7 N 1 O 2 101.1 101.047676 T natural (2S,3R)-2-amino-3-hydroxybutanoic acid 2-azanyl-3-hydroxybutanoic acid L-threo-threonine L-threonine Thr alpha-amino-beta-hydroxybutyric acid beta-methylserine PSI-MOD MOD:00026 L-threonine residue A protein modification that effectively converts a source amino acid residue to L-threonine. ChEBI:30013 DeltaMass:0 PubMed:2989287 PubMed:6692818 RESID:AA0017 (2S,3R)-2-amino-3-hydroxybutanoic acid 2-azanyl-3-hydroxybutanoic acid L-threo-threonine L-threonine Thr alpha-amino-beta-hydroxybutyric acid beta-methylserine A protein modification that effectively converts a source amino acid residue to L-tryptophan. 0.0 C 0 H 0 N 0 O 0 0.0 C 11 H 10 N 2 O 1 186.21 186.07932 W natural (2S)-2-amino-3-(1H-indol-3-yl)propanoic acid 2-azanyl-3-(1H-indol-3-yl)propanoic acid L-tryptophan Trp alpha-amino-beta-(3-indolyl)propionoic acid beta(3-indolyl)alanine PSI-MOD MOD:00027 L-tryptophan residue A protein modification that effectively converts a source amino acid residue to L-tryptophan. ChEBI:29954 DeltaMass:0 PubMed:2059637 PubMed:6692818 PubMed:9324768 RESID:AA0018 (2S)-2-amino-3-(1H-indol-3-yl)propanoic acid 2-azanyl-3-(1H-indol-3-yl)propanoic acid L-tryptophan Trp alpha-amino-beta-(3-indolyl)propionoic acid beta(3-indolyl)alanine A protein modification that effectively converts a source amino acid residue to L-tyrosine. 0.0 C 0 H 0 N 0 O 0 0.0 C 9 H 9 N 1 O 2 163.18 163.06332 Y natural (2S)-2-amino-3-(4-hydoxyphenyl)propanoic acid 2-azanyl-3-(4-hydoxyphenyl)propanoic acid L-tyrosine Tyr alpha-amino-beta-(para-hydroxyphenyl)propionic acid p-tyrosine para-hydroxyphenylalanine PSI-MOD MOD:00028 L-tyrosine residue A protein modification that effectively converts a source amino acid residue to L-tyrosine. ChEBI:29975 DeltaMass:0 PubMed:2190093 PubMed:2542938 PubMed:5550972 PubMed:6061414 PubMed:6120171 PubMed:6692818 RESID:AA0019 (2S)-2-amino-3-(4-hydoxyphenyl)propanoic acid 2-azanyl-3-(4-hydoxyphenyl)propanoic acid L-tyrosine Tyr alpha-amino-beta-(para-hydroxyphenyl)propionic acid p-tyrosine para-hydroxyphenylalanine A protein modification that effectively converts a source amino acid residue to an L-valine. 0.0 C 0 H 0 N 0 O 0 0.0 C 5 H 9 N 1 O 1 99.13 99.06841 V natural (2S)-2-amino-3-methylbutanoic acid 2-azanyl-3-methylbutanoic acid L-valine Val alpha-amino-beta-methylbutyric acid alpha-aminoisovaleric acid PSI-MOD MOD:00029 L-valine residue A protein modification that effectively converts a source amino acid residue to an L-valine. ChEBI:30015 DeltaMass:0 PubMed:6692818 RESID:AA0020 (2S)-2-amino-3-methylbutanoic acid 2-azanyl-3-methylbutanoic acid L-valine Val alpha-amino-beta-methylbutyric acid alpha-aminoisovaleric acid A protein modification that effectively converts a source amino acid residue to an N-formyl-L-methionine, a natural pretranslational modification. 0.0 C 0 H 0 N 0 O 0 S 0 0.0 C 6 H 10 N 1 O 2 S 1 160.21 160.04323 M natural N-term (2S)-2-formylamino-4-(methylsulfanyl)butanoic acid 2-formamido-4-(methylsulfanyl)butanoic acid 2-formylamino-4-(methylthio)butanoic acid 2-formylazanyl-4-(methylsulfanyl)butanoic acid MOD_RES N-formylmethionine N-formyl-L-methionine N-formylated L-methionine fMet nformylmet PSI-MOD FormylMet MOD:00030 N-formyl-L-methionine residue A protein modification that effectively converts a source amino acid residue to an N-formyl-L-methionine, a natural pretranslational modification. ChEBI:33718 OMSSA:22 PubMed:10825024 PubMed:11152118 PubMed:2165784 PubMed:3042771 PubMed:8758896 RESID:AA0021#FMET (2S)-2-formylamino-4-(methylsulfanyl)butanoic acid 2-formamido-4-(methylsulfanyl)butanoic acid 2-formylamino-4-(methylthio)butanoic acid 2-formylazanyl-4-(methylsulfanyl)butanoic acid MOD_RES N-formylmethionine N-formyl-L-methionine N-formylated L-methionine fMet nformylmet FormylMet A protein modification that effectively converts a source amino acid residue to an L-selenocysteine, a natural pretranslational modification. 0.0 C 0 H 0 N 0 O 0 Se 0 0.0 C 3 H 5 N 1 O 1 Se 1 150.05 150.95363 U natural (2R)-2-amino-3-selanylpropanoic acid 2-azanyl-3-selanylpropanoic acid 3-selenylalanine L-selenocysteine NON_STD Selenocysteine SeCys Sec selenium cysteine PSI-MOD MOD:00031 L-selenocysteine residue A protein modification that effectively converts a source amino acid residue to an L-selenocysteine, a natural pretranslational modification. ChEBI:30000 PubMed:10523135 PubMed:1066676 PubMed:2037562 PubMed:2963330 PubMed:4734725 PubMed:6076213 PubMed:6217842 PubMed:6714945 RESID:AA0022 (2R)-2-amino-3-selanylpropanoic acid 2-azanyl-3-selanylpropanoic acid 3-selenylalanine L-selenocysteine NON_STD Selenocysteine SeCys Sec selenium cysteine A protein modification that is not chemically categorized. PSI-MOD MOD:00032 This term is for organizational use only and should not be assigned. [JSG] uncategorized protein modification A protein modification that is not chemically categorized. PubMed:18688235 A protein modification that crosslinks two or more amino acid residues with covalent bonds. XLNK-Res-Res PSI-MOD MOD:00033 The covalent bond is formed directly between sidechain atoms. If non-aminoacid atoms are involved in connecting two or more peptide chain residues peptide chain, the connection is classified as a multivalent binding site. crosslinked residues A protein modification that crosslinks two or more amino acid residues with covalent bonds. PubMed:18688235 XLNK-Res-Res A protein modification that effectively cross-links two L-cysteine residues to form L-cystine. -2.02 C 0 H -2 N 0 O 0 S 0 -2.01565 C 6 H 8 N 2 O 2 S 2 204.26 204.00272 C, C natural (2R,2'R)-3,3'-disulfane-1,2-diylbis(2-aminopropanoic acid) 3,3'-disulfane-1,2-diylbis(2-azanylpropanoic acid) 3,3'-dithiobis(2-aminopropanoic acid) 3,3'-dithiobisalanine 3,3'-dithiodialanine Cys2 Cystine ((Cys)2) DISULFID DISULFID Interchain L-cystine XLNK-SCys-SCys beta,beta'-diamino-beta,beta'-dicarboxydiethyldisulfide beta,beta'-dithiodialanine bis(alpha-aminopropionic acid)-beta-disulfide bis(beta-amino-beta-carboxyethyl)disulfide dicysteine PSI-MOD 2-amino-3-(2-amino-2-carboxy-ethyl)disulfanyl-propanoic acid MOD:00034 Cross-link 2; for formation of a disulfide bond between a peptide cysteine and a free cysteine, see MOD:00765. L-cystine (cross-link) A protein modification that effectively cross-links two L-cysteine residues to form L-cystine. ChEBI:16283 DeltaMass:0 PubMed:1988019 PubMed:2001356 PubMed:2076469 PubMed:3083866 PubMed:366603 PubMed:7918467 PubMed:8344916 RESID:AA0025#CYS2 (2R,2'R)-3,3'-disulfane-1,2-diylbis(2-aminopropanoic acid) 3,3'-disulfane-1,2-diylbis(2-azanylpropanoic acid) 3,3'-dithiobis(2-aminopropanoic acid) 3,3'-dithiobisalanine 3,3'-dithiodialanine Cys2 Cystine ((Cys)2) DISULFID DISULFID Interchain L-cystine XLNK-SCys-SCys beta,beta'-diamino-beta,beta'-dicarboxydiethyldisulfide beta,beta'-dithiodialanine bis(alpha-aminopropionic acid)-beta-disulfide bis(beta-amino-beta-carboxyethyl)disulfide dicysteine 2-amino-3-(2-amino-2-carboxy-ethyl)disulfanyl-propanoic acid A protein modification that effectively converts an L-asparagine residue to (2S,3R)-3-hydroxyasparagine. 16.0 C 0 H 0 N 0 O 1 15.994915 C 4 H 6 N 2 O 3 130.1 130.03784 N natural uniprot.ptm:PTM-0369 (2S,3R)-2,4-diamino-3-hydroxy-4-oxobutanoic acid (2S,3R)-2-amino-3-hydroxy-4-butanediamic acid (2S,3R)-3-hydroxyasparagine (3R)3HyAsn 2-azanyl-3-hydroxy-4-butanediamic acid L-erythro-beta-hydroxyasparagine MOD_RES (3R)-3-hydroxyasparagine erythro-beta-hydroxylated L-asparagine PSI-MOD MOD:00035 (2S,3R)-3-hydroxyasparagine A protein modification that effectively converts an L-asparagine residue to (2S,3R)-3-hydroxyasparagine. ChEBI:141853 PubMed:11823643 PubMed:2820791 RESID:AA0026 (2S,3R)-2,4-diamino-3-hydroxy-4-oxobutanoic acid (2S,3R)-2-amino-3-hydroxy-4-butanediamic acid (2S,3R)-3-hydroxyasparagine (3R)3HyAsn 2-azanyl-3-hydroxy-4-butanediamic acid L-erythro-beta-hydroxyasparagine MOD_RES (3R)-3-hydroxyasparagine erythro-beta-hydroxylated L-asparagine A protein modification that effectively converts an L-aspartic acid residue to (2S,3R)-3-hydroxyaspartic acid. 16.0 C 0 H 0 N 0 O 1 15.994915 C 4 H 5 N 1 O 4 131.09 131.02185 D natural Unimod:35 uniprot.ptm:PTM-0371 (2S,3R)-2-amino-3-hydroxybutanedioic acid (2S,3R)-3-hydroxyaspartic acid (3R)3HyAsp 2-amino-3-hydroxysuccinic acid 2-azanyl-3-hydroxybutanedioic acid 3-hydroxyaspartic acid L-erythro-beta-hydroxyaspartic acid MOD_RES (3R)-3-hydroxyaspartate erythro-beta-hydroxylated L-aspartic acid hydroxylationd PSI-MOD Oxidation MOD:00036 (2S,3R)-3-hydroxyaspartic acid A protein modification that effectively converts an L-aspartic acid residue to (2S,3R)-3-hydroxyaspartic acid. ChEBI:141848 OMSSA:59 PubMed:6572939 PubMed:6871167 PubMed:8355279 RESID:AA0027 Unimod:35#D (2S,3R)-2-amino-3-hydroxybutanedioic acid (2S,3R)-3-hydroxyaspartic acid (3R)3HyAsp 2-amino-3-hydroxysuccinic acid 2-azanyl-3-hydroxybutanedioic acid 3-hydroxyaspartic acid L-erythro-beta-hydroxyaspartic acid MOD_RES (3R)-3-hydroxyaspartate erythro-beta-hydroxylated L-aspartic acid hydroxylationd Oxidation A protein modification that effectively converts an L-lysine residue to one of the diastereomeric 5-hydroxy-L-lysine residues. 16.0 C 0 H 0 N 0 O 1 15.994915 C 6 H 12 N 2 O 2 144.17 144.08987 K natural uniprot.ptm:PTM-0044 5-hydroxylated L-lysine 5HyLys PSI-MOD MOD:00037 5-hydroxy-L-lysine A protein modification that effectively converts an L-lysine residue to one of the diastereomeric 5-hydroxy-L-lysine residues. ChEBI:60175 PubMed:18688235 5-hydroxylated L-lysine 5HyLys A protein modification that effectively converts an L-proline residue to 3-hydroxy-L-proline. 16.0 C 0 H 0 N 0 O 1 15.994915 C 5 H 7 N 1 O 2 113.12 113.047676 P natural uniprot.ptm:PTM-0030 (2S,3S)-3-hydroxypyrrolidine-2-carboxylic acid 3-hydroxy-L-proline 3-hydroxylated L-proline 3-trans-hydroxy-L-proline 3HyPro L-threo-3-hydroxyproline MOD_RES 3-hydroxyproline beta-hydroxypyrrolidine-alpha-carboxylic acid PSI-MOD MOD:00038 3-hydroxy-L-proline A protein modification that effectively converts an L-proline residue to 3-hydroxy-L-proline. ChEBI:16889 PubMed:2400108 PubMed:3734192 PubMed:4343807 RESID:AA0029 (2S,3S)-3-hydroxypyrrolidine-2-carboxylic acid 3-hydroxy-L-proline 3-hydroxylated L-proline 3-trans-hydroxy-L-proline 3HyPro L-threo-3-hydroxyproline MOD_RES 3-hydroxyproline beta-hydroxypyrrolidine-alpha-carboxylic acid A protein modification that effectively converts an L-proline residue to 4-hydroxy-L-proline 16.0 C 0 H 0 N 0 O 1 15.994915 C 5 H 7 N 1 O 2 113.12 113.047676 P natural uniprot.ptm:PTM-0043 (2S,4R)-4-hydroxypyrrolidine-2-carboxylic acid 4-hydroxy-L-proline 4-hydroxylated L-proline 4-hydroxyproline 4-trans-hydroxy-L-proline 4HyPro L-threo-4-hydroxyproline MOD_RES 4-hydroxyproline gamma-hydroxypyrrolidine-alpha-carboxylic acid PSI-MOD MOD:00039 4-hydroxy-L-proline A protein modification that effectively converts an L-proline residue to 4-hydroxy-L-proline ChEBI:18095 PubMed:11292863 PubMed:2400108 PubMed:3734192 RESID:AA0030 (2S,4R)-4-hydroxypyrrolidine-2-carboxylic acid 4-hydroxy-L-proline 4-hydroxylated L-proline 4-hydroxyproline 4-trans-hydroxy-L-proline 4HyPro L-threo-4-hydroxyproline MOD_RES 4-hydroxyproline gamma-hydroxypyrrolidine-alpha-carboxylic acid A protein modification that effectively converts an L-glutamine residue to 2-pyrrolidone-5-carboxylic acid. -17.03 C 0 H -3 N -1 O 0 -17.026548 C 5 H 6 N 1 O 2 112.11 112.039856 Q natural N-term Unimod:28 uniprot.ptm:PTM-0261 (2S)-5-oxo-2-pyrrolidinecarboxylic acid 2-oxopyrrolidine-5-carboxylic acid 2-pyrrolidone-5-carboxylic acid 5-oxoproline 5-oxopyrrolidine-2-carboxylic acid 5-pyrrolidone-2-carboxylic acid MOD_RES Pyrrolidone carboxylic acid N-pyrrolidone carboxyl (N terminus) PCA PyrGlu(Gln) Pyroglutamic Acid formed from Gln Pyroglutamyl ntermpeppyroq pyroglutamic acid PSI-MOD Gln->pyro-Glu Pyro-glu from Q MOD:00040 DeltaMass gives a formula C 5 H 5 N 1 O 2 with mass 111.1 2-pyrrolidone-5-carboxylic acid (Gln) A protein modification that effectively converts an L-glutamine residue to 2-pyrrolidone-5-carboxylic acid. ChEBI:30652 DeltaMass:123 OMSSA:110 PubMed:10214721 PubMed:1836357 PubMed:26343 PubMed:3473473 RESID:AA0031#GLN Unimod:28#Q (2S)-5-oxo-2-pyrrolidinecarboxylic acid 2-oxopyrrolidine-5-carboxylic acid 2-pyrrolidone-5-carboxylic acid 5-oxoproline 5-oxopyrrolidine-2-carboxylic acid 5-pyrrolidone-2-carboxylic acid MOD_RES Pyrrolidone carboxylic acid N-pyrrolidone carboxyl (N terminus) PCA PyrGlu(Gln) Pyroglutamic Acid formed from Gln Pyroglutamyl ntermpeppyroq pyroglutamic acid Gln->pyro-Glu Pyro-glu from Q A protein modification that effectively converts an L-glutamic acid residue to L-gamma-carboxyglutamic acid. 44.01 C 1 H 0 N 0 O 2 43.98983 C 6 H 7 N 1 O 5 173.12 173.03242 E natural Unimod:299 uniprot.ptm:PTM-0039 (3S)-3-aminopropane-1,1,3-tricarboxylic acid (3S)-3-azanylpropane-1,1,3-tricarboxylic acid 3-amino-1,1,3-propanetricarboxylic acid 3-azanylpropane-1,1,3-tricarboxylic acid 4-carboxyglutamic acid 4CbxGlu Carboxy Glutamyl L-gamma-carboxyglutamic acid MOD_RES 4-carboxyglutamate gamma-carboxylated L-glutamic acid gammacarboxyle PSI-MOD 1-carboxyglutamic acid Carboxy Carboxylation MOD:00041 DeltaMass has an incorrect formula C 6 H 7 N 5 O 1 (N and O reversed) with mass 173. L-gamma-carboxyglutamic acid A protein modification that effectively converts an L-glutamic acid residue to L-gamma-carboxyglutamic acid. DeltaMass:217 OMSSA:48 PubMed:10517147 PubMed:1807167 PubMed:3263814 PubMed:4528109 PubMed:7457858 PubMed:8135347 PubMed:8868490 PubMed:9188685 RESID:AA0032 Unimod:299#E (3S)-3-aminopropane-1,1,3-tricarboxylic acid (3S)-3-azanylpropane-1,1,3-tricarboxylic acid 3-amino-1,1,3-propanetricarboxylic acid 3-azanylpropane-1,1,3-tricarboxylic acid 4-carboxyglutamic acid 4CbxGlu Carboxy Glutamyl L-gamma-carboxyglutamic acid MOD_RES 4-carboxyglutamate gamma-carboxylated L-glutamic acid gammacarboxyle 1-carboxyglutamic acid Carboxy Carboxy Carboxylation A protein modification that effectively converts an L-aspartic acid residue to L-aspartic 4-phosphoric anhydride. 79.98 C 0 H 1 N 0 O 3 P 1 79.96633 C 4 H 6 N 1 O 6 P 1 195.07 194.99327 D natural Unimod:21 uniprot.ptm:PTM-0038 (2S)-2-amino-4-oxo-4-(phosphonooxy)butanoic acid 2-aminobutanedioic 4-phosphoric anhydride 2-azanyl-4-oxo-4-(phosphonooxy)butanoic acid 4-oxo-O-phosphono-L-homoserine 4-phosphoaspartic acid 4-phosphorylated L-aspartatic acid ACT_SITE 4-aspartylphosphate intermediate L-aspartic 4-phosphoric anhydride MOD_RES 4-aspartylphosphate PAsp beta-aspartyl phosphate PSI-MOD Phospho Phosphorylation MOD:00042 L-aspartic 4-phosphoric anhydride A protein modification that effectively converts an L-aspartic acid residue to L-aspartic 4-phosphoric anhydride. ChEBI:15836 PubMed:4357737 RESID:AA0033 Unimod:21#D (2S)-2-amino-4-oxo-4-(phosphonooxy)butanoic acid 2-aminobutanedioic 4-phosphoric anhydride 2-azanyl-4-oxo-4-(phosphonooxy)butanoic acid 4-oxo-O-phosphono-L-homoserine 4-phosphoaspartic acid 4-phosphorylated L-aspartatic acid ACT_SITE 4-aspartylphosphate intermediate L-aspartic 4-phosphoric anhydride MOD_RES 4-aspartylphosphate PAsp beta-aspartyl phosphate Phospho Phosphorylation A protein modification that effectively converts an L-cysteine residue to S-phospho-L-cysteine. 79.98 C 0 H 1 N 0 O 3 P 1 S 0 79.96633 C 3 H 6 N 1 O 4 P 1 S 1 183.12 182.97551 C natural Unimod:21 uniprot.ptm:PTM-0251 (2R)-2-amino-3-(phosphonosulfanyl)propanoic acid 2-azanyl-3-(phosphonosulfanyl)propanoic acid ACT_SITE Phosphocysteine intermediate MOD_RES Phosphocysteine PCys S-phospho-L-cysteine S-phosphonocysteine S-phosphorylated L-cysteine S3-phosphocysteine cysteine phosphate thioester PSI-MOD Phospho Phosphorylation MOD:00043 S-phospho-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-phospho-L-cysteine. PubMed:3142516 PubMed:7961745 PubMed:8128219 RESID:AA0034 Unimod:21#C (2R)-2-amino-3-(phosphonosulfanyl)propanoic acid 2-azanyl-3-(phosphonosulfanyl)propanoic acid ACT_SITE Phosphocysteine intermediate MOD_RES Phosphocysteine PCys S-phospho-L-cysteine S-phosphonocysteine S-phosphorylated L-cysteine S3-phosphocysteine cysteine phosphate thioester Phospho Phosphorylation A protein modification that effectively converts an L-histidine residue to tele-phospho-L-histidine (N-tau-phospho-L-histidine, 1'-phospho-L-histidine). 79.98 C 0 H 1 N 0 O 3 P 1 79.96633 C 6 H 8 N 3 O 4 P 1 217.12 217.02524 H natural uniprot.ptm:PTM-0325 (2S)-2-amino-3-(1-phosphono-1H-imidazol-4-yl)propanoic acid 1'-phospho-L-histidine 2-azanyl-3-(1-phosphono-1H-imidazol-4-yl)propanoic acid ACT_SITE Tele-phosphohistidine intermediate MOD_RES Tele-phosphohistidine N(tau)-phosphohistidine N1-phosphonohistidine NE2-phosphonohistidine NtPHis Ntau-phosphorylated L-histidine histidine-N(epsilon)-phosphate histidine-N1'-phosphate tele-phosphohistidine PSI-MOD Phospho Phosphorylation histidine-3-phosphate MOD:00044 1'-phospho-L-histidine A protein modification that effectively converts an L-histidine residue to tele-phospho-L-histidine (N-tau-phospho-L-histidine, 1'-phospho-L-histidine). PubMed:11038361 PubMed:5642389 PubMed:6692818 RESID:AA0035 (2S)-2-amino-3-(1-phosphono-1H-imidazol-4-yl)propanoic acid 1'-phospho-L-histidine 2-azanyl-3-(1-phosphono-1H-imidazol-4-yl)propanoic acid ACT_SITE Tele-phosphohistidine intermediate MOD_RES Tele-phosphohistidine N(tau)-phosphohistidine N1-phosphonohistidine NE2-phosphonohistidine NtPHis Ntau-phosphorylated L-histidine histidine-N(epsilon)-phosphate histidine-N1'-phosphate tele-phosphohistidine Phospho Phosphorylation histidine-3-phosphate A protein modification that effectively converts an L-histidine residue to pros-phospho-L-histidine (N-pi-phospho-L-histidine, 3'-phospho-L-histidine). 79.98 C 0 H 1 N 0 O 3 P 1 79.96633 C 6 H 8 N 3 O 4 P 1 217.12 217.02524 H natural uniprot.ptm:PTM-0260 (2S)-2-amino-3-(3-phosphono-3H-imidazol-4-yl)propanoic acid 2-azanyl-3-(3-phosphono-3H-imidazol-4-yl)propanoic acid 3'-phospho-L-histidine ACT_SITE Pros-phosphohistidine intermediate MOD_RES Pros-phosphohistidine N(pi)-phosphohistidine N3-phosphonohistidine ND1-phosphonohistidine NpPHis Npi-phosphorylated L-histidine histidine-N(delta)-phosphate histidine-N3'-phosphate pros-phosphohistidine PSI-MOD Phospho Phosphorylation histidine-1-phosphate MOD:00045 3'-phospho-L-histidine A protein modification that effectively converts an L-histidine residue to pros-phospho-L-histidine (N-pi-phospho-L-histidine, 3'-phospho-L-histidine). PubMed:1549615 PubMed:5642389 PubMed:6692818 PubMed:7669763 PubMed:7803390 RESID:AA0036 (2S)-2-amino-3-(3-phosphono-3H-imidazol-4-yl)propanoic acid 2-azanyl-3-(3-phosphono-3H-imidazol-4-yl)propanoic acid 3'-phospho-L-histidine ACT_SITE Pros-phosphohistidine intermediate MOD_RES Pros-phosphohistidine N(pi)-phosphohistidine N3-phosphonohistidine ND1-phosphonohistidine NpPHis Npi-phosphorylated L-histidine histidine-N(delta)-phosphate histidine-N3'-phosphate pros-phosphohistidine Phospho Phosphorylation histidine-1-phosphate A protein modification that effectively converts an L-serine residue to O-phospho-L-serine. 79.98 C 0 H 1 N 0 O 3 P 1 79.96633 C 3 H 6 N 1 O 5 P 1 167.06 166.99835 S natural Unimod:21 uniprot.ptm:PTM-0253 (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine OPSer Phospho Seryl phosphorylations serine phosphate ester PSI-MOD Phospho Phosphorylation MOD:00046 O-phospho-L-serine A protein modification that effectively converts an L-serine residue to O-phospho-L-serine. ChEBI:15811 DeltaMass:0 OMSSA:6 PubMed:12923550 PubMed:4065410 PubMed:8061611 RESID:AA0037 Unimod:21#S (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine OPSer Phospho Seryl phosphorylations serine phosphate ester Phospho Phosphorylation A protein modification that effectively converts an L-threonine residue to O-phospho-L-threonine. 79.98 C 0 H 1 N 0 O 3 P 1 79.96633 C 4 H 8 N 1 O 5 P 1 181.08 181.014 T natural Unimod:21 uniprot.ptm:PTM-0254 (2S,3R)-2-amino-3-(phosphonooxy)butanoic acid 2-amino-3-hydroxybutanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)butanoic acid MOD_RES Phosphothreonine O-phospho-L-threonine O-phosphorylated L-threonine O3-phosphothreonine OPThr Phospho Threonyl phosphorylationt threonine phosphate ester PSI-MOD Phospho Phosphorylation MOD:00047 O-phospho-L-threonine A protein modification that effectively converts an L-threonine residue to O-phospho-L-threonine. ChEBI:21967 DeltaMass:0 OMSSA:7 PubMed:12923550 PubMed:7678926 RESID:AA0038 Unimod:21#T (2S,3R)-2-amino-3-(phosphonooxy)butanoic acid 2-amino-3-hydroxybutanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)butanoic acid MOD_RES Phosphothreonine O-phospho-L-threonine O-phosphorylated L-threonine O3-phosphothreonine OPThr Phospho Threonyl phosphorylationt threonine phosphate ester Phospho Phosphorylation A protein modification that effectively converts an L-tyrosine residue to O4'-phospho-L-tyrosine. 79.98 C 0 H 1 N 0 O 3 P 1 79.96633 C 9 H 10 N 1 O 5 P 1 243.15 243.02966 Y natural Unimod:21 uniprot.ptm:PTM-0255 (2S)-2-amino-3-(4-phosphonooxyphenyl)propanoic acid 2-amino-3-(4-hydroxyphenyl)propanoic acid 4'-phosphate 2-azanyl-3-(4-phosphonooxyphenyl)propanoic acid MOD_RES Phosphotyrosine O4'-phospho-L-tyrosine O4'-phosphorylated L-tyrosine O4-phosphotyrosine OPTyr Phospho Tyrosinyl phosphorylationy tyrosine phosphate PSI-MOD Phospho Phosphorylation MOD:00048 O4'-phospho-L-tyrosine A protein modification that effectively converts an L-tyrosine residue to O4'-phospho-L-tyrosine. DeltaMass:0 OMSSA:8 PubMed:10226369 PubMed:1725475 RESID:AA0039 Unimod:21#Y (2S)-2-amino-3-(4-phosphonooxyphenyl)propanoic acid 2-amino-3-(4-hydroxyphenyl)propanoic acid 4'-phosphate 2-azanyl-3-(4-phosphonooxyphenyl)propanoic acid MOD_RES Phosphotyrosine O4'-phospho-L-tyrosine O4'-phosphorylated L-tyrosine O4-phosphotyrosine OPTyr Phospho Tyrosinyl phosphorylationy tyrosine phosphate Phospho Phosphorylation A protein modification that effectively converts an L-histidine residue to diphthamide. 143.21 C 7 H 15 N 2 O 1 143.11789 1+ C 13 H 22 N 5 O 2 280.35 280.1768 H natural Unimod:375 uniprot.ptm:PTM-0118 (2R)-1-amino-4-(4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-2-yl)-N,N,N-trimethyl-1-oxobutan-2-aminium (3-[4-(2-amino-2-carboxy-ethyl)-1H-imidazol-2-yl]-1-carbamoyl-propyl)-trimethylammonium 1-azanyl-4-(4-[2-azanyl-2-carboxyethyl]-1H-imidazol-2-yl)-N,N,N-trimethyl-1-oxobutan-2-azanium 2'-[3-carboxamido-3-(trimethylammonio)propyl]-L-histidine 2-[(R)-3-carboxamido-3-(trimethylammonio)propyl]-4-((S)-2-amino-2-carboxyethyl)-1H-imidazole 2-[3-carboxamido-3-(trimethylammonio)propyl]histidine 2-amino-3-[[2-(3-amino-3-carbamoyl-prop-1-enyl)-1,1,3-trimethyl-2,3-dihydroimidazol-5-yl]]propanoic acid 2-amino-4-[[5-(2-amino-2-carboxylato-ethyl)-1,1,3-trimethyl-2,3-dihydroimidazol-2-yl]]but-3-enamide Diphth MOD_RES Diphthamide alpha-(aminocarbonyl)-4-(2-amino-2-carboxyethyl)-N,N,N-trimethyl-1H-imidazole-2-propanaminium diphthamide diphthamide (from histidine) PSI-MOD Diphthamide MOD:00049 2'-[3-carboxamido-3-(trimethylammonio)propyl]-L-histidine A protein modification that effectively converts an L-histidine residue to diphthamide. ChEBI:16692 DeltaMass:122 PubMed:15316019 PubMed:7430147 RESID:AA0040 Unimod:375#H (2R)-1-amino-4-(4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-2-yl)-N,N,N-trimethyl-1-oxobutan-2-aminium (3-[4-(2-amino-2-carboxy-ethyl)-1H-imidazol-2-yl]-1-carbamoyl-propyl)-trimethylammonium 1-azanyl-4-(4-[2-azanyl-2-carboxyethyl]-1H-imidazol-2-yl)-N,N,N-trimethyl-1-oxobutan-2-azanium 2'-[3-carboxamido-3-(trimethylammonio)propyl]-L-histidine 2-[(R)-3-carboxamido-3-(trimethylammonio)propyl]-4-((S)-2-amino-2-carboxyethyl)-1H-imidazole 2-[3-carboxamido-3-(trimethylammonio)propyl]histidine 2-amino-3-[[2-(3-amino-3-carbamoyl-prop-1-enyl)-1,1,3-trimethyl-2,3-dihydroimidazol-5-yl]]propanoic acid 2-amino-4-[[5-(2-amino-2-carboxylato-ethyl)-1,1,3-trimethyl-2,3-dihydroimidazol-2-yl]]but-3-enamide Diphth MOD_RES Diphthamide alpha-(aminocarbonyl)-4-(2-amino-2-carboxyethyl)-N,N,N-trimethyl-1H-imidazole-2-propanaminium diphthamide diphthamide (from histidine) Diphthamide Diphthamide A protein modification that effectively converts an L-alanine residue to N-acetyl-L-alanine. 42.04 C 2 H 2 N 0 O 1 42.010567 C 5 H 8 N 1 O 2 114.12 114.055504 A natural N-term uniprot.ptm:PTM-0199 (2S)-2-(acetamido)propanoic acid 2-(acetylamino)propanoic acid 2-(acetylazanyl)propanoic acid AcAla MOD_RES N-acetylalanine N-acetyl-L-alanine N-acetylated L-alanine acetylalanine PSI-MOD MOD:00050 N-acetyl-L-alanine A protein modification that effectively converts an L-alanine residue to N-acetyl-L-alanine. PubMed:363452 PubMed:4700463 RESID:AA0041 (2S)-2-(acetamido)propanoic acid 2-(acetylamino)propanoic acid 2-(acetylazanyl)propanoic acid AcAla MOD_RES N-acetylalanine N-acetyl-L-alanine N-acetylated L-alanine acetylalanine A protein modification that effectively converts an L-aspartic acid residue to N-acetyl-L-aspartic acid. 42.04 C 2 H 2 N 0 O 1 42.010567 C 6 H 8 N 1 O 4 158.13 158.04533 D natural N-term uniprot.ptm:PTM-0200 (2S)-2-(acetamido)butanedioic acid 2-(acetylamino)butanedioic acid 2-(acetylazanyl)butanedioic acid AcAsp MOD_RES N-acetylaspartate N-acetyl-L-aspartic acid N-acetylated L-aspartic acid acetylaspartic acid PSI-MOD MOD:00051 N-acetyl-L-aspartic acid A protein modification that effectively converts an L-aspartic acid residue to N-acetyl-L-aspartic acid. ChEBI:21547 PubMed:1560020 PubMed:2395459 RESID:AA0042 (2S)-2-(acetamido)butanedioic acid 2-(acetylamino)butanedioic acid 2-(acetylazanyl)butanedioic acid AcAsp MOD_RES N-acetylaspartate N-acetyl-L-aspartic acid N-acetylated L-aspartic acid acetylaspartic acid A protein modification that effectively converts an L-cysteine residue to N-acetyl-L-cysteine. 42.04 C 2 H 2 N 0 O 1 S 0 42.010567 C 5 H 8 N 1 O 2 S 1 146.18 146.02757 C natural N-term uniprot.ptm:PTM-0201 (2R)-2-acetamido-3-sulfanylpropanoic acid 2-acetylamino-3-mercaptopropanoic acid 2-acetylamino-3-sulfanylpropanoic acid 2-acetylazanyl-3-sulfanylpropanoic acid MOD_RES N-acetylcysteine N-acetyl-L-cysteine N-acetylated cysteine N-acetylcysteine NAcCys PSI-MOD Acetyl MOD:00052 incidental to RESID:AA0223 N-acetyl-L-cysteine A protein modification that effectively converts an L-cysteine residue to N-acetyl-L-cysteine. ChEBI:28939 PubMed:11857757 PubMed:11999733 PubMed:12175151 PubMed:14730666 PubMed:1500421 PubMed:15350136 PubMed:6725286 RESID:AA0043 (2R)-2-acetamido-3-sulfanylpropanoic acid 2-acetylamino-3-mercaptopropanoic acid 2-acetylamino-3-sulfanylpropanoic acid 2-acetylazanyl-3-sulfanylpropanoic acid MOD_RES N-acetylcysteine N-acetyl-L-cysteine N-acetylated cysteine N-acetylcysteine NAcCys Acetyl A protein modification that effectively converts an L-glutamic acid residue to N-acetyl-L-glutamic acid. 42.04 C 2 H 2 N 0 O 1 42.010567 C 7 H 10 N 1 O 4 172.16 172.06099 E natural N-term uniprot.ptm:PTM-0202 (2S)-2-(acetamido)pentanedioic acid 2-(acetylamino)pentanedioic acid 2-(acetylazanyl)pentanedioic acid AcGlu MOD_RES N-acetylglutamate N-acetyl-L-glutamic acid N-acetylated L-glutamic acid acetylglutamic acid PSI-MOD MOD:00053 N-acetyl-L-glutamic acid A protein modification that effectively converts an L-glutamic acid residue to N-acetyl-L-glutamic acid. ChEBI:17533 PubMed:6725286 RESID:AA0044 (2S)-2-(acetamido)pentanedioic acid 2-(acetylamino)pentanedioic acid 2-(acetylazanyl)pentanedioic acid AcGlu MOD_RES N-acetylglutamate N-acetyl-L-glutamic acid N-acetylated L-glutamic acid acetylglutamic acid A protein modification that effectively converts an L-glutamine residue to N-acetyl-L-glutamine. 42.04 C 2 H 2 N 0 O 1 42.010567 C 7 H 11 N 2 O 3 171.18 171.07697 Q artifact N-term (2S)-2-acetamido-5-pentanediamic acid 2-acetylamino-5-amino-5-oxopentanoic acid 2-acetylamino-5-pentanediamic acid 2-acetylazanyl-5-azanyl-5-oxopentanoic acid AcGln N-acetyl-L-glutamine N-acetylated L-glutamine acetylglutamine PSI-MOD MOD:00054 This is a deprecated entry in RESID. It probably does not occur naturally [JSG]. N-acetyl-L-glutamine A protein modification that effectively converts an L-glutamine residue to N-acetyl-L-glutamine. RESID:AA0045 (2S)-2-acetamido-5-pentanediamic acid 2-acetylamino-5-amino-5-oxopentanoic acid 2-acetylamino-5-pentanediamic acid 2-acetylazanyl-5-azanyl-5-oxopentanoic acid AcGln N-acetyl-L-glutamine N-acetylated L-glutamine acetylglutamine A protein modification that effectively converts a glycine residue to N-acetylglycine. 42.04 C 2 H 2 N 0 O 1 42.010567 C 4 H 6 N 1 O 2 100.1 100.039856 G natural N-term uniprot.ptm:PTM-0203 (acetylamino)acetic acid (acetylazanyl)ethanoic acid 2-(acetamido)ethanoic acid 2-(acetylamino)ethanoic acid AcGly MOD_RES N-acetylglycine N-acetylated glycine N-acetylglycine aceturic acid PSI-MOD MOD:00055 N-acetylglycine A protein modification that effectively converts a glycine residue to N-acetylglycine. PubMed:272676 PubMed:5545094 PubMed:6754709 RESID:AA0046 (acetylamino)acetic acid (acetylazanyl)ethanoic acid 2-(acetamido)ethanoic acid 2-(acetylamino)ethanoic acid AcGly MOD_RES N-acetylglycine N-acetylated glycine N-acetylglycine aceturic acid A protein modification that effectively converts an L-isoleucine residue to N-acetyl-L-isoleucine. 42.04 C 2 H 2 N 0 O 1 42.010567 C 8 H 14 N 1 O 2 156.2 156.10245 I artifact N-term uniprot.ptm:PTM-0204 (2S,3S)-2-acetamido-3-methylpentanoic acid 2-acetylamino-3-methylpentanoic acid 2-acetylazanyl-3-methylpentanoic acid AcIle N-acetyl-L-isoleucine N-acetylated L-isoleucine acetylisoleucine PSI-MOD MOD:00056 This is a deprecated entry in RESID. It probably does not occur naturally [JSG]. N-acetyl-L-isoleucine A protein modification that effectively converts an L-isoleucine residue to N-acetyl-L-isoleucine. PubMed:8034631 RESID:AA0047 (2S,3S)-2-acetamido-3-methylpentanoic acid 2-acetylamino-3-methylpentanoic acid 2-acetylazanyl-3-methylpentanoic acid AcIle N-acetyl-L-isoleucine N-acetylated L-isoleucine acetylisoleucine A protein modification that effectively converts an L-lysine residue to N2-acetyl-L-lysine. 42.04 C 2 H 2 N 0 O 1 42.010567 C 8 H 15 N 2 O 2 171.22 171.11336 K artifact N-term (2S)-2-acetamido-6-aminohexanoic acid 2-acetylamino-6-aminohexanoic acid 2-acetylazanyl-6-azanylhexanoic acid N2-acetyl-L-lysine N2-acetylated L-lysine N2-acetyllysine N2AcLys PSI-MOD Acetyl MOD:00057 This is a deprecated entry in RESID. It probably does not occur naturally [JSG]. N2-acetyl-L-lysine A protein modification that effectively converts an L-lysine residue to N2-acetyl-L-lysine. PubMed:11857757 PubMed:11999733 PubMed:12175151 PubMed:14730666 PubMed:15350136 RESID:AA0048 (2S)-2-acetamido-6-aminohexanoic acid 2-acetylamino-6-aminohexanoic acid 2-acetylazanyl-6-azanylhexanoic acid N2-acetyl-L-lysine N2-acetylated L-lysine N2-acetyllysine N2AcLys Acetyl A protein modification that effectively converts an L-methionine to N-acetyl-L-methionine. 42.04 C 2 H 2 N 0 O 1 S 0 42.010567 C 7 H 12 N 1 O 2 S 1 174.24 174.05887 M natural N-term uniprot.ptm:PTM-0205 (2S)-2-acetamido-4-(methylsulfanyl)butanoic acid 2-acetylamino-4-(methylsulfanyl)butanoic acid 2-acetylamino-4-(methylthio)butanoic acid 2-acetylazanyl-4-(methylsulfanyl)butanoic acid AcMet MOD_RES N-acetylmethionine N-acetyl-L-methionine N-acetylated L-methionine acetylmethionine methionamine PSI-MOD MOD:00058 N-acetyl-L-methionine A protein modification that effectively converts an L-methionine to N-acetyl-L-methionine. PubMed:7944406 RESID:AA0049 (2S)-2-acetamido-4-(methylsulfanyl)butanoic acid 2-acetylamino-4-(methylsulfanyl)butanoic acid 2-acetylamino-4-(methylthio)butanoic acid 2-acetylazanyl-4-(methylsulfanyl)butanoic acid AcMet MOD_RES N-acetylmethionine N-acetyl-L-methionine N-acetylated L-methionine acetylmethionine methionamine A protein modification that effectively converts an L-proline residue to N-acetyl-L-proline. 42.04 C 2 H 2 N 0 O 1 42.010567 C 7 H 10 N 1 O 2 140.16 140.07115 P natural N-term uniprot.ptm:PTM-0206 (2S)-1-acetyl-2-pyrrolidinecarboxylic acid 1-acetylproline MOD_RES N-acetylproline N-acetyl-L-proline N-acetylated L-proline N-acetylproline NAcPro acetylproline PSI-MOD MOD:00059 N-acetyl-L-proline A protein modification that effectively converts an L-proline residue to N-acetyl-L-proline. PubMed:2928307 RESID:AA0050 (2S)-1-acetyl-2-pyrrolidinecarboxylic acid 1-acetylproline MOD_RES N-acetylproline N-acetyl-L-proline N-acetylated L-proline N-acetylproline NAcPro acetylproline A protein modification that effectively converts an L-serine residue to N-acetyl-L-serine. 42.04 C 2 H 2 N 0 O 1 42.010567 C 5 H 8 N 1 O 3 130.12 130.05042 S natural N-term uniprot.ptm:PTM-0207 (2S)-2-acetamido-3-hydroxypropanoic acid 2-acetylamino-3-hydroxypropanoic acid 2-acetylazanyl-3-hydroxypropanoic acid MOD_RES N-acetylserine N-acetyl-L-serine N-acetylated L-serine N-acetylserine NAcSer PSI-MOD Acetyl MOD:00060 N-acetyl-L-serine A protein modification that effectively converts an L-serine residue to N-acetyl-L-serine. PubMed:11857757 PubMed:11999733 PubMed:12175151 PubMed:14730666 PubMed:15350136 PubMed:1880797 PubMed:2106685 PubMed:6997045 RESID:AA0051 (2S)-2-acetamido-3-hydroxypropanoic acid 2-acetylamino-3-hydroxypropanoic acid 2-acetylazanyl-3-hydroxypropanoic acid MOD_RES N-acetylserine N-acetyl-L-serine N-acetylated L-serine N-acetylserine NAcSer Acetyl A protein modification that effectively converts an L-threonine residue to N-acetyl-L-threonine. 42.04 C 2 H 2 N 0 O 1 42.010567 C 6 H 10 N 1 O 3 144.15 144.06607 T natural N-term uniprot.ptm:PTM-0208 (2S,3R)-2-acetamido-3-hydroxybutanoic acid 2-acetylamino-3-hydroxybutanoic acid 2-acetylazanyl-3-hydroxybutanoic acid MOD_RES N-acetylthreonine N-acetyl-L-threonine N-acetylated L-threonine N-acetylthreonine N-methylcarbonylthreonine NAcThr PSI-MOD Acetyl Acetylation MOD:00061 N-acetyl-L-threonine A protein modification that effectively converts an L-threonine residue to N-acetyl-L-threonine. PubMed:11857757 PubMed:11999733 PubMed:12175151 PubMed:14730666 PubMed:15350136 PubMed:2106685 PubMed:6997045 RESID:AA0052 (2S,3R)-2-acetamido-3-hydroxybutanoic acid 2-acetylamino-3-hydroxybutanoic acid 2-acetylazanyl-3-hydroxybutanoic acid MOD_RES N-acetylthreonine N-acetyl-L-threonine N-acetylated L-threonine N-acetylthreonine N-methylcarbonylthreonine NAcThr Acetyl Acetylation A protein modification that effectively converts an L-tyrosine residue to N-acetyl-L-tyrosine. 42.04 C 2 H 2 N 0 O 1 42.010567 C 11 H 12 N 1 O 3 206.22 206.08171 Y natural N-term uniprot.ptm:PTM-0209 (2S)-2-acetamido-3-(4-hydoxyphenyl)propanoic acid 2-acetylamino-3-(4-hydoxyphenyl)propanoic acid 2-acetylazanyl-3-(4-hydoxyphenyl)propanoic acid AcTyr MOD_RES N-acetyltyrosine N-acetyl-L-tyrosine N-acetylated L-tyrosine N-acetyltyrosine PSI-MOD Acetyl MOD:00062 N-acetyl-L-tyrosine A protein modification that effectively converts an L-tyrosine residue to N-acetyl-L-tyrosine. PubMed:11857757 PubMed:11999733 PubMed:12175151 PubMed:14730666 PubMed:15350136 PubMed:2506074 PubMed:475783 RESID:AA0053 (2S)-2-acetamido-3-(4-hydoxyphenyl)propanoic acid 2-acetylamino-3-(4-hydoxyphenyl)propanoic acid 2-acetylazanyl-3-(4-hydoxyphenyl)propanoic acid AcTyr MOD_RES N-acetyltyrosine N-acetyl-L-tyrosine N-acetylated L-tyrosine N-acetyltyrosine Acetyl A protein modification that effectively converts an L-valine residue to N-acetyl-L-valine. 42.04 C 2 H 2 N 0 O 1 42.010567 C 7 H 12 N 1 O 2 142.18 142.0868 V natural N-term uniprot.ptm:PTM-0210 (2S)-2-acetamido-3-methylbutanoic acid 2-acetylamino-3-methylbutanoic acid 2-acetylazanyl-3-methylbutanoic acid AcVal MOD_RES N-acetylvaline N-acetyl-L-valine N-acetylated L-valine N-acetylvaline PSI-MOD MOD:00063 N-acetyl-L-valine A protein modification that effectively converts an L-valine residue to N-acetyl-L-valine. PubMed:1735421 RESID:AA0054 (2S)-2-acetamido-3-methylbutanoic acid 2-acetylamino-3-methylbutanoic acid 2-acetylazanyl-3-methylbutanoic acid AcVal MOD_RES N-acetylvaline N-acetyl-L-valine N-acetylated L-valine N-acetylvaline A protein modification that effectively converts an L-lysine residue to N6-acetyl-L-lysine. 42.04 C 2 H 2 N 0 O 1 42.010567 C 8 H 14 N 2 O 2 170.21 170.10553 K natural Unimod:1 uniprot.ptm:PTM-0190 (2S)-6-acetamido-2-aminohexanoic acid 6-acetylamino-2-aminohexanoic acid 6-acetylazanyl-2-aminohexanoic acid MOD_RES N6-acetyllysine N(zeta)-acetyllysine N6-acetyl-L-lysine N6-acetylated L-lysine N6AcLys acetylk epsilon-acetyllysine PSI-MOD Acetyl Acetylation MOD:00064 N6-acetyl-L-lysine A protein modification that effectively converts an L-lysine residue to N6-acetyl-L-lysine. ChEBI:17752 DeltaMass:214 OMSSA:24 PubMed:11369851 PubMed:11857757 PubMed:11999733 PubMed:12175151 PubMed:14730666 PubMed:15350136 PubMed:1680872 PubMed:670159 RESID:AA0055 Unimod:1#K (2S)-6-acetamido-2-aminohexanoic acid 6-acetylamino-2-aminohexanoic acid 6-acetylazanyl-2-aminohexanoic acid MOD_RES N6-acetyllysine N(zeta)-acetyllysine N6-acetyl-L-lysine N6-acetylated L-lysine N6AcLys acetylk epsilon-acetyllysine Acetyl Acetylation A protein modification that effectively converts an L-cysteine residue to S-acetyl-L-cysteine. 42.04 C 2 H 2 N 0 O 1 S 0 42.010567 C 5 H 7 N 1 O 2 S 1 145.18 145.01974 C natural Unimod:1 (2R)-3-acetylsulfanyl-2-aminopropanoic acid 2-amino-3-(acetylthio)propanoic acid 2-azanyl-3-(acetylsulfanyl)propanoic acid ACT_SITE S-acetylcysteine intermediate S-acetyl-L-cysteine S-acetylcysteine SAcCys cysteine acetate thioester PSI-MOD Acetyl Acetylation MOD:00065 S-acetyl-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-acetyl-L-cysteine. PubMed:11857757 PubMed:11999733 PubMed:12175151 PubMed:1310545 PubMed:14730666 PubMed:15350136 RESID:AA0056 Unimod:1#C (2R)-3-acetylsulfanyl-2-aminopropanoic acid 2-amino-3-(acetylthio)propanoic acid 2-azanyl-3-(acetylsulfanyl)propanoic acid ACT_SITE S-acetylcysteine intermediate S-acetyl-L-cysteine S-acetylcysteine SAcCys cysteine acetate thioester Acetyl Acetylation A protein modification that effectively converts a glycine residue to N-formylglycine. 28.01 C 1 H 0 N 0 O 1 27.994915 C 3 H 4 N 1 O 2 86.07 86.0242 G natural N-term uniprot.ptm:PTM-0211 (formylamino)acetic acid (formylamino)ethanoic acid (formylazanyl)ethanoic acid 2-formamidoacetic acid 2-formamidoethanoic acid MOD_RES N-formylglycine N(alpha)-formylglycine N-formylated glycine N-formylglycine NFoGly PSI-MOD MOD:00066 N-formylglycine A protein modification that effectively converts a glycine residue to N-formylglycine. PubMed:5139483 RESID:AA0057 (formylamino)acetic acid (formylamino)ethanoic acid (formylazanyl)ethanoic acid 2-formamidoacetic acid 2-formamidoethanoic acid MOD_RES N-formylglycine N(alpha)-formylglycine N-formylated glycine N-formylglycine NFoGly A protein modification that effectively converts a glycine residue to N-D-glucuronoylglycine. 176.12 C 6 H 8 N 0 O 6 176.03209 C 8 H 12 N 1 O 7 234.18 234.06137 G natural N-term uniprot.ptm:PTM-0331 2-(glucuronoylamino)ethanoic acid MOD_RES N-D-glucuronoyl glycine N-D-glucuronoyl-glycine N-D-glucuronyl-glycine NGlcAGly ntermpepglucuronylg PSI-MOD Glucuronyl MOD:00067 N-D-glucuronoylglycine A protein modification that effectively converts a glycine residue to N-D-glucuronoylglycine. OMSSA:50 PubMed:10858503 PubMed:12716131 PubMed:6493057 PubMed:7398618 RESID:AA0058 2-(glucuronoylamino)ethanoic acid MOD_RES N-D-glucuronoyl glycine N-D-glucuronoyl-glycine N-D-glucuronyl-glycine NGlcAGly ntermpepglucuronylg Glucuronyl A protein modification that effectively converts a glycine residue to N-myristoylglycine. 210.36 C 14 H 26 N 0 O 1 210.19836 C 16 H 30 N 1 O 2 268.42 268.22766 G natural N-term Unimod:45 uniprot.ptm:PTM-0221 (tetradecanoylamino)ethanoic acid LIPID N-myristoyl glycine N-(1-oxotetradecyl)glycine N-(C14:0 aliphatic acyl)glycine N-myristoyl-glycine N-myristoylated glycine N-myristylglycine N-tetradecanoylglycine NMyrGly ntermpepmyristoylationg PSI-MOD Myristoyl Myristoylation MOD:00068 N-myristoylglycine A protein modification that effectively converts a glycine residue to N-myristoylglycine. OMSSA:80 PubMed:11955007 PubMed:11955008 PubMed:1326520 PubMed:1386601 PubMed:6436247 PubMed:7543369 RESID:AA0059 Unimod:45#G (tetradecanoylamino)ethanoic acid LIPID N-myristoyl glycine N-(1-oxotetradecyl)glycine N-(C14:0 aliphatic acyl)glycine N-myristoyl-glycine N-myristoylated glycine N-myristylglycine N-tetradecanoylglycine NMyrGly ntermpepmyristoylationg Myristoyl Myristoylation A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-L-cysteine. 238.41 C 16 H 30 N 0 O 1 S 0 238.22966 C 19 H 36 N 1 O 2 S 1 342.56 342.24667 C natural N-term uniprot.ptm:PTM-0222 (2R)-2-hexadecanoylamino-3-sulfanylpropanoic acid 2-hexadecanamido-3-sulfanylpropanoic acid 2-hexadecanoylamino-3-mercaptopropanoic acid LIPID N-palmitoyl cysteine N-(1-oxahexadecyl)-L-cysteine N-hexadecanoylated L-cysteine N-palmitoyl-L-cysteine N-palmitoylated L-cysteine NPamCys PSI-MOD Palmitoyl Palmitoylation MOD:00069 incidental to RESID:AA0107 incidental to RESID:AA0309 N-palmitoyl-L-cysteine A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-L-cysteine. PubMed:10896212 PubMed:4575979 PubMed:9056182 PubMed:9593755 RESID:AA0060 (2R)-2-hexadecanoylamino-3-sulfanylpropanoic acid 2-hexadecanamido-3-sulfanylpropanoic acid 2-hexadecanoylamino-3-mercaptopropanoic acid LIPID N-palmitoyl cysteine N-(1-oxahexadecyl)-L-cysteine N-hexadecanoylated L-cysteine N-palmitoyl-L-cysteine N-palmitoylated L-cysteine NPamCys Palmitoyl Palmitoylation A protein modification that effectively converts an L-alanine residue to N-methyl-L-alanine. 14.03 C 1 H 2 N 0 O 0 14.01565 C 4 H 7 N 1 O 1 85.11 85.052765 A natural N-term uniprot.ptm:PTM-0214 (2S)-2-methylaminopropanoic acid 2-methylazanylpropanoic acid MOD_RES N-methylalanine N-methyl-L-alanine N-methylalanine N-methylated L-alanine NMe1Ala PSI-MOD Methyl Methylation MOD:00070 Polypeptides with monomethylated amino terminals can undergo premature cleavage during the coupling step of an Edman degradation. This can result in "preview" with both a residue and the following residue being seen from the first step on through a sequence [JSG]. N-methyl-L-alanine A protein modification that effectively converts an L-alanine residue to N-methyl-L-alanine. ChEBI:17519 PubMed:323502 PubMed:337304 PubMed:7007074 RESID:AA0061 (2S)-2-methylaminopropanoic acid 2-methylazanylpropanoic acid MOD_RES N-methylalanine N-methyl-L-alanine N-methylalanine N-methylated L-alanine NMe1Ala Methyl Methylation A protein modification that effectively converts an L-alanine residue to N,N,N-trimethyl-L-alanine. 43.09 C 3 H 7 N 0 O 0 43.054226 1+ C 6 H 13 N 1 O 1 115.18 115.09917 A natural N-term uniprot.ptm:PTM-0177 (1S)-1-carboxy-N,N,N-trimethylethanaminium (1S)-1-carboxy-N,N,N-trimethylethanazanium (2S)-2-(trimethylammonio)propanoic acid MOD_RES N,N,N-trimethylalanine N,N,N-trimethyl-L-alanine N,N,N-trimethylalanine cation N,N,N-trimethylalaninium N,N,N-trimethylated L-alanine N2Me3+Ala NMe3Ala PSI-MOD Trimethyl tri-Methylation MOD:00071 N,N,N-trimethyl-L-alanine A protein modification that effectively converts an L-alanine residue to N,N,N-trimethyl-L-alanine. PubMed:12590383 PubMed:332162 PubMed:3979397 PubMed:6778808 PubMed:7715456 RESID:AA0062 (1S)-1-carboxy-N,N,N-trimethylethanaminium (1S)-1-carboxy-N,N,N-trimethylethanazanium (2S)-2-(trimethylammonio)propanoic acid MOD_RES N,N,N-trimethylalanine N,N,N-trimethyl-L-alanine N,N,N-trimethylalanine cation N,N,N-trimethylalaninium N,N,N-trimethylated L-alanine N2Me3+Ala NMe3Ala Trimethyl tri-Methylation A protein modification that effectively converts a glycine residue to N-methylglycine. 14.03 C 1 H 2 N 0 O 0 14.01565 C 3 H 5 N 1 O 1 71.08 71.03712 G natural N-term uniprot.ptm:PTM-0483 L-sarcosine MOD_RES N-methylglycine N-methylated glycine N-methylglycine NMe1Gly Sar Sarcosine Sarcosyl methylaminoacetic acid methylaminoethanoic acid PSI-MOD Methyl Methylation MOD:00072 DeltaMass also has an entry for the free amino acid. Polypeptides with monomethylated amino terminals can undergo premature cleavage during the coupling step of an Edman degradation. This can result in "preview" with both a residue and the following residue being seen from the first step on through a sequence [JSG]. N-methylglycine A protein modification that effectively converts a glycine residue to N-methylglycine. ChEBI:15611 DeltaMass:0 PubMed:1593629 RESID:AA0063 L-sarcosine MOD_RES N-methylglycine N-methylated glycine N-methylglycine NMe1Gly Sar Sarcosine Sarcosyl methylaminoacetic acid methylaminoethanoic acid Methyl Methylation A protein modification that effectively converts an L-methionine residue to N-methyl-L-methionine. 14.03 C 1 H 2 N 0 O 0 S 0 14.01565 C 6 H 11 N 1 O 1 S 1 145.22 145.05614 M natural N-term uniprot.ptm:PTM-0217 (2S)-2-methylamino-4-(methylsulfanyl)butanoic acid 2-methylamino-4-(methylthio)butanoic acid MOD_RES N-methylmethionine Methyl Methionyl N-methyl-L-methionine N-methylated L-methionine N-methylmethionine NMe1Met PSI-MOD Methyl Methylation MOD:00073 Polypeptides with monomethylated amino terminals can undergo premature cleavage during the coupling step of an Edman degradation. This can result in "preview" with both a residue and the following residue being seen from the first step on through a sequence [JSG]. N-methyl-L-methionine A protein modification that effectively converts an L-methionine residue to N-methyl-L-methionine. DeltaMass:169 PubMed:323502 PubMed:3298225 RESID:AA0064 (2S)-2-methylamino-4-(methylsulfanyl)butanoic acid 2-methylamino-4-(methylthio)butanoic acid MOD_RES N-methylmethionine Methyl Methionyl N-methyl-L-methionine N-methylated L-methionine N-methylmethionine NMe1Met Methyl Methylation A protein modification that effectively converts an L-phenylalanine residue to N-methyl-L-phenylalanine. 14.03 C 1 H 2 N 0 O 0 14.01565 C 10 H 11 N 1 O 1 161.2 161.08406 F natural N-term uniprot.ptm:PTM-0218 (2S)-2-methylamino-3-phenylpropanoic acid MOD_RES N-methylphenylalanine N-methyl-L-phenylalanine N-methylated L-phenylalanine N-methylphenylalanine NMe1Phe PSI-MOD Methyl Methylation MOD:00074 Polypeptides with monomethylated amino terminals can undergo premature cleavage during the coupling step of an Edman degradation. This can result in "preview" with both a residue and the following residue being seen from the first step on through a sequence [JSG]. N-methyl-L-phenylalanine A protein modification that effectively converts an L-phenylalanine residue to N-methyl-L-phenylalanine. PubMed:2577730 PubMed:413571 RESID:AA0065 (2S)-2-methylamino-3-phenylpropanoic acid MOD_RES N-methylphenylalanine N-methyl-L-phenylalanine N-methylated L-phenylalanine N-methylphenylalanine NMe1Phe Methyl Methylation A protein modification that effectively converts an L-proline residue to N,N-dimethyl-L-proline. 29.06 C 2 H 5 N 0 O 0 29.038576 1+ C 7 H 13 N 1 O 1 127.19 127.09917 P natural N-term Unimod:529 uniprot.ptm:PTM-0179 (2S)-2-carboxy-1,1-dimethylpyrrolidinium 1,1-dimethyl-L-prolinium MOD_RES N,N-dimethylproline N,N-dimethyl-L-proline N,N-dimethyl-L-prolinium N,N-dimethylated L-proline NMe2Pro stachydrin PSI-MOD Delta:H(5)C(2) Dimethyl Dimethylation of proline residue MOD:00075 Unimod terminal specification corrected [JSG]. N,N-dimethyl-L-proline A protein modification that effectively converts an L-proline residue to N,N-dimethyl-L-proline. ChEBI:21451 PubMed:12964758 PubMed:14570711 PubMed:193025 PubMed:3882426 PubMed:6254758 RESID:AA0066 Unimod:529 (2S)-2-carboxy-1,1-dimethylpyrrolidinium 1,1-dimethyl-L-prolinium MOD_RES N,N-dimethylproline N,N-dimethyl-L-proline N,N-dimethyl-L-prolinium N,N-dimethylated L-proline NMe2Pro stachydrin Delta:H(5)C(2) Dimethyl Dimethylation of proline residue A protein modification that effectively converts an L-arginine residue to symmetric dimethylarginine, N(omega),N'(omega)-dimethyl-L-arginine. 28.05 C 2 H 4 N 0 O 0 28.0313 C 8 H 16 N 4 O 1 184.24 184.13242 R natural Unimod:36 uniprot.ptm:PTM-0287 (2S)-2-amino-5-[((methylamino)(methylimino)methyl)amino]pentanoic acid MOD_RES Omega-N-methylated arginine MOD_RES Symmetric dimethylarginine N3,N4-dimethylarginine N5-[(methylamino)(methylimino)methyl]ornithine NG,N'G-dimethylarginine NoNo'Me2Arg omega-N,omega-N'-dimethyl-L-arginine omega-N,omega-N'-dimethylated L-arginine symmetric dimethylarginine PSI-MOD Dimethyl di-Methylation MOD:00076 symmetric dimethyl-L-arginine A protein modification that effectively converts an L-arginine residue to symmetric dimethylarginine, N(omega),N'(omega)-dimethyl-L-arginine. PubMed:12964758 PubMed:14570711 PubMed:15835918 PubMed:2426402 PubMed:5128665 RESID:AA0067 Unimod:36#R (2S)-2-amino-5-[((methylamino)(methylimino)methyl)amino]pentanoic acid MOD_RES Omega-N-methylated arginine MOD_RES Symmetric dimethylarginine N3,N4-dimethylarginine N5-[(methylamino)(methylimino)methyl]ornithine NG,N'G-dimethylarginine NoNo'Me2Arg omega-N,omega-N'-dimethyl-L-arginine omega-N,omega-N'-dimethylated L-arginine symmetric dimethylarginine Dimethyl di-Methylation A protein modification that effectively converts an L-arginine residue to asymmetric dimethylarginine, N(omega),N(omega)-dimethyl-L-arginine. 28.05 C 2 H 4 N 0 O 0 28.0313 C 8 H 16 N 4 O 1 184.24 184.13242 R natural Unimod:36 uniprot.ptm:PTM-0066 (2S)-2-amino-5-([(dimethylamino)(imino)methyl]amino)pentanoic acid MOD_RES Asymmetric dimethylarginine MOD_RES Omega-N-methylated arginine N5-[(dimethylamino)(imino)methyl]ornithine NG,NG-dimethylarginine NoNoMe2Arg asymmetric dimethylarginine omega-N,omega-N-dimethlyated L-arginine omega-N,omega-N-dimethyl-L-arginine PSI-MOD Dimethyl di-Methylation MOD:00077 asymmetric dimethyl-L-arginine A protein modification that effectively converts an L-arginine residue to asymmetric dimethylarginine, N(omega),N(omega)-dimethyl-L-arginine. ChEBI:17929 PubMed:11152131 PubMed:12964758 PubMed:14570711 PubMed:15835918 PubMed:3032834 RESID:AA0068 Unimod:36#R (2S)-2-amino-5-([(dimethylamino)(imino)methyl]amino)pentanoic acid MOD_RES Asymmetric dimethylarginine MOD_RES Omega-N-methylated arginine N5-[(dimethylamino)(imino)methyl]ornithine NG,NG-dimethylarginine NoNoMe2Arg asymmetric dimethylarginine omega-N,omega-N-dimethlyated L-arginine omega-N,omega-N-dimethyl-L-arginine Dimethyl di-Methylation A protein modification that effectively converts an L-arginine residue to N(omega)-methyl-L-arginine. 14.03 C 1 H 2 N 0 O 0 14.01565 C 7 H 14 N 4 O 1 170.22 170.11676 R natural uniprot.ptm:PTM-0237 (2S)-2-amino-5-[(imino(methylamino)methyl)amino]pentanoic acid MOD_RES Omega-N-methylarginine MOD_RES Omega-N-methylated arginine NG-methylarginine NoMeArg omega-N-methyl-L-arginine omega-N-methylated L-arginine PSI-MOD Methyl Methylation MOD:00078 omega-N-methyl-L-arginine A protein modification that effectively converts an L-arginine residue to N(omega)-methyl-L-arginine. PubMed:11875433 PubMed:15835918 PubMed:2426402 PubMed:5128665 RESID:AA0069 (2S)-2-amino-5-[(imino(methylamino)methyl)amino]pentanoic acid MOD_RES Omega-N-methylarginine MOD_RES Omega-N-methylated arginine NG-methylarginine NoMeArg omega-N-methyl-L-arginine omega-N-methylated L-arginine Methyl Methylation A protein modification that effectively converts an L-asparagine residue to N4-methyl-L-asparagine. 14.03 C 1 H 2 N 0 O 0 14.01565 C 5 H 8 N 2 O 2 128.13 128.05858 N natural Unimod:34 uniprot.ptm:PTM-0183 (2S)-2-amino-N4-methylbutanediamic acid MOD_RES N4-methylasparagine N(gamma)-methylasparagine N-methylasparagine N4-methyl-L-asparagine N4-methylated L-asparagine N4Me1Asn beta-aspartyl methylamide methyln PSI-MOD Methyl Methylation beta-methylasparagine MOD:00079 N4-methyl-L-asparagine A protein modification that effectively converts an L-asparagine residue to N4-methyl-L-asparagine. OMSSA:75 PubMed:11875433 PubMed:2356973 PubMed:3782095 RESID:AA0070 Unimod:34#N (2S)-2-amino-N4-methylbutanediamic acid MOD_RES N4-methylasparagine N(gamma)-methylasparagine N-methylasparagine N4-methyl-L-asparagine N4-methylated L-asparagine N4Me1Asn beta-aspartyl methylamide methyln Methyl Methylation beta-methylasparagine A protein modification that effectively converts an L-glutamine residue to N5-methyl-L-glutamine. 14.03 C 1 H 2 N 0 O 0 14.01565 C 6 H 10 N 2 O 2 142.16 142.07423 Q natural uniprot.ptm:PTM-0185 (2S)-2-amino-5-methylamino-5-oxopentanoic acid 2-amino-N5-methylpentanediamic acid MOD_RES N5-methylglutamine N(delta)-methylglutamine N-methylglutamine N5-methyl-L-glutamine N5-methylated L-glutamine N5Me1Gln gamma-methylglutamine PSI-MOD Methyl Methylation MOD:00080 N5-methyl-L-glutamine A protein modification that effectively converts an L-glutamine residue to N5-methyl-L-glutamine. ChEBI:17592 DeltaMass:166 PubMed:11118225 PubMed:11875433 PubMed:365579 RESID:AA0071 (2S)-2-amino-5-methylamino-5-oxopentanoic acid 2-amino-N5-methylpentanediamic acid MOD_RES N5-methylglutamine N(delta)-methylglutamine N-methylglutamine N5-methyl-L-glutamine N5-methylated L-glutamine N5Me1Gln gamma-methylglutamine Methyl Methylation A protein modification that effectively converts an L-glutamic acid residue to L-glutamate 5-methyl ester. 14.03 C 1 H 2 N 0 O 0 14.01565 C 6 H 9 N 1 O 3 143.14 143.05824 E natural Unimod:34 uniprot.ptm:PTM-0128 (2S)-2-amino-5-methoxy-5-oxopentanoic acid (5)-methyl L-hydrogen glutamate 2-aminopentanedioic acid 5-methyl ester 5-methyl L-2-aminoglutarate 5-methyl L-glutamate 5-methyl esterified L-glutamic acid L-glutamic acid 5-methyl ester MOD_RES Glutamate methyl ester (Glu) O-methyl Glutamyl O5MeGlu glutamic acid 5-methyl ester glutamic acid gamma-methyl ester meestere methyle PSI-MOD Methyl Methylation methyl ester MOD:00081 DeltaMass gives the formula "C 6 H 9 O 1 N 3" with mass 143 (formula incorrect, N and O reversed) [JSG]. L-glutamic acid 5-methyl ester (Glu) A protein modification that effectively converts an L-glutamic acid residue to L-glutamate 5-methyl ester. DeltaMass:167 OMSSA:17 OMSSA:70 PubMed:16888 PubMed:6300110 RESID:AA0072#GLU Unimod:34#E (2S)-2-amino-5-methoxy-5-oxopentanoic acid (5)-methyl L-hydrogen glutamate 2-aminopentanedioic acid 5-methyl ester 5-methyl L-2-aminoglutarate 5-methyl L-glutamate 5-methyl esterified L-glutamic acid L-glutamic acid 5-methyl ester MOD_RES Glutamate methyl ester (Glu) O-methyl Glutamyl O5MeGlu glutamic acid 5-methyl ester glutamic acid gamma-methyl ester meestere methyle Methyl Methylation methyl ester A protein modification that effectively converts an L-histidine residue to pros-methyl-L-histidine (N-pi-methyl-L-histidine, 3'-methyl-L-histidine). 14.03 C 1 H 2 N 0 O 0 14.01565 C 7 H 9 N 3 O 1 151.17 151.07455 H natural uniprot.ptm:PTM-0259 (2S)-2-amino-3-(3-methyl-3H-imidazol-4-yl)propanoic acid 3'-methyl-L-histidine MOD_RES Pros-methylhistidine N(delta)-methylhistidine N(pi)-methylhistidine NpMeHis pros-methylated L-histidine pros-methylhistidine PSI-MOD 1-methylhistidine Methyl Methylation MOD:00082 3'-methyl-L-histidine A protein modification that effectively converts an L-histidine residue to pros-methyl-L-histidine (N-pi-methyl-L-histidine, 3'-methyl-L-histidine). PubMed:10660523 PubMed:11875433 PubMed:3467365 PubMed:6692818 PubMed:8076 PubMed:8645219 RESID:AA0073 (2S)-2-amino-3-(3-methyl-3H-imidazol-4-yl)propanoic acid 3'-methyl-L-histidine MOD_RES Pros-methylhistidine N(delta)-methylhistidine N(pi)-methylhistidine NpMeHis pros-methylated L-histidine pros-methylhistidine 1-methylhistidine Methyl Methylation A protein modification that effectively converts an L-lysine residue to N6,N6,N6-trimethyl-L-lysine. 43.09 C 3 H 7 N 0 O 0 43.054226 1+ C 9 H 19 N 2 O 1 171.26 171.14919 K natural uniprot.ptm:PTM-0187 (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N-trimethylation (of lysine) N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation N6Me3+Lys epsilon-trimethyllysine PSI-MOD Trimethyl tri-Methylation MOD:00083 DeltaMass calculates the mass difference from protonated lysine rather than neutral lysine; for trimethylated lysine starting from protonated lysine see MOD:00855 N6,N6,N6-trimethyl-L-lysine A protein modification that effectively converts an L-lysine residue to N6,N6,N6-trimethyl-L-lysine. ChEBI:17311 PubMed:12590383 PubMed:3145979 PubMed:4304194 PubMed:6778808 PubMed:7093227 PubMed:8453381 RESID:AA0074 (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N-trimethylation (of lysine) N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation N6Me3+Lys epsilon-trimethyllysine Trimethyl tri-Methylation A protein modification that effectively converts an L-lysine residue to N6,N6-dimethyl-L-lysine. 28.05 C 2 H 4 N 0 O 0 28.0313 C 8 H 16 N 2 O 1 156.23 156.12627 K natural Unimod:36 uniprot.ptm:PTM-0188 (2S)-2-amino-6-(dimethylamino)hexanoic acid MOD_RES N6,N6-dimethyllysine N(zeta)-dimethyllysine N6,N6-dimethyl-L-lysine N6,N6-dimethylated L-lysine N6Me2Lys dimethylk epsilon-dimethyllysine lysine derivative Lys(y) PSI-MOD Dimethyl di-Methylation MOD:00084 N6,N6-dimethyl-L-lysine A protein modification that effectively converts an L-lysine residue to N6,N6-dimethyl-L-lysine. OMSSA:36 PubMed:10550045 PubMed:12964758 PubMed:14570711 PubMed:3100523 PubMed:8453381 RESID:AA0075 Unimod:36#K (2S)-2-amino-6-(dimethylamino)hexanoic acid MOD_RES N6,N6-dimethyllysine N(zeta)-dimethyllysine N6,N6-dimethyl-L-lysine N6,N6-dimethylated L-lysine N6Me2Lys dimethylk epsilon-dimethyllysine lysine derivative Lys(y) Dimethyl di-Methylation A protein modification that effectively converts an L-lysine residue to N6-methyl-L-lysine. 14.03 C 1 H 2 N 0 O 0 14.01565 C 7 H 14 N 2 O 1 142.2 142.11061 K natural Unimod:34 uniprot.ptm:PTM-0194 (2S)-2-amino-6-methylaminohexanoic acid MOD_RES N6-methyllysine N(zeta)-methyllysine N-methyl Lysyl N6-methyl-L-lysine N6-methylated L-lysine N6Me1Lys epsilon-methyllysine PSI-MOD Methyl Methylation MOD:00085 N6-methyl-L-lysine A protein modification that effectively converts an L-lysine residue to N6-methyl-L-lysine. ChEBI:17604 DeltaMass:165 PubMed:11875433 PubMed:3926756 RESID:AA0076 Unimod:34#K (2S)-2-amino-6-methylaminohexanoic acid MOD_RES N6-methyllysine N(zeta)-methyllysine N-methyl Lysyl N6-methyl-L-lysine N6-methylated L-lysine N6Me1Lys epsilon-methyllysine Methyl Methylation A protein modification that effectively converts an L-lysine residue to N6-palmitoyl-L-lysine. 238.41 C 16 H 30 N 0 O 1 238.22966 C 22 H 42 N 2 O 2 366.59 366.32462 K natural Unimod:47 uniprot.ptm:PTM-0197 (2S)-2-amino-6-(hexadecanoylamino)hexanoic acid 2-amino-6-(hexadecanamido)hexanoic acid LIPID N6-palmitoyl lysine N(zeta)-palmitoyllysine N6-(1-oxohexadecyl)-L-lysine N6-hexadecanoylated L-lysine N6-palmitoyl-L-lysine N6-palmitoylated L-lysine N6PamLys epsilon-palmitoyllysine palmitoylationk PSI-MOD Palmitoyl Palmitoylation MOD:00086 N6-palmitoyl-L-lysine A protein modification that effectively converts an L-lysine residue to N6-palmitoyl-L-lysine. OMSSA:93 PubMed:2498336 PubMed:7801126 PubMed:7939682 RESID:AA0077 Unimod:47#K (2S)-2-amino-6-(hexadecanoylamino)hexanoic acid 2-amino-6-(hexadecanamido)hexanoic acid LIPID N6-palmitoyl lysine N(zeta)-palmitoyllysine N6-(1-oxohexadecyl)-L-lysine N6-hexadecanoylated L-lysine N6-palmitoyl-L-lysine N6-palmitoylated L-lysine N6PamLys epsilon-palmitoyllysine palmitoylationk Palmitoyl Palmitoylation A protein modification that effectively converts an L-lysine residue to N6-myristoyl-L-lysine. 210.36 C 14 H 26 N 0 O 1 210.19836 C 20 H 38 N 2 O 2 338.54 338.29333 K natural Unimod:45 uniprot.ptm:PTM-0196 (2S)-2-amino-6-(tetradecanoylamino)hexanoic acid 2-amino-6-(tetradecanamido)hexanoic acid LIPID N6-myristoyl lysine N(zeta)-myristoyllysine N6-(1-oxotetradecyl)-L-lysine N6-(C14:0 aliphatic acyl)lysine N6-myristoyl-L-lysine N6-myristoylated L-lysine N6MyrLys epsilon-myristoyllysine myristoylationk PSI-MOD Myristoyl Myristoylation MOD:00087 N6-myristoyl-L-lysine A protein modification that effectively converts an L-lysine residue to N6-myristoyl-L-lysine. OMSSA:81 PubMed:1402651 PubMed:8346241 RESID:AA0078 Unimod:45#K (2S)-2-amino-6-(tetradecanoylamino)hexanoic acid 2-amino-6-(tetradecanamido)hexanoic acid LIPID N6-myristoyl lysine N(zeta)-myristoyllysine N6-(1-oxotetradecyl)-L-lysine N6-(C14:0 aliphatic acyl)lysine N6-myristoyl-L-lysine N6-myristoylated L-lysine N6MyrLys epsilon-myristoyllysine myristoylationk Myristoyl Myristoylation A protein modification that effectively converts an L-threonine residue to O-palmitoyl-L-threonine. 238.41 C 16 H 30 N 0 O 1 238.22966 C 20 H 37 N 1 O 3 339.52 339.27734 T natural Unimod:47 uniprot.ptm:PTM-0242 (2S,3R)-2-amino-3-(hexadecanoyloxy)butanoic acid L-threonine hexadecanoate ester LIPID O-palmitoyl threonine O-hexadecanoylated L-threonine O-palmitoyl-L-threonine O-palmitoylated L-threonine O3-palmitoyl-threonine OPamThr palmitoylationt threonine palmitate ester PSI-MOD Palmitoyl Palmitoylation MOD:00088 O-palmitoyl-L-threonine A protein modification that effectively converts an L-threonine residue to O-palmitoyl-L-threonine. OMSSA:95 PubMed:6642431 PubMed:8413602 RESID:AA0079 Unimod:47#T (2S,3R)-2-amino-3-(hexadecanoyloxy)butanoic acid L-threonine hexadecanoate ester LIPID O-palmitoyl threonine O-hexadecanoylated L-threonine O-palmitoyl-L-threonine O-palmitoylated L-threonine O3-palmitoyl-threonine OPamThr palmitoylationt threonine palmitate ester Palmitoyl Palmitoylation A protein modification that effectively converts an L-serine residue to O-palmitoyl-L-serine. 238.41 C 16 H 30 N 0 O 1 238.22966 C 19 H 35 N 1 O 3 325.49 325.2617 S natural Unimod:47 uniprot.ptm:PTM-0241 (2S)-2-amino-3-(hexadecanoyloxy)propanoic acid ACT_SITE O-palmitoyl serine intermediate L-serine hexadecanoate ester LIPID O-palmitoyl serine O-hexadecanoylated L-serine O-palmitoyl-L-serine O-palmitoylated L-serine O3-palmitoyl-serine OPamSer palmitoylations serine palmitate ester PSI-MOD Palmitoyl Palmitoylation MOD:00089 O-palmitoyl-L-serine A protein modification that effectively converts an L-serine residue to O-palmitoyl-L-serine. OMSSA:94 PubMed:3467339 RESID:AA0080 Unimod:47#S (2S)-2-amino-3-(hexadecanoyloxy)propanoic acid ACT_SITE O-palmitoyl serine intermediate L-serine hexadecanoate ester LIPID O-palmitoyl serine O-hexadecanoylated L-serine O-palmitoyl-L-serine O-palmitoylated L-serine O3-palmitoyl-serine OPamSer palmitoylations serine palmitate ester Palmitoyl Palmitoylation A protein modification that effectively converts an L-alanine residue to L-alanine amide. -0.98 C 0 H 1 N 1 O -1 -0.984016 C 3 H 7 N 2 O 1 87.1 87.05584 A natural C-term uniprot.ptm:PTM-0057 (2S)-2-aminopropanamide AlaN L-alanine amide MOD_RES Alanine amide alaninamide amidated L-alanine PSI-MOD MOD:00090 L-alanine amide A protein modification that effectively converts an L-alanine residue to L-alanine amide. PubMed:1377792 PubMed:2069951 PubMed:8472537 PubMed:952951 RESID:AA0081 (2S)-2-aminopropanamide AlaN L-alanine amide MOD_RES Alanine amide alaninamide amidated L-alanine A protein modification that effectively converts an L-arginine residue to L-arginine amide. -0.98 C 0 H 1 N 1 O -1 -0.984016 C 6 H 14 N 5 O 1 172.21 172.11984 R natural C-term uniprot.ptm:PTM-0060 (2S)-2-amino-5-[(diaminomethylidene)amino]pentanamide 2-amino-5-carbamimidamidopentanamide 2-amino-5-guanidinopentanamide ArgN L-arginine amide MOD_RES Arginine amide amidated L-arginine argininamide PSI-MOD MOD:00091 L-arginine amide A protein modification that effectively converts an L-arginine residue to L-arginine amide. ChEBI:145897 PubMed:2229025 PubMed:2753890 PubMed:743209 RESID:AA0082 (2S)-2-amino-5-[(diaminomethylidene)amino]pentanamide 2-amino-5-carbamimidamidopentanamide 2-amino-5-guanidinopentanamide ArgN L-arginine amide MOD_RES Arginine amide amidated L-arginine argininamide A protein modification that effectively converts an L-asparagine residue to L-asparagine amide. -0.98 C 0 H 1 N 1 O -1 -0.984016 C 4 H 8 N 3 O 2 130.13 130.06165 N natural C-term uniprot.ptm:PTM-0062 (2S)-2-aminobutanediamide AsnN L-asparagine amide MOD_RES Asparagine amide amidated L-asparagine asparaginamide PSI-MOD MOD:00092 L-asparagine amide A protein modification that effectively converts an L-asparagine residue to L-asparagine amide. ChEBI:145898 PubMed:2753132 PubMed:279902 PubMed:3415690 RESID:AA0083 (2S)-2-aminobutanediamide AsnN L-asparagine amide MOD_RES Asparagine amide amidated L-asparagine asparaginamide A protein modification that effectively converts an L-aspartic acid residue to L-aspartic acid 1-amide. -0.98 C 0 H 1 N 1 O -1 -0.984016 C 4 H 7 N 2 O 3 131.11 131.04567 D natural C-term uniprot.ptm:PTM-0063 (2S)-2-amino-1-butanediamic acid 1-amidated L-aspartic acid 3,4-diamino-4-oxobutanoic acid 3-amino-succinamic acid AspN L-aspartic acid 1-amide MOD_RES Aspartic acid 1-amide alpha-asparagine isoasparagine PSI-MOD MOD:00093 L-aspartic acid 1-amide A protein modification that effectively converts an L-aspartic acid residue to L-aspartic acid 1-amide. PubMed:2542051 RESID:AA0084 (2S)-2-amino-1-butanediamic acid 1-amidated L-aspartic acid 3,4-diamino-4-oxobutanoic acid 3-amino-succinamic acid AspN L-aspartic acid 1-amide MOD_RES Aspartic acid 1-amide alpha-asparagine isoasparagine A protein modification that effectively converts an L-cysteine residue to L-cysteine amide. -0.98 C 0 H 1 N 1 O -1 S 0 -0.984016 C 3 H 7 N 2 O 1 S 1 119.16 119.02791 C natural C-term uniprot.ptm:PTM-0102 (2R)-2-amino-3-sulfanylpropanamide 2-amino-3-mercaptopropanamide CysN L-cysteine amide MOD_RES Cysteine amide amidated L-cysteine cysteinamide PSI-MOD MOD:00094 L-cysteine amide A protein modification that effectively converts an L-cysteine residue to L-cysteine amide. PubMed:1892838 PubMed:7149738 RESID:AA0085 (2R)-2-amino-3-sulfanylpropanamide 2-amino-3-mercaptopropanamide CysN L-cysteine amide MOD_RES Cysteine amide amidated L-cysteine cysteinamide A protein modification that effectively converts an L-glutamine residue to L-glutamine amide. -0.98 C 0 H 1 N 1 O -1 -0.984016 C 5 H 10 N 3 O 2 144.15 144.0773 Q natural C-term uniprot.ptm:PTM-0130 (2S)-2-aminopentanediamide GlnN L-glutamine amide MOD_RES Glutamine amide amidated L-glutamine glutaminamide PSI-MOD MOD:00095 L-glutamine amide A protein modification that effectively converts an L-glutamine residue to L-glutamine amide. PubMed:7673220 PubMed:9048550 RESID:AA0086 (2S)-2-aminopentanediamide GlnN L-glutamine amide MOD_RES Glutamine amide amidated L-glutamine glutaminamide A protein modification that effectively converts an L-glutamic acid residue to L-glutamic acid 1-amide. -0.98 C 0 H 1 N 1 O -1 -0.984016 C 5 H 9 N 2 O 3 145.14 145.06131 E natural C-term uniprot.ptm:PTM-0129 (2S)-2-amino-1-pentanediamic acid 1-amidated L-glutamic acid 4,5-diamino-5-oxopentanoic acid GluN L-glutamic acid 1-amide MOD_RES Glutamic acid 1-amide isoglutamine PSI-MOD MOD:00096 L-glutamic acid 1-amide A protein modification that effectively converts an L-glutamic acid residue to L-glutamic acid 1-amide. PubMed:1093875 PubMed:14550575 RESID:AA0087 (2S)-2-amino-1-pentanediamic acid 1-amidated L-glutamic acid 4,5-diamino-5-oxopentanoic acid GluN L-glutamic acid 1-amide MOD_RES Glutamic acid 1-amide isoglutamine A protein modification that effectively converts a glycine residue to glycine amide. -0.98 C 0 H 1 N 1 O -1 -0.984016 C 2 H 5 N 2 O 1 73.07 73.04019 G natural C-term uniprot.ptm:PTM-0132 2-aminoacetamide 2-aminoethanamide 2-azanylethanamide GlyN MOD_RES Glycine amide amidated glycine glycinamide glycine amide PSI-MOD MOD:00097 glycine amide A protein modification that effectively converts a glycine residue to glycine amide. PubMed:13591312 RESID:AA0088 2-aminoacetamide 2-aminoethanamide 2-azanylethanamide GlyN MOD_RES Glycine amide amidated glycine glycinamide glycine amide A protein modification that effectively converts an L-histidine residue to L-histidine amide. -0.98 C 0 H 1 N 1 O -1 -0.984016 C 6 H 9 N 4 O 1 153.16 153.07764 H natural C-term uniprot.ptm:PTM-0148 (2S)-2-amino-3-(1H-imidazol-4-yl)propanamide HisN L-histidine amide MOD_RES Histidine amide amidated L-histidine histidinamide PSI-MOD MOD:00098 L-histidine amide A protein modification that effectively converts an L-histidine residue to L-histidine amide. PubMed:2153586 PubMed:2307683 PubMed:2839478 RESID:AA0089 (2S)-2-amino-3-(1H-imidazol-4-yl)propanamide HisN L-histidine amide MOD_RES Histidine amide amidated L-histidine histidinamide A protein modification that effectively converts an L-isoleucine residue to L-isoleucine amide. -0.98 C 0 H 1 N 1 O -1 -0.984016 C 6 H 13 N 2 O 1 129.18 129.10278 I natural C-term uniprot.ptm:PTM-0161 (2S,3S)-2-amino-3-methylpentanamide IleN L-isoleucine amide MOD_RES Isoleucine amide amidated L-isoleucine isoleucinamide PSI-MOD MOD:00099 L-isoleucine amide A protein modification that effectively converts an L-isoleucine residue to L-isoleucine amide. RESID:AA0090 (2S,3S)-2-amino-3-methylpentanamide IleN L-isoleucine amide MOD_RES Isoleucine amide amidated L-isoleucine isoleucinamide A protein modification that effectively converts an L-leucine residue to L-leucine amide. -0.98 C 0 H 1 N 1 O -1 -0.984016 C 6 H 13 N 2 O 1 129.18 129.10278 L natural C-term uniprot.ptm:PTM-0166 (2S)-2-amino-4-methylpentanamide 2-amino-4-methylvaleramide 2-azanyl-4-methylpentanamide L-leucine amide LeuN MOD_RES Leucine amide alpha-aminoisocaproamide amidated L-leucine leucinamide PSI-MOD MOD:00100 L-leucine amide A protein modification that effectively converts an L-leucine residue to L-leucine amide. PubMed:2578459 RESID:AA0091 (2S)-2-amino-4-methylpentanamide 2-amino-4-methylvaleramide 2-azanyl-4-methylpentanamide L-leucine amide LeuN MOD_RES Leucine amide alpha-aminoisocaproamide amidated L-leucine leucinamide A protein modification that effectively converts an L-lysine residue to L-lysine amide. -0.98 C 0 H 1 N 1 O -1 -0.984016 C 6 H 14 N 3 O 1 144.2 144.1137 K natural C-term uniprot.ptm:PTM-0168 (2S)-2,6-diaminohexanamide L-lysine amide LysN MOD_RES Lysine amide amidated L-lysine lysinamide PSI-MOD MOD:00101 L-lysine amide A protein modification that effectively converts an L-lysine residue to L-lysine amide. PubMed:6579533 RESID:AA0092 (2S)-2,6-diaminohexanamide L-lysine amide LysN MOD_RES Lysine amide amidated L-lysine lysinamide A protein modification that effectively converts an L-methionine residue to L-methionine amide. -0.98 C 0 H 1 N 1 O -1 S 0 -0.984016 C 5 H 11 N 2 O 1 S 1 147.22 147.0592 M natural C-term uniprot.ptm:PTM-0164 (2S)-2-amino-4-(methylsulfanyl)butanamide 2-amino-4-(methylthio)butanamide L-methionine amide MOD_RES Methionine amide MetN amidated L-methionine methioninamide PSI-MOD MOD:00102 L-methionine amide methioninamide A protein modification that effectively converts an L-methionine residue to L-methionine amide. PubMed:4375977 RESID:AA0093 (2S)-2-amino-4-(methylsulfanyl)butanamide 2-amino-4-(methylthio)butanamide L-methionine amide MOD_RES Methionine amide MetN amidated L-methionine A protein modification that effectively converts an L-phenylalanine residue to L-phenylalanine amide. -0.98 C 0 H 1 N 1 O -1 -0.984016 C 9 H 11 N 2 O 1 163.2 163.08714 F natural C-term uniprot.ptm:PTM-0248 (2S)-2-amino-3-phenylpropanamide L-phenylalanine amide MOD_RES Phenylalanine amide PheN amidated L-phenylalanine phenylalaninamide PSI-MOD MOD:00103 L-phenylalanine amide A protein modification that effectively converts an L-phenylalanine residue to L-phenylalanine amide. PubMed:2905621 PubMed:8868490 RESID:AA0094 (2S)-2-amino-3-phenylpropanamide L-phenylalanine amide MOD_RES Phenylalanine amide PheN amidated L-phenylalanine phenylalaninamide A protein modification that effectively converts an L-proline residue to L-proline amide. -0.98 C 0 H 1 N 1 O -1 -0.984016 C 5 H 9 N 2 O 1 113.14 113.07149 P natural C-term uniprot.ptm:PTM-0257 (2S)-pyrrolidine-2-carboxamide L-proline amide MOD_RES Proline amide ProN amidated L-proline prolinamide PSI-MOD MOD:00104 L-proline amide A protein modification that effectively converts an L-proline residue to L-proline amide. PubMed:4982117 PubMed:5760861 RESID:AA0095 (2S)-pyrrolidine-2-carboxamide L-proline amide MOD_RES Proline amide ProN amidated L-proline prolinamide A protein modification that effectively converts an L-serine residue to L-serine amide. -0.98 C 0 H 1 N 1 O -1 -0.984016 C 3 H 7 N 2 O 2 103.1 103.05075 S natural C-term uniprot.ptm:PTM-0275 (2S)-2-amino-3-hydroxypropanamide L-serine amide MOD_RES Serine amide SerN amidated L-serine serinamide PSI-MOD MOD:00105 L-serine amide A protein modification that effectively converts an L-serine residue to L-serine amide. PubMed:743209 RESID:AA0096 (2S)-2-amino-3-hydroxypropanamide L-serine amide MOD_RES Serine amide SerN amidated L-serine serinamide A protein modification that effectively converts an L-threonine residue to L-threonine amide. -0.98 C 0 H 1 N 1 O -1 -0.984016 C 4 H 9 N 2 O 2 117.13 117.06641 T natural C-term uniprot.ptm:PTM-0293 (2S,3R)-2-amino-3-hydroxybutanamide L-threonine amide MOD_RES Threonine amide ThrN amidated L-threonine threoninamide PSI-MOD MOD:00106 L-threonine amide A protein modification that effectively converts an L-threonine residue to L-threonine amide. PubMed:1390774 RESID:AA0097 (2S,3R)-2-amino-3-hydroxybutanamide L-threonine amide MOD_RES Threonine amide ThrN amidated L-threonine threoninamide A protein modification that effectively converts an L-tryptophan residue to L-tryptophan amide. -0.98 C 0 H 1 N 1 O -1 -0.984016 C 11 H 12 N 3 O 1 202.24 202.09804 W natural C-term uniprot.ptm:PTM-0296 (2S)-2-amino-3-(1H-indol-3-yl)propanamide L-tryptophan amide MOD_RES Tryptophan amide TrpN amidated L-tryptophan tryptophanamide PSI-MOD MOD:00107 L-tryptophan amide A protein modification that effectively converts an L-tryptophan residue to L-tryptophan amide. PubMed:3947348 RESID:AA0098 (2S)-2-amino-3-(1H-indol-3-yl)propanamide L-tryptophan amide MOD_RES Tryptophan amide TrpN amidated L-tryptophan tryptophanamide A protein modification that effectively converts an L-tyrosine residue to L-tyrosine amide. -0.98 C 0 H 1 N 1 O -1 -0.984016 C 9 H 11 N 2 O 2 179.2 179.08205 Y natural C-term uniprot.ptm:PTM-0302 (2S)-2-amino-3-(4-hydoxyphenyl)propanamide L-tyrosine amide MOD_RES Tyrosine amide TyrN amidated L-tyrosine tyrosinamide PSI-MOD MOD:00108 L-tyrosine amide A protein modification that effectively converts an L-tyrosine residue to L-tyrosine amide. PubMed:1377792 PubMed:3562898 PubMed:6509012 RESID:AA0099 (2S)-2-amino-3-(4-hydoxyphenyl)propanamide L-tyrosine amide MOD_RES Tyrosine amide TyrN amidated L-tyrosine tyrosinamide A protein modification that effectively converts an L-valine residue to L-valine amide. -0.98 C 0 H 1 N 1 O -1 -0.984016 C 5 H 11 N 2 O 1 115.16 115.087135 V natural C-term uniprot.ptm:PTM-0303 (2S)-2-amino-3-methylbutanamide L-valine amide MOD_RES Valine amide ValN valinamide PSI-MOD MOD:00109 L-valine amide A protein modification that effectively converts an L-valine residue to L-valine amide. PubMed:2578459 PubMed:5465996 RESID:AA0100 (2S)-2-amino-3-methylbutanamide L-valine amide MOD_RES Valine amide ValN valinamide A protein modification that effectively converts an L-cysteine residue to L-cysteine methyl disulfide. 46.09 C 1 H 2 N 0 O 0 S 1 45.98772 C 4 H 7 N 1 O 1 S 2 149.23 148.9969 C natural Unimod:39 uniprot.ptm:PTM-0104 (2R)-2-amino-3-(methyldisulfanediyl)propanoic acid 2-amino-3-(methyldisulfanediyl)propanoic acid 2-amino-3-(methyldithio)propanoic acid 2-amino-3-methyldisulfanylpropanoic acid 2-azanyl-3-(methyldisulfanediyl)-propanoic acid L-3-(methyldithio)alanine L-cysteine methyl disulfide MOD_RES Cysteine methyl disulfide S-methylthio-L-cysteine S-methylthiocysteine methyl methanethiolsulfonate derivatized cysteine methyl methanethiosulfonate derivatized cysteine mmts PSI-MOD Beta-methylthiolation Methylthio MOD:00110 Produced artifactually by reaction of cysteine residues with methyl methanethiosulfonate (MMTS) [JSG], but also naturally in bacteria [PMT]. L-cysteine methyl disulfide A protein modification that effectively converts an L-cysteine residue to L-cysteine methyl disulfide. OMSSA:179 PubMed:10555576 PubMed:163643 PubMed:2056535 PubMed:6381494 RESID:AA0101 Unimod:39#C (2R)-2-amino-3-(methyldisulfanediyl)propanoic acid 2-amino-3-(methyldisulfanediyl)propanoic acid 2-amino-3-(methyldithio)propanoic acid 2-amino-3-methyldisulfanylpropanoic acid 2-azanyl-3-(methyldisulfanediyl)-propanoic acid L-3-(methyldithio)alanine L-cysteine methyl disulfide MOD_RES Cysteine methyl disulfide S-methylthio-L-cysteine S-methylthiocysteine methyl methanethiolsulfonate derivatized cysteine methyl methanethiosulfonate derivatized cysteine mmts Beta-methylthiolation Methylthio Methylthio A protein modification that effectively converts an L-cysteine residue to S-farnesyl-L-cysteine. 204.36 C 15 H 24 N 0 O 0 S 0 204.1878 C 18 H 29 N 1 O 1 S 1 307.5 307.197 C natural Unimod:44 uniprot.ptm:PTM-0277 (2R)-2-amino-3-([(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]sulfanyl)propanoic acid 2-amino-3-(3,7,11-trimethyl-2,6,10-dodecatrienylthio)propanoic acid LIPID S-farnesyl cysteine S-farnesyl Cystenyl S-farnesyl-L-cysteine SFarnCys farnesylationc PSI-MOD Farnesyl Farnesylation MOD:00111 From DeltaMass: (name misspelled "S-farnesyl cystenyl") S-farnesyl-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-farnesyl-L-cysteine. DeltaMass:293 OMSSA:42 PubMed:1409665 PubMed:15609361 PubMed:1872463 PubMed:2684976 RESID:AA0102 Unimod:44#C (2R)-2-amino-3-([(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]sulfanyl)propanoic acid 2-amino-3-(3,7,11-trimethyl-2,6,10-dodecatrienylthio)propanoic acid LIPID S-farnesyl cysteine S-farnesyl Cystenyl S-farnesyl-L-cysteine SFarnCys farnesylationc Farnesyl Farnesylation A protein modification that effectively converts an L-cysteine residue to S-12-hydroxyfarnesyl-L-cysteine. 220.36 C 15 H 24 N 0 O 1 S 0 220.18271 C 18 H 29 N 1 O 2 S 1 323.5 323.1919 C natural Unimod:376 uniprot.ptm:PTM-0269 (2R)-2-amino-3-([(2E,6E,10Z)-12-hydroxy-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]sulfanyl)propanoic acid 2-amino-3-(12-hydroxy-3,7,11-trimethyl-3,6,10-dodecatrienylthio)propanoic acid LIPID S-12-hydroxyfarnesyl cysteine S-12-hydroxyfarnesyl-L-cysteine S12HyFarnCys PSI-MOD Hydroxyfarnesyl hydroxyfarnesyl MOD:00112 S-12-hydroxyfarnesyl-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-12-hydroxyfarnesyl-L-cysteine. PubMed:17790543 RESID:AA0103 Unimod:376 (2R)-2-amino-3-([(2E,6E,10Z)-12-hydroxy-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]sulfanyl)propanoic acid 2-amino-3-(12-hydroxy-3,7,11-trimethyl-3,6,10-dodecatrienylthio)propanoic acid LIPID S-12-hydroxyfarnesyl cysteine S-12-hydroxyfarnesyl-L-cysteine S12HyFarnCys Hydroxyfarnesyl hydroxyfarnesyl A protein modification that effectively converts an L-cysteine residue to S-geranylgeranyl-L-cysteine. 272.48 C 20 H 32 N 0 O 0 S 0 272.2504 C 23 H 37 N 1 O 1 S 1 375.62 375.25958 C natural Unimod:48 uniprot.ptm:PTM-0278 (2R)-2-amino-3-([(2E,6E,10Z)-12-hydroxy-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]sulfanyl)propanoic acid 2-amino-3-(3,7,11,15-tetramethyl-2,6,10,14-hexadecatetraenylthio)propanoic acid LIPID S-geranylgeranyl cysteine S-geranylgeranyl S-geranylgeranyl-L-cysteine SGergerCys geranylgeranylc PSI-MOD Geranyl-geranyl GeranylGeranyl MOD:00113 DeltaMass calculates the mass with two double bonds rather than four S-geranylgeranyl-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-geranylgeranyl-L-cysteine. DeltaMass:0 OMSSA:49 PubMed:1483450 PubMed:15609361 RESID:AA0104 Unimod:48#C (2R)-2-amino-3-([(2E,6E,10Z)-12-hydroxy-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]sulfanyl)propanoic acid 2-amino-3-(3,7,11,15-tetramethyl-2,6,10,14-hexadecatetraenylthio)propanoic acid LIPID S-geranylgeranyl cysteine S-geranylgeranyl S-geranylgeranyl-L-cysteine SGergerCys geranylgeranylc Geranyl-geranyl GeranylGeranyl A protein modification that effectively converts an L-cysteine residue to L-cysteine methyl ester. 14.03 C 1 H 2 N 0 O 0 S 0 14.01565 C 4 H 8 N 1 O 2 S 1 134.17 134.02757 C natural C-term Unimod:34 uniprot.ptm:PTM-0105 2-amino-3-mercaptopropanoic methyl ester 2-amino-3-sulfanylpropanoic methyl ester L-cysteine methyl ester MOD_RES Cysteine methyl ester OMeCys mecysteine methyl (2R)-2-amino-3-sulfanylpropanoate methyl L-cysteinate methyl esterified L-cysteine PSI-MOD Methyl Methylation MOD:00114 Secondary to RESID:AA0102; secondary to RESID:AA0103; secondary to RESID:AA0104. L-cysteine methyl ester A protein modification that effectively converts an L-cysteine residue to L-cysteine methyl ester. PubMed:11875433 PubMed:1872463 RESID:AA0105 Unimod:34#C-term 2-amino-3-mercaptopropanoic methyl ester 2-amino-3-sulfanylpropanoic methyl ester L-cysteine methyl ester MOD_RES Cysteine methyl ester OMeCys mecysteine methyl (2R)-2-amino-3-sulfanylpropanoate methyl L-cysteinate methyl esterified L-cysteine Methyl Methylation A protein modification that effectively converts an L-cysteine residue to S-palmitoyl-L-cysteine. 238.41 C 16 H 30 N 0 O 1 S 0 238.22966 C 19 H 35 N 1 O 2 S 1 341.55 341.23886 C natural Unimod:47 uniprot.ptm:PTM-0281 (2R)-2-amino-3-(hexadecanoylsulfanyl)propanoic acid 2-amino-3-(hexadecanoylthio)propanoic acid ACT_SITE S-palmitoyl cysteine intermediate LIPID S-palmitoyl cysteine S-hexadecanoylated L-cysteine S-palmitoyl-L-cysteine S-palmitoylated L-cysteine S-palmityl Cystenyl SPamCys cysteine hexadecanoate thioester cysteine palmitate thioester PSI-MOD Palmitoyl Palmitoylation MOD:00115 From DeltaMass: (name misspelled "S-palmityl Cystenyl" and formula incorrect, N and O reversed) Formula: C19H35O1N2S1 Monoisotopic Mass Change: 341.239 Average Mass Change: 341.556 S-palmitoyl-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-palmitoyl-L-cysteine. DeltaMass:303 PubMed:1872406 PubMed:3166978 PubMed:8180229 PubMed:8824274 RESID:AA0106 Unimod:47#C (2R)-2-amino-3-(hexadecanoylsulfanyl)propanoic acid 2-amino-3-(hexadecanoylthio)propanoic acid ACT_SITE S-palmitoyl cysteine intermediate LIPID S-palmitoyl cysteine S-hexadecanoylated L-cysteine S-palmitoyl-L-cysteine S-palmitoylated L-cysteine S-palmityl Cystenyl SPamCys cysteine hexadecanoate thioester cysteine palmitate thioester Palmitoyl Palmitoylation A protein modification that effectively converts an L-cysteine residue to S-diacylglycerol-L-cysteine. C natural uniprot.ptm:PTM-0274 (2R)-2-amino-3-[(2S)-2-((9Z)-9-octadecenoyloxy)-3-(hexadecanoyloxy)propyl]sulfanylpropanoic acid 2-amino-3-[(S)-2-((Z)-9-octadecenoyloxy)-3-(hexadecanoyloxy)propyl]thiopropanoic acid LIPID S-diacylglycerol cysteine S-(1-2'-oleoyl-3'-palmitoyl-glycerol)cysteine S-(2',3'-diacylglycerol)-L-cysteine S-diacylglycerol-L-cysteine SAcyl2GlyceroCys PSI-MOD Diacylglycerol diacylglycerol MOD:00116 Incidental to RESID:AA0060. S-diacylglycerol-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-diacylglycerol-L-cysteine. PubMed:10896212 PubMed:4575979 PubMed:9056182 RESID:AA0107 Unimod:377#C (2R)-2-amino-3-[(2S)-2-((9Z)-9-octadecenoyloxy)-3-(hexadecanoyloxy)propyl]sulfanylpropanoic acid 2-amino-3-[(S)-2-((Z)-9-octadecenoyloxy)-3-(hexadecanoyloxy)propyl]thiopropanoic acid LIPID S-diacylglycerol cysteine S-(1-2'-oleoyl-3'-palmitoyl-glycerol)cysteine S-(2',3'-diacylglycerol)-L-cysteine S-diacylglycerol-L-cysteine SAcyl2GlyceroCys Diacylglycerol diacylglycerol A protein modification that effectively crosslinks an L-cysteine residue and an L-glutamine residue by a thioester bond with the formation of S-(L-isoglutamyl)-L-cysteine and the release of ammonia. -17.03 C 0 H -3 N -1 O 0 S 0 -17.026548 C 8 H 10 N 2 O 3 S 1 214.24 214.04121 C, Q natural uniprot.ptm:PTM-0156 (2S)-2-amino-5-[(2R)-2-amino-2-carboxyethyl]sulfanyl-5-oxopentanoic acid (S,R)-2-amino-4-[S-(2-amino-2-carboxyethyl)thiocarboxy]butanoic acid 2-amino-5-(2-amino-2-carboxyethyl)thio-5-oxopentanoic acid CROSSLNK Isoglutamyl cysteine thioester (Cys-Gln) S-(L-isoglutamyl)-L-cysteine S-gamma-glutamyl (crosslinked to cysteine) XLNK-SCys-5Glu(Gln) gamma-(S-cysteinyl)glutamic acid PSI-MOD MOD:00117 Cross-link 2; DeltaMass calculates the mass difference from glutamic acid rather than glutamine. S-(L-isoglutamyl)-L-cysteine A protein modification that effectively crosslinks an L-cysteine residue and an L-glutamine residue by a thioester bond with the formation of S-(L-isoglutamyl)-L-cysteine and the release of ammonia. ChEBI:22021 DeltaMass:0 PubMed:6838833 RESID:AA0108 (2S)-2-amino-5-[(2R)-2-amino-2-carboxyethyl]sulfanyl-5-oxopentanoic acid (S,R)-2-amino-4-[S-(2-amino-2-carboxyethyl)thiocarboxy]butanoic acid 2-amino-5-(2-amino-2-carboxyethyl)thio-5-oxopentanoic acid CROSSLNK Isoglutamyl cysteine thioester (Cys-Gln) S-(L-isoglutamyl)-L-cysteine S-gamma-glutamyl (crosslinked to cysteine) XLNK-SCys-5Glu(Gln) gamma-(S-cysteinyl)glutamic acid A protein modification that effectively cross-links an L-cysteine residue and an L-histidine residue by a thioether bond to form 2'-(S-L-cysteinyl)-L-histidine. -2.02 C 0 H -2 N 0 O 0 S 0 -2.01565 C 9 H 10 N 4 O 2 S 1 238.26 238.05244 C, H natural uniprot.ptm:PTM-0005 (2R)-2-amino-3-[(4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-2-yl)sulfanyl]propanoic acid (2S)-2-amino-3-[2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-1H-imidazol-4-yl]propanoic acid 2'-(L-cystein-S-yl)-L-histidine CROSSLNK 2'-(S-cysteinyl)-histidine (Cys-His) S-(2'-histidyl)cysteine S-(2-histidyl)- (crosslinked to cysteine) XLNK-SCys-2'His PSI-MOD MOD:00118 Cross-link 2. 2'-(S-L-cysteinyl)-L-histidine A protein modification that effectively cross-links an L-cysteine residue and an L-histidine residue by a thioether bond to form 2'-(S-L-cysteinyl)-L-histidine. DeltaMass:0 PubMed:6210696 RESID:AA0109 (2R)-2-amino-3-[(4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-2-yl)sulfanyl]propanoic acid (2S)-2-amino-3-[2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-1H-imidazol-4-yl]propanoic acid 2'-(L-cystein-S-yl)-L-histidine CROSSLNK 2'-(S-cysteinyl)-histidine (Cys-His) S-(2'-histidyl)cysteine S-(2-histidyl)- (crosslinked to cysteine) XLNK-SCys-2'His A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form L-lanthionine. -18.02 C 0 H -2 N 0 O -1 S 0 -18.010565 C 6 H 8 N 2 O 2 S 1 172.2 172.03065 C, S artifact (2R,2'R)-3,3'-sulfanediylbis(2-aminopropanoic acid) (R)-S-(2-amino-2-carboxyethyl)-L-cysteine (R,R)-2,6-diamino-4-thiaheptanedioic acid (R,R)-3,3'-thiobis-(2-aminopropanoic acid) (R,R)-bis(2-amino-2-carboxyethyl)sulfide 2-amino-3-(2-amino-2-carboxyethyl)sulfanylpropanoic acid 3,3'-thiobis-L-alanine L-lanthionine XLNK-SCys-(L)3Dha PSI-MOD MOD:00119 Cross-link 2. The natural occurrence of this modification is rare. For the more common modification see MOD:00120 meso-lanthionine [JSG]. L-lanthionine (Cys-Ser) A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form L-lanthionine. ChEBI:21347 DeltaMass:7 RESID:AA0110#CSX (2R,2'R)-3,3'-sulfanediylbis(2-aminopropanoic acid) (R)-S-(2-amino-2-carboxyethyl)-L-cysteine (R,R)-2,6-diamino-4-thiaheptanedioic acid (R,R)-3,3'-thiobis-(2-aminopropanoic acid) (R,R)-bis(2-amino-2-carboxyethyl)sulfide 2-amino-3-(2-amino-2-carboxyethyl)sulfanylpropanoic acid 3,3'-thiobis-L-alanine L-lanthionine XLNK-SCys-(L)3Dha A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form meso-lanthionine. -18.02 C 0 H -2 N 0 O -1 S 0 -18.010565 C 6 H 8 N 2 O 2 S 1 172.2 172.03065 C, S natural uniprot.ptm:PTM-0164 (2R,2'S)-3,3'-sulfanediylbis(2-aminopropanoic acid) (2R,2'S)-3,3'-thiobis-(2-aminopropanoic acid) (2R,6S)-2,6-diamino-4-thiaheptanedioic acid (2R,6S)-meso-lanthionine (2S)-2-amino-3-[[(2R)-2-amino-2-carboxyethyl]sulfanyl]propanoic acid (R)-S-(2-amino-2-carboxyethyl)-D-cysteine (R,S)-bis(2-amino-2-carboxyethyl)sulfide 3,3'-thiobis-meso-alanine CROSSLNK Lanthionine (Cys-Ser) CROSSLNK Lanthionine (Ser-Cys) XLNK-SCys-(D)3Dha cysteine-3-D-alanine thioether meso-lanthionine PSI-MOD (2S,6R)-meso-lanthionine MOD:00120 Cross-link 2. meso-lanthionine A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form meso-lanthionine. PubMed:15023056 PubMed:3769923 RESID:AA0111 (2R,2'S)-3,3'-sulfanediylbis(2-aminopropanoic acid) (2R,2'S)-3,3'-thiobis-(2-aminopropanoic acid) (2R,6S)-2,6-diamino-4-thiaheptanedioic acid (2R,6S)-meso-lanthionine (2S)-2-amino-3-[[(2R)-2-amino-2-carboxyethyl]sulfanyl]propanoic acid (R)-S-(2-amino-2-carboxyethyl)-D-cysteine (R,S)-bis(2-amino-2-carboxyethyl)sulfide 3,3'-thiobis-meso-alanine CROSSLNK Lanthionine (Cys-Ser) CROSSLNK Lanthionine (Ser-Cys) XLNK-SCys-(D)3Dha cysteine-3-D-alanine thioether meso-lanthionine (2S,6R)-meso-lanthionine A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form (2S,3S,2'R)-3-methyllanthionine. -18.02 C 0 H -2 N 0 O -1 S 0 -18.010565 C 7 H 10 N 2 O 2 S 1 186.23 186.0463 C, T natural uniprot.ptm:PTM-0067 (2S,3S)-2-amino-3-([(2R)-2-amino-2-carboxyethyl]sulfanyl)butanoic acid (2S,3S,2'R)-2-amino-3-[(2-amino-2-carboxyethyl)thio]butanoic acid (2S,3S,2'R)-3-methyllanthionine (2S,3S,6R)-2,6-diamino-3-methyl-4-thiaheptanedioic acid (2S,3S,6R)-3-methyllanthionine (2S-[2R*,3R*(S*)])-2-amino-3-[(2-amino-2-carboxyethyl)thio]butanoic acid 3-methyl-D,L-lanthionine CROSSLNK Beta-methyllanthionine (Cys-Thr) CROSSLNK Beta-methyllanthionine (Thr-Cys) XLNK-SCys-3Dhb cysteine-3-D-butyrine thioether PSI-MOD MOD:00121 Cross-link 2. (2S,3S,2'R)-3-methyllanthionine A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form (2S,3S,2'R)-3-methyllanthionine. PubMed:3769923 RESID:AA0112 (2S,3S)-2-amino-3-([(2R)-2-amino-2-carboxyethyl]sulfanyl)butanoic acid (2S,3S,2'R)-2-amino-3-[(2-amino-2-carboxyethyl)thio]butanoic acid (2S,3S,2'R)-3-methyllanthionine (2S,3S,6R)-2,6-diamino-3-methyl-4-thiaheptanedioic acid (2S,3S,6R)-3-methyllanthionine (2S-[2R*,3R*(S*)])-2-amino-3-[(2-amino-2-carboxyethyl)thio]butanoic acid 3-methyl-D,L-lanthionine CROSSLNK Beta-methyllanthionine (Cys-Thr) CROSSLNK Beta-methyllanthionine (Thr-Cys) XLNK-SCys-3Dhb cysteine-3-D-butyrine thioether A protein modification that effectively cross-links an L-cysteine residue and an L-tyrosine residue by a thioether bond to form 2-(S-L-cysteinyl)-L-tyrosine. -2.02 C 0 H -2 N 0 O 0 S 0 -2.01565 C 12 H 12 N 2 O 3 S 1 264.3 264.05685 C, Y natural uniprot.ptm:PTM-0019 (2S)-2-amino-3-(3-[(2R)2-amino-2-carboxyethylsulfanyl]-4-hydroxyphenyl)propanoic acid 2-amino-3-[3-(2-amino-2-carboxyethylthio)-4-hydroxyphenyl]propanoic acid 3'-(L-cystein-S-yl)-L-tyrosine 3'-(cystein-S-yl)tyrosine CROSSLNK 3'-(S-cysteinyl)-tyrosine (Cys-Tyr) CROSSLNK 3'-(S-cysteinyl)-tyrosine (Tyr-Cys) S-(3-Tyr) (Crosslinked to Cysteine) S-(tyros-3'-yl)cysteine XLNK-SCys-3'Tyr PSI-MOD MOD:00122 Cross-link 2. 3'-(S-L-cysteinyl)-L-tyrosine A protein modification that effectively cross-links an L-cysteine residue and an L-tyrosine residue by a thioether bond to form 2-(S-L-cysteinyl)-L-tyrosine. DeltaMass:0 PubMed:15917234 PubMed:2002850 RESID:AA0113 (2S)-2-amino-3-(3-[(2R)2-amino-2-carboxyethylsulfanyl]-4-hydroxyphenyl)propanoic acid 2-amino-3-[3-(2-amino-2-carboxyethylthio)-4-hydroxyphenyl]propanoic acid 3'-(L-cystein-S-yl)-L-tyrosine 3'-(cystein-S-yl)tyrosine CROSSLNK 3'-(S-cysteinyl)-tyrosine (Cys-Tyr) CROSSLNK 3'-(S-cysteinyl)-tyrosine (Tyr-Cys) S-(3-Tyr) (Crosslinked to Cysteine) S-(tyros-3'-yl)cysteine XLNK-SCys-3'Tyr A protein modification that effectively converts an L-lysine residue to N6-carboxy-L-lysine. 44.01 C 1 H 0 N 0 O 2 43.98983 C 7 H 12 N 2 O 3 172.18 172.0848 K natural Unimod:299 uniprot.ptm:PTM-0191 (2S)-2-amino-6-(carboxyamino)hexanoic acid 2-amino-6-carbamic hexanoic acid MOD_RES N6-carboxylysine N6-carboxy-L-lysine N6-carboxylysine N6CbxLys lysine NZ-carboxylic acid PSI-MOD Carboxy Carboxylation N6-carbamyllysine MOD:00123 N6-carboxy-L-lysine A protein modification that effectively converts an L-lysine residue to N6-carboxy-L-lysine. PubMed:11369851 PubMed:4436319 PubMed:637859 PubMed:7754395 RESID:AA0114 Unimod:299#K (2S)-2-amino-6-(carboxyamino)hexanoic acid 2-amino-6-carbamic hexanoic acid MOD_RES N6-carboxylysine N6-carboxy-L-lysine N6-carboxylysine N6CbxLys lysine NZ-carboxylic acid Carboxy Carboxylation N6-carbamyllysine A protein modification that effectively converts an L-lysine residue to N6-1-carboxyethyl-L-lysine. 72.06 C 3 H 4 N 0 O 2 72.021126 C 9 H 16 N 2 O 3 200.24 200.11609 K natural Unimod:378 uniprot.ptm:PTM-0189 (2S)-2-amino-6-([(1S)-1-carboxyethyl]amino)hexanoic acid MOD_RES N6-1-carboxyethyl lysine N6-(1-carboxyethyl)-L-lysine N6-(1-carboxyethyl)lysine N6CbzEtLys NZ-(1-carboxyethyl)lysine PSI-MOD Carboxyethyl carboxyethyl MOD:00124 N6-1-carboxyethyl-L-lysine A protein modification that effectively converts an L-lysine residue to N6-1-carboxyethyl-L-lysine. PubMed:3123486 PubMed:8253186 PubMed:8421682 RESID:AA0115 Unimod:378#K (2S)-2-amino-6-([(1S)-1-carboxyethyl]amino)hexanoic acid MOD_RES N6-1-carboxyethyl lysine N6-(1-carboxyethyl)-L-lysine N6-(1-carboxyethyl)lysine N6CbzEtLys NZ-(1-carboxyethyl)lysine Carboxyethyl carboxyethyl A protein modification that effectively converts an L-lysine residue to hypusine, N6-(4-amino-2-hydroxybutyl)-L-lysine. 87.12 C 4 H 9 N 1 O 1 87.06841 C 10 H 21 N 3 O 2 215.3 215.16338 K natural Unimod:379 uniprot.ptm:PTM-0150 (2S)-2-amino-6-([(2R)-4-amino-2-hydroxybutyl]amino)hexanoic acid (2S,9R)-2,11-diazanyl-9-hydroxy-7-azaundecanoic acid (2S,9R)-hypusine 2-azanyl-6-[(4-azanyl-2-hydroxybutyl)azanyl]hexanoic acid Hypu L-hypusine MOD_RES Hypusine N-(4-NH2-2-OH-butyl)- (of Lysine) N6-(4-amino-2-hydroxybutyl)-L-lysine PSI-MOD Hypusine hypusine MOD:00125 This modification occurs uniquely in translation initiation factor eIF-5A [JSG]. hypusine A protein modification that effectively converts an L-lysine residue to hypusine, N6-(4-amino-2-hydroxybutyl)-L-lysine. DeltaMass:0 PubMed:6806267 PubMed:8108861 RESID:AA0116 Unimod:379#K (2S)-2-amino-6-([(2R)-4-amino-2-hydroxybutyl]amino)hexanoic acid (2S,9R)-2,11-diazanyl-9-hydroxy-7-azaundecanoic acid (2S,9R)-hypusine 2-azanyl-6-[(4-azanyl-2-hydroxybutyl)azanyl]hexanoic acid Hypu L-hypusine MOD_RES Hypusine N-(4-NH2-2-OH-butyl)- (of Lysine) N6-(4-amino-2-hydroxybutyl)-L-lysine Hypusine hypusine A protein modification that effectively converts an L-lysine residue to N6-biotinyl-L-lysine. 226.29 C 10 H 14 N 2 O 2 S 1 226.0776 C 16 H 26 N 4 O 3 S 1 354.47 354.17258 K natural Unimod:3 uniprot.ptm:PTM-0382 (2S)-2-amino-6-(5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoylamino)hexanoic acid (3aS-(3aalpha,4beta,6aalpha))-N6-(5-(hexahydro-2-oxo-1H-thieno(3,4-d)imidazol-4-yl)-1-oxopentyl)-L-lysine MOD_RES N6-biotinyllysine N6-[5-((3aS,4S,6aR)-hexahydro-2-oxo-1H-thieno[3,4-d]imidazol-4-yl)-1-oxopentyl]-L-lysine N6-biotinyl-L-lysine N6-biotinyllysine N6BtnLys biocytin biotinyl lysyl epsilon-N-biotinyllysine PSI-MOD Biotin Biotinylation MOD:00126 From DeltaMass: Average Mass: 354 Formula:C 16 H 26 O 4 N 3 S 1 (formula incorrect, N and O reversed) Monoisotopic Mass Change:354.172 Average Mass Change:354.471 References:PE Sciex. N6-biotinyl-L-lysine A protein modification that effectively converts an L-lysine residue to N6-biotinyl-L-lysine. DeltaMass:305 PubMed:16109483 PubMed:3178228 PubMed:7948875 PubMed:8747466 RESID:AA0117 Unimod:3#K (2S)-2-amino-6-(5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoylamino)hexanoic acid (3aS-(3aalpha,4beta,6aalpha))-N6-(5-(hexahydro-2-oxo-1H-thieno(3,4-d)imidazol-4-yl)-1-oxopentyl)-L-lysine MOD_RES N6-biotinyllysine N6-[5-((3aS,4S,6aR)-hexahydro-2-oxo-1H-thieno[3,4-d]imidazol-4-yl)-1-oxopentyl]-L-lysine N6-biotinyl-L-lysine N6-biotinyllysine N6BtnLys biocytin biotinyl lysyl epsilon-N-biotinyllysine Biotin Biotinylation A protein modification that effectively converts an L-lysine residue to N6-lipoyl-L-lysine. 188.3 C 8 H 12 N 0 O 1 S 2 188.03296 C 14 H 24 N 2 O 2 S 2 316.48 316.12793 K natural Unimod:42 uniprot.ptm:PTM-0383 (2S)-2-amino-6-(5-[(3R)-1,2-dithiolan-3-yl]pentanamido)hexanoic acid (2S)-2-amino-6-[(5-[(3R)-1,2-dithiolan-3-yl]pentanoyl)amino]hexanoic acid (2S,6'R)-2-amino-6-(6,8-dithiooctanamido)hexanoic acid 2-amino-6-(5-[1,2-dithiolan-3-yl]-1-oxopentyl)aminohexanoic acid MOD_RES N6-lipoyllysine N-Lipoyl- (on Lysine) N6-6,8-dithiooctanoyllysine N6-lipoyl-L-lysine N6-lipoyllysine N6LipLys lipoylk PSI-MOD Lipoyl MOD:00127 N6-lipoyl-L-lysine A protein modification that effectively converts an L-lysine residue to N6-lipoyl-L-lysine. DeltaMass:0 OMSSA:67 PubMed:3421911 PubMed:3522581 PubMed:7719855 RESID:AA0118 Unimod:42#K (2S)-2-amino-6-(5-[(3R)-1,2-dithiolan-3-yl]pentanamido)hexanoic acid (2S)-2-amino-6-[(5-[(3R)-1,2-dithiolan-3-yl]pentanoyl)amino]hexanoic acid (2S,6'R)-2-amino-6-(6,8-dithiooctanamido)hexanoic acid 2-amino-6-(5-[1,2-dithiolan-3-yl]-1-oxopentyl)aminohexanoic acid MOD_RES N6-lipoyllysine N-Lipoyl- (on Lysine) N6-6,8-dithiooctanoyllysine N6-lipoyl-L-lysine N6-lipoyllysine N6LipLys lipoylk Lipoyl Lipoyl A protein modification that effectively converts an L-lysine residue to N6-pyridoxal phosphate-L-lysine. 229.13 C 8 H 8 N 1 O 5 P 1 229.014 C 14 H 20 N 3 O 6 P 1 357.3 357.10898 K natural Unimod:46 uniprot.ptm:PTM-0387 (2S)-2-amino-6-[([3-hydroxy-2-methyl-5-phosphonooxymethylpyridin-4-yl]methylidene)amino]hexanoic acid MOD_RES N6-(pyridoxal phosphate)lysine N6-pyridoxal phosphate-L-lysine N6PydoxLys Pyridoxal phosphate (Schiff Base formed to lysine) PSI-MOD Pyridoxal phosphate PyridoxalPhosphate MOD:00128 From DeltaMass: Average Mass: 231 N6-pyridoxal phosphate-L-lysine A protein modification that effectively converts an L-lysine residue to N6-pyridoxal phosphate-L-lysine. DeltaMass:0 PubMed:1544460 RESID:AA0119 Unimod:46#K (2S)-2-amino-6-[([3-hydroxy-2-methyl-5-phosphonooxymethylpyridin-4-yl]methylidene)amino]hexanoic acid MOD_RES N6-(pyridoxal phosphate)lysine N6-pyridoxal phosphate-L-lysine N6PydoxLys Pyridoxal phosphate (Schiff Base formed to lysine) Pyridoxal phosphate PyridoxalPhosphate A protein modification that effectively converts an L-lysine residue to N6-retinylidene-L-lysine, the adduct of retinal. 266.43 C 20 H 26 N 0 O 0 266.20346 C 26 H 38 N 2 O 1 394.6 394.2984 K natural Unimod:380 uniprot.ptm:PTM-0388 (2S)-2-amino-6-[(2E,4E,6E,8E)-3,7-dimethyl-9-(2,6,6-trimethylcyclohex-1-en-1-yl)-2,4,6,8-nonatetraenylidene]aminohexanoic acid MOD_RES N6-(retinylidene)lysine N6-retinal-L-lysine N6-retinyl-lysine N6-retinylidene-L-lysine N6RetalLys PSI-MOD Retinylidene retinal MOD:00129 N6-retinylidene-L-lysine A protein modification that effectively converts an L-lysine residue to N6-retinylidene-L-lysine, the adduct of retinal. PubMed:6794028 PubMed:6870827 RESID:AA0120 Unimod:380#K (2S)-2-amino-6-[(2E,4E,6E,8E)-3,7-dimethyl-9-(2,6,6-trimethylcyclohex-1-en-1-yl)-2,4,6,8-nonatetraenylidene]aminohexanoic acid MOD_RES N6-(retinylidene)lysine N6-retinal-L-lysine N6-retinyl-lysine N6-retinylidene-L-lysine N6RetalLys Retinylidene retinal A protein modification that effectively converts an L-lysine residue to L-allysine. -1.03 C 0 H -3 N -1 O 1 -1.031634 C 6 H 9 N 1 O 2 127.14 127.06333 K natural Unimod:352 uniprot.ptm:PTM-0059 (2S)-2-amino-6-oxohexanoic acid 2-amino-5-formylvaleric acid 2-amino-adipic acid semialdahyde 2-aminoadipate 6-semialdehyde 5-formyl-norvaline 6-oxonorleucine AASA Allysine (from Lysine) L-allysine Lysal MOD_RES Allysine Oxidation of lysine (to aminoadipic semialdehyde) alpha-amino-adipic acid delta-semialdahyde PSI-MOD Lys->Allysine Lysine oxidation to aminoadipic semialdehyde MOD:00130 From DeltaMass: Average Mass: -1 L-allysine A protein modification that effectively converts an L-lysine residue to L-allysine. ChEBI:17917 DeltaMass:0 PubMed:11120890 PubMed:11332453 PubMed:358196 PubMed:5337886 PubMed:5529814 RESID:AA0121 Unimod:352#K (2S)-2-amino-6-oxohexanoic acid 2-amino-5-formylvaleric acid 2-amino-adipic acid semialdahyde 2-aminoadipate 6-semialdehyde 5-formyl-norvaline 6-oxonorleucine AASA Allysine (from Lysine) L-allysine Lysal MOD_RES Allysine Oxidation of lysine (to aminoadipic semialdehyde) alpha-amino-adipic acid delta-semialdahyde Lys->Allysine Lysine oxidation to aminoadipic semialdehyde A protein modification that effectively converts an L-lysine residue to L-2-aminoadipic acid. 14.97 C 0 H -3 N -1 O 2 14.96328 C 6 H 9 N 1 O 3 143.14 143.05824 K natural Unimod:381 (2S)-2-aminohexanedioic acid 2-amino-1,4-butanedicarboxylic acid L-2-aminoadipic acid L-alpha-aminoadipic acid Lysoic Oxidation of lysine (to aminoadipic acid) PSI-MOD Lys->AminoadipicAcid alpha-amino adipic acid MOD:00131 From DeltaMass: References:Amici A, Levine, RL, Tsai, L, and Stadtman, ER: Conversion of amino acid residues in proteins and amino acid homopolymers to carbonyl derivatives by metal-catalyzed oxidation reactions. Journal of Biological Chemistry 264: 3341-3346 1989.Requena JR, Chao CC, Levine RL, and Stadtman ER: Glutamic and aminoadipic semialdehydes are the main carbonyl products of metal-catalyzed oxidation of proteins. Proceedings of the National Academy of Sciences USA 98: 69-74 2001. Notes:Expected reaction following oxidation of lysine to aminoadipic semialdehyde. Not proven experimentally but deduced by reference to the similar known reaction of oxidation of Arg to Glu via the semialdehyde. [This has been observed as a natural modification, see RESID:AA0122. JSG] L-2-aminoadipic acid A protein modification that effectively converts an L-lysine residue to L-2-aminoadipic acid. DeltaMass:353 PubMed:336041 PubMed:358196 PubMed:7419498 RESID:AA0122 Unimod:381#K (2S)-2-aminohexanedioic acid 2-amino-1,4-butanedicarboxylic acid L-2-aminoadipic acid L-alpha-aminoadipic acid Lysoic Oxidation of lysine (to aminoadipic acid) Lys->AminoadipicAcid alpha-amino adipic acid A protein modification that effectively crosslinks an L-serine residue and an L-lysine residue to release water and form 2-amino-6-(2-amino-2-carboxyethylamino)hexanoic acid. -18.02 C 0 H -2 N 0 O -1 -18.010565 C 9 H 15 N 3 O 2 197.24 197.11642 K, S natural uniprot.ptm:PTM-0172 (2R,9S)-lysinoalanine (2S)-2-amino-6-([(2R)-2-amino-2-carboxyethyl]amino)hexanoic acid CROSSLNK Lysinoalanine (Ser-Lys) L-lysinoalanine LAL Lysinoalanine (from Cysteine) N-epsilon-(2-amino-2-carboxyethyl)-L-lysine N6-(2-amino-2-carboxyethyl)-L-lysine XLNK-N6Lys-3Dha(Ser) alaninolysine PSI-MOD MOD:00132 Cross-link 2. This entry is for the crosslink of peptidyl serine and peptidyl lysine. For the modification of peptidyl lysine by a free serine see MOD:01838. From DeltaMass: Average Mass: -34. L-lysinoalanine (Lys-Ser) A protein modification that effectively crosslinks an L-serine residue and an L-lysine residue to release water and form 2-amino-6-(2-amino-2-carboxyethylamino)hexanoic acid. DeltaMass:0 PubMed:2544544 RESID:AA0123#KSX (2R,9S)-lysinoalanine (2S)-2-amino-6-([(2R)-2-amino-2-carboxyethyl]amino)hexanoic acid CROSSLNK Lysinoalanine (Ser-Lys) L-lysinoalanine LAL Lysinoalanine (from Cysteine) N-epsilon-(2-amino-2-carboxyethyl)-L-lysine N6-(2-amino-2-carboxyethyl)-L-lysine XLNK-N6Lys-3Dha(Ser) alaninolysine A protein modification that effectively crosslinks an L-glutamine residue and an L-lysine residue by an isopeptide bond with the formation of N6-(L-isoglutamyl)-L-lysine and the release of ammonia. -17.03 C 0 H -3 N -1 O 0 -17.026548 C 11 H 17 N 3 O 3 239.27 239.12698 K, Q natural uniprot.ptm:PTM-0158 (2S)-2-amino-6-([(4S)-4-amino-4-carboxybutanoyl]amino)hexanoic acid 2-azanyl-6-([4-azanyl-4-carboxybutanoyl]azanyl)hexanoic acid 5-glutamyl N6-lysine CROSSLNK Isoglutamyl lysine isopeptide (Lys-Gln) N alpha -(gamma-Glutamyl)-lysine N(epsilon)-(gamma-glutamyl)lysine N6-(L-isoglutamyl)-L-lysine XLNK-N6Lys-5Glu(Gln) PSI-MOD MOD:00133 Cross-link 2. N6-(L-isoglutamyl)-L-lysine (Gln) A protein modification that effectively crosslinks an L-glutamine residue and an L-lysine residue by an isopeptide bond with the formation of N6-(L-isoglutamyl)-L-lysine and the release of ammonia. ChEBI:21863 DeltaMass:0 PubMed:2461365 PubMed:5637041 PubMed:5656070 PubMed:8598899 RESID:AA0124#GLN (2S)-2-amino-6-([(4S)-4-amino-4-carboxybutanoyl]amino)hexanoic acid 2-azanyl-6-([4-azanyl-4-carboxybutanoyl]azanyl)hexanoic acid 5-glutamyl N6-lysine CROSSLNK Isoglutamyl lysine isopeptide (Lys-Gln) N alpha -(gamma-Glutamyl)-lysine N(epsilon)-(gamma-glutamyl)lysine N6-(L-isoglutamyl)-L-lysine XLNK-N6Lys-5Glu(Gln) A protein modification that effectively crosslinks an L-lysine residue and a glycine residue by an isopeptide bond to form N6-glycyl-L-lysine. -18.02 C 0 H -2 N 0 O -1 -18.010565 C 8 H 14 N 3 O 2 184.22 184.1086 G, K natural C-term uniprot.ptm:PTM-0134 (2S)-2-amino-6-[(aminoacetyl)amino]hexanoic acid CROSSLNK Glycyl lysine isopeptide (Gly-Lys) (interchain with K-...) CROSSLNK Glycyl lysine isopeptide (Lys-Gly) (interchain with G-...) N6-(glycyl)-L-lysine N6-glycyllysine XLNK-N6Lys-1Gly PSI-MOD MOD:00134 Cross-link 2; this is the common crosslink structure formed by ubiquitin, SUMO, and similar proteins. N6-glycyl-L-lysine A protein modification that effectively crosslinks an L-lysine residue and a glycine residue by an isopeptide bond to form N6-glycyl-L-lysine. ChEBI:21885 RESID:AA0125 (2S)-2-amino-6-[(aminoacetyl)amino]hexanoic acid CROSSLNK Glycyl lysine isopeptide (Gly-Lys) (interchain with K-...) CROSSLNK Glycyl lysine isopeptide (Lys-Gly) (interchain with G-...) N6-(glycyl)-L-lysine N6-glycyllysine XLNK-N6Lys-1Gly A protein modification that effectively crosslinks an L-asparagine residue and a glycine residue by an isopeptide bond with formation of N-(L-isoaspartyl)glycine and the release of ammonia. -17.03 C 0 H -3 N -1 O 0 -17.026548 C 6 H 7 N 2 O 3 155.13 155.04567 G, N natural N-term uniprot.ptm:PTM-0489 (2S)-2-amino-4-(carboxymethyl)amino-4-oxobutanoic acid 2-amino-N4-(carboxymethyl)-butanediamic acid CROSSLNK Isoaspartyl glycine isopeptide (Asn-Gly) CROSSLNK Isoaspartyl glycine isopeptide (Gly-Asn) N-(L-isoaspartyl)-glycine N-beta-aspartylglycine N4-(carboxymethyl)-asparagine XLNK-4Asp-NGly(Asn) isoaspartyl glycine PSI-MOD MOD:00135 Cross-link 2. N-(L-isoaspartyl)-glycine (Asn) A protein modification that effectively crosslinks an L-asparagine residue and a glycine residue by an isopeptide bond with formation of N-(L-isoaspartyl)glycine and the release of ammonia. ChEBI:21479 PubMed:1826288 RESID:AA0126 (2S)-2-amino-4-(carboxymethyl)amino-4-oxobutanoic acid 2-amino-N4-(carboxymethyl)-butanediamic acid CROSSLNK Isoaspartyl glycine isopeptide (Asn-Gly) CROSSLNK Isoaspartyl glycine isopeptide (Gly-Asn) N-(L-isoaspartyl)-glycine N-beta-aspartylglycine N4-(carboxymethyl)-asparagine XLNK-4Asp-NGly(Asn) isoaspartyl glycine A protein modification that effectively converts an L-cysteine residue to pyruvic acid. -33.09 C 0 H -3 N -1 O 1 S -1 -33.003704 C 3 H 3 O 2 71.06 71.013306 C natural N-term Unimod:382 uniprot.ptm:PTM-0265 2-oxopropanoic acid MOD_RES Pyruvic acid (Cys) Pyruv(Cys) pyruvic acid PSI-MOD MOD:00136 pyruvic acid (Cys) A protein modification that effectively converts an L-cysteine residue to pyruvic acid. PubMed:10085076 PubMed:3042771 PubMed:8464063 RESID:AA0127#CYS Unimod:382 2-oxopropanoic acid MOD_RES Pyruvic acid (Cys) Pyruv(Cys) pyruvic acid A protein modification that effectively converts an L-phenylalanine residue into L-3-phenyllactic acid. 0.98 C 0 H -1 N -1 O 1 0.984016 C 9 H 9 O 2 149.17 149.06026 F N-term Unimod:7 uniprot.ptm:PTM-0035 (2S)-2-hydroxy-3-phenylpropanoic acid L-3-phenyllactic acid MOD_RES 3-phenyllactic acid PSI-MOD Deamidated Deamidation MOD:00137 This modification is not the result of deamidation, instead the alpha amino group is replaced with an hydroxyl group. L-3-phenyllactic acid A protein modification that effectively converts an L-phenylalanine residue into L-3-phenyllactic acid. PubMed:1973541 RESID:AA0128 Unimod:7#F (2S)-2-hydroxy-3-phenylpropanoic acid L-3-phenyllactic acid MOD_RES 3-phenyllactic acid Deamidated Deamidation A protein modification that effectively converts an L-threonine residue into 2-oxobutanoic acid. -17.03 C 0 H -3 N -1 O 0 -17.026548 C 4 H 5 O 2 85.08 85.02895 T N-term Unimod:385 uniprot.ptm:PTM-0017 2-ketobutyric acid 2-oxobutanoic acid 2-oxobutyric acid MOD_RES 2-oxobutanoic acid PSI-MOD Ammonia-loss Loss of ammonia MOD:00138 2-oxobutanoic acid A protein modification that effectively converts an L-threonine residue into 2-oxobutanoic acid. ChEBI:149508 PubMed:15023056 PubMed:1680314 PubMed:2253617 PubMed:2764678 RESID:AA0129 Unimod:385#T 2-ketobutyric acid 2-oxobutanoic acid 2-oxobutanoic acid 2-oxobutyric acid MOD_RES 2-oxobutanoic acid Ammonia-loss Loss of ammonia A protein modification that effectively converts an L-tryptophan residue to N2-succinyl-L-tryptophan. 100.07 C 4 H 4 N 0 O 3 100.016045 C 15 H 15 N 2 O 4 287.29 287.10318 W natural N-term Unimod:64 uniprot.ptm:PTM-0181 (2S)-2-(3-carboxypropanoyl)amino-3-(1H-indol-3-yl)propanoic acid (2S)-2-amino-(6,7-dihydro-6,7-dioxo-1H-indole)-3-propanoic acid MOD_RES N2-succinyltryptophan N2-succinyl-L-tryptophan PSI-MOD Succinic anhydride labeling reagent light form (N-term) Succinyl MOD:00139 N2-succinyl-L-tryptophan A protein modification that effectively converts an L-tryptophan residue to N2-succinyl-L-tryptophan. PubMed:11857757 PubMed:12175151 PubMed:8471040 RESID:AA0130 Unimod:64#N-term (2S)-2-(3-carboxypropanoyl)amino-3-(1H-indol-3-yl)propanoic acid (2S)-2-amino-(6,7-dihydro-6,7-dioxo-1H-indole)-3-propanoic acid MOD_RES N2-succinyltryptophan N2-succinyl-L-tryptophan Succinic anhydride labeling reagent light form (N-term) Succinyl A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycocyanobilin. 586.69 C 33 H 38 N 4 O 6 S 0 586.2791 C 36 H 43 N 5 O 7 S 1 689.83 689.2883 C natural Unimod:387 (2R,3R)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-18-ethyl-1,2,3,19,21,22,24-heptahydro-2,7,13,17-tetramethyl-1,19-dioxo-(21H,22H,24H)-bilin-8,12-dipropanoic acid (2R,3R)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-18-ethyl-2,7,13,17-tetramethyl-1,2,3,19,21,22,24-heptahydrobilin-1,19(21H,22H,24H)-dione BINDING Phycocyanobilin chromophore (covalent; via 1 link) PCB S-Phycocyanobilin (on Cysteine) S-phycocyanobilin-L-cysteine phycobilin cysteine phycocyanobilin cysteine adduct PSI-MOD Phycocyanobilin phycocyanobilin MOD:00140 From DeltaMass: Average Mass: 587. S-phycocyanobilin-L-cysteine A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycocyanobilin. ChEBI:15617 DeltaMass:0 PubMed:16644722 PubMed:3208761 PubMed:3838747 PubMed:7918400 RESID:AA0131 Unimod:387#C (2R,3R)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-18-ethyl-1,2,3,19,21,22,24-heptahydro-2,7,13,17-tetramethyl-1,19-dioxo-(21H,22H,24H)-bilin-8,12-dipropanoic acid (2R,3R)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-18-ethyl-2,7,13,17-tetramethyl-1,2,3,19,21,22,24-heptahydrobilin-1,19(21H,22H,24H)-dione BINDING Phycocyanobilin chromophore (covalent; via 1 link) PCB S-Phycocyanobilin (on Cysteine) S-phycocyanobilin-L-cysteine phycobilin cysteine phycocyanobilin cysteine adduct Phycocyanobilin phycocyanobilin A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycoerythrobilin. 588.7 C 33 H 40 N 4 O 6 S 0 588.2948 C 36 H 45 N 5 O 7 S 1 691.84 691.30396 C natural Unimod:388 (2S,3R,16R)-18-ethenyl-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-2,7,13,17-tetramethyl-2,3,15,16-tetrahydrobilin-1,19(21H,22H,24H)-dione 18-ethenyl-3-[1-((2-amino-2-carboxy)ethylsulfanyl)ethyl]-2,3,15,16-tetrahydro-2,7,13,17-tetramethyl-1,19-dioxo-(21H,22H,24H)-bilin-8,12-dipropanoic acid BINDING Phycoerythrobilin chromophore (covalent; via 1 link) PEB S-phycoerythrobilin-L-cysteine phycoerythrobilin cysteine adduct PSI-MOD Phycoerythrobilin phycoerythrobilin MOD:00141 S-phycoerythrobilin-L-cysteine A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycoerythrobilin. ChEBI:15618 PubMed:14588022 PubMed:3208761 PubMed:3838747 PubMed:8876649 RESID:AA0132 Unimod:388#C (2S,3R,16R)-18-ethenyl-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-2,7,13,17-tetramethyl-2,3,15,16-tetrahydrobilin-1,19(21H,22H,24H)-dione 18-ethenyl-3-[1-((2-amino-2-carboxy)ethylsulfanyl)ethyl]-2,3,15,16-tetrahydro-2,7,13,17-tetramethyl-1,19-dioxo-(21H,22H,24H)-bilin-8,12-dipropanoic acid BINDING Phycoerythrobilin chromophore (covalent; via 1 link) PEB S-phycoerythrobilin-L-cysteine phycoerythrobilin cysteine adduct Phycoerythrobilin phycoerythrobilin A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phytochromobilin. 584.67 C 33 H 36 N 4 O 6 S 0 584.2635 C 36 H 41 N 5 O 7 S 1 687.81 687.27264 C natural Unimod:389 (2R,3R)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-18-ethyl-2,7,13,17-tetramethyl-1,2,3,19,21,22,24-heptahydrobilin-1,19(21H,22H,24H)-dione 18-ethenyl-3-[1-((2-amino-2-carboxy)ethylsulfanyl)ethyl]-1,2,3,19,22,24-hexahydro-2,7,13,17-tetramethyl-1,19-dioxo-21H-biline-8,12-dipropanoic acid BINDING Phytochromobilin chromophore (covalent; via 1 link) S-phytochromobilin-L-cysteine phytochrome chromophore phytochromobilin cysteine adduct PSI-MOD Phytochromobilin phytochromobilin MOD:00142 S-phytochromobilin-L-cysteine A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phytochromobilin. ChEBI:15619 PubMed:1634523 PubMed:16593380 PubMed:3208761 PubMed:7918400 RESID:AA0133 Unimod:389#C (2R,3R)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-18-ethyl-2,7,13,17-tetramethyl-1,2,3,19,21,22,24-heptahydrobilin-1,19(21H,22H,24H)-dione 18-ethenyl-3-[1-((2-amino-2-carboxy)ethylsulfanyl)ethyl]-1,2,3,19,22,24-hexahydro-2,7,13,17-tetramethyl-1,19-dioxo-21H-biline-8,12-dipropanoic acid BINDING Phytochromobilin chromophore (covalent; via 1 link) S-phytochromobilin-L-cysteine phytochrome chromophore phytochromobilin cysteine adduct Phytochromobilin phytochromobilin A protein modification that effectively results from forming an adduct between two cysteine residues and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. 616.5 C 34 Fe 1 H 32 N 4 O 4 S 0 616.1773 C 40 Fe 1 H 42 N 6 O 6 S 2 822.78 822.1957 C, C natural (7,12-bis[(1S)-1-([(2R)-2-amino-2-carboxyethyl]sulfanyl)ethyl]-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis[2-carboxyethyl]-N21,N22,N23,N24)-ferrate 2,4-bis[1-(S-cysteinyl)ethyl]protoporphyrin IX BINDING Heme (covalent) HemeCys2 biscysteinyl heme heme-bis-L-cysteine PSI-MOD MOD:00143 Cross-link 2. heme-bis-L-cysteine A protein modification that effectively results from forming an adduct between two cysteine residues and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. ChEBI:17627 PubMed:5545094 PubMed:8827449 RESID:AA0134 (7,12-bis[(1S)-1-([(2R)-2-amino-2-carboxyethyl]sulfanyl)ethyl]-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis[2-carboxyethyl]-N21,N22,N23,N24)-ferrate 2,4-bis[1-(S-cysteinyl)ethyl]protoporphyrin IX BINDING Heme (covalent) HemeCys2 biscysteinyl heme heme-bis-L-cysteine A protein modification that effectively results from forming an adduct between a cysteine residue and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. 616.5 C 34 Fe 1 H 32 N 4 O 4 S 0 616.1773 C 37 Fe 1 H 37 N 5 O 5 S 1 719.64 719.18646 C natural Unimod:390 (12-ethenyl-7-[(1S)-1-([(2R)-2-amino-2-carboxyethyl]sulfanyl)ethyl]-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis[2-carboxyethyl]-N21,N22,N23,N24)-ferrate 4-[1-(S-cysteinyl)ethyl]protoporphyrin IX BINDING Heme (covalent; via 1 link) HemeCys1 S-Heme (on Cysteine) cysteinyl heme heme-L-cysteine PSI-MOD Heme heme MOD:00144 From DeltaMass: Average Mass: 617. heme-L-cysteine A protein modification that effectively results from forming an adduct between a cysteine residue and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. ChEBI:17627 DeltaMass:0 PubMed:170910 PubMed:192772 PubMed:2536325 PubMed:9535866 RESID:AA0135 Unimod:390#C (12-ethenyl-7-[(1S)-1-([(2R)-2-amino-2-carboxyethyl]sulfanyl)ethyl]-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis[2-carboxyethyl]-N21,N22,N23,N24)-ferrate 4-[1-(S-cysteinyl)ethyl]protoporphyrin IX BINDING Heme (covalent; via 1 link) HemeCys1 S-Heme (on Cysteine) cysteinyl heme heme-L-cysteine Heme heme A protein modification that effectively converts four L-cysteine residues iron atom to tetrakis-L-cysteinyl iron. 51.81 C 0 Fe 1 H -4 N 0 O 0 S 0 51.904736 2- C 12 Fe 1 H 16 N 4 O 4 S 4 464.37 463.94147 C, C, C, C natural METAL Iron tetrakis(cysteinato-kappaS)-iron tetrakis-L-cysteinyl iron PSI-MOD MOD:00145 Cross-link 4. tetrakis-L-cysteinyl iron A protein modification that effectively converts four L-cysteine residues iron atom to tetrakis-L-cysteinyl iron. PubMed:1303768 PubMed:2244884 RESID:AA0136 METAL Iron tetrakis(cysteinato-kappaS)-iron tetrakis-L-cysteinyl iron A protein modification that effectively converts four L-cysteine residues and a two-iron two-sulfur cluster to tetrakis-L-cysteinyl diiron disulfide. 171.78 C 0 Fe 2 H -4 N 0 O 0 S 2 171.78381 2- C 12 Fe 2 H 16 N 4 O 4 S 6 584.34 583.82056 C, C, C, C natural METAL Iron-sulfur (2Fe-2S) METAL Iron-sulfur (2Fe-2S); shared with dimeric partner tetrakis-L-cysteinyl diiron disulfide tetrakiscysteinato-1kappa(2)S,2kappa(2)S-di-mu-sulfido-diiron PSI-MOD MOD:00146 Cross-link 4. tetrakis-L-cysteinyl diiron disulfide A protein modification that effectively converts four L-cysteine residues and a two-iron two-sulfur cluster to tetrakis-L-cysteinyl diiron disulfide. PubMed:2123937 PubMed:6801028 PubMed:7763242 PubMed:8688437 RESID:AA0137 METAL Iron-sulfur (2Fe-2S) METAL Iron-sulfur (2Fe-2S); shared with dimeric partner tetrakis-L-cysteinyl diiron disulfide tetrakiscysteinato-1kappa(2)S,2kappa(2)S-di-mu-sulfido-diiron A protein modification that effectively converts six L-cysteine residues and a three-iron three-sulfur cluster to hexakis-L-cysteinyl triiron trisulfide. 257.67 C 0 Fe 3 H -6 N 0 O 0 S 3 257.67572 3- C 18 Fe 3 H 24 N 6 O 6 S 9 876.5 875.73083 C, C, C, C, C, C hypothetical hexakis-L-cysteinyl triiron trisulfide tri-mu-sulfido-hexakiscysteinato-1kappa(2)S,2kappa(2)S,3kappa(2)S-triiron tri-mu-sulfidotris(biscysteinato-kappaS-iron) PSI-MOD MOD:00147 Cross-link 6. This is a deprecated entry in RESID. It probably does not occur naturally [JSG]. hexakis-L-cysteinyl triiron trisulfide A protein modification that effectively converts six L-cysteine residues and a three-iron three-sulfur cluster to hexakis-L-cysteinyl triiron trisulfide. PubMed:3379067 PubMed:3932661 PubMed:7354058 RESID:AA0138 hexakis-L-cysteinyl triiron trisulfide tri-mu-sulfido-hexakiscysteinato-1kappa(2)S,2kappa(2)S,3kappa(2)S-triiron tri-mu-sulfidotris(biscysteinato-kappaS-iron) A protein modification that effectively converts three L-cysteine residues and a three-iron four-sulfur cluster to tris-L-cysteinyl triiron tetrasulfide. 292.75 C 0 Fe 3 H -3 N 0 O 0 S 4 292.67126 3- C 9 Fe 3 H 12 N 3 O 3 S 7 602.17 601.6988 C, C, C natural METAL Iron-sulfur (3Fe-4S) mu3-sulfido tri-mu-sulfido tris-S-L-cysteinyl triiron mu3-sulfido-tri-mu-sulfido-triscysteinato-1kappaS,2kappaS,3kappaS-triiron tris-L-cysteinyl triiron tetrasulfide tris-L-cysteinyl triiron tetrasulfide C3 cluster tris-L-cysteinyl triiron tetrasulfide cubane form tris-L-cysteinyl triiron tetrasulfide cuboid cluster tris-L-cysteinyl triiron tetrasulfide trigonal cluster PSI-MOD MOD:00148 Cross-link 3. tris-L-cysteinyl triiron tetrasulfide A protein modification that effectively converts three L-cysteine residues and a three-iron four-sulfur cluster to tris-L-cysteinyl triiron tetrasulfide. PubMed:10555576 PubMed:2056535 PubMed:3422475 PubMed:6848518 PubMed:7819255 PubMed:9063899 RESID:AA0139 METAL Iron-sulfur (3Fe-4S) mu3-sulfido tri-mu-sulfido tris-S-L-cysteinyl triiron mu3-sulfido-tri-mu-sulfido-triscysteinato-1kappaS,2kappaS,3kappaS-triiron tris-L-cysteinyl triiron tetrasulfide tris-L-cysteinyl triiron tetrasulfide C3 cluster tris-L-cysteinyl triiron tetrasulfide cubane form tris-L-cysteinyl triiron tetrasulfide cuboid cluster tris-L-cysteinyl triiron tetrasulfide trigonal cluster A protein modification that effectively converts four L-cysteine residues and a four-iron four-sulfur cluster to tetrakis-L-cysteinyl tetrairon tetrasulfide. 347.59 C 0 Fe 4 H -4 N 0 O 0 S 4 347.59784 2- C 12 Fe 4 H 16 N 4 O 4 S 8 760.15 759.6346 C, C, C, C natural METAL Iron-sulfur (4Fe-4S) METAL Iron-sulfur (4Fe-4S); shared with dimeric partner tetra-mu3-sulfido-tetrakis(cysteinato)-1kappaS,2kappaS,3kappaS,4kappaS-tetrahedro-tetrairon tetra-mu3-sulfidotetrakis(S-cysteinyliron) tetrakis-L-cysteinyl tetrairon tetrasulfide PSI-MOD MOD:00149 Cross-link 4. tetrakis-L-cysteinyl tetrairon tetrasulfide A protein modification that effectively converts four L-cysteine residues and a four-iron four-sulfur cluster to tetrakis-L-cysteinyl tetrairon tetrasulfide. PubMed:3351918 PubMed:7803404 PubMed:7819196 PubMed:932007 RESID:AA0140 METAL Iron-sulfur (4Fe-4S) METAL Iron-sulfur (4Fe-4S); shared with dimeric partner tetra-mu3-sulfido-tetrakis(cysteinato)-1kappaS,2kappaS,3kappaS,4kappaS-tetrahedro-tetrairon tetra-mu3-sulfidotetrakis(S-cysteinyliron) tetrakis-L-cysteinyl tetrairon tetrasulfide A protein modification that effectively converts an L-cysteine residue, an L-histidine residue, homocitric acid and a one-molybdenum seven-iron nine-sulfur cluster to L-cysteinyl-L-histidino-homocitryl molybdenum heptairon nonasulfide. 991.53 C 7 Fe 7 H 6 Mo 1 N 1 O 7 S 9 993.213 C 16 Fe 7 H 18 Mo 1 N 5 O 9 S 10 1231.81 1233.2811 C, H natural L-cysteinyl-L-histidino-homocitryl molybdenum heptairon nonasulfide carbide cysteinato-8kappaS-histidino-1kappaN(tau)-[(2R)-4-carboxy-2-(carboxymethyl)-2-oxidobutanoate-1kappaO(1),1kappaO(2)]-mu6-carbido-2:3:4:5:6:7kappa(6)C-hexa-mu3-sulfido-1:2:3kappa(3)S;1:2:4kappa(3)S;1:3:4kappa(3)S;5:6:8kappa(3)S;5:7:8kappa(3)S;6:7:8kappa(3)S-tri-mu2-sulfido-2:5kappa(2)S;3:6kappa(2)S;4:7kappa(2)S molybdenum heptairon nitrogenase iron-molybdenum cofactor PSI-MOD MOD:00150 Cross-link 2; incidental to RESID:AA0300. L-cysteinyl-L-histidino-homocitryl molybdenum heptairon nonasulfide A protein modification that effectively converts an L-cysteine residue, an L-histidine residue, homocitric acid and a one-molybdenum seven-iron nine-sulfur cluster to L-cysteinyl-L-histidino-homocitryl molybdenum heptairon nonasulfide. PubMed:10525412 PubMed:12215645 PubMed:12733878 PubMed:1529354 PubMed:8027059 RESID:AA0141 L-cysteinyl-L-histidino-homocitryl molybdenum heptairon nonasulfide carbide cysteinato-8kappaS-histidino-1kappaN(tau)-[(2R)-4-carboxy-2-(carboxymethyl)-2-oxidobutanoate-1kappaO(1),1kappaO(2)]-mu6-carbido-2:3:4:5:6:7kappa(6)C-hexa-mu3-sulfido-1:2:3kappa(3)S;1:2:4kappa(3)S;1:3:4kappa(3)S;5:6:8kappa(3)S;5:7:8kappa(3)S;6:7:8kappa(3)S-tri-mu2-sulfido-2:5kappa(2)S;3:6kappa(2)S;4:7kappa(2)S molybdenum heptairon nitrogenase iron-molybdenum cofactor A protein modification that effectively converts an L-cysteine residue to L-cysteinyl molybdopterin. 520.27 C 10 H 11 Mo 1 N 5 O 8 P 1 S 2 521.8841 C 13 H 16 Mo 1 N 6 O 9 P 1 S 3 623.41 624.89325 C natural Unimod:391 (4R,5aR,11aR)-8-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-4,5a,6,9,10,11,11a-heptahydro-4-(phosphoric acid)methyl-2,2,10-trioxo-pteridino[6,7-5,6]pyrano[3,4-4,3][1,2,5]molybdadithiolene L-cysteinyl molybdopterin METAL Molybdenum-pterin MoPterCys cysteinyl Mo-molybdopterin cysteinyl Mo-pterin molybdoenzyme molybdenum cofactor PSI-MOD Molybdopterin molybdopterin MOD:00151 L-cysteinyl molybdopterin A protein modification that effectively converts an L-cysteine residue to L-cysteinyl molybdopterin. PubMed:14527393 PubMed:7878465 PubMed:9428520 RESID:AA0142 Unimod:391#C (4R,5aR,11aR)-8-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-4,5a,6,9,10,11,11a-heptahydro-4-(phosphoric acid)methyl-2,2,10-trioxo-pteridino[6,7-5,6]pyrano[3,4-4,3][1,2,5]molybdadithiolene L-cysteinyl molybdopterin METAL Molybdenum-pterin MoPterCys cysteinyl Mo-molybdopterin cysteinyl Mo-pterin molybdoenzyme molybdenum cofactor Molybdopterin molybdopterin A protein modification that effectively converts an L-cysteine residue to S'-(8alpha-FAD)-L-cystine. 783.54 C 27 H 31 N 9 O 15 P 2 S 0 783.1415 C 30 H 36 N 10 O 16 P 2 S 1 886.68 886.1507 C natural Unimod:50 uniprot.ptm:PTM-0272 (2R)-2-amino-3-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]sulfanylpropanoic acid 8alpha-(S-cysteinyl)FAD MOD_RES S-8alpha-FAD cysteine S-(8alpha-FAD)-L-cysteine S8aFADCys PSI-MOD FAD Flavin adenine dinucleotide MOD:00152 S-(8alpha-FAD)-L-cysteine A protein modification that effectively converts an L-cysteine residue to S'-(8alpha-FAD)-L-cystine. PubMed:10220347 RESID:AA0143 Unimod:50#C (2R)-2-amino-3-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]sulfanylpropanoic acid 8alpha-(S-cysteinyl)FAD MOD_RES S-8alpha-FAD cysteine S-(8alpha-FAD)-L-cysteine S8aFADCys FAD Flavin adenine dinucleotide A protein modification that effectively converts an L-histidine residue to 3'-(8alpha-FAD)-L-histidine. 783.54 C 27 H 31 N 9 O 15 P 2 783.1415 C 33 H 38 N 12 O 16 P 2 920.68 920.2004 H natural Unimod:50 uniprot.ptm:PTM-0258 (2S)-2-amino-3-(3-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]imidazol-4-yl)propanoic acid 3'-(8alpha-FAD)-L-histidine 8alpha-(N(delta)-histidyl)FAD 8alpha-(N3'-histidyl)FAD MOD_RES Pros-8alpha-FAD histidine N(pi)-(8alpha-FAD)-histidine Np8aFADHis pros-(8alpha-FAD)-histidine PSI-MOD 8alpha-N1-histidyl FAD FAD Flavin adenine dinucleotide MOD:00153 3'-(8alpha-FAD)-L-histidine A protein modification that effectively converts an L-histidine residue to 3'-(8alpha-FAD)-L-histidine. PubMed:241294 PubMed:8076 RESID:AA0144 Unimod:50#H (2S)-2-amino-3-(3-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]imidazol-4-yl)propanoic acid 3'-(8alpha-FAD)-L-histidine 8alpha-(N(delta)-histidyl)FAD 8alpha-(N3'-histidyl)FAD MOD_RES Pros-8alpha-FAD histidine N(pi)-(8alpha-FAD)-histidine Np8aFADHis pros-(8alpha-FAD)-histidine 8alpha-N1-histidyl FAD FAD Flavin adenine dinucleotide A protein modification that effectively converts an L-tyrosine residue to O4'-(8alpha-FAD)-L-tyrosine. 783.54 C 27 H 31 N 9 O 15 P 2 783.1415 C 36 H 40 N 10 O 17 P 2 946.72 946.20483 Y natural Unimod:50 uniprot.ptm:PTM-0231 (2S)-2-amino-3-(4-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]oxyphenyl)propanoic acid 8alpha-(O4'-tyrosyl)FAD MOD_RES O-8alpha-FAD tyrosine O-8 alpha-Flavin [FAD])- (of Tyrosine) O4'-(8alpha-FAD)-L-tyrosine O8aFADTyr PSI-MOD FAD Flavin adenine dinucleotide MOD:00154 From DeltaMass: Average Mass: 783 O4'-(8alpha-FAD)-L-tyrosine A protein modification that effectively converts an L-tyrosine residue to O4'-(8alpha-FAD)-L-tyrosine. DeltaMass:0 PubMed:7391034 RESID:AA0145 Unimod:50#Y (2S)-2-amino-3-(4-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]oxyphenyl)propanoic acid 8alpha-(O4'-tyrosyl)FAD MOD_RES O-8alpha-FAD tyrosine O-8 alpha-Flavin [FAD])- (of Tyrosine) O4'-(8alpha-FAD)-L-tyrosine O8aFADTyr FAD Flavin adenine dinucleotide A protein modification that effectively converts an L-tyrosine residue to L-3',4'-dihydroxyphenylalanine. 16.0 C 0 H 0 N 0 O 1 15.994915 C 9 H 9 N 1 O 3 179.18 179.05824 Y natural Unimod:35 uniprot.ptm:PTM-0023 (2S)-2-amino-3-(3,4-dihydroxyphenyl)propanoic acid 3,4-Dihydroxy-Phenylalanine (from Tyrosine) (DOPA) 3HyTyr L-3',4'-dihydroxyphenylalanine L-3'-hydroxytyrosine L-DOPA MOD_RES 3',4'-dihydroxyphenylalanine hydroxylationy levodopa mod194 PSI-MOD MOD:00155 incidental to RESID:AA0368 From DeltaMass: Average Mass: 16 L-3',4'-dihydroxyphenylalanine A protein modification that effectively converts an L-tyrosine residue to L-3',4'-dihydroxyphenylalanine. ChEBI:141815 DeltaMass:0 OMSSA:194 OMSSA:64 PubMed:1610822 PubMed:1903612 PubMed:3734192 RESID:AA0146 Unimod:35#Y (2S)-2-amino-3-(3,4-dihydroxyphenyl)propanoic acid 3,4-Dihydroxy-Phenylalanine (from Tyrosine) (DOPA) 3HyTyr L-3',4'-dihydroxyphenylalanine L-3'-hydroxytyrosine L-DOPA MOD_RES 3',4'-dihydroxyphenylalanine hydroxylationy levodopa mod194 A protein modification that effectively converts an L-tyrosine residue to an L-2',4',5'-topaquinone. 29.98 C 0 H -2 N 0 O 2 29.974178 C 9 H 7 N 1 O 4 193.16 193.0375 Y natural Unimod:392 uniprot.ptm:PTM-0009 (2S)-2-amino-3-(5-hydroxy-2,5-cyclohexadien-1,4-dion-2-yl)propanoic acid 2,4,5-trihydroxyphenylalanine quinone 5-(2-carboxy-2-aminoethyl)-2-hydroxy-1,4-benzoquinone L-2',4',5'-topaquinone L-2,4,5-TOPAquinone MOD_RES 2',4',5'-topaquinone TPQ TopaQ PSI-MOD Quinone quinone MOD:00156 L-2',4',5'-topaquinone A protein modification that effectively converts an L-tyrosine residue to an L-2',4',5'-topaquinone. ChEBI:21187 PubMed:10387067 PubMed:1457410 PubMed:1569055 PubMed:2111581 RESID:AA0147 Unimod:392#Y (2S)-2-amino-3-(5-hydroxy-2,5-cyclohexadien-1,4-dion-2-yl)propanoic acid 2,4,5-trihydroxyphenylalanine quinone 5-(2-carboxy-2-aminoethyl)-2-hydroxy-1,4-benzoquinone L-2',4',5'-topaquinone L-2,4,5-TOPAquinone MOD_RES 2',4',5'-topaquinone TPQ TopaQ Quinone quinone A protein modification that effectively converts an L-tryptophan residue to an L-tryptophan quinone. 29.98 C 0 H -2 N 0 O 2 29.974178 C 11 H 8 N 2 O 3 216.2 216.0535 W natural Unimod:392 uniprot.ptm:PTM-0299 (2S)-2-amino-3-(6,7-dioxo-1H-indol-3-yl)propanoic acid 2-amino-3-(6,7-dioxo-6,7-dihydro-1H-indol-3-yl)-propionic acid 3-[(2S)-2-amino-2-carboxyethyl]-6,7-indolinedione 6,7 Dione (from Tryptophan) L-tryptophyl quinone MOD_RES Tryptophylquinone N-(3-carboxy-1-oxopropyl)-L-tryptophan TrpQ PSI-MOD Quinone quinone MOD:00157 incidental to RESID:AA0149; incidental to RESID:AA0313; From DeltaMass: Average Mass: 30. L-tryptophyl quinone A protein modification that effectively converts an L-tryptophan residue to an L-tryptophan quinone. DeltaMass:0 PubMed:2028257 RESID:AA0148 Unimod:392#W (2S)-2-amino-3-(6,7-dioxo-1H-indol-3-yl)propanoic acid 2-amino-3-(6,7-dioxo-6,7-dihydro-1H-indol-3-yl)-propionic acid 3-[(2S)-2-amino-2-carboxyethyl]-6,7-indolinedione 6,7 Dione (from Tryptophan) L-tryptophyl quinone MOD_RES Tryptophylquinone N-(3-carboxy-1-oxopropyl)-L-tryptophan TrpQ Quinone quinone A protein modification that effectively cross-links two L-tryptophan residues by a carbon-carbon bond to form 4'-(L-tryptophan)-L-tryptophyl quinone. 27.97 C 0 H -4 N 0 O 2 27.958529 C 22 H 16 N 4 O 4 400.39 400.11716 W, W natural uniprot.ptm:PTM-0298 2,4-BisTrp-6,7-dione (from Tryptophan) 2-amino-3-[2-[2-amino-3-(2-carboxyethyl)-6,7-dioxo-1H-indol-4-yl]-1H-indol-3-yl]propanoic acid 3-[(2S)-2-amino-2-carboxyethyl]-4-(3-[(2S)-2-amino-2-carboxyethyl]-1H-indol-2-yl)-6,7-indolinedione 4'-tryptophan-tryptophylquinone 4-(2'-tryptophyl)tryptophan-6,7-dione 4-(L-tryptophan-2-yl)-L-tryptophyl quinone CROSSLNK Tryptophan tryptophylquinone (Trp-Trp) TTQ XLNK-4'Trp-TrpQ alpha,alpha'-diamino-6',7'-dihydro-6',7'-dioxo-(2,4'-bi-1H-indole)-3,3'-dipropanoic acid PSI-MOD MOD:00158 Cross-link 2; secondary to RESID:AA0148; From DeltaMass: Average Mass: 28. 4'-(L-tryptophan)-L-tryptophyl quinone A protein modification that effectively cross-links two L-tryptophan residues by a carbon-carbon bond to form 4'-(L-tryptophan)-L-tryptophyl quinone. ChEBI:20251 DeltaMass:0 PubMed:2028257 RESID:AA0149 2,4-BisTrp-6,7-dione (from Tryptophan) 2-amino-3-[2-[2-amino-3-(2-carboxyethyl)-6,7-dioxo-1H-indol-4-yl]-1H-indol-3-yl]propanoic acid 3-[(2S)-2-amino-2-carboxyethyl]-4-(3-[(2S)-2-amino-2-carboxyethyl]-1H-indol-2-yl)-6,7-indolinedione 4'-tryptophan-tryptophylquinone 4-(2'-tryptophyl)tryptophan-6,7-dione 4-(L-tryptophan-2-yl)-L-tryptophyl quinone CROSSLNK Tryptophan tryptophylquinone (Trp-Trp) TTQ XLNK-4'Trp-TrpQ alpha,alpha'-diamino-6',7'-dihydro-6',7'-dioxo-(2,4'-bi-1H-indole)-3,3'-dipropanoic acid A protein modification that effectively converts an L-serine residue to O-phosphopantetheine-L-serine. 340.33 C 11 H 21 N 2 O 6 P 1 S 1 340.0858 C 14 H 26 N 3 O 8 P 1 S 1 427.41 427.11783 S natural Unimod:49 uniprot.ptm:PTM-0391 (2R)-2-hydroxy-3,3-dimethyl-4-[(2S)-2-amino-2-carboxyethyl]phosphonato-N-(3-oxo-3-[(2-sulfanylethyl)amino]propyl)butanamide 4'-Phosphopantetheine MOD_RES O-(pantetheine 4'-phosphoryl)serine O-phosphopantetheine-L-serine OPpantSer PSI-MOD Phosphopantetheine MOD:00159 Unimod has DiffFormula C 11 H 20 N 2 O 6 P 1 S 1 From DeltaMass: Average Mass: 339 O-phosphopantetheine-L-serine A protein modification that effectively converts an L-serine residue to O-phosphopantetheine-L-serine. DeltaMass:0 PubMed:10320345 PubMed:10997907 PubMed:12057197 PubMed:12869567 PubMed:4568609 RESID:AA0150 Unimod:49#S (2R)-2-hydroxy-3,3-dimethyl-4-[(2S)-2-amino-2-carboxyethyl]phosphonato-N-(3-oxo-3-[(2-sulfanylethyl)amino]propyl)butanamide 4'-Phosphopantetheine MOD_RES O-(pantetheine 4'-phosphoryl)serine O-phosphopantetheine-L-serine OPpantSer Phosphopantetheine Phosphopantetheine A protein modification that effectively converts an L-asparagine residue to an N4-glycosyl-L-asparagine. N natural N4GlycoAsn PSI-MOD MOD:00160 N4-glycosyl-L-asparagine A protein modification that effectively converts an L-asparagine residue to an N4-glycosyl-L-asparagine. PubMed:111247 PubMed:1694179 PubMed:5490222 RESID:AA0151#var N4GlycoAsn A protein modification that effectively converts an L-cysteine residue to S-glucosylated L-cysteine. 162.14 C 6 H 10 N 0 O 5 S 0 162.05283 C 9 H 15 N 1 O 6 S 1 265.28 265.062 C natural Unimod:41 uniprot.ptm:PTM-0626 (2R)-2-amino-3-[(beta-D-glucopyranosyl)sulfanyl]propanoic acid CARBOHYD S-linked (Glc) cysteine S-(beta-D-glucopyranosyl)cysteine S-glucosyl-L-cysteine S-glycosyl-cysteine SGlcCys PSI-MOD Hex Hexose MOD:00161 S-glucosyl-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-glucosylated L-cysteine. PubMed:1145128 PubMed:15279557 PubMed:5286858 RESID:AA0152 Unimod:41#C (2R)-2-amino-3-[(beta-D-glucopyranosyl)sulfanyl]propanoic acid CARBOHYD S-linked (Glc) cysteine S-(beta-D-glucopyranosyl)cysteine S-glucosyl-L-cysteine S-glycosyl-cysteine SGlcCys Hex Hexose A protein modification that effectively converts an L-lysine residue to O5-glucosylgalactosyl-L-hydroxylysine. 340.28 C 12 H 20 N 0 O 11 340.10056 C 18 H 32 N 2 O 12 468.46 468.19553 K natural Unimod:393 (2S,5R)-2,6-diamino-5-[2-O-(alpha-D-glucopyranosyl)-beta-D-galactopyranosyloxy]hexanoic acid 5-(2-O-alpha-D-glucopyranosyl-beta-D-galactopyranosyl)oxy-L-lysine O5-glucosylgalactosyl-L-hydroxylysine OGlcGal5HyLys PSI-MOD Glucosylgalactosyl glucosylgalactosyl hydroxylysine MOD:00162 Secondary to RESID:AA0028. O5-glucosylgalactosyl-L-hydroxylysine A protein modification that effectively converts an L-lysine residue to O5-glucosylgalactosyl-L-hydroxylysine. PubMed:15149698 PubMed:4288358 PubMed:4319110 RESID:AA0153 Unimod:393 (2S,5R)-2,6-diamino-5-[2-O-(alpha-D-glucopyranosyl)-beta-D-galactopyranosyloxy]hexanoic acid 5-(2-O-alpha-D-glucopyranosyl-beta-D-galactopyranosyl)oxy-L-lysine O5-glucosylgalactosyl-L-hydroxylysine OGlcGal5HyLys Glucosylgalactosyl glucosylgalactosyl hydroxylysine A protein modification that effectively converts an L-serine residue to O-(N-acetylaminogalactosyl)-L-serine. 203.19 C 8 H 13 N 1 O 5 203.07938 C 11 H 18 N 2 O 7 290.27 290.1114 S natural uniprot.ptm:PTM-0564 (2S)-2-amino-3-(2-acetamido-2-deoxy-alpha-D-galactopyranosyloxy)propanoic acid CARBOHYD O-linked (GalNAc) serine O-(N-acetylamino)galactosyl-L-serine O3-(N-acetylgalactosaminyl)serine OGalNAcSer mucin type O-glycosylserine PSI-MOD HexNAc MOD:00163 O-(N-acetylamino)galactosyl-L-serine A protein modification that effectively converts an L-serine residue to O-(N-acetylaminogalactosyl)-L-serine. PubMed:115869 PubMed:16005634 PubMed:3086323 PubMed:8948436 PubMed:9092502 RESID:AA0154 (2S)-2-amino-3-(2-acetamido-2-deoxy-alpha-D-galactopyranosyloxy)propanoic acid CARBOHYD O-linked (GalNAc) serine O-(N-acetylamino)galactosyl-L-serine O3-(N-acetylgalactosaminyl)serine OGalNAcSer mucin type O-glycosylserine HexNAc A protein modification that effectively converts an L-asparagine residue to O-(N-acetylaminogalactosyl)-L-threonine. 203.19 C 8 H 13 N 1 O 5 203.07938 C 12 H 20 N 2 O 7 304.3 304.12704 T natural uniprot.ptm:PTM-0567 (2S,3R)-2-amino-3-(2-acetamido-2-deoxy-alpha-D-galactopyranosyloxy)butanoic acid CARBOHYD O-linked (GalNAc) threonine CARBOHYD O-linked (HexNAc) O-(N-acetylamino)galactosyl-L-threonine O3-(N-acetylgalactosaminyl)threonine OGalNAcThr mucin type O-glycosylthreonine PSI-MOD HexNAc MOD:00164 O-(N-acetylamino)galactosyl-L-threonine A protein modification that effectively converts an L-asparagine residue to O-(N-acetylaminogalactosyl)-L-threonine. PubMed:16005634 PubMed:1997327 PubMed:3086323 PubMed:8948436 PubMed:9092502 RESID:AA0155 (2S,3R)-2-amino-3-(2-acetamido-2-deoxy-alpha-D-galactopyranosyloxy)butanoic acid CARBOHYD O-linked (GalNAc) threonine CARBOHYD O-linked (HexNAc) O-(N-acetylamino)galactosyl-L-threonine O3-(N-acetylgalactosaminyl)threonine OGalNAcThr mucin type O-glycosylthreonine HexNAc A protein modification that effectively converts an L-tryptophan residue to 1'-mannosyl-L-tryptophan. 162.14 C 6 H 10 N 0 O 5 162.05283 C 17 H 20 N 2 O 6 348.36 348.13214 W natural uniprot.ptm:PTM-0535 (2S)-2-amino-3-(1-D-mannopyranosyloxy-1H-indol-3-yl)propanoic acid 1'-glycosyl-L-tryptophan 1'-mannosyl-L-tryptophan CARBOHYD N-linked (Man) tryptophan N-mannosyl-tryptophan N1'ManTrp N1-mannosyl-tryptophan PSI-MOD MOD:00165 1'-mannosyl-L-tryptophan A protein modification that effectively converts an L-tryptophan residue to 1'-mannosyl-L-tryptophan. PubMed:1482345 PubMed:16150691 RESID:AA0156 (2S)-2-amino-3-(1-D-mannopyranosyloxy-1H-indol-3-yl)propanoic acid 1'-glycosyl-L-tryptophan 1'-mannosyl-L-tryptophan CARBOHYD N-linked (Man) tryptophan N-mannosyl-tryptophan N1'ManTrp N1-mannosyl-tryptophan A protein modification that effectively converts an L-tyrosine residue to O4'-glucosyl-tyrosine. 162.14 C 6 H 10 N 0 O 5 162.05283 C 15 H 19 N 1 O 7 325.32 325.11615 Y natural Unimod:41 uniprot.ptm:PTM-0575 (2S)-2-amino-3-(4-alpha-D-glucopyranosyloxy)phenylpropanoic acid CARBOHYD O-linked (Glc) tyrosine O4'-glucosyl-L-tyrosine O4'-glycosyl-L-tyrosine O4GlcTyr PSI-MOD Hex Hexose MOD:00166 O4'-glucosyl-L-tyrosine A protein modification that effectively converts an L-tyrosine residue to O4'-glucosyl-tyrosine. PubMed:15279557 PubMed:3181138 RESID:AA0157 Unimod:41#Y (2S)-2-amino-3-(4-alpha-D-glucopyranosyloxy)phenylpropanoic acid CARBOHYD O-linked (Glc) tyrosine O4'-glucosyl-L-tyrosine O4'-glycosyl-L-tyrosine O4GlcTyr Hex Hexose A protein modification that effectively converts an L-asparagine residue to N-asparaginyl-glycosylphosphatidylinositolethanolamine. 123.05 C 2 H 6 N 1 O 3 P 1 123.00853 C 6 H 13 N 3 O 6 P 1 254.16 254.0542 N natural C-term uniprot.ptm:PTM-0137 GPIAsn LIPID GPI-anchor amidated asparagine N-asparaginyl-glycosylphosphatidylinositolethanolamine PSI-MOD MOD:00167 N-asparaginyl-glycosylphosphatidylinositolethanolamine A protein modification that effectively converts an L-asparagine residue to N-asparaginyl-glycosylphosphatidylinositolethanolamine. PubMed:1824714 PubMed:8276756 RESID:AA0158 GPIAsn LIPID GPI-anchor amidated asparagine N-asparaginyl-glycosylphosphatidylinositolethanolamine A protein modification that effectively converts an L-aspartic acid residue to N-(aspart-1-yl)-glycosylphosphatidylinositolethanolamine. 123.05 C 2 H 6 N 1 O 3 P 1 123.00853 C 6 H 12 N 2 O 7 P 1 255.14 255.03821 D natural C-term uniprot.ptm:PTM-0138 GPIAsp LIPID GPI-anchor amidated aspartate N-aspartyl-glycosylphosphatidylinositolethanolamine PSI-MOD MOD:00168 N-aspartyl-glycosylphosphatidylinositolethanolamine A protein modification that effectively converts an L-aspartic acid residue to N-(aspart-1-yl)-glycosylphosphatidylinositolethanolamine. PubMed:7120400 RESID:AA0159 GPIAsp LIPID GPI-anchor amidated aspartate N-aspartyl-glycosylphosphatidylinositolethanolamine A protein modification that effectively converts an L-cysteine residue to N-cysteinyl-glycosylphosphatidylinositolethanolamine. 123.05 C 2 H 6 N 1 O 3 P 1 S 0 123.00853 C 5 H 12 N 2 O 5 P 1 S 1 243.19 243.02045 C natural C-term uniprot.ptm:PTM-0140 GPICys LIPID GPI-anchor amidated cysteine N-cysteinyl-glycosylphosphatidylinositolethanolamine PSI-MOD MOD:00169 N-cysteinyl-glycosylphosphatidylinositolethanolamine A protein modification that effectively converts an L-cysteine residue to N-cysteinyl-glycosylphosphatidylinositolethanolamine. PubMed:2897081 RESID:AA0160 GPICys LIPID GPI-anchor amidated cysteine N-cysteinyl-glycosylphosphatidylinositolethanolamine A protein modification that effectively converts a glycine residue to N-glycyl-glycosylphosphatidylinositolethanolamine. 123.05 C 2 H 6 N 1 O 3 P 1 123.00853 C 4 H 10 N 2 O 5 P 1 197.11 197.03273 G natural C-term uniprot.ptm:PTM-0141 GPIGly LIPID GPI-anchor amidated glycine N-glycyl-glycosylphosphatidylinositolethanolamine PSI-MOD MOD:00170 N-glycyl-glycosylphosphatidylinositolethanolamine A protein modification that effectively converts a glycine residue to N-glycyl-glycosylphosphatidylinositolethanolamine. PubMed:2341397 RESID:AA0161 GPIGly LIPID GPI-anchor amidated glycine N-glycyl-glycosylphosphatidylinositolethanolamine A protein modification that effectively converts an L-serine residue to N-seryl-glycosylphosphatidylinositolethanolamine. 123.05 C 2 H 6 N 1 O 3 P 1 123.00853 C 5 H 12 N 2 O 6 P 1 227.13 227.0433 S natural C-term uniprot.ptm:PTM-0142 GPISer LIPID GPI-anchor amidated serine N-seryl-glycosylphosphatidylinositolethanolamine PSI-MOD MOD:00171 N-seryl-glycosylphosphatidylinositolethanolamine A protein modification that effectively converts an L-serine residue to N-seryl-glycosylphosphatidylinositolethanolamine. PubMed:2111324 PubMed:8448158 RESID:AA0162 GPISer LIPID GPI-anchor amidated serine N-seryl-glycosylphosphatidylinositolethanolamine A protein modification that effectively converts an L-alanine residue to N-alanyl-glycosylphosphatidylinositolethanolamine. 123.05 C 2 H 6 N 1 O 3 P 1 123.00853 C 5 H 12 N 2 O 5 P 1 211.13 211.04839 A natural C-term uniprot.ptm:PTM-0136 GPIAla LIPID GPI-anchor amidated alanine N-alanyl-glycosylphosphatidylinositolethanolamine PSI-MOD MOD:00172 N-alanyl-glycosylphosphatidylinositolethanolamine A protein modification that effectively converts an L-alanine residue to N-alanyl-glycosylphosphatidylinositolethanolamine. PubMed:7682556 PubMed:7744038 RESID:AA0163 GPIAla LIPID GPI-anchor amidated alanine N-alanyl-glycosylphosphatidylinositolethanolamine A protein modification that effectively converts an L-threonine residue to N-threonyl-glycosylphosphatidylinositolethanolamine. 123.05 C 2 H 6 N 1 O 3 P 1 123.00853 C 6 H 14 N 2 O 6 P 1 241.16 241.05894 T hypothetical C-term uniprot.ptm:PTM-0143 GPIThr LIPID GPI-anchor amidated threonine N-threonyl-glycosylphosphatidylinositolethanolamine PSI-MOD MOD:00173 N-threonyl-glycosylphosphatidylinositolethanolamine A protein modification that effectively converts an L-threonine residue to N-threonyl-glycosylphosphatidylinositolethanolamine. RESID:AA0164 GPIThr LIPID GPI-anchor amidated threonine N-threonyl-glycosylphosphatidylinositolethanolamine A protein modification that effectively converts a glycine residue to N-glycyl-glycosylsphingolipidinositolethanolamine. 123.05 C 2 H 6 N 1 O 3 P 1 123.00853 C 4 H 10 N 2 O 5 P 1 197.11 197.03273 G hypothetical C-term uniprot.ptm:PTM-0146 GSIGly LIPID GPI-like-anchor amidated glycine N-glycyl-glycosylsphingolipidinositolethanolamine PSI-MOD MOD:00174 N-glycyl-glycosylsphingolipidinositolethanolamine A protein modification that effectively converts a glycine residue to N-glycyl-glycosylsphingolipidinositolethanolamine. PubMed:12626404 PubMed:8404891 RESID:AA0165 GSIGly LIPID GPI-like-anchor amidated glycine N-glycyl-glycosylsphingolipidinositolethanolamine A protein modification that effectively converts an L-serine residue to N-seryl-glycosylsphingolipidinositolethanolamine. 123.05 C 2 H 6 N 1 O 3 P 1 123.00853 C 5 H 12 N 2 O 6 P 1 227.13 227.0433 S natural C-term uniprot.ptm:PTM-0147 GSISer LIPID GPI-like-anchor amidated serine N-seryl-glycosylsphingolipidinositolethanolamine PSI-MOD MOD:00175 N-seryl-glycosylsphingolipidinositolethanolamine A protein modification that effectively converts an L-serine residue to N-seryl-glycosylsphingolipidinositolethanolamine. PubMed:12626404 PubMed:2721485 PubMed:8269952 RESID:AA0166 GSISer LIPID GPI-like-anchor amidated serine N-seryl-glycosylsphingolipidinositolethanolamine A protein modification that effectively converts an L-serine residue to O-(phosphoribosyl dephospho-coenzyme A)-L-serine. 881.63 C 26 H 42 N 7 O 19 P 3 S 1 881.1469 C 29 H 47 N 8 O 21 P 3 S 1 968.71 968.17896 S natural Unimod:395 uniprot.ptm:PTM-0389 MOD_RES O-(phosphoribosyl dephospho-coenzyme A)serine O-(phosphoribosyl dephospho-coenzyme A)-L-serine O3-(phosphate-5-ribosyl-alpha-2-adenosine-5-diphosphate pantetheine)-L-serine O3-(phosphoribosyl dephospho-coenzyme A)-L-serine O3-2'-(5''-phosphoribosyl-3'-dephosphocoenzyme A)-L-serine OPRibdPCoASer PSI-MOD PhosphoribosyldephosphoCoA phosphoribosyl dephospho-coenzyme A MOD:00176 pRibodePcoA O-(phosphoribosyl dephospho-coenzyme A)-L-serine A protein modification that effectively converts an L-serine residue to O-(phosphoribosyl dephospho-coenzyme A)-L-serine. PubMed:10924139 PubMed:11052675 PubMed:179809 PubMed:180526 PubMed:368065 RESID:AA0167 Unimod:395#S MOD_RES O-(phosphoribosyl dephospho-coenzyme A)serine O-(phosphoribosyl dephospho-coenzyme A)-L-serine O3-(phosphate-5-ribosyl-alpha-2-adenosine-5-diphosphate pantetheine)-L-serine O3-(phosphoribosyl dephospho-coenzyme A)-L-serine O3-2'-(5''-phosphoribosyl-3'-dephosphocoenzyme A)-L-serine OPRibdPCoASer PhosphoribosyldephosphoCoA phosphoribosyl dephospho-coenzyme A A protein modification that effectively converts an L-argininine residue to omega-N-(ADP-ribosyl)-L-arginine. 541.3 C 15 H 21 N 5 O 13 P 2 541.0611 C 21 H 33 N 9 O 14 P 2 697.49 697.16223 R natural Unimod:213 uniprot.ptm:PTM-0053 (S)-2-amino-5-([imino([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]amino)methyl]amino)pentanoic acid ADPRibArg MOD_RES ADP-ribosylarginine N(omega)-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-arginine N(omega)-alpha-D-ribofuranosyl-L-arginine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate) N-(ADP-ribosyl)- (on Arginine) omega-N-(ADP-ribosyl)-L-arginine PSI-MOD ADP Ribose addition ADP-Ribosyl MOD:00177 From DeltaMass: Average Mass: 541. omega-N-(ADP-ribosyl)-L-arginine A protein modification that effectively converts an L-argininine residue to omega-N-(ADP-ribosyl)-L-arginine. DeltaMass:0 PubMed:15842200 PubMed:209022 PubMed:3090031 PubMed:3923473 PubMed:6582062 RESID:AA0168 Unimod:213#R (S)-2-amino-5-([imino([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]amino)methyl]amino)pentanoic acid ADPRibArg MOD_RES ADP-ribosylarginine N(omega)-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-arginine N(omega)-alpha-D-ribofuranosyl-L-arginine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate) N-(ADP-ribosyl)- (on Arginine) omega-N-(ADP-ribosyl)-L-arginine ADP Ribose addition ADP-Ribosyl A protein modification that effectively converts an L-cysteine residue to S-(ADP-ribosyl)-L-cysteine. 541.3 C 15 H 21 N 5 O 13 P 2 S 0 541.0611 C 18 H 26 N 6 O 14 P 2 S 1 644.44 644.0703 C natural Unimod:213 uniprot.ptm:PTM-0055 (R)-2-amino-3-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]sulfanyl)propanoic acid ADPRibCys MOD_RES ADP-ribosylcysteine S-(ADP-ribosyl)- (on Cysteine) S-(ADP-ribosyl)-L-cysteine S-L-cysteine alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate) S-alpha-D-ribofuranosyl-L-cysteine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate) PSI-MOD ADP Ribose addition ADP-Ribosyl MOD:00178 From DeltaMass: Average Mass: 541. S-(ADP-ribosyl)-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-(ADP-ribosyl)-L-cysteine. DeltaMass:0 PubMed:15842200 PubMed:3863818 RESID:AA0169 Unimod:213#C (R)-2-amino-3-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]sulfanyl)propanoic acid ADPRibCys MOD_RES ADP-ribosylcysteine S-(ADP-ribosyl)- (on Cysteine) S-(ADP-ribosyl)-L-cysteine S-L-cysteine alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate) S-alpha-D-ribofuranosyl-L-cysteine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate) ADP Ribose addition ADP-Ribosyl A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl 5-glycerylphosphorylethanolamine. 197.13 C 5 H 12 N 1 O 5 P 1 197.0453 C 10 H 19 N 2 O 8 P 1 326.24 326.0879 E natural Unimod:396 uniprot.ptm:PTM-0403 (S)-2-amino-5-[2-([([2,3-dihydroxypropyl]oxy)(hydroxy)phosphoryl]oxy)ethyl]amino-5-oxopentanoic acid 5-L-glutamyl glycerylphosphorylethanolamine 5GlyceroPEtAGlu L-glutamyl 5-glycerophosphoethanolamine L-glutamyl 5-glycerophosphorylethanolamine L-glutamyl 5-glycerylphosphorylethanolamine MOD_RES 5-glutamyl glycerylphosphorylethanolamine PSI-MOD GlycerylPE glycerylphosphorylethanolamine MOD:00179 glycerylPE L-glutamyl 5-glycerylphosphorylethanolamine A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl 5-glycerylphosphorylethanolamine. PubMed:2511205 PubMed:2569467 PubMed:9662537 RESID:AA0170 Unimod:396#E (S)-2-amino-5-[2-([([2,3-dihydroxypropyl]oxy)(hydroxy)phosphoryl]oxy)ethyl]amino-5-oxopentanoic acid 5-L-glutamyl glycerylphosphorylethanolamine 5GlyceroPEtAGlu L-glutamyl 5-glycerophosphoethanolamine L-glutamyl 5-glycerophosphorylethanolamine L-glutamyl 5-glycerylphosphorylethanolamine MOD_RES 5-glutamyl glycerylphosphorylethanolamine GlycerylPE glycerylphosphorylethanolamine A protein modification that effectively converts an L-cysteine residue to S-sulfo-L-cysteine. 80.06 C 0 H 0 N 0 O 3 S 1 79.95682 C 3 H 5 N 1 O 4 S 2 183.2 182.966 C natural Unimod:40 (2R)-2-amino-3-(sulfosulfanyl)propanoic acid 2-amino-3-(sulfothio)propanoic acid 3-(sulfosulfanyl)-L-alanine S-sulfo-L-cysteine S-sulfocysteine SSulfCys cysteine sulfate thioester cysteine-S-sulfonic acid PSI-MOD O-Sulfonation Sulfo MOD:00180 S-sulfo-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-sulfo-L-cysteine. PubMed:12876326 PubMed:14752058 PubMed:643076 RESID:AA0171 Unimod:40#C (2R)-2-amino-3-(sulfosulfanyl)propanoic acid 2-amino-3-(sulfothio)propanoic acid 3-(sulfosulfanyl)-L-alanine S-sulfo-L-cysteine S-sulfocysteine S-sulfocysteine SSulfCys cysteine sulfate thioester cysteine-S-sulfonic acid O-Sulfonation Sulfo A protein modification that effectively converts an L-tyrosine residue to O4'-sulfo-L-tyrosine. 80.06 C 0 H 0 N 0 O 3 S 1 79.95682 C 9 H 9 N 1 O 5 S 1 243.23 243.02014 Y natural Unimod:40 uniprot.ptm:PTM-0286 (S)-2-amino-3-(4-sulfooxyphenyl)propanoic acid 2-amino-3-(4-hydroxyphenyl)propanoic acid 4'-sulfate MOD_RES Sulfotyrosine O4'-sulfo-L-tyrosine O4-sulfotyrosine OSulfTyr Sulphation (of O of Tyrosine) Tyrosinyl Sulphate sulfationy tyrosine sulfate tyrosine-O-sulfonic acid tyrosine-O-sulphonic acid PSI-MOD O-Sulfonation Sulfo MOD:00181 From DeltaMass: Average Mass: 80 Average Mass Change:80 PubMed:9624161. O4'-sulfo-L-tyrosine A protein modification that effectively converts an L-tyrosine residue to O4'-sulfo-L-tyrosine. DeltaMass:88 OMSSA:114 PubMed:10226369 PubMed:14752058 PubMed:2303439 PubMed:3778455 PubMed:3801003 RESID:AA0172 Unimod:40#Y (S)-2-amino-3-(4-sulfooxyphenyl)propanoic acid 2-amino-3-(4-hydroxyphenyl)propanoic acid 4'-sulfate MOD_RES Sulfotyrosine O4'-sulfo-L-tyrosine O4-sulfotyrosine OSulfTyr Sulphation (of O of Tyrosine) Tyrosinyl Sulphate sulfationy tyrosine sulfate tyrosine-O-sulfonic acid tyrosine-O-sulphonic acid O-Sulfonation Sulfo A protein modification that effectively converts an L-histidine residue to L-bromohistidine. 78.9 Br 1 C 0 H -1 N 0 O 0 77.910515 Br 1 C 6 H 6 N 3 O 1 216.04 214.96942 H natural Unimod:340 uniprot.ptm:PTM-0089 Br1His L-bromohistidine MOD_RES Bromohistidine PSI-MOD Bromo bromination MOD:00182 L-bromohistidine A protein modification that effectively converts an L-histidine residue to L-bromohistidine. PubMed:2076468 PubMed:9033387 RESID:AA0173 Unimod:340#H Br1His L-bromohistidine MOD_RES Bromohistidine Bromo bromination A protein modification that effectively converts an L-phenylalanine residue to L-2'-bromophenylalanine. 78.9 Br 1 C 0 H -1 N 0 O 0 77.910515 Br 1 C 9 H 8 N 1 O 1 226.07 224.97893 F natural (S)-2-amino-3-(2-bromophenyl)propanoic acid 2'BrPhe L-2'-bromophenylalanine L-o-bromination of Phe with 79Br o-bromophenylalanine ortho-bromophenylalanine PSI-MOD Bromo bromination MOD:00183 From DeltaMass: Average Mass: 78 Average Mass Change:78 References:Yoshino,K et.al. Biochemistry Vol. 30 pg 6203-9 (1991) Identifidation of a novel amino acid, o-bromo-L-phenylananine, in egg-associated peptides that activate spermatozoa. L-2'-bromophenylalanine A protein modification that effectively converts an L-phenylalanine residue to L-2'-bromophenylalanine. DeltaMass:83 PubMed:2059627 PubMed:2076468 PubMed:9033387 RESID:AA0174 (S)-2-amino-3-(2-bromophenyl)propanoic acid 2'BrPhe L-2'-bromophenylalanine L-o-bromination of Phe with 79Br o-bromophenylalanine ortho-bromophenylalanine Bromo bromination A protein modification that effectively converts an L-phenylalanine residue to L-3'-bromophenylalanine. 78.9 Br 1 C 0 H -1 N 0 O 0 77.910515 Br 1 C 9 H 8 N 1 O 1 226.07 224.97893 F natural (S)-2-amino-3-(3-bromophenyl)propanoic acid 3'BrPhe L-3'-bromophenylalanine m-bromophenylalanine meta-bromophenylalanine PSI-MOD Bromo bromination MOD:00184 L-3'-bromophenylalanine A protein modification that effectively converts an L-phenylalanine residue to L-3'-bromophenylalanine. PubMed:2076468 PubMed:9033387 RESID:AA0175 (S)-2-amino-3-(3-bromophenyl)propanoic acid 3'BrPhe L-3'-bromophenylalanine m-bromophenylalanine meta-bromophenylalanine Bromo bromination A protein modification that effectively converts an L-phenylalanine residue to L-4'-bromophenylalanine. 78.9 Br 1 C 0 H -1 N 0 O 0 77.910515 Br 1 C 9 H 8 N 1 O 1 226.07 224.97893 F natural (2S)-2-amino-3-(4-bromophenyl)propanoic acid 4'BrPhe L-4'-bromophenylalanine p-bromophenylalanine para-bromophenylalanine PSI-MOD Bromo bromination MOD:00185 L-4'-bromophenylalanine A protein modification that effectively converts an L-phenylalanine residue to L-4'-bromophenylalanine. PubMed:2076468 PubMed:9033387 RESID:AA0176 (2S)-2-amino-3-(4-bromophenyl)propanoic acid 4'BrPhe L-4'-bromophenylalanine p-bromophenylalanine para-bromophenylalanine Bromo bromination A protein modification that effectively substitutes an L-tyrosine residue with 3,3',5-triiodo-L-thyronine. 469.79 C 6 H 1 I 3 N 0 O 1 469.71616 C 15 H 10 I 3 N 1 O 3 632.96 632.7795 Y natural Unimod:397 uniprot.ptm:PTM-0295 (S)-2-amino-3-[4-(4-hydroxy-3-iodophenoxy)-3,5-diiodophenyl]propanoic acid 3',3'',5'-triiodo-L-thyronine 3,3',5-triiodo-L-thyronine 3,5,3'-Triiodothyronine (from Tyrosine) 3,5,3'-triiodo-L-thyronine 4-(4-hydroxy-3-iodophenoxy)-3,5-diiodo-L-phenylalanine I3Thy MOD_RES Triiodothyronine O-(4-hydroxy-3-iodophenyl)-3,5-diiodo-L-tyrosine T3 liothyronine PSI-MOD Triiodothyronine triiodo MOD:00186 From DeltaMass: Average Mass: 470. 3,3',5-triiodo-L-thyronine A protein modification that effectively substitutes an L-tyrosine residue with 3,3',5-triiodo-L-thyronine. ChEBI:18258 DeltaMass:0 RESID:AA0177 Unimod:397 (S)-2-amino-3-[4-(4-hydroxy-3-iodophenoxy)-3,5-diiodophenyl]propanoic acid 3',3'',5'-triiodo-L-thyronine 3,3',5-triiodo-L-thyronine 3,5,3'-Triiodothyronine (from Tyrosine) 3,5,3'-triiodo-L-thyronine 4-(4-hydroxy-3-iodophenoxy)-3,5-diiodo-L-phenylalanine I3Thy MOD_RES Triiodothyronine O-(4-hydroxy-3-iodophenyl)-3,5-diiodo-L-tyrosine T3 liothyronine Triiodothyronine triiodo A protein modification that effectively substitutes an L-tyrosine residue with L-thyroxine. 595.68 C 6 H 0 I 4 N 0 O 1 595.6128 C 15 H 9 I 4 N 1 O 3 758.86 758.67615 Y natural Unimod:398 uniprot.ptm:PTM-0294 (S)-2-amino-3-[4-(4-hydroxy-3,5-diiodophenoxy)-3,5-diiodophenyl]propanoic acid 3',3'',5',5''-tetraiodo-L-thyronine 3,3',5,5'-tetraiodo-L-thyronine 3,5,3',5'-tetraiodo-L-thyronine 4-(4-hydroxy-3,5-diiodophenoxy)-3,5-diiodo-L-phenylalanine I4Thy L-thyroxine MOD_RES Thyroxine O-(4-hydroxy-3,5-diiodophenyl)-3,5-diiodo-L-tyrosine T4 PSI-MOD Thyroxine tetraiodo MOD:00187 L-thyroxine A protein modification that effectively substitutes an L-tyrosine residue with L-thyroxine. ChEBI:18332 PubMed:6704086 RESID:AA0178 Unimod:398 (S)-2-amino-3-[4-(4-hydroxy-3,5-diiodophenoxy)-3,5-diiodophenyl]propanoic acid 3',3'',5',5''-tetraiodo-L-thyronine 3,3',5,5'-tetraiodo-L-thyronine 3,5,3',5'-tetraiodo-L-thyronine 4-(4-hydroxy-3,5-diiodophenoxy)-3,5-diiodo-L-phenylalanine I4Thy L-thyroxine MOD_RES Thyroxine O-(4-hydroxy-3,5-diiodophenyl)-3,5-diiodo-L-tyrosine T4 Thyroxine tetraiodo A protein modification that effectively converts an L-tryptophan residue to 6'-bromo-L-tryptophan. 78.9 Br 1 C 0 H -1 N 0 O 0 77.910515 Br 1 C 11 H 9 N 2 O 1 265.11 263.98984 W natural Unimod:398 uniprot.ptm:PTM-0051 (2S)-2-amino-3-(6-bromo-1H-indol-3-yl)propanoic acid 6'-BrTrp 6'-bromo-L-tryptophan MOD_RES 6'-bromotryptophan PSI-MOD Bromo bromination MOD:00188 6'-bromo-L-tryptophan A protein modification that effectively converts an L-tryptophan residue to 6'-bromo-L-tryptophan. PubMed:12118011 PubMed:9030520 PubMed:9033387 PubMed:9434739 RESID:AA0179 Unimod:340#W (2S)-2-amino-3-(6-bromo-1H-indol-3-yl)propanoic acid 6'-BrTrp 6'-bromo-L-tryptophan MOD_RES 6'-bromotryptophan Bromo bromination A protein modification that effectively converts an L-serine residue to dehydroalanine. -18.02 C 0 H -2 N 0 O -1 -18.010565 C 3 H 3 N 1 O 1 69.06 69.02146 S natural Unimod:23 uniprot.ptm:PTM-0006 2,3-didehydroalanine 2-aminoacrylic acid 2-aminopropenoic acid 4-methylidene-imidazole-5-one (MIO) active site Dha Dha(Ser) MOD_RES 2,3-didehydroalanine (Ser) anhydroserine beta-elim-s dehydro dehydroalanine phospholosss PSI-MOD Dehydrated MOD:00189 dehydroalanine (Ser) A protein modification that effectively converts an L-serine residue to dehydroalanine. DeltaMass:0 OMSSA:140 OMSSA:164 OMSSA:96 PubMed:10220322 PubMed:1547888 PubMed:1815586 PubMed:2914619 PubMed:7947813 PubMed:8239649 RESID:AA0181#SER Unimod:23#S 2,3-didehydroalanine 2-aminoacrylic acid 2-aminopropenoic acid 4-methylidene-imidazole-5-one (MIO) active site Dha Dha(Ser) MOD_RES 2,3-didehydroalanine (Ser) anhydroserine beta-elim-s dehydro dehydroalanine phospholosss Dehydrated A protein modification that effectively converts an L-threonine residue to dehydrobutyrine. -18.02 C 0 H -2 N 0 O -1 -18.010565 C 4 H 5 N 1 O 1 83.09 83.03712 T natural Unimod:23 uniprot.ptm:PTM-0007 (2Z)-2-aminobut-2-enoic acid (Z)-2-amino-2-butenoic acid (Z)-2-aminobutenoic acid (Z)-dehydrobutyrine 2,3-didehydrobutyrine 3-methyldehydroalanine Dehydroamino butyric acid Dhb Dhb(Thr) MOD_RES 2,3-didehydrobutyrine alpha,beta-dehydroaminobutyric acid anhydrothreonine beta-elim-t dehydro methyl-dehydroalanine phospholosst PSI-MOD Dehydrated Dehydration MOD:00190 dehydrobutyrine (Thr) A protein modification that effectively converts an L-threonine residue to dehydrobutyrine. DeltaMass:0 OMSSA:141 OMSSA:164 OMSSA:97 PubMed:1547888 PubMed:3769923 RESID:AA0182 Unimod:23#T (2Z)-2-aminobut-2-enoic acid (Z)-2-amino-2-butenoic acid (Z)-2-aminobutenoic acid (Z)-dehydrobutyrine 2,3-didehydrobutyrine 3-methyldehydroalanine Dehydroamino butyric acid Dhb Dhb(Thr) MOD_RES 2,3-didehydrobutyrine alpha,beta-dehydroaminobutyric acid anhydrothreonine beta-elim-t dehydro methyl-dehydroalanine phospholosst Dehydrated Dehydrated Dehydration A protein modification that effectively converts L-tyrosine to (Z)-2,3-didehydrotyrosine. -2.02 C 0 H -2 N 0 O 0 -2.01565 C 9 H 7 N 1 O 2 161.16 161.04768 Y natural uniprot.ptm:PTM-0002 (2Z)-2-amino-3-(4-hydroxyphenyl)prop-2-enoic acid (Z)-2,3-didehydrogenated tyrosine (Z)-2,3-didehydrotyrosine MOD_RES (Z)-2,3-didehydrotyrosine Z-dHTyr amino-(para-hydroxybenzylidenyl)acetic acid cis-dehydrotyrosine green fluorescent protein chromophore para-hydroxybenzylidene-imidazolidinone chromophore red fluorescent protein chromophore PSI-MOD 2-amino-3-oxo-butanoic_acid Didehydro MOD:00191 incidental to RESID:AA0184; incidental to RESID:AA0187; incidental to RESID:AA0188; incidental to RESID:AA0189; incidental to RESID:AA0378; incidental to RESID:AA0379; incidental to RESID:AA0380; incidental to RESID:AA0381 (Z)-2,3-didehydrotyrosine A protein modification that effectively converts L-tyrosine to (Z)-2,3-didehydrotyrosine. PubMed:1347277 PubMed:9631087 RESID:AA0183 (2Z)-2-amino-3-(4-hydroxyphenyl)prop-2-enoic acid (Z)-2,3-didehydrogenated tyrosine (Z)-2,3-didehydrotyrosine MOD_RES (Z)-2,3-didehydrotyrosine Z-dHTyr amino-(para-hydroxybenzylidenyl)acetic acid cis-dehydrotyrosine green fluorescent protein chromophore para-hydroxybenzylidene-imidazolidinone chromophore red fluorescent protein chromophore 2-amino-3-oxo-butanoic_acid Didehydro A protein modification that effectively crosslinks an L-serine residue and a glycine residue to form L-serine 5-imidazolinone glycine. -18.02 C 0 H -2 N 0 O -1 -18.010565 C 5 H 6 N 2 O 2 126.11 126.04293 G, S natural uniprot.ptm:PTM-0049 (2-[(1R)-1-amino-2-hydroxyethyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid 2-[1-amino-2-hydroxyethyl]-1-carboxymethyl-1-imidazolin-5-one 4-methylidene-imidazole-5-one (MIO) active site CROSSLNK 5-imidazolinone (Ser-Gly) L-serine 5-imidazolinone glycine green fluorescent protein chromophore para-hydroxybenzylidene-imidazolidinone chromophore seryl-5-imidazolinone glycine PSI-MOD MOD:00192 Cross-link 2; carboxamidine; incidental to RESID:AA0183; incidental to RESID:AA0365. L-serine 5-imidazolinone glycine A protein modification that effectively crosslinks an L-serine residue and a glycine residue to form L-serine 5-imidazolinone glycine. ChEBI:21393 PubMed:1347277 PubMed:9631087 RESID:AA0184 (2-[(1R)-1-amino-2-hydroxyethyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid 2-[1-amino-2-hydroxyethyl]-1-carboxymethyl-1-imidazolin-5-one 4-methylidene-imidazole-5-one (MIO) active site CROSSLNK 5-imidazolinone (Ser-Gly) L-serine 5-imidazolinone glycine green fluorescent protein chromophore para-hydroxybenzylidene-imidazolidinone chromophore seryl-5-imidazolinone glycine A protein modification that effectively converts an L-cysteine residue to L-oxoalanine. -18.08 C 0 H -2 N 0 O 1 S -1 -17.992805 C 3 H 3 N 1 O 2 85.06 85.01638 C natural Unimod:402 uniprot.ptm:PTM-0034 (S)-2-amino-3-oxopropanoic acid 2-amino-3-oxopropionic acid L-3-oxoalanine L-amino-malonic acid semialdehyde L-aminomalonaldehydic acid MOD_RES 3-oxoalanine (Cys) Oxala(Cys) PSI-MOD C(alpha)-formylglycine L-serinesemialdehyde MOD:00193 L-3-oxoalanine (Cys) A protein modification that effectively converts an L-cysteine residue to L-oxoalanine. DeltaMass:350 PubMed:14563551 PubMed:7628016 PubMed:8681943 PubMed:9478923 RESID:AA0185#CYS Unimod:402#C (S)-2-amino-3-oxopropanoic acid 2-amino-3-oxopropionic acid L-3-oxoalanine L-amino-malonic acid semialdehyde L-aminomalonaldehydic acid MOD_RES 3-oxoalanine (Cys) Oxala(Cys) C(alpha)-formylglycine L-serinesemialdehyde A protein modification that effectively converts an L-serine residue to an amino-terminal lactic acid. -15.02 C 0 H -1 N -1 O 0 -15.010899 C 3 H 5 O 2 73.07 73.02895 S N-term Unimod:403 uniprot.ptm:PTM-0163 (2R)-2-hydroxypropanoic acid 2-hydroxypropionic acid Lac(Ser) MOD_RES Lactic acid alpha-hydroxypropionic acid lactic acid PSI-MOD Ser->LacticAcid lactic acid from N-term Ser MOD:00194 lactic acid A protein modification that effectively converts an L-serine residue to an amino-terminal lactic acid. PubMed:7607233 RESID:AA0186 Unimod:403#S (2R)-2-hydroxypropanoic acid 2-hydroxypropionic acid Lac(Ser) MOD_RES Lactic acid alpha-hydroxypropionic acid lactic acid Ser->LacticAcid lactic acid from N-term Ser A protein modification that effectively crosslinks an L-alanine residue and a glycine residue to form L-alanine 5-imidazolinone glycine. -18.02 C 0 H -2 N 0 O -1 -18.010565 C 5 H 6 N 2 O 1 110.12 110.04801 A, G natural uniprot.ptm:PTM-0045 (2-[(1S)-1-aminoethyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid 2-[1-aminoethyl]-1-carboxymethyl-1-imidazolin-5-one 4-methylidene-imidazole-5-one active site CROSSLNK 5-imidazolinone (Ala-Gly) L-alanine 5-imidazolinone glycine XLNK-1Ala-NGly(Imidazole) alanyl-5-imidazolinone glycine para-hydroxybenzylidene-imidazolidinone chromophore PSI-MOD MOD:00195 Cross-link 2; carboxamidine; incidental to RESID:AA0181; incidental to RESID:AA0183; incidental to RESID:AA0365. L-alanine 5-imidazolinone glycine A protein modification that effectively crosslinks an L-alanine residue and a glycine residue to form L-alanine 5-imidazolinone glycine. PubMed:10220322 RESID:AA0187 (2-[(1S)-1-aminoethyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid 2-[1-aminoethyl]-1-carboxymethyl-1-imidazolin-5-one 4-methylidene-imidazole-5-one active site CROSSLNK 5-imidazolinone (Ala-Gly) L-alanine 5-imidazolinone glycine XLNK-1Ala-NGly(Imidazole) alanyl-5-imidazolinone glycine para-hydroxybenzylidene-imidazolidinone chromophore A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue to form L-cysteine 5-imidazolinone glycine. -18.02 C 0 H -2 N 0 O -1 S 0 -18.010565 C 5 H 6 N 2 O 1 S 1 142.18 142.02008 C, G natural uniprot.ptm:PTM-0047 (2-[(1R)-1-amino-2-sulfanylethyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid 2-[1-amino-2-sulfanylethyl]-1-carboxymethyl-1-imidazolin-5-one 4-methylidene-imidazole-5-one (MIO) active site CROSSLNK 5-imidazolinone (Cys-Gly) L-cysteine 5-imidazolinone glycine XLNK-1Cys-NGly(Imidazole) cysteinyl-5-imidazolinone glycine para-hydroxybenzylidene-imidazolidinone chromophore PSI-MOD MOD:00196 Cross-link 2; carboxamidine; incidental to RESID:AA0181; incidental to RESID:AA0183; incidental to RESID:AA0365. L-cysteine 5-imidazolinone glycine A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue to form L-cysteine 5-imidazolinone glycine. PubMed:1537807 RESID:AA0188 (2-[(1R)-1-amino-2-sulfanylethyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid 2-[1-amino-2-sulfanylethyl]-1-carboxymethyl-1-imidazolin-5-one 4-methylidene-imidazole-5-one (MIO) active site CROSSLNK 5-imidazolinone (Cys-Gly) L-cysteine 5-imidazolinone glycine XLNK-1Cys-NGly(Imidazole) cysteinyl-5-imidazolinone glycine para-hydroxybenzylidene-imidazolidinone chromophore A protein modification that effectively crosslinks an L-glutamine residue and a glycine residue to form 2-imino-glutamine 5-imidazolinone glycine. -20.03 C 0 H -4 N 0 O -1 -20.026215 C 7 H 7 N 3 O 2 165.15 165.05383 G, Q natural uniprot.ptm:PTM-0013 2,N-didehydroglutaminyl-5-imidazolinone glycine 2-(3-carbamoyl-1-imino-propyl)-1-carboxymethyl-1-imidazolin-5-one 2-imino-glutamine 5-imidazolinone glycine CROSSLNK 2-iminomethyl-5-imidazolinone (Gln-Gly) [2-(3-carbamoyl-1-imino-propyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid [2-(4-amino-4-oxobutanimidoyl)-5-oxo-4,5-dihydro-1H-imidazol-1-yl]acetic acid fluorescent protein FP583 chromophore para-hydroxybenzylidene-imidazolidinone chromophore red fluorescent protein chromophore PSI-MOD MOD:00197 Cross-link 2; carboxamidine; incidental to RESID:AA0183; incidental to RESID:AA0365. 2-imino-glutamine 5-imidazolinone glycine A protein modification that effectively crosslinks an L-glutamine residue and a glycine residue to form 2-imino-glutamine 5-imidazolinone glycine. PubMed:11050230 PubMed:11209050 RESID:AA0189 2,N-didehydroglutaminyl-5-imidazolinone glycine 2-(3-carbamoyl-1-imino-propyl)-1-carboxymethyl-1-imidazolin-5-one 2-imino-glutamine 5-imidazolinone glycine CROSSLNK 2-iminomethyl-5-imidazolinone (Gln-Gly) [2-(3-carbamoyl-1-imino-propyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid [2-(4-amino-4-oxobutanimidoyl)-5-oxo-4,5-dihydro-1H-imidazol-1-yl]acetic acid fluorescent protein FP583 chromophore para-hydroxybenzylidene-imidazolidinone chromophore red fluorescent protein chromophore A protein modification that effectively converts an L-alanine residue to D-alanine. 0.0 C 0 H 0 N 0 O 0 0.0 C 3 H 5 N 1 O 1 71.08 71.03712 A natural uniprot.ptm:PTM-0112 (R)-2-aminopropanoic acid D-Ala(Ala) D-alanine MOD_RES D-alanine (Ala) PSI-MOD MOD:00198 D-alanine (Ala) A protein modification that effectively converts an L-alanine residue to D-alanine. PubMed:15023056 PubMed:7287302 PubMed:7961627 RESID:AA0191#ALA (R)-2-aminopropanoic acid D-Ala(Ala) D-alanine MOD_RES D-alanine (Ala) A protein modification that effectively converts an L-isoleucine residue to a D-allo-isoleucine. 0.0 C 0 H 0 N 0 O 0 0.0 C 6 H 11 N 1 O 1 113.16 113.08406 I natural uniprot.ptm:PTM-0114 (2R,3S)-2-amino-3-methylpentanoic acid 2-azanyl-3-methylpentanoic acid 3-methyl-norvaline D-Ile D-allo-isoleucine D-threo-isoleucine MOD_RES D-allo-isoleucine allo-D-isoleucine alpha-amino-beta-methylvaleric acid PSI-MOD MOD:00199 D-allo-isoleucine A protein modification that effectively converts an L-isoleucine residue to a D-allo-isoleucine. ChEBI:30007 PubMed:8223491 RESID:AA0192 (2R,3S)-2-amino-3-methylpentanoic acid 2-azanyl-3-methylpentanoic acid 3-methyl-norvaline D-Ile D-allo-isoleucine D-threo-isoleucine MOD_RES D-allo-isoleucine allo-D-isoleucine alpha-amino-beta-methylvaleric acid A protein modification that effectively converts an L-methionine residue to D-methionine. 0.0 C 0 H 0 N 0 O 0 S 0 0.0 C 5 H 9 N 1 O 1 S 1 131.19 131.04048 M natural uniprot.ptm:PTM-0120 (2R)-2-amino-4-(methylsulfanyl)butanoic acid 2-amino-4-(methylthio)butanoic acid 2-amino-4-(methylthio)butyric acid D-Met D-methionine MOD_RES D-methionine PSI-MOD MOD:00200 D-methionine A protein modification that effectively converts an L-methionine residue to D-methionine. ChEBI:29984 PubMed:16033333 PubMed:2542051 RESID:AA0193 (2R)-2-amino-4-(methylsulfanyl)butanoic acid 2-amino-4-(methylthio)butanoic acid 2-amino-4-(methylthio)butyric acid D-Met D-methionine MOD_RES D-methionine A protein modification that effectively converts an L-phenylalanine residue to D-phenylalanine. 0.0 C 0 H 0 N 0 O 0 0.0 C 9 H 9 N 1 O 1 147.18 147.06842 F natural uniprot.ptm:PTM-0121 (R)-2-amino-3-phenylpropanoic acid D-Phe D-phenylalanine MOD_RES D-phenylalanine PSI-MOD MOD:00201 D-phenylalanine A protein modification that effectively converts an L-phenylalanine residue to D-phenylalanine. ChEBI:29996 PubMed:1548227 PubMed:1644179 PubMed:2597281 RESID:AA0194 (R)-2-amino-3-phenylpropanoic acid D-Phe D-phenylalanine MOD_RES D-phenylalanine A protein modification that effectively converts an L-serine residue to D-serine. 0.0 C 0 H 0 N 0 O 0 0.0 C 3 H 5 N 1 O 2 87.08 87.03203 S natural uniprot.ptm:PTM-0308 (R)-2-amino-3-hydroxypropanoic acid D-Ser(Ser) D-serine MOD_RES D-serine (Ser) PSI-MOD MOD:00202 D-serine (Ser) A protein modification that effectively converts an L-serine residue to D-serine. PubMed:7973665 RESID:AA0195#SER (R)-2-amino-3-hydroxypropanoic acid D-Ser(Ser) D-serine MOD_RES D-serine (Ser) A protein modification that effectively converts an L-asparagine residue to D-asparagine. 0.0 C 0 H 0 N 0 O 0 0.0 C 4 H 6 N 2 O 2 114.1 114.04293 N natural uniprot.ptm:PTM-0115 (R)-2-amino-4-butanediamic acid D-Asn D-alpha-aminosuccinamic acid D-asparagine D-aspartic acid beta-amide MOD_RES D-asparagine PSI-MOD MOD:00203 D-asparagine A protein modification that effectively converts an L-asparagine residue to D-asparagine. ChEBI:29957 PubMed:1859408 RESID:AA0196 (R)-2-amino-4-butanediamic acid D-Asn D-alpha-aminosuccinamic acid D-asparagine D-aspartic acid beta-amide MOD_RES D-asparagine A protein modification that effectively converts an L-leucine residue to D-leucine. 0.0 C 0 H 0 N 0 O 0 0.0 C 6 H 11 N 1 O 1 113.16 113.08406 L natural uniprot.ptm:PTM-0119 (2R)-2-amino-4-methylpentanoic acid D-Leu D-leucine MOD_RES D-leucine alpha-aminoisocaproic acid PSI-MOD MOD:00204 D-leucine A protein modification that effectively converts an L-leucine residue to D-leucine. ChEBI:30005 PubMed:10461743 PubMed:12135762 PubMed:1358533 PubMed:1548227 RESID:AA0197 (2R)-2-amino-4-methylpentanoic acid D-Leu D-leucine MOD_RES D-leucine alpha-aminoisocaproic acid A protein modification that effectively converts an L-tryptophan residue to D-tryptophan. 0.0 C 0 H 0 N 0 O 0 0.0 C 11 H 10 N 2 O 1 186.21 186.07932 W natural uniprot.ptm:PTM-0123 (R)-2-amino-3-(1H-indol-3-yl)propanoic acid D-Trp D-tryptophan MOD_RES D-tryptophan alpha-amino-beta-(3-indolyl)propionoic acid PSI-MOD MOD:00205 D-tryptophan A protein modification that effectively converts an L-tryptophan residue to D-tryptophan. ChEBI:29955 PubMed:8910408 RESID:AA0198 (R)-2-amino-3-(1H-indol-3-yl)propanoic acid D-Trp D-tryptophan MOD_RES D-tryptophan alpha-amino-beta-(3-indolyl)propionoic acid A protein modification that effectively converts an L-glutamic acid residue to L-isoglutamyl-polyglycine. E natural uniprot.ptm:PTM-0394 L-isoglutamyl-polyglycine MOD_RES 5-glutamyl polyglycine gamma-glutamylpolyglycine PSI-MOD MOD:00206 L-isoglutamyl-polyglycine A protein modification that effectively converts an L-glutamic acid residue to L-isoglutamyl-polyglycine. ChEBI:21343 PubMed:10074368 PubMed:16368691 PubMed:7992051 RESID:AA0201 L-isoglutamyl-polyglycine MOD_RES 5-glutamyl polyglycine gamma-glutamylpolyglycine A protein modification that effectively converts an L-glutamic acid residue to isoglutamyl-polyglutamic acid, forming an isopeptide bond with a polyglutamic acid. E natural uniprot.ptm:PTM-0395 L-isoglutamyl-polyglutamic acid gamma-glutamylpolyglutamic acid PSI-MOD MOD:00207 L-isoglutamyl-polyglutamic acid A protein modification that effectively converts an L-glutamic acid residue to isoglutamyl-polyglutamic acid, forming an isopeptide bond with a polyglutamic acid. PubMed:10747868 PubMed:1680872 RESID:AA0202 L-isoglutamyl-polyglutamic acid gamma-glutamylpolyglutamic acid A protein modification that effectively crosslinks an L-tyrosine residue and 5'-phosphoadenosine through a phosphodiester bond to form O4'-(phospho-5'-adenosine)-L-tyrosine. 329.21 C 10 H 12 N 5 O 6 P 1 329.05252 C 19 H 21 N 6 O 8 P 1 492.38 492.11584 Y natural Unimod:405 uniprot.ptm:PTM-0332 (2S)-2-amino-3-[4-(5'-adenosine phosphonoxy)phenyl]propanoic acid 5'-adenylic-O-tyrosine MOD_RES O-AMP-tyrosine O-5'-Adenosylation ( of Tyrosine) O4'-(phospho-5'-adenosine)-L-tyrosine O4'-L-tyrosine 5'-adenosine phosphodiester OAMPTyr hydrogen 5'-adenylate tyrosine ester PSI-MOD AMP binding site Phosphoadenosine MOD:00208 From DeltaMass: Average Mass: 329. O4'-(phospho-5'-adenosine)-L-tyrosine A protein modification that effectively crosslinks an L-tyrosine residue and 5'-phosphoadenosine through a phosphodiester bond to form O4'-(phospho-5'-adenosine)-L-tyrosine. DeltaMass:0 PubMed:5543675 RESID:AA0203 Unimod:405#Y (2S)-2-amino-3-[4-(5'-adenosine phosphonoxy)phenyl]propanoic acid 5'-adenylic-O-tyrosine MOD_RES O-AMP-tyrosine O-5'-Adenosylation ( of Tyrosine) O4'-(phospho-5'-adenosine)-L-tyrosine O4'-L-tyrosine 5'-adenosine phosphodiester OAMPTyr hydrogen 5'-adenylate tyrosine ester AMP binding site Phosphoadenosine A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form S-(2-aminovinyl)-D-cysteine. -64.04 C -1 H -4 N 0 O -3 S 0 -64.016045 C 5 H 7 N 2 O 1 S 1 143.18 143.02791 C, S C-term uniprot.ptm:PTM-0268 (2S)-2-amino-3-([(Z)-2-aminoethenyl]sulfanyl)propanoic acid (S,Z)-S-(2-aminovinyl)cysteine CROSSLNK S-(2-aminovinyl)-D-cysteine (Ser-Cys) S-(2-aminovinyl)-D-cysteine XLNK-(D)SCys-VinAm PSI-MOD MOD:00209 Cross-link 2. S-(2-aminovinyl)-D-cysteine (Cys-Ser) A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form S-(2-aminovinyl)-D-cysteine. PubMed:3181159 PubMed:3769923 RESID:AA0204#SER (2S)-2-amino-3-([(Z)-2-aminoethenyl]sulfanyl)propanoic acid (S,Z)-S-(2-aminovinyl)cysteine CROSSLNK S-(2-aminovinyl)-D-cysteine (Ser-Cys) S-(2-aminovinyl)-D-cysteine XLNK-(D)SCys-VinAm A protein modification that effectively monooxygenates an L-cysteine residue to L-cysteine sulfenic acid. 16.0 C 0 H 0 N 0 O 1 S 0 15.994915 C 3 H 5 N 1 O 2 S 1 119.14 119.0041 C natural Unimod:35 uniprot.ptm:PTM-0107 (2R)-2-amino-3-(hydroxysulfanyl)propanoic acid (2R)-2-amino-3-(oxido-lambda(4)-sulfanyl)propanoic acid [tautomer] 2-amino-2-carboxyethanesulfenic acid 2-amino-3-sulfinylpropanoic acid [tautomer] 3-sulfenoalanine ACT_SITE Cysteine sulfenic acid (-SOH) intermediate CysOH L-cysteine sulfenic acid MOD_RES Cysteine sulfenic acid (-SOH) S-hydroxycysteine S-oxocysteine [tautomer] S-oxycysteine [tautomer] Sulfenic Acid (from Cysteine) cysteine S-oxide [tautomer] cysteine sulfoxide [tautomer] cysteine sulphenic acid mod193 PSI-MOD Oxidation MOD:00210 From DeltaMass: Average Mass: 16 Average Mass Change:16 Notes:Green et al. in J. B. C. 270, 18209-18211 (1995) quote Kim and Raines in Eur. J. Biochem. 224, 109-114 (1994). Kim and Raines using ESI-MS and sulfhydryl group titration found that bovine seminal ribonuclease contains a single oxidized sulfhydryl group, which cannot participate in a disulfide bond. This form of cysteine is called sulfenic acid (-SOH). L-cysteine sulfenic acid A protein modification that effectively monooxygenates an L-cysteine residue to L-cysteine sulfenic acid. DeltaMass:41 OMSSA:193 PubMed:10964927 PubMed:2501303 PubMed:8756456 PubMed:9214307 PubMed:9586994 PubMed:9587003 RESID:AA0205 Unimod:35#C (2R)-2-amino-3-(hydroxysulfanyl)propanoic acid (2R)-2-amino-3-(oxido-lambda(4)-sulfanyl)propanoic acid [tautomer] 2-amino-2-carboxyethanesulfenic acid 2-amino-3-sulfinylpropanoic acid [tautomer] 3-sulfenoalanine ACT_SITE Cysteine sulfenic acid (-SOH) intermediate CysOH L-cysteine sulfenic acid MOD_RES Cysteine sulfenic acid (-SOH) S-hydroxycysteine S-oxocysteine [tautomer] S-oxycysteine [tautomer] Sulfenic Acid (from Cysteine) cysteine S-oxide [tautomer] cysteine sulfoxide [tautomer] cysteine sulphenic acid mod193 Oxidation A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue by a thioester bond to form S-glycyl-L-cysteine. -18.02 C 0 H -2 N 0 O -1 S 0 -18.010565 C 5 H 7 N 2 O 2 S 1 159.18 159.02283 C, G C-term uniprot.ptm:PTM-0429 (2R)-2-amino-3-[(aminoacetyl)sulfanyl]propanoic acid 1-(cystein-S-yl)-glycinate ACT_SITE Glycyl thioester intermediate S-(2-amino-1-oxoethyl)cysteine S-(glycyl)-L-cysteine XLNK-SCys-1Gly glycine cysteine thioester PSI-MOD MOD:00211 Cross-link 2. For the modification of a C-terminal glycine by formation of a thioester bond with free L-cysteine see MOD:01777 [JSG]. S-(glycyl)-L-cysteine (Cys-Gly) A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue by a thioester bond to form S-glycyl-L-cysteine. ChEBI:22050 PubMed:3306404 RESID:AA0206 (2R)-2-amino-3-[(aminoacetyl)sulfanyl]propanoic acid 1-(cystein-S-yl)-glycinate ACT_SITE Glycyl thioester intermediate S-(2-amino-1-oxoethyl)cysteine S-(glycyl)-L-cysteine XLNK-SCys-1Gly glycine cysteine thioester A protein modification that effectively converts an L-cysteine residue to S-4-hydroxycinnamyl-L-cysteine. 146.14 C 9 H 6 N 0 O 2 S 0 146.03677 C 12 H 11 N 1 O 3 S 1 249.28 249.04596 C natural Unimod:407 uniprot.ptm:PTM-0414 (2R)-2-amino-3-([(2E)-3-(4-hydroxyphenyl)prop-2-enoyl]sulfanyl)propanoic acid MOD_RES S-(4-hydroxycinnamyl)cysteine S-4-hydroxycinnamyl-L-cysteine S-para-coumaryl-L-cysteine cinnamate cysteine thioester PSI-MOD Hydroxycinnamyl hydroxycinnamyl MOD:00212 S-4-hydroxycinnamyl-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-4-hydroxycinnamyl-L-cysteine. PubMed:7947803 PubMed:7981196 RESID:AA0207 Unimod:407 (2R)-2-amino-3-([(2E)-3-(4-hydroxyphenyl)prop-2-enoyl]sulfanyl)propanoic acid MOD_RES S-(4-hydroxycinnamyl)cysteine S-4-hydroxycinnamyl-L-cysteine S-para-coumaryl-L-cysteine cinnamate cysteine thioester Hydroxycinnamyl hydroxycinnamyl A protein modification that effectively cross-links an L-serine residue to the polymer chondroitin sulfate by a D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl tetrasaccharide. S natural chondroitin 4-sulfate (chondroitin sulfate A) chondroitin 6-sulfate (chondroitin sulfate C) chondroitin sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine poly[beta-1,4-D-glucopyranuronosyl-beta-1,3-(2-acetamido-2-deoxy-4-sulfate-D-galactosyl)]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-serine; poly[beta-1,4-D-glucopyranuronosyl-beta-1,3-(2-acetamido-2-deoxy-6-sulfate D-galactosyl)]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-serine PSI-MOD MOD:00213 chondroitin sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine A protein modification that effectively cross-links an L-serine residue to the polymer chondroitin sulfate by a D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl tetrasaccharide. PubMed:1794445 PubMed:1898736 PubMed:3472204 RESID:AA0208 chondroitin 4-sulfate (chondroitin sulfate A) chondroitin 6-sulfate (chondroitin sulfate C) chondroitin sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine poly[beta-1,4-D-glucopyranuronosyl-beta-1,3-(2-acetamido-2-deoxy-4-sulfate-D-galactosyl)]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-serine; poly[beta-1,4-D-glucopyranuronosyl-beta-1,3-(2-acetamido-2-deoxy-6-sulfate D-galactosyl)]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-serine A protein modification that effectively cross-links an L-serine residue to the polymer dermatan 4-sulfate by a D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl tetrasaccharide. S natural beta-heparin chondroitin sulfate B dermatan 4-sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine poly[beta-1,4-L-idopyranuronosyl-alpha-1,3-(2-acetamido-2-deoxy-4-sulfate D-galactosyl)]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-serine PSI-MOD MOD:00214 dermatan 4-sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine A protein modification that effectively cross-links an L-serine residue to the polymer dermatan 4-sulfate by a D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl tetrasaccharide. PubMed:2914936 PubMed:3472204 RESID:AA0209 beta-heparin chondroitin sulfate B dermatan 4-sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine poly[beta-1,4-L-idopyranuronosyl-alpha-1,3-(2-acetamido-2-deoxy-4-sulfate D-galactosyl)]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-serine A protein modification that effectively cross-links an L-serine residue to the polymer heparan sulfate by a D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl tetrasaccharide. S natural heparan sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine heparin heparitin sulfate poly[alpha-1,4-(2-sulfate D-glucopyranuronosyl)-beta-1,4-(2-sulfamino-2-deoxy-6-sulfate D-glucosyl)]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-serine PSI-MOD MOD:00215 heparan sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine A protein modification that effectively cross-links an L-serine residue to the polymer heparan sulfate by a D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl tetrasaccharide. PubMed:3472204 RESID:AA0210 heparan sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine heparin heparitin sulfate poly[alpha-1,4-(2-sulfate D-glucopyranuronosyl)-beta-1,4-(2-sulfamino-2-deoxy-6-sulfate D-glucosyl)]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-serine A protein modification that effectively converts an L-lysine residue to N6-formyl-L-lysine. 28.01 C 1 H 0 N 0 O 1 27.994915 C 7 H 12 N 2 O 2 156.19 156.08987 K natural Unimod:122 uniprot.ptm:PTM-0192 (2S)-2-amino-6-(formylamino)hexanoic acid MOD_RES N6-formyllysine N(zeta)-formyllysine N6-formyl-L-lysine N6-formylated L-lysine N6FoLys epsilon-formyllysine formylk PSI-MOD Formyl Formylation MOD:00216 N6-formyl-L-lysine A protein modification that effectively converts an L-lysine residue to N6-formyl-L-lysine. OMSSA:43 PubMed:15799070 RESID:AA0211 Unimod:122#K (2S)-2-amino-6-(formylamino)hexanoic acid MOD_RES N6-formyllysine N(zeta)-formyllysine N6-formyl-L-lysine N6-formylated L-lysine N6FoLys epsilon-formyllysine formylk Formyl Formylation A protein modification that effectively converts an L-proline residue to O4-arabinosyl-L-hydroxyproline. 148.11 C 5 H 8 N 0 O 5 148.03717 C 10 H 15 N 1 O 6 245.23 245.08994 P natural Unimod:408 uniprot.ptm:PTM-0545 (2S,4R)-4-(beta-L-arabinofuranosyloxy)pyrrolidine-2-carboxylic acid 4-(beta-L-arabinofuranosyloxy)proline 4-Glycosyloxy- (pentosyl,C5) (of Proline) O4-arabinosyl-L-hydroxyproline O4-glycosyl-hydroxyproline OAra4HyPro beta-arabinofuranosyl-4-hydroxyproline PSI-MOD Glycosyl glycosyl-L-hydroxyproline MOD:00217 secondary to RESID:AA0030; From DeltaMass: Average Mass: 147. O4-arabinosyl-L-hydroxyproline A protein modification that effectively converts an L-proline residue to O4-arabinosyl-L-hydroxyproline. DeltaMass:0 PubMed:666730 PubMed:7852316 RESID:AA0212 Unimod:408 (2S,4R)-4-(beta-L-arabinofuranosyloxy)pyrrolidine-2-carboxylic acid 4-(beta-L-arabinofuranosyloxy)proline 4-Glycosyloxy- (pentosyl,C5) (of Proline) O4-arabinosyl-L-hydroxyproline O4-glycosyl-hydroxyproline OAra4HyPro beta-arabinofuranosyl-4-hydroxyproline Glycosyl glycosyl-L-hydroxyproline A protein modification that effectively crosslinks an L-serine residue and the 5'-end of RNA through a phosphodiester to form O4'-(phospho-5'-RNA)-L-serine. S natural uniprot.ptm:PTM-0227 (S)-2-amino-3-(5'-ribonucleic acid phosphonoxy)propanoic acid MOD_RES O-(5'-phospho-RNA)-serine O-(phospho-5'-RNA)-L-serine O3-(phospho-5'-RNA)-L-serine O3-L-serine 5'-RNA phosphodiester PSI-MOD MOD:00218 O-(phospho-5'-RNA)-L-serine A protein modification that effectively crosslinks an L-serine residue and the 5'-end of RNA through a phosphodiester to form O4'-(phospho-5'-RNA)-L-serine. PubMed:1705009 RESID:AA0213 (S)-2-amino-3-(5'-ribonucleic acid phosphonoxy)propanoic acid MOD_RES O-(5'-phospho-RNA)-serine O-(phospho-5'-RNA)-L-serine O3-(phospho-5'-RNA)-L-serine O3-L-serine 5'-RNA phosphodiester A protein modification that effectively converts an L-arginine residue to L-citrulline. 0.98 C 0 H -1 N -1 O 1 0.984016 C 6 H 11 N 3 O 2 157.17 157.08513 R natural Unimod:7 uniprot.ptm:PTM-0092 (S)-2-amino-5-(carbamoylamino)pentanoic acid 2-amino-5-(aminocarbonyl)aminopentanoic acid Cit Citrulline L-citrulline MOD_RES Citrulline N5-(aminocarbonyl)ornithine N5-carbamoylornithine N5-carbamylornithine alpha-amino-delta-ureidovaleric acid citrullinationr delta-ureidonorvaline PSI-MOD Deamidated Deamidation MOD:00219 This modification is not the result of deamidation, instead the guanidino group is replaced with an ureido group. L-citrulline A protein modification that effectively converts an L-arginine residue to L-citrulline. DeltaMass:0 OMSSA:33 PubMed:2466844 RESID:AA0214 Unimod:7#R (S)-2-amino-5-(carbamoylamino)pentanoic acid 2-amino-5-(aminocarbonyl)aminopentanoic acid Cit Citrulline L-citrulline MOD_RES Citrulline N5-(aminocarbonyl)ornithine N5-carbamoylornithine N5-carbamylornithine alpha-amino-delta-ureidovaleric acid citrullinationr delta-ureidonorvaline Deamidated Deamidated Deamidation A protein modification that effectively converts an L-arginine residue to a 4-hydroxy-L-arginine. 16.0 C 0 H 0 N 0 O 1 15.994915 C 6 H 12 N 4 O 2 172.19 172.09602 R natural uniprot.ptm:PTM-0042 (2S,4Xi)-2-amino-5-[(diaminomethylidene)amino]-4-hydroxypentanoic acid 2-amino-5-(carbamimidamido)-4-hydroxypentanoic acid [tautomer] 2-amino-5-[(aminoiminomethyl)amino]-4-hydroxypentanoic acid [tautomer] 2-amino-5-guanidino-4-hydroxypentanoic acid 4-hydroxy-L-arginine 4-hydroxylated L-arginine 4HyArg C(gamma)-hydroxyarginine MOD_RES 4-hydroxyarginine gamma-hydroxyarginine PSI-MOD MOD:00220 4-hydroxy-L-arginine A protein modification that effectively converts an L-arginine residue to a 4-hydroxy-L-arginine. PubMed:10966817 PubMed:7650037 RESID:AA0215 (2S,4Xi)-2-amino-5-[(diaminomethylidene)amino]-4-hydroxypentanoic acid 2-amino-5-(carbamimidamido)-4-hydroxypentanoic acid [tautomer] 2-amino-5-[(aminoiminomethyl)amino]-4-hydroxypentanoic acid [tautomer] 2-amino-5-guanidino-4-hydroxypentanoic acid 4-hydroxy-L-arginine 4-hydroxylated L-arginine 4HyArg C(gamma)-hydroxyarginine MOD_RES 4-hydroxyarginine gamma-hydroxyarginine A protein modification that effectively crosslinks L-aspartic acid and L-cysteine residues via an isopeptide bond to form N-(L-isoaspartyl)-L-cysteine. -17.03 C 0 H -3 N -1 O 0 S 0 -17.026548 C 7 H 9 N 2 O 3 S 1 201.22 201.03339 C, N natural N-term uniprot.ptm:PTM-0151 (S)-2-amino-4-((R)-1-carboxy-2-sulfanylethyl)amino-4-oxobutanoic acid 2-(3-amino-3-carboxypropanoyl)amino-3-mercaptopropanoic acid 2-amino-N4-(1-carboxy-2-mercaptoethyl)butanediamic acid CROSSLNK Isoaspartyl cysteine isopeptide (Cys-Asn) N-(L-isoaspartyl)-L-cysteine N-beta-aspartylcysteine N-isoaspartyl cysteine PSI-MOD MOD:00221 Cross-link 2. N-(L-isoaspartyl)-L-cysteine A protein modification that effectively crosslinks L-aspartic acid and L-cysteine residues via an isopeptide bond to form N-(L-isoaspartyl)-L-cysteine. PubMed:8286361 RESID:AA0216 (S)-2-amino-4-((R)-1-carboxy-2-sulfanylethyl)amino-4-oxobutanoic acid 2-(3-amino-3-carboxypropanoyl)amino-3-mercaptopropanoic acid 2-amino-N4-(1-carboxy-2-mercaptoethyl)butanediamic acid CROSSLNK Isoaspartyl cysteine isopeptide (Cys-Asn) N-(L-isoaspartyl)-L-cysteine N-beta-aspartylcysteine N-isoaspartyl cysteine A protein modification that effectively converts an L-tryptophan residue to 2'-alpha-mannosyl-L-tryptophan. 162.14 C 6 H 10 N 0 O 5 162.05283 C 17 H 20 N 2 O 6 348.36 348.13214 W natural Unimod:41 uniprot.ptm:PTM-0505 (2S)-2-amino-3-(2-beta-D-mannopyranosyl-1H-indol-3-yl)propanoic acid 2'-mannosyl-L-tryptophan 2'-tryptophan C-mannoside C2'ManTrp CARBOHYD C-linked (Man) tryptophan PSI-MOD Hex Hexose MOD:00222 2'-alpha-mannosyl-L-tryptophan A protein modification that effectively converts an L-tryptophan residue to 2'-alpha-mannosyl-L-tryptophan. PubMed:15279557 PubMed:7547911 PubMed:7947762 RESID:AA0217 Unimod:41#W (2S)-2-amino-3-(2-beta-D-mannopyranosyl-1H-indol-3-yl)propanoic acid 2'-mannosyl-L-tryptophan 2'-tryptophan C-mannoside C2'ManTrp CARBOHYD C-linked (Man) tryptophan Hex Hexose A protein modification that effectively converts an L-lysine residue to N6-mureinyl-L-lysine. K natural uniprot.ptm:PTM-0195 MOD_RES N6-murein peptidoglycan lysine N6-[(2R,6S)-2-(N-(N-mureinyl-(R)-alanyl)-(S)-glutamyl)amino-6-amino-6-carboxy-1-oxohex-1-yl]lysine N6-mureinyl-L-lysine PSI-MOD MOD:00223 N6-mureinyl-L-lysine A protein modification that effectively converts an L-lysine residue to N6-mureinyl-L-lysine. PubMed:4261992 RESID:AA0218 MOD_RES N6-murein peptidoglycan lysine N6-[(2R,6S)-2-(N-(N-mureinyl-(R)-alanyl)-(S)-glutamyl)amino-6-amino-6-carboxy-1-oxohex-1-yl]lysine N6-mureinyl-L-lysine A protein modification that effectively converts an L-aspartic acid residue to 1-chondroitin sulfate-L-aspartic acid ester D C-term uniprot.ptm:PTM-0334 1-aspartic acid ester with 6-chondroitin 4-sulfate 1-chondroitin sulfate-L-aspartic acid ester MOD_RES Aspartate 1-(chondroitin 4-sulfate)-ester poly[beta-1,4-D-glucopyranuronosyl-beta-1,3-(2-acetamido-2-deoxy-4-sulfate D-galactosyl)]beta-1,4-D-glucopyranuronosyl-beta-1,3-(2-acetamido-2-deoxy-4-sulfate-6-(1-L-aspartyl)-D-galactose) protein-glycosaminoglycan-protein cross-link PSI-MOD MOD:00224 1-chondroitin sulfate-L-aspartic acid ester A protein modification that effectively converts an L-aspartic acid residue to 1-chondroitin sulfate-L-aspartic acid ester PubMed:1898736 RESID:AA0219 1-aspartic acid ester with 6-chondroitin 4-sulfate 1-chondroitin sulfate-L-aspartic acid ester MOD_RES Aspartate 1-(chondroitin 4-sulfate)-ester poly[beta-1,4-D-glucopyranuronosyl-beta-1,3-(2-acetamido-2-deoxy-4-sulfate D-galactosyl)]beta-1,4-D-glucopyranuronosyl-beta-1,3-(2-acetamido-2-deoxy-4-sulfate-6-(1-L-aspartyl)-D-galactose) protein-glycosaminoglycan-protein cross-link A protein modification that effectively converts an L-cysteine residue to S-(6-FMN)-L-cysteine. 454.33 C 17 H 19 N 4 O 9 P 1 S 0 454.08896 C 20 H 24 N 5 O 10 P 1 S 1 557.47 557.09814 C natural Unimod:409 uniprot.ptm:PTM-0271 (R)-2-amino-3-[6-riboflavin 5'-dihydrogen phosphate]sulfanylpropanoic acid 6-[S-cysteinyl]FMN 6-[S-cysteinyl]flavin mononucleotide MOD_RES S-6-FMN cysteine S-(6-FMN)-L-cysteine S6FMNCys PSI-MOD FMNH flavin mononucleotide MOD:00225 S-(6-FMN)-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-(6-FMN)-L-cysteine. PubMed:10869173 PubMed:1551870 PubMed:620783 RESID:AA0220 Unimod:409#C (R)-2-amino-3-[6-riboflavin 5'-dihydrogen phosphate]sulfanylpropanoic acid 6-[S-cysteinyl]FMN 6-[S-cysteinyl]flavin mononucleotide MOD_RES S-6-FMN cysteine S-(6-FMN)-L-cysteine S6FMNCys FMNH flavin mononucleotide A protein modification that effectively converts an L-histidine residue to 1'-(8alpha-FAD)-L-histidine. 783.54 C 27 H 31 N 9 O 15 P 2 783.1415 C 33 H 38 N 12 O 16 P 2 920.68 920.2004 H natural Unimod:50 uniprot.ptm:PTM-0288 (S)-2-amino-3-(1-[8alpha riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]imidazol-4-yl)propanoic acid 1'-(8alpha-FAD)-L-histidine 8alpha-(N(epsilon)-histidyl)FAD 8alpha-(N1'-histidyl)FAD MOD_RES Tele-8alpha-FAD histidine N theta and N pi-(8alpha-Flavin) (on Histidine) N(tau)-(8alpha-FAD)-histidine Nt8aFADHis tele-(8alpha-FAD)-histidine PSI-MOD 8alpha-N3-histidyl FAD FAD Flavin adenine dinucleotide MOD:00226 From DeltaMass: Average Mass: 784 1'-(8alpha-FAD)-L-histidine A protein modification that effectively converts an L-histidine residue to 1'-(8alpha-FAD)-L-histidine. DeltaMass:0 PubMed:10585424 PubMed:1396672 PubMed:4339951 PubMed:9261083 RESID:AA0221 Unimod:50#H (S)-2-amino-3-(1-[8alpha riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]imidazol-4-yl)propanoic acid 1'-(8alpha-FAD)-L-histidine 8alpha-(N(epsilon)-histidyl)FAD 8alpha-(N1'-histidyl)FAD MOD_RES Tele-8alpha-FAD histidine N theta and N pi-(8alpha-Flavin) (on Histidine) N(tau)-(8alpha-FAD)-histidine Nt8aFADHis tele-(8alpha-FAD)-histidine 8alpha-N3-histidyl FAD FAD Flavin adenine dinucleotide A protein modification that effectively converts an L-arginine residue to omega-N-phospho-L-arginine. 79.98 C 0 H 1 N 0 O 3 P 1 79.96633 C 6 H 13 N 4 O 4 P 1 236.17 236.06744 R natural Unimod:21 uniprot.ptm:PTM-0250 (2S)-2-amino-5-(N'-phosphonocarbamimidamido)pentanoic acid (2S)-2-amino-5-([amino(phosphonoamino)methylidene]amino)pentanoic acid MOD_RES Phosphoarginine N(gamma)-phosphoarginine N(omega)-phosphono-L-arginine N5-[imino(phosphonoamino)methyl]-L-ornithine PArg alpha-amino-delta-phosphonoguanidinovaleric acid omega-N-phospho-L-arginine phosphoarginine PSI-MOD Phospho Phosphorylation MOD:00227 omega-N-phospho-L-arginine A protein modification that effectively converts an L-arginine residue to omega-N-phospho-L-arginine. PubMed:8300603 RESID:AA0222 Unimod:21#R (2S)-2-amino-5-(N'-phosphonocarbamimidamido)pentanoic acid (2S)-2-amino-5-([amino(phosphonoamino)methylidene]amino)pentanoic acid MOD_RES Phosphoarginine N(gamma)-phosphoarginine N(omega)-phosphono-L-arginine N5-[imino(phosphonoamino)methyl]-L-ornithine PArg alpha-amino-delta-phosphonoguanidinovaleric acid omega-N-phospho-L-arginine phosphoarginine Phospho Phosphorylation A protein modification that effectively converts an L-cysteine residue to S-diphytanylglycerol diether-L-cysteine. 635.16 C 43 H 86 N 0 O 2 S 0 634.6628 C 46 H 91 N 1 O 3 S 1 738.3 737.672 C natural Unimod:410 uniprot.ptm:PTM-0273 (2R)-2-amino-3-([(2S)-2,3-bis(3,7,11,15-tetramethylhexadecanyloxy)propyl]sulfanyl)propanoic acid LIPID S-archaeol cysteine S-(diphytanylglyceryl)-L-cysteine S-[2',3'-bis(phytanyloxy)propyl]cysteine S-archaeol cysteine SPhyt2GlyceroCys PSI-MOD Archaeol S-diphytanylglycerol diether MOD:00228 incidental to RESID:AA0043. S-diphytanylglycerol diether-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-diphytanylglycerol diether-L-cysteine. PubMed:7797461 PubMed:8195126 RESID:AA0223 Unimod:410 (2R)-2-amino-3-([(2S)-2,3-bis(3,7,11,15-tetramethylhexadecanyloxy)propyl]sulfanyl)propanoic acid LIPID S-archaeol cysteine S-(diphytanylglyceryl)-L-cysteine S-[2',3'-bis(phytanyloxy)propyl]cysteine S-archaeol cysteine SPhyt2GlyceroCys Archaeol S-diphytanylglycerol diether A protein modification that effectively converts two L-cysteine residues to form alpha-1-microglobulin-Ig alpha complex chromophore. -2.02 C 0 H -2 N 0 O 0 S 0 -2.01565 C 6 H 8 N 2 O 2 S 2 204.26 204.00272 C, C natural BINDING Multimeric 3-hydroxykynurenine chromophore (covalent) alpha-1-microglobulin-Ig alpha complex chromophore PSI-MOD MOD:00229 Cross-link 2. alpha-1-microglobulin-Ig alpha complex chromophore A protein modification that effectively converts two L-cysteine residues to form alpha-1-microglobulin-Ig alpha complex chromophore. PubMed:11058759 PubMed:11877257 PubMed:7506257 PubMed:7535251 RESID:AA0224 BINDING Multimeric 3-hydroxykynurenine chromophore (covalent) alpha-1-microglobulin-Ig alpha complex chromophore A protein modification that effectively converts two L-cysteine residues, two L-histidine residues and a two-iron two-sulfur cluster to bis-L-cysteinyl bis-L-histidino diiron disulfide. 171.78 C 0 Fe 2 H -4 N 0 O 0 S 2 171.78381 2- C 18 Fe 2 H 20 N 8 O 4 S 4 652.34 651.92 C, C, H, H natural METAL Iron-sulfur (2Fe-2S) METAL Iron-sulfur (2Fe-2S); via pros nitrogen Rieske iron-sulfur cofactor bis-L-cysteinyl bis-L-histidino diiron disulfide di-mu-sulfido(bis-S-cysteinyliron)(bis-N3'-histidinoiron) PSI-MOD MOD:00230 Cross-link 4. bis-L-cysteinyl bis-L-histidino diiron disulfide A protein modification that effectively converts two L-cysteine residues, two L-histidine residues and a two-iron two-sulfur cluster to bis-L-cysteinyl bis-L-histidino diiron disulfide. PubMed:2765515 PubMed:9651245 RESID:AA0225 METAL Iron-sulfur (2Fe-2S) METAL Iron-sulfur (2Fe-2S); via pros nitrogen Rieske iron-sulfur cofactor bis-L-cysteinyl bis-L-histidino diiron disulfide di-mu-sulfido(bis-S-cysteinyliron)(bis-N3'-histidinoiron) A protein modification that effectively converts six L-cysteine residues and a six-iron six-sulfur cluster to hexakis-L-cysteinyl hexairon hexasulfide. 521.38 C 0 Fe 6 H -6 N 0 O 0 S 6 521.3956 1- C 18 Fe 6 H 24 N 6 O 6 S 12 1140.22 1139.4508 C, C, C, C, C, C hypothetical hexa-mu3-sulfido-hexakis(S-cysteinyliron) hexa-mu3-sulfido-hexakis(cysteinato-kappaS)-hexairon hexakis-L-cysteinyl hexairon hexasulfide prismane iron-sulfur cofactor PSI-MOD MOD:00231 Cross-link 6. This is a deprecated entry in RESID. It probably does not occur naturally [JSG]. hexakis-L-cysteinyl hexairon hexasulfide A protein modification that effectively converts six L-cysteine residues and a six-iron six-sulfur cluster to hexakis-L-cysteinyl hexairon hexasulfide. PubMed:1311311 PubMed:1318833 RESID:AA0226 hexa-mu3-sulfido-hexakis(S-cysteinyliron) hexa-mu3-sulfido-hexakis(cysteinato-kappaS)-hexairon hexakis-L-cysteinyl hexairon hexasulfide prismane iron-sulfur cofactor A protein modification that effectively crosslinks an L-lysine residue and 5'-phosphoadenosine through a phosphoramide ester bond to form N6-(phospho-5'-adenosine)-L-lysine. 329.21 C 10 H 12 N 5 O 6 P 1 329.05252 C 16 H 24 N 7 O 7 P 1 457.38 457.1475 K natural Unimod:405 (2S)-2-amino-6-(5'-adenosine phosphonamino)hexanoic acid 5'-adenylic-N6-L-lysine ACT_SITE N6-AMP-lysine intermediate AMP Lysyl L-lysine monoanhydride with 5'-adenylic acid N(zeta)-5'-adenylic-L-lysine N6-(phospho-5'-adenosine)-L-lysine N6-L-lysine 5'-adenosine phosphoramidester N6AMPLys epsilon-5'-adenylic-L-lysine PSI-MOD AMP binding site Phosphoadenosine MOD:00232 N6-(phospho-5'-adenosine)-L-lysine A protein modification that effectively crosslinks an L-lysine residue and 5'-phosphoadenosine through a phosphoramide ester bond to form N6-(phospho-5'-adenosine)-L-lysine. DeltaMass:316 PubMed:3882425 PubMed:4944632 RESID:AA0227 Unimod:405#K (2S)-2-amino-6-(5'-adenosine phosphonamino)hexanoic acid 5'-adenylic-N6-L-lysine ACT_SITE N6-AMP-lysine intermediate AMP Lysyl L-lysine monoanhydride with 5'-adenylic acid N(zeta)-5'-adenylic-L-lysine N6-(phospho-5'-adenosine)-L-lysine N6-L-lysine 5'-adenosine phosphoramidester N6AMPLys epsilon-5'-adenylic-L-lysine AMP binding site Phosphoadenosine A protein modification that effectively crosslinks an L-lysine residue and 5'-phosphoguanosine through a phosphoramide ester bond to form N6-(phospho-5'-guanosine)-L-lysine. 345.21 C 10 H 12 N 5 O 7 P 1 345.04742 C 16 H 24 N 7 O 8 P 1 473.38 473.1424 K natural Unimod:413 (2S)-2-amino-6-(5'-guanosine phosphonamino)hexanoic acid 5'-guanylic-N6-L-lysine 5'phos Guanosyl ACT_SITE N6-GMP-lysine intermediate L-lysine monoanhydride with 5'-guanylic acid N(zeta)-5'-guanylic-lysine N6-(5'-guanylyl)-lysine N6-(phospho-5'-guanosine)-L-lysine N6-L-lysine 5'-guanosine phosphoramidester N6GMPLys epsilon-5'-guanylic-L-lysine lysine guanosine-5'-monophosphate PSI-MOD Phosphoguanosine phospho-guanosine MOD:00233 From DeltaMass: Average Mass: 345 Formula:C10H12O5N7P1 Monoisotopic Mass Change:345.047 Average Mass Change:345.209 References:PE Sciex N6-(phospho-5'-guanosine)-L-lysine A protein modification that effectively crosslinks an L-lysine residue and 5'-phosphoguanosine through a phosphoramide ester bond to form N6-(phospho-5'-guanosine)-L-lysine. DeltaMass:304 PubMed:6092377 PubMed:6264433 RESID:AA0228 Unimod:413#K (2S)-2-amino-6-(5'-guanosine phosphonamino)hexanoic acid 5'-guanylic-N6-L-lysine 5'phos Guanosyl ACT_SITE N6-GMP-lysine intermediate L-lysine monoanhydride with 5'-guanylic acid N(zeta)-5'-guanylic-lysine N6-(5'-guanylyl)-lysine N6-(phospho-5'-guanosine)-L-lysine N6-L-lysine 5'-guanosine phosphoramidester N6GMPLys epsilon-5'-guanylic-L-lysine lysine guanosine-5'-monophosphate Phosphoguanosine phospho-guanosine A protein modification that effectively converts an L-cysteine residue to S-glutathionyl-L-cysteine. 305.3 C 10 H 15 N 3 O 6 S 1 305.06815 C 13 H 20 N 4 O 7 S 2 408.44 408.07733 C natural Unimod:55 uniprot.ptm:PTM-0311 (2S)-2-amino-3-((2S)-2-((4R)-4-amino-4-carboxyl-1-oxobutyl)amino-3-(carboxylmethyl)amino-3-oxo-propyl)dithio-propanoic acid Glutathionation L-cysteine glutathione disulfide L-gamma-glutamyl-L-cysteinyl-glycine (2-1')-disulfide with L-cysteine MOD_RES S-glutathionyl cysteine N-(N-gamma-glutamyl-cystinyl)-glycine SGltCys cysteinyl glutathione glutathionec PSI-MOD Glutathione glutathione disulfide MOD:00234 From DeltaMass: Average Mass: 305 Glutamyl-transpeptidase cleaves glutathione into cysteinylglycine (Cys-Gly) and a Glu residue. [PubMed: 28537416] L-cysteine glutathione disulfide A protein modification that effectively converts an L-cysteine residue to S-glutathionyl-L-cysteine. ChEBI:21264 DeltaMass:0 OMSSA:51 PubMed:3083866 PubMed:8344916 RESID:AA0229 Unimod:55 (2S)-2-amino-3-((2S)-2-((4R)-4-amino-4-carboxyl-1-oxobutyl)amino-3-(carboxylmethyl)amino-3-oxo-propyl)dithio-propanoic acid Glutathionation L-cysteine glutathione disulfide L-gamma-glutamyl-L-cysteinyl-glycine (2-1')-disulfide with L-cysteine MOD_RES S-glutathionyl cysteine N-(N-gamma-glutamyl-cystinyl)-glycine SGltCys cysteinyl glutathione glutathionec Glutathione glutathione disulfide A protein modification that effectively converts an L-cysteine residue to S-nitrosyl-L-cysteine. 29.0 C 0 H -1 N 1 O 1 S 0 28.990164 C 3 H 4 N 2 O 2 S 1 132.14 131.99934 C natural Unimod:275 uniprot.ptm:PTM-0280 (2R)-2-amino-3-nitrososulfanyl-propanoic acid L-cysteine nitrite ester MOD_RES S-nitrosocysteine S-nitrosocysteine S-nitrosyl-L-cysteine SNOCys PSI-MOD Nitrosyl S-nitrosylation MOD:00235 S-nitrosyl-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-nitrosyl-L-cysteine. PubMed:10442087 PubMed:11562475 PubMed:15688001 PubMed:8626764 PubMed:8637569 RESID:AA0230 Unimod:275 (2R)-2-amino-3-nitrososulfanyl-propanoic acid L-cysteine nitrite ester MOD_RES S-nitrosocysteine S-nitrosocysteine S-nitrosyl-L-cysteine SNOCys Nitrosyl S-nitrosylation A protein modification that effectively converts an L-asparagine residue to N4-(ADP-ribosyl)-L-asparagine. 541.3 C 15 H 21 N 5 O 13 P 2 541.0611 C 19 H 27 N 7 O 15 P 2 655.41 655.10406 N natural Unimod:213 uniprot.ptm:PTM-0054 (S)-2-amino-4-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]amino)-4-oxobutanoic acid MOD_RES ADP-ribosylasparagine N4-(ADP-ribosyl)-L-asparagine N4-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-asparagine N4-alpha-D-ribofuranosyl-L-asparagine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate) PSI-MOD ADP Ribose addition ADP-Ribosyl MOD:00236 N4-(ADP-ribosyl)-L-asparagine A protein modification that effectively converts an L-asparagine residue to N4-(ADP-ribosyl)-L-asparagine. PubMed:15842200 PubMed:2498316 RESID:AA0231 Unimod:213#N (S)-2-amino-4-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]amino)-4-oxobutanoic acid MOD_RES ADP-ribosylasparagine N4-(ADP-ribosyl)-L-asparagine N4-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-asparagine N4-alpha-D-ribofuranosyl-L-asparagine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate) ADP Ribose addition ADP-Ribosyl A protein modification that effectively converts an L-aspartic acid residue to L-beta-methylthioaspartic acid. 46.09 C 1 H 2 N 0 O 0 S 1 45.98772 C 5 H 7 N 1 O 3 S 1 161.18 161.01466 D natural Unimod:39 uniprot.ptm:PTM-0032 (2R,3Xi)-2-amino-3-(methylsulfanyl)butanedioic acid 3-(methylthio)-L-aspartic acid 3-carboxy-S-methyl-cysteine 3-methylthio-aspartic acid 3MeSAsp MOD_RES 3-methylthioaspartic acid beta-Methylthio-aspartic acid beta-methylthio-aspartic acid bmethylthiold methythiold PSI-MOD Beta-methylthiolation Methylthio MOD:00237 L-beta-methylthioaspartic acid A protein modification that effectively converts an L-aspartic acid residue to L-beta-methylthioaspartic acid. ChEBI:73599 DeltaMass:61 OMSSA:13 OMSSA:26 PubMed:15473684 PubMed:8844851 RESID:AA0232 Unimod:39#D (2R,3Xi)-2-amino-3-(methylsulfanyl)butanedioic acid 3-(methylthio)-L-aspartic acid 3-carboxy-S-methyl-cysteine 3-methylthio-aspartic acid 3MeSAsp MOD_RES 3-methylthioaspartic acid beta-Methylthio-aspartic acid beta-methylthio-aspartic acid bmethylthiold methythiold Beta-methylthiolation Methylthio A protein modification that effectively cross-links an L-lysine residue and an L-tyrosine residue by a carbon-nitrogen bond to form 5'-(N6-L-lysine)-L-topaquinone. 11.97 C 0 H -4 N 0 O 1 11.963614 C 15 H 17 N 3 O 4 303.32 303.12192 K, Y natural uniprot.ptm:PTM-0171 1-[(S)-5-amino-5-carboxypentyl]amino-2-[(S)-2-amino-2-carboxyethyl]-2,6-cyclohexadien-4,5-dione 2'-(L-lys-N6-yl)-L-4',5'-topaquinone 2'-(L-lysine)-L-tyrosyl-4',5'-quinone CROSSLNK Lysine tyrosylquinone (Lys-Tyr) CROSSLNK Lysine tyrosylquinone (Tyr-Lys) LTQ lysyl oxidase cofactor PSI-MOD MOD:00238 Cross-link 2; secondary to RESID:AA0147. 5'-(N6-L-lysine)-L-topaquinone A protein modification that effectively cross-links an L-lysine residue and an L-tyrosine residue by a carbon-nitrogen bond to form 5'-(N6-L-lysine)-L-topaquinone. PubMed:8688089 RESID:AA0233 1-[(S)-5-amino-5-carboxypentyl]amino-2-[(S)-2-amino-2-carboxyethyl]-2,6-cyclohexadien-4,5-dione 2'-(L-lys-N6-yl)-L-4',5'-topaquinone 2'-(L-lysine)-L-tyrosyl-4',5'-quinone CROSSLNK Lysine tyrosylquinone (Lys-Tyr) CROSSLNK Lysine tyrosylquinone (Tyr-Lys) LTQ lysyl oxidase cofactor A protein modification that effectively converts an L-cysteine residue to S-methyl-L-cysteine. 14.03 C 1 H 2 N 0 O 0 S 0 14.01565 C 4 H 7 N 1 O 1 S 1 117.17 117.02483 C natural Unimod:34 uniprot.ptm:PTM-0636 (R)-2-amino-3-(methylsulfanyl)propanoic acid ACT_SITE S-methylcysteine intermediate L-3-(methylthio)alanine MOD_RES S-methylcysteine S-methyl-L-cysteine S-methylated L-cysteine SMeCys PSI-MOD Methyl Methylation MOD:00239 S-methyl-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-methyl-L-cysteine. PubMed:10660523 PubMed:11875433 PubMed:1339288 RESID:AA0234 Unimod:34#C (R)-2-amino-3-(methylsulfanyl)propanoic acid ACT_SITE S-methylcysteine intermediate L-3-(methylthio)alanine MOD_RES S-methylcysteine S-methyl-L-cysteine S-methylated L-cysteine SMeCys Methyl Methylation A protein modification that effectively converts an L-lysine residue to 4-hydroxy-L-lysine. 16.0 C 0 H 0 N 0 O 1 15.994915 C 6 H 12 N 2 O 2 144.17 144.08987 K artifact uniprot.ptm:PTM-0664 (2S,4R)-2,6-diamino-4-hydroxyhexanoic acid 4-hydroxy-L-lysine 4-hydroxylated L-lysine 4HyLys L-threo-gamma-hydroxylysine MOD_RES 4-hydroxylysine alpha,epsilon-diamino-gamma-hydroxycaproic acid PSI-MOD MOD:00240 This modification was not structurally confirmed. Later 5-hydroxy-L-lysine was found at a homologous position in the same protein from closely related species. This is a deprecated entry in RESID. It probably does not occur naturally [JSG]. 4-hydroxy-L-lysine A protein modification that effectively converts an L-lysine residue to 4-hydroxy-L-lysine. ChEBI:141495 PubMed:4005040 RESID:AA0235 (2S,4R)-2,6-diamino-4-hydroxyhexanoic acid 4-hydroxy-L-lysine 4-hydroxylated L-lysine 4HyLys L-threo-gamma-hydroxylysine MOD_RES 4-hydroxylysine alpha,epsilon-diamino-gamma-hydroxycaproic acid A protein modification that effectively converts an L-asparagine residue to N4-hydroxymethyl-L-asparagine. 30.03 C 1 H 2 N 0 O 1 30.010565 C 5 H 8 N 2 O 3 144.13 144.0535 N artifact Unimod:414 (2S)-2-amino-4-[(hydroxymethyl)amino]-4-oxobutanoic acid 2-amino-N4-hydroxymethylbutanediamic acid N(gamma)-hydroxymethylasparagine N4-hydroxymethyl-L-asparagine N4-hydroxymethylasparagine beta-hydroxymethylasparagine PSI-MOD Hydroxymethyl hydroxymethyl MOD:00241 N4-methyl-L-asparagine, see MOD:0079, was found at a homologous position of the same protein in a closely related species. Since the peptide containing this modification was obtained by enzymatic cleavage, not cyanogen bromide cleavage, it could have experienced oxidation of the following methionine residue, leading to the erroneous attribution of a mass of 29 for the modification rather than 14. comment: This is a deprecated entry in RESID. It probably does not occur naturally [JSG]. N4-hydroxymethyl-L-asparagine A protein modification that effectively converts an L-asparagine residue to N4-hydroxymethyl-L-asparagine. RESID:AA0236 Unimod:414 (2S)-2-amino-4-[(hydroxymethyl)amino]-4-oxobutanoic acid 2-amino-N4-hydroxymethylbutanediamic acid N(gamma)-hydroxymethylasparagine N4-hydroxymethyl-L-asparagine N4-hydroxymethylasparagine beta-hydroxymethylasparagine Hydroxymethyl hydroxymethyl A protein modification that effectively converts an L-serine residue to O-(ADP-ribosyl)-L-serine. 541.3 C 15 H 21 N 5 O 13 P 2 541.0611 C 18 H 26 N 6 O 15 P 2 628.38 628.09314 S natural Unimod:213 uniprot.ptm:PTM-0056 (S)-2-amino-3-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]oxy)-propanoic acid MOD_RES ADP-ribosylserine O-(ADP-ribosyl)-L-serine O3-(ADP-ribosyl)-L-serine O3-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-serine O3-alpha-D-ribofuranosyl-L-serine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate) OADPRibSer PSI-MOD ADP Ribose addition ADP-Ribosyl MOD:00242 O-(ADP-ribosyl)-L-serine A protein modification that effectively converts an L-serine residue to O-(ADP-ribosyl)-L-serine. PubMed:15842200 PubMed:3141412 RESID:AA0237 Unimod:213#S (S)-2-amino-3-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]oxy)-propanoic acid MOD_RES ADP-ribosylserine O-(ADP-ribosyl)-L-serine O3-(ADP-ribosyl)-L-serine O3-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-serine O3-alpha-D-ribofuranosyl-L-serine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate) OADPRibSer ADP Ribose addition ADP-Ribosyl A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-cysteine oxazole-4-carboxylic acid. -20.03 C 0 H -4 N 0 O -1 S 0 -20.026215 C 6 H 6 N 2 O 2 S 1 170.19 170.015 C, S natural uniprot.ptm:PTM-0376 2-(1-azanyl-2-sulfanylethyl)-4-oxazolecarboxylic acid 2-[(1R)-1-amino-2-sulfanylethyl]-1,3-oxazole-4-carboxylic acid CROSSLNK Oxazole-4-carboxylic acid (Cys-Ser) L-cysteine oxazole-4-carboxylic acid PSI-MOD MOD:00243 Cross-link 2. L-cysteine oxazole-4-carboxylic acid A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-cysteine oxazole-4-carboxylic acid. PubMed:8183941 PubMed:8895467 RESID:AA0238 2-(1-azanyl-2-sulfanylethyl)-4-oxazolecarboxylic acid 2-[(1R)-1-amino-2-sulfanylethyl]-1,3-oxazole-4-carboxylic acid CROSSLNK Oxazole-4-carboxylic acid (Cys-Ser) L-cysteine oxazole-4-carboxylic acid A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-cysteine oxazoline-4-carboxylic acid. -18.02 C 0 H -2 N 0 O -1 S 0 -18.010565 C 6 H 8 N 2 O 2 S 1 172.2 172.03065 C, S natural uniprot.ptm:PTM-0381 (4S)-2-[(1R)-1-amino-2-sulfanylethyl]-4,5-dihydro-1,3-oxazole-4-carboxylic acid 2-[1-azanyl-2-sulfanylethyl]-4,5-dihydro-1,3-oxazole-4-carboxylic acid CROSSLNK Oxazoline-4-carboxylic acid (Cys-Ser) L-cysteine oxazoline-4-carboxylic acid PSI-MOD MOD:00244 Cross-link 2. L-cysteine oxazoline-4-carboxylic acid A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-cysteine oxazoline-4-carboxylic acid. PubMed:1880060 RESID:AA0239 (4S)-2-[(1R)-1-amino-2-sulfanylethyl]-4,5-dihydro-1,3-oxazole-4-carboxylic acid 2-[1-azanyl-2-sulfanylethyl]-4,5-dihydro-1,3-oxazole-4-carboxylic acid CROSSLNK Oxazoline-4-carboxylic acid (Cys-Ser) L-cysteine oxazoline-4-carboxylic acid A protein modification that effectively crosslinks a glycine residue and an L-serine residue to form glycine oxazole-4-carboxylic acid. -20.03 C 0 H -4 N 0 O -1 -20.026215 C 5 H 4 N 2 O 2 124.1 124.027275 G, S natural uniprot.ptm:PTM-0377 2-aminomethyl-1,3-oxazole-4-carboxylic acid 2-azanylmethyl-1,3-oxazole-4-carboxylic acid CROSSLNK Oxazole-4-carboxylic acid (Gly-Ser) glycine oxazole-4-carboxylic acid PSI-MOD MOD:00245 Cross-link 2. glycine oxazole-4-carboxylic acid A protein modification that effectively crosslinks a glycine residue and an L-serine residue to form glycine oxazole-4-carboxylic acid. PubMed:8183941 PubMed:8895467 RESID:AA0240 2-aminomethyl-1,3-oxazole-4-carboxylic acid 2-azanylmethyl-1,3-oxazole-4-carboxylic acid CROSSLNK Oxazole-4-carboxylic acid (Gly-Ser) glycine oxazole-4-carboxylic acid A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue to form glycine thiazole-4-carboxylic acid. -20.03 C 0 H -4 N 0 O -1 S 0 -20.026215 C 5 H 4 N 2 O 1 S 1 140.16 140.00444 C, G natural uniprot.ptm:PTM-0378 2-(aminomethyl)-1,3-thiazole-4-carboxylic acid 2-(azanylmethyl)-1,3-thiazole-4-carboxylic acid CROSSLNK Thiazole-4-carboxylic acid (Gly-Cys) glycine thiazole-4-carboxylic acid PSI-MOD MOD:00246 Cross-link 2. glycine thiazole-4-carboxylic acid A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue to form glycine thiazole-4-carboxylic acid. ChEBI:21276 PubMed:8183941 PubMed:8895467 RESID:AA0241 2-(aminomethyl)-1,3-thiazole-4-carboxylic acid 2-(azanylmethyl)-1,3-thiazole-4-carboxylic acid CROSSLNK Thiazole-4-carboxylic acid (Gly-Cys) glycine thiazole-4-carboxylic acid A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-serine thiazole-4-carboxylic acid. -20.03 C 0 H -4 N 0 O -1 S 0 -20.026215 C 6 H 6 N 2 O 2 S 1 170.19 170.015 C, S natural uniprot.ptm:PTM-0363 2-[(1S)-1-amino-2-hydroxyethyl]-1,3-thiazole-4-carboxylic acid 2-[1-azanyl-2-hydroxyethyl]-1,3-thiazole-4-carboxylic acid CROSSLNK Thiazole-4-carboxylic acid (Ser-Cys) L-serine thiazole-4-carboxylic acid PSI-MOD MOD:00247 Cross-link 2. L-serine thiazole-4-carboxylic acid A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-serine thiazole-4-carboxylic acid. PubMed:8183941 PubMed:8895467 RESID:AA0242 2-[(1S)-1-amino-2-hydroxyethyl]-1,3-thiazole-4-carboxylic acid 2-[1-azanyl-2-hydroxyethyl]-1,3-thiazole-4-carboxylic acid CROSSLNK Thiazole-4-carboxylic acid (Ser-Cys) L-serine thiazole-4-carboxylic acid A protein modification that effectively crosslinks an L-cysteine residue and an L-phenylalanine residue to form L-phenylalanine thiazole-4-carboxylic acid. -20.03 C 0 H -4 N 0 O -1 S 0 -20.026215 C 12 H 10 N 2 O 1 S 1 230.29 230.05139 C, F natural uniprot.ptm:PTM-0375 2-[(1S)-1-amino-2-phenylethyl]-1,3-thiazole-4-carboxylic acid 2-[1-azanyl-2-phenylethyl]-1,3-thiazole-4-carboxylic acid CROSSLNK Thiazole-4-carboxylic acid (Phe-Cys) L-phenylalanine thiazole-4-carboxylic acid PSI-MOD MOD:00248 Cross-link 2. L-phenylalanine thiazole-4-carboxylic acid A protein modification that effectively crosslinks an L-cysteine residue and an L-phenylalanine residue to form L-phenylalanine thiazole-4-carboxylic acid. PubMed:1880060 RESID:AA0243 2-[(1S)-1-amino-2-phenylethyl]-1,3-thiazole-4-carboxylic acid 2-[1-azanyl-2-phenylethyl]-1,3-thiazole-4-carboxylic acid CROSSLNK Thiazole-4-carboxylic acid (Phe-Cys) L-phenylalanine thiazole-4-carboxylic acid A protein modification that effectively crosslinks two L-cysteine residues to form L-cysteine thiazole-4-carboxylic acid. -20.03 C 0 H -4 N 0 O -1 S 0 -20.026215 C 6 H 6 N 2 O 1 S 2 186.25 185.99216 C, C natural uniprot.ptm:PTM-0360 2-[(1S)-1-amino-2-sulfanylethyl]-1,3-thiazole-4-carboxylic acid 2-[1-azanyl-2-sulfanylethyl]-1,3-thiazole-4-carboxylic acid CROSSLNK Thiazole-4-carboxylic acid (Cys-Cys) L-cysteine thiazole-4-carboxylic acid PSI-MOD MOD:00249 Cross-link 2. L-cysteine thiazole-4-carboxylic acid A protein modification that effectively crosslinks two L-cysteine residues to form L-cysteine thiazole-4-carboxylic acid. PubMed:1880060 RESID:AA0244 2-[(1S)-1-amino-2-sulfanylethyl]-1,3-thiazole-4-carboxylic acid 2-[1-azanyl-2-sulfanylethyl]-1,3-thiazole-4-carboxylic acid CROSSLNK Thiazole-4-carboxylic acid (Cys-Cys) L-cysteine thiazole-4-carboxylic acid A protein modification that effectively crosslinks an L-cysteine residue and an L-lysine residue to form L-lysine thiazole-4-carboxylic acid. -20.03 C 0 H -4 N 0 O -1 S 0 -20.026215 C 9 H 13 N 3 O 1 S 1 211.28 211.07793 C, K hypothetical 2-[(1S)-1,5-diaminopentyl]-1,3-thiazole-4-carboxylic acid 2-[1,5-bis(azanyl)pentyl]-1,3-thiazole-4-carboxylic acid L-lysine thiazole-4-carboxylic acid PSI-MOD MOD:00250 Cross-link 2. Lysine is now thought not to be encoded in the peptide sequence modified to produce GE2270. See RESID:AA0470. This is a deprecated entry in RESID. It probably does not occur naturally [JSG]. L-lysine thiazole-4-carboxylic acid A protein modification that effectively crosslinks an L-cysteine residue and an L-lysine residue to form L-lysine thiazole-4-carboxylic acid. PubMed:1880060 RESID:AA0245 2-[(1S)-1,5-diaminopentyl]-1,3-thiazole-4-carboxylic acid 2-[1,5-bis(azanyl)pentyl]-1,3-thiazole-4-carboxylic acid L-lysine thiazole-4-carboxylic acid A protein modification that effectively crosslinks an L-serine residue and the 5'-end of DNA through a phosphodiester bond to form O-(phospho-5'-DNA)-L-serine. S natural uniprot.ptm:PTM-0226 (S)-2-amino-3-(5'-deoxyribonucleic acid phosphonoxy)propanoic acid ACT_SITE O-(5'-phospho-DNA)-serine intermediate MOD_RES O-(5'-phospho-DNA)-serine O-(phospho-5'-DNA)-L-serine O3-(phospho-5'-DNA)-L-serine O3-L-serine 5'-DNA phosphodiester PSI-MOD MOD:00251 O-(phospho-5'-DNA)-L-serine A protein modification that effectively crosslinks an L-serine residue and the 5'-end of DNA through a phosphodiester bond to form O-(phospho-5'-DNA)-L-serine. PubMed:7142163 PubMed:7265205 RESID:AA0246 (S)-2-amino-3-(5'-deoxyribonucleic acid phosphonoxy)propanoic acid ACT_SITE O-(5'-phospho-DNA)-serine intermediate MOD_RES O-(5'-phospho-DNA)-serine O-(phospho-5'-DNA)-L-serine O3-(phospho-5'-DNA)-L-serine O3-L-serine 5'-DNA phosphodiester A protein modification that effectively cross-links an L-threonine residue to the polymer keratan sulfate by a D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl tetrasaccharide. T natural keratan sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-threonine keratosulfate poly[beta-1,4-(2-acetamido-2-deoxy-6-sulfate D-glucosyl)-beta-1,3-D-galactosyl]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-threonine PSI-MOD MOD:00252 keratan sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-threonine A protein modification that effectively cross-links an L-threonine residue to the polymer keratan sulfate by a D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl tetrasaccharide. PubMed:1417734 PubMed:3472204 RESID:AA0247 keratan sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-threonine keratosulfate poly[beta-1,4-(2-acetamido-2-deoxy-6-sulfate D-glucosyl)-beta-1,3-D-galactosyl]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-threonine A protein modification that effectively converts an L-selenocysteine residue to L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide). 1572.02 C 40 H 47 Mo 1 N 20 O 26 P 4 S 4 Se 0 1572.9857 C 43 H 52 Mo 1 N 21 O 27 P 4 S 4 Se 1 1722.07 1723.9395 U natural Unimod:415 PSI-MOD MOD:00253 L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide) (Sec) A protein modification that effectively converts an L-selenocysteine residue to L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide). PubMed:14235557 PubMed:2211698 PubMed:8052647 PubMed:9036855 RESID:AA0248#SEC Unimod:415 A protein modification that effectively crosslinks an L-tyrosine residue and the 5'-end of RNA through a phosphodiester to form O4'-(phospho-5'-RNA)-L-tyrosine. Y natural uniprot.ptm:PTM-0229 (S)-2-amino-3-[4-(5'-ribonucleic acid phosphonoxy)phenyl]propanoic acid MOD_RES O-(5'-phospho-RNA)-tyrosine O4'-(phospho-5'-RNA)-L-tyrosine O4'-L-tyrosine 5'-RNA phosphodiester PSI-MOD MOD:00254 O4'-(phospho-5'-RNA)-L-tyrosine A protein modification that effectively crosslinks an L-tyrosine residue and the 5'-end of RNA through a phosphodiester to form O4'-(phospho-5'-RNA)-L-tyrosine. PubMed:1702164 PubMed:209034 PubMed:217003 PubMed:6264310 RESID:AA0249 (S)-2-amino-3-[4-(5'-ribonucleic acid phosphonoxy)phenyl]propanoic acid MOD_RES O-(5'-phospho-RNA)-tyrosine O4'-(phospho-5'-RNA)-L-tyrosine O4'-L-tyrosine 5'-RNA phosphodiester A protein modification that effectively cross-links an L-histidine residue and an L-tyrosine residue by a carbon-nitrogen bond to form 3-(3'-L-histidyl)-L-tyrosine. -2.02 C 0 H -2 N 0 O 0 -2.01565 C 15 H 14 N 4 O 3 298.3 298.1066 H, Y natural uniprot.ptm:PTM-0027 (2S,3R)-2-amino-3-(5-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl)-3-(4-hydroxyphenyl)propanoic acid 3-(3'-L-histidyl)-L-tyrosine 3-(N3'-histidyl)tyrosine 3-(pi-histidyl)tyrosine 3-(pros-histidyl)tyrosine CROSSLNK 3'-histidyl-3-tyrosine (His-Tyr) beta-(N(delta)-histidyl)tyrosine beta-(N3'-histidyl)tyrosine PSI-MOD MOD:00255 Cross-link 2. 3-(3'-L-histidyl)-L-tyrosine A protein modification that effectively cross-links an L-histidine residue and an L-tyrosine residue by a carbon-nitrogen bond to form 3-(3'-L-histidyl)-L-tyrosine. PubMed:9144772 RESID:AA0250 (2S,3R)-2-amino-3-(5-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl)-3-(4-hydroxyphenyl)propanoic acid 3-(3'-L-histidyl)-L-tyrosine 3-(N3'-histidyl)tyrosine 3-(pi-histidyl)tyrosine 3-(pros-histidyl)tyrosine CROSSLNK 3'-histidyl-3-tyrosine (His-Tyr) beta-(N(delta)-histidyl)tyrosine beta-(N3'-histidyl)tyrosine A protein modification that dioxygenates an L-methionine residue to L-methionine sulfone. 32.0 C 0 H 0 N 0 O 2 S 0 31.989828 C 5 H 9 N 1 O 3 S 1 163.19 163.03032 M natural Unimod:425 uniprot.ptm:PTM-0175 (2S)-2-amino-4-(methylsulfonyl)butanoic acid L-methionine S,S-dioxide L-methionine sulfone MOD_RES Methionine sulfone MetO2 MethionylSulphone Oxidation of Methionine (to Sulphone) S,S-dioxymethionine suphonem PSI-MOD Dioxidation dihydroxy MOD:00256 DeltaMass gives the formula C 5 H 9 N 3 O 1 S 1 with mass 163 L-methionine sulfone A protein modification that dioxygenates an L-methionine residue to L-methionine sulfone. DeltaMass:205 OMSSA:115 PubMed:12686488 PubMed:7786407 PubMed:7791219 PubMed:9252331 RESID:AA0251 Unimod:425#M (2S)-2-amino-4-(methylsulfonyl)butanoic acid L-methionine S,S-dioxide L-methionine sulfone MOD_RES Methionine sulfone MetO2 MethionylSulphone Oxidation of Methionine (to Sulphone) S,S-dioxymethionine suphonem Dioxidation dihydroxy A protein modification that effectively converts an L-cysteine residue to dipyrrolylmethanemethyl-L-cysteine. 418.4 C 20 H 22 N 2 O 8 S 0 418.1376 C 23 H 27 N 3 O 9 S 1 521.54 521.1468 C natural Unimod:416 uniprot.ptm:PTM-0421 (2S)-3-[5-[4-(2-carboxy)ethyl-3-carboxymethyl-1-pyrrol-2-yl]methyl-4-(2-carboxy)ethyl-3-carboxymethyl-1-pyrrol-2-yl]methylthio-2-aminopropanoic acid 3-[5-(3-acetic acid-4-propanoic acid-1-pyrrol-2-yl)methyl-3-acetic acid-4-propanoic acid-1-pyrrol-2-yl]methylthio-2-aminopropanoic acid MOD_RES S-(dipyrrolylmethanemethyl)cysteine dipyrrole cofactor dipyrrolylmethanemethyl-L-cysteine dipyrrolylmethyl-L-cysteine dipyrromethane cofactor pyrromethane cofactor PSI-MOD Dipyrrolylmethanemethyl dipyrrolylmethanemethyl MOD:00257 dipyrrolylmethanemethyl-L-cysteine A protein modification that effectively converts an L-cysteine residue to dipyrrolylmethanemethyl-L-cysteine. PubMed:3042456 PubMed:3196304 PubMed:3421931 PubMed:8727319 RESID:AA0252 Unimod:416 (2S)-3-[5-[4-(2-carboxy)ethyl-3-carboxymethyl-1-pyrrol-2-yl]methyl-4-(2-carboxy)ethyl-3-carboxymethyl-1-pyrrol-2-yl]methylthio-2-aminopropanoic acid 3-[5-(3-acetic acid-4-propanoic acid-1-pyrrol-2-yl)methyl-3-acetic acid-4-propanoic acid-1-pyrrol-2-yl]methylthio-2-aminopropanoic acid MOD_RES S-(dipyrrolylmethanemethyl)cysteine dipyrrole cofactor dipyrrolylmethanemethyl-L-cysteine dipyrrolylmethyl-L-cysteine dipyrromethane cofactor pyrromethane cofactor Dipyrrolylmethanemethyl dipyrrolylmethanemethyl A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form S-(2-aminovinyl)-3-methyl-D-cysteine. -64.04 C -1 H -4 N 0 O -3 S 0 -64.016045 C 6 H 9 N 2 O 1 S 1 157.21 157.04356 C, T natural C-term uniprot.ptm:PTM-0267 (2S,3S)-2-amino-3-[((Z)-2-aminoethenyl)sulfanyl]butanoic acid 2-amino-3-[(2-aminovinyl)sulfanyl]butanoic acid CROSSLNK S-(2-aminovinyl)-3-methyl-D-cysteine (Thr-Cys) S-(2-aminovinyl)-3-methyl-D-cysteine decarboxylated methyllanthionine PSI-MOD MOD:00258 Cross-link 2. S-(2-aminovinyl)-3-methyl-D-cysteine A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form S-(2-aminovinyl)-3-methyl-D-cysteine. PubMed:9119018 RESID:AA0253 (2S,3S)-2-amino-3-[((Z)-2-aminoethenyl)sulfanyl]butanoic acid 2-amino-3-[(2-aminovinyl)sulfanyl]butanoic acid CROSSLNK S-(2-aminovinyl)-3-methyl-D-cysteine (Thr-Cys) S-(2-aminovinyl)-3-methyl-D-cysteine decarboxylated methyllanthionine A protein modification that effectively crosslinks an L-tyrosine residue and the 5'-end of DNA through a phosphodiester bond to form O4'-(phospho-5'-DNA)-L-tyrosine. Y natural uniprot.ptm:PTM-0228 (S)-2-amino-3-[4-(5'-deoxyribonucleic acid phosphonoxy)phenyl]propanoic acid ACT_SITE O-(5'-phospho-DNA)-tyrosine intermediate MOD_RES O-(5'-phospho-DNA)-tyrosine O4'-(phospho-5'-DNA)-L-tyrosine O4'-L-tyrosine 5'-DNA phosphodiester PSI-MOD MOD:00259 O4'-(phospho-5'-DNA)-L-tyrosine A protein modification that effectively crosslinks an L-tyrosine residue and the 5'-end of DNA through a phosphodiester bond to form O4'-(phospho-5'-DNA)-L-tyrosine. PubMed:1861973 PubMed:2940511 PubMed:3684578 RESID:AA0254 (S)-2-amino-3-[4-(5'-deoxyribonucleic acid phosphonoxy)phenyl]propanoic acid ACT_SITE O-(5'-phospho-DNA)-tyrosine intermediate MOD_RES O-(5'-phospho-DNA)-tyrosine O4'-(phospho-5'-DNA)-L-tyrosine O4'-L-tyrosine 5'-DNA phosphodiester A protein modification that effectively crosslinks an L-threonine residue and the 5'-end of DNA through a phosphodiester bond to form O-(phospho-5'-DNA)-L-threonine. 78.97 C 0 H 0 N 0 O 3 P 1 78.9585 C 4 H 7 N 1 O 5 P 1 180.08 180.00618 T natural (S)-2-amino-3-(5'-deoxyribonucleic acid phosphonoxy)butanoic acid O-(phospho-5'-DNA)-L-threonine O3-(phospho-5'-DNA)-L-threonine O3-L-threonine 5'-DNA phosphodiester PSI-MOD MOD:00260 O-(phospho-5'-DNA)-L-threonine A protein modification that effectively crosslinks an L-threonine residue and the 5'-end of DNA through a phosphodiester bond to form O-(phospho-5'-DNA)-L-threonine. PubMed:3081736 RESID:AA0255 (S)-2-amino-3-(5'-deoxyribonucleic acid phosphonoxy)butanoic acid O-(phospho-5'-DNA)-L-threonine O3-(phospho-5'-DNA)-L-threonine O3-L-threonine 5'-DNA phosphodiester A protein modification that effectively crosslinks an L-tyrosine residue and 5'-phosphouridine through a phosphodiester bond to form O4'-(phospho-5'-uridine)-L-tyrosine. 306.17 C 9 H 11 N 2 O 8 P 1 306.0253 C 18 H 20 N 3 O 10 P 1 469.34 469.08862 Y natural Unimod:417 uniprot.ptm:PTM-0333 (S)-2-amino-3-[4-(5'-uridine phosphonoxy)phenyl]propanoic acid 5'-uridylic-O-tyrosine MOD_RES O-UMP-tyrosine O-Uridinylylation (of Tyrosine) O4'-(phospho-5'-uridine)-L-tyrosine O4'-L-tyrosine 5'-uridine phosphodiester OUMPTyr hydrogen 5'-uridylate tyrosine ester PSI-MOD PhosphoUridine uridine phosphodiester MOD:00261 From DeltaMass: Average Mass: 306. O4'-(phospho-5'-uridine)-L-tyrosine A protein modification that effectively crosslinks an L-tyrosine residue and 5'-phosphouridine through a phosphodiester bond to form O4'-(phospho-5'-uridine)-L-tyrosine. DeltaMass:0 PubMed:11467524 PubMed:2885322 RESID:AA0256 Unimod:417#Y (S)-2-amino-3-[4-(5'-uridine phosphonoxy)phenyl]propanoic acid 5'-uridylic-O-tyrosine MOD_RES O-UMP-tyrosine O-Uridinylylation (of Tyrosine) O4'-(phospho-5'-uridine)-L-tyrosine O4'-L-tyrosine 5'-uridine phosphodiester OUMPTyr hydrogen 5'-uridylate tyrosine ester PhosphoUridine uridine phosphodiester A protein modification that effectively forms a peptide bond between a C-terminal L-glutamic acid residue and a free L-tyrosine. -17.01 C 0 H -1 N 0 O -1 -17.00274 C 14 H 16 N 2 O 5 292.29 292.10593 E, Y natural C-term (S,S)-2-(2-aminopentanedio-1-yl)amino-3-(4-hydoxyphenyl)propanoic acid L-glutamyl L-tyrosine N-(L-glutamyl)-L-tyrosine SITE Involved in polymerization PSI-MOD MOD:00262 Cross-link 2. N-(L-glutamyl)-L-tyrosine A protein modification that effectively forms a peptide bond between a C-terminal L-glutamic acid residue and a free L-tyrosine. ChEBI:21477 PubMed:6387372 PubMed:8093886 RESID:AA0257 (S,S)-2-(2-aminopentanedio-1-yl)amino-3-(4-hydoxyphenyl)propanoic acid L-glutamyl L-tyrosine N-(L-glutamyl)-L-tyrosine SITE Involved in polymerization A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycoviolobilin. 586.69 C 33 H 38 N 4 O 6 S 0 586.2791 C 36 H 43 N 5 O 7 S 1 689.83 689.2883 C natural Unimod:387 (4S)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-18-ethyl-4,5-dihydro-2,7,13,17-tetramethyl-(21H,22H,24H)-biladiene-bc-1,19-dione BINDING Phycoviolobilin chromophore (covalent; via 1 link) PBV PVB PXB S-phycobiliviolin-L-cysteine S-phycoviolobilin-L-cysteine cryptobiliviolin cryptoviolin cryptoviolobilin PSI-MOD Phycocyanobilin phycocyanobilin MOD:00263 S-phycoviolobilin-L-cysteine A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycoviolobilin. PubMed:2106585 PubMed:3208761 RESID:AA0258 Unimod:387 (4S)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-18-ethyl-4,5-dihydro-2,7,13,17-tetramethyl-(21H,22H,24H)-biladiene-bc-1,19-dione BINDING Phycoviolobilin chromophore (covalent; via 1 link) PBV PVB PXB S-phycobiliviolin-L-cysteine S-phycoviolobilin-L-cysteine cryptobiliviolin cryptoviolin cryptoviolobilin Phycocyanobilin phycocyanobilin A protein modification that effectively results from forming an adduct between two cysteine residues and the tetrapyrrole compound phycoerythrobilin. 586.69 C 33 H 38 N 4 O 6 S 0 586.2791 C 39 H 48 N 6 O 8 S 2 792.97 792.2975 C, C natural (2S,3R,16R)-3,18-bis-[(R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-2,7,13,17-tetramethyl-2,3,15,16-tetrahydrobilin-1,19(21H,22H,24H)-dione 3,18-bis-[1-((2-amino-2-carboxy)ethylsulfanyl)ethyl]-2,3,15,16-tetrahydro-2,7,13,17-tetramethyl-1,19-dioxo-(21H,22H,24H)-biladiene-ab-8,12-dipropanoic acid BINDING Phycoerythrobilin chromophore (covalent; via 2 links) PEB phycoerythrobilin biscysteine adduct phycoerythrobilin-bis-L-cysteine PSI-MOD MOD:00264 Cross-link 2. phycoerythrobilin-bis-L-cysteine A protein modification that effectively results from forming an adduct between two cysteine residues and the tetrapyrrole compound phycoerythrobilin. PubMed:3208761 PubMed:3838747 RESID:AA0259 (2S,3R,16R)-3,18-bis-[(R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-2,7,13,17-tetramethyl-2,3,15,16-tetrahydrobilin-1,19(21H,22H,24H)-dione 3,18-bis-[1-((2-amino-2-carboxy)ethylsulfanyl)ethyl]-2,3,15,16-tetrahydro-2,7,13,17-tetramethyl-1,19-dioxo-(21H,22H,24H)-biladiene-ab-8,12-dipropanoic acid BINDING Phycoerythrobilin chromophore (covalent; via 2 links) PEB phycoerythrobilin biscysteine adduct phycoerythrobilin-bis-L-cysteine A protein modification that effectively results from forming an adduct between two cysteine residues and the tetrapyrrole compound phycourobilin. 586.69 C 33 H 38 N 4 O 6 S 0 586.2791 C 39 H 48 N 6 O 8 S 2 792.97 792.2975 C, C natural 3,18-bis(1-[(R)-2-amino-2-carboxyethyl]sulfanylethyl)-2,7,13,17-tetramethyl-1,19-dioxo-4,5,15,16-tetrahydro-(21H,22H,24H)-bilene-b-8,12-dipropanoic acid 3,18-bis(1-[(R)-2-amino-2-carboxyethyl]sulfanylethyl)-8,12-bis(2-carboxyethyl)-2,7,13,17-tetramethyl-4,5,15,16-tetrahydro-(21H,22H,24H)-bilene-b-1,19(4H,16H)-dione BINDING Phycourobilin chromophore (covalent; via 2 links) PUB phycourobilin biscysteine adduct phycourobilin-bis-L-cysteine PSI-MOD MOD:00265 Cross-link 2. phycourobilin-bis-L-cysteine A protein modification that effectively results from forming an adduct between two cysteine residues and the tetrapyrrole compound phycourobilin. PubMed:3208761 PubMed:3838665 PubMed:3838747 PubMed:8876649 RESID:AA0260 3,18-bis(1-[(R)-2-amino-2-carboxyethyl]sulfanylethyl)-2,7,13,17-tetramethyl-1,19-dioxo-4,5,15,16-tetrahydro-(21H,22H,24H)-bilene-b-8,12-dipropanoic acid 3,18-bis(1-[(R)-2-amino-2-carboxyethyl]sulfanylethyl)-8,12-bis(2-carboxyethyl)-2,7,13,17-tetramethyl-4,5,15,16-tetrahydro-(21H,22H,24H)-bilene-b-1,19(4H,16H)-dione BINDING Phycourobilin chromophore (covalent; via 2 links) PUB phycourobilin biscysteine adduct phycourobilin-bis-L-cysteine A protein modification that effectively forms a peptide bond between a C-terminal L-glutamic acid residue and one or more free L-glutamic acid molecules to form N-(L-glutamyl)-poly-L-glutamic acid. E natural C-term PSI-MOD MOD:00266 N-L-glutamyl-poly-L-glutamic acid A protein modification that effectively forms a peptide bond between a C-terminal L-glutamic acid residue and one or more free L-glutamic acid molecules to form N-(L-glutamyl)-poly-L-glutamic acid. PubMed:2570347 PubMed:328274 RESID:AA0261 A protein modification that effectively dioxygenates an L-cysteine residue to L-cysteine sulfinic acid. 32.0 C 0 H 0 N 0 O 2 S 0 31.989828 C 3 H 5 N 1 O 3 S 1 135.14 134.99901 C natural Unimod:425 uniprot.ptm:PTM-0108 (2R)-2-amino-3-sulfinopropanoic acid 2-amino-2-carboxyethanesulfinic acid 2-amino-3-(dioxido-lambda(6)-sulfanyl)propanoic acid [tautomer] 2-amino-3-sulfonylpropanoic acid [tautomer] 3-sulfinoalanine 3-sulphinoalanine CysO2H L-cysteine sulfinic acid MOD_RES Cysteine sulfinic acid (-SO2H) S-cysteinesulfinic acid S-sulfinocysteine cysteine sulphinic acid cysteine-S,S-dioxide [tautomer] sulfinicacid PSI-MOD Dioxidation dihydroxy MOD:00267 "Hyun Ae Woo, et. al., Science 300 (5619), 653-656" L-cysteine sulfinic acid A protein modification that effectively dioxygenates an L-cysteine residue to L-cysteine sulfinic acid. ChEBI:16345 OMSSA:162 PubMed:12686488 PubMed:9252331 PubMed:9586994 RESID:AA0262 Unimod:425#C (2R)-2-amino-3-sulfinopropanoic acid 2-amino-2-carboxyethanesulfinic acid 2-amino-3-(dioxido-lambda(6)-sulfanyl)propanoic acid [tautomer] 2-amino-3-sulfonylpropanoic acid [tautomer] 3-sulfinoalanine 3-sulphinoalanine CysO2H L-cysteine sulfinic acid MOD_RES Cysteine sulfinic acid (-SO2H) S-cysteinesulfinic acid S-sulfinocysteine cysteine sulphinic acid cysteine-S,S-dioxide [tautomer] sulfinicacid Dioxidation dihydroxy A protein modification that effectively converts an L-tyrosine residue to L-3',4',5'-trihydroxyphenylalanine. 32.0 C 0 H 0 N 0 O 2 31.989828 C 9 H 9 N 1 O 4 195.17 195.05316 Y natural Unimod:425 uniprot.ptm:PTM-0667 (S)-2-amino-3-(3,4,5-trihydroxyphenyl)propanoic acid 3,4,6-Trihydroxy-Phenylalanine (from Tyrosine) (TOPA) 35Hy2Tyr L-3',4',5'-trihydroxyphenylalanine L-3,4,5-TOPA MOD_RES 3',4',5'-trihydroxyphenylalanine PSI-MOD Dioxidation dihydroxy MOD:00268 From DeltaMass: Average Mass: 32 L-3',4',5'-trihydroxyphenylalanine A protein modification that effectively converts an L-tyrosine residue to L-3',4',5'-trihydroxyphenylalanine. ChEBI:141811 DeltaMass:0 PubMed:12686488 PubMed:12771378 PubMed:8554314 PubMed:9252331 PubMed:9434739 RESID:AA0263 Unimod:425#Y (S)-2-amino-3-(3,4,5-trihydroxyphenyl)propanoic acid 3,4,6-Trihydroxy-Phenylalanine (from Tyrosine) (TOPA) 35Hy2Tyr L-3',4',5'-trihydroxyphenylalanine L-3,4,5-TOPA MOD_RES 3',4',5'-trihydroxyphenylalanine Dioxidation dihydroxy A protein modification that effectively converts an L-serine residue to O-(sn-1-glycerophosphoryl)-L-serine. 154.06 C 3 H 7 N 0 O 5 P 1 154.00311 C 6 H 12 N 1 O 7 P 1 241.14 241.03514 S natural Unimod:419 uniprot.ptm:PTM-0230 (2S)-2-amino-3-[(2Xi)-2,3-dihydroxypropyl]phosphonoxypropanoic acid MOD_RES O-(sn-1-glycerophosphoryl)serine O-(sn-1-glycerophosphoryl)-L-serine O3-(sn-1-glycerophosphoryl)-L-serine O3-2,3-dihydroxypropyl hydrogen phosphate-L-serine ester O3-L-serine glyceryl-1-phosphodiester alpha-glycerophosphoryl serine glycerophosphoserine PSI-MOD Glycerophospho glycerophospho MOD:00269 O-(sn-1-glycerophosphoryl)-L-serine A protein modification that effectively converts an L-serine residue to O-(sn-1-glycerophosphoryl)-L-serine. PubMed:8645220 RESID:AA0264 Unimod:419#S (2S)-2-amino-3-[(2Xi)-2,3-dihydroxypropyl]phosphonoxypropanoic acid MOD_RES O-(sn-1-glycerophosphoryl)serine O-(sn-1-glycerophosphoryl)-L-serine O3-(sn-1-glycerophosphoryl)-L-serine O3-2,3-dihydroxypropyl hydrogen phosphate-L-serine ester O3-L-serine glyceryl-1-phosphodiester alpha-glycerophosphoryl serine glycerophosphoserine Glycerophospho glycerophospho A protein modification that effectively converts a glycine residue to an internal 1-thioglycine. 16.06 C 0 H 0 N 0 O -1 S 1 15.977156 C 2 H 3 N 1 S 1 73.11 72.99862 G natural uniprot.ptm:PTM-0004 1-thioglycine 2-amino-1-sulfanylethanone MOD_RES 1-thioglycine S(O)Gly aminoethanethioic O-acid aminoethanethioic acid aminoethanethionic acid aminothioacetic acid PSI-MOD Carboxy->Thiocarboxy thiocarboxylic acid MOD:00270 This modification occurs naturally in two forms. At an interior peptide location it exists as aminoethanethionic acid (or aminoethanethioic O-acid). At the carboxyl-terminal it exists as aminoethanethiolic acid (or aminoethanethioic S-acid). 1-thioglycine (internal) A protein modification that effectively converts a glycine residue to an internal 1-thioglycine. PubMed:11463785 PubMed:9367957 RESID:AA0265#INT 1-thioglycine 2-amino-1-sulfanylethanone MOD_RES 1-thioglycine S(O)Gly aminoethanethioic O-acid aminoethanethioic acid aminoethanethionic acid aminothioacetic acid Carboxy->Thiocarboxy thiocarboxylic acid A protein modification that effectively results from forming an adduct between two cysteine residues, the C-3' of a tyrosine residue, and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. 614.48 C 34 Fe 1 H 30 N 4 O 4 S 0 614.1616 C 49 Fe 1 H 49 N 7 O 8 S 2 983.94 983.24335 C, C, Y natural (10S,11S)-[7,12-bis((S)-1-[((R)-2-amino-2-carboxy)ethylsulfanyl]ethyl)-10-(2-hydroxy-5-[(S)-2-amino-2-carboxy]ethylphenyl)-3,8,13,17-tetramethyl-21H,23H-10,11-dihydroporphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate BINDING Heme (covalent; via 3 links) bis(S-cysteinyl)-(tyros-3'-yl)-heme heme P460-bis-L-cysteine-L-tyrosine PSI-MOD MOD:00271 Cross-link 3. heme P460-bis-L-cysteine-L-tyrosine A protein modification that effectively results from forming an adduct between two cysteine residues, the C-3' of a tyrosine residue, and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. PubMed:8325841 PubMed:9095195 RESID:AA0266 (10S,11S)-[7,12-bis((S)-1-[((R)-2-amino-2-carboxy)ethylsulfanyl]ethyl)-10-(2-hydroxy-5-[(S)-2-amino-2-carboxy]ethylphenyl)-3,8,13,17-tetramethyl-21H,23H-10,11-dihydroporphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate BINDING Heme (covalent; via 3 links) bis(S-cysteinyl)-(tyros-3'-yl)-heme heme P460-bis-L-cysteine-L-tyrosine A protein modification that effectively crosslinks an L-threonine residue and 5'-phosphoadenosine through a phosphodiester bond to form O-(phospho-5'-adenosine)-L-threonine. 329.21 C 10 H 12 N 5 O 6 P 1 329.05252 C 14 H 19 N 6 O 8 P 1 430.31 430.1002 T natural Unimod:405 uniprot.ptm:PTM-0393 (2S,3R)-2-amino-3-(5'-adenosine phosphonoxy)butanoic acid 5'-adenylic-O3-L-threonine ACT_SITE O-AMP-threonine intermediate L-threonine monoanhydride with 5'-adenylic acid MOD_RES O-AMP-threonine O(gamma)-5'-adenylic-L-threonine O-(phospho-5'-adenosine)-L-threonine O3-(phospho-5'-adenosine)-L-threonine O3-L-threonine 5'-adenosine phosphodiester beta-5'-adenylic-L-threonine PSI-MOD AMP binding site Phosphoadenosine MOD:00272 O-(phospho-5'-adenosine)-L-threonine A protein modification that effectively crosslinks an L-threonine residue and 5'-phosphoadenosine through a phosphodiester bond to form O-(phospho-5'-adenosine)-L-threonine. PubMed:2989287 PubMed:8917428 RESID:AA0267 Unimod:405#T (2S,3R)-2-amino-3-(5'-adenosine phosphonoxy)butanoic acid 5'-adenylic-O3-L-threonine ACT_SITE O-AMP-threonine intermediate L-threonine monoanhydride with 5'-adenylic acid MOD_RES O-AMP-threonine O(gamma)-5'-adenylic-L-threonine O-(phospho-5'-adenosine)-L-threonine O3-(phospho-5'-adenosine)-L-threonine O3-L-threonine 5'-adenosine phosphodiester beta-5'-adenylic-L-threonine AMP binding site Phosphoadenosine A protein modification that effectively converts four L-cysteine residues, two L-glutamic acid residues, an L-histidine residue and a four-iron three-sulfur three-oxygen cluster to tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino tetrairon disulfide trioxide. 360.5 C 0 Fe 4 H -7 N 0 O 3 S 3 360.58594 C 28 Fe 4 H 34 N 9 O 14 S 7 1168.43 1167.7667 C, C, C, C, E, E, H natural 4Fe-2S-3O cluster METAL Iron-oxo-sulfur (4Fe-2O-2S) METAL Iron-oxo-sulfur (4Fe-2O-2S); via persulfide group METAL Iron-oxo-sulfur (4Fe-2O-2S); via tele nitrogen hybrid four iron cluster 2 mu-1:2kappaO-oxido-mu-1:3kappaO-oxido-mu-2:4kappaO-oxido-mu-3:4kappaS-sulfido-mu3-2:3:4kappaS-sulfido-S-cysteinyl-N1'-histidino-O5-glutamato 1-iron-S5-cysteine persulfido-O5-glutamato 2-iron-3,4-bis-(S-cysteinyl iron) tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino tetrairon disulfide trioxide PSI-MOD prismane iron-sulfur cofactor MOD:00273 Cross-link 7; secondary to RESID:AA0269. tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino tetrairon disulfide trioxide A protein modification that effectively converts four L-cysteine residues, two L-glutamic acid residues, an L-histidine residue and a four-iron three-sulfur three-oxygen cluster to tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino tetrairon disulfide trioxide. PubMed:12764602 RESID:AA0268 4Fe-2S-3O cluster METAL Iron-oxo-sulfur (4Fe-2O-2S) METAL Iron-oxo-sulfur (4Fe-2O-2S); via persulfide group METAL Iron-oxo-sulfur (4Fe-2O-2S); via tele nitrogen hybrid four iron cluster 2 mu-1:2kappaO-oxido-mu-1:3kappaO-oxido-mu-2:4kappaO-oxido-mu-3:4kappaS-sulfido-mu3-2:3:4kappaS-sulfido-S-cysteinyl-N1'-histidino-O5-glutamato 1-iron-S5-cysteine persulfido-O5-glutamato 2-iron-3,4-bis-(S-cysteinyl iron) tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino tetrairon disulfide trioxide prismane iron-sulfur cofactor A protein modification that effectively replaces the hydrogen atom of a cysteine sulfanyl group with a sulfanyl group, forming a disulfanyl group, and converting an L-cysteine residue to L-cysteine persulfide. 32.06 C 0 H 0 N 0 O 0 S 1 31.97207 C 3 H 5 N 1 O 1 S 2 135.2 134.98126 C natural Unimod:421 uniprot.ptm:PTM-0106 (R)-2-amino-3-disulfanylpropanoic acid 2-amino-3-disulfanylpropanoic acid 2-amino-3-hydrodisulfidopropanoic acid 2-amino-3-hydropersulfidopropanoic acid 2-amino-3-persulfhydrylpropanoic acid 3-(thiosulfeno)-alanine 3-disulfanylalanine ACT_SITE Cysteine persulfide intermediate L-cysteine persulfide MOD_RES Cysteine persulfide S-mercaptocysteine S-sulfanylcysteine thiocysteine PSI-MOD Sulfide persulfide MOD:00274 L-cysteine persulfide A protein modification that effectively replaces the hydrogen atom of a cysteine sulfanyl group with a sulfanyl group, forming a disulfanyl group, and converting an L-cysteine residue to L-cysteine persulfide. ChEBI:28839 PubMed:15096637 PubMed:4276457 PubMed:8161529 RESID:AA0269 Unimod:421 (R)-2-amino-3-disulfanylpropanoic acid 2-amino-3-disulfanylpropanoic acid 2-amino-3-hydrodisulfidopropanoic acid 2-amino-3-hydropersulfidopropanoic acid 2-amino-3-persulfhydrylpropanoic acid 3-(thiosulfeno)-alanine 3-disulfanylalanine ACT_SITE Cysteine persulfide intermediate L-cysteine persulfide MOD_RES Cysteine persulfide S-mercaptocysteine S-sulfanylcysteine thiocysteine Sulfide persulfide A protein modification that effectively cross-links an L-histidine residue and an L-tyrosine residue by a carbon-nitrogen bond to form 3'-(1'-L-histidyl)-L-tyrosine. -2.02 C 0 H -2 N 0 O 0 -2.01565 C 15 H 14 N 4 O 3 298.3 298.1066 H, Y natural uniprot.ptm:PTM-0003 (2S)-2-amino-3-[1-(5-[(2S)-2-amino-2-carboxyethyl]-2-hydroxyphenyl)-1H-imidazol-4-yl]propanoic acid 3'-(1'-L-histidyl)-L-tyrosine 3'-(N(epsilon)-histidyl)tyrosine 3'-(N1'-histidyl)tyrosine 3'-(tau-histidyl)tyrosine 3'-(tele-histidyl)tyrosine CROSSLNK 1'-histidyl-3'-tyrosine (His-Tyr) PSI-MOD MOD:00275 Cross-link 2. 3'-(1'-L-histidyl)-L-tyrosine A protein modification that effectively cross-links an L-histidine residue and an L-tyrosine residue by a carbon-nitrogen bond to form 3'-(1'-L-histidyl)-L-tyrosine. ChEBI:19837 PubMed:10338009 RESID:AA0270 (2S)-2-amino-3-[1-(5-[(2S)-2-amino-2-carboxyethyl]-2-hydroxyphenyl)-1H-imidazol-4-yl]propanoic acid 3'-(1'-L-histidyl)-L-tyrosine 3'-(N(epsilon)-histidyl)tyrosine 3'-(N1'-histidyl)tyrosine 3'-(tau-histidyl)tyrosine 3'-(tele-histidyl)tyrosine CROSSLNK 1'-histidyl-3'-tyrosine (His-Tyr) A protein modification that effectively results from forming an adduct between two cysteine residues, a lysine residue, and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. 614.48 C 34 Fe 1 H 30 N 4 O 4 S 0 614.1616 C 46 Fe 1 H 52 N 8 O 7 S 2 948.94 948.27496 C, C, K natural (19S,20S)-[7,12-bis((S)-1-[((R)-2-amino-2-carboxy)ethylsulfanyl]ethyl)-20-([(S)-5-amino-5-carboxypentyl]amino)-3,8,13,17-tetramethyl-21H,23H-19,20-dihydroporphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate BINDING Heme (covalent; via 3 links) bis(S-cysteinyl)-N6-lysino-heme heme P460-bis-L-cysteine-L-lysine PSI-MOD MOD:00276 Cross-link 3. heme P460-bis-L-cysteine-L-lysine A protein modification that effectively results from forming an adduct between two cysteine residues, a lysine residue, and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. PubMed:12709052 PubMed:9237682 RESID:AA0271 (19S,20S)-[7,12-bis((S)-1-[((R)-2-amino-2-carboxy)ethylsulfanyl]ethyl)-20-([(S)-5-amino-5-carboxypentyl]amino)-3,8,13,17-tetramethyl-21H,23H-19,20-dihydroporphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate BINDING Heme (covalent; via 3 links) bis(S-cysteinyl)-N6-lysino-heme heme P460-bis-L-cysteine-L-lysine A protein modification that effectively converts an L-arginine residue to 5-methyl-L-arginine. 14.03 C 1 H 2 N 0 O 0 14.01565 C 7 H 14 N 4 O 1 170.22 170.11676 R natural uniprot.ptm:PTM-0050 (2S,5S)-2-amino-5-carbamimidamidohexanoic acid 2-amino-5-guanidinohexanoic acid 5-methyl-L-arginine 5-methylated L-arginine C5Me1Arg MOD_RES 5-methylarginine delta-methylarginine PSI-MOD 4-methylarginine Methyl Methylation MOD:00277 5-methyl-L-arginine A protein modification that effectively converts an L-arginine residue to 5-methyl-L-arginine. PubMed:10660523 PubMed:11875433 PubMed:9367957 RESID:AA0272 (2S,5S)-2-amino-5-carbamimidamidohexanoic acid 2-amino-5-guanidinohexanoic acid 5-methyl-L-arginine 5-methylated L-arginine C5Me1Arg MOD_RES 5-methylarginine delta-methylarginine 4-methylarginine Methyl Methylation A protein modification that effectively converts an L-glutamine residue to 2-methyl-L-glutamine. 14.03 C 1 H 2 N 0 O 0 14.01565 C 6 H 10 N 2 O 2 142.16 142.07423 Q natural uniprot.ptm:PTM-0016 (S)-2-amino-2-methylpentanediamic acid 2-methyl-L-glutamine 2-methylated L-glutamine 2-methylglutamine C2MeGln MOD_RES 2-methylglutamine alpha-methylglutamine PSI-MOD Methyl Methylation MOD:00278 2-methyl-L-glutamine A protein modification that effectively converts an L-glutamine residue to 2-methyl-L-glutamine. PubMed:10660523 PubMed:11875433 PubMed:9367957 RESID:AA0273 (S)-2-amino-2-methylpentanediamic acid 2-methyl-L-glutamine 2-methylated L-glutamine 2-methylglutamine C2MeGln MOD_RES 2-methylglutamine alpha-methylglutamine Methyl Methylation A protein modification that effectively converts an L-cysteine residue to N-pyruvic acid 2-iminyl-L-cysteine. 70.05 C 3 H 2 N 0 O 2 S 0 70.00548 C 6 H 8 N 1 O 3 S 1 174.19 174.02249 C natural N-term Unimod:422 uniprot.ptm:PTM-0224 (R)-2-(1-carboxy-2-sulfanylethanimino)propanoic acid MOD_RES N-pyruvate 2-iminyl-cysteine N-pyruvic acid 2-iminyl-L-cysteine PSI-MOD N-pyruvic acid 2-iminyl PyruvicAcidIminyl MOD:00279 N-pyruvic acid 2-iminyl-L-cysteine A protein modification that effectively converts an L-cysteine residue to N-pyruvic acid 2-iminyl-L-cysteine. PubMed:1388164 RESID:AA0274 Unimod:422#C (R)-2-(1-carboxy-2-sulfanylethanimino)propanoic acid MOD_RES N-pyruvate 2-iminyl-cysteine N-pyruvic acid 2-iminyl-L-cysteine N-pyruvic acid 2-iminyl PyruvicAcidIminyl A protein modification that effectively converts an L-valine residue to N-pyruvic acid 2-iminyl-L-valine. 70.05 C 3 H 2 N 0 O 2 70.00548 C 8 H 12 N 1 O 3 170.19 170.08171 V natural N-term Unimod:422 uniprot.ptm:PTM-0225 (S)-2-(1-carboxy-2-methylpropanimino)propanoic acid MOD_RES N-pyruvate 2-iminyl-valine N-pyruvic acid 2-iminyl-L-valine PSI-MOD N-pyruvic acid 2-iminyl PyruvicAcidIminyl MOD:00280 N-pyruvic acid 2-iminyl-L-valine A protein modification that effectively converts an L-valine residue to N-pyruvic acid 2-iminyl-L-valine. PubMed:2071591 RESID:AA0275 Unimod:422#V (S)-2-(1-carboxy-2-methylpropanimino)propanoic acid MOD_RES N-pyruvate 2-iminyl-valine N-pyruvic acid 2-iminyl-L-valine N-pyruvic acid 2-iminyl PyruvicAcidIminyl A protein modification that effectively results from forming an adduct between the pros nitrogen of a histidine residue and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. 616.5 C 34 Fe 1 H 32 N 4 O 4 616.1773 C 40 Fe 1 H 39 N 7 O 5 753.64 753.2362 H natural 2-[1-(N3'-histidyl)ethyl]protoporphyrin IX 3'-heme-L-histidine BINDING Heme (covalent; via pros nitrogen) N(delta)-histidyl heme N(pi)-histidyl heme N3'-histidyl heme [7-ethenyl-12-((S)-1-[((R)-2-amino-2-carboxyethyl)-3H-imidazol-3-yl]ethyl)-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate pros-histidyl heme PSI-MOD MOD:00281 3'-heme-L-histidine A protein modification that effectively results from forming an adduct between the pros nitrogen of a histidine residue and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. PubMed:12119398 PubMed:12429096 PubMed:12486054 PubMed:9712585 RESID:AA0276 2-[1-(N3'-histidyl)ethyl]protoporphyrin IX 3'-heme-L-histidine BINDING Heme (covalent; via pros nitrogen) N(delta)-histidyl heme N(pi)-histidyl heme N3'-histidyl heme [7-ethenyl-12-((S)-1-[((R)-2-amino-2-carboxyethyl)-3H-imidazol-3-yl]ethyl)-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate pros-histidyl heme A protein modification that effectively converts an L-cysteine residue to S-selenyl-L-cysteine. 78.97 C 0 H 0 N 0 O 0 S 0 Se 1 79.91652 C 3 H 5 N 1 O 1 S 1 Se 1 182.11 182.9257 C hypothetical Unimod:423 uniprot.ptm:PTM-0282 (R)-2-amino-3-(selanylsulfanyl)propanoic acid 2-amino-3-hydroselenosulfidopropanoic acid 2-amino-3-hydroselenylsulfidopropanoic acid 2-amino-3-hydroselenylthiopropanoic acid ACT_SITE S-selanylcysteine intermediate MOD_RES S-selenylcysteine S-selanyl-L-cysteine S-selanylcysteine S-selenylcysteine PSI-MOD Delta:Se(1) cysteine perselenide selenyl MOD:00282 S-selenyl-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-selenyl-L-cysteine. PubMed:10430865 PubMed:10966817 PubMed:11827487 PubMed:12716131 PubMed:14594807 RESID:AA0277 Unimod:423#C (R)-2-amino-3-(selanylsulfanyl)propanoic acid 2-amino-3-hydroselenosulfidopropanoic acid 2-amino-3-hydroselenylsulfidopropanoic acid 2-amino-3-hydroselenylthiopropanoic acid ACT_SITE S-selanylcysteine intermediate MOD_RES S-selenylcysteine S-selanyl-L-cysteine S-selanylcysteine S-selenylcysteine Delta:Se(1) cysteine perselenide selenyl A protein modification that effectively converts an L-lysine residue to an N6-propylamino-poly(propylmethylamino)-propyldimethylamine-L-lysine. K natural uniprot.ptm:PTM-0198 (alpha)- ([([(5S)-5-amino-5-carboxypentyl]amino)propyl][(methyl)amino])-(omega)-methyl poly[propane-1,3-diyl(methylimino)] MOD_RES N6-poly(methylaminopropyl)lysine N6-[3-([(omega)-(dimethyl)aminopropyl-poly(3-[methylamino]propyl)]amino)propyl]lysine N6-propylamino-poly(propylmethylamino)-propyldimethylamine-L-lysine lysine derivative Lys(x) silaffin polycationic lysine derivative PSI-MOD MOD:00283 N6-propylamino-poly(propylmethylamino)-propyldimethylamine-L-lysine A protein modification that effectively converts an L-lysine residue to an N6-propylamino-poly(propylmethylamino)-propyldimethylamine-L-lysine. PubMed:10550045 PubMed:11349130 RESID:AA0278 (alpha)- ([([(5S)-5-amino-5-carboxypentyl]amino)propyl][(methyl)amino])-(omega)-methyl poly[propane-1,3-diyl(methylimino)] MOD_RES N6-poly(methylaminopropyl)lysine N6-[3-([(omega)-(dimethyl)aminopropyl-poly(3-[methylamino]propyl)]amino)propyl]lysine N6-propylamino-poly(propylmethylamino)-propyldimethylamine-L-lysine lysine derivative Lys(x) silaffin polycationic lysine derivative A protein modification that effectively results from forming an adduct between an aspartic acid residue, a glutamic acid residue, and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. 612.47 C 34 Fe 1 H 28 N 4 O 4 612.146 C 43 Fe 1 H 40 N 6 O 10 856.67 856.2155 D, E hypothetical 1,5-bishydroxymethyl protoporphyrin IX 1-glutamate ester 5-aspartate ester BINDING Heme (covalent; via 2 links) [13-[(S)-(4-amino-4-carboxy)butanoyloxymethyl]-3-[(S)-(3-amino-3-carboxy)propanoyloxymethyl]-7,12-diethenyl-8,17-dimethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate dihydroxyheme-L-aspartate ester-L-glutamate ester peroxidase heme cofactor PSI-MOD MOD:00284 Cross-link 2. dihydroxyheme-L-aspartate ester-L-glutamate ester A protein modification that effectively results from forming an adduct between an aspartic acid residue, a glutamic acid residue, and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. PubMed:10447690 RESID:AA0279 1,5-bishydroxymethyl protoporphyrin IX 1-glutamate ester 5-aspartate ester BINDING Heme (covalent; via 2 links) [13-[(S)-(4-amino-4-carboxy)butanoyloxymethyl]-3-[(S)-(3-amino-3-carboxy)propanoyloxymethyl]-7,12-diethenyl-8,17-dimethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate dihydroxyheme-L-aspartate ester-L-glutamate ester peroxidase heme cofactor A protein modification that effectively results from forming an adduct between an aspartic acid residue, a glutamic acid residue, a methionine residue (forming a sulfonium ether), and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. 613.47 C 34 Fe 1 H 29 N 4 O 4 S 0 613.15326 1+ C 48 Fe 1 H 50 N 7 O 11 S 1 988.87 988.2633 D, E, M natural 1,5-bishydroxymethyl protoporphyrin IX 1-glutamate ester 5-aspartate ester 2-methionine sulfonium BINDING Heme (covalent; via 3 links) [13-[(S)-(4-amino-4-carboxy)butanoyloxymethyl]-3-[(S)-(3-amino-3-carboxy)propanoyloxymethyl]-12-[(S)-(3-amino-3-carboxy)propylsulfoniumethyl]-7-ethenyl-8,17-dimethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate dihydroxyheme-L-aspartate ester-L-glutamate ester-L-methionine sulfonium myeloperoxidase heme cofactor PSI-MOD MOD:00285 Cross-link 3. dihydroxyheme-L-aspartate ester-L-glutamate ester-L-methionine sulfonium A protein modification that effectively results from forming an adduct between an aspartic acid residue, a glutamic acid residue, a methionine residue (forming a sulfonium ether), and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. PubMed:10447690 PubMed:10480885 PubMed:1320128 PubMed:7840679 RESID:AA0280 1,5-bishydroxymethyl protoporphyrin IX 1-glutamate ester 5-aspartate ester 2-methionine sulfonium BINDING Heme (covalent; via 3 links) [13-[(S)-(4-amino-4-carboxy)butanoyloxymethyl]-3-[(S)-(3-amino-3-carboxy)propanoyloxymethyl]-12-[(S)-(3-amino-3-carboxy)propylsulfoniumethyl]-7-ethenyl-8,17-dimethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate dihydroxyheme-L-aspartate ester-L-glutamate ester-L-methionine sulfonium myeloperoxidase heme cofactor A protein modification that effectively converts an L-cysteine residue to L-cysteinyl molybdenum bis(molybdopterin guanine dinucleotide). 1572.02 C 40 H 47 Mo 1 N 20 O 26 P 4 S 4 1572.9857 C 43 H 52 Mo 1 N 21 O 27 P 4 S 5 1675.15 1675.995 C hypothetical Unimod:424 2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraazaanthracen-4-one guanosine dinucleotide L-cysteinyl molybdenum bis(molybdopterin guanine dinucleotide) bis[8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with guanosine)methyl-6-oxo-3,4-disulfanyl-pteridino[6,7-5,6]pyranoato-S3,S4]-cystein-S-yl-molybdenum PSI-MOD MolybdopterinGD molybdenum bis(molybdopterin guanine dinucleotide) MOD:00286 L-cysteinyl molybdenum bis(molybdopterin guanine dinucleotide) A protein modification that effectively converts an L-cysteine residue to L-cysteinyl molybdenum bis(molybdopterin guanine dinucleotide). RESID:AA0281 Unimod:424#C 2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraazaanthracen-4-one guanosine dinucleotide L-cysteinyl molybdenum bis(molybdopterin guanine dinucleotide) bis[8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with guanosine)methyl-6-oxo-3,4-disulfanyl-pteridino[6,7-5,6]pyranoato-S3,S4]-cystein-S-yl-molybdenum MolybdopterinGD molybdenum bis(molybdopterin guanine dinucleotide) A protein modification that effectively converts an L-proline residue to a (2S,3R,4S)-3,4-dihydroxyproline. 32.0 C 0 H 0 N 0 O 2 31.989828 C 5 H 7 N 1 O 3 129.12 129.04259 P natural Unimod:425 uniprot.ptm:PTM-0306 (2S,3R,4S)-3,4-dihydroxyproline (2S,3R,4S)-3,4-dihydroxypyrrolidine-2-carboxylic acid 2,3-trans-3,4-cis-3,4-dihydroxy-L-proline 2-alpha-3-beta-4-beta-3,4-dihydroxyproline 3,4-Dihydroxylation (of Proline) 3,4-dihydroxylated L-proline 34Hy2Pro MOD_RES (3R,4S)-3,4-dihydroxyproline trans-2,3-cis-3,4-dihydroxy-L-proline PSI-MOD Dioxidation dihydroxy MOD:00287 From DeltaMass: Average Mass: 32. (2S,3R,4S)-3,4-dihydroxyproline A protein modification that effectively converts an L-proline residue to a (2S,3R,4S)-3,4-dihydroxyproline. ChEBI:141803 DeltaMass:0 PubMed:12686488 RESID:AA0282 Unimod:425#P (2S,3R,4S)-3,4-dihydroxyproline (2S,3R,4S)-3,4-dihydroxypyrrolidine-2-carboxylic acid 2,3-trans-3,4-cis-3,4-dihydroxy-L-proline 2-alpha-3-beta-4-beta-3,4-dihydroxyproline 3,4-Dihydroxylation (of Proline) 3,4-dihydroxylated L-proline 34Hy2Pro MOD_RES (3R,4S)-3,4-dihydroxyproline trans-2,3-cis-3,4-dihydroxy-L-proline Dioxidation dihydroxy A protein modification that effectively doubly cross-links an L-glutamic acid residue and an L-tyrosine residue with a carbon-carbon bond and a carbon-nitrogen bond to form pyrroloquinoline quinone. 37.92 C 0 H -10 N 0 O 3 37.906494 C 14 H 6 N 2 O 8 330.21 330.01242 E, Y natural uniprot.ptm:PTM-0263 2,4,6-tricarboxylic-pyrrolo[2,3-5,6]quinoline 8,9-quinone 2,7,9-tricarboxy-1H-pyrrolo(2,3-f)quinoline-4,5-dione 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-5,6]quinoline-2,7,9-tricarboxylic acid CROSSLNK Pyrroloquinoline quinone (Glu-Tyr) coenzyme PQQ methoxatin pyrroloquinoline quinone PSI-MOD MOD:00288 Cross-link 2. pyrroloquinoline quinone A protein modification that effectively doubly cross-links an L-glutamic acid residue and an L-tyrosine residue with a carbon-carbon bond and a carbon-nitrogen bond to form pyrroloquinoline quinone. ChEBI:18315 PubMed:1310505 PubMed:7665488 RESID:AA0283 2,4,6-tricarboxylic-pyrrolo[2,3-5,6]quinoline 8,9-quinone 2,7,9-tricarboxy-1H-pyrrolo(2,3-f)quinoline-4,5-dione 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-5,6]quinoline-2,7,9-tricarboxylic acid CROSSLNK Pyrroloquinoline quinone (Glu-Tyr) coenzyme PQQ methoxatin pyrroloquinoline quinone A protein modification that effectively converts three L-cysteine residues, an L-histidine residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-N1'-histidino tetrairon tetrasulfide. 347.59 C 0 Fe 4 H -4 N 0 O 0 S 4 347.59784 2- C 15 Fe 4 H 18 N 6 O 4 S 7 794.15 793.6843 C, C, C, H natural METAL Iron-sulfur (4Fe-4S) METAL Iron-sulfur (4Fe-4S); via tele nitrogen tetra-mu3-sulfidotris(S-cysteinyliron)(N1'-histidinoiron) tris-L-cysteinyl L-N1'-histidino tetrairon tetrasulfide PSI-MOD MOD:00289 Cross-link 4. tris-L-cysteinyl L-N1'-histidino tetrairon tetrasulfide A protein modification that effectively converts three L-cysteine residues, an L-histidine residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-N1'-histidino tetrairon tetrasulfide. PubMed:9836629 RESID:AA0284 METAL Iron-sulfur (4Fe-4S) METAL Iron-sulfur (4Fe-4S); via tele nitrogen tetra-mu3-sulfidotris(S-cysteinyliron)(N1'-histidinoiron) tris-L-cysteinyl L-N1'-histidino tetrairon tetrasulfide A protein modification that effectively converts three L-cysteine residues, an L-histidine residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-N3'-histidino tetrairon tetrasulfide. 347.59 C 0 Fe 4 H -4 N 0 O 0 S 4 347.59784 2- C 15 Fe 4 H 18 N 6 O 4 S 7 794.15 793.6843 C, C, C, H natural METAL Iron-sulfur (4Fe-4S) METAL Iron-sulfur (4Fe-4S); via pros nitrogen tetra-mu3-sulfidotris(S-cysteinyliron)(N3'-histidinoiron) tris-L-cysteinyl L-N3'-histidino tetrairon tetrasulfide PSI-MOD MOD:00290 Cross-link 4. tris-L-cysteinyl L-N3'-histidino tetrairon tetrasulfide A protein modification that effectively converts three L-cysteine residues, an L-histidine residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-N3'-histidino tetrairon tetrasulfide. PubMed:7854413 RESID:AA0285 METAL Iron-sulfur (4Fe-4S) METAL Iron-sulfur (4Fe-4S); via pros nitrogen tetra-mu3-sulfidotris(S-cysteinyliron)(N3'-histidinoiron) tris-L-cysteinyl L-N3'-histidino tetrairon tetrasulfide A protein modification that effectively converts three L-cysteine residues, an L-aspartic acid residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-aspartato tetrairon tetrasulfide. 347.59 C 0 Fe 4 H -4 N 0 O 0 S 4 347.59784 2- C 13 Fe 4 H 16 N 4 O 6 S 7 772.09 771.65234 C, C, C, D natural METAL Iron-sulfur (4Fe-4S) tetra-mu3-sulfidotris(S-cysteinyliron)(O4-aspartatoiron) tris-L-cysteinyl L-aspartato tetrairon tetrasulfide PSI-MOD MOD:00291 Cross-link 4. tris-L-cysteinyl L-aspartato tetrairon tetrasulfide A protein modification that effectively converts three L-cysteine residues, an L-aspartic acid residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-aspartato tetrairon tetrasulfide. PubMed:7819255 PubMed:9283079 RESID:AA0286 METAL Iron-sulfur (4Fe-4S) tetra-mu3-sulfidotris(S-cysteinyliron)(O4-aspartatoiron) tris-L-cysteinyl L-aspartato tetrairon tetrasulfide A protein modification that effectively converts an L-lysine residue to N6-pyruvic acid 2-iminyl-L-lysine. 70.05 C 3 H 2 N 0 O 2 70.00548 C 9 H 14 N 2 O 3 198.22 198.10045 K natural Unimod:422 (2S)-2-amino-6-([1-carboxyethylidene]amino)hexanoic acid ACT_SITE Schiff-base intermediate with substrate N6-pyruvic acid 2-iminyl-L-lysine PSI-MOD N-pyruvic acid 2-iminyl PyruvicAcidIminyl MOD:00292 N6-pyruvic acid 2-iminyl-L-lysine A protein modification that effectively converts an L-lysine residue to N6-pyruvic acid 2-iminyl-L-lysine. PubMed:1463470 PubMed:7853400 PubMed:9047371 RESID:AA0287 Unimod:422#K (2S)-2-amino-6-([1-carboxyethylidene]amino)hexanoic acid ACT_SITE Schiff-base intermediate with substrate N6-pyruvic acid 2-iminyl-L-lysine N-pyruvic acid 2-iminyl PyruvicAcidIminyl A protein modification that effectively converts three L-cysteine residues, an L-serine residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-serinyl tetrairon tetrasulfide. 347.59 C 0 Fe 4 H -4 N 0 O 0 S 4 347.59784 2- C 12 Fe 4 H 16 N 4 O 5 S 7 744.08 743.6574 C, C, C, S hypothetical tetra-mu3-sulfidotris(S-cysteinyliron)(O3-serinyliron) tris-L-cysteinyl L-serinyl tetrairon tetrasulfide PSI-MOD MOD:00293 Cross-link 4. tris-L-cysteinyl L-serinyl tetrairon tetrasulfide A protein modification that effectively converts three L-cysteine residues, an L-serine residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-serinyl tetrairon tetrasulfide. RESID:AA0288 tetra-mu3-sulfidotris(S-cysteinyliron)(O3-serinyliron) tris-L-cysteinyl L-serinyl tetrairon tetrasulfide A protein modification that effectively converts two L-cysteine residues, an L-histidine residues, an L-serine residue and a four-iron four-sulfur cluster to bis-L-cysteinyl L-N3'-histidino L-serinyl tetrairon tetrasulfide. 347.59 C 0 Fe 4 H -4 N 0 O 0 S 4 347.59784 2- C 15 Fe 4 H 18 N 6 O 5 S 6 778.09 777.70715 C, C, H, S hypothetical METAL Iron-sulfur (4Fe-4S) METAL Iron-sulfur (4Fe-4S); via pros nitrogen bis-L-cysteinyl L-N3'-histidino L-serinyl tetrairon tetrasulfide tetra-mu3-sulfidobis(S-cysteinyliron)(N3'-histidinoiron)(O3-serinyliron) PSI-MOD MOD:00294 Cross-link 4. bis-L-cysteinyl L-N3'-histidino L-serinyl tetrairon tetrasulfide A protein modification that effectively converts two L-cysteine residues, an L-histidine residues, an L-serine residue and a four-iron four-sulfur cluster to bis-L-cysteinyl L-N3'-histidino L-serinyl tetrairon tetrasulfide. RESID:AA0289 METAL Iron-sulfur (4Fe-4S) METAL Iron-sulfur (4Fe-4S); via pros nitrogen bis-L-cysteinyl L-N3'-histidino L-serinyl tetrairon tetrasulfide tetra-mu3-sulfidobis(S-cysteinyliron)(N3'-histidinoiron)(O3-serinyliron) A protein modification that effectively converts an L-serine residue to O-octanoyl-L-serine. 126.2 C 8 H 14 N 0 O 1 126.10446 C 11 H 19 N 1 O 3 213.28 213.13649 S natural Unimod:426 uniprot.ptm:PTM-0239 (2S)-2-amino-3-(octanoyloxy)propanoic acid L-serine octanoate ester LIPID O-octanoyl serine O-octanoyl-L-serine O-octanoylated L-serine O3-octanoyl-L-serine OOctSer PSI-MOD Octanoyl octanoyl MOD:00295 O-octanoyl-L-serine A protein modification that effectively converts an L-serine residue to O-octanoyl-L-serine. PubMed:10604470 PubMed:12716131 RESID:AA0290 Unimod:426#S (2S)-2-amino-3-(octanoyloxy)propanoic acid L-serine octanoate ester LIPID O-octanoyl serine O-octanoyl-L-serine O-octanoylated L-serine O3-octanoyl-L-serine OOctSer Octanoyl octanoyl A protein modification that effectively converts an L-serine residue to O-D-glucuronosyl-L-serine. 176.12 C 6 H 8 N 0 O 6 176.03209 C 9 H 13 N 1 O 8 263.2 263.06412 S natural Unimod:54 uniprot.ptm:PTM-0577 (2S)-2-amino-3-(beta-D-glucopyranuronosyl)propanoic acid CARBOHYD O-linked (GlcA) serine O-D-glucuronosyl-L-serine O3-D-glucuronosyl-L-serine PSI-MOD Glucuronyl N-glucuronylation MOD:00296 O-D-glucuronosyl-L-serine A protein modification that effectively converts an L-serine residue to O-D-glucuronosyl-L-serine. PubMed:10858503 PubMed:12716131 PubMed:7398618 RESID:AA0291 Unimod:54#S (2S)-2-amino-3-(beta-D-glucopyranuronosyl)propanoic acid CARBOHYD O-linked (GlcA) serine O-D-glucuronosyl-L-serine O3-D-glucuronosyl-L-serine Glucuronyl N-glucuronylation A protein modification that effectively converts four L-cysteine residues, two L-glutamic acid residues, an L-histidine residue and a three-iron three-sulfur three-oxygen cluster to tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino nickel triiron disulfide trioxide. 363.35 C 0 Fe 3 H -7 N 0 Ni 1 O 3 S 3 362.58633 C 28 Fe 3 H 34 N 9 Ni 1 O 14 S 7 1171.28 1169.7672 C, C, C, C, E, E, H artifact Ni-3Fe-2S-3O cluster carbon monoxide dehydrogenase nickel-iron cofactor hybrid nickel-triiron cluster mu-1:2kappaO-oxido-mu-1:3kappaO-oxido-mu-2:4kappaO-oxido-mu-3:4kappaS-sulfido-mu3-2:3:4kappaS-sulfido-S-cysteinyl-N1'-histidino-O5-glutamato 1-iron-S5-cysteine persulfido-O5-glutamato 2-nickel-3,4-bis-(S-cysteinyl iron) tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino nickel triiron disulfide trioxide PSI-MOD MOD:00297 Cross-link 7; secondary to RESID:AA0269. This is a deprecated entry in RESID. It probably does not occur naturally [JSG]. tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino nickel triiron disulfide trioxide A protein modification that effectively converts four L-cysteine residues, two L-glutamic acid residues, an L-histidine residue and a three-iron three-sulfur three-oxygen cluster to tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino nickel triiron disulfide trioxide. RESID:AA0292 Ni-3Fe-2S-3O cluster carbon monoxide dehydrogenase nickel-iron cofactor hybrid nickel-triiron cluster mu-1:2kappaO-oxido-mu-1:3kappaO-oxido-mu-2:4kappaO-oxido-mu-3:4kappaS-sulfido-mu3-2:3:4kappaS-sulfido-S-cysteinyl-N1'-histidino-O5-glutamato 1-iron-S5-cysteine persulfido-O5-glutamato 2-nickel-3,4-bis-(S-cysteinyl iron) tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino nickel triiron disulfide trioxide A protein modification that effectively converts four L-cysteine residues, an L-glutamic acid residue, an L-histidine residue, an L-serine residue and a one-nickel three-iron three-sulfur three-oxygen cluster to tris-L-cysteinyl L-cysteine persulfido L-glutamato L-histidino L-serinyl nickel triiron disulfide trioxide. 363.35 C 0 Fe 3 H -7 N 0 Ni 1 O 3 S 3 362.58633 C 26 Fe 3 H 32 N 9 Ni 1 O 13 S 7 1129.24 1127.7566 C, C, C, C, E, H, S artifact Ni-3Fe-2S-3O cluster carbon monoxide dehydrogenase nickel-iron cofactor hybrid nickel-triiron cluster mu-1:2kappaO-oxido-mu-1:3kappaO-oxido-mu-2:4kappaO-oxido-mu-3:4kappaS-sulfido-mu3-2:3:4kappaS-sulfido-S-cysteinyl-N1'-histidino-O5-glutamato 1-iron-S5-cysteine persulfido-O3-serinyl 2-nickel-3,4-bis-(S-cysteinyl iron) tris-L-cysteinyl L-cysteine persulfido L-glutamato L-histidino L-serinyl nickel triiron disulfide trioxide PSI-MOD MOD:00298 Cross-link 7; secondary to RESID:AA0269. This is a deprecated entry in RESID. It probably does not occur naturally [JSG]. tris-L-cysteinyl L-cysteine persulfido L-glutamato L-histidino L-serinyl nickel triiron disulfide trioxide A protein modification that effectively converts four L-cysteine residues, an L-glutamic acid residue, an L-histidine residue, an L-serine residue and a one-nickel three-iron three-sulfur three-oxygen cluster to tris-L-cysteinyl L-cysteine persulfido L-glutamato L-histidino L-serinyl nickel triiron disulfide trioxide. PubMed:2550436 RESID:AA0293 Ni-3Fe-2S-3O cluster carbon monoxide dehydrogenase nickel-iron cofactor hybrid nickel-triiron cluster mu-1:2kappaO-oxido-mu-1:3kappaO-oxido-mu-2:4kappaO-oxido-mu-3:4kappaS-sulfido-mu3-2:3:4kappaS-sulfido-S-cysteinyl-N1'-histidino-O5-glutamato 1-iron-S5-cysteine persulfido-O3-serinyl 2-nickel-3,4-bis-(S-cysteinyl iron) tris-L-cysteinyl L-cysteine persulfido L-glutamato L-histidino L-serinyl nickel triiron disulfide trioxide A protein modification that effectively crosslinks an L-asparagine residue and an L-lysine residue by an isopeptide bond with the formation of N6-(L-isoaspartyl)-L-lysine and the release of ammonia. -17.03 C 0 H -3 N -1 O 0 -17.026548 C 10 H 15 N 3 O 3 225.25 225.11134 K, N natural uniprot.ptm:PTM-0153 (2S)-2-amino-6-([(3S)-3-amino-3-carboxypropanoyl]amino)hexanoic acid CROSSLNK Isoaspartyl lysine isopeptide (Lys-Asn) N(epsilon)-(beta-aspartyl)lysine N-(beta-Aspartyl)-Lysine (Crosslink) N6-(L-isoaspartyl)-L-lysine XLNK-4Asp-N6Lys(Asn) beta-(N6-lysyl)aspartyl acid isoaspartyl N6-lysine PSI-MOD MOD:00299 Cross-link 2. N6-(L-isoaspartyl)-L-lysine (Asn) A protein modification that effectively crosslinks an L-asparagine residue and an L-lysine residue by an isopeptide bond with the formation of N6-(L-isoaspartyl)-L-lysine and the release of ammonia. ChEBI:21862 DeltaMass:0 PubMed:11000116 PubMed:6503713 RESID:AA0294 (2S)-2-amino-6-([(3S)-3-amino-3-carboxypropanoyl]amino)hexanoic acid CROSSLNK Isoaspartyl lysine isopeptide (Lys-Asn) N(epsilon)-(beta-aspartyl)lysine N-(beta-Aspartyl)-Lysine (Crosslink) N6-(L-isoaspartyl)-L-lysine XLNK-4Asp-N6Lys(Asn) beta-(N6-lysyl)aspartyl acid isoaspartyl N6-lysine A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl-5-poly(ADP-ribose). E natural Unimod:213 (S)-2-amino-5-poly[2'-adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with 1alpha-D-ribofuranosyl]oxy-5-oxopentanoic acid L-glutamyl-5-poly(ADP-ribose) L-isoglutamyl-poly(ADP-ribose) MOD_RES PolyADP-ribosyl glutamic acid O-ADP-ribosylation (on Glutamate or C terminus) PSI-MOD ADP Ribose addition ADP-Ribosyl MOD:00300 L-glutamyl-5-poly(ADP-ribose) A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl-5-poly(ADP-ribose). DeltaMass:0 PubMed:11246023 PubMed:15842200 PubMed:8533153 RESID:AA0295 Unimod:213#E (S)-2-amino-5-poly[2'-adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with 1alpha-D-ribofuranosyl]oxy-5-oxopentanoic acid L-glutamyl-5-poly(ADP-ribose) L-isoglutamyl-poly(ADP-ribose) MOD_RES PolyADP-ribosyl glutamic acid O-ADP-ribosylation (on Glutamate or C terminus) ADP Ribose addition ADP-Ribosyl A protein modification that effectively converts an L-serine residue to O-(N-acetylglucosamine-1-phosphoryl)-L-serine. 283.17 C 8 H 14 N 1 O 8 P 1 283.04572 C 11 H 19 N 2 O 10 P 1 370.25 370.07773 S natural Unimod:428 uniprot.ptm:PTM-0586 (2S)-2-amino-3-[([(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)oxy][hydroxy]phosphoryl)oxy]propanoic acid CARBOHYD O-linked (GalNAcP) serine O-(N-acetylglucosamine-1-phosphoryl)-L-serine O-GlcNAc-1-phosphorylation (of Serine) O-beta(N-acetyl-glucosamine-alpha1-phosphate)serine O3-(N-acetylglucosamine-1-phosphoryl)-L-serine O3-L-serine 2-(acetylamino)-2-deoxy-D-glucopyranose 1-phosphodiester PSI-MOD N-acetylglucosamine-1-phosphoryl PhosphoHexNAc MOD:00301 O-(N-acetylglucosamine-1-phosphoryl)-L-serine A protein modification that effectively converts an L-serine residue to O-(N-acetylglucosamine-1-phosphoryl)-L-serine. DeltaMass:0 PubMed:6438439 PubMed:6993483 PubMed:8631906 RESID:AA0296 Unimod:428 (2S)-2-amino-3-[([(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)oxy][hydroxy]phosphoryl)oxy]propanoic acid CARBOHYD O-linked (GalNAcP) serine O-(N-acetylglucosamine-1-phosphoryl)-L-serine O-GlcNAc-1-phosphorylation (of Serine) O-beta(N-acetyl-glucosamine-alpha1-phosphate)serine O3-(N-acetylglucosamine-1-phosphoryl)-L-serine O3-L-serine 2-(acetylamino)-2-deoxy-D-glucopyranose 1-phosphodiester N-acetylglucosamine-1-phosphoryl PhosphoHexNAc A protein modification that effectively converts an L-serine residue to O-(phosphoglycosyl-D-mannose-1-phosphoryl)-L-serine. 242.12 C 6 H 11 N 0 O 8 P 1 242.01915 C 9 H 16 N 1 O 10 P 1 329.2 329.05118 S natural Unimod:429 uniprot.ptm:PTM-0594 CARBOHYD O-linked (Man1P) serine O-(D-mannose-1-phosphoryl)-L-serine O-(alpha-D-mannosyl-1-phosphoryl)-L-serine O-[alpha-D-mannopyranosyloxy(hydroxy)phosphoryl]-L-serine O3-(D-mannose-1-phosphoryl)-L-serine O3-L-serine alpha-D-mannopyranose 1-phosphodiester PSI-MOD PhosphoHex phosphoglycosyl-D-mannose-1-phosphoryl MOD:00302 O-(phosphoglycosyl-D-mannose-1-phosphoryl)-L-serine A protein modification that effectively converts an L-serine residue to O-(phosphoglycosyl-D-mannose-1-phosphoryl)-L-serine. PubMed:10037765 PubMed:15649890 RESID:AA0297 Unimod:429 CARBOHYD O-linked (Man1P) serine O-(D-mannose-1-phosphoryl)-L-serine O-(alpha-D-mannosyl-1-phosphoryl)-L-serine O-[alpha-D-mannopyranosyloxy(hydroxy)phosphoryl]-L-serine O3-(D-mannose-1-phosphoryl)-L-serine O3-L-serine alpha-D-mannopyranose 1-phosphodiester PhosphoHex phosphoglycosyl-D-mannose-1-phosphoryl A protein modification that effectively converts seven L-histidinine residues and a four-copper one-sulfur one-hydroxide cluster to heptakis-L-histidino tetracopper mu4-sulfide hydroxide. 296.19 C 0 Cu 4 H -6 N 0 O 1 S 1 293.63843 C 42 Cu 4 H 43 N 21 O 8 S 1 1256.19 1253.0508 H, H, H, H, H, H, H natural heptakis-L-histidino tetracopper mu4-sulfide hydroxide mu4-sulfido bis(bis-N1'-histidino copper)(N1'-histidino-N3'-histidino copper)(N3'-histidino hydroxide copper) nitrous oxide reductase nosZ CuZ cluster pentakis-L-N1'-histidino-bis-L-N3'-histidino tetracopper sulfide hydroxide PSI-MOD MOD:00303 Cross-link 7. heptakis-L-histidino tetracopper mu4-sulfide hydroxide A protein modification that effectively converts seven L-histidinine residues and a four-copper one-sulfur one-hydroxide cluster to heptakis-L-histidino tetracopper mu4-sulfide hydroxide. PubMed:11024061 PubMed:11041839 RESID:AA0298 heptakis-L-histidino tetracopper mu4-sulfide hydroxide mu4-sulfido bis(bis-N1'-histidino copper)(N1'-histidino-N3'-histidino copper)(N3'-histidino hydroxide copper) nitrous oxide reductase nosZ CuZ cluster pentakis-L-N1'-histidino-bis-L-N3'-histidino tetracopper sulfide hydroxide A protein modification that effectively converts an L-leucine residue to L-leucine methyl ester. 14.03 C 1 H 2 N 0 O 0 14.01565 C 7 H 14 N 1 O 2 144.19 144.10245 L natural C-term Unimod:34 uniprot.ptm:PTM-0167 2-amino-4-methylpentanoic methyl ester L-leucine methyl ester MOD_RES Leucine methyl ester OMeLeu alpha-aminoisocaproic methyl ester methyl (2S)-2-amino-4-methylpentanoate methyl L-leucinate methyl esterified L-leucine PSI-MOD Methyl Methylation MOD:00304 incidental to RESID:AA0039 L-leucine methyl ester A protein modification that effectively converts an L-leucine residue to L-leucine methyl ester. PubMed:10191253 PubMed:11875433 PubMed:8206937 RESID:AA0299 Unimod:34#C-term 2-amino-4-methylpentanoic methyl ester L-leucine methyl ester MOD_RES Leucine methyl ester OMeLeu alpha-aminoisocaproic methyl ester methyl (2S)-2-amino-4-methylpentanoate methyl L-leucinate methyl esterified L-leucine Methyl Methylation A protein modification that effectively converts six L-cysteine residues, an L-serine residue and a eight-iron seven-sulfur cluster to hexakis-L-cysteinyl L-serinyl octairon heptasulfide. 663.12 C 0 Fe 8 H -8 N 0 O 0 S 7 663.223 3- C 21 Fe 8 H 27 N 7 O 8 S 13 1369.03 1368.3102 C, C, C, C, C, C, S natural Cys6Ser-[8Fe7S] METAL Iron-sulfur (8Fe-7S) hexakis-L-cysteinyl L-serinyl octairon heptasulfide nitrogenase P-cluster PSI-MOD MOD:00305 Cross-link 7; incidental to RESID:AA0141. hexakis-L-cysteinyl L-serinyl octairon heptasulfide A protein modification that effectively converts six L-cysteine residues, an L-serine residue and a eight-iron seven-sulfur cluster to hexakis-L-cysteinyl L-serinyl octairon heptasulfide. PubMed:10525412 PubMed:12215645 PubMed:9063865 RESID:AA0300 Cys6Ser-[8Fe7S] METAL Iron-sulfur (8Fe-7S) hexakis-L-cysteinyl L-serinyl octairon heptasulfide nitrogenase P-cluster Natural or modified residues with a mass of 113.084064 Da. 0.0 C 0 H 0 N 0 O 0 0.0 C 6 H 11 N 1 O 1 113.16 113.08406 X L-isoleucine or L-leucine Xle PSI-MOD MOD:00306 residues isobaric at 113.084064 Da Natural or modified residues with a mass of 113.084064 Da. PubMed:10523135 RESID:AA0301 L-isoleucine or L-leucine Xle A protein modification that effectively cyclizes an L-asparagine residue to form a carboxyl-terminal L-aspartimide. -18.02 C 0 H -2 N 0 O -1 -18.010565 C 4 H 5 N 2 O 2 113.1 113.0351 N natural C-term Unimod:23 (3S)-3-amino-2,5-pyrrolidinedione 2-amino-butanimide ASI L-2-aminosuccinimide L-asparaginimide L-aspartimide Succinimide formation from asparagine alpha-aminosuccinimide PSI-MOD Dehydrated Dehydration L-3-aminosuccinimide MOD:00307 From DeltaMass: Average Mass: -17 Average Mass Change:-17 References:Clarke, S., Lability of Aspargine and Aspartic Acid Residues in Protein and Peptides, in: Stability of Protein Pharmaceuticals : Chemical and Physical Paths of Protein Degradation, Part A (T.J. Ahern and M.C. Manning, eds.), 1992,Plenum Press, New York, pp.1-29Xie, M.; Vander Velde, D.; Morton, M.; Borchardt, R.T.; Schowen,R.L.: pH-Induced Change in the Rate-Determining Step for the Hydrolysis of the Asp/Asn-Derived Cyclic-Imide Intermediate in Protein Degradation. (1996) J. Am. Chem. Soc. 118: 8955-8956. L-aspartimide A protein modification that effectively cyclizes an L-asparagine residue to form a carboxyl-terminal L-aspartimide. DeltaMass:18 PubMed:12771378 PubMed:2378679 PubMed:7662664 PubMed:7988548 PubMed:9309583 RESID:AA0302 Unimod:23#N (3S)-3-amino-2,5-pyrrolidinedione 2-amino-butanimide ASI L-2-aminosuccinimide L-asparaginimide L-aspartimide Succinimide formation from asparagine alpha-aminosuccinimide Dehydrated Dehydration L-3-aminosuccinimide A protein modification that effectively cyclizes an L-glutamine residue to form a carboxyl-terminal L-glutamimide. -18.02 C 0 H -2 N 0 O -1 -18.010565 C 5 H 7 N 2 O 2 127.12 127.05075 Q hypothetical C-term Unimod:23 (3S)-3-aminopiperidine-2,6-dione 2-aminopentanimide 3-amino-2,6-piperidinedione L-glutamimide alpha-aminoglutarimide PSI-MOD Dehydrated Dehydration MOD:00308 L-glutamimide A protein modification that effectively cyclizes an L-glutamine residue to form a carboxyl-terminal L-glutamimide. PubMed:12771378 PubMed:14593103 RESID:AA0303 Unimod:23#Q (3S)-3-aminopiperidine-2,6-dione 2-aminopentanimide 3-amino-2,6-piperidinedione L-glutamimide alpha-aminoglutarimide Dehydrated Dehydration A protein modification that effectively converts an L-aspartic acid residue to L-beta-carboxyaspartic acid. 44.01 C 1 H 0 N 0 O 2 43.98983 C 5 H 5 N 1 O 5 159.1 159.01677 D hypothetical Unimod:299 (2S)-2-aminoethane-1,1,2-tricarboxylic acid 2-amino-3-carboxybutanedioic acid 3-carboxy-L-aspartic acid 3-carboxyaspartic acid 3CbxAsp beta-carboxyaspartic acid gammacarboxyld PSI-MOD Carboxy Carboxylation MOD:00309 References to this modification as a gamma-carboxylation are in error [JSG]. L-beta-carboxyaspartic acid A protein modification that effectively converts an L-aspartic acid residue to L-beta-carboxyaspartic acid. OMSSA:47 PubMed:6390094 PubMed:7138832 PubMed:7457858 PubMed:8135347 RESID:AA0304 Unimod:299#D (2S)-2-aminoethane-1,1,2-tricarboxylic acid 2-amino-3-carboxybutanedioic acid 3-carboxy-L-aspartic acid 3-carboxyaspartic acid 3CbxAsp beta-carboxyaspartic acid gammacarboxyld Carboxy Carboxy Carboxylation A protein modification that effectively converts an L-arginine residue to N5-methyl-L-arginine. 14.03 C 1 H 2 N 0 O 0 14.01565 C 7 H 14 N 4 O 1 170.22 170.11676 R hypothetical uniprot.ptm:PTM-0185 (2S)-2-amino-5-(N-methylcarbamimidamido)pentanoic acid MOD_RES N5-methylarginine N5-carbamimidoyl-N5-methyl-L-ornithine N5-methyl-L-arginine N5-methylated L-arginine N5Me1Arg delta-N-methylarginine PSI-MOD Methyl Methylation MOD:00310 N5-methyl-L-arginine A protein modification that effectively converts an L-arginine residue to N5-methyl-L-arginine. PubMed:11875433 PubMed:9792625 PubMed:9873020 RESID:AA0305 (2S)-2-amino-5-(N-methylcarbamimidamido)pentanoic acid MOD_RES N5-methylarginine N5-carbamimidoyl-N5-methyl-L-ornithine N5-methyl-L-arginine N5-methylated L-arginine N5Me1Arg delta-N-methylarginine Methyl Methylation A protein modification that effectively converts an L-cysteine residue to L-cysteine coenzyme A disulfide. 765.52 C 21 H 34 N 7 O 16 P 3 S 1 765.09955 C 24 H 39 N 8 O 17 P 3 S 2 868.66 868.10876 C hypothetical Unimod:281 (2R)-2-amino-3-(2-((3-(((2R)-2,4-dihydroxy-3,3-dimethyl-1-oxobutyl)amino)-1-oxopropyl)amino)ethyl)dithio-propanoic acid 4'-ester with adenosine 5'-(trihydrogen diphosphate) 3'-(dihydrogen phosphate) L-cysteine coenzyme A disulfide SCoACys coenzyme A L-cysteine mixed disulfide PSI-MOD CoenzymeA Cysteine modified Coenzyme A MOD:00311 DeltaMass gives no formula with mass as 454. L-cysteine coenzyme A disulfide A protein modification that effectively converts an L-cysteine residue to L-cysteine coenzyme A disulfide. DeltaMass:0 PubMed:1734967 RESID:AA0306 Unimod:281#C (2R)-2-amino-3-(2-((3-(((2R)-2,4-dihydroxy-3,3-dimethyl-1-oxobutyl)amino)-1-oxopropyl)amino)ethyl)dithio-propanoic acid 4'-ester with adenosine 5'-(trihydrogen diphosphate) 3'-(dihydrogen phosphate) L-cysteine coenzyme A disulfide SCoACys coenzyme A L-cysteine mixed disulfide CoenzymeA Cysteine modified Coenzyme A A protein modification that effectively converts an L-cysteine residue to S-myristoyl-L-cysteine. 210.36 C 14 H 26 N 0 O 1 S 0 210.19836 C 17 H 31 N 1 O 2 S 1 313.5 313.20755 C hypothetical Unimod:45 (R)-2-amino-3-(tetradecanoylsulfanyl)propanoic acid LIPID S-myristoyl cysteine S-(C14:1 aliphatic acyl)cysteine S-myristoyl-L-cysteine S-myristoylated L-cysteine SMyrCys tetradecanoate cysteine thioester PSI-MOD Myristoyl Myristoylation MOD:00312 S-myristoyl-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-myristoyl-L-cysteine. PubMed:10026218 PubMed:10080938 PubMed:8824274 RESID:AA0307 Unimod:45#C (R)-2-amino-3-(tetradecanoylsulfanyl)propanoic acid LIPID S-myristoyl cysteine S-(C14:1 aliphatic acyl)cysteine S-myristoyl-L-cysteine S-myristoylated L-cysteine SMyrCys tetradecanoate cysteine thioester Myristoyl Myristoylation A protein modification that effectively converts an L-cysteine residue to S-palmitoleyl-L-cysteine. 236.4 C 16 H 28 N 0 O 1 S 0 236.21402 C 19 H 33 N 1 O 2 S 1 339.54 339.2232 C hypothetical Unimod:431 uniprot.ptm:PTM-0645 (R)-2-amino-3-((Z)-9-hexadecenoylsulfanyl)propanoic acid S-palmitoleyl-L-cysteine S-palmitoleylated L-cysteine SPamD1Cys cis-9-hexadecenoate cysteine thioester mod187 PSI-MOD Palmitoleyl palmitoleyl MOD:00313 S-palmitoleyl-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-palmitoleyl-L-cysteine. OMSSA:187 PubMed:8294460 RESID:AA0308 Unimod:431#C (R)-2-amino-3-((Z)-9-hexadecenoylsulfanyl)propanoic acid S-palmitoleyl-L-cysteine S-palmitoleylated L-cysteine SPamD1Cys cis-9-hexadecenoate cysteine thioester mod187 Palmitoleyl palmitoleyl A protein modification that effectively converts a glycine residue to glycine cholesterol ester. 368.65 C 27 H 44 N 0 O 0 368.3443 C 29 H 48 N 1 O 2 442.71 442.3685 G natural C-term Unimod:432 uniprot.ptm:PTM-0090 LIPID Cholesterol glycine ester cholesteryl glycinate glycine cholest-5-en-3beta-ol ester glycine cholesterol ester hedgehog lipophilic adduct PSI-MOD C-cholesterol cholesterol ester MOD:00314 Incidental to RESID:AA0060. Unimod origin corrected [JSG]. glycine cholesterol ester A protein modification that effectively converts a glycine residue to glycine cholesterol ester. ChEBI:143135 PubMed:11111088 PubMed:8824192 RESID:AA0309 Unimod:432#C-term LIPID Cholesterol glycine ester cholesteryl glycinate glycine cholest-5-en-3beta-ol ester glycine cholesterol ester hedgehog lipophilic adduct C-cholesterol cholesterol ester A protein modification that effectively converts five L-cysteine residues, an L-histidine residue and a one-nickel four-iron five-sulfur cluster to pentakis-L-cysteinyl L-histidino nickel tetrairon pentasulfide. 436.33 C 0 Fe 4 H -6 N 0 Ni 1 O 0 S 5 435.4885 C 21 Fe 4 H 26 N 8 Ni 1 O 6 S 10 1089.16 1087.5934 C, C, C, C, C, H natural METAL Nickel-iron-sulfur (Ni-4Fe-5S) METAL Nickel-iron-sulfur (Ni-4Fe-5S); via tele nitrogen Ni-4Fe-5S cluster carbon monoxide dehydrogenase nickel-iron cofactor mu-1:2kappaS-sulfido-mu3-1:3:5kappaS-sulfido-mu3-2:3:4kappaS-sulfido-mu3-2:4:5kappaS-sulfido-mu3-3:4:5kappaS-sulfido-N1'-histidino-S-cysteinyl-1-iron-S-cysteinyl-2-nickel-3,4,5-tris-(S-cysteinyl iron) pentakis-L-cysteinyl L-histidino nickel tetrairon pentasulfide PSI-MOD MOD:00315 Cross-link 6. pentakis-L-cysteinyl L-histidino nickel tetrairon pentasulfide A protein modification that effectively converts five L-cysteine residues, an L-histidine residue and a one-nickel four-iron five-sulfur cluster to pentakis-L-cysteinyl L-histidino nickel tetrairon pentasulfide. PubMed:11509720 PubMed:2550436 RESID:AA0310 METAL Nickel-iron-sulfur (Ni-4Fe-5S) METAL Nickel-iron-sulfur (Ni-4Fe-5S); via tele nitrogen Ni-4Fe-5S cluster carbon monoxide dehydrogenase nickel-iron cofactor mu-1:2kappaS-sulfido-mu3-1:3:5kappaS-sulfido-mu3-2:3:4kappaS-sulfido-mu3-2:4:5kappaS-sulfido-mu3-3:4:5kappaS-sulfido-N1'-histidino-S-cysteinyl-1-iron-S-cysteinyl-2-nickel-3,4,5-tris-(S-cysteinyl iron) pentakis-L-cysteinyl L-histidino nickel tetrairon pentasulfide A protein modification that effectively converts an L-asparagine residue to N4,N4-dimethyl-L-asparagine. 28.05 C 2 H 4 N 0 O 0 28.0313 C 6 H 10 N 2 O 2 142.16 142.07423 N hypothetical Unimod:36 uniprot.ptm:PTM-0182 (2S)-2-amino-4-(dimethylamino)-4-oxobutanoic acid 2-amino-N4,N4-dimethylbutanediamic acid MOD_RES N4,N4-dimethylasparagine N(gamma),N(gamma)-dimethylasparagine N4,N4-dimethyl-L-asparagine N4,N4-dimethylated L-asparagine N4Me2Asn PSI-MOD Dimethyl beta-dimethylasparagine di-Methylation MOD:00316 N4,N4-dimethyl-L-asparagine A protein modification that effectively converts an L-asparagine residue to N4,N4-dimethyl-L-asparagine. PubMed:12964758 PubMed:14570711 PubMed:8783012 RESID:AA0311 Unimod:36#N (2S)-2-amino-4-(dimethylamino)-4-oxobutanoic acid 2-amino-N4,N4-dimethylbutanediamic acid MOD_RES N4,N4-dimethylasparagine N(gamma),N(gamma)-dimethylasparagine N4,N4-dimethyl-L-asparagine N4,N4-dimethylated L-asparagine N4Me2Asn Dimethyl beta-dimethylasparagine di-Methylation A protein modification that effectively converts an L-lysine residue to N6-3,4-didehydroretinylidene-L-lysine. 264.41 C 20 H 24 N 0 O 0 264.1878 C 26 H 36 N 2 O 1 392.59 392.28278 K natural Unimod:433 (S)-2-amino-6-[(2E,4E,6E,8E)-3,7-dimethyl-9-(2,6,6-trimethylcyclohexa-1,3-dien-1-yl)-2,4,6,8-nonatetraenylidene]aminohexanoic acid N6-(3,4-didehydroretinylidene)-L-lysine N6-3-dehydroretinal-L-lysine N6-3-dehydroretinyl-lysine PSI-MOD 3,4-didehydroretinylidene Didehydroretinylidene MOD:00317 N6-3,4-didehydroretinylidene-L-lysine A protein modification that effectively converts an L-lysine residue to N6-3,4-didehydroretinylidene-L-lysine. PubMed:10717661 PubMed:3257009 PubMed:4056688 RESID:AA0312 Unimod:433#K (S)-2-amino-6-[(2E,4E,6E,8E)-3,7-dimethyl-9-(2,6,6-trimethylcyclohexa-1,3-dien-1-yl)-2,4,6,8-nonatetraenylidene]aminohexanoic acid N6-(3,4-didehydroretinylidene)-L-lysine N6-3-dehydroretinal-L-lysine N6-3-dehydroretinyl-lysine 3,4-didehydroretinylidene Didehydroretinylidene A protein modification that effectively cross-links an L-cysteine residue and an L-tryptophan residue by a thioether bond to form 4'-(S-L-cysteinyl)-L-tryptophyl quinone. 27.97 C 0 H -4 N 0 O 2 S 0 27.958529 C 14 H 11 N 3 O 4 S 1 317.32 317.04703 C, W natural uniprot.ptm:PTM-0041 (2R)-2-amino-3-[(3-[(2S)-2-amino-2-carboxyethyl]-6,7-dioxo-6,7-dihydro-1H-indol-4-yl)sulfanyl]propanoic acid 3-(2-amino-2-carboxyethyl)-4-[2-amino-2-carboxyethyl]sulfanyl-6,7-indolinedione 4'-(L-cystein-S-yl)-L-tryptophyl quinone 4-(S-cysteinyl)tryptophan-6,7-dione CROSSLNK 4'-cysteinyl-tryptophylquinone (Cys-Trp) CTQ cysteine tryptophylquinone PSI-MOD MOD:00318 Cross-link 2; secondary to RESID:AA0148. 4'-(S-L-cysteinyl)-L-tryptophyl quinone A protein modification that effectively cross-links an L-cysteine residue and an L-tryptophan residue by a thioether bond to form 4'-(S-L-cysteinyl)-L-tryptophyl quinone. PubMed:11555656 PubMed:11717396 RESID:AA0313 (2R)-2-amino-3-[(3-[(2S)-2-amino-2-carboxyethyl]-6,7-dioxo-6,7-dihydro-1H-indol-4-yl)sulfanyl]propanoic acid 3-(2-amino-2-carboxyethyl)-4-[2-amino-2-carboxyethyl]sulfanyl-6,7-indolinedione 4'-(L-cystein-S-yl)-L-tryptophyl quinone 4-(S-cysteinyl)tryptophan-6,7-dione CROSSLNK 4'-cysteinyl-tryptophylquinone (Cys-Trp) CTQ cysteine tryptophylquinone A protein modification that effectively cross-links an L-cysteine residue and an L-aspartic acid residue by a thioether bond to form 2-(S-L-cysteinyl)-L-aspartic acid. -2.02 C 0 H -2 N 0 O 0 S 0 -2.01565 C 7 H 8 N 2 O 4 S 1 216.21 216.02048 C, D natural uniprot.ptm:PTM-0025 (2R,3S)-2-amino-3-([(2R)-2-amino-2-carboxyethyl]sulfanyl)butanedioic acid (2R,3S,6R)-2,6-diamino-3-carboxy-4-thiaheptanedioic acid 3-(L-cystein-S-yl)-L-aspartic acid 3-carboxy-L-lanthionine CROSSLNK 3-cysteinyl-aspartic acid (Cys-Asp) PSI-MOD MOD:00319 Cross-link 2. 3-(S-L-cysteinyl)-L-aspartic acid A protein modification that effectively cross-links an L-cysteine residue and an L-aspartic acid residue by a thioether bond to form 2-(S-L-cysteinyl)-L-aspartic acid. PubMed:11555656 PubMed:11717396 RESID:AA0314 (2R,3S)-2-amino-3-([(2R)-2-amino-2-carboxyethyl]sulfanyl)butanedioic acid (2R,3S,6R)-2,6-diamino-3-carboxy-4-thiaheptanedioic acid 3-(L-cystein-S-yl)-L-aspartic acid 3-carboxy-L-lanthionine CROSSLNK 3-cysteinyl-aspartic acid (Cys-Asp) A protein modification that effectively cross-links an L-cysteine residue and an L-glutamic acid residue by a thioether bond to form 4-(S-L-cysteinyl)-L-glutamic acid. -2.02 C 0 H -2 N 0 O 0 S 0 -2.01565 C 8 H 10 N 2 O 4 S 1 230.24 230.03613 C, E natural uniprot.ptm:PTM-0040 (2S,3S,7R)-2,7-diamino-4-carboxy-5-thiaoctanedioic acid (2S,4S)-2-amino-4-[(R)-2-amino-2-carboxyethyl]sulfanylpentanedioic acid 4-(L-cystein-S-yl)-L-glutamic acid CROSSLNK 4-cysteinyl-glutamic acid (Cys-Glu) PSI-MOD MOD:00320 Cross-link 2. 4-(S-L-cysteinyl)-L-glutamic acid A protein modification that effectively cross-links an L-cysteine residue and an L-glutamic acid residue by a thioether bond to form 4-(S-L-cysteinyl)-L-glutamic acid. ChEBI:20293 PubMed:11555656 PubMed:11717396 RESID:AA0315 (2S,3S,7R)-2,7-diamino-4-carboxy-5-thiaoctanedioic acid (2S,4S)-2-amino-4-[(R)-2-amino-2-carboxyethyl]sulfanylpentanedioic acid 4-(L-cystein-S-yl)-L-glutamic acid CROSSLNK 4-cysteinyl-glutamic acid (Cys-Glu) A protein modification that effectively converts an L-aspartic acid residue to cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid L-aspartate ester. 294.39 C 17 H 26 N 0 O 4 294.1831 C 21 H 31 N 1 O 7 409.48 409.21005 D natural Unimod:434 uniprot.ptm:PTM-0091 (7Z,14Xi)-14-[(S)-3-amino-3-carboxy-propanoyl]oxy-10,13-dioxo-7-heptadecenoic acid LIPID Cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid aspartate ester barley lipid transfer protein modification cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid L-aspartate ester PSI-MOD CHDH cis-14-hydroxy-10,13-dioxo-7-heptadecenoic ester MOD:00321 cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid L-aspartate ester A protein modification that effectively converts an L-aspartic acid residue to cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid L-aspartate ester. PubMed:11435437 PubMed:7949339 RESID:AA0316 Unimod:434#D (7Z,14Xi)-14-[(S)-3-amino-3-carboxy-propanoyl]oxy-10,13-dioxo-7-heptadecenoic acid LIPID Cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid aspartate ester barley lipid transfer protein modification cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid L-aspartate ester CHDH cis-14-hydroxy-10,13-dioxo-7-heptadecenoic ester A protein modification that effectively converts an L-histidine residue to tele-methyl-L-histidine. 14.03 C 1 H 2 N 0 O 0 14.01565 C 7 H 9 N 3 O 1 151.17 151.07455 H natural uniprot.ptm:PTM-0290 (S)-2-amino-3-(1-methyl-1H-imidazol-4-yl)propanoic acid 1'-methyl-L-histidine MOD_RES Tele-methylhistidine N(epsilon)-methylhistidine N(tau)-methylhistidine NteleMeHis tele-methylated L-histidine tele-methylhistidine PSI-MOD 3-methylhistidine 4-methyl-histidine Methyl Methylation MOD:00322 1'-methyl-L-histidine A protein modification that effectively converts an L-histidine residue to tele-methyl-L-histidine. PubMed:10601317 PubMed:11474090 PubMed:11875433 PubMed:6692818 PubMed:8076 PubMed:8645219 RESID:AA0317 (S)-2-amino-3-(1-methyl-1H-imidazol-4-yl)propanoic acid 1'-methyl-L-histidine MOD_RES Tele-methylhistidine N(epsilon)-methylhistidine N(tau)-methylhistidine NteleMeHis tele-methylated L-histidine tele-methylhistidine 3-methylhistidine 4-methyl-histidine Methyl Methylation A protein modification that effectively converts an L-lysine residue to L-lysine methyl ester. 14.03 C 1 H 2 N 0 O 0 14.01565 C 7 H 15 N 2 O 2 159.21 159.11336 K natural C-term Unimod:34 uniprot.ptm:PTM-0170 2,6-diaminohexanoic methyl ester L-lysine methyl ester MOD_RES Lysine methyl ester OMeLys alpha,epsilon-diaminocaproic methyl ester methyl (S)-2,6-diaminohexanoate methyl L-lysinate methyl esterified L-lysine PSI-MOD Methyl Methylation MOD:00323 L-lysine methyl ester A protein modification that effectively converts an L-lysine residue to L-lysine methyl ester. PubMed:10973948 PubMed:11875433 RESID:AA0318 Unimod:34#C-term 2,6-diaminohexanoic methyl ester L-lysine methyl ester MOD_RES Lysine methyl ester OMeLys alpha,epsilon-diaminocaproic methyl ester methyl (S)-2,6-diaminohexanoate methyl L-lysinate methyl esterified L-lysine Methyl Methylation A protein modification that effectively converts an L-serine residue to L-serinyl molybdenum bis(molybdopterin guanine dinucleotide). 1588.01 C 40 H 47 Mo 1 N 20 O 27 P 4 S 4 1588.9807 C 43 H 52 Mo 1 N 21 O 29 P 4 S 4 1675.09 1676.0127 S natural 2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraazaanthracen-4-one guanosine dinucleotide L-serinyl molybdenum bis(molybdopterin guanine dinucleotide) bis[8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with guanosine)methyl-6-oxo-3,4-disulfanyl-pteridino[6,7-5,6]pyranoato-S3,S4]-O3-serinyl-molybdenum oxide PSI-MOD MOD:00324 L-serinyl molybdenum bis(molybdopterin guanine dinucleotide) A protein modification that effectively converts an L-serine residue to L-serinyl molybdenum bis(molybdopterin guanine dinucleotide). PubMed:8658132 PubMed:8658134 RESID:AA0319 2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraazaanthracen-4-one guanosine dinucleotide L-serinyl molybdenum bis(molybdopterin guanine dinucleotide) bis[8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with guanosine)methyl-6-oxo-3,4-disulfanyl-pteridino[6,7-5,6]pyranoato-S3,S4]-O3-serinyl-molybdenum oxide A protein modification that effectively converts an L-asparagine residue to L-beta-methylthioasparagine. 46.09 C 1 H 2 N 0 O 0 S 1 45.98772 C 5 H 8 N 2 O 2 S 1 160.19 160.03065 N hypothetical Unimod:39 (2R,3Xi)-2-amino-3-(methylsulfanyl)-4-butanediamic acid 2,4-diamino-3-(methylsulfanyl)-4-oxobutanoic acid 3-(methylthio)-L-asparagine 3-carboxamido-S-methyl-cysteine beta-(methylthio)asparagine PSI-MOD Beta-methylthiolation Methylthio MOD:00325 This modification was predicted for ribosomal protein S12 in Bacillus subtilis when the sequence in the original version of the genome was reported to have asparagine rather than aspartic acid at the position of the methylthioaspartic acid modification (see MOD:00237). Two groups independently confirmed that the genome sequence was incorrect. The sequence in the revised genome has aspartic acid at that position. This is a deprecated entry in RESID. It probably does not occur naturally [JSG]. L-beta-methylthioasparagine A protein modification that effectively converts an L-asparagine residue to L-beta-methylthioasparagine. RESID:AA0320 Unimod:39#N (2R,3Xi)-2-amino-3-(methylsulfanyl)-4-butanediamic acid 2,4-diamino-3-(methylsulfanyl)-4-oxobutanoic acid 3-(methylthio)-L-asparagine 3-carboxamido-S-methyl-cysteine beta-(methylthio)asparagine Beta-methylthiolation Methylthio A protein modification that effectively converts an L-lysine residue to L-pyrrolysine (not known as a natural, post-translational modification process). 109.13 C 6 H 7 N 1 O 1 109.052765 C 12 H 19 N 3 O 2 237.3 237.14772 K artifact Unimod:435 (2S)-2-amino-6-[(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-ylcarbonyl]aminohexanoic acid 2-azanyl-6-[(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-ylcarbonyl]azanylhexanoic acid L-pyrrolysine N6-(4-methyl-1,2-didehydropyrrolidine-5-carboxyl)-L-lysine N6-(4-methyl-delta-1-pyrroline-5-carboxyl)-L-lysine N6-([(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-yl]carbonyl)-L-lysine NON_STD Pyrrolysine Pyl(Lys) monomethylamine methyltransferase cofactor lysine adduct PSI-MOD MOD:00326 This entry is for the artifactual formation of L-pyrrolysine from lysine. For encoded L-pyrrolysine, use MOD:01187 [JSG]. L-pyrrolysine (Lys) A protein modification that effectively converts an L-lysine residue to L-pyrrolysine (not known as a natural, post-translational modification process). PubMed:11435424 PubMed:12029131 PubMed:12029132 PubMed:15314242 PubMed:16096277 RESID:AA0321#LYS Unimod:435#K (2S)-2-amino-6-[(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-ylcarbonyl]aminohexanoic acid 2-azanyl-6-[(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-ylcarbonyl]azanylhexanoic acid L-pyrrolysine N6-(4-methyl-1,2-didehydropyrrolidine-5-carboxyl)-L-lysine N6-(4-methyl-delta-1-pyrroline-5-carboxyl)-L-lysine N6-([(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-yl]carbonyl)-L-lysine NON_STD Pyrrolysine Pyl(Lys) monomethylamine methyltransferase cofactor lysine adduct A protein modification that effectively converts an L-tryptophan residue to a 3-hydroxy-L-tryptophan. 16.0 C 0 H 0 N 0 O 1 15.994915 C 11 H 10 N 2 O 2 202.21 202.07423 W hypothetical uniprot.ptm:PTM-0031 (2S,3S)-2-amino-3-hydroxy-3-(1H-indol-3-yl)propanoic acid 3-hydroxy-L-tryptophan 3-hydroxylated L-tryptophan 3-hydroxytryptophan 3HyTrp MOD_RES 3-hydroxytryptophan beta-hydroxytryptophan PSI-MOD MOD:00327 3-hydroxy-L-tryptophan A protein modification that effectively converts an L-tryptophan residue to a 3-hydroxy-L-tryptophan. ChEBI:141794 PubMed:10024453 PubMed:11457355 RESID:AA0322 (2S,3S)-2-amino-3-hydroxy-3-(1H-indol-3-yl)propanoic acid 3-hydroxy-L-tryptophan 3-hydroxylated L-tryptophan 3-hydroxytryptophan 3HyTrp MOD_RES 3-hydroxytryptophan beta-hydroxytryptophan A protein modification that effectively crosslinks an L-tyrosine residue and the 3'-end of DNA through a phosphodiester bond to form O4'-(phospho-3'-DNA)-L-tyrosine. Y natural (S)-2-amino-3-[4-(3'-deoxyribonucleic acid phosphonoxy)phenyl]propanoic acid ACT_SITE O-(3'-phospho-DNA)-tyrosine intermediate O4'-(phospho-3'-DNA)-L-tyrosine O4'-L-tyrosine 3'-DNA phosphodiester PSI-MOD MOD:00328 O4'-(phospho-3'-DNA)-L-tyrosine A protein modification that effectively crosslinks an L-tyrosine residue and the 3'-end of DNA through a phosphodiester bond to form O4'-(phospho-3'-DNA)-L-tyrosine. PubMed:2211714 RESID:AA0323 (S)-2-amino-3-[4-(3'-deoxyribonucleic acid phosphonoxy)phenyl]propanoic acid ACT_SITE O-(3'-phospho-DNA)-tyrosine intermediate O4'-(phospho-3'-DNA)-L-tyrosine O4'-L-tyrosine 3'-DNA phosphodiester A protein modification that effectively results from forming an adduct between a glutamic acid residue and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. 614.48 C 34 Fe 1 H 30 N 4 O 4 614.1616 C 39 Fe 1 H 37 N 5 O 7 743.6 743.2042 E natural Unimod:436 5-hydroxymethyl protoporphyrin IX 5-glutamate ester BINDING Heme (covalent; via 1 link) [3-[(S)-(4-amino-4-carboxy)butanoyloxymethyl]-7,12-diethenyl-8,13,17-trimethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate cytochrome P450 CYP4A family heme cofactor hydroxyheme-L-glutamate ester PSI-MOD Hydroxyheme hydroxyheme MOD:00329 hydroxyheme-L-glutamate ester A protein modification that effectively results from forming an adduct between a glutamic acid residue and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. PubMed:11139583 PubMed:11821421 PubMed:11980497 RESID:AA0324 Unimod:436#E 5-hydroxymethyl protoporphyrin IX 5-glutamate ester BINDING Heme (covalent; via 1 link) [3-[(S)-(4-amino-4-carboxy)butanoyloxymethyl]-7,12-diethenyl-8,13,17-trimethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate cytochrome P450 CYP4A family heme cofactor hydroxyheme-L-glutamate ester Hydroxyheme hydroxyheme A protein modification that effectively converts an L-histidine residue to a (phospho-5'-guanosine)-L-histidine. 345.21 C 10 H 12 N 5 O 7 P 1 345.04742 C 16 H 19 N 8 O 8 P 1 482.35 482.10635 H natural Unimod:413 (2S)-2-amino-3-(1-(5'-adenosine phosphono)imidazol-4-yl)propanoic acid 1'-(phospho-5'-guanosine)-L-histidine ACT_SITE GMP-histidine intermediate L-histidine 5'-guanosine phosphoramidester L-histidine monoanhydride with 5'-guanylic acid N(tau)-5'-guanylic-L-histidine N1'-guanylylated histidine tele-5'-guanylic-L-histidine PSI-MOD Phosphoguanosine phospho-guanosine MOD:00330 (phospho-5'-guanosine)-L-histidine A protein modification that effectively converts an L-histidine residue to a (phospho-5'-guanosine)-L-histidine. PubMed:10529169 PubMed:10869342 PubMed:7559521 RESID:AA0325 Unimod:413#H (2S)-2-amino-3-(1-(5'-adenosine phosphono)imidazol-4-yl)propanoic acid 1'-(phospho-5'-guanosine)-L-histidine ACT_SITE GMP-histidine intermediate L-histidine 5'-guanosine phosphoramidester L-histidine monoanhydride with 5'-guanylic acid N(tau)-5'-guanylic-L-histidine N1'-guanylylated histidine tele-5'-guanylic-L-histidine Phosphoguanosine phospho-guanosine A protein modification that effectively converts four L-cysteine residues and a three-iron four-sulfur cluster to tetrakis-L-cysteinyl triiron tetrasulfide. 291.74 C 0 Fe 3 H -4 N 0 O 0 S 4 291.66345 3- C 12 Fe 3 H 16 N 4 O 4 S 8 704.3 703.7002 C, C, C, C hypothetical bis[bis-L-cysteinyl iron disulfido]iron di-mu-1:2kappaS-sulfido di-mu-2:3kappaS-sulfido iron bis(bis-S-cysteinyliron) tetra-mu-sulfido tetrakis-S-L-cysteinyl triiron tetrakis-L-cysteinyl linear [3Fe-4S] cluster tetrakis-L-cysteinyl triiron tetrasulfide tetrakis-L-cysteinyl triiron tetrasulfide D2 cluster PSI-MOD MOD:00331 Cross-link 4. tetrakis-L-cysteinyl triiron tetrasulfide A protein modification that effectively converts four L-cysteine residues and a three-iron four-sulfur cluster to tetrakis-L-cysteinyl triiron tetrasulfide. PubMed:11592901 PubMed:11941493 PubMed:2511202 PubMed:6094558 RESID:AA0326 bis[bis-L-cysteinyl iron disulfido]iron di-mu-1:2kappaS-sulfido di-mu-2:3kappaS-sulfido iron bis(bis-S-cysteinyliron) tetra-mu-sulfido tetrakis-S-L-cysteinyl triiron tetrakis-L-cysteinyl linear [3Fe-4S] cluster tetrakis-L-cysteinyl triiron tetrasulfide tetrakis-L-cysteinyl triiron tetrasulfide D2 cluster A protein modification that effectively converts an L-arginine residue to N4-glucosyl-arginine. 162.14 C 6 H 10 N 0 O 5 162.05283 C 12 H 22 N 4 O 6 318.33 318.15393 R natural Unimod:41 uniprot.ptm:PTM-0515 (2S)-2-amino-5-(beta-D-glucopyranosyl[imino(methylamino)methyl]amino)pentanoic acid CARBOHYD N-linked (Glc) arginine NG-beta-D-glucosylarginine omega-N-(beta-D-glucosyl)-L-arginine omega-N-glucosyl-L-arginine omega-N-glycosyl-L-arginine PSI-MOD Hex Hexose MOD:00332 omega-N-glucosyl-L-arginine A protein modification that effectively converts an L-arginine residue to N4-glucosyl-arginine. PubMed:15279557 PubMed:8521968 PubMed:9536051 RESID:AA0327 Unimod:41#R (2S)-2-amino-5-(beta-D-glucopyranosyl[imino(methylamino)methyl]amino)pentanoic acid CARBOHYD N-linked (Glc) arginine NG-beta-D-glucosylarginine omega-N-(beta-D-glucosyl)-L-arginine omega-N-glucosyl-L-arginine omega-N-glycosyl-L-arginine Hex Hexose A protein modification that effectively converts an L-asparagine residue to (3-aminopropyl)(L-aspartyl-1-amino)phosphoryl-5'-adenosine. 386.3 C 13 H 19 N 6 O 6 P 1 386.11038 C 17 H 26 N 8 O 9 P 1 517.42 517.156 N natural C-term Unimod:437 uniprot.ptm:PTM-0335 (3-aminopropyl)(L-aspartyl-1-amino)phosphoryl-5'-adenosine 5'-O-[(3-aminopropoxy)(L-aspart-1-ylamino)phosphoryl]adenosine 9-(5'-O-[(3-aminopropoxy)(L-aspart-1-ylamino)phosphoryl]-beta-D-ribofuranosyl)adenine MOD_RES Aspartic acid 1-[(3-aminopropyl)(5'-adenosyl)phosphono]amide N-(aspart-1-yl)-O-(3-aminopropyl)-O-(5'-adenosyl)phosphoramide microcin C7 asparagine modification PSI-MOD (3-aminopropyl)(L-aspartyl-1-amino)phosphoryl-5-adenosine C-Asn-deriv MOD:00333 Unimod origin shown as C-term [JSG]. (3-aminopropyl)(L-aspartyl-1-amino)phosphoryl-5'-adenosine A protein modification that effectively converts an L-asparagine residue to (3-aminopropyl)(L-aspartyl-1-amino)phosphoryl-5'-adenosine. PubMed:7559516 PubMed:7835418 PubMed:8183363 RESID:AA0328 Unimod:437#C-term (3-aminopropyl)(L-aspartyl-1-amino)phosphoryl-5'-adenosine 5'-O-[(3-aminopropoxy)(L-aspart-1-ylamino)phosphoryl]adenosine 9-(5'-O-[(3-aminopropoxy)(L-aspart-1-ylamino)phosphoryl]-beta-D-ribofuranosyl)adenine MOD_RES Aspartic acid 1-[(3-aminopropyl)(5'-adenosyl)phosphono]amide N-(aspart-1-yl)-O-(3-aminopropyl)-O-(5'-adenosyl)phosphoramide microcin C7 asparagine modification (3-aminopropyl)(L-aspartyl-1-amino)phosphoryl-5-adenosine C-Asn-deriv A protein modification that effectively results from forming an adduct between the tele nitrogen of a histidine residue and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. 616.5 C 34 Fe 1 H 32 N 4 O 4 616.1773 C 40 Fe 1 H 39 N 7 O 5 753.64 753.2362 H hypothetical Unimod:390 (S)-[7-ethenyl-12-[1-((2-amino-2-carboxyethyl)-1H-imidazol-1-yl)ethyl]-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate 1'-heme-L-histidine 2-[1-(N1'-histidyl)ethyl]protoporphyrin IX BINDING Heme (covalent; via tele nitrogen) N(epsilon)-histidyl heme N(tau)-histidyl heme N1'-histidyl heme tele-histidyl heme PSI-MOD Heme heme MOD:00334 1'-heme-L-histidine A protein modification that effectively results from forming an adduct between the tele nitrogen of a histidine residue and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron. PubMed:12033922 PubMed:12121092 RESID:AA0329 Unimod:390#H (S)-[7-ethenyl-12-[1-((2-amino-2-carboxyethyl)-1H-imidazol-1-yl)ethyl]-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate 1'-heme-L-histidine 2-[1-(N1'-histidyl)ethyl]protoporphyrin IX BINDING Heme (covalent; via tele nitrogen) N(epsilon)-histidyl heme N(tau)-histidyl heme N1'-histidyl heme tele-histidyl heme Heme heme A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form (2S,3S,2'R)-3-methyllanthionine sulfoxide. -2.02 C 0 H -2 N 0 O 0 S 0 -2.01565 C 7 H 10 N 2 O 3 S 1 202.23 202.04121 C, T natural uniprot.ptm:PTM-0069 (2S,3S,4Xi,6R)-2,6-diamino-3-methyl-4-oxo-4-thiaheptanedioic acid (2S,3S,SXi)-2-amino-3-([(R)-2-amino-2-carboxyethyl]sulfinyl)butanoic acid 3-methyl-L-lanthionine S-oxide 3-methyl-L-lanthionine sulfoxide CROSSLNK Beta-methyllanthionine sulfoxide (Thr-Cys) S-oxy-3-methyllanthionine PSI-MOD MOD:00335 Cross-link 2. (2S,3S,2'R)-3-methyllanthionine sulfoxide A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form (2S,3S,2'R)-3-methyllanthionine sulfoxide. PubMed:7737178 PubMed:9219543 RESID:AA0330 (2S,3S,4Xi,6R)-2,6-diamino-3-methyl-4-oxo-4-thiaheptanedioic acid (2S,3S,SXi)-2-amino-3-([(R)-2-amino-2-carboxyethyl]sulfinyl)butanoic acid 3-methyl-L-lanthionine S-oxide 3-methyl-L-lanthionine sulfoxide CROSSLNK Beta-methyllanthionine sulfoxide (Thr-Cys) S-oxy-3-methyllanthionine A protein modification that effectively converts three L-cysteine residues, an L-aspartic acid residue and a two-iron two-sulfur cluster to tris-L-cysteinyl L-aspartato diiron disulfide. 171.78 C 0 Fe 2 H -4 N 0 O 0 S 2 171.78381 2- C 13 Fe 2 H 16 N 4 O 6 S 5 596.28 595.8383 C, C, C, D hypothetical METAL Iron-sulfur (2Fe-2S) di-mu-sulfido(bis-S-cysteinyliron)(S-cysteinyl-O4-aspartatoiron) tris-L-cysteinyl L-aspartato diiron disulfide PSI-MOD MOD:00336 Cross-link 4. tris-L-cysteinyl L-aspartato diiron disulfide A protein modification that effectively converts three L-cysteine residues, an L-aspartic acid residue and a two-iron two-sulfur cluster to tris-L-cysteinyl L-aspartato diiron disulfide. PubMed:10968624 PubMed:1312028 PubMed:7947772 RESID:AA0331 METAL Iron-sulfur (2Fe-2S) di-mu-sulfido(bis-S-cysteinyliron)(S-cysteinyl-O4-aspartatoiron) tris-L-cysteinyl L-aspartato diiron disulfide A protein modification that effectively converts an L-cysteine residue to S-carbamoyl-L-cysteine. 43.02 C 1 H 1 N 1 O 1 S 0 43.005814 C 4 H 6 N 2 O 2 S 1 146.16 146.015 C natural Unimod:5 uniprot.ptm:PTM-0649 (R)-2-amino-3-(carbamoylsulfanyl)propanoic acid 2-amino-3-(aminocarbonyl)sulfanylpropanoic acid 2-amino-3-(aminocarbonyl)thiopropanoic acid MOD_RES S-carbamoylcysteine S-(aminocarbonyl)cysteine S-carbamoyl-L-cysteine S-carbamoylcysteine S-carbamylcysteine S-cysteinyl carbamate ester SCbmCys alpha-amino-beta-carbamylthiopropionic acid beta-carbamylthioalanine PSI-MOD MOD:00337 S-carbamoyl-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-carbamoyl-L-cysteine. PubMed:12586941 PubMed:240389 RESID:AA0332 Unimod:5#C (R)-2-amino-3-(carbamoylsulfanyl)propanoic acid 2-amino-3-(aminocarbonyl)sulfanylpropanoic acid 2-amino-3-(aminocarbonyl)thiopropanoic acid MOD_RES S-carbamoylcysteine S-(aminocarbonyl)cysteine S-carbamoyl-L-cysteine S-carbamoylcysteine S-carbamylcysteine S-cysteinyl carbamate ester SCbmCys alpha-amino-beta-carbamylthiopropionic acid beta-carbamylthioalanine A protein modification that effectively converts an L-cysteine residue to S-cyano-L-cysteine. 25.01 C 1 H -1 N 1 O 0 S 0 24.995249 C 4 H 4 N 2 O 1 S 1 128.15 128.00444 C natural Unimod:438 uniprot.ptm:PTM-0650 (2R)-2-amino-3-thiocyanatopropanoic acid MOD_RES S-cyanocysteine S-cyano-L-cysteine S-cyanocysteine alpha-amino-beta-thiocyanatopropionic acid beta-thiocyanatoalanine serine thiocyanic acid ester PSI-MOD Cyano cyano MOD:00338 S-cyano-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-cyano-L-cysteine. PubMed:12586941 PubMed:4808702 RESID:AA0333 Unimod:438#C (2R)-2-amino-3-thiocyanatopropanoic acid MOD_RES S-cyanocysteine S-cyano-L-cysteine S-cyanocysteine alpha-amino-beta-thiocyanatopropionic acid beta-thiocyanatoalanine serine thiocyanic acid ester Cyano cyano A protein modification that effectively converts an L-cysteine residue to L-cysteinyl hydrogenase diiron subcluster. 342.87 C 5 Fe 2 H -1 N 2 O 5 S 2 342.78693 C 8 Fe 2 H 4 N 3 O 6 S 3 446.01 445.7961 C natural Unimod:439 1,7-biscarbonyl-1-(cystein-S-yl)-8-oxo-4-aza-2lambda(3),6 lambda(3)-dithia-1,7-diferratricyclo[4.2.0.0(2,7)]octane-1,7-dicarbonitrile L-cysteinyl hydrogenase diiron subcluster METAL Diiron subcluster mu-carbonyl-dicarbonyl-1kappaC,2kappaC-dicyanido-1kappaC,2kappaC-cysteinato-1kS-1,2-azadimethanthiol-1kS,2kS'-diiron PSI-MOD Diironsubcluster hydrogenase diiron subcluster MOD:00339 incidental to RESID:AA0140. L-cysteinyl hydrogenase diiron subcluster A protein modification that effectively converts an L-cysteine residue to L-cysteinyl hydrogenase diiron subcluster. PubMed:10694885 PubMed:9836629 RESID:AA0334 Unimod:439#C 1,7-biscarbonyl-1-(cystein-S-yl)-8-oxo-4-aza-2lambda(3),6 lambda(3)-dithia-1,7-diferratricyclo[4.2.0.0(2,7)]octane-1,7-dicarbonitrile L-cysteinyl hydrogenase diiron subcluster METAL Diiron subcluster mu-carbonyl-dicarbonyl-1kappaC,2kappaC-dicyanido-1kappaC,2kappaC-cysteinato-1kS-1,2-azadimethanthiol-1kS,2kS'-diiron Diironsubcluster hydrogenase diiron subcluster A protein modification that effectively converts an L-cysteine residue to S-amidino-L-cysteine. 42.04 C 1 H 2 N 2 O 0 S 0 42.021797 C 4 H 7 N 3 O 1 S 1 145.18 145.03099 C natural Unimod:440 (2R)-2-amino-3-(carbamimidoylsulfanyl)propanoic acid 2-amino-3-amidinosulfanylpropanoic acid 2-amino-3-amidinothiopropanoic acid ACT_SITE Amidino-cysteine intermediate S-amidino-L-cysteine S-amidinocysteine alpha-amino-beta-amidinothiopropionic acid beta-(S-isothiourea)alanine beta-amidinothioalanine PSI-MOD Amidino amidino MOD:00340 S-amidino-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-amidino-L-cysteine. PubMed:9148748 RESID:AA0335 Unimod:440#C (2R)-2-amino-3-(carbamimidoylsulfanyl)propanoic acid 2-amino-3-amidinosulfanylpropanoic acid 2-amino-3-amidinothiopropanoic acid ACT_SITE Amidino-cysteine intermediate S-amidino-L-cysteine S-amidinocysteine alpha-amino-beta-amidinothiopropionic acid beta-(S-isothiourea)alanine beta-amidinothioalanine Amidino amidino A protein modification that effectively converts an L-isoleucine residue to N-methyl-L-isoleucine. 14.03 C 1 H 2 N 0 O 0 14.01565 C 7 H 13 N 1 O 1 127.19 127.09972 I hypothetical uniprot.ptm:PTM-0215 (2S,3S)-2-methylamino-3-methylpentanoic acid MOD_RES N-methylisoleucine N-methyl-L-isoleucine N-methylated L-isoleucine N-methylisoleucine NMe1Ile PSI-MOD Methyl Methylation MOD:00341 Polypeptides with monomethylated amino terminals can undergo premature cleavage during the coupling step of an Edman degradation. This can result in "preview" with both a residue and the following residue being seen from the first step on through a sequence [JSG]. N-methyl-L-isoleucine A protein modification that effectively converts an L-isoleucine residue to N-methyl-L-isoleucine. PubMed:11875433 RESID:AA0336 (2S,3S)-2-methylamino-3-methylpentanoic acid MOD_RES N-methylisoleucine N-methyl-L-isoleucine N-methylated L-isoleucine N-methylisoleucine NMe1Ile Methyl Methylation A protein modification that effectively converts an L-leucine residue to N-methyl-L-leucine. 14.03 C 1 H 2 N 0 O 0 14.01565 C 7 H 13 N 1 O 1 127.19 127.09972 L hypothetical uniprot.ptm:PTM-0216 (S)-2-methylamino-4-methylpentanoic acid 2-(methylamino)-4-methyl-valeric acid MOD_RES N-methylleucine N-methyl-L-leucine N-methylated L-leucine N-methylleucine NMe1Leu PSI-MOD Methyl Methylation MOD:00342 Polypeptides with monomethylated amino terminals can undergo premature cleavage during the coupling step of an Edman degradation. This can result in "preview" with both a residue and the following residue being seen from the first step on through a sequence [JSG]. N-methyl-L-leucine A protein modification that effectively converts an L-leucine residue to N-methyl-L-leucine. PubMed:11875433 RESID:AA0337 (S)-2-methylamino-4-methylpentanoic acid 2-(methylamino)-4-methyl-valeric acid MOD_RES N-methylleucine N-methyl-L-leucine N-methylated L-leucine N-methylleucine NMe1Leu Methyl Methylation A protein modification that effectively converts an L-tyrosine residue to N-methyl-L-tyrosine. 14.03 C 1 H 2 N 0 O 0 14.01565 C 10 H 11 N 1 O 2 177.2 177.07898 Y hypothetical uniprot.ptm:PTM-0220 (2S)-3-(4-hydroxyphenyl)-2-(methylamino)propanoic acid MOD_RES N-methyltyrosine N-methyl Tyrosinyl N-methyl-L-tyrosine N-methylated L-tyrosine N-methyltyrosine NMe1Tyr PSI-MOD Methyl MOD:00343 Polypeptides with monomethylated amino terminals can undergo premature cleavage during the coupling step of an Edman degradation. This can result in "preview" with both a residue and the following residue being seen from the first step on through a sequence [JSG]. N-methyl-L-tyrosine A protein modification that effectively converts an L-tyrosine residue to N-methyl-L-tyrosine. DeltaMass:0 RESID:AA0338 (2S)-3-(4-hydroxyphenyl)-2-(methylamino)propanoic acid MOD_RES N-methyltyrosine N-methyl Tyrosinyl N-methyl-L-tyrosine N-methylated L-tyrosine N-methyltyrosine NMe1Tyr Methyl A protein modification that effectively converts a glycine residue to N-palmitoylglycine. 238.41 C 16 H 30 N 0 O 1 S 0 238.22966 C 18 H 34 N 1 O 2 296.47 296.25894 G natural N-term uniprot.ptm:PTM-0223 (hexadecanamido)acetic acid (hexadecanoylamino)acetic acid (hexadecanoylamino)ethanoic acid LIPID N-palmitoyl glycine N-(1-oxohexadecyl)glycine N-hexadecanoylated glycine N-palmitoyl-glycine N-palmitoylated glycine NPamGly PSI-MOD MOD:00344 incidental to RESID:AA0060 N-palmitoylglycine A protein modification that effectively converts a glycine residue to N-palmitoylglycine. PubMed:12574119 RESID:AA0339 (hexadecanamido)acetic acid (hexadecanoylamino)acetic acid (hexadecanoylamino)ethanoic acid LIPID N-palmitoyl glycine N-(1-oxohexadecyl)glycine N-hexadecanoylated glycine N-palmitoyl-glycine N-palmitoylated glycine NPamGly A protein modification that effectively cross-links an L-cysteine residue and an L-phenylalanine residue by a thioether bond to form 2-(S-L-cysteinyl)-L-phenylalanine. -2.02 C 0 H -2 N 0 O 0 S 0 -2.01565 C 12 H 12 N 2 O 2 S 1 248.3 248.06195 C, F natural uniprot.ptm:PTM-0012 (2R)-2-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-3-phenylpropanoic acid (2R,5R)-2,5-diamino-3-thia-2-phenylmethylhexanedioic acid 2-(L-cystein-S-yl)-L-phenylalanine CROSSLNK 2-cysteinyl-L-phenylalanine (Cys-Phe) alpha-(L-cystein-S-yl)-L-phenylalanine PSI-MOD MOD:00345 Cross-link 2. 2-(S-L-cysteinyl)-L-phenylalanine A protein modification that effectively cross-links an L-cysteine residue and an L-phenylalanine residue by a thioether bond to form 2-(S-L-cysteinyl)-L-phenylalanine. PubMed:12696888 PubMed:3936839 RESID:AA0340 (2R)-2-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-3-phenylpropanoic acid (2R,5R)-2,5-diamino-3-thia-2-phenylmethylhexanedioic acid 2-(L-cystein-S-yl)-L-phenylalanine CROSSLNK 2-cysteinyl-L-phenylalanine (Cys-Phe) alpha-(L-cystein-S-yl)-L-phenylalanine A protein modification that effectively cross-links an L-cysteine residue and an L-phenylalanine residue by a thioether bond to form 2-(S-L-cysteinyl)-D-phenylalanine. -2.02 C 0 H -2 N 0 O 0 S 0 -2.01565 C 12 H 12 N 2 O 2 S 1 248.3 248.06195 C, F natural uniprot.ptm:PTM-0011 (2S)-2-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-3-phenylpropanoic acid (2S,5R)-2,5-diamino-3-thia-2-phenylmethylhexanedioic acid 2-(L-cystein-S-yl)-D-phenylalanine CROSSLNK 2-cysteinyl-D-phenylalanine (Cys-Phe) alpha-(L-cystein-S-yl)-D-phenylalanine PSI-MOD MOD:00346 Cross-link 2. 2-(S-L-cysteinyl)-D-phenylalanine A protein modification that effectively cross-links an L-cysteine residue and an L-phenylalanine residue by a thioether bond to form 2-(S-L-cysteinyl)-D-phenylalanine. PubMed:12696888 PubMed:3936839 RESID:AA0341 (2S)-2-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-3-phenylpropanoic acid (2S,5R)-2,5-diamino-3-thia-2-phenylmethylhexanedioic acid 2-(L-cystein-S-yl)-D-phenylalanine CROSSLNK 2-cysteinyl-D-phenylalanine (Cys-Phe) alpha-(L-cystein-S-yl)-D-phenylalanine A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form 2-(S-L-cysteinyl)-D-allo-threonine. -2.02 C 0 H -2 N 0 O 0 S 0 -2.01565 C 7 H 10 N 2 O 3 S 1 202.23 202.04121 C, T natural uniprot.ptm:PTM-0010 (2R,5S,6R)-2,5-diamino-5-carboxy-6-hydroxy-4-thiaheptanoic acid (2S,3R)-2-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-3-hydroxybutanoic acid 2-(L-cystein-S-yl)-D-allo-threonine CROSSLNK 2-cysteinyl-D-allo-threonine (Cys-Thr) alpha-(L-cystein-S-yl)-D-allo-threonine PSI-MOD MOD:00347 Cross-link 2. 2-(S-L-cysteinyl)-D-allo-threonine A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form 2-(S-L-cysteinyl)-D-allo-threonine. PubMed:12696888 PubMed:3936839 RESID:AA0342 (2R,5S,6R)-2,5-diamino-5-carboxy-6-hydroxy-4-thiaheptanoic acid (2S,3R)-2-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-3-hydroxybutanoic acid 2-(L-cystein-S-yl)-D-allo-threonine CROSSLNK 2-cysteinyl-D-allo-threonine (Cys-Thr) alpha-(L-cystein-S-yl)-D-allo-threonine A protein modification that effectively converts an L-alanine residue to N-carbamoyl-L-alanine. 43.02 C 1 H 1 N 1 O 1 43.005814 C 4 H 7 N 2 O 2 115.11 115.05075 A natural N-term uniprot.ptm:PTM-0374 (S)-2-(carbamoylamino)propanoic acid 2-ureidopropanoic acid MOD_RES N-carbamoylalanine N-carbamoyl-L-alanine N-carbamylalanine N2CbmAla PSI-MOD MOD:00348 N-carbamoyl-L-alanine A protein modification that effectively converts an L-alanine residue to N-carbamoyl-L-alanine. PubMed:12203680 RESID:AA0343 (S)-2-(carbamoylamino)propanoic acid 2-ureidopropanoic acid MOD_RES N-carbamoylalanine N-carbamoyl-L-alanine N-carbamylalanine N2CbmAla A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form 4-amino-3-isothiazolidinone-L-serine. -2.02 C 0 H -2 N 0 O 0 S 0 -2.01565 C 6 H 8 N 2 O 3 S 1 188.2 188.02556 C, S natural uniprot.ptm:PTM-0037 (2S)-2-[(4R)-4-amino-3-oxo-1,2-thiazolidin-2-yl]-3-hydroxypropanoic acid 2-(4-amino-3-oxo-isothiazolidin-2-yl)-3-hydroxy-propanoic acid 4-amino-3-isothiazolidinone-L-serine CROSSLNK N,N-(cysteine-1,S-diyl)serine (Cys-Ser) N,N-(L-cysteine-1,S-diyl)-L-serine serine-cysteine sulfenyl amide cross-link serine-cysteine sulphenyl amide cross-link PSI-MOD MOD:00349 Cross-link 2. 4-amino-3-isothiazolidinone-L-serine A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form 4-amino-3-isothiazolidinone-L-serine. PubMed:12802338 PubMed:12802339 RESID:AA0344 (2S)-2-[(4R)-4-amino-3-oxo-1,2-thiazolidin-2-yl]-3-hydroxypropanoic acid 2-(4-amino-3-oxo-isothiazolidin-2-yl)-3-hydroxy-propanoic acid 4-amino-3-isothiazolidinone-L-serine CROSSLNK N,N-(cysteine-1,S-diyl)serine (Cys-Ser) N,N-(L-cysteine-1,S-diyl)-L-serine serine-cysteine sulfenyl amide cross-link serine-cysteine sulphenyl amide cross-link A protein modification that effectively attaches an L-threonine residue to murein peptidoglycan by a pentaglycine linker peptide. T natural C-term uniprot.ptm:PTM-0246 (2R,6S)-2-(N-mureinyl-(R)-alanyl-(S)-isoglutamyl)amino-6-(threonyl-pentaglycyl)amino-pimeloyl-(S)-alanyl-(S)-alanine L-threonyl-pentaglycyl-murein peptidoglycan MOD_RES Pentaglycyl murein peptidoglycan amidated threonine PSI-MOD MOD:00350 L-threonyl-pentaglycyl-murein peptidoglycan A protein modification that effectively attaches an L-threonine residue to murein peptidoglycan by a pentaglycine linker peptide. PubMed:10754567 PubMed:1638631 RESID:AA0345 (2R,6S)-2-(N-mureinyl-(R)-alanyl-(S)-isoglutamyl)amino-6-(threonyl-pentaglycyl)amino-pimeloyl-(S)-alanyl-(S)-alanine L-threonyl-pentaglycyl-murein peptidoglycan MOD_RES Pentaglycyl murein peptidoglycan amidated threonine A protein modification that effectively converts a glycine residue to N-glycyl-1-(phosphatidyl)ethanolamine. 699.99 C 39 H 74 N 1 O 7 P 1 699.52026 C 41 H 78 N 2 O 9 P 1 774.05 773.5445 G natural C-term uniprot.ptm:PTM-0249 (R)-1-hexadecanoyloxy-2-((Z)-9-octadecenoyloxy)-3-[2-(aminoacetylamino)ethyloxyphospho]propane LIPID Phosphatidylethanolamine amidated glycine N-glycyl-1-(phosphatidyl)ethanolamine N-glycyl-1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine PSI-MOD MOD:00351 N-glycyl-1-(phosphatidyl)ethanolamine A protein modification that effectively converts a glycine residue to N-glycyl-1-(phosphatidyl)ethanolamine. PubMed:11100732 RESID:AA0346 (R)-1-hexadecanoyloxy-2-((Z)-9-octadecenoyloxy)-3-[2-(aminoacetylamino)ethyloxyphospho]propane LIPID Phosphatidylethanolamine amidated glycine N-glycyl-1-(phosphatidyl)ethanolamine N-glycyl-1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl 5-omega-hydroxyceramide ester. 761.31 C 50 H 96 N 0 O 4 760.73083 C 55 H 104 N 2 O 6 889.44 888.7894 Q natural uniprot.ptm:PTM-0236 (S)-2-amino-5-[30-((2S,3R,4E)-1,3-dihydroxyicos-4-en-2-ylamino)-30-oxotriacontan-1-yloxy]-5-oxopentanoic acid 2-[30-(isoglutamyloxy)triacontanoyl]icosasphingosine L-glutamyl 5-omega-hydroxyceramide ester LIPID Omega-hydroxyceramide glutamate ester PSI-MOD MOD:00352 L-glutamyl 5-omega-hydroxyceramide ester A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl 5-omega-hydroxyceramide ester. PubMed:10411887 PubMed:9651377 RESID:AA0347 (S)-2-amino-5-[30-((2S,3R,4E)-1,3-dihydroxyicos-4-en-2-ylamino)-30-oxotriacontan-1-yloxy]-5-oxopentanoic acid 2-[30-(isoglutamyloxy)triacontanoyl]icosasphingosine L-glutamyl 5-omega-hydroxyceramide ester LIPID Omega-hydroxyceramide glutamate ester A protein modification that effectively cross-links an L-tryptophan residue with an L-tyrosine residue by a carbon-carbon bond, and cross-links the L-tyrosine residue to an L-methionine residue by a thioether bond to form S-[5'-(L-tryptoph-6'-yl)-L-tyrosin-3'-yl]-L-methionin-S-ium. -3.02 C 0 H -3 N 0 O 0 S 0 -3.024024 1+ C 25 H 25 N 4 O 4 S 1 477.56 477.1591 M, W, Y natural uniprot.ptm:PTM-0328 5'-(6'-tryptophyl)-tyrosin-3'-yl-methionin-S-ium S-[5'-(L-tryptoph-6'-yl)-L-tyrosin-3'-yl]-L-methionin-S-ium PSI-MOD MOD:00353 Cross-link 3. S-[5'-(L-tryptoph-6'-yl)-L-tyrosin-3'-yl]-L-methionin-S-ium A protein modification that effectively cross-links an L-tryptophan residue with an L-tyrosine residue by a carbon-carbon bond, and cross-links the L-tyrosine residue to an L-methionine residue by a thioether bond to form S-[5'-(L-tryptoph-6'-yl)-L-tyrosin-3'-yl]-L-methionin-S-ium. PubMed:12172540 PubMed:16285713 RESID:AA0348 5'-(6'-tryptophyl)-tyrosin-3'-yl-methionin-S-ium S-[5'-(L-tryptoph-6'-yl)-L-tyrosin-3'-yl]-L-methionin-S-ium A protein modification that effectively converts an L-threonine residue to O-(riboflavin phosphoryl)-L-threonine. 438.33 C 17 H 19 N 4 O 8 P 1 438.09406 C 21 H 26 N 5 O 10 P 1 539.44 539.1417 T natural Unimod:442 uniprot.ptm:PTM-0126 (2S,3R)-2-amino-3-(riboflavin 5'-hydrogen phosphonoxy)butanoic acid MOD_RES FMN phosphoryl threonine O-(riboflavin phosphoryl)-L-threonine O3-threonyl FMN O3-threonyl flavin mononucleotide OFMNThr PSI-MOD FMN O3-(riboflavin phosphoryl) MOD:00354 O-(riboflavin phosphoryl)-L-threonine A protein modification that effectively converts an L-threonine residue to O-(riboflavin phosphoryl)-L-threonine. PubMed:10587447 PubMed:11163785 PubMed:11248234 RESID:AA0349 Unimod:442#T (2S,3R)-2-amino-3-(riboflavin 5'-hydrogen phosphonoxy)butanoic acid MOD_RES FMN phosphoryl threonine O-(riboflavin phosphoryl)-L-threonine O3-threonyl FMN O3-threonyl flavin mononucleotide OFMNThr FMN O3-(riboflavin phosphoryl) A protein modification that effectively converts an L-serine residue to O-(riboflavin phosphoryl)-L-serine. 438.33 C 17 H 19 N 4 O 8 P 1 438.09406 C 20 H 24 N 5 O 10 P 1 525.41 525.1261 S natural Unimod:442 uniprot.ptm:PTM-0125 (R)-2-amino-3-(riboflavin 5'-hydrogen phosphonoxy)propanoic acid MOD_RES FMN phosphoryl serine O-(riboflavin phosphoryl)-L-serine O3-seryl FMN O3-seryl flavin mononucleotide OFMNSer PSI-MOD FMN O3-(riboflavin phosphoryl) MOD:00355 O-(riboflavin phosphoryl)-L-serine A protein modification that effectively converts an L-serine residue to O-(riboflavin phosphoryl)-L-serine. RESID:AA0350 Unimod:442#S (R)-2-amino-3-(riboflavin 5'-hydrogen phosphonoxy)propanoic acid MOD_RES FMN phosphoryl serine O-(riboflavin phosphoryl)-L-serine O3-seryl FMN O3-seryl flavin mononucleotide OFMNSer FMN O3-(riboflavin phosphoryl) A protein modification that effectively converts an L-cysteine residue to S-(4a-FMN)-L-cysteine. 456.35 C 17 H 21 N 4 O 9 P 1 S 0 456.1046 C 20 H 26 N 5 O 10 P 1 S 1 559.49 559.1138 C natural Unimod:443 uniprot.ptm:PTM-0270 (R)-2-amino-3-(4a-riboflavin 5'-dihydrogen phosphate)sulfanylpropanoic acid 4a-(S-cysteinyl)FMN 4a-(S-cysteinyl)flavin mononucleotide MOD_RES S-4a-FMN cysteine S-(4a-FMN)-L-cysteine S4aFMNCys PSI-MOD FMNC S-(4a-FMN) MOD:00356 S-(4alpha-FMN)-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-(4a-FMN)-L-cysteine. PubMed:12668455 PubMed:12846567 PubMed:7692961 RESID:AA0351 Unimod:443#C (R)-2-amino-3-(4a-riboflavin 5'-dihydrogen phosphate)sulfanylpropanoic acid 4a-(S-cysteinyl)FMN 4a-(S-cysteinyl)flavin mononucleotide MOD_RES S-4a-FMN cysteine S-(4a-FMN)-L-cysteine S4aFMNCys FMNC S-(4a-FMN) A protein modification that effectively converts an L-histidine residue to 1'-(8alpha-FMN)-L-histidine. 454.33 C 17 H 19 N 4 O 9 P 1 454.08896 C 23 H 26 N 7 O 10 P 1 591.47 591.1479 H natural Unimod:409 uniprot.ptm:PTM-0289 (S)-2-amino-3-(1-[8alpha riboflavin 5'-dihydrogen phosphate]imidazol-4-yl)propanoic acid 1'-(8alpha-FMN)-L-histidine 8alpha-(N(epsilon)-histidyl)FMN 8alpha-(N1'-histidyl)FMN MOD_RES Tele-8alpha-FMN histidine N(tau)-(8alpha-FMN)-histidine Ntele8aFMNHis tele-(8alpha-FMN)-histidine PSI-MOD FMNH flavin mononucleotide MOD:00357 1'-(8alpha-FMN)-L-histidine A protein modification that effectively converts an L-histidine residue to 1'-(8alpha-FMN)-L-histidine. PubMed:11902668 PubMed:8611516 RESID:AA0352 Unimod:409#H (S)-2-amino-3-(1-[8alpha riboflavin 5'-dihydrogen phosphate]imidazol-4-yl)propanoic acid 1'-(8alpha-FMN)-L-histidine 8alpha-(N(epsilon)-histidyl)FMN 8alpha-(N1'-histidyl)FMN MOD_RES Tele-8alpha-FMN histidine N(tau)-(8alpha-FMN)-histidine Ntele8aFMNHis tele-(8alpha-FMN)-histidine FMNH flavin mononucleotide A protein modification that effectively converts an L-histidine residue to 3'-(8alpha-FMN)-L-histidine. 454.33 C 17 H 19 N 4 O 9 P 1 454.08896 C 23 H 26 N 7 O 10 P 1 591.47 591.1479 H hypothetical Unimod:409 (S)-2-amino-3-(3-[8alpha riboflavin 5'-dihydrogen phosphate]imidazol-4-yl)propanoic acid 3'-(8alpha-FMN)-L-histidine 8alpha-(N(delta)-histidyl)FMN 8alpha-(N3'-histidyl)FMN N(pi)-(8alpha-FMN)-histidine Npros8aFMNHis pros-(8alpha-FMN)-histidine PSI-MOD FMNH flavin mononucleotide MOD:00358 In a later publication, PubMed:19438211, the authors changed the enzyme activity, the connection from a histidine nitrogen to a cysteine sulfur, and the identity of the flavin from FMN to FAD. They now believe the modification is S-(8alpha-FAD)-L-cysteine, see MOD:00152. This is a deprecated entry in RESID. It probably does not occur naturally [JSG]. 3'-(8alpha-FMN)-L-histidine A protein modification that effectively converts an L-histidine residue to 3'-(8alpha-FMN)-L-histidine. PubMed:12417325 RESID:AA0353 Unimod:409#H (S)-2-amino-3-(3-[8alpha riboflavin 5'-dihydrogen phosphate]imidazol-4-yl)propanoic acid 3'-(8alpha-FMN)-L-histidine 8alpha-(N(delta)-histidyl)FMN 8alpha-(N3'-histidyl)FMN N(pi)-(8alpha-FMN)-histidine Npros8aFMNHis pros-(8alpha-FMN)-histidine FMNH flavin mononucleotide A protein modification that effectively converts an L-arginine residue to N2-acetyl-L-arginine. 42.04 C 2 H 2 N 0 O 1 42.010567 C 8 H 15 N 4 O 2 199.23 199.1195 R natural N-term uniprot.ptm:PTM-0180 (S)-2-acetamido-5-carbamimidamidopentanoic acid 2-acetamido-5-guanidinopentanoic acid 2-acetylamino-5-guanidinopentanoic acid AcArg MOD_RES N2-acetylarginine N(alpha)-acetylarginine N2-acetyl-L-arginine N2-acetylated L-arginine acetylarginine alpha-acetylamino-delta-guanidinovaleric acid PSI-MOD MOD:00359 N2-acetyl-L-arginine A protein modification that effectively converts an L-arginine residue to N2-acetyl-L-arginine. PubMed:12883043 PubMed:1894641 RESID:AA0354 (S)-2-acetamido-5-carbamimidamidopentanoic acid 2-acetamido-5-guanidinopentanoic acid 2-acetylamino-5-guanidinopentanoic acid AcArg MOD_RES N2-acetylarginine N(alpha)-acetylarginine N2-acetyl-L-arginine N2-acetylated L-arginine acetylarginine alpha-acetylamino-delta-guanidinovaleric acid A protein modification that effectively converts an L-cysteine residue to L-cysteinyl copper sulfido molybdopterin cytosine dinuncleotide. 922.07 C 19 Cu 1 H 24 Mo 1 N 8 O 15 P 2 S 3 922.83484 C 22 Cu 1 H 29 Mo 1 N 9 O 16 P 2 S 4 1025.2 1025.844 C natural Unimod:444 L-cysteinyl copper sulfido molybdopterin cytosine dinucleotide [8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with cytosine)methyl-6-oxo-3,4-dimercapto-pteridino[6,7-5,6]pyranoato-S3,S4]-cysteinyl-S-copper-mu-sulfido-molybdenum hydroxide oxide cysteinyl copper mu-sulfido Mo-pterin cytosine dinucleotide PSI-MOD CuSMo copper sulfido molybdopterin cytosine dinuncleotide MOD:00360 L-cysteinyl copper sulfido molybdopterin cytosine dinuncleotide A protein modification that effectively converts an L-cysteine residue to L-cysteinyl copper sulfido molybdopterin cytosine dinuncleotide. PubMed:12475995 RESID:AA0355 Unimod:444#C L-cysteinyl copper sulfido molybdopterin cytosine dinucleotide [8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with cytosine)methyl-6-oxo-3,4-dimercapto-pteridino[6,7-5,6]pyranoato-S3,S4]-cysteinyl-S-copper-mu-sulfido-molybdenum hydroxide oxide cysteinyl copper mu-sulfido Mo-pterin cytosine dinucleotide CuSMo copper sulfido molybdopterin cytosine dinuncleotide A protein modification that effectively converts three L-cysteine residues, an S-adenosylmethionine and a four-iron four-sulfur cluster to tris-L-cysteinyl S-adenosylmethion-N,O-diyl tetrairon tetrasulfide. 747.03 C 15 Fe 4 H 19 N 6 O 5 S 5 746.7424 1- C 24 Fe 4 H 34 N 9 O 8 S 8 1056.45 1055.7699 C, C, C natural METAL Iron-sulfur (4Fe-4S-S-AdoMet) tetra-mu3-sulfido(S-adenosylmethion-N,O-diyliron)tris(S-cysteinyliron) tris-L-cysteinyl S-adenosylmethion-N,O-diyl tetrairon tetrasulfide PSI-MOD MOD:00361 Cross-link 3. tris-L-cysteinyl S-adenosylmethion-N,O-diyl tetrairon tetrasulfide A protein modification that effectively converts three L-cysteine residues, an S-adenosylmethionine and a four-iron four-sulfur cluster to tris-L-cysteinyl S-adenosylmethion-N,O-diyl tetrairon tetrasulfide. PubMed:11222759 PubMed:14704425 RESID:AA0356 METAL Iron-sulfur (4Fe-4S-S-AdoMet) tetra-mu3-sulfido(S-adenosylmethion-N,O-diyliron)tris(S-cysteinyliron) tris-L-cysteinyl S-adenosylmethion-N,O-diyl tetrairon tetrasulfide A protein modification that effectively converts three L-cysteine residues, an L-arginine residue and a two-iron two-sulfur cluster to tris-L-cysteinyl L-arginyl diiron disulfide. 172.79 C 0 Fe 2 H -3 N 0 O 0 S 2 172.79164 2- C 15 Fe 2 H 24 N 7 O 4 S 5 638.39 637.9203 C, C, C, R natural METAL Iron-sulfur (2Fe-2S) di-mu-sulfido(N(eta1)-arginyl-S-cysteinyliron)(bis-S-cysteinyliron) tris-L-cysteinyl L-arginyl diiron disulfide PSI-MOD MOD:00362 Cross-link 4. tris-L-cysteinyl L-arginyl diiron disulfide A protein modification that effectively converts three L-cysteine residues, an L-arginine residue and a two-iron two-sulfur cluster to tris-L-cysteinyl L-arginyl diiron disulfide. PubMed:14704425 RESID:AA0357 METAL Iron-sulfur (2Fe-2S) di-mu-sulfido(N(eta1)-arginyl-S-cysteinyliron)(bis-S-cysteinyliron) tris-L-cysteinyl L-arginyl diiron disulfide A protein modification that effectively cross-links an L-cysteine residue and an L-selenocysteine residues to form L-cysteinyl-L-selenocystine. -2.02 C 0 H -2 N 0 O 0 S 0 Se 0 -2.01565 C 6 H 8 N 2 O 2 S 1 Se 1 251.17 251.94717 C, U natural uniprot.ptm:PTM-0109 (R,R)-2-amino-3-[3-(2-aminopropanoic acid)sulfanyl]selanylpropanoic acid CROSSLNK Cysteinyl-selenocysteine (Cys-Sec) CROSSLNK Cysteinyl-selenocysteine (Sec-Cys) L-cysteinyl-L-selenocysteine PSI-MOD MOD:00363 Cross-link 2. L-cysteinyl-L-selenocysteine (Cys-Sec) A protein modification that effectively cross-links an L-cysteine residue and an L-selenocysteine residues to form L-cysteinyl-L-selenocystine. PubMed:12911312 RESID:AA0358#SEC (R,R)-2-amino-3-[3-(2-aminopropanoic acid)sulfanyl]selanylpropanoic acid CROSSLNK Cysteinyl-selenocysteine (Cys-Sec) CROSSLNK Cysteinyl-selenocysteine (Sec-Cys) L-cysteinyl-L-selenocysteine A protein modification that effectively converts an L-lysine residue to 5-hydroxy-N6,N6,N6-trimethyl-L-lysine. 59.09 C 3 H 7 N 0 O 1 59.04914 1+ C 9 H 19 N 2 O 2 187.26 187.1441 K natural Unimod:445 uniprot.ptm:PTM-0186 (2R,5Xi)-5-amino-5-carboxy-2-hydroxy-N,N,N-trimethylpentan-1-aminium (2Xi,5S)-5-amino-5-carboxy-2-hydroxy-N,N,N-trimethylpentanaminium (2Xi,5S)-5-azanyl-5-carboxy-2-hydroxy-N,N,N-trimethylpentanazanium 5-hydroxy-N(zeta)-trimethyllysine 5-hydroxy-N6,N6,N6-trimethyl-L-lysine 5-hydroxy-N6,N6,N6-trimethyllysin-N6-ium 5-hydroxy-N6,N6,N6-trimethyllysine cation 5-hydroxylated N6,N6,N6-trimethylated L-lysine 5HyN6Me3Lys MOD_RES N6,N6,N6-trimethyl-5-hydroxylysine alpha-amino-epsilon-dimethylamino-delta-hydroxycaproic acid delta-hydroxy-epsilon-N,N,N-trimethyllysine lysine derivative Lys(z) PSI-MOD 5-hydroxy-N6,N6,N6-trimethyl Hydroxytrimethyl MOD:00364 Incidental to RESID:AA0278; secondary to RESID:AA0028; secondary to RESID:AA0074. 5-hydroxy-N6,N6,N6-trimethyl-L-lysine A protein modification that effectively converts an L-lysine residue to 5-hydroxy-N6,N6,N6-trimethyl-L-lysine. PubMed:11349130 PubMed:14661085 RESID:AA0359 Unimod:445#K (2R,5Xi)-5-amino-5-carboxy-2-hydroxy-N,N,N-trimethylpentan-1-aminium (2Xi,5S)-5-amino-5-carboxy-2-hydroxy-N,N,N-trimethylpentanaminium (2Xi,5S)-5-azanyl-5-carboxy-2-hydroxy-N,N,N-trimethylpentanazanium 5-hydroxy-N(zeta)-trimethyllysine 5-hydroxy-N6,N6,N6-trimethyl-L-lysine 5-hydroxy-N6,N6,N6-trimethyllysin-N6-ium 5-hydroxy-N6,N6,N6-trimethyllysine cation 5-hydroxylated N6,N6,N6-trimethylated L-lysine 5HyN6Me3Lys MOD_RES N6,N6,N6-trimethyl-5-hydroxylysine alpha-amino-epsilon-dimethylamino-delta-hydroxycaproic acid delta-hydroxy-epsilon-N,N,N-trimethyllysine lysine derivative Lys(z) 5-hydroxy-N6,N6,N6-trimethyl Hydroxytrimethyl A protein modification that effectively crosslinks an L-glutamic acid residue and a glycine residue by an isopeptide bond to form N-(L-isoglutamyl)-glycine. -18.02 C 0 H -2 N 0 O -1 -18.010565 C 7 H 9 N 2 O 3 169.16 169.06131 E, G natural N-term uniprot.ptm:PTM-0157 (S)-2-amino-5-(carboxymethyl)amino-5-oxopentanoic acid 2-amino-N5-(carboxymethyl)-pentanediamic acid CROSSLNK Isoglutamyl glycine isopeptide (Gly-Glu) N-(L-isoglutamyl)-glycine N-gamma-glutamylglycine isoglutamyl glycine PSI-MOD MOD:00365 Cross-link 2. N-(L-isoglutamyl)-glycine A protein modification that effectively crosslinks an L-glutamic acid residue and a glycine residue by an isopeptide bond to form N-(L-isoglutamyl)-glycine. PubMed:14531691 RESID:AA0360 (S)-2-amino-5-(carboxymethyl)amino-5-oxopentanoic acid 2-amino-N5-(carboxymethyl)-pentanediamic acid CROSSLNK Isoglutamyl glycine isopeptide (Gly-Glu) N-(L-isoglutamyl)-glycine N-gamma-glutamylglycine isoglutamyl glycine A protein modification that effectively converts an L-serine residue to O-sulfo-L-serine. 80.06 C 0 H 0 N 0 O 3 S 1 79.95682 C 3 H 5 N 1 O 5 S 1 167.13 166.98885 S natural Unimod:40 uniprot.ptm:PTM-0284 (2S)-2-amino-3-(sulfooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-sulfate MOD_RES Sulfoserine O-sulfo-L-serine O3-sulfonoserine O3-sulfoserine serine sulfate ester PSI-MOD O-Sulfonation Sulfo MOD:00366 O-sulfo-L-serine A protein modification that effectively converts an L-serine residue to O-sulfo-L-serine. PubMed:14752058 RESID:AA0361 Unimod:40#S (2S)-2-amino-3-(sulfooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-sulfate MOD_RES Sulfoserine O-sulfo-L-serine O3-sulfonoserine O3-sulfoserine serine sulfate ester O-Sulfonation Sulfo A protein modification that effectively converts an L-threonine residue to O-sulfo-L-threonine. 80.06 C 0 H 0 N 0 O 3 S 1 79.95682 C 4 H 7 N 1 O 5 S 1 181.16 181.00449 T natural Unimod:40 uniprot.ptm:PTM-0285 (2S,3R)-2-amino-3-(sulfooxy)butanoic acid 2-amino-3-hydroxybutanoic acid 3-sulfate MOD_RES Sulfothreonine O-sulfo-L-threonine O3-sulfonothreonine O3-sulfothreonine threonine sulfate ester PSI-MOD O-Sulfonation Sulfo MOD:00367 O-sulfo-L-threonine A protein modification that effectively converts an L-threonine residue to O-sulfo-L-threonine. PubMed:14752058 RESID:AA0362 Unimod:40#T (2S,3R)-2-amino-3-(sulfooxy)butanoic acid 2-amino-3-hydroxybutanoic acid 3-sulfate MOD_RES Sulfothreonine O-sulfo-L-threonine O3-sulfonothreonine O3-sulfothreonine threonine sulfate ester O-Sulfonation Sulfo A protein modification that effectively converts an L-methionine residue to N-carboxy-L-methionine. 44.01 C 1 H 0 N 0 O 2 S 0 43.98983 C 6 H 10 N 1 O 3 S 1 176.21 176.03813 M hypothetical N-term Unimod:299 (S)-2-carboxyamino-4-(methylsulfanyl)butanoic acid 2-carbamic-4-(methylsulfanyl)butanoic acid 2-carbamic-4-(methylthio)butanoic acid N-carboxy-L-methionine N-carboxymethionine PSI-MOD Carboxy Carboxylation MOD:00368 At least three protein crystallographic structures have been reported with this modification. However, no chemical evidence for this modification is provided, there were no reports of this modification before these crystallographic reports, and there is no metabolic explanation for the conversion of a formyl group to a carboxy group. There is confusion in its description, and misnaming is common. This modification is probably a misidentification of N-(dihydroxymethyl)methionine, the hydrated form of N-formylmethionine. See MOD:01446 [JSG]. N-carboxy-L-methionine A protein modification that effectively converts an L-methionine residue to N-carboxy-L-methionine. PubMed:10368287 PubMed:11120890 PubMed:12595263 PubMed:8312270 RESID:AA0363 Unimod:299#M (S)-2-carboxyamino-4-(methylsulfanyl)butanoic acid 2-carbamic-4-(methylsulfanyl)butanoic acid 2-carbamic-4-(methylthio)butanoic acid N-carboxy-L-methionine N-carboxymethionine Carboxy Carboxylation A protein modification that effectively converts an L-serine residue to O-acetyl-L-serine. 42.04 C 2 H 2 N 0 O 1 42.010567 C 5 H 7 N 1 O 3 129.12 129.04259 S natural Unimod:1 uniprot.ptm:PTM-0232 (2S)-3-(acetyloxy)-2-aminopropanoic acid MOD_RES O-acetylserine O-acetyl-L-serine O-acetylated L-serine O-acetylserine OAcSer serine acetate ester PSI-MOD Acetyl Acetylation MOD:00369 incidental to RESID:AA0051 O-acetyl-L-serine A protein modification that effectively converts an L-serine residue to O-acetyl-L-serine. ChEBI:17981 PubMed:11857757 PubMed:11999733 PubMed:12175151 PubMed:14730666 PubMed:15350136 PubMed:16731519 PubMed:489587 PubMed:7309355 RESID:AA0364 Unimod:1#S (2S)-3-(acetyloxy)-2-aminopropanoic acid MOD_RES O-acetylserine O-acetyl-L-serine O-acetylated L-serine O-acetylserine OAcSer serine acetate ester Acetyl Acetylation A protein modification that effectively converts an L-tyrosine residue to (E)-2,3-didehydrotyrosine. -2.02 C 0 H -2 N 0 O 0 -2.01565 C 9 H 7 N 1 O 2 161.16 161.04768 Y natural uniprot.ptm:PTM-0001 (2E)-2-amino-3-(4-hydroxyphenyl)prop-2-enoic acid (E)-2,3-didehydrogenated tyrosine (E)-2,3-didehydrotyrosine E-dHTyr MOD_RES (E)-2,3-didehydrotyrosine amino-(para-hydroxybenzylidenyl)acetic acid blue non-fluorescent pocilloporin chromophore para-hydroxybenzylidene-imidazolidinone chromophore trans-dehydrotyrosine PSI-MOD 2-amino-3-oxo-butanoic_acid Didehydro MOD:00370 incidental to RESID:AA0184; incidental to RESID:AA0187; incidental to RESID:AA0188; incidental to RESID:AA0189; incidental to RESID:AA0378; incidental to RESID:AA0379; incidental to RESID:AA0380; incidental to RESID:AA0381 (E)-2,3-didehydrotyrosine A protein modification that effectively converts an L-tyrosine residue to (E)-2,3-didehydrotyrosine. PubMed:12623015 RESID:AA0365 (2E)-2-amino-3-(4-hydroxyphenyl)prop-2-enoic acid (E)-2,3-didehydrogenated tyrosine (E)-2,3-didehydrotyrosine E-dHTyr MOD_RES (E)-2,3-didehydrotyrosine amino-(para-hydroxybenzylidenyl)acetic acid blue non-fluorescent pocilloporin chromophore para-hydroxybenzylidene-imidazolidinone chromophore trans-dehydrotyrosine 2-amino-3-oxo-butanoic_acid Didehydro A protein modification that effectively converts two L-aspartic acid residues, three L-glutamic acid residues, an L-histidine residue, and a one-calcium, four-iron, four-oxygen cluster to bis-L-aspartato tris-L-glutamato L-histidino calcium tetramanganese tetroxide. 317.78 C 0 Ca 1 H -6 Mn 4 N 0 O 4 317.6475 C 29 Ca 1 H 32 Mn 4 N 8 O 20 1072.44 1071.8881 D, D, E, E, E, H hypothetical 4Mn-Ca-4O cluster bis-L-aspartato tris-L-glutamato L-histidino calcium tetramanganese tetroxide mu3-1:2:3kappaO-oxido-mu3-1:3:4kappaO-oxido-mu3-2:3:4kappaO-oxido-mu4-1:2:4:5kappaO-oxido-N1'-histidino-O5-glutamato 2-manganese-O5,O5-glutamato 3-manganese-O4-aspartato 4-manganese-O4-aspartato-O5-glutamato 5-manganese photosystem II catalytic cluster PSI-MOD MOD:00371 Cross-link 6. bis-L-aspartato tris-L-glutamato L-histidino calcium tetramanganese tetroxide A protein modification that effectively converts two L-aspartic acid residues, three L-glutamic acid residues, an L-histidine residue, and a one-calcium, four-iron, four-oxygen cluster to bis-L-aspartato tris-L-glutamato L-histidino calcium tetramanganese tetroxide. PubMed:14764885 RESID:AA0366 4Mn-Ca-4O cluster bis-L-aspartato tris-L-glutamato L-histidino calcium tetramanganese tetroxide mu3-1:2:3kappaO-oxido-mu3-1:3:4kappaO-oxido-mu3-2:3:4kappaO-oxido-mu4-1:2:4:5kappaO-oxido-N1'-histidino-O5-glutamato 2-manganese-O5,O5-glutamato 3-manganese-O4-aspartato 4-manganese-O4-aspartato-O5-glutamato 5-manganese photosystem II catalytic cluster A protein modification that effectively cross-links two L-tyrosine residues with a carbon-carbon bond to form 3'-(3'-L-tyrosinyl)-L-tyrosine. -2.02 C 0 H -2 N 0 O 0 -2.01565 C 18 H 16 N 2 O 4 324.34 324.111 Y, Y natural (2S,2'S)-3,3'-(6,6'-dihydroxybiphenyl-3,3'-diyl)bis(2-aminopropanoic acid) 3'-(L-tyros-3'-yl)-L-tyrosine 3,3'-BiTyr (Crosslink) 6,6'-dihydroxy-(1,1'-biphenyl)-3,3'-bis(2-aminopropanoic acid) alpha,alpha'-diamino-6,6'-dihydroxy-(1,1'-biphenyl)-3,3'-dipropanoic acid bityrosine o,o-dityrosine PSI-MOD MOD:00372 Cross-link 2; From DeltaMass: Average Mass: -2. 3'-(3'-L-tyrosinyl)-L-tyrosine A protein modification that effectively cross-links two L-tyrosine residues with a carbon-carbon bond to form 3'-(3'-L-tyrosinyl)-L-tyrosine. DeltaMass:0 PubMed:14249161 PubMed:637884 PubMed:8702710 PubMed:8937563 RESID:AA0367 (2S,2'S)-3,3'-(6,6'-dihydroxybiphenyl-3,3'-diyl)bis(2-aminopropanoic acid) 3'-(L-tyros-3'-yl)-L-tyrosine 3,3'-BiTyr (Crosslink) 6,6'-dihydroxy-(1,1'-biphenyl)-3,3'-bis(2-aminopropanoic acid) alpha,alpha'-diamino-6,6'-dihydroxy-(1,1'-biphenyl)-3,3'-dipropanoic acid bityrosine o,o-dityrosine A protein modification that effectively cross-links L-tyrosine residues with an ether bond to form 3'-(O4'-L-tyrosinyl)-L-tyrosine. -2.02 C 0 H -2 N 0 O 0 -2.01565 C 18 H 16 N 2 O 4 324.34 324.111 Y, Y natural uniprot.ptm:PTM-0155 (2S)-2-amino-3-[3-(4-[(2S)-2-amino-2-carboxyethyl]phenoxy)-4-hydroxyphenyl]propanoic acid 2-amino-3-[4-(5-[(2S)-2-amino-2-carboxyethyl]-2-hydroxyphenoxy)phenyl]propanoic acid 3'-(L-tyros-O4'-yl)-L-tyrosine CROSSLNK Isodityrosine (Tyr-Tyr) IsodiTyr (Crosslink) O-(5-(2-amino-2-carboxyethyl)-2-hydroxyphenyl)-L-tyrosine isodityrosine PSI-MOD MOD:00373 Cross-link 2; secondary to RESID:AA0146; From DeltaMass: Average Mass: -2. 3'-(O4'-L-tyrosinyl)-L-tyrosine A protein modification that effectively cross-links L-tyrosine residues with an ether bond to form 3'-(O4'-L-tyrosinyl)-L-tyrosine. DeltaMass:0 PubMed:12719529 PubMed:7115340 PubMed:8702710 RESID:AA0368 (2S)-2-amino-3-[3-(4-[(2S)-2-amino-2-carboxyethyl]phenoxy)-4-hydroxyphenyl]propanoic acid 2-amino-3-[4-(5-[(2S)-2-amino-2-carboxyethyl]-2-hydroxyphenoxy)phenyl]propanoic acid 3'-(L-tyros-O4'-yl)-L-tyrosine CROSSLNK Isodityrosine (Tyr-Tyr) IsodiTyr (Crosslink) O-(5-(2-amino-2-carboxyethyl)-2-hydroxyphenyl)-L-tyrosine isodityrosine A protein modification that effectively converts an L-arginine residue to 3,4-dihydroxy-L-arginine. 32.0 C 0 H 0 N 0 O 2 31.989828 C 6 H 12 N 4 O 3 188.19 188.09094 R natural Unimod:425 uniprot.ptm:PTM-0022 (2S,3Xi,4Xi)-2-amino-5-carbamimidamido-3,4-dihydroxypentanoic acid 2-amino-5-guanidino-3,4-dihydroxypentanoic acid 3,4-dihydroxy-L-arginine 3,4-dihydroxylated L-arginine 34Hy2Arg MOD_RES 3,4-dihydroxyarginine beta,gamma-dihydroxyarginine PSI-MOD Dioxidation dihydroxy MOD:00374 3,4-dihydroxy-L-arginine A protein modification that effectively converts an L-arginine residue to 3,4-dihydroxy-L-arginine. ChEBI:141829 PubMed:10978343 PubMed:12686488 RESID:AA0369 Unimod:425#R (2S,3Xi,4Xi)-2-amino-5-carbamimidamido-3,4-dihydroxypentanoic acid 2-amino-5-guanidino-3,4-dihydroxypentanoic acid 3,4-dihydroxy-L-arginine 3,4-dihydroxylated L-arginine 34Hy2Arg MOD_RES 3,4-dihydroxyarginine beta,gamma-dihydroxyarginine Dioxidation dihydroxy A protein modification that effectively converts an L-lysine residue to 4,5-dihydroxy-L-lysine. 32.0 C 0 H 0 N 0 O 2 31.989828 C 6 H 12 N 2 O 3 160.17 160.0848 K natural Unimod:425 uniprot.ptm:PTM-0036 (2S,4Xi,5Xi)-2,6-diamino-4,5-dihydroxyhexanoic acid 4,5-dihydroxy-L-lysine 4,5-dihydroxylated L-lysine 45Hy2Lys MOD_RES 4,5-dihydroxylysine alpha,epsilon-diamino-delta,gamma-dihydroxycaproic acid delta,gamma-dihydroxylysine PSI-MOD Dioxidation dihydroxy MOD:00375 4,5-dihydroxy-L-lysine A protein modification that effectively converts an L-lysine residue to 4,5-dihydroxy-L-lysine. PubMed:10978343 PubMed:12686488 RESID:AA0370 Unimod:425#K (2S,4Xi,5Xi)-2,6-diamino-4,5-dihydroxyhexanoic acid 4,5-dihydroxy-L-lysine 4,5-dihydroxylated L-lysine 45Hy2Lys MOD_RES 4,5-dihydroxylysine alpha,epsilon-diamino-delta,gamma-dihydroxycaproic acid delta,gamma-dihydroxylysine Dioxidation dihydroxy A protein modification that effectively crosslinks an L-histidine residue and 5'-phosphoadenosine through a phosphoramide ester bond to form 1'-(phospho-5'-adenosine)-L-histidine. 329.21 C 10 H 12 N 5 O 6 P 1 329.05252 C 16 H 19 N 8 O 7 P 1 466.35 466.11142 H natural Unimod:405 (2S)-2-amino-3-[1-(5'-adenosine phosphono)imidazol-4-yl]propanoic acid 1'-(phospho-5'-adenosine)-L-histidine ACT_SITE Tele-AMP-histidine intermediate L-histidine 5'-adenosine phosphoramidester L-histidine monoanhydride with 5'-adenylic acid N(tau)-5'-adenylic-L-histidine N1'-adenylylated histidine tele-5'-adenylic-L-histidine PSI-MOD AMP binding site Phosphoadenosine MOD:00376 1'-(phospho-5'-adenosine)-L-histidine A protein modification that effectively crosslinks an L-histidine residue and 5'-phosphoadenosine through a phosphoramide ester bond to form 1'-(phospho-5'-adenosine)-L-histidine. PubMed:15182206 PubMed:9323207 RESID:AA0371 Unimod:405#H (2S)-2-amino-3-[1-(5'-adenosine phosphono)imidazol-4-yl]propanoic acid 1'-(phospho-5'-adenosine)-L-histidine ACT_SITE Tele-AMP-histidine intermediate L-histidine 5'-adenosine phosphoramidester L-histidine monoanhydride with 5'-adenylic acid N(tau)-5'-adenylic-L-histidine N1'-adenylylated histidine tele-5'-adenylic-L-histidine AMP binding site Phosphoadenosine A protein modification that effectively crosslinks an L-histidine residue and 5'-phosphouridine through a phosphoramide ester bond to form 1'-(phospho-5'-uridine)-L-histidine. 306.17 C 9 H 11 N 2 O 8 P 1 306.0253 C 15 H 18 N 5 O 9 P 1 443.31 443.08423 H natural Unimod:417 uniprot.ptm:PTM-0500 (S)-2-amino-3-[1-(5'-uridine phosphono)imidazol-4-yl]propanoic acid 1'-(phospho-5'-uridine)-L-histidine ACT_SITE Tele-UMP-histidine intermediate L-histidine 5'-uridine phosphoramidester L-histidine monoanhydride with 5'-uridylic acid MOD_RES O-UMP-histidine N(tau)-5'-uridylic-L-histidine N1'-uridylylated histidine tele-5'-uridylic-L-histidine PSI-MOD PhosphoUridine uridine phosphodiester MOD:00377 1'-(phospho-5'-uridine)-L-histidine A protein modification that effectively crosslinks an L-histidine residue and 5'-phosphouridine through a phosphoramide ester bond to form 1'-(phospho-5'-uridine)-L-histidine. PubMed:11467524 PubMed:321007 PubMed:380639 PubMed:8794735 RESID:AA0372 Unimod:417#H (S)-2-amino-3-[1-(5'-uridine phosphono)imidazol-4-yl]propanoic acid 1'-(phospho-5'-uridine)-L-histidine ACT_SITE Tele-UMP-histidine intermediate L-histidine 5'-uridine phosphoramidester L-histidine monoanhydride with 5'-uridylic acid MOD_RES O-UMP-histidine N(tau)-5'-uridylic-L-histidine N1'-uridylylated histidine tele-5'-uridylic-L-histidine PhosphoUridine uridine phosphodiester A protein modification that effectively converts an L-aspartic acid residue to L-aspartyl semialdehyde. -16.0 C 0 H 0 N 0 O -1 -15.994915 C 4 H 5 N 1 O 2 99.09 99.03203 D natural Unimod:447 uniprot.ptm:PTM-0064 (S)-2-amino-4-oxobutanoic acid L-aminosuccinaldehydic acid L-aminosuccinic acid semialdehyde L-aspartate-beta-semialdehyde L-aspartic beta-semialdehyde L-aspartyl aldehyde L-beta-formylalanine MOD_RES Aspartyl aldehyde aspartyl 4-semialdehyde aspartyl aldehyde PSI-MOD Deoxy reduction MOD:00378 L-aspartyl semialdehyde A protein modification that effectively converts an L-aspartic acid residue to L-aspartyl semialdehyde. PubMed:1093385 PubMed:14235557 PubMed:15237995 RESID:AA0373 Unimod:447#D (S)-2-amino-4-oxobutanoic acid L-aminosuccinaldehydic acid L-aminosuccinic acid semialdehyde L-aspartate-beta-semialdehyde L-aspartic beta-semialdehyde L-aspartyl aldehyde L-beta-formylalanine MOD_RES Aspartyl aldehyde aspartyl 4-semialdehyde aspartyl aldehyde Deoxy reduction A protein modification that effectively converts an L-serine residue to L-serine microcin E492 siderophore ester. 831.69 C 36 H 37 N 3 O 20 831.197 C 39 H 43 N 4 O 23 935.78 935.2318 S natural C-term Unimod:448 uniprot.ptm:PTM-0276 L-serine microcin E492 siderophore ester MOD_RES Serine microcin E492 siderophore ester N-[5-(6-O-seryl-beta-glucosyl)-2,3-dihydroxybenzoyl]-O-[N-(2,3-dihydroxybenzoyl)-O-[N-(2,3-dihydroxybenzoyl)seryl]seryl]serine PSI-MOD Microcin microcin E492 siderophore ester from serine MOD:00379 Unimod origin corrected [JSG]. L-serine microcin E492 siderophore ester A protein modification that effectively converts an L-serine residue to L-serine microcin E492 siderophore ester. PubMed:15102848 RESID:AA0374 Unimod:448#C-term L-serine microcin E492 siderophore ester MOD_RES Serine microcin E492 siderophore ester N-[5-(6-O-seryl-beta-glucosyl)-2,3-dihydroxybenzoyl]-O-[N-(2,3-dihydroxybenzoyl)-O-[N-(2,3-dihydroxybenzoyl)seryl]seryl]serine Microcin microcin E492 siderophore ester from serine A protein modification that effectively converts an L-aspartic acid residue to L-aspartyl molybdenum bis(molybdopterin guanine dinucleotide). 1572.02 C 40 H 47 Mo 1 N 20 O 26 P 4 S 4 1572.9857 C 44 H 52 Mo 1 N 21 O 29 P 4 S 4 1687.1 1688.0127 D natural Unimod:424 2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraazaanthracen-4-one guanosine dinucleotide L-aspartyl molybdenum bis(molybdopterin guanine dinucleotide) bis[8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with guanosine)methyl-6-oxo-3,4-disulfanyl-pteridino[6,7-5,6]pyranoato-S3,S4]-aspartyl-molybdenum nitrate reductase A aspartyl Mo-bisMGD cofactor phosphoric acid 4-(2-amino-4-oxo-3,4,5,6,-tetrahydro-pteridin-6-yl)-2-hydroxy-3,4-dimercapto-but-3-en-yl ester guanylate ester PSI-MOD MolybdopterinGD molybdenum bis(molybdopterin guanine dinucleotide) MOD:00380 L-aspartyl molybdenum bis(molybdopterin guanine dinucleotide) A protein modification that effectively converts an L-aspartic acid residue to L-aspartyl molybdenum bis(molybdopterin guanine dinucleotide). PubMed:12910261 PubMed:14725769 RESID:AA0375 Unimod:424#D 2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraazaanthracen-4-one guanosine dinucleotide L-aspartyl molybdenum bis(molybdopterin guanine dinucleotide) bis[8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with guanosine)methyl-6-oxo-3,4-disulfanyl-pteridino[6,7-5,6]pyranoato-S3,S4]-aspartyl-molybdenum nitrate reductase A aspartyl Mo-bisMGD cofactor phosphoric acid 4-(2-amino-4-oxo-3,4,5,6,-tetrahydro-pteridin-6-yl)-2-hydroxy-3,4-dimercapto-but-3-en-yl ester guanylate ester MolybdopterinGD molybdenum bis(molybdopterin guanine dinucleotide) A protein modification that effectively converts an L-selenocysteine residue to L-selenocysteinyl tungsten bis(molybdopterin guanine dinucleotide). 1691.97 C 40 H 47 N 20 O 26 P 4 S 5 Se 0 W 1 1691.0034 C 43 H 52 N 21 O 27 P 4 S 5 Se 1 W 1 1842.02 1841.957 U natural PSI-MOD MOD:00381 L-selenocysteinyl tungsten bis(molybdopterin guanine dinucleotide) (Sec) A protein modification that effectively converts an L-selenocysteine residue to L-selenocysteinyl tungsten bis(molybdopterin guanine dinucleotide). PubMed:11372198 PubMed:12220497 RESID:AA0376#SEC A protein modification that effectively crosslinks an L-methionyl-L-tyrosine dipeptide to form 3-(2-methylthio)ethyl-6-(4-hydroxybenzylidene)-5-iminopiperazin-2-one. -20.03 C 0 H -4 N 0 O -1 S 0 -20.026215 C 14 H 15 N 2 O 2 S 1 275.35 275.08542 M, Y hypothetical N-term 3-(2-methylsulfanyl)ethyl-6-(4-hydroxybenzylidene)-5-iminopiperazin-2-one 3-(2-methylthio)ethyl-6-(4-hydroxybenzylidene)-5-amino-3,6-didehydropyrazin-2-ol 3-(2-methylthio)ethyl-6-(4-hydroxybenzylidene)-5-iminopiperazin-2-one GFP-like chromoprotein asFP595 chromophore L-methionyl-L-tyrosyl-2-keto-5-iminopiperazine PSI-MOD MOD:00382 carboxamidine; cross-link 1. This is a deprecated entry in RESID. It probably does not occur naturally [JSG]. 3-(2-methylthio)ethyl-6-(4-hydroxybenzylidene)-5-iminopiperazin-2-one A protein modification that effectively crosslinks an L-methionyl-L-tyrosine dipeptide to form 3-(2-methylthio)ethyl-6-(4-hydroxybenzylidene)-5-iminopiperazin-2-one. PubMed:10852900 PubMed:11259412 PubMed:15491166 RESID:AA0377 3-(2-methylsulfanyl)ethyl-6-(4-hydroxybenzylidene)-5-iminopiperazin-2-one 3-(2-methylthio)ethyl-6-(4-hydroxybenzylidene)-5-amino-3,6-didehydropyrazin-2-ol 3-(2-methylthio)ethyl-6-(4-hydroxybenzylidene)-5-iminopiperazin-2-one GFP-like chromoprotein asFP595 chromophore L-methionyl-L-tyrosyl-2-keto-5-iminopiperazine A protein modification that effectively crosslinks an L-glutamic acid residue and a glycine residue to form 2-imino-glutamic acid 5-imidazolinone glycine. -20.03 C 0 H -4 N 0 O -1 -20.026215 C 7 H 6 N 2 O 3 166.14 166.03784 E, G hypothetical uniprot.ptm:PTM-0014 2,N-didehydroglutamyl-5-imidazolinone glycine 2-(3-carboxy-1-iminopropyl)-1-carboxymethyl-1-imidazolin-5-one 2-imino-glutamic acid 5-imidazolinone glycine 2-imino-glutamyl-5-imidazolinone glycine 4-[1-(carboxymethyl)-5-oxo-4,5-dihydro-1H-imidazol-2-yl]-4-iminobutanoic acid CROSSLNK 2-iminomethyl-5-imidazolinone (Glu-Gly) [2-(3-carboxy-1-iminopropyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid para-hydroxybenzylidene-imidazolidinone chromophore PSI-MOD MOD:00383 Cross-link 2; carboxamidine; cross-link 1; incidental to RESID:AA0183; incidental to RESID:AA0365. 2-imino-glutamic acid 5-imidazolinone glycine A protein modification that effectively crosslinks an L-glutamic acid residue and a glycine residue to form 2-imino-glutamic acid 5-imidazolinone glycine. PubMed:11682051 RESID:AA0378 2,N-didehydroglutamyl-5-imidazolinone glycine 2-(3-carboxy-1-iminopropyl)-1-carboxymethyl-1-imidazolin-5-one 2-imino-glutamic acid 5-imidazolinone glycine 2-imino-glutamyl-5-imidazolinone glycine 4-[1-(carboxymethyl)-5-oxo-4,5-dihydro-1H-imidazol-2-yl]-4-iminobutanoic acid CROSSLNK 2-iminomethyl-5-imidazolinone (Glu-Gly) [2-(3-carboxy-1-iminopropyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid para-hydroxybenzylidene-imidazolidinone chromophore A protein modification that effectively crosslinks an L-methionine residue and a glycine residue to form 2-imino-methionine 5-imidazolinone glycine. -20.03 C 0 H -4 N 0 O -1 S 0 -20.026215 C 7 H 8 N 2 O 1 S 1 168.21 168.03574 G, M natural uniprot.ptm:PTM-0015 (2-[1-imino-3-(methylsulfanyl)propyl]-5-oxo-4,5-dihydro-imidazol-1-yl)acetic acid (2-[3-(methylsulfanyl)propanimidoyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid 2,N-didehydromethionyl-5-imidazolinone glycine 2-[1-imino-3-(methylsulfanyl)propyl]-1-carboxymethyl-1-imidazolin-5-one 2-imino-methionine 5-imidazolinone glycine 2-imino-methionyl-5-imidazolinone glycine CROSSLNK 2-iminomethyl-5-imidazolinone (Met-Gly) GFP-like chromoprotein asFP595 chromophore para-hydroxybenzylidene-imidazolidinone chromophore red fluorescent protein eqFP611 chromophore PSI-MOD MOD:00384 Cross-link 2; carboxamidine; cross-link 1; incidental to RESID:AA0183; incidental to RESID:AA0365. 2-imino-methionine 5-imidazolinone glycine A protein modification that effectively crosslinks an L-methionine residue and a glycine residue to form 2-imino-methionine 5-imidazolinone glycine. PubMed:10852900 PubMed:12185250 PubMed:12909624 PubMed:15542608 RESID:AA0379 (2-[1-imino-3-(methylsulfanyl)propyl]-5-oxo-4,5-dihydro-imidazol-1-yl)acetic acid (2-[3-(methylsulfanyl)propanimidoyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid 2,N-didehydromethionyl-5-imidazolinone glycine 2-[1-imino-3-(methylsulfanyl)propyl]-1-carboxymethyl-1-imidazolin-5-one 2-imino-methionine 5-imidazolinone glycine 2-imino-methionyl-5-imidazolinone glycine CROSSLNK 2-iminomethyl-5-imidazolinone (Met-Gly) GFP-like chromoprotein asFP595 chromophore para-hydroxybenzylidene-imidazolidinone chromophore red fluorescent protein eqFP611 chromophore A protein modification that effectively crosslinks an L-asparagine residue and a glycine residue to form L-asparagine 5-imidazolinone glycine. -18.02 C 0 H -2 N 0 O -1 -18.010565 C 6 H 7 N 3 O 2 153.14 153.05383 G, N hypothetical uniprot.ptm:PTM-0046 (2-[(1S)-1,3-diamino-3-oxopropyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid 2-[(S)-1,3-diamino-3-oxopropyl]-1-carboxymethyl-1-imidazolin-5-one CROSSLNK 5-imidazolinone (Asn-Gly) L-asparagine 5-imidazolinone glycine Zoanthus sp. fluorescent protein FP506 chromophore [2-(1,3-diamino-3-oxopropyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid asparaginyl-5-imidazolinone glycine para-hydroxybenzylidene-imidazolidinone chromophore PSI-MOD MOD:00385 Cross-link 2; carboxamidine; incidental to RESID:AA0183; incidental to RESID:AA0365. L-asparagine 5-imidazolinone glycine A protein modification that effectively crosslinks an L-asparagine residue and a glycine residue to form L-asparagine 5-imidazolinone glycine. PubMed:10504696 RESID:AA0380 (2-[(1S)-1,3-diamino-3-oxopropyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid 2-[(S)-1,3-diamino-3-oxopropyl]-1-carboxymethyl-1-imidazolin-5-one CROSSLNK 5-imidazolinone (Asn-Gly) L-asparagine 5-imidazolinone glycine Zoanthus sp. fluorescent protein FP506 chromophore [2-(1,3-diamino-3-oxopropyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid asparaginyl-5-imidazolinone glycine para-hydroxybenzylidene-imidazolidinone chromophore A protein modification that effectively crosslinks an L-lysine residue and a glycine residue to form L-lysine 5-imidazolinone glycine. -18.02 C 0 H -2 N 0 O -1 -18.010565 C 8 H 13 N 3 O 1 167.21 167.10587 G, K hypothetical uniprot.ptm:PTM-0048 (2-[(1S)-1,5-diaminopentyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid 2-[(S)-1,5-diaminopentanyl]-1-carboxymethyl-1-imidazolin-5-one Anemonia majano fluorescent protein FP486 chromophore CROSSLNK 5-imidazolinone (Lys-Gly) L-lysine 5-imidazolinone glycine [2-(1,5-diaminopentanyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid lysyl-5-imidazolinone glycine para-hydroxybenzylidene-imidazolidinone chromophore PSI-MOD MOD:00386 Cross-link 2; carboxamidine; incidental to RESID:AA0183; incidental to RESID:AA0365. L-lysine 5-imidazolinone glycine A protein modification that effectively crosslinks an L-lysine residue and a glycine residue to form L-lysine 5-imidazolinone glycine. PubMed:10504696 RESID:AA0381 (2-[(1S)-1,5-diaminopentyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid 2-[(S)-1,5-diaminopentanyl]-1-carboxymethyl-1-imidazolin-5-one Anemonia majano fluorescent protein FP486 chromophore CROSSLNK 5-imidazolinone (Lys-Gly) L-lysine 5-imidazolinone glycine [2-(1,5-diaminopentanyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid lysyl-5-imidazolinone glycine para-hydroxybenzylidene-imidazolidinone chromophore A protein modification that effectively crosslinks an L-lysine residue and a glycine residue to form 2-tetrahydropyridinyl-5-imidazolinone glycine. -37.06 C 0 H -7 N -1 O -1 -37.052765 C 8 H 9 N 2 O 1 149.17 149.07149 G, K natural N-term uniprot.ptm:PTM-0018 2-(3,4,5,6-tetrahydropyridin-2-yl)-1-carboxymethyl-1-imidazolin-5-one 2-(tetrahydropyrid-2-yl)-5-imidazolinone glycine 2-tetrahydropyridinyl-5-imidazolinone glycine CROSSLNK 2-tetrahydro-2-pyridyl-5-imidazolinone (Lys-Gly) Zoanthus sp. fluorescent protein zFP538 chromophore [5-oxo-2-(3,4,5,6-tetrahydropyridin-2-yl)-4,5-dihydro-1H-imidazol-1-yl]acetic acid para-hydroxybenzylidene-imidazolidinone chromophore PSI-MOD MOD:00387 Cross-link 2; carboxamidine; incidental to RESID:AA0183; incidental to RESID:AA0365. 2-tetrahydropyridinyl-5-imidazolinone glycine A protein modification that effectively crosslinks an L-lysine residue and a glycine residue to form 2-tetrahydropyridinyl-5-imidazolinone glycine. PubMed:10504696 PubMed:15628861 RESID:AA0382 2-(3,4,5,6-tetrahydropyridin-2-yl)-1-carboxymethyl-1-imidazolin-5-one 2-(tetrahydropyrid-2-yl)-5-imidazolinone glycine 2-tetrahydropyridinyl-5-imidazolinone glycine CROSSLNK 2-tetrahydro-2-pyridyl-5-imidazolinone (Lys-Gly) Zoanthus sp. fluorescent protein zFP538 chromophore [5-oxo-2-(3,4,5,6-tetrahydropyridin-2-yl)-4,5-dihydro-1H-imidazol-1-yl]acetic acid [5-oxo-2-(3,4,5,6-tetrahydropyridin-2-yl)-4,5-dihydro-1H-imidazol-1-yl]acetic acid para-hydroxybenzylidene-imidazolidinone chromophore A protein modification that effectively attaches an L-alanine residue to murein peptidoglycan by a pentaglycine linker peptide. A hypothetical C-term uniprot.ptm:PTM-0245 (2R,6S)-2-(N-mureinyl-(R)-alanyl-(S)-isoglutamyl)amino-6-(alanyl-pentaglycyl)amino-pimeloyl-(S)-alanyl-(S)-alanine L-alanyl-pentaglycyl-murein peptidoglycan MOD_RES Pentaglycyl murein peptidoglycan amidated alanine PSI-MOD MOD:00388 L-alanyl-pentaglycyl-murein peptidoglycan A protein modification that effectively attaches an L-alanine residue to murein peptidoglycan by a pentaglycine linker peptide. PubMed:8163519 RESID:AA0383 (2R,6S)-2-(N-mureinyl-(R)-alanyl-(S)-isoglutamyl)amino-6-(alanyl-pentaglycyl)amino-pimeloyl-(S)-alanyl-(S)-alanine L-alanyl-pentaglycyl-murein peptidoglycan MOD_RES Pentaglycyl murein peptidoglycan amidated alanine A protein modification that effectively converts an L-proline residue to N-formyl-L-proline. 28.01 C 1 H 0 N 0 O 1 27.994915 C 6 H 8 N 1 O 2 126.14 126.055504 P hypothetical N-term Unimod:122 (2S)-1-formylpyrrolidine-2-carboxylic acid 1-formyl-2-pyrrolidinecarboxylic acid 1-formylproline N-formyl-L-proline N-formylated L-proline NFoPro PSI-MOD MOD:00389 CAUTION - observations of this modification can be attributed to unintended artifactual production, or to spurious peptide MS identification. This modification is probably not a natural post-translational modification [JSG]. N-formyl-L-proline A protein modification that effectively converts an L-proline residue to N-formyl-L-proline. PubMed:12051774 PubMed:5464655 RESID:AA0384 Unimod:122#N-term (2S)-1-formylpyrrolidine-2-carboxylic acid 1-formyl-2-pyrrolidinecarboxylic acid 1-formylproline N-formyl-L-proline N-formylated L-proline NFoPro A protein modification that effectively converts an L-serine residue to O-decanoyl-L-serine. 154.25 C 10 H 18 N 0 O 1 154.13576 C 13 H 23 N 1 O 3 241.33 241.1678 S natural Unimod:449 uniprot.ptm:PTM-0234 (2S)-2-amino-3-(decanoyloxy)propanoic acid L-serine decanoate ester LIPID O-decanoyl serine O-decanoyl-L-serine O-decanoylated L-serine O3-decanoyl-L-serine ODecSer PSI-MOD Decanoyl lipid MOD:00390 O-decanoyl-L-serine A protein modification that effectively converts an L-serine residue to O-decanoyl-L-serine. PubMed:12630926 RESID:AA0385 Unimod:449#S (2S)-2-amino-3-(decanoyloxy)propanoic acid L-serine decanoate ester LIPID O-decanoyl serine O-decanoyl-L-serine O-decanoylated L-serine O3-decanoyl-L-serine ODecSer Decanoyl lipid A protein modification that effectively converts an L-threonine residue to O-octanoyl-L-threonine. 126.2 C 8 H 14 N 0 O 1 126.10446 C 12 H 21 N 1 O 3 227.3 227.15215 T natural Unimod:426 uniprot.ptm:PTM-0240 (2S)-2-amino-3-(octanoyloxy)butanoic acid L-threonine octanoate ester LIPID O-octanoyl threonine O-octanoyl-L-threonine O-octanoylated L-threonine O3-octanoyl-L-threonine OOctThr PSI-MOD Octanoyl octanoyl MOD:00391 O-octanoyl-L-threonine A protein modification that effectively converts an L-threonine residue to O-octanoyl-L-threonine. PubMed:11546772 PubMed:12716131 RESID:AA0386 Unimod:426#T (2S)-2-amino-3-(octanoyloxy)butanoic acid L-threonine octanoate ester LIPID O-octanoyl threonine O-octanoyl-L-threonine O-octanoylated L-threonine O3-octanoyl-L-threonine OOctThr Octanoyl octanoyl A protein modification that effectively converts an L-threonine residue to O-decanoyl-L-threonine. 154.25 C 10 H 18 N 0 O 1 154.13576 C 14 H 25 N 1 O 3 255.36 255.18344 T natural Unimod:449 uniprot.ptm:PTM-0235 (2S)-2-amino-3-(decanoyloxy)propanoic acid L-threonine decanoate ester LIPID O-decanoyl threonine O-decanoyl-L-threonine O-decanoylated L-threonine O3-decanoyl-L-threonine ODecThr PSI-MOD Decanoyl lipid MOD:00392 O-decanoyl-L-threonine A protein modification that effectively converts an L-threonine residue to O-decanoyl-L-threonine. PubMed:11546772 RESID:AA0387 Unimod:449#T (2S)-2-amino-3-(decanoyloxy)propanoic acid L-threonine decanoate ester LIPID O-decanoyl threonine O-decanoyl-L-threonine O-decanoylated L-threonine O3-decanoyl-L-threonine ODecThr Decanoyl lipid A protein modification that effectively replaces a hydroxyl group hydrogen with a methyl group to produce either an ether from an alcohol or an ester from an acid. OMeRes PSI-MOD MOD:00393 O-methylated residue A protein modification that effectively replaces a hydroxyl group hydrogen with a methyl group to produce either an ether from an alcohol or an ester from an acid. PubMed:18688235 OMeRes A protein modification that effectively replaces one hydrogen atom with one acetyl group. 42.04 C 2 H 2 O 1 42.010567 X artifact Unimod:1 Ac1Res Acetylation (N terminus, N epsilon of Lysine, O of Serine) (Ac) PSI-MOD Acetyl Acetylation MOD:00394 Amino hydrogens are replaced to produce amides; hydroxyl hydrogens are replaced to produce esters; and hydrosulfanyl (thiol) hydrogens are replaced to produce sulfanyl esters (thiol esters). From DeltaMass: Average Mass: 42 monoacetylated residue A protein modification that effectively replaces one hydrogen atom with one acetyl group. DeltaMass:0 PubMed:11857757 PubMed:11999733 PubMed:12175151 PubMed:14730666 PubMed:15350136 Unimod:1 Ac1Res Acetylation (N terminus, N epsilon of Lysine, O of Serine) (Ac) Acetyl Acetylation A protein modification that crosslinks two residues by formation of a thioester bond between a cysteine thiol and either an alpha-carbonyl, as in S-(L-methionyl-L-cysteine), or a sidechain carbonyl, as in S-(L-isoglutamyl)-L-cysteine. PSI-MOD MOD:00395 thioester crosslinked residues A protein modification that crosslinks two residues by formation of a thioester bond between a cysteine thiol and either an alpha-carbonyl, as in S-(L-methionyl-L-cysteine), or a sidechain carbonyl, as in S-(L-isoglutamyl)-L-cysteine. PubMed:18688235 A protein modification that effectively replaces a residue hydrogen atom on an oxygen with a carbohydrate-like group through a glycosidic bond. OGlycoRes PSI-MOD MOD:00396 O-glycosylated residue A protein modification that effectively replaces a residue hydrogen atom on an oxygen with a carbohydrate-like group through a glycosidic bond. PubMed:18688235 OGlycoRes A protein modification that is produced by reaction with iodoacetamide, usually replacement of a reactive hydrogen with a methylcarboxamido group. 57.05 C 2 H 3 N 1 O 1 57.021465 X artifact Unimod:4 PSI-MOD Carbamidomethyl Iodoacetamide derivative MOD:00397 iodoacetamide derivatized residue A protein modification that is produced by reaction with iodoacetamide, usually replacement of a reactive hydrogen with a methylcarboxamido group. PubMed:11327326 PubMed:11510821 PubMed:12422359 Unimod:4 Carbamidomethyl Iodoacetamide derivative A protein modification that effectively replaces a hydrogen atom with a carbamoyl (carboxamido) group. Replacement of an amino hydrogen produces a ureido group. 43.02 C 1 H 1 N 1 O 1 43.005814 X Unimod:5 Carbamylation PSI-MOD Carbamyl Carbamylation MOD:00398 This modification can be produced by hydrogen cyanate, either used as a reagent or as released by urea degradation in solution [JSG]. carbamoylated residue A protein modification that effectively replaces a hydrogen atom with a carbamoyl (carboxamido) group. Replacement of an amino hydrogen produces a ureido group. DeltaMass:56 PubMed:10978403 PubMed:12203680 Unimod:5 Carbamylation Carbamyl Carbamylation A protein modification that is produced by reaction with iodoacetic acid, usually replacement of a reactive hydrogen with a methylcarboxy group. 58.04 C 2 H 2 O 2 58.005478 X artifact Unimod:6 Carboxymethyl (on Cysteine) PSI-MOD Carboxymethyl Iodoacetic acid derivative MOD:00399 From DeltaMass: Average Mass: 58 Abbreviation:CmC Average Mass Change:58 Notes:Cysteine reacts with iodoacetic acid to produce carboxymethyl cysteine. iodoacetic acid derivatized residue A protein modification that is produced by reaction with iodoacetic acid, usually replacement of a reactive hydrogen with a methylcarboxy group. DeltaMass:64 Unimod:6 Carboxymethyl (on Cysteine) Carboxymethyl Iodoacetic acid derivative A protein modification that effectively replaces a carboxamido group with a carboxyl group, with both a gain of oxygen and loss of a nitrogen and a hydrogen. 0.98 H -1 N -1 O 1 0.984016 X Unimod:7 Deamidation of Asparagine and Glutamine to Aspartate and Glutamate dNRes deamidationkq PSI-MOD Deamidated Deamidation MOD:00400 From DeltaMass: References:Vish Katta. deamidated residue A protein modification that effectively replaces a carboxamido group with a carboxyl group, with both a gain of oxygen and loss of a nitrogen and a hydrogen. DeltaMass:32 OMSSA:4 Unimod:7 Deamidation of Asparagine and Glutamine to Aspartate and Glutamate dNRes deamidationkq Deamidated Deamidation A protein modification that is produced by formation of an adduct of a cysteine residue with the Gygi isotope-coded affinity tag d0 reagent. 486.63 C 22 H 38 N 4 O 6 S 1 486.25122 C 25 H 43 N 5 O 7 S 2 589.77 589.2604 C artifact Unimod:8 PSI-MOD Gygi ICAT(TM) d0 ICAT-G MOD:00401 Gygi ICAT(TM) d0 modified cysteine A protein modification that is produced by formation of an adduct of a cysteine residue with the Gygi isotope-coded affinity tag d0 reagent. PubMed:10504701 Unimod:8#C Gygi ICAT(TM) d0 ICAT-G A protein modification that is produced by formation of an adduct of a cysteine residue with the Gygi isotope-coded affinity tag d8 reagent. 494.3 C 22 (1)H 30 (2)H 8 N 4 O 6 S 1 494.30142 C 25 (1)H 35 (2)H 8 N 5 O 7 S 2 597.31 597.3106 C artifact Unimod:9 PSI-MOD Gygi ICAT(TM) d8 ICAT-G:2H(8) MOD:00402 Gygi ICAT(TM) d8 modified cysteine A protein modification that is produced by formation of an adduct of a cysteine residue with the Gygi isotope-coded affinity tag d8 reagent. PubMed:10504701 Unimod:9#C Gygi ICAT(TM) d8 ICAT-G:2H(8) A protein modification that effectively converts an L-methionine residue to homoserine. -30.09 C -1 H -2 O 1 S -1 -29.992805 C 4 H 7 N 1 O 2 101.1 101.047676 M artifact C-term Unimod:10 Homoserine formed from Met by CNBr treatment ctermpephsem PSI-MOD Homoserine Met->Hse MOD:00403 Usually formed from methionine by reaction with cyanogen bromide, CNBr, which cleaves the peptide at the methionine carboxyl group and the following residue amino group. homoserine A protein modification that effectively converts an L-methionine residue to homoserine. DeltaMass:113 OMSSA:56 Unimod:10#M Homoserine formed from Met by CNBr treatment ctermpephsem Homoserine Met->Hse A protein modification that effectively converts an L-methionine residue to homoserine lactone. -48.1 C -1 H -4 S -1 -48.003372 C 4 H 5 N 1 O 1 83.09 83.03712 M artifact C-term Unimod:11 ctermpephselactm PSI-MOD Homoserine lactone Met->Hsl MOD:00404 Usually formed from methionine by reaction with cyanogen bromide, CNBr, which cleaves the peptide at the methionine carboxyl group. Under acid conditions the homoserine dehydrates to form the cyclic lactone. homoserine lactone A protein modification that effectively converts an L-methionine residue to homoserine lactone. DeltaMass:90 OMSSA:57 Unimod:11#M ctermpephselactm Homoserine lactone Met->Hsl A protein modification that is produced by formation of an adduct of a cysteine residue with the Applied Biosystems original isotope-coded affinity tag d8 reagent. 450.28 C 20 (1)H 26 (2)H 8 N 4 O 5 S 1 450.2752 C 23 (1)H 31 (2)H 8 N 5 O 6 S 2 553.28 553.28436 C artifact Unimod:12 PSI-MOD Applied Biosystems original ICAT(TM) d8 ICAT-D:2H(8) MOD:00405 Applied Biosystems original ICAT(TM) d8 modified cysteine A protein modification that is produced by formation of an adduct of a cysteine residue with the Applied Biosystems original isotope-coded affinity tag d8 reagent. Unimod:12#C Applied Biosystems original ICAT(TM) d8 ICAT-D:2H(8) A protein modification that is produced by formation of an adduct of a cysteine residue with the Applied Biosystems original isotope-coded affinity tag d0 reagent. 442.22 C 20 (1)H 34 N 4 O 5 S 1 442.225 C 23 (1)H 39 N 5 O 6 S 2 545.23 545.2342 C artifact Unimod:13 PSI-MOD Applied Biosystems original ICAT(TM) d0 ICAT-D MOD:00406 Applied Biosystems original ICAT(TM) d0 modified cysteine A protein modification that is produced by formation of an adduct of a cysteine residue with the Applied Biosystems original isotope-coded affinity tag d0 reagent. Unimod:13#C Applied Biosystems original ICAT(TM) d0 ICAT-D A protein modification that effectively replaces a carboxyl group with a carboxy methyl ester group. OBSOLETE because Unimod:14 merged with entry 34, remap to MOD:00599. MOD:00599 14.03 C 1 H 2 14.01565 X ResOMe PSI-MOD MOD:00407 residue methyl ester true A protein modification that effectively replaces a carboxyl group with a carboxy methyl ester group. OBSOLETE because Unimod:14 merged with entry 34, remap to MOD:00599. PubMed:18688235 ResOMe A protein modification that effectively replaces a residue amino or imino hydrogen with an acetyl group. 42.04 C 2 H 2 O 1 42.010567 X N-Acetyl N-Acetylation NAcRes PSI-MOD MOD:00408 mono N-acetylated residue A protein modification that effectively replaces a residue amino or imino hydrogen with an acetyl group. PubMed:18688235 N-Acetyl N-Acetylation NAcRes A protein modification that effectively replaces a residue amino group with a formamido group. 28.01 C 1 O 1 27.994915 X NFoRes ntermformyl ntermpepformyl PSI-MOD Formyl MOD:00409 N-formylated residue A protein modification that effectively replaces a residue amino group with a formamido group. OMSSA:44 OMSSA:82 NFoRes ntermformyl ntermpepformyl Formyl A protein modification that effectively converts an L-cysteine residue to S-(N-isopropylcarboxamidomethyl)-L-cysteine. 99.13 C 5 H 9 N 1 O 1 S 0 99.06841 C 8 H 14 N 2 O 2 S 1 202.27 202.0776 C artifact Unimod:17 nipcam PSI-MOD N-isopropylcarboxamidomethyl NIPCAM MOD:00410 S-(N-isopropylcarboxamidomethyl)-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-(N-isopropylcarboxamidomethyl)-L-cysteine. OMSSA:84 PubMed:11465505 PubMed:8465942 Unimod:17#C nipcam N-isopropylcarboxamidomethyl NIPCAM modification from Unimod Isotopic label. OBSOLETE because Unimod:18 is now merged with entry 258 remap to MOD:00581 'single 018 label' MOD:00581 2.0 (16)O -1 (18)O 1 2.004246 X artifact PSI-MOD MOD:00411 A modification from Unimod:18 O18 label true modification from Unimod Isotopic label. OBSOLETE because Unimod:18 is now merged with entry 258 remap to MOD:00581 'single 018 label' PubMed:18688235 modification from Unimod artifact. OBSOLETE because Unimod entry 19 is now merged with Unimod 35 remap to MOD:00425 'monohydroxylated residue'. MOD:00425 16.0 O 1 15.994915 X PSI-MOD MOD:00412 oxidation true modification from Unimod artifact. OBSOLETE because Unimod entry 19 is now merged with Unimod 35 remap to MOD:00425 'monohydroxylated residue'. PubMed:18688235 A protein modification that is produced by reaction of a cysteine residue with biotinyl-iodoacetamidyl-3,6-dioxaoctanediamine. 414.52 C 18 H 30 N 4 O 5 S 1 414.1937 C 21 H 35 N 5 O 6 S 2 517.66 517.2029 C artifact Unimod:20 PSI-MOD Biotinyl-iodoacetamidyl-3,6-dioxaoctanediamine PEO-Iodoacetyl-LC-Biotin MOD:00413 biotinyl-iodoacetamidyl-3,6-dioxaoctanediamine derivatized cysteine A protein modification that is produced by reaction of a cysteine residue with biotinyl-iodoacetamidyl-3,6-dioxaoctanediamine. Unimod:20#C Biotinyl-iodoacetamidyl-3,6-dioxaoctanediamine PEO-Iodoacetyl-LC-Biotin A protein modification that effectively replaces one hydrogen atom of an L-arginine residue with one methyl group. 14.03 C 1 H 2 N 0 O 0 14.01565 C 7 H 14 N 4 O 1 170.22 170.11676 R Unimod:34 Me1Arg N-methyl Arginyl methylr PSI-MOD Methyl MOD:00414 From DeltaMass: formula incorrect, N and O reversed monomethylated L-arginine A protein modification that effectively replaces one hydrogen atom of an L-arginine residue with one methyl group. DeltaMass:215 OMSSA:77 Unimod:34#R Me1Arg N-methyl Arginyl methylr Methyl modification from Unimod - OBSOLETE because Unimod entry 22 is now merged with entry 21 remap to MOD:00696 'phosphorylated residue'. MOD:00696 79.98 H 1 O 3 P 1 79.96633 X artifact PSI-MOD MOD:00415 phosphorylation without neutral loss true modification from Unimod - OBSOLETE because Unimod entry 22 is now merged with entry 21 remap to MOD:00696 'phosphorylated residue'. PubMed:18688235 A change resulting in an alteration of the measured molecular mass of a peptide or protein hydroxyl amino acid phosphorylated promptly followed by secondary loss of a neutral trihydrogen phosphate molecular fragment. -18.02 H -2 O -1 -18.010565 X artifact Unimod:23 PSI-MOD Dehydrated Dehydration MOD:00416 O4-phosphotyrosine does not lose phosphate by this mechanism. Unimod does not provide a citation for this particular modification [JSG]. phosphorylation of an hydroxyl amino acid with prompt loss of phosphate A change resulting in an alteration of the measured molecular mass of a peptide or protein hydroxyl amino acid phosphorylated promptly followed by secondary loss of a neutral trihydrogen phosphate molecular fragment. Unimod:23 Dehydrated Dehydration A protein modification that effectively converts an L-cysteine residue to S-carboxamidoethyl-L-cysteine. 71.08 C 3 H 5 N 1 O 1 S 0 71.03712 C 6 H 10 N 2 O 2 S 1 174.22 174.0463 C artifact Unimod:24 PAM-Cys Propionamide or Acrylamide adduct S-(3-amino-3-oxopropyl)cysteine S-carbamoylethyl-L-cysteine S-propanamide-L-cysteine propionamidec PSI-MOD Acrylamide adduct Propionamide MOD:00417 From DeltaMass: References: Anal. Biochem. Vol 216 No. 1 p131 (citation not found) Notes: Residual acrylamide in SDS gels can label free cysteines to produce propionamido-Cys (also known as PAM-Cys) S-carboxamidoethyl-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-carboxamidoethyl-L-cysteine. DeltaMass:72 OMSSA:5 PubMed:1481983 Unimod:24#C PAM-Cys Propionamide or Acrylamide adduct S-(3-amino-3-oxopropyl)cysteine S-carbamoylethyl-L-cysteine S-propanamide-L-cysteine propionamidec Acrylamide adduct Propionamide A protein modification that effectively replaces a hydrogen atom with an (pyridin-3-yl)acetyl group. 119.12 C 7 H 5 N 1 O 1 119.03712 X artifact Unimod:25 PSI-MOD Pyridylacetyl pyridylacetyl MOD:00418 Produced by reaction with N-[(pyrid-3-yl)acetyl]oxy-succinimide [JSG]. pyridylacetylated residue A protein modification that effectively replaces a hydrogen atom with an (pyridin-3-yl)acetyl group. PubMed:9276974 Unimod:25 Pyridylacetyl pyridylacetyl A protein modification that effectively converts an L-cysteine residue to (R)-5-oxo-1,4-tetrahydrothiazine-3-carboxylic acid. 40.02 C 2 H 0 N 0 O 1 S 0 39.994915 C 5 H 6 N 1 O 2 S 1 144.17 144.01192 C artifact N-term Unimod:26 (R)-5-oxoperhydro-1,4-thiazine-3-carboxylic acid 5-oxothiomorpholine-3-carboxylic acid Otc S-carbamoylmethylcysteine cyclization (N-terminus) PSI-MOD Pyro-carbamidomethyl S-carbamoylmethylcysteine cyclization (N-terminus) MOD:00419 From DeltaMass: A secondary modification affecting peptides with S-carbamoylmethyl-L-cysteine (CamC) at the N-terminus. These exist in enzymatic digests of proteins that have been S-alkylated with iodoacetamide. Cyclization of N-terminal CamC gives a residue of (R)-5-oxoperhydro-1,4-thiazine-3-carboxylic acid. Peptides in which this has occurred become more hydrophobic, and lose 17 Da from the N-terminal residue. (R)-5-oxo-1,4-tetrahydrothiazine-3-carboxylic acid A protein modification that effectively converts an L-cysteine residue to (R)-5-oxo-1,4-tetrahydrothiazine-3-carboxylic acid. DeltaMass:336 PubMed:12643538 Unimod:26#C (R)-5-oxoperhydro-1,4-thiazine-3-carboxylic acid 5-oxothiomorpholine-3-carboxylic acid Otc S-carbamoylmethylcysteine cyclization (N-terminus) Pyro-carbamidomethyl S-carbamoylmethylcysteine cyclization (N-terminus) A protein modification that effectively converts an L-glutamic acid residue to 2-pyrrolidone-5-carboxylic acid. -18.02 C 0 H -2 N 0 O -1 -18.010565 C 5 H 6 N 1 O 2 112.11 112.039856 E artifact N-term Unimod:27 uniprot.ptm:PTM-0262 (2S)-5-oxo-2-pyrrolidinecarboxylic acid 2-oxopyrrolidine-5-carboxylic acid 2-pyrrolidone-5-carboxylic acid 5-oxoproline 5-oxopyrrolidine-2-carboxylic acid 5-pyrrolidone-2-carboxylic acid MOD_RES Pyrrolidone carboxylic acid (Glu) PCA PyrGlu(Glu) Pyroglutamic Acid formed from Glutamic Acid ntermpeppyroe pyroglutamic acid PSI-MOD Glu->pyro-Glu Pyro-glu from E MOD:00420 From DeltaMass: References: The conversion of glutamic acid to pyroglutamic was reported for the beta-amyloid protein. Miller et al. Arch. Biochem. Biophy. (1993) 301, 41-52 [DeltaMass]. The modification in amyloid protein is probably an artifact of treatment with strong acid under anhydrous conditions. Peptides with N-terminal glutamic acid isolated from single cells of Aplysia neurons show partial conversion to pyroglutamic acid, possibly dependent on a temperature sensitive factor [JSG]. 2-pyrrolidone-5-carboxylic acid (Glu) A protein modification that effectively converts an L-glutamic acid residue to 2-pyrrolidone-5-carboxylic acid. DeltaMass:16 OMSSA:109 PubMed:10214721 PubMed:1836357 PubMed:3473473 PubMed:8382902 RESID:AA0031#GLU Unimod:27#E (2S)-5-oxo-2-pyrrolidinecarboxylic acid 2-oxopyrrolidine-5-carboxylic acid 2-pyrrolidone-5-carboxylic acid 5-oxoproline 5-oxopyrrolidine-2-carboxylic acid 5-pyrrolidone-2-carboxylic acid MOD_RES Pyrrolidone carboxylic acid (Glu) PCA PyrGlu(Glu) Pyroglutamic Acid formed from Glutamic Acid ntermpeppyroe pyroglutamic acid Glu->pyro-Glu Pyro-glu from E A protein modification that effectively replaces a residue hydrogen atom on a carbon with a carbohydrate-like group through a glycosidic bond. CGlycoRes PSI-MOD MOD:00421 C-glycosylated residue A protein modification that effectively replaces a residue hydrogen atom on a carbon with a carbohydrate-like group through a glycosidic bond. PubMed:18688235 CGlycoRes A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a morpholine-2-acetyl group. 127.14 C 6 H 9 N 1 O 2 127.06333 X artifact N-term Unimod:29 N-succinimidylmorpholine-2-acetate alpha-amino derivative PSI-MOD N-Succinimidyl-2-morpholine acetate SMA MOD:00422 The Unimod name "N-Succinimidyl-3-morpholine acetate" appears to have been a typographical error [JSG]. alpha-amino morpholine-2-acetylated residue A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a morpholine-2-acetyl group. PubMed:10446193 Unimod:29#N-term N-succinimidylmorpholine-2-acetate alpha-amino derivative N-Succinimidyl-2-morpholine acetate SMA A protein modification that effectively substitutes one sodium atom for one hydrogen atom. 21.98 H -1 Na 1 21.981943 X Unimod:30 Na1Res Sodium PSI-MOD Cation:Na Sodium adduct MOD:00423 monosodium salt A protein modification that effectively substitutes one sodium atom for one hydrogen atom. DeltaMass:0 Unimod:30 Na1Res Sodium Cation:Na Sodium adduct A protein modification that effectively converts an L-cysteine residue to S-pyridylethyl-L-cysteine. 105.14 C 7 H 7 N 1 105.057846 C 10 H 12 N 2 O 1 S 1 208.28 208.06703 C artifact Unimod:31 PECys Pyridylethyl Cystenyl S-pyridinylethyl-L-cysteine spyridylethylc vinylpyridine derivatized cysteine residue PSI-MOD Pyridylethyl S-pyridylethylation MOD:00424 From DeltaMass: Formula:C10H12O2N1S1 (formula incorrect, N and O reversed) Monoisotopic Mass Change:208.067 Average Mass Change:208.286 (mass incorrect, aggregate not delta) References:PE Sciex S-pyridylethyl-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-pyridylethyl-L-cysteine. DeltaMass:253 OMSSA:112 PubMed:11760118 PubMed:626389 PubMed:8297018 PubMed:8783016 Unimod:31#C PECys Pyridylethyl Cystenyl S-pyridinylethyl-L-cysteine spyridylethylc vinylpyridine derivatized cysteine residue Pyridylethyl S-pyridylethylation A protein modification that effectively replaces one hydrogen atom with a hydroxyl group. 16.0 O 1 15.994915 X Unimod:35 Hy1Res PSI-MOD Oxidation Oxidation or Hydroxylation MOD:00425 monohydroxylated residue A protein modification that effectively replaces one hydrogen atom with a hydroxyl group. Unimod:35 Hy1Res Oxidation Oxidation or Hydroxylation A protein modification that effectively replaces a residue hydrogen atom on a sulfur with a carbohydrate-like group through a glycosidic bond. SGlycoRes PSI-MOD MOD:00426 S-glycosylated residue A protein modification that effectively replaces a residue hydrogen atom on a sulfur with a carbohydrate-like group through a glycosidic bond. PubMed:18688235 SGlycoRes A protein modification that effectively replaces a hydrogen atom with a methyl group. MeRes Methylation (N terminus, N epsilon of Lysine, O of Serine, Threonine or C terminus, N of Asparagine) PSI-MOD MOD:00427 From DeltaMass: Average Mass: 14 Average Mass Change:14 References:Methylation of Asparagine (found in phycobiliproteins) Klotz and Glazer (1987) J. Biol. Chem. 262; 17350-17355 methylated residue A protein modification that effectively replaces a hydrogen atom with a methyl group. DeltaMass:36 MeRes Methylation (N terminus, N epsilon of Lysine, O of Serine, Threonine or C terminus, N of Asparagine) A protein modification that effectively replaces two hydrogen atoms with two hydroxyl groups. 32.0 C 0 H 0 N 0 O 2 31.989828 X Unimod:425 Hy2Res PSI-MOD Dioxidation dihydroxy MOD:00428 dihydroxylated residue A protein modification that effectively replaces two hydrogen atoms with two hydroxyl groups. PubMed:12686488 Unimod:425 Hy2Res Dioxidation dihydroxy A protein modification that effectively replaces two hydrogen atoms with two methyl groups. 28.05 C 2 H 4 28.0313 X Unimod:36 Me2Res N,N dimethylation (of Arginine or Lysine) PSI-MOD Dimethyl di-Methylation MOD:00429 For amino-terminal proline residues, dimethylation can effectively only be accomplished with a protonated imino group. This process accounts only for dimethylation and not protonation. The alternative Me2+Res process accounts for both protonation and dimethylation [JSG]. dimethylated residue A protein modification that effectively replaces two hydrogen atoms with two methyl groups. DeltaMass:0 PubMed:12964758 PubMed:14570711 Unimod:36 Me2Res N,N dimethylation (of Arginine or Lysine) Dimethyl di-Methylation A protein modification that effectively replaces three hydrogen atoms with three methyl groups. 42.08 C 3 H 6 42.04695 X Unimod:37 Me3Res PSI-MOD Trimethyl tri-Methylation MOD:00430 For amino acids residues, amine trimethylation can effectively only be accomplished with an aminium, protonated primary amino, group. This process accounts only for trimethylation and not protonation. The alternative Me3+Res process accounts for both protonation and trimethylation. trimethylated residue A protein modification that effectively replaces three hydrogen atoms with three methyl groups. PubMed:12590383 PubMed:3145979 PubMed:4304194 PubMed:6778808 PubMed:7093227 PubMed:8453381 Unimod:37 Me3Res Trimethyl tri-Methylation Covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid residue with a secondary loss of a neutral molecular fragment. NLModRes PSI-MOD MOD:00431 modified residue with a secondary neutral loss Covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid residue with a secondary loss of a neutral molecular fragment. PubMed:18688235 NLModRes Covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid residue with a secondary loss of a neutral trihydrogen phosphate molecular fragment. dPhosModRes PSI-MOD MOD:00432 modified residue with neutral loss of phosphate Covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid residue with a secondary loss of a neutral trihydrogen phosphate molecular fragment. PubMed:18688235 dPhosModRes A protein modification that effectively replaces a hydrogen atom with an glucose group through a glycosidic bond. 162.14 C 6 H 10 N 0 O 5 162.05283 X GlcRes PSI-MOD MOD:00433 monoglucosylated residue A protein modification that effectively replaces a hydrogen atom with an glucose group through a glycosidic bond. PubMed:18688235 GlcRes A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a hexose sugar group through a glycosidic bond. X natural Unimod:41 Hex Hexoses (Fru, Gal, Glc, Man) O-Glycosyl- PSI-MOD Hex Hexose MOD:00434 From DeltaMass: Average Mass: 162 Formula:C6 H10 05 Monoisotopic Mass Change:162.053 Average Mass Change:162.143 References:PE Sciex. hexosylated residue A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a hexose sugar group through a glycosidic bond. DeltaMass:203 PubMed:15279557 Unimod:41 Hex Hexoses (Fru, Gal, Glc, Man) O-Glycosyl- Hex Hexose Covalent modification of a peptide or protein amino acid phosphorylated serine with a secondary loss of a neutral trihydrogen phosphate molecular fragment. -97.99 C 0 H -3 N 0 O -4 P -1 -97.9769 C 3 H 3 N 1 O 1 69.06 69.02146 MOD:00046 artifact dPhosOPhosSer PSI-MOD MOD:00435 O-phospho-L-serine with neutral loss of phosphate Covalent modification of a peptide or protein amino acid phosphorylated serine with a secondary loss of a neutral trihydrogen phosphate molecular fragment. PubMed:18688235 dPhosOPhosSer A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with an N-acetylhexosamine group through a glycosidic bond. 203.19 C 8 H 13 N 1 O 5 203.07938 X GNO:G29068FM HexNAc PSI-MOD HexNAc N-Acetylhexosamine MOD:00436 N-acetylhexosaminylated residue A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with an N-acetylhexosamine group through a glycosidic bond. PubMed:18688235 HexNAc HexNAc N-Acetylhexosamine A protein modification that effectively replaces a hydrogen atom with a farnesyl group. 204.36 C 15 H 24 204.1878 X natural Unimod:44 FarnRes Farnesylation PSI-MOD Farnesyl Farnesylation MOD:00437 From DeltaMass: Average Mass: 204 farnesylated residue A protein modification that effectively replaces a hydrogen atom with a farnesyl group. DeltaMass:0 PubMed:15609361 Unimod:44 FarnRes Farnesylation Farnesyl Farnesylation A protein modification that effectively replaces a hydrogen atom with a myristoyl group. 210.36 C 14 H 26 O 1 210.19836 X natural Unimod:45 C14:0 aliphatic acylated residue MyrRes Myristoylation PSI-MOD Myristoyl Myristoylation MOD:00438 From DeltaMass: Average Mass: 210 myristoylated residue A protein modification that effectively replaces a hydrogen atom with a myristoyl group. DeltaMass:0 Unimod:45 C14:0 aliphatic acylated residue MyrRes Myristoylation Myristoyl Myristoylation Covalent modification of a peptide or protein amino acid phosphorylated threonine with a secondary loss of a neutral trihydrogen phosphate molecular fragment. -97.99 C 0 H -3 N 0 O -4 P -1 -97.9769 C 4 H 5 N 1 O 1 83.09 83.03712 MOD:00047 artifact dPhosOPhosThr PSI-MOD MOD:00439 O-phospho-L-threonine with neutral loss of phosphate Covalent modification of a peptide or protein amino acid phosphorylated threonine with a secondary loss of a neutral trihydrogen phosphate molecular fragment. PubMed:18688235 dPhosOPhosThr A protein modification that effectively replaces a hydrogen atom with a palmitoyl group. 238.41 C 16 H 30 O 1 238.22966 X natural Hexadecanoylated residue Palmitoylation PamRes PSI-MOD Palmitoyl Palmitoylation MOD:00440 From DeltaMass: Average Mass: 238 palmitoylated residue A protein modification that effectively replaces a hydrogen atom with a palmitoyl group. DeltaMass:0 Hexadecanoylated residue Palmitoylation PamRes Palmitoyl Palmitoylation A protein modification that effectively replaces a hydrogen atom with a geranylgeranyl group. 272.48 C 20 H 32 272.2504 X natural Unimod:48 Geranylgeranylation GergerRes PSI-MOD Geranyl-geranyl GeranylGeranyl MOD:00441 From DeltaMass: Average Mass: 272 geranylgeranylated residue A protein modification that effectively replaces a hydrogen atom with a geranylgeranyl group. DeltaMass:0 PubMed:15609361 Unimod:48 Geranylgeranylation GergerRes Geranyl-geranyl GeranylGeranyl Covalent modification of a peptide or protein L-arginine residue to protonated omega-N,omega-N'-dimethylated L-arginine with secondary loss of an N,N'-carbodiimide molecular fragment. 42.04 C 1 H 2 N 2 O 0 42.021797 C 7 H 14 N 2 O 1 142.2 142.11061 R artifact dCDI-NNMe2+Arg PSI-MOD MOD:00442 protonated omega-N,omega-N'-dimethylated L-arginine with secondary neutral loss of N,N'-carbodiimide Covalent modification of a peptide or protein L-arginine residue to protonated omega-N,omega-N'-dimethylated L-arginine with secondary loss of an N,N'-carbodiimide molecular fragment. PubMed:15835918 PubMed:18688235 dCDI-NNMe2+Arg Covalent modification of a peptide or protein L-arginine residue to protonated omega-N,omega-N-dimethlyated L-arginine with secondary neutral loss of an N,N-dimethylamine molecular fragment. 59.09 C 2 H 7 N 2 59.060925 C 6 H 10 N 3 O 1 140.17 140.08238 R artifact dDMA-NoMe2+Arg PSI-MOD MOD:00443 protonated omega-N,omega-N-dimethlyated L-arginine with secondary neutral loss of N,N-dimethylamine Covalent modification of a peptide or protein L-arginine residue to protonated omega-N,omega-N-dimethlyated L-arginine with secondary neutral loss of an N,N-dimethylamine molecular fragment. PubMed:15835918 PubMed:18688235 dDMA-NoMe2+Arg A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-S-(sn-1-2,3-dipalmitoyl-glycerol)cysteine. 789.32 C 51 H 96 O 5 788.72577 C 54 H 101 N 1 O 6 S 1 892.46 891.735 C natural N-term Unimod:51 ntermpeptripalmitatec PSI-MOD N-acyl diglyceride cysteine Tripalmitate MOD:00444 N-palmitoyl-S-(sn-1-2,3-dipalmitoyl-glycerol)cysteine A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-S-(sn-1-2,3-dipalmitoyl-glycerol)cysteine. OMSSA:118 PubMed:10356335 Unimod:51 ntermpeptripalmitatec N-acyl diglyceride cysteine Tripalmitate A protein modification that effectively converts an L-lysine residue to L-homoarginine, such as reaction with O-methylisourea. 42.04 C 1 H 2 N 2 42.021797 C 7 H 14 N 4 O 1 170.22 170.11676 K artifact Unimod:52 guanidinationk PSI-MOD Guanidination Guanidinyl MOD:00445 L-homoarginine A protein modification that effectively converts an L-lysine residue to L-homoarginine, such as reaction with O-methylisourea. OMSSA:53 PubMed:11078590 PubMed:11085420 PubMed:11821862 Unimod:52 guanidinationk Guanidination Guanidinyl A protein modification produced by formation of an adduct of a residue with 4-hydroxynonenal. 156.22 C 9 H 16 O 2 156.11504 X artifact Unimod:53 PSI-MOD 4-hydroxynonenal (HNE) HNE MOD:00446 4-hydroxynonenal, a toxic lipid aldehyde, is a product of the hydroperoxide beta-cleavage degradation of omega-6 polyunsaturated fatty acids, such as arachidonic and linoleic acids [JSG]. 4-hydroxynonenal adduct A protein modification produced by formation of an adduct of a residue with 4-hydroxynonenal. PubMed:11327326 PubMed:15133838 Unimod:53 4-hydroxynonenal (HNE) HNE A protein modification that effectively results from forming an adduct with a glucuronic acid either through a carboxyl group amide or ester bond, or through C1-glycosylation. 176.12 C 6 H 8 O 6 176.03209 X Unimod:54 N-Glucuronyl (N terminus) PSI-MOD Glucuronyl N-glucuronylation MOD:00447 N-glucuronylated residue A protein modification that effectively results from forming an adduct with a glucuronic acid either through a carboxyl group amide or ester bond, or through C1-glycosylation. DeltaMass:0 PubMed:7398618 Unimod:54#N-term N-Glucuronyl (N terminus) Glucuronyl N-glucuronylation A protein modification that effectively replaces a hydrogen atom with an N-acetylaminoglucose group through a glycosidic bond. 203.19 C 8 H 13 N 1 O 5 203.07938 X GlcNAcRes PSI-MOD HexNAc MOD:00448 mono-N-acetylaminoglucosylated residue A protein modification that effectively replaces a hydrogen atom with an N-acetylaminoglucose group through a glycosidic bond. PubMed:18688235 GlcNAcRes HexNAc modification from Unimod Isotopic label 45.03 C 2 (1)H -1 (2)H 3 O 1 45.029396 X artifact N-term Unimod:56 PSI-MOD Acetate labeling reagent (N-term & K) (heavy form, +3amu) Acetyl:2H(3) MOD:00449 acetate labeling reagent (N-term) (heavy form, +3amu) modification from Unimod Isotopic label PubMed:11857757 PubMed:11999733 PubMed:12175151 Unimod:56 Acetate labeling reagent (N-term & K) (heavy form, +3amu) Acetyl:2H(3) OBSOLETE because this isotopic label from Unimod entry 57 is deprecated 42.01 C 2 (1)H 2 O 1 42.010567 K artifact PSI-MOD MOD:00450 acetate labeling reagent light form (K) true OBSOLETE because this isotopic label from Unimod entry 57 is deprecated PubMed:11857757 A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a propanoyl group. 56.06 C 3 H 4 O 1 56.026215 X artifact N-term Unimod:58 PSI-MOD Propionate labeling reagent light form (N-term & K) Propionyl MOD:00451 alpha-amino propanoylated residue A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a propanoyl group. PubMed:11857757 PubMed:11999733 PubMed:12175151 Unimod:58#N-term Propionate labeling reagent light form (N-term & K) Propionyl A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a 3x(13)C-labeled propanoyl group. 59.04 (13)C 3 H 4 O 1 59.036278 (12)C 6 (13)C 3 H 16 N 2 O 2 187.13 187.13124 X artifact N-term Unimod:59 PSI-MOD Propionate labeling reagent heavy form (+3amu), N-term & K Propionyl:13C(3) MOD:00452 alpha-amino 3x(13)C-labeled propanoylated residue A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a 3x(13)C-labeled propanoyl group. PubMed:11857757 PubMed:11999733 PubMed:12175151 Unimod:59#N-term Propionate labeling reagent heavy form (+3amu), N-term & K Propionyl:13C(3) A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent light form group. 127.19 C 7 H 13 N 1 O 1 127.09972 X artifact Unimod:60 PSI-MOD GIST-Quat Quaternary amine labeling reagent light form (N-term & K) MOD:00453 quaternary amine labeling reagent light form (N-term & K) A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent light form group. PubMed:11857757 Unimod:60 GIST-Quat Quaternary amine labeling reagent light form (N-term & K) A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent heavy (+3amu) form group. 130.12 C 7 (1)H 10 (2)H 3 N 1 O 1 130.11855 C 13 (1)H 22 (2)H 3 N 3 O 2 258.21 258.2135 X artifact Unimod:61 PSI-MOD GIST-Quat:2H(3) Quaternary amine labeling reagent heavy (+3amu) form, N-term & K MOD:00454 quaternary amine labeling reagent heavy form (+3amu) (N-term & K) A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent heavy (+3amu) form group. PubMed:11857757 Unimod:61 GIST-Quat:2H(3) Quaternary amine labeling reagent heavy (+3amu) form, N-term & K A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent heavy (+6amu) form group. 133.14 C 7 H 7 (2)H 6 N 1 O 1 133.13737 X artifact Unimod:62 PSI-MOD GIST-Quat:2H(6) Quaternary amine labeling reagent heavy form (+6amu), N-term & K MOD:00455 quaternary amine labeling reagent heavy form (+6amu) (N-term & K) A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent heavy (+6amu) form group. PubMed:11857757 Unimod:62 GIST-Quat:2H(6) Quaternary amine labeling reagent heavy form (+6amu), N-term & K A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent heavy (+9amu) form group. 136.16 C 7 (1)H 4 (2)H 9 N 1 O 1 136.1562 C 13 (1)H 16 (2)H 9 N 3 O 2 264.25 264.25116 X artifact Unimod:63 PSI-MOD GIST-Quat:2H(9) Quaternary amine labeling reagent heavy form (+9amu), N-term & K MOD:00456 quaternary amine labeling reagent heavy form (+9amu) (N-term & K) A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent heavy (+9amu) form group. PubMed:11857757 Unimod:63 GIST-Quat:2H(9) Quaternary amine labeling reagent heavy form (+9amu), N-term & K A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a light succinyl group. 100.03 (12)C 4 (1)H 4 O 3 100.016045 X natural N-term Unimod:64 PSI-MOD Succinic anhydride labeling reagent light form (N-term) Succinyl MOD:00457 4x(12)C, 4x(1)H labeled alpha-amino succinylated residue A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a light succinyl group. PubMed:11857757 PubMed:12175151 Unimod:64#N-term Succinic anhydride labeling reagent light form (N-term) Succinyl A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a 4x(2)H labeled succinyl group. 104.04 C 4 (2)H 4 O 3 104.04115 X artifact N-term Unimod:65 PSI-MOD Succinic anhydride labeling reagent, heavy form (+4amu, 4H2), N-term Succinyl:2H(4) MOD:00458 4x(2)H labeled alpha-amino succinylated residue A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a 4x(2)H labeled succinyl group. PubMed:11857757 PubMed:12175151 Unimod:65#N-term Succinic anhydride labeling reagent, heavy form (+4amu, 4H2), N-term Succinyl:2H(4) A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a 4x(13)C labeled succinyl group. 104.03 (13)C 4 H 4 O 3 104.029465 X Unimod:66 PSI-MOD Succinic anhydride labeling reagent, heavy form (+4amu, 4C13), N-term & K Succinyl:13C(4) MOD:00459 4x(13)C labeled alpha-amino succinylated residue A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a 4x(13)C labeled succinyl group. PubMed:11857757 PubMed:12175151 Unimod:66#N-term Succinic anhydride labeling reagent, heavy form (+4amu, 4C13), N-term & K Succinyl:13C(4) A protein modification that effectively trioxygenates an L-cysteine residue to L-cysteine sulfonic acid. 48.0 C 0 H 0 N 0 O 3 S 0 47.984745 C 3 H 5 N 1 O 4 S 1 151.14 150.99393 C artifact Unimod:345 uniprot.ptm:PTM-0634 (2R)-2-amino-3-sulfopropanoic acid 2-amino-2-carboxyethanesulfonic acid 2-azanyl-3-sulfopropanoic acid 3-sulfoalanine Cya CysO3H Cysteic acid, oxidation of cysteine L-cysteine sulfonic acid MOD_RES Cysteine sulfonic acid (-SO3H) cysteic acid cysteicacidc cysteine sulphonic acid PSI-MOD Trioxidation cysteine oxidation to cysteic acid MOD:00460 From DeltaMass: Notes:Treatment of cysteine by strongly oxidising reagents such as performic acid results in the complete oxidation of the sulphur atom. Such treatment is often carried out prior to amino acid analysis as the resulting cysteic acid is then resistant to acid degradation during the hydrolysis procedure. L-cysteic acid (L-cysteine sulfonic acid) A protein modification that effectively trioxygenates an L-cysteine residue to L-cysteine sulfonic acid. ChEBI:17285 DeltaMass:334 OMSSA:34 PubMed:14678012 PubMed:18306178 PubMed:19522542 PubMed:9252331 RESID:AA0556 Unimod:345#C (2R)-2-amino-3-sulfopropanoic acid 2-amino-2-carboxyethanesulfonic acid 2-azanyl-3-sulfopropanoic acid 3-sulfoalanine Cya CysO3H Cysteic acid, oxidation of cysteine L-cysteine sulfonic acid MOD_RES Cysteine sulfonic acid (-SO3H) cysteic acid cysteicacidc cysteine sulphonic acid Trioxidation cysteine oxidation to cysteic acid A protein modification that effectively substitutes a nitrite (NO2) group for a hydrogen atom. 45.0 H -1 N 1 O 2 44.985077 X Unimod:354 Nitro (NO2) PSI-MOD Nitro Oxidation to nitro MOD:00461 Note, this is often misrepresented as the introduction of a nitrate (NO3) group [JSG]. nitrated residue A protein modification that effectively substitutes a nitrite (NO2) group for a hydrogen atom. DeltaMass:0 PubMed:8839040 PubMed:9252331 Unimod:354 Nitro (NO2) Nitro Oxidation to nitro A protein modification that effectively converts an L-tryptophan residue to L-kynurenine. 3.99 C -1 O 1 3.994915 C 10 H 10 N 2 O 2 190.2 190.07423 W artifact Unimod:351 (2S)-2-amino-4-(2-aminophenyl)-4-oxo-butanoic acid kynureninw PSI-MOD Trp->Kynurenin tryptophan oxidation to kynurenin MOD:00462 L-kynurenine A protein modification that effectively converts an L-tryptophan residue to L-kynurenine. DeltaMass:357 OMSSA:66 PubMed:11029593 PubMed:9252331 Unimod:351#W (2S)-2-amino-4-(2-aminophenyl)-4-oxo-butanoic acid kynureninw Trp->Kynurenin tryptophan oxidation to kynurenin A protein modification that effectively converts an L-tryptophan residue to 3'-hydroxy-L-kynurenine. 19.99 C -1 O 2 19.989828 C 10 H 10 N 2 O 3 206.2 206.06914 W artifact Unimod:350 hydroxykynureninw PSI-MOD Trp->Hydroxykynurenin tryptophan oxidation to hydroxykynurenin MOD:00463 3'-hydroxy-L-kynurenine A protein modification that effectively converts an L-tryptophan residue to 3'-hydroxy-L-kynurenine. OMSSA:58 PubMed:9252331 Unimod:350#W hydroxykynureninw Trp->Hydroxykynurenin tryptophan oxidation to hydroxykynurenin A protein modification that effectively converts an L-tryptophan residue to N'-formyl-L-kynurenine. 32.0 O 2 31.989828 C 11 H 10 N 2 O 3 218.21 218.06914 W artifact Unimod:425 Double oxidation of Trp formylkynureninw PSI-MOD Dioxidation dihydroxy tryptophan oxidation to formylkynurenin MOD:00464 From DeltaMass: References:Willy V. Bienvenut, Catherine Déon, Carla Pasquarello, Jennifer M. Campbell, Jean-Charles Sanchez, Marvin L. Vestal, Denis F. Hochstrasser Matrix-assisted laser desorption/ionization-tandemmass spectrometry with high resolution andsensitivity for identification and characterizationof proteins. Proteomics 2002, 2, 868-876 Notes: A double oxidation of tryptophan for which the N-formylkynurenine (+32) structure can be proposed. Many minor peaks accompanying the main peak might also be attributed to other oxidation products of the tryptophan such as kynurenine (+4), an unknown by-product found in all oxidized tryptophan patterns (+13), hydroxytryptophan (+16), 3-hydroxykynurenine (+20) and hydroxy-N-formylkynurenine (+48). See proposed structures at http://www.abrf.org/images/misc/dmass32.jpg. N'-formyl-L-kynurenine A protein modification that effectively converts an L-tryptophan residue to N'-formyl-L-kynurenine. DeltaMass:356 OMSSA:45 PubMed:12124932 PubMed:12686488 PubMed:9252331 Unimod:425#W Double oxidation of Trp formylkynureninw Dioxidation dihydroxy tryptophan oxidation to formylkynurenin A protein modification that effectively converts an L-phenylalanine residue to a dihydroxyphenylalanine. 32.0 O 2 31.989828 C 9 H 9 N 1 O 3 179.17 179.05824 F artifact Unimod:425 dihydroxyf PSI-MOD Dioxidation dihydroxy MOD:00465 Dihydroxyphenyalanines with a 4'-hydroxyl orginate naturally by a monohydroxylation of tyrosine, and not by dihydroxylation of phenylalanine [JSG]. dihydroxyphenylalanine (Phe) A protein modification that effectively converts an L-phenylalanine residue to a dihydroxyphenylalanine. OMSSA:39 PubMed:1610822 PubMed:1903612 PubMed:3734192 PubMed:9252331 RESID:AA0146#var Unimod:425#F dihydroxyf Dioxidation dihydroxy A protein modification that effectively converts a residue to a glycosylsphingolipidinositolethanolamidated. GSIRes PSI-MOD MOD:00466 glycosylsphingolipidinositolated residue A protein modification that effectively converts a residue to a glycosylsphingolipidinositolethanolamidated. PubMed:12626404 PubMed:18688235 PubMed:8404891 GSIRes A protein modification that effectively substitutes an iminobiotinyl group for a hydrogen atom. 225.31 C 10 H 15 N 3 O 1 S 1 225.09358 X artifact Unimod:89 PSI-MOD Iminobiotin Iminobiotinylation MOD:00467 iminobiotinyl modified residue A protein modification that effectively substitutes an iminobiotinyl group for a hydrogen atom. PubMed:9750125 Unimod:89 Iminobiotin Iminobiotinylation modification from Unimod Isotopic label 338.47 C 16 H 26 N 4 O 2 S 1 338.17764 X artifact Unimod:90 PSI-MOD ESP ESP-Tag light d0 MOD:00468 ESP-Tag light d0 modification from Unimod Isotopic label Unimod:90 ESP ESP-Tag light d0 modification from Unimod Isotopic label 348.24 C 16 (1)H 16 (2)H 10 N 4 O 2 S 1 348.24042 X artifact Unimod:91 PSI-MOD ESP-Tag heavy d10 ESP:2H(10) MOD:00469 ESP-Tag heavy d10 modification from Unimod Isotopic label Unimod:91 ESP-Tag heavy d10 ESP:2H(10) modification from Unimod Chemical derivative 339.45 C 16 H 25 N 3 O 3 S 1 339.16165 X artifact Unimod:92 PSI-MOD NHS-LC-Biotin MOD:00470 NHS-LC-Biotin modification from Unimod Chemical derivative Unimod:92 NHS-LC-Biotin NHS-LC-Biotin modification from Unimod Chemical derivative 601.8 C 25 H 39 N 5 O 6 S 3 601.20624 X artifact Unimod:93 PSI-MOD EDT-maleimide-PEO-biotin MOD:00471 EDT-maleimide-PEO-biotin modification from Unimod Chemical derivative Unimod:93 EDT-maleimide-PEO-biotin EDT-maleimide-PEO-biotin modification from Unimod Isotopic label 68.04 C 3 (1)H 4 N 2 68.037445 C 9 H 16 N 4 O 1 196.13 196.13242 K artifact Unimod:94 PSI-MOD IMID IMID d0 MOD:00472 IMID d0 modification from Unimod Isotopic label PubMed:11746907 URL:http://dx.doi.org/10.1002/rcm.517 Unimod:94 IMID IMID d0 modification from Unimod Isotopic label 72.06 C 3 (2)H 4 N 2 72.06255 C 9 (1)H 12 (2)H 4 N 4 O 1 200.16 200.15752 K artifact Unimod:95 PSI-MOD IMID d4 IMID:2H(4) MOD:00473 IMID d4 modification from Unimod Isotopic label PubMed:11746907 URL:http://dx.doi.org/10.1002/rcm.517 Unimod:95 IMID d4 IMID:2H(4) A protein modification that effectively converts an L-cysteine residue to S-(1,1,2-(2)H3)-propanamide-L-cysteine. 74.06 C 3 (1)H 2 (2)H 3 N 1 O 1 74.05595 C 6 (1)H 7 (2)H 3 N 2 O 2 S 1 177.07 177.06512 C artifact Unimod:97 S-([1,1,2-(2)H3]-3-amino-3-oxopropyl)cysteine S-([1,1,2-(2)H3]-carbamoylethyl)-L-cysteine S-([1,1,2-(2)H3]-propanamide)-L-cysteine PSI-MOD Acrylamide d3 Propionamide:2H(3) MOD:00474 S-([1,1,2-(2)H3]-carboxamidoethyl)-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-(1,1,2-(2)H3)-propanamide-L-cysteine. Unimod:97#C S-([1,1,2-(2)H3]-3-amino-3-oxopropyl)cysteine S-([1,1,2-(2)H3]-carbamoylethyl)-L-cysteine S-([1,1,2-(2)H3]-propanamide)-L-cysteine Acrylamide d3 Propionamide:2H(3) A protein modification that effectively converts an L-tyrosine residue to 2-amino-L-tyrosine. 15.02 H 1 N 1 15.010899 C 9 H 10 N 2 O 2 178.19 178.07423 Y artifact Unimod:342 PSI-MOD Amino Tyrosine oxidation to 2-aminotyrosine MOD:00475 2-amino-L-tyrosine A protein modification that effectively converts an L-tyrosine residue to 2-amino-L-tyrosine. PubMed:8839040 PubMed:9252331 Unimod:342#Y Amino Tyrosine oxidation to 2-aminotyrosine A protein modification that effectively replaces a hydrogen atom with an galactose group through a glycosidic bond. 162.14 C 6 H 10 O 5 162.05283 X natural GalRes PSI-MOD MOD:00476 monogalactosylated residue A protein modification that effectively replaces a hydrogen atom with an galactose group through a glycosidic bond. PubMed:18688235 GalRes A protein modification that effectively converts, by oxidative decarboxylation, an L-proline residue to 2-pyrrolidone with breakage of the peptide chain. -13.02 C -1 H -1 N 0 O 0 -13.007825 C 4 H 6 N 1 O 1 84.1 84.04494 P artifact Unimod:360 PSI-MOD Pro->Pyrrolidinone Proline oxidation to pyrrolidinone MOD:00477 The oxidative decarboxylation of a proline residue results in breaking of the peptide chain, leaving a peptidyl-2-pyrrolidone at the C-terminus. The difference formula, derived from the result in the original citation, has been corrected from the Unimod entry. 2-pyrrolidone A protein modification that effectively converts, by oxidative decarboxylation, an L-proline residue to 2-pyrrolidone with breakage of the peptide chain. PubMed:2161657 PubMed:9252331 Unimod:360#P Pro->Pyrrolidinone Proline oxidation to pyrrolidinone A protein modification that effectively converts an L-proline residue to L-glutamyl semialdehyde. 16.0 C 0 H 0 N 0 O 1 15.994915 C 5 H 7 N 1 O 2 113.12 113.047676 P artifact Unimod:35 Oxidation of proline to gamma-glutamyl semialdehyde gamma-glutamyl semialdehyde glutamyl 5-semialdehyde glutamyl aldehyde PSI-MOD Oxidation Oxidation or Hydroxylation MOD:00478 glutamyl semialdehyde (Pro) A protein modification that effectively converts an L-proline residue to L-glutamyl semialdehyde. DeltaMass:354 PubMed:11120890 PubMed:2563380 PubMed:9252331 Unimod:35#P Oxidation of proline to gamma-glutamyl semialdehyde gamma-glutamyl semialdehyde glutamyl 5-semialdehyde glutamyl aldehyde Oxidation Oxidation or Hydroxylation A protein modification that effectively converts an L-arginine residue to L-glutamyl semialdehyde. -43.07 C -1 H -5 N -3 O 1 -43.053432 C 5 H 7 N 1 O 2 113.12 113.047676 R artifact Unimod:344 Oxidation of arginine (to glutamic acid) PSI-MOD Arg->GluSA Arginine oxidation to glutamic semialdehyde MOD:00479 From DeltaMass: Average Mass: -27 Monoisotopic Mass Change:-27.06 Average Mass Change:-27.07 References:Amici A, Levine, RL, Tsai, L, and Stadtman, ER: Conversion of amino acid residues in proteins and amino acid homopolymers to carbonyl derivatives by metal-catalyzed oxidation reactions. Journal of Biological Chemistry 264: 3341-3346 1989.Requena JR, Chao CC, Levine RL, and Stadtman ER: Glutamic and aminoadipic semialdehydes are the main carbonyl products of metal-catalyzed oxidation of proteins. Proceedings of the National Academy of Sciences USA 98: 69-74 2001. glutamyl semialdehyde (Arg) A protein modification that effectively converts an L-arginine residue to L-glutamyl semialdehyde. DeltaMass:351 PubMed:11120890 PubMed:1680314 PubMed:9252331 Unimod:344#R Oxidation of arginine (to glutamic acid) Arg->GluSA Arginine oxidation to glutamic semialdehyde modification from Unimod Isotopic label 227.26 C 10 H 17 N 3 O 3 227.12698 C 13 H 22 N 4 O 4 S 1 330.4 330.13617 C artifact Unimod:105 icatlight PSI-MOD Applied Biosystems cleavable ICAT(TM) light ICAT-C MOD:00480 Applied Biosystems cleavable ICAT(TM) light modification from Unimod Isotopic label OMSSA:129 URL:http://www.appliedbiosystems.com/products/productdetail.cfm?prod_id=153 Unimod:105#C icatlight Applied Biosystems cleavable ICAT(TM) light ICAT-C modification from Unimod Isotopic label 236.16 (12)C 1 (13)C 9 H 17 N 3 O 3 236.15718 (12)C 4 (13)C 9 H 22 N 4 O 4 S 1 339.17 339.16638 C artifact Unimod:106 icatheavy PSI-MOD Applied Biosystems cleavable ICAT(TM) heavy ICAT-C:13C(9) MOD:00481 Applied Biosystems cleavable ICAT(TM) heavy modification from Unimod Isotopic label OMSSA:130 URL:http://www.appliedbiosystems.com/products/productdetail.cfm?prod_id=153 Unimod:106#C icatheavy Applied Biosystems cleavable ICAT(TM) heavy ICAT-C:13C(9) A protein modification that effectively converts an L-methionine residue to N-formyl-L-methionine (not known as a natural, post-translational modification process). 28.01 C 1 H 0 N 0 O 1 S 0 27.994915 C 6 H 10 N 1 O 2 S 1 160.21 160.04323 M artifact N-term Unimod:122 uniprot.ptm:PTM-0212 (2S)-2-formylamino-4-(methylsulfanyl)butanoic acid 2-formamido-4-(methylsulfanyl)butanoic acid 2-formylamino-4-(methylthio)butanoic acid 2-formylazanyl-4-(methylsulfanyl)butanoic acid MOD_RES N-formylmethionine N-formyl-L-methionine N-formylated L-methionine NFoMet PSI-MOD MOD:00482 This entry is for the artifactual formation of N-formyl-L-methionine from methionine. For encoded N-formyl-L-methionine, use MOD:00030 [JSG]. N-formyl-L-methionine (Met) A protein modification that effectively converts an L-methionine residue to N-formyl-L-methionine (not known as a natural, post-translational modification process). PubMed:11152118 PubMed:2165784 PubMed:3042771 RESID:AA0021#MET Unimod:122#M (2S)-2-formylamino-4-(methylsulfanyl)butanoic acid 2-formamido-4-(methylsulfanyl)butanoic acid 2-formylamino-4-(methylthio)butanoic acid 2-formylazanyl-4-(methylsulfanyl)butanoic acid MOD_RES N-formylmethionine N-formyl-L-methionine N-formylated L-methionine NFoMet A protein modification that is produced by reaction with N-ethylmaleimide. 125.13 C 6 H 7 N 1 O 2 125.047676 C 9 H 12 N 2 O 3 S 1 228.27 228.05687 C artifact Unimod:108 nemc PSI-MOD N-ethylmaleimide on cysteines Nethylmaleimide MOD:00483 N-ethylmaleimide derivatized cysteine A protein modification that is produced by reaction with N-ethylmaleimide. OMSSA:83 PubMed:11813307 PubMed:12777388 Unimod:108#C nemc N-ethylmaleimide on cysteines Nethylmaleimide modification from Unimod Chemical derivative 354.47 C 16 H 26 N 4 O 3 S 1 354.17258 C 22 H 38 N 6 O 4 S 1 482.64 482.26752 K artifact Unimod:112 PSI-MOD OxLysBiotinRed Oxidized lysine biotinylated with biotin-LC-hydrazide, reduced MOD:00484 oxidized lysine biotinylated with biotin-LC-hydrazide, reduced modification from Unimod Chemical derivative Unimod:112#K OxLysBiotinRed Oxidized lysine biotinylated with biotin-LC-hydrazide, reduced modification from Unimod Chemical derivative 352.45 C 16 H 24 N 4 O 3 S 1 352.15692 C 22 H 36 N 6 O 4 S 1 480.63 480.25186 K artifact Unimod:113 PSI-MOD OxLysBiotin Oxidized lysine biotinylated with biotin-LC-hydrazide MOD:00485 oxidized lysine biotinylated with biotin-LC-hydrazide modification from Unimod Chemical derivative Unimod:113#K OxLysBiotin Oxidized lysine biotinylated with biotin-LC-hydrazide modification from Unimod Chemical derivative 371.5 C 16 H 29 N 5 O 3 S 1 371.1991 C 21 H 36 N 6 O 4 S 1 468.62 468.25186 P artifact Unimod:114 PSI-MOD OxProBiotinRed Oxidized proline biotinylated with biotin-LC-hydrazide, reduced MOD:00486 oxidized proline biotinylated with biotin-LC-hydrazide, reduced modification from Unimod Chemical derivative Unimod:114#C OxProBiotinRed Oxidized proline biotinylated with biotin-LC-hydrazide, reduced modification from Unimod Chemical derivative 369.48 C 16 H 27 N 5 O 3 S 1 369.18347 C 21 H 34 N 6 O 4 S 1 466.6 466.23624 P artifact Unimod:115 PSI-MOD OxProBiotin Oxidized Proline biotinylated with biotin-LC-hydrazide MOD:00487 oxidized proline biotinylated with biotin-LC-hydrazide modification from Unimod Chemical derivative Unimod:115#C OxProBiotin Oxidized Proline biotinylated with biotin-LC-hydrazide modification from Unimod Chemical derivative 310.41 C 15 H 22 N 2 O 3 S 1 310.1351 C 21 H 34 N 6 O 4 S 1 466.6 466.23624 R artifact PSI-MOD OxArgBiotin Oxidized arginine biotinylated with biotin-LC-hydrazide MOD:00488 oxidized arginine biotinylated with biotin-LC-hydrazide modification from Unimod Chemical derivative Unimod:116#C OxArgBiotin Oxidized arginine biotinylated with biotin-LC-hydrazide modification from Unimod Chemical derivative 312.43 C 15 H 24 N 2 O 3 S 1 312.15076 C 21 H 36 N 6 O 4 S 1 468.62 468.25186 R artifact Unimod:117 PSI-MOD OxArgBiotinRed Oxidized arginine biotinylated with biotin-LC-hydrazide, reduced MOD:00489 oxidized arginine biotinylated with biotin-LC-hydrazide, reduced modification from Unimod Chemical derivative Unimod:117#C OxArgBiotinRed Oxidized arginine biotinylated with biotin-LC-hydrazide, reduced modification from Unimod Chemical derivative 490.7 C 20 H 34 N 4 O 4 S 3 490.17422 X Unimod:118 PSI-MOD EDT-iodo-PEO-biotin EDT-iodoacetyl-PEO-biotin MOD:00490 EDT-iodo-PEO-biotin modification from Unimod Chemical derivative Unimod:118 EDT-iodo-PEO-biotin EDT-iodoacetyl-PEO-biotin modification from Unimod Chemical derivative 316.38 C 22 H 21 P 1 316.1381 C 25 H 26 N 1 O 1 P 1 S 1 419.52 419.14728 C artifact Unimod:119 PSI-MOD IBTP Thio Ether Formation - BTP Adduct MOD:00491 thio ether formation - BTP Adduct modification from Unimod Chemical derivative PubMed:11861642 Unimod:119#C IBTP Thio Ether Formation - BTP Adduct A protein modification that crosslinks the N6-amino of a peptidyl lysine with the carboxyl of glycylglycine, the two glycine residues left after tryptic digestion of ubiquitin. 114.1 C 4 H 6 N 2 O 2 114.04293 C 10 H 18 N 4 O 3 242.28 242.1379 K artifact Unimod:121 N6-(glycylglycyl)lysine N6-glycylglycyl-L-lysine glyglyk PSI-MOD GlyGly ubiquitinylation residue MOD:00492 ubiquitination signature dipeptidyl lysine A protein modification that crosslinks the N6-amino of a peptidyl lysine with the carboxyl of glycylglycine, the two glycine residues left after tryptic digestion of ubiquitin. OMSSA:52 PubMed:11125103 PubMed:12612601 PubMed:12872131 RESID:AA0125#var Unimod:121#K N6-(glycylglycyl)lysine N6-glycylglycyl-L-lysine glyglyk GlyGly ubiquitinylation residue A protein modification that effectively replaces a hydrogen atom with a formyl group. 28.01 C 1 O 1 27.994915 X Unimod:122 FoRes Formylation (CHO) PSI-MOD Formyl Formylation MOD:00493 From DeltaMass: Average Mass: 28 formylated residue A protein modification that effectively replaces a hydrogen atom with a formyl group. DeltaMass:0 PubMed:15799070 Unimod:122 FoRes Formylation (CHO) Formyl Formylation modification from Unimod Isotopic label 345.78 C 15 Cl 1 H 20 N 1 O 6 S 0 345.0979 C 18 Cl 1 H 25 N 2 O 7 S 1 448.91 448.1071 C artifact Unimod:123 PSI-MOD ICAT-H N-iodoacetyl, p-chlorobenzyl-12C6-glucamine MOD:00494 N-iodoacetyl, p-chlorobenzyl-12C6-glucamine modification from Unimod Isotopic label PubMed:12185208 Unimod:123#C ICAT-H N-iodoacetyl, p-chlorobenzyl-12C6-glucamine modification from Unimod Isotopic label 351.12 (12)C 9 (13)C 6 Cl 1 H 20 N 1 O 6 S 0 351.11804 (12)C 12 (13)C 6 Cl 1 H 25 N 2 O 7 S 1 454.13 454.12723 C artifact Unimod:124 PSI-MOD ICAT-H:13C(6) N-iodoacetyl, p-chlorobenzyl-13C6-glucamine MOD:00495 N-iodoacetyl, p-chlorobenzyl-13C6-glucamine modification from Unimod Isotopic label PubMed:12185208 Unimod:124#C ICAT-H:13C(6) N-iodoacetyl, p-chlorobenzyl-13C6-glucamine OBSOLETE because Unimod entry 125 is merged with entry 199, remap to id: MOD:00552 MOD:00552 32.06 C 2 (2)H 4 32.056408 K artifact Unimod:125 PSI-MOD MOD:00496 reductive amination-D true OBSOLETE because Unimod entry 125 is merged with entry 199, remap to id: MOD:00552 Unimod:125 modification from Unimod [(35)S]dithiobis(succinimidyl propionate) crosslinking 88.12 C 3 H 4 O 1 S 1 87.99828 C 9 H 16 N 2 O 2 S 1 216.3 216.09325 K artifact Unimod:126 PSI-MOD 3,3-Dithio-bis-(sulfosuccinimidyl)propionate 3-sulfanylpropanoyl Thioacyl MOD:00497 The name "thioacylation of primary amines" in Unimod was a misdescription [JSG]. 3-sulfanylpropanoyl (N-term and Lys) modification from Unimod [(35)S]dithiobis(succinimidyl propionate) crosslinking PubMed:957432 Unimod:126 3,3-Dithio-bis-(sulfosuccinimidyl)propionate 3-sulfanylpropanoyl Thioacyl A protein modification that effectively substitutes a hydrogen of a residue with a fluorine atom. X artifact FRes Fluorophenylalanyl PSI-MOD Fluoro fluorophenylalanine replacement of phenylalanine MOD:00498 fluorinated residue A protein modification that effectively substitutes a hydrogen of a residue with a fluorine atom. PubMed:18688235 FRes Fluorophenylalanyl Fluoro fluorophenylalanine replacement of phenylalanine modification from Unimod Chemical derivative 388.35 C 22 H 14 N 1 O 6 388.08212 C 25 H 19 N 2 O 7 S 1 491.49 491.0913 C artifact Unimod:128 PSI-MOD 5-Iodoacetamidofluorescein (Molecular Probe, Eugene, OR) Fluorescein MOD:00499 5-iodoacetamidofluorescein modification from Unimod Chemical derivative PubMed:3311742 PubMed:3578767 Unimod:128#C 5-Iodoacetamidofluorescein (Molecular Probe, Eugene, OR) Fluorescein A protein modification that effectively substitutes one hydrogen atom of a residue with one iodine atom. 125.9 H -1 I 1 125.896645 X Unimod:129 I1Res Iodination (of Histidine[C4] or Tyrosine[C3]) PSI-MOD Iodination Iodo MOD:00500 From DeltaMass: Average Mass: 126 monoiodinated residue A protein modification that effectively substitutes one hydrogen atom of a residue with one iodine atom. DeltaMass:0 PubMed:15627961 PubMed:2026710 Unimod:129 I1Res Iodination (of Histidine[C4] or Tyrosine[C3]) Iodination Iodo A protein modification that effectively substitutes two hydrogen atoms of a residue with two iodine atoms. 251.79 H -2 I 2 251.79329 X Unimod:130 I2Res PSI-MOD Diiodo di-Iodination MOD:00501 From DeltaMass: Average Mass: 252 diiodinated residue A protein modification that effectively substitutes two hydrogen atoms of a residue with two iodine atoms. Unimod:130 I2Res Diiodo di-Iodination A protein modification that effectively substitutes three hydrogen atoms of a residue with three iodine atoms. 377.69 H -3 I 3 377.68994 X artifact Unimod:131 I3Res triiodinationy PSI-MOD Triiodo tri-Iodination MOD:00502 From Unimod. In PubMed:2026710, mono- and diiodination of tyrosine are discussed, but triiodination of tyrosine is not mentioned. In PubMed:15627961, triiodothyronine (see MOD:00186) is discussed, but triiodotyrosine is not mentioned. This modification probably does not exist, and may be a confusion of "tyrosine" for "thyronine", a common error [JSG]. triiodinated residue A protein modification that effectively substitutes three hydrogen atoms of a residue with three iodine atoms. OMSSA:116 PubMed:15627961 PubMed:2026710 Unimod:131 I3Res triiodinationy Triiodo tri-Iodination A protein modification that effectively converts a glycine residue to N-(cis-delta 5)-tetradecaenoylglycine. 208.35 C 14 H 24 N 0 O 1 208.18271 C 16 H 27 N 1 O 2 265.4 265.2042 G natural N-term Unimod:134 N-(C14:1 aliphatic acyl)glycine myristoleylation (one double bond) ntermpepmyristoyeylationg PSI-MOD (cis-delta 5)-tetradecaenoyl Myristoleyl MOD:00503 N-(cis-delta 5)-tetradecaenoylglycine A protein modification that effectively converts a glycine residue to N-(cis-delta 5)-tetradecaenoylglycine. OMSSA:78 PubMed:11955007 PubMed:11955008 PubMed:1326520 PubMed:1386601 PubMed:6436247 PubMed:7543369 RESID:AA0059#var Unimod:134#G N-(C14:1 aliphatic acyl)glycine myristoleylation (one double bond) ntermpepmyristoyeylationg (cis-delta 5)-tetradecaenoyl Myristoleyl A protein modification that effectively converts a glycine residue to N-(cis,cis-delta 5,delta 8)-tetradecadienoylglycine. 206.33 C 14 H 22 O 1 206.16707 C 16 H 25 N 1 O 2 263.38 263.18854 G natural N-term Unimod:135 N-(C14:2 aliphatic acyl)glycine myristoylation-4H (two double bonds) ntermpepmyristoyl4hg PSI-MOD (cis,cis-delta 5, delta 8)-tetradecadienoyl Myristoyl+Delta:H(-4) MOD:00504 N-(cis,cis-delta 5,delta 8)-tetradecadienoylglycine A protein modification that effectively converts a glycine residue to N-(cis,cis-delta 5,delta 8)-tetradecadienoylglycine. OMSSA:79 PubMed:11955007 PubMed:11955008 PubMed:1326520 PubMed:1386601 PubMed:6436247 PubMed:7543369 RESID:AA0059#var Unimod:135#G N-(C14:2 aliphatic acyl)glycine myristoylation-4H (two double bonds) ntermpepmyristoyl4hg (cis,cis-delta 5, delta 8)-tetradecadienoyl Myristoyl+Delta:H(-4) modification from Unimod Isotopic label 104.11 C 7 H 4 O 1 104.026215 X artifact Unimod:136 Benzoyl (Bz) PSI-MOD Benzoyl labeling reagent light form (N-term & K) MOD:00505 From DeltaMass: Average Mass: 104 benzoyl labeling reagent light form (N-term and K) modification from Unimod Isotopic label DeltaMass:0 PubMed:15456300 Unimod:136 Benzoyl (Bz) Benzoyl labeling reagent light form (N-term & K) modification from Unimod N-linked glycosylation, Hex(5) HexNAc(2) 1217.09 C 46 H 76 N 2 O 35 1216.4229 C 50 H 82 N 4 O 37 1331.2 1330.4658 N natural GNO:G02815KT Unimod:137 PSI-MOD Hex(5)HexNAc(2) N-linked glycan core MOD:00506 N-linked glycan core N4-glycosylated asparagine modification from Unimod N-linked glycosylation, Hex(5) HexNAc(2) PubMed:111247 PubMed:1694179 PubMed:5490222 RESID:AA0151#var Unimod:137#N Hex(5)HexNAc(2) N-linked glycan core OBSOLETE because redundant, replaced by MOD:01653. Remap to MOD:01653. MOD:01653 233.29 C 12 H 11 N 1 O 2 S 1 233.05106 X artifact Unimod:139 Dansyl (Dns) PSI-MOD 5-dimethylaminonaphthalene-1-sulfonyl Dansyl MOD:00507 From DeltaMass: Average Mass: 233 5-dimethylaminonaphthalene-1-sulfonyl true OBSOLETE because redundant, replaced by MOD:01653. Remap to MOD:01653. DeltaMass:0 Unimod:139 Dansyl (Dns) 5-dimethylaminonaphthalene-1-sulfonyl Dansyl OBSOLETE because this is an ion type and is not a biological or chemical modification to a polypeptide, can be handled by PSI-MS CV term, MS:1001229 X artifact C-term Unimod:140 PSI-MOD ISD a-series (C-Term) a-type-ion MOD:00508 Virtual Modification for MS/MS of a-type ions, by decarboxylation of C-terminus as reaction inside the mass spectrometer. ISD a-series (C-Term) true OBSOLETE because this is an ion type and is not a biological or chemical modification to a polypeptide, can be handled by PSI-MS CV term, MS:1001229 PubMed:14588022 Unimod:140 ISD a-series (C-Term) a-type-ion modification from Unimod Chemical derivative 41.05 C 2 H 3 N 1 41.02655 X artifact Unimod:141 PSI-MOD Amidine amidination of lysines or N-terminal amines with methyl acetimidate MOD:00509 amidination of lysines or N-terminal amines with methyl acetimidate modification from Unimod Chemical derivative PubMed:12643539 PubMed:6273432 Unimod:141 Amidine amidination of lysines or N-terminal amines with methyl acetimidate modification from Unimod N-linked glycosylation, dHex HexNAc 349.34 C 14 H 23 N 1 O 9 349.13727 C 18 H 29 N 3 O 11 463.44 463.1802 N natural GNO:G00194GV Unimod:142 dHexHexNAcN PSI-MOD HexNAc(1)dHex(1) HexNAc1dHex1 MOD:00510 HexNAc1dHex1 N4-glycosylated asparagine modification from Unimod N-linked glycosylation, dHex HexNAc OMSSA:183 PubMed:111247 PubMed:1694179 PubMed:5490222 RESID:AA0151#var Unimod:142 dHexHexNAcN HexNAc(1)dHex(1) HexNAc1dHex1 modification from Unimod N-linked glycosylation, HexNAc(2) 406.39 C 16 H 26 N 2 O 10 406.15875 C 20 H 32 N 4 O 12 520.49 520.20166 N natural GNO:G27391WQ Unimod:143 PSI-MOD HexNAc(2) HexNAc2 MOD:00511 HexNAc2 N4-glycosylated asparagine modification from Unimod N-linked glycosylation, HexNAc(2) PubMed:111247 PubMed:1694179 PubMed:5490222 RESID:AA0151#var Unimod:143 HexNAc(2) HexNAc2 modification from Unimod N-linked glycosylation, Hex3 486.42 C 18 H 30 O 15 486.15848 C 22 H 36 N 2 O 17 600.53 600.2014 N natural GNO:G39365VM Unimod:144 PSI-MOD Hex(3) Hex3 MOD:00512 Hex3 N4-glycosylated asparagine modification from Unimod N-linked glycosylation, Hex3 PubMed:111247 PubMed:1694179 PubMed:5490222 RESID:AA0151#var Unimod:144 Hex(3) Hex3 modification from Unimod N-linked glycosylation, dHex(2) HexNAc 495.48 C 20 H 33 N 1 O 13 495.1952 C 24 H 39 N 3 O 15 609.58 609.2381 N natural GNO:G74392IM Unimod:145 PSI-MOD HexNAc(1)dHex(2) HexNAc1dHex2 MOD:00513 HexNAc1dHex2 N4-glycosylated asparagine modification from Unimod N-linked glycosylation, dHex(2) HexNAc PubMed:111247 PubMed:1694179 PubMed:5490222 RESID:AA0151#var Unimod:145 HexNAc(1)dHex(2) HexNAc1dHex2 modification from Unimod N-linked glycosylation, dHex Hex HexNAc 511.48 C 20 H 33 N 1 O 14 511.1901 C 24 H 39 N 3 O 16 625.58 625.23303 N natural GNO:G54129SE Unimod:146 PSI-MOD Hex(1)HexNAc(1)dHex(1) Hex1HexNAc1dHex1 MOD:00514 Hex1HexNAc1dHex1 N4-glycosylated asparagine modification from Unimod N-linked glycosylation, dHex Hex HexNAc PubMed:111247 PubMed:1694179 PubMed:5490222 RESID:AA0151#var Unimod:146 Hex(1)HexNAc(1)dHex(1) Hex1HexNAc1dHex1 modification from Unimod N-linked glycosylation, dHex HexNAc(2) 552.53 C 22 H 36 N 2 O 14 552.2167 C 26 H 42 N 4 O 16 666.63 666.2596 N natural GNO:G06042JP Unimod:147 PSI-MOD HexNAc(2)dHex(1) HexNAc2dHex1 MOD:00515 HexNAc2dHex1 N4-glycosylated asparagine modification from Unimod N-linked glycosylation, dHex HexNAc(2) PubMed:111247 PubMed:1694179 PubMed:5490222 RESID:AA0151#var Unimod:147 HexNAc(2)dHex(1) HexNAc2dHex1 modification from Unimod N-linked glycosylation 568.53 C 22 H 36 N 2 O 15 568.21155 C 26 H 42 N 4 O 17 682.63 682.2545 N natural GNO:G58001LT Unimod:148 PSI-MOD Hex(1)HexNAc(2) Hex1HexNAc2 MOD:00516 Hex1HexNAc2 N4-glycosylated asparagine modification from Unimod N-linked glycosylation RESID:AA0151#var Unimod:148 Hex(1)HexNAc(2) Hex1HexNAc2 A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a carbohydrate-like group composed of Hex1HexNAc1NeuAc1 linked through a glycosidic bond. 657.6 C 25 H 41 N 2 O 18 657.2354 X natural GNO:G17015OC NeuAc-Hex-HexNAc PSI-MOD Hex(1)HexNAc(1)NeuAc(1) Hex1HexNAc1NeuAc1 MOD:00517 From DeltaMass: Average Mass: 657 Hex1HexNAc1NeuAc1 glycosylated residue A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a carbohydrate-like group composed of Hex1HexNAc1NeuAc1 linked through a glycosidic bond. DeltaMass:0 Unimod:149 NeuAc-Hex-HexNAc Hex(1)HexNAc(1)NeuAc(1) Hex1HexNAc1NeuAc1 modification from Unimod N-linked glycosylation 698.67 C 28 H 46 N 2 O 18 698.27454 C 32 H 52 N 4 O 20 812.78 812.3175 N natural GNO:G90423UY Unimod:150 PSI-MOD HexNAc(2)dHex(2) HexNAc2dHex2 MOD:00518 HexNAc2dHex2 N4-glycosylated asparagine modification from Unimod N-linked glycosylation RESID:AA0151#var Unimod:150 HexNAc(2)dHex(2) HexNAc2dHex2 modification from Unimod N-linked glycosylation 700.64 C 27 H 44 N 2 O 19 700.25385 C 31 H 50 N 4 O 21 814.75 814.29675 N natural GNO:G54968WM Unimod:151 PSI-MOD Hex(1)HexNAc(2)Pent(1) Hex1HexNAc2Pent1 MOD:00519 Hex1HexNAc2Pent1 N4-glycosylated asparagine modification from Unimod N-linked glycosylation RESID:AA0151#var Unimod:151 Hex(1)HexNAc(2)Pent(1) Hex1HexNAc2Pent1 modification from Unimod N-linked glycosylation 714.67 C 28 H 46 N 2 O 19 714.2695 C 32 H 52 N 4 O 21 828.77 828.3124 N natural GNO:G94583DZ Unimod:152 PSI-MOD Hex(1)HexNAc(2)dHex(1) Hex1HexNAc2dHex1 MOD:00520 Hex1HexNAc2dHex1 N4-glycosylated asparagine modification from Unimod N-linked glycosylation RESID:AA0151#var Unimod:152 Hex(1)HexNAc(2)dHex(1) Hex1HexNAc2dHex1 modification from Unimod N-linked glycosylation 730.67 C 28 H 46 N 2 O 20 730.2644 C 32 H 52 N 4 O 22 844.77 844.3073 N natural GNO:G53434XO Unimod:153 PSI-MOD Hex(2)HexNAc(2) Hex2HexNAc2 MOD:00521 Hex2HexNAc2 N4-glycosylated asparagine modification from Unimod N-linked glycosylation RESID:AA0151#var Unimod:153 Hex(2)HexNAc(2) Hex2HexNAc2 modification from Unimod N-linked glycosylation 821.73 C 31 H 51 N 1 O 24 821.2801 C 35 H 57 N 3 O 26 935.84 935.32306 N natural GNO:G64686LL Unimod:154 PSI-MOD Hex(3)HexNAc(1)Pent(1) Hex3HexNAc1Pent1 MOD:00522 Hex3HexNAc1Pent1 N4-glycosylated asparagine modification from Unimod N-linked glycosylation RESID:AA0151#var Unimod:154 Hex(3)HexNAc(1)Pent(1) Hex3HexNAc1Pent1 modification from Unimod N-linked glycosylation 846.79 C 33 H 54 N 2 O 23 846.3117 C 35 H 57 N 3 O 26 960.89 960.3547 N natural GNO:G84825UQ Unimod:155 PSI-MOD Hex(1)HexNAc(2)dHex(1)Pent(1) Hex1HexNAc2dHex1Pent1 MOD:00523 Hex1HexNAc2dHex1Pent1 N4-glycosylated asparagine modification from Unimod N-linked glycosylation RESID:AA0151#var Unimod:155 Hex(1)HexNAc(2)dHex(1)Pent(1) Hex1HexNAc2dHex1Pent1 modification from Unimod N-linked glycosylation 860.81 C 34 H 56 N 2 O 23 860.3274 C 38 H 62 N 4 O 25 974.92 974.3703 N natural GNO:G05460KC Unimod:156 PSI-MOD Hex(1)HexNAc(2)dHex(2) Hex1HexNAc2dHex2 MOD:00524 Hex1HexNAc2dHex2 N4-glycosylated asparagine modification from Unimod N-linked glycosylation RESID:AA0151#var Unimod:156 Hex(1)HexNAc(2)dHex(2) Hex1HexNAc2dHex2 modification from Unimod N-linked glycosylation 862.79 C 33 H 54 N 2 O 24 862.30664 C 37 H 60 N 4 O 26 976.89 976.34955 N natural GNO:G18999EB Unimod:157 PSI-MOD Hex(2)HexNAc(2)Pent(1) Hex2HexNAc2Pent1 MOD:00525 Hex2HexNAc2Pent1 N4-glycosylated asparagine modification from Unimod N-linked glycosylation RESID:AA0151#var Unimod:157 Hex(2)HexNAc(2)Pent(1) Hex2HexNAc2Pent1 modification from Unimod N-linked glycosylation 876.81 C 34 H 56 N 2 O 24 876.3223 C 38 H 62 N 4 O 26 990.92 990.36523 N natural GNO:G93579XB Unimod:158 PSI-MOD Hex(2)HexNAc(2)dHex(1) Hex2HexNAc2dHex1 MOD:00526 Hex2HexNAc2dHex1 N4-glycosylated asparagine modification from Unimod N-linked glycosylation RESID:AA0151#var Unimod:158 Hex(2)HexNAc(2)dHex(1) Hex2HexNAc2dHex1 modification from Unimod N-linked glycosylation 892.81 C 34 H 56 N 2 O 25 892.3172 C 38 H 62 N 4 O 27 1006.92 1006.36017 N natural GNO:G28681TP Unimod:159 (Hex)3-HexNAc-HexNAc PSI-MOD Hex(3)HexNAc(2) Hex3HexNAc2 MOD:00527 From DeltaMass: Average Mass: 893 Hex3HexNAc2 N4-glycosylated asparagine modification from Unimod N-linked glycosylation DeltaMass:0 RESID:AA0151#var Unimod:159 (Hex)3-HexNAc-HexNAc Hex(3)HexNAc(2) Hex3HexNAc2 A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a carbohydrate-like group composed of Hex1HexNAc1NeuAc2 linked through a glycosidic bond. 947.85 C 36 H 57 N 3 O 26 947.32306 X natural GNO:G23729WG Unimod:160 PSI-MOD Hex(1)HexNAc(1)NeuAc(2) Hex1HexNAc1NeuAc2 MOD:00528 Hex1HexNAc1NeuAc2 glycosylated residue A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a carbohydrate-like group composed of Hex1HexNAc1NeuAc2 linked through a glycosidic bond. Unimod:160 Hex(1)HexNAc(1)NeuAc(2) Hex1HexNAc1NeuAc2 modification from Unimod N-linked glycosylation 972.79 C 34 H 57 N 2 O 28 P 1 972.28357 C 38 H 63 N 4 O 30 P 1 1086.89 1086.3264 N natural GNO:G88520YF Unimod:161 PSI-MOD Hex(3)HexNAc(2)P(1) Hex3HexNAc2P1 MOD:00529 Hex3HexNAc2P1 N4-glycosylated asparagine modification from Unimod N-linked glycosylation RESID:AA0151#var Unimod:161 Hex(3)HexNAc(2)P(1) Hex3HexNAc2P1 A protein modification that effectively converts an L-methionine residue to L-selenomethionine. 46.91 C 0 H 0 N 0 S -1 Se 1 47.94445 C 5 H 9 N 1 O 1 Se 1 178.1 178.98494 M artifact Unimod:162 Se(S)Met semetm PSI-MOD Delta:S(-1)Se(1) Selenium replaces sulphur MOD:00530 L-selenomethionine A protein modification that effectively converts an L-methionine residue to L-selenomethionine. OMSSA:113 PubMed:12148805 Unimod:162#M Se(S)Met semetm Delta:S(-1)Se(1) Selenium replaces sulphur A protein modification that effectively converts an L-asparagine residue to L-aspartic acid with one (18)O as the result of having been deglycosylated in (18)O water. 2.99 H -1 N -1 (18)O 1 2.988262 C 4 H 5 N 1 (16)O 2 (18)O 1 117.03 117.03119 N artifact Unimod:170 PSI-MOD Delta:H(1)O(-1)18O(1) glycosylated asparagine 18O labeling MOD:00531 (18)O labeled deglycosylated asparagine A protein modification that effectively converts an L-asparagine residue to L-aspartic acid with one (18)O as the result of having been deglycosylated in (18)O water. PubMed:14435542 Unimod:170 Delta:H(1)O(-1)18O(1) glycosylated asparagine 18O labeling modification from Unimod Chemical derivative 159.01 (13)C 6 H 3 N 1 O 2 S 1 159.00858 (12)C 11 (13)C 6 H 13 N 3 O 3 S 1 345.09 345.0879 W artifact Unimod:171 PSI-MOD NBS:13C(6) Shimadzu NBS-13C MOD:00532 Shimadzu 13CNBS modification from Unimod Chemical derivative PubMed:12845591 Unimod:171 NBS:13C(6) Shimadzu NBS-13C modification from Unimod Chemical derivative 152.99 (12)C 6 H 3 N 1 O 2 S 1 152.98845 (12)C 17 H 13 N 3 O 3 S 1 339.07 339.06775 W artifact Unimod:172 PSI-MOD NBS Shimadzu NBS-12C MOD:00533 Shimadzu 12CNBS modification from Unimod Chemical derivative PubMed:12845591 Unimod:172 NBS Shimadzu NBS-12C modification from Unimod Post-translational 218.34 C 15 H 22 O 1 218.16707 X artifact Unimod:176 PSI-MOD BHT Michael addition of BHT quinone methide to Cysteine and Lysine MOD:00534 Butylated Hydroxytoluene adduct. Michael addition of BHT quinone methide to cysteine and lysine modification from Unimod Post-translational PubMed:9448752 Unimod:176 BHT Michael addition of BHT quinone methide to Cysteine and Lysine modification from Unimod Chemical derivative 87.18 C 4 H 9 N 1 O -1 S 1 87.05066 X artifact Unimod:178 PSI-MOD DAET phosphorylation to amine thiol MOD:00535 DAET = 2-(dimethylamino)ethanethiol. The phosphorylation to amine is the beta elimination of phosphate and Michael addition of 2-(dimethylamino)ethanethiol to the site. phosphorylation to amine thiol modification from Unimod Chemical derivative PubMed:12216740 Unimod:178 DAET phosphorylation to amine thiol OBSOLETE because Unimod 179 merged with Unimod 447 remap to ??? a protein modification that replaces an L-serine residue with an L-alanine residue -16.0 O -1 -15.994915 S artifact Unimod:179 Ser_Ala PSI-MOD MOD:00536 L-serine to L-alanine replacement true OBSOLETE because Unimod 179 merged with Unimod 447 remap to ??? a protein modification that replaces an L-serine residue with an L-alanine residue Unimod:179 Ser_Ala A protein modification that effectively converts an L-threonine residue to L-alanine. -30.03 C -1 H -2 O -1 -30.010565 C 3 H 5 N 1 O 1 71.08 71.03712 T Unimod:659 Thr(Ala) PSI-MOD Thr->Ala Thr->Ala substitution MOD:00537 This could represent either an engineered replacement or a chemical modification. L-alanine residue (Thr) A protein modification that effectively converts an L-threonine residue to L-alanine. Unimod:659 Thr(Ala) Thr->Ala Thr->Ala substitution Modified amino acid residues groups into isobaric sets at particular mass resolution cut-offs. PSI-MOD MOD:00538 protein modification categorized by isobaric sets Modified amino acid residues groups into isobaric sets at particular mass resolution cut-offs. PubMed:18688235 OBSOLETE because Unimod 179 merged wth Unimod 447 remap to ??? modification from Unimod O-linked glycosylation -17.01 H -1 O -1 -17.00274 T artifact Unimod:182 PSI-MOD MOD:00539 threonine reduced to aminobutynate true OBSOLETE because Unimod 179 merged wth Unimod 447 remap to ??? modification from Unimod O-linked glycosylation Unimod:182 A protein modification that effectively converts a residue containing common isotopes to a 9x(13)C labeled residue. 9.03 (12)C -9 (13)C 9 9.030194 X artifact Unimod:184 PSI-MOD 13C(9) Silac label Label:13C(9) MOD:00540 9x(13)C labeled residue A protein modification that effectively converts a residue containing common isotopes to a 9x(13)C labeled residue. PubMed:12716131 Unimod:184 13C(9) Silac label Label:13C(9) A protein modification that effectively converts an L-tyrosine residue to 9x(13)C labeled L-phosphotyrosine. 89.0 (12)C -9 (13)C 9 H 1 O 3 P 1 88.99652 (13)C 9 H 10 N 1 O 5 P 1 252.06 252.05986 Y artifact Unimod:185 PSI-MOD C13 label (Phosphotyrosine) Label:13C(9)+Phospho MOD:00541 9x(13)C labeled L-phosphotyrosine A protein modification that effectively converts an L-tyrosine residue to 9x(13)C labeled L-phosphotyrosine. PubMed:12716131 Unimod:185 C13 label (Phosphotyrosine) Label:13C(9)+Phospho modification from Unimod Chemical derivative 132.12 C 8 H 4 O 2 132.02113 C 14 H 16 N 4 O 3 288.31 288.12225 R artifact Unimod:186 PSI-MOD HPG Hydroxyphenylglyoxal arginine MOD:00542 hydroxyphenylglyoxal arginine modification from Unimod Chemical derivative PubMed:11698400 PubMed:11914093 Unimod:186 HPG Hydroxyphenylglyoxal arginine modification from Unimod Chemical derivative 282.25 C 16 H 10 O 5 282.05283 C 22 H 22 N 4 O 6 438.44 438.15393 R artifact Unimod:187 PSI-MOD 2HPG bis(hydroxphenylglyoxal) arginine MOD:00543 OH-PGO and PGO react with arginine at a stoichiometry of 2:1 [Unimod]. bis(hydroxyphenylglyoxal) arginine modification from Unimod Chemical derivative PubMed:11698400 Unimod:187 2HPG bis(hydroxphenylglyoxal) arginine A protein modification that effectively converts a residue containing common isotopes to a 6x(13)C labeled residue. 6.02 (12)C -6 (13)C 6 6.020129 X artifact Unimod:188 PSI-MOD 13C(6) Silac label Label:13C(6) MOD:00544 6x(13)C labeled residue A protein modification that effectively converts a residue containing common isotopes to a 6x(13)C labeled residue. PubMed:12716131 Unimod:188 13C(6) Silac label Label:13C(6) OBSOLETE because redundant with MOD:00927. Remap to MOD:00927. MOD:00927 X artifact N-term PSI-MOD MOD:00545 deuterated dimethyl labeling (D) true OBSOLETE because redundant with MOD:00927. Remap to MOD:00927. PubMed:14670044 A protein modification that effectively substitutes two (18)O atom for the two (16)O atoms of an alpha-carboxyl (1-carboxyl) group. 4.01 (16)O -2 (18)O 2 4.008493 X artifact C-term Unimod:193 ctermpepdio18 PSI-MOD Label:18O(2) O18 label at both C-terminal oxygens MOD:00546 (18)O label at both C-terminal oxygens A protein modification that effectively substitutes two (18)O atom for the two (16)O atoms of an alpha-carboxyl (1-carboxyl) group. OMSSA:88 PubMed:11467524 Unimod:193 ctermpepdio18 Label:18O(2) O18 label at both C-terminal oxygens modification from Unimod Chemical derivative used for amino acid analysis 170.17 C 10 H 6 N 2 O 1 170.04802 X artifact Unimod:194 PSI-MOD 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate AccQTag MOD:00547 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate modification from Unimod Chemical derivative used for amino acid analysis PubMed:14997490 Unimod:194 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate AccQTag modification from Unimod Chemical derivative 171.26 C 9 H 19 N 2 O 1 171.14973 C 12 H 24 N 3 O 2 S 1 274.4 274.15894 C artifact Unimod:195 PSI-MOD APTA-d0 QAT MOD:00548 Derivatization of cysteine with 3-acrylamidopropyl)trimethylammonium chloride [JSG]. APTA modification from Unimod Chemical derivative PubMed:15283597 Unimod:195 APTA-d0 QAT modification from Unimod Isotopic label 174.17 C 9 (1)H 16 (2)H 3 N 2 O 1 174.16856 C 12 (1)H 21 (2)H 3 N 3 O 2 S 1 277.18 277.17776 C artifact Unimod:196 PSI-MOD (3-acrylamidopropyl)trimethylammonium APTA d3 QAT:2H(3) MOD:00549 Derivatization of cysteine with 3-acrylamidopropyl)trimethylammonium chloride (difference formula correct) [JSG]. APTA d3 modification from Unimod Isotopic label PubMed:15283597 Unimod:196 (3-acrylamidopropyl)trimethylammonium APTA d3 QAT:2H(3) modification from Unimod Chemical derivative 184.28 C 10 H 20 N 2 O 1 184.15756 C 13 H 25 N 3 O 2 S 1 287.42 287.16675 C artifact Unimod:197 PSI-MOD EAPTA d0 EQAT MOD:00550 EAPTA d0 modification from Unimod Chemical derivative Unimod:197 EAPTA d0 EQAT modification from Unimod Isotopic label 189.19 C 10 (1)H 15 (2)H 5 N 2 O 1 189.18895 C 13 (1)H 20 (2)H 5 N 3 O 2 S 1 292.2 292.19812 C artifact Unimod:198 PSI-MOD EAPTA d5 EQAT:2H(5) MOD:00551 EAPTA d5 modification from Unimod Isotopic label Unimod:198 EAPTA d5 EQAT:2H(5) A protein modification that effectively converts a residue containing common isotopes to a 4x(2)H labeled dimethylated residue. 32.06 C 2 (2)H 4 32.056408 X artifact Unimod:199 PSI-MOD DiMethyl-CHD2 Dimethyl:2H(4) MOD:00552 Supposed to be alpha-amino and Lys-N6 derivatized by C(2)H2O and reduction. 4x(2)H labeled dimethylated residue A protein modification that effectively converts a residue containing common isotopes to a 4x(2)H labeled dimethylated residue. PubMed:14670044 Unimod:199 DiMethyl-CHD2 Dimethyl:2H(4) A protein modification that effectively substitutes a (2-sulfanylethyl)sulfanyl (or thioethylthiol) group for a hydroxy group. 76.18 C 2 H 4 O -1 S 2 75.98053 X artifact Unimod:200 1,2-ethanedithiol (EDT) PSI-MOD EDT Ethanedithiol MOD:00553 From DeltaMass: Average Mass: 93; supposed to be derivatization of serine and threonine. 1,2-ethanedithiol modified residue A protein modification that effectively substitutes a (2-sulfanylethyl)sulfanyl (or thioethylthiol) group for a hydroxy group. DeltaMass:0 PubMed:11507762 Unimod:200 1,2-ethanedithiol (EDT) EDT Ethanedithiol OBSOLETE because Unimod entry 202 was merged with entry 195, remap to MOD:00548. modification from Unimod Chemical derivative MOD:00548 170.26 C 9 H 18 N 2 O 1 170.1419 C artifact Unimod:202 PSI-MOD MOD:00554 APTA-d0 with no neutral loss true OBSOLETE because Unimod entry 202 was merged with entry 195, remap to MOD:00548. modification from Unimod Chemical derivative Unimod:202 OBSOLETE because Unimod entry 202 was merged with entry 195, remap to MOD:00548. modification from Unimod Chemical derivative MOD:00548 170.26 C 9 H 18 N 2 O 1 170.1419 C artifact Unimod:203 PSI-MOD MOD:00555 APTA-d0 with quaternary amine loss true OBSOLETE because Unimod entry 202 was merged with entry 195, remap to MOD:00548. modification from Unimod Chemical derivative Unimod:203 OBSOLETE because this modification not supported by any literature that I can find[PMT] 94.11 C 6 H 6 O 1 94.04186 C 12 H 18 N 2 O 2 222.29 222.13683 K artifact Unimod:205 PSI-MOD Acrolein addition +94 Delta:H(6)C(6)O(1) MOD:00556 acrolein addition +94 true OBSOLETE because this modification not supported by any literature that I can find[PMT] Unimod:205 Acrolein addition +94 Delta:H(6)C(6)O(1) OBSOLETE because this modification not supported by the papers listed or any other that I can find[PMT] 56.06 C 3 H 4 O 1 56.026215 X artifact Unimod:206 PSI-MOD Acrolein addition +56 Delta:H(4)C(3)O(1) MOD:00557 acrolein addition +56 true OBSOLETE because this modification not supported by the papers listed or any other that I can find[PMT] PubMed:10825247 PubMed:15541752 Unimod:206 Acrolein addition +56 Delta:H(4)C(3)O(1) OBSOLETE because this modification not supported by any literature that I can find[PMT] 38.05 C 3 H 2 38.01565 C 9 H 14 N 2 O 1 166.22 166.11061 K artifact Unimod:207 PSI-MOD Acrolein addition +38 Delta:H(2)C(3) MOD:00558 acrolein addition +38 true OBSOLETE because this modification not supported by any literature that I can find[PMT] Unimod:207 Acrolein addition +38 Delta:H(2)C(3) OBSOLETE because this modification not supported by any literature that I can find[PMT] 76.1 C 6 H 4 76.0313 C 12 H 16 N 2 O 1 204.27 204.12627 K artifact Unimod:208 PSI-MOD Acrolein addition +76 Delta:H(4)C(6) MOD:00559 acrolein addition +76 true OBSOLETE because this modification not supported by any literature that I can find[PMT] Unimod:208 Acrolein addition +76 Delta:H(4)C(6) OBSOLETE because this modification not supported by any literature that I can find[PMT] 112.13 C 6 H 8 O 2 112.05243 C 12 H 20 N 2 O 3 240.3 240.1474 K artifact Unimod:209 PSI-MOD Acrolein addition +112 Delta:H(8)C(6)O(2) MOD:00560 acrolein addition +112 true OBSOLETE because this modification not supported by any literature that I can find[PMT] Unimod:209 Acrolein addition +112 Delta:H(8)C(6)O(2) modification from Unimod Isotopic label 85.11 C 4 H 7 N 1 O 1 85.052765 X artifact Unimod:211 PSI-MOD N-ethyl iodoacetamide-d0 NEIAA MOD:00561 N-ethyl iodoacetamide- modification from Unimod Isotopic label PubMed:12766232 Unimod:211 N-ethyl iodoacetamide-d0 NEIAA modification from Unimod Isotopic label 90.08 C 4 (1)H 2 (2)H 5 N 1 O 1 90.084145 X artifact Unimod:212 PSI-MOD N-ethyl iodoacetamide-d5 NEIAA:2H(5) MOD:00562 N-ethyl iodoacetamide-d5 modification from Unimod Isotopic label PubMed:12766232 Unimod:212 N-ethyl iodoacetamide-d5 NEIAA:2H(5) A protein modification that effectively replaces a hydrogen atom with an N-acetylaminogalactose group through a glycosidic bond. 203.19 C 8 H 13 N 1 O 5 203.07938 X GalNAcRes PSI-MOD HexNAc MOD:00563 mono-N-acetylaminogalactosylated residue A protein modification that effectively replaces a hydrogen atom with an N-acetylaminogalactose group through a glycosidic bond. PubMed:18688235 GalNAcRes HexNAc Modification from Unimod Isotopic label. The Unimod term was extracted when it had not been approved. OBSOLETE because redundant to MOD:01505. Remap to MOD:01505, or one of the child terms MOD:01493 or MOD:01497. MOD:01505 X artifact Unimod:214 PSI-MOD Representative mass and accurate mass for 116 & 117 iTRAQ4plex MOD:00564 Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry true Modification from Unimod Isotopic label. The Unimod term was extracted when it had not been approved. OBSOLETE because redundant to MOD:01505. Remap to MOD:01505, or one of the child terms MOD:01493 or MOD:01497. URL:http://docs.appliedbiosystems.com/pebiodocs/04351918.pdf Unimod:214 Representative mass and accurate mass for 116 & 117 iTRAQ4plex modification from Unimod N-linked glycosylation 0.98 H -1 N -1 O 1 0.984016 C 4 H 5 N 1 O 3 115.09 115.02694 N artifact Unimod:7 PSI-MOD Deamidated Deamidation MOD:00565 Conversion of glycosylated asparagine residues upon deglycosylation with PGNase F in H2O. CAUTION - the difference formula appears to be based on a partial structure [JSG]. deglycosylated asparagine modification from Unimod N-linked glycosylation Unimod:7#N Deamidated Deamidation modification from Unimod Chemical derivative 297.15 Br 1 C 12 H 13 N 2 O 2 296.01605 Br 1 C 15 H 18 N 3 O 3 S 1 400.29 399.02524 C artifact Unimod:243 PSI-MOD IGBP Light IDBEST tag for quantitation MOD:00566 "IDBEST tag for quantitation, http://www.targetdiscovery.com/index.php?topic=prod.idbe" label cysteine with IGBP reagent modification from Unimod Chemical derivative Unimod:243 IGBP Light IDBEST tag for quantitation OBSOLETE because Unimod entry 244 is redundant with Unimod 348. Remap to MOD:00775. -23.04 C -2 H -1 N -1 O 1 -23.015984 H artifact Unimod:244 PSI-MOD MOD:00567 histidine oxidation to asparagine true OBSOLETE because Unimod entry 244 is redundant with Unimod 348. Remap to MOD:00775. ChEBI:29956 PubMed:15736973 PubMed:5681232 PubMed:6692818 PubMed:9789001 RESID:AA0003 Unimod:244 OBSOLETE because Unimod entry 245 is redundant with Unimod 349. Remap to MOD:00776 MOD:00776 -22.05 C -2 H -2 N -2 O 2 -22.03197 H artifact Unimod:245 PSI-MOD MOD:00568 histidine oxidation to aspartic acid true OBSOLETE because Unimod entry 245 is redundant with Unimod 349. Remap to MOD:00776 PubMed:1097438 PubMed:339692 PubMed:4399050 PubMed:5764436 PubMed:6692818 PubMed:8089117 PubMed:9521123 PubMed:9582379 Unimod:245 Natural or modified residues that are isobaric at a resolution below 0.000001 Da. PSI-MOD MOD:00569 residues isobaric at a resolution below 0.000001 Da Natural or modified residues that are isobaric at a resolution below 0.000001 Da. PubMed:18688235 Natural or modified residues with a mass of 71.037114 Da. PSI-MOD MOD:00570 residues isobaric at 71.037114 Da Natural or modified residues with a mass of 71.037114 Da. PubMed:18688235 A modification that effectively oxygenates C5 of an L-proline residue to form a 2-pyrrolidone-5-carboxylic acid, pyroglutamic acid. 13.98 H -2 O 1 13.979265 C 5 H 6 N 1 O 2 112.11 112.039856 P artifact Unimod:359 PyrGlu(Pro) pyroglutamicp PSI-MOD Pro->pyro-Glu Pyroglutamic MOD:00571 The review article PubMed:9252331 does not provide an original citation for this modification [JSG]. 2-pyrrolidone-5-carboxylic acid (Pro) A modification that effectively oxygenates C5 of an L-proline residue to form a 2-pyrrolidone-5-carboxylic acid, pyroglutamic acid. OMSSA:111 PubMed:9252331 Unimod:359 PyrGlu(Pro) pyroglutamicp Pro->pyro-Glu Pyroglutamic modification from Unimod Chemical derivative 199.27 C 9 H 13 N 1 O 2 S 1 199.0667 C 15 H 25 N 5 O 3 S 1 355.46 355.16782 R artifact Unimod:343 PSI-MOD Argbiotinhydrazide oxidized Arginine biotinylated with biotin hydrazide MOD:00572 oxidized arginine biotinylated with biotin hydrazide modification from Unimod Chemical derivative PubMed:15174056 PubMed:15828771 Unimod:343 Argbiotinhydrazide oxidized Arginine biotinylated with biotin hydrazide modification from Unimod Chemical derivative 241.31 C 10 H 15 N 3 O 2 S 1 241.0885 C 16 H 27 N 5 O 3 S 1 369.48 369.18347 K artifact Unimod:353 PSI-MOD Lysbiotinhydrazide oxidized Lysine biotinylated with biotin hydrazide MOD:00573 "http://www.piercenet.com/Proteomics/browse.cfm?fldID=84EBE112-F871-4CA5-807F-47327153CFCB" oxidized lysine biotinylated with biotin hydrazide modification from Unimod Chemical derivative PubMed:15174056 Unimod:353 Lysbiotinhydrazide oxidized Lysine biotinylated with biotin hydrazide modification from Unimod Chemical derivative 258.34 C 10 H 18 N 4 O 2 S 1 258.11505 C 15 H 25 N 5 O 3 S 1 355.46 355.16782 P artifact Unimod:357 PSI-MOD oxidized proline biotinylated with biotin hydrazide probiotinhydrazide MOD:00574 "http://www.piercenet.com/Proteomics/browse.cfm?fldID=84EBE112-F871-4CA5-807F-47327153CFCB" oxidized proline biotinylated with biotin hydrazide modification from Unimod Chemical derivative PubMed:15174056 Unimod:357 oxidized proline biotinylated with biotin hydrazide probiotinhydrazide modification from Unimod Chemical derivative 240.32 C 10 H 16 N 4 O 1 S 1 240.10448 C 14 H 23 N 5 O 3 S 1 341.43 341.15216 T artifact Unimod:361 PSI-MOD Thrbiotinhydrazide oxidized Threonine biotinylated with biotin hydrazide MOD:00575 "http://www.piercenet.com/Proteomics/browse.cfm?fldID=84EBE112-F871-4CA5-807F-47327153CFCB" oxidized threonine biotinylated with biotin hydrazide modification from Unimod Chemical derivative PubMed:15174056 Unimod:361 Thrbiotinhydrazide oxidized Threonine biotinylated with biotin hydrazide modification from Unimod Other 70.09 C 4 H 6 O 1 70.04186 X artifact Unimod:253 PSI-MOD Crotonaldehyde MOD:00576 crotonylated residue modification from Unimod Other PubMed:11283024 PubMed:25907603 Unimod:253 Crotonaldehyde Crotonaldehyde modification occurs as a Schiff base in the presence of pentalysine 26.04 C 2 H 2 26.01565 C 8 H 14 N 2 O 1 666.91 666.4905 K, K, K, K, K artifact Unimod:254 PSI-MOD Acetaldehyde +26 Delta:H(2)C(2) MOD:00577 acetaldehyde crosslinked penta-L-lysine modification occurs as a Schiff base in the presence of pentalysine PubMed:7744761 Unimod:254 Acetaldehyde +26 Delta:H(2)C(2) OBSOLETE because this modification not supported by any literature that I can find [PMT] 28.05 C 2 H 4 28.0313 C X artifact Unimod:255 PSI-MOD Acetaldehyde +28 Delta:H(4)C(2) MOD:00578 acetaldehyde +28 true OBSOLETE because this modification not supported by any literature that I can find [PMT] Unimod:255 Acetaldehyde +28 Delta:H(4)C(2) OBSOLETE because not supported by the linked literature [PMT]. modification from Unimod Other 40.06 C 3 H 4 40.0313 X artifact Unimod:256 PSI-MOD Delta:H(4)C(3) Propionaldehyde +40 MOD:00579 propionaldehyde +40 true OBSOLETE because not supported by the linked literature [PMT]. modification from Unimod Other Unimod:256 Delta:H(4)C(3) Propionaldehyde +40 OBSOLETE because entry removed from Unimod. Remap potentially to MOD:00579 propionaldehyde +40 MOD:00579 42.08 C 3 H 6 42.04695 X artifact Unimod:257 PSI-MOD MOD:00580 propionaldehyde +42 true OBSOLETE because entry removed from Unimod. Remap potentially to MOD:00579 propionaldehyde +40 Unimod:257 A protein modification that effectively substitutes one (18)O atom for one (16)O atom. 2.0 (16)O -1 (18)O 1 2.004246 X artifact C-term Unimod:258 ctermpepo18 PSI-MOD Label:18O(1) O18 Labeling MOD:00581 (18)O monosubstituted residue A protein modification that effectively substitutes one (18)O atom for one (16)O atom. OMSSA:87 PubMed:11467524 Unimod:258 ctermpepo18 Label:18O(1) O18 Labeling A protein modification that effectively converts an L-lysine residue to 6x(13)C,2x(15)N labeled L-lysine. 8.01 (12)C -6 (13)C 6 (14)N -2 (15)N 2 8.014199 (13)C 6 H 12 (15)N 2 O 1 136.11 136.10916 K artifact Unimod:259 lys-13C615N2 PSI-MOD 13C(6) 15N(2) Silac label Label:13C(6)15N(2) MOD:00582 6x(13)C,2x(15)N labeled L-lysine A protein modification that effectively converts an L-lysine residue to 6x(13)C,2x(15)N labeled L-lysine. OMSSA:181 PubMed:12716131 Unimod:259 lys-13C615N2 13C(6) 15N(2) Silac label Label:13C(6)15N(2) A protein modification that effectively replaces a hydrogen atom with a thiophosphono group (H2PO2S, 'thiophosphate'). 96.04 H 1 O 2 P 1 S 1 95.94349 X artifact Unimod:260 PSI-MOD Thiophospho Thiophosphorylation MOD:00583 thiophosphorylated residue A protein modification that effectively replaces a hydrogen atom with a thiophosphono group (H2PO2S, 'thiophosphate'). PubMed:12110917 Unimod:260 Thiophospho Thiophosphorylation A protein modification produced by formation of an adduct with 4-sulfophenyl isothiocyanate. 215.24 C 7 H 5 N 1 O 3 S 2 214.97108 X artifact N-term Unimod:261 PSI-MOD 4-sulfophenyl isothiocyanate SPITC MOD:00584 4-sulfophenyl isothiocyanate derivatized residue A protein modification produced by formation of an adduct with 4-sulfophenyl isothiocyanate. PubMed:14689565 PubMed:14745769 PubMed:16526082 Unimod:261 4-sulfophenyl isothiocyanate SPITC A protein modification that effectively substitutes three (2)H deuterium atoms for three (1)H protium atoms. 3.02 (1)H -3 (2)H 3 3.01883 X artifact Unimod:262 D(H)3Res PSI-MOD Label:2H(3) Trideuteration MOD:00585 deuterium trisubstituted residue A protein modification that effectively substitutes three (2)H deuterium atoms for three (1)H protium atoms. Unimod:262 D(H)3Res Label:2H(3) Trideuteration modification from Unimod Chemical derivative 121.2 C 7 H 7 N 1 O -1 S 1 121.035 X artifact Unimod:264 PSI-MOD PET phosphorylation to pyridyl thiol MOD:00586 pyridyl thiol modified residue modification from Unimod Chemical derivative Unimod:264 PET phosphorylation to pyridyl thiol A protein modification that effectively converts an L-arginine residue to 6x(13)C, 4x(15)N labeled L-arginine. 10.01 (12)C -6 (13)C 6 (14)N -4 (15)N 4 10.008269 (13)C 6 H 12 (15)N 4 O 1 166.11 166.10938 R artifact Unimod:267 arg-13c6-15n4 PSI-MOD 13C(6) 15N(4) Silac label Label:13C(6)15N(4) MOD:00587 6x(13)C,4x(15)N labeled L-arginine A protein modification that effectively converts an L-arginine residue to 6x(13)C, 4x(15)N labeled L-arginine. OMSSA:137 PubMed:12716131 Unimod:267 arg-13c6-15n4 13C(6) 15N(4) Silac label Label:13C(6)15N(4) A protein modification that effectively converts an L-valine residue to 5x(13)C,1x(15)N labeled L-valine. 6.01 (12)C -5 (13)C 5 (14)N -1 (15)N 1 6.013809 (13)C 5 H 9 (15)N 1 O 1 105.08 105.08222 V artifact Unimod:268 PSI-MOD 13C(5) 15N(1) Silac label Label:13C(5)15N(1) MOD:00588 5x(13)C,1x(15)N labeled L-valine A protein modification that effectively converts an L-valine residue to 5x(13)C,1x(15)N labeled L-valine. PubMed:12771378 Unimod:268#V 13C(5) 15N(1) Silac label Label:13C(5)15N(1) A protein modification that effectively converts an L-phenylalanine residue to (13)C,(15)N labeled L-phenylalanine. 10.03 (12)C -9 (13)C 9 (14)N -1 (15)N 1 10.027228 (13)C 9 H 9 (15)N 1 O 1 157.1 157.09564 F artifact Unimod:269 PSI-MOD 13C(9) 15N(1) Silac label Label:13C(9)15N(1) MOD:00589 9x(13)C,1x(15)N labeled L-phenylalanine A protein modification that effectively converts an L-phenylalanine residue to (13)C,(15)N labeled L-phenylalanine. PubMed:12771378 Unimod:269 13C(9) 15N(1) Silac label Label:13C(9)15N(1) OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative 362.38 C 19 H 22 O 7 362.13657 X artifact Unimod:270 PSI-MOD Cytopiloyne nucleophilic addtion to cytopiloyne MOD:00590 nucleophilic addtion to cytopiloyne true OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative PubMed:15549660 Unimod:270 Cytopiloyne nucleophilic addtion to cytopiloyne OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative 380.39 C 19 H 24 O 8 380.14713 X artifact Unimod:271 PSI-MOD Cytopiloyne+water nucleophilic addition to cytopiloyne+H2O MOD:00591 nucleophilic addition to cytopiloyne+H2O true OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative PubMed:15549660 Unimod:271 Cytopiloyne+water nucleophilic addition to cytopiloyne+H2O modification from Unimod Chemical derivative 136.12 C 3 H 4 O 4 S 1 135.98303 X artifact N-term Unimod:272 PSI-MOD CAF sulfonation of N-terminus MOD:00592 sulfonation of N-terminal modification from Unimod Chemical derivative PubMed:12705581 PubMed:15732931 PubMed:16046801 Unimod:272 CAF sulfonation of N-terminus OBSOLETE because removed from Unimod. modification from Unimod Chemical derivative 253.25 C 12 H 15 N 1 O 5 253.09502 C 18 H 27 N 3 O 6 381.43 381.18997 K artifact Unimod:273 PSI-MOD Xlink:SSD covalent modification of lysine by cross-linking reagent MOD:00593 J. Prot. Chem. 2, 263-277, 1983 covalent modification of lysine by omega-maleimido alkanoyl N-hydroxysuccinimido esters true OBSOLETE because removed from Unimod. modification from Unimod Chemical derivative Unimod:273 Xlink:SSD covalent modification of lysine by cross-linking reagent Natural or modified resiues with a mass of 113.047678 Da. PSI-MOD MOD:00594 residues isobaric at 113.047678 Da Natural or modified resiues with a mass of 113.047678 Da. PubMed:18688235 A protein modification that effectively replaces a hydrogen atom with an manose group through a glycosidic bond 162.14 C 6 H 10 O 5 162.05283 X natural ManRes PSI-MOD MOD:00595 monomannosylated residue A protein modification that effectively replaces a hydrogen atom with an manose group through a glycosidic bond PubMed:18688235 ManRes A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS. 183.23 C 8 H 9 N 1 O 2 S 1 183.0354 X artifact Unimod:276 AEBSF PSI-MOD AEBS Aminoethylbenzenesulfonylation MOD:00596 From DeltaMass: Average Mass: 183 Average Mass Change:183 References:We have found that AEBSF modifies many proteins by covalent attachment, preferentially on Tyr, and to a lesser extent on Lys, His, and the amino-terminus. These modifications were identified by electrospray MS of the proteins (adds 183 Da per AEBS-group) and by peptide mapping and MS/MS. All the proteins we examined were modified after 24 hrs. at 4 C with 1 mM AEBSF in TRIS, pH 8.0. The reaction is 10-20x slower at pH 7; however AEBSF is quite stable in aqueous solution and the extent of to which the protein is modified continues to increase for several days. We have seen the addition of 10 or more AEBS-groups to proteins after prolonged storage. We found no equivalent modification from PMSF, probably because it degrades so quickly. We no longer use AEBSF, and urge caution to those who do. To address the problem, Boehringer Mannheim (now Roche Molecular Biochemicals) introduced Pefabloc PLUS which includes an additional component to compete for these side reactions. In our limited experience with Pefabloc PLUS, it reduces the +183 modifications, but does not always eliminate them. As a result, we prefer PMSF, despite its own set of drawbacks. We have never found PMSF-induced modification of proteins (except trypsin), probably due to its short half-life in aqeous solution. 4-(2-aminoethyl)benzenesulfonyl fluoride derivatized residue A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS. DeltaMass:235 PubMed:8597590 Unimod:276 AEBSF AEBS Aminoethylbenzenesulfonylation OBSOLETE because Unimod entry 277 redundant with Unimod 39. Remap to MOD:00110. MOD:00110 46.09 C 1 H 2 S 1 45.98772 C artifact Unimod:277 PSI-MOD MOD:00597 methyl methanethiosulfonate true OBSOLETE because Unimod entry 277 redundant with Unimod 39. Remap to MOD:00110. Unimod:277 A protein modification that effectively converts an L-cysteine residue to S-(2-hydroxyethyl)cysteine 44.05 C 2 H 4 O 1 44.026215 C 5 H 9 N 1 O 2 S 1 147.19 147.0354 C artifact Unimod:278 PSI-MOD Ethanolation of Cys Ethanolyl MOD:00598 This modification of cysteine is produced by the reagent iodoethanol with triethylphosphine [JSG]. S-(2-hydroxyethyl)cysteine A protein modification that effectively converts an L-cysteine residue to S-(2-hydroxyethyl)cysteine PubMed:15351294 Unimod:278 Ethanolation of Cys Ethanolyl A protein modification that effectively replaces one hydrogen atom with one methyl group. 14.03 C 1 H 2 14.01565 X Unimod:34 Me1Res PSI-MOD Methyl Methylation MOD:00599 monomethylated residue A protein modification that effectively replaces one hydrogen atom with one methyl group. PubMed:11875433 Unimod:34 Me1Res Methyl Methylation A protein modification that effectively converts an L-glutamic acid residue to L-glutamate 5-ethyl ester. 28.05 C 2 H 4 28.0313 C 7 H 11 N 1 O 3 157.17 157.0739 E artifact Unimod:280 Ethyl PSI-MOD Ethyl Ethylation MOD:00600 From DeltaMass: Average Mass: 28 with no citation. The Unimod citation refers to the formation of glutamate ethyl ester and not to either lysine or N-terminal alkylation. For dimethylated residues, see MOD:00429 and its children [JSG]. L-glutamic acid 5-ethyl ester A protein modification that effectively converts an L-glutamic acid residue to L-glutamate 5-ethyl ester. DeltaMass:0 PubMed:9629898 Unimod:280#E Ethyl Ethyl Ethylation A protein modification that effectively produces an heterocyclic amino acid with a covalent bond between the side chain and either its alpha amino or 1-carboxyl group, possibly breaking the peptide chain. CycRes PSI-MOD MOD:00601 cyclized residue A protein modification that effectively produces an heterocyclic amino acid with a covalent bond between the side chain and either its alpha amino or 1-carboxyl group, possibly breaking the peptide chain. PubMed:18688235 CycRes A protein modification that effectively replaces a hydrogen atom of a residue amino or imino group with an methyl group. NMeRes PSI-MOD MOD:00602 N-methylated residue A protein modification that effectively replaces a hydrogen atom of a residue amino or imino group with an methyl group. PubMed:18688235 NMeRes OBSOLETE because Unimod entry 283 is redundant with Unimod 280. Remap to MOD:00600 MOD:00600 28.05 C 2 H 4 28.0313 X artifact N-term Unimod:283 PSI-MOD MOD:00603 N-ethylation true OBSOLETE because Unimod entry 283 is redundant with Unimod 280. Remap to MOD:00600 Unimod:283 A protein modification that effectively converts an L-lysine residue to 2x(2)H labeled monomethylated L-lysine. 16.03 C 1 (2)H 2 16.028204 C 7 (1)H 12 (2)H 2 N 2 O 1 144.12 144.12317 K artifact Unimod:284 PSI-MOD Deuterium Methylation of Lysine Methyl:2H(2) MOD:00604 2x(2)H monomethylated L-lysine A protein modification that effectively converts an L-lysine residue to 2x(2)H labeled monomethylated L-lysine. PubMed:15525938 Unimod:284 Deuterium Methylation of Lysine Methyl:2H(2) modification from Unimod Chemical derivative, C-Terminal/Glutamate/Aspartate sulfonation 155.0 (12)C 6 H 5 N 1 O 2 S 1 155.0041 X artifact C-term Unimod:285 PSI-MOD Light Sulfanilic Acid (SA) C12 SulfanilicAcid MOD:00605 Sulfanilic Acid (SA), light C12 modification from Unimod Chemical derivative, C-Terminal/Glutamate/Aspartate sulfonation Unimod:285 Light Sulfanilic Acid (SA) C12 SulfanilicAcid modification from Unimod Chemical derivative 161.02 (13)C 6 H 5 N 1 O 2 S 1 161.02423 X artifact C-term Unimod:286 PSI-MOD Heavy Sulfanilic Acid (SA) C13 SulfanilicAcid:13C(6) MOD:00606 Sulfanilic Acid (SA), heavy C13 modification from Unimod Chemical derivative PubMed:9254591 Unimod:286 Heavy Sulfanilic Acid (SA) C13 SulfanilicAcid:13C(6) modification from Unimod Chemical derivative 30.99 H -1 O 2 30.982004 C 11 H 9 N 2 O 3 217.2 217.06131 W artifact C-term Unimod:288 PSI-MOD Trp->Oxolactone Tryptophan oxidation to oxolactone MOD:00607 Unimod name, formula, and terminal specification corrected. Formula corresponded to uncleaved intermediate [JSG]. dioxoindolealanine lactone modification from Unimod Chemical derivative PubMed:7949339 Unimod:288 Trp->Oxolactone Tryptophan oxidation to oxolactone modification from Unimod Chemical derivative X artifact Unimod:289 PSI-MOD Biotin polyethyleneoxide amine Biotin-PEO-Amine MOD:00608 biotin polyethyleneoxide amine modification from Unimod Chemical derivative Unimod:289 Biotin polyethyleneoxide amine Biotin-PEO-Amine modification from Unimod Chemical derivative 428.61 C 19 H 32 N 4 O 3 S 2 428.1916 C 22 H 37 N 5 O 4 S 3 531.75 531.20074 C artifact Unimod:290 PSI-MOD Biotin-HPDP Pierce EZ-Link Biotin-HPDP MOD:00609 Pierce EZ-Link Biotin-HPDP modified L-cysteine modification from Unimod Chemical derivative Unimod:290 Biotin-HPDP Pierce EZ-Link Biotin-HPDP modification from Unimod Chemical derivative 200.59 Hg 1 201.97064 C 3 H 5 Hg 1 N 1 O 1 S 1 303.73 304.97983 C artifact Unimod:291 PSI-MOD Delta:Hg(1) Mercury Mercaptan MOD:00610 cysteinyl mercury modification from Unimod Chemical derivative PubMed:10695144 Unimod:291 Delta:Hg(1) Mercury Mercaptan A protein modification that is produced by reaction of iodouridine monophosphate with a residue. 322.17 C 9 H 11 N 2 O 9 P 1 322.0202 X artifact Unimod:292 PSI-MOD Cross-link of (Iodo)-uracil MP with W,F,Y IodoU-AMP MOD:00611 iodouridine monophosphate derivatized residue A protein modification that is produced by reaction of iodouridine monophosphate with a residue. PubMed:11112526 PubMed:11567090 PubMed:6540775 Unimod:292 Cross-link of (Iodo)-uracil MP with W,F,Y IodoU-AMP A protein modification that is produced by derivatization of a residue with 3,3-dithiobis[sulfosuccinimidyl propanoate], DTSSP, or with Pierce EZ-Link Sulfo-NHS-SS-Biotin reagent, sulfosuccinimidyl 3-[(2-[biotinamido]ethyl)disulfanyl]propanoate, followed by reduction with dithiothreitol and then reaction with iodoacetamide. 145.18 C 5 H 7 N 1 O 2 S 1 145.01974 X artifact Unimod:293 PSI-MOD 3-(carbamidomethylthio)propanoyl CAMthiopropanoyl MOD:00612 3-(carboxamidomethylthio)propanoylated residue A protein modification that is produced by derivatization of a residue with 3,3-dithiobis[sulfosuccinimidyl propanoate], DTSSP, or with Pierce EZ-Link Sulfo-NHS-SS-Biotin reagent, sulfosuccinimidyl 3-[(2-[biotinamido]ethyl)disulfanyl]propanoate, followed by reduction with dithiothreitol and then reaction with iodoacetamide. PubMed:15121203 Unimod:293 3-(carbamidomethylthio)propanoyl CAMthiopropanoyl modification from Unimod Chemical derivative 326.42 C 14 H 22 N 4 O 3 S 1 326.14127 C 17 H 27 N 5 O 4 S 2 429.55 429.15045 C artifact Unimod:294 PSI-MOD IED-Biotin biotinoyl-iodoacetyl-ethylenediamine MOD:00613 biotinoyl-iodoacetyl-ethylenediamine modification from Unimod Chemical derivative PubMed:10906242 Unimod:294 IED-Biotin biotinoyl-iodoacetyl-ethylenediamine A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a fucose (6-deoxy-D-galactose) group through a glycosidic bond. 146.14 C 6 H 10 O 4 146.0579 X natural GNO:G49112ZN Unimod:295 Fuc PSI-MOD Fucose dHex MOD:00614 fucosylated residue A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a fucose (6-deoxy-D-galactose) group through a glycosidic bond. PubMed:11344537 PubMed:15189151 Unimod:295 Fuc Fucose dHex OBSOLETE because entry Unimod:261 site N-term R was abandoned. Remap to MOD:00584 MOD:00584 215.24 C 7 H 5 N 1 O 3 S 2 214.97108 R artifact N-term Unimod:261 PSI-MOD MOD:00615 4-sulfophenyl isothiocyante modification to N-term R true OBSOLETE because entry Unimod:261 site N-term R was abandoned. Remap to MOD:00584 PubMed:14689565 Unimod:261 Natural or modified residues that are isobaric at a resolution below 0.1 Da. PSI-MOD MOD:00616 residues isobaric at a resolution below 0.1 Da Natural or modified residues that are isobaric at a resolution below 0.1 Da. PubMed:18688235 A protein modification that effectively converts a residue containing common isotopes to a 3x(2)H labeled residue methyl ester. 17.03 C 1 (1)H -1 (2)H 3 17.03448 X artifact C-term Unimod:298 ctermpeptrideuteromethyl PSI-MOD Methyl:2H(3) deuterated methyl ester MOD:00617 3x(2)H residue methyl ester A protein modification that effectively converts a residue containing common isotopes to a 3x(2)H labeled residue methyl ester. OMSSA:21 Unimod:298 ctermpeptrideuteromethyl Methyl:2H(3) deuterated methyl ester modification from Unimod Chemical derivative 44.01 C 1 O 2 43.98983 C 12 H 10 N 2 O 3 230.22 230.06914 W artifact Unimod:299 PSI-MOD Carboxy Carboxylation MOD:00618 There is no literature citation for this Unimod entry [JSG]. tryptophan carboxylation modification from Unimod Chemical derivative Unimod:299#W Carboxy Carboxylation OBSOLETE because entry 300 is redundant with Unimod 6 remap to MOD:01328 MOD:01328 58.04 C 2 H 2 O 2 58.005478 W artifact Unimod:300 PSI-MOD MOD:00619 hydroxylethanone true OBSOLETE because entry 300 is redundant with Unimod 6 remap to MOD:01328 Unimod:300 modification from Unimod Chemical derivative 190.2 C 10 H 10 N 2 O 2 190.07423 C 13 H 15 N 3 O 3 S 1 293.34 293.0834 C artifact Unimod:301 PSI-MOD Bromobimane Monobromobimane derivative MOD:00620 1-(bromomethyl)-2,6,7-trimethylpyrazolo[1,2-a]pyrazole-3,5-dione, C 10 H 11 Br 1 N 2 O 2. cysteine monobromobimane derivative modification from Unimod Chemical derivative PubMed:7856876 Unimod:301 Bromobimane Monobromobimane derivative modification from Unimod Chemical derivative 170.17 C 11 H 6 O 2 170.03677 X artifact Unimod:302 PSI-MOD Menadione Menadione quinone derivative MOD:00621 menadione quinone derivative modification from Unimod Chemical derivative PubMed:15939799 Unimod:302 Menadione Menadione quinone derivative modification from Unimod Chemical derivative 76.11 C 2 H 4 O 1 S 1 75.99828 C 5 H 9 N 1 O 2 S 2 179.25 179.00748 C artifact Unimod:303 Beta mercaptoethanol adduct PSI-MOD Cysteine mercaptoethanol DeStreak MOD:00622 From DeltaMass: Average Mass: 76 Average Mass Change:76 PubMed:8019414. cysteine mercaptoethanol modification from Unimod Chemical derivative DeltaMass:80 PubMed:12442261 Unimod:303 Beta mercaptoethanol adduct Cysteine mercaptoethanol DeStreak modification from Unimod N-linked glycosylation 1443.33 C 56 H 90 N 4 O 39 1442.5182 C 60 H 96 N 6 O 41 1557.43 1556.5612 N natural GNO:G25987BV Unimod:305 PSI-MOD Fucosylated biantennary (-2 galactose) dHex(1)Hex(3)HexNAc(4) MOD:00623 fucosylated biantennary (-2 galactose) N4-glycosylated asparagine modification from Unimod N-linked glycosylation Unimod:305 Fucosylated biantennary (-2 galactose) dHex(1)Hex(3)HexNAc(4) Natural or modified residues with a mass of 113.0-113.1 Da. PSI-MOD MOD:00624 residues isobaric at 113.0-113.1 Da Natural or modified residues with a mass of 113.0-113.1 Da. PubMed:18688235 modification from Unimod Chemical derivative 111.1 C 5 H 5 N 1 O 2 111.03203 X artifact Unimod:314 PSI-MOD Nmethylmaleimide MOD:00625 N-methylmaleimide derivatized residue modification from Unimod Chemical derivative Unimod:314 Nmethylmaleimide Nmethylmaleimide modification from Unimod Chemical derivative 421.43 C 21 H 15 N 3 O 5 S 1 421.07324 X artifact Unimod:478 PSI-MOD FTC fluorescein-5-thiosemicarbazide MOD:00626 fluorescein-5-thiosemicarbazide modified residue modification from Unimod Chemical derivative PubMed:2883911 Unimod:478 FTC fluorescein-5-thiosemicarbazide modification from Unimod Chemical derivative 78.11 C 6 H 6 78.04695 C 12 H 18 N 2 O 1 206.29 206.1419 K artifact Unimod:316 (2S)-2-amino-6-(2,5-dimethylpyrrolidin-1-yl)hexanoic acid 6-(2,5-dimethylpyrrolidin-1-yl)norleucine PSI-MOD 2,5-dimethypyrrole DimethylpyrroleAdduct MOD:00627 There is no citation for this Unimod entry. Add PubMed:7981420, correct spelling [JSG]. 2,5-dimethylpyrrole lysine from 2,5-hexanedione adduct modification from Unimod Chemical derivative Unimod:316 (2S)-2-amino-6-(2,5-dimethylpyrrolidin-1-yl)hexanoic acid 6-(2,5-dimethylpyrrolidin-1-yl)norleucine 2,5-dimethypyrrole DimethylpyrroleAdduct a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with two hexose sugar groups through glycosidic bonds 324.28 C 12 H 20 O 10 324.10565 X natural GNO:G90627TW PSI-MOD MOD:00628 Hex2 a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with two hexose sugar groups through glycosidic bonds PubMed:18688235 modification from Unimod Chemical derivative 62.07 C 5 H 2 62.01565 C 11 H 14 N 2 O 1 190.25 190.11061 K artifact Unimod:318 PSI-MOD Delta:H(2)C(5) MDA adduct +62 MOD:00629 Usually major adduct formed from malondialdehyde (MDA) with the amino group of lysine residues [UniProt]. MDA adduct +62 modification from Unimod Chemical derivative Unimod:318 Delta:H(2)C(5) MDA adduct +62 modification from Unimod Chemical derivative 54.05 C 3 H 2 O 1 54.010567 X artifact Unimod:319 PSI-MOD Delta:H(2)C(3)O(1) MDA adduct +54 MOD:00630 This is not a legitimate ontological entry and will become obsolete when the children are reassigned [JSG] C3-H2-O adduct (+54 amu) of malondialdehyde with lysine or methylglyoxal with arginine. modification from Unimod Chemical derivative PubMed:9328283 Unimod:319 Delta:H(2)C(3)O(1) MDA adduct +54 modification from Unimod Chemical derivative 143.14 C 6 H 9 N 1 O 3 143.05824 X artifact Unimod:320 PSI-MOD Nethylmaleimide+water Nethylmaleimidehydrolysis MOD:00631 N-ethylmaeimide adduct + H20 (a mixture of isobaric products) [JSG]. hydrolyzed N-ethylmaleimide adduct modification from Unimod Chemical derivative Unimod:320 Nethylmaleimide+water Nethylmaleimidehydrolysis OBSOLETE because this chemical derivative modification from Unimod 321 is deprecated. -17.01 H -1 O -1 -17.00274 N artifact Unimod:321 PSI-MOD MOD:00632 N-succinimide true OBSOLETE because this chemical derivative modification from Unimod 321 is deprecated. Unimod:321 modification from Unimod Chemical derivative 713.57 C 31 H 30 I 1 N 4 O 6 S 1 713.0931 C 34 H 35 I 1 N 5 O 7 S 2 816.71 816.10223 C artifact Unimod:323 bis-((N-iodoacetyl)piperazinyl)sulfonerhodamine PSI-MOD Xlink:B10621 bis-N-I-sulfonerahodamine MOD:00633 Invitrogen B-10621, a red fluorescent cross-linking reagent (only link to Cys is indicated) [Unimod]. bis-N-I-sulfonerahodamine modification from Unimod Chemical derivative Unimod:323 bis-((N-iodoacetyl)piperazinyl)sulfonerhodamine Xlink:B10621 bis-N-I-sulfonerahodamine modification from Unimod Chemical derivative 123.6 C 3 Cl 1 H 6 N 1 S 1 122.99095 X artifact Unimod:324 PSI-MOD DTBP dimethyl 3,3'-dithiobispropionimidate MOD:00634 Pierce reagent, needs sites for N, Q, R, K, and N-term [JSG]. dimethyl 3,3'-dithiobispropionimidate modification from Unimod Chemical derivative PubMed:770170 Unimod:324 DTBP dimethyl 3,3'-dithiobispropionimidate modification from Unimod Chemical derivative 572.75 C 27 H 49 N 4 O 5 P 1 S 1 572.3161 C 30 H 54 N 5 O 7 P 1 S 1 659.82 659.34814 S artifact Unimod:325 PSI-MOD 10-ethoxyphosphinyl-N-(biotinamidopentyl)decanamide FP-Biotin MOD:00635 10-fluoroethoxyphosphinyl-N-(biotinamidopentyl)decanamide modification from Unimod Chemical derivative PubMed:10611275 Unimod:325 10-ethoxyphosphinyl-N-(biotinamidopentyl)decanamide FP-Biotin A protein modification that effectively converts an L-serine residue to S-ethylcysteine. 44.11 C 2 H 4 O -1 S 1 44.008457 C 5 H 9 N 1 O 1 S 1 131.19 131.04048 S artifact Unimod:327 PSI-MOD Delta:H(4)C(2)O(-1)S(1) S-Ethylcystine from Serine MOD:00636 Modification from Unimod. Phosphoserine is converted to dehydroalanine then by Michael addition of ethanethiol to S-ethylcysteine. Needs parent and sibling for S-ethyl-cysteine. S-ethylcysteine (Ser) A protein modification that effectively converts an L-serine residue to S-ethylcysteine. Unimod:327 Delta:H(4)C(2)O(-1)S(1) S-Ethylcystine from Serine A protein modification that effectively replaces one hydrogen atom of an L-arginine residue with a (13)C,3x(2)H labeled methyl group to form a 1x(13)C,3x(2)H labeled monomethylated L-arginine. 18.04 (13)C 1 (1)H -1 (2)H 3 18.037834 (12)C 6 (13)C 1 (1)H 11 (2)H 3 N 4 O 1 174.14 174.13895 R artifact Unimod:329 PSI-MOD Methyl:2H(3)13C(1) monomethylated arginine MOD:00637 1x(13)C,3x(2)H labeled monomethylated L-arginine A protein modification that effectively replaces one hydrogen atom of an L-arginine residue with a (13)C,3x(2)H labeled methyl group to form a 1x(13)C,3x(2)H labeled monomethylated L-arginine. Unimod:329 Methyl:2H(3)13C(1) monomethylated arginine A protein modification that effectively replaces two hydrogen atoms of an L-arginine residue with two (13)C,3x(2)H labeled methyl groups to form a 2x(13)C,6x(2)H labeled dimethylated L-arginine. 36.08 (13)C 2 (1)H -2 (2)H 6 36.07567 (12)C 6 (13)C 2 (1)H 10 (2)H 6 N 4 O 1 192.18 192.17679 R artifact Unimod:330 PSI-MOD Dimethyl:2H(6)13C(2) dimethylated arginine MOD:00638 2x(13)C,6x(2)H labeled dimethylated L-arginine A protein modification that effectively replaces two hydrogen atoms of an L-arginine residue with two (13)C,3x(2)H labeled methyl groups to form a 2x(13)C,6x(2)H labeled dimethylated L-arginine. PubMed:15782174 Unimod:330 Dimethyl:2H(6)13C(2) dimethylated arginine modification from Unimod Chemical derivative 525.66 C 19 H 34 N 4 O 5 P 1 S 3 525.1429 X artifact Unimod:332 PSI-MOD Thiophos-S-S-biotin thiophosphate labeled with biotin-HPDP MOD:00639 thiophosphate labeled with biotin-HPDP modification from Unimod Chemical derivative Unimod:332 Thiophos-S-S-biotin thiophosphate labeled with biotin-HPDP modification from Unimod Chemical derivative 467.54 C 19 F 1 H 35 N 3 O 5 P 1 S 1 467.2019 C 22 F 1 H 40 N 4 O 7 P 1 S 1 554.62 554.23395 S artifact Unimod:333 PSI-MOD 6-N-biotinylaminohexyl isopropyl phosphate Can-FP-biotin MOD:00640 6-N-biotinylaminohexyl isopropyl phosphorofluoridate modification from Unimod Chemical derivative Unimod:333 6-N-biotinylaminohexyl isopropyl phosphate Can-FP-biotin OBSOLETE because Unimod entry 334 is merged with Unimod 293. Remap to MOD:00612 MOD:00612 146.18 C 5 H 8 N 1 O 2 S 1 146.02757 K artifact Unimod:334 PSI-MOD MOD:00641 CAMthiopropanoyl of Lys true OBSOLETE because Unimod entry 334 is merged with Unimod 293. Remap to MOD:00612 Unimod:334 A protein modification produced by formation of an adduct of a residue with 4-hydroxynonenal artificially reduced by a reagent such as NaBH4. 158.24 C 9 H 18 O 2 158.13068 X artifact Unimod:335 PSI-MOD HNE+Delta:H(2) reduced 4-Hydroxynonenal MOD:00642 4-hydroxynonenal, a toxic lipid aldehyde, is a product of the hydroperoxide beta-cleavage degradation of omega-6 polyunsaturated fatty acids, such as arachidonic and linoleic acids [JSG]. reduced 4-hydroxynonenal adduct A protein modification produced by formation of an adduct of a residue with 4-hydroxynonenal artificially reduced by a reagent such as NaBH4. PubMed:11910026 PubMed:15133838 Unimod:335 HNE+Delta:H(2) reduced 4-Hydroxynonenal modification from Unimod Artifact 13.04 C 1 H 3 N 1 O -1 13.031634 X artifact Unimod:337 PSI-MOD Methylamine Michael addition with methylamine MOD:00643 methylamine Michael addition derivatized residue modification from Unimod Artifact PubMed:11968134 Unimod:337 Methylamine Michael addition with methylamine A protein modification that effectively replaces a residue hydroxyl group with an acetoxy group. 42.04 C 2 H 2 O 1 42.010567 X natural OAcRes PSI-MOD MOD:00644 mono O-acetylated residue A protein modification that effectively replaces a residue hydroxyl group with an acetoxy group. PubMed:18688235 OAcRes A protein modification that effectively replaces a residue sulfanyl group with an acetylsulfanyl group. 42.04 C 2 H 2 O 1 S 0 42.010567 X natural SAcRes PSI-MOD MOD:00645 mono S-acetylated residue A protein modification that effectively replaces a residue sulfanyl group with an acetylsulfanyl group. PubMed:18688235 SAcRes A protein modification that effectively converts an L-cysteine residue to either N-acetyl-L-cysteine or S-acetyl-L-cysteine. 42.04 C 2 H 2 N 0 O 1 S 0 42.010567 C 5 H 7 N 1 O 2 S 1 145.18 145.01974 C natural AcCys PSI-MOD MOD:00646 monoacetylated L-cysteine A protein modification that effectively converts an L-cysteine residue to either N-acetyl-L-cysteine or S-acetyl-L-cysteine. PubMed:18688235 AcCys A protein modification that effectively converts an L-serine residue to either N-acetyl-L-serine, O-acetyl-L-serine, or N,O-diacetyl-L-serine. 42.04 C 2 H 2 N 0 O 1 42.010567 S natural AcSer PSI-MOD MOD:00647 monoacetylated L-serine A protein modification that effectively converts an L-serine residue to either N-acetyl-L-serine, O-acetyl-L-serine, or N,O-diacetyl-L-serine. PubMed:18688235 AcSer A protein modification that effectively converts an L-serine residue to N,O-diacetyl-L-serine. 84.07 C 4 H 4 N 0 O 2 84.021126 C 7 H 10 N 1 O 4 172.16 172.06099 S artifact N-term (S)-2-acetamido-3-acetyloxypropanoic acid N,O-diacetyl-L-serine N,O-diacetylserine NOAc2Ser PSI-MOD MOD:00648 In one paper, the samples were prepared using glacial acetic acid, and were probably artifactual [JSG]. N,O-diacetylated L-serine A protein modification that effectively converts an L-serine residue to N,O-diacetyl-L-serine. PubMed:16731519 PubMed:489587 PubMed:7309355 RESID:AA0051#var RESID:AA0364#var (S)-2-acetamido-3-acetyloxypropanoic acid N,O-diacetyl-L-serine N,O-diacetylserine NOAc2Ser A protein modification that effectively replaces a hydrogen atom with an acyl group. AcylRes PSI-MOD MOD:00649 acylated residue A protein modification that effectively replaces a hydrogen atom with an acyl group. PubMed:18688235 AcylRes A protein modification that effectively replaces a residue amino group with a myristoylamino group. 210.36 C 14 H 26 O 1 210.19836 X natural NMyrRes PSI-MOD MOD:00650 N-myristoylated residue A protein modification that effectively replaces a residue amino group with a myristoylamino group. PubMed:18688235 NMyrRes A protein modification that effectively replaces a residue amino group with a palmitoylamino group. 238.41 C 16 H 30 O 1 238.22966 X natural N-hexadecanoylated residue NPamRes PSI-MOD MOD:00651 N-palmitoylated residue A protein modification that effectively replaces a residue amino group with a palmitoylamino group. PubMed:18688235 N-hexadecanoylated residue NPamRes A protein modification that effectively replaces a residue hydroxyl group with a palmitoyloxy group. 238.41 C 16 H 30 O 1 238.22966 X natural O-hexadecanoylated residue OPamRes PSI-MOD MOD:00652 O-palmitoylated residue A protein modification that effectively replaces a residue hydroxyl group with a palmitoyloxy group. PubMed:18688235 O-hexadecanoylated residue OPamRes A protein modification that effectively replaces a residue sulfanyl group with an palmitoylsulfanyl group. 238.41 C 16 H 30 O 1 S 0 238.22966 X natural S-hexadecanoylated residue SPamRes PSI-MOD MOD:00653 S-palmitoylated residue A protein modification that effectively replaces a residue sulfanyl group with an palmitoylsulfanyl group. PubMed:18688235 S-hexadecanoylated residue SPamRes a protein modification that effectively replaces a sulfanyl group with a methylsulfanyl group SMeRes PSI-MOD MOD:00654 S-methylated residue a protein modification that effectively replaces a sulfanyl group with a methylsulfanyl group PubMed:18688235 SMeRes A protein modification that effectively replaces a residue sulfanyl group with an myristoylsulfanyl group. 210.36 C 14 H 26 O 1 S 0 210.19836 X natural SMyrRes PSI-MOD MOD:00655 S-myristoylated residue A protein modification that effectively replaces a residue sulfanyl group with an myristoylsulfanyl group. PubMed:18688235 SMyrRes A protein modification that effectively replaces a residue hydrocarbyl hydrogen with an methyl group. CMeRes PSI-MOD MOD:00656 C-methylated residue A protein modification that effectively replaces a residue hydrocarbyl hydrogen with an methyl group. PubMed:18688235 CMeRes A protein modification that effectively converts an L-glutamine residue to L-glutamate 5-methyl ester. 15.01 C 1 H 1 N -1 O 1 14.999666 C 6 H 9 N 1 O 3 143.14 143.05824 Q natural Unimod:528 uniprot.ptm:PTM-0127 (2S)-2-amino-5-methoxy-5-oxopentanoic acid (5)-methyl L-hydrogen glutamate 2-aminopentanedioic acid 5-methyl ester 5-methyl L-2-aminoglutarate 5-methyl L-glutamate L-glutamic acid 5-methyl ester MOD_RES Glutamate methyl ester (Gln) O5MeGlu(Gln) deamidated 5-methyl esterified glutamine glutamic acid 5-methyl ester glutamic acid gamma-methyl ester PSI-MOD Deamidation followed by a methylation Methyl+Deamidated MOD:00657 This is known to be a natural modification of glutamine in prokaryotes. L-glutamic acid 5-methyl ester (Gln) A protein modification that effectively converts an L-glutamine residue to L-glutamate 5-methyl ester. PubMed:16888 PubMed:6300110 RESID:AA0072#GLN Unimod:528 (2S)-2-amino-5-methoxy-5-oxopentanoic acid (5)-methyl L-hydrogen glutamate 2-aminopentanedioic acid 5-methyl ester 5-methyl L-2-aminoglutarate 5-methyl L-glutamate L-glutamic acid 5-methyl ester MOD_RES Glutamate methyl ester (Gln) O5MeGlu(Gln) deamidated 5-methyl esterified glutamine glutamic acid 5-methyl ester glutamic acid gamma-methyl ester Deamidation followed by a methylation Methyl+Deamidated A protein modification that effectively converts an L-arginine residue to a methylated arginine, either 5-methylargine, N5-methylarginine, or an omega-N-methylated L-arginine. R uniprot.ptm:PTM-0238 MeArg PSI-MOD MOD:00658 methylated arginine A protein modification that effectively converts an L-arginine residue to a methylated arginine, either 5-methylargine, N5-methylarginine, or an omega-N-methylated L-arginine. PubMed:18688235 MeArg A protein modification that effectively converts an L-glutamine residue to a methylated glutamine, either 2-methylated glutamine, N5-methylated glutamine, or methyl esterified deamidated glutamine. Q natural MeGln PSI-MOD MOD:00659 methylated glutamine A protein modification that effectively converts an L-glutamine residue to a methylated glutamine, either 2-methylated glutamine, N5-methylated glutamine, or methyl esterified deamidated glutamine. PubMed:18688235 MeGln A protein modification that effectively converts an L-cysteine residue to a methylated cysteine, either S-methylcysteine, or cysteine methyl ester. C natural MeCys PSI-MOD MOD:00660 methylated cysteine A protein modification that effectively converts an L-cysteine residue to a methylated cysteine, either S-methylcysteine, or cysteine methyl ester. PubMed:18688235 MeCys A protein modification that effectively converts an L-histidine residue to a methylated histidine, such as pros-methylhistidine, or tele-methylhistidine. H natural MeHis PSI-MOD MOD:00661 methylated histidine A protein modification that effectively converts an L-histidine residue to a methylated histidine, such as pros-methylhistidine, or tele-methylhistidine. PubMed:18688235 MeHis A protein modification that effectively converts an L-leucine residue to a methylated leucine, either N-methylleucine, or leucine methyl ester. L natural MeLeu PSI-MOD MOD:00662 methylated leucine A protein modification that effectively converts an L-leucine residue to a methylated leucine, either N-methylleucine, or leucine methyl ester. PubMed:18688235 MeLeu A protein modification that effectively converts an L-lysine residue to a methylated lysine. K natural uniprot.ptm:PTM-0193 MeLys PSI-MOD MOD:00663 methylated lysine A protein modification that effectively converts an L-lysine residue to a methylated lysine. PubMed:18688235 MeLys A protein modification that effectively replaces a residue L-enantiomer (stereoisomer) with a D-enantiomer or with a different diastereomeric isomer. D-Res PSI-MOD MOD:00664 stereoisomerized residue A protein modification that effectively replaces a residue L-enantiomer (stereoisomer) with a D-enantiomer or with a different diastereomeric isomer. PubMed:18688235 D-Res A protein modification that effectively converts an L-alanine residue to a methylated alanine, such as N-methylalanine, N,N-dimethylalanine, or N,N,N-trimethylalanine. A natural MeAla PSI-MOD MOD:00665 methylated alanine A protein modification that effectively converts an L-alanine residue to a methylated alanine, such as N-methylalanine, N,N-dimethylalanine, or N,N,N-trimethylalanine. PubMed:18688235 MeAla A protein modification that effectively replaces a hydrogen atom with an octanoyl group. 126.2 C 8 H 14 N 0 O 1 126.10446 X natural OctRes PSI-MOD MOD:00666 octanoylated residue A protein modification that effectively replaces a hydrogen atom with an octanoyl group. PubMed:18688235 OctRes A protein modification that effectively replaces a hydrogen atom with a decanoyl group. 154.25 C 10 H 18 N 0 O 1 154.13576 X natural DecRes PSI-MOD MOD:00667 decanoylated residue A protein modification that effectively replaces a hydrogen atom with a decanoyl group. PubMed:18688235 DecRes A protein modification that effectively replaces a residue hydroxyl group with a decanoyloxy group. 154.25 C 10 H 18 N 0 O 1 154.13576 X natural Unimod:449 ODecRes PSI-MOD Decanoyl lipid MOD:00668 O-decanoylated residue A protein modification that effectively replaces a residue hydroxyl group with a decanoyloxy group. Unimod:449 ODecRes Decanoyl lipid A protein modification that effectively replaces a residue hydroxyl group with a octanoyloxy group. 126.2 C 8 H 14 N 0 O 1 126.10446 X natural Unimod:426 OOctRes PSI-MOD Octanoyl octanoyl MOD:00669 O-octanoylated residue A protein modification that effectively replaces a residue hydroxyl group with a octanoyloxy group. Unimod:426 OOctRes Octanoyl octanoyl A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an acyl group. NAcylRes PSI-MOD MOD:00670 N-acylated residue A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an acyl group. PubMed:18688235 NAcylRes A protein modification that effectively replaces a residue hydroxyl group with a acyloxy group. OAcylRes PSI-MOD MOD:00671 O-acylated residue A protein modification that effectively replaces a residue hydroxyl group with a acyloxy group. PubMed:18688235 OAcylRes A protein modification that effectively replaces a residue sulfanyl group with an acylsulfanyl group. SAcylRes PSI-MOD MOD:00672 S-acylated residue A protein modification that effectively replaces a residue sulfanyl group with an acylsulfanyl group. PubMed:18688235 SAcylRes A protein modification that effectively converts an L-asparagine residue to a methylated asparagine, such as N4-methyl-L-asparagine, or N4,N4-dimethyl-L-asparagine. N natural MeAsn PSI-MOD MOD:00673 methylated asparagine A protein modification that effectively converts an L-asparagine residue to a methylated asparagine, such as N4-methyl-L-asparagine, or N4,N4-dimethyl-L-asparagine. PubMed:18688235 MeAsn A protein modification that effectively replaces a carboxyl group with a carboxamido group. -0.98 C 0 H 1 N 1 O -1 -0.984016 X PSI-MOD MOD:00674 amidated residue A protein modification that effectively replaces a carboxyl group with a carboxamido group. PubMed:18688235 A protein modification that effectively either removes neutral hydrogen atoms (proton and electron), or adds oxygen atoms to a residue with or without the removal of hydrogen atoms. X OxRes PSI-MOD MOD:00675 oxidized residue A protein modification that effectively either removes neutral hydrogen atoms (proton and electron), or adds oxygen atoms to a residue with or without the removal of hydrogen atoms. PubMed:18688235 OxRes A protein modification that effectively adds oxygen atoms to a residue with or without the removal of hydrogen atoms. X OxyRes PSI-MOD MOD:00676 oxygenated residue A protein modification that effectively adds oxygen atoms to a residue with or without the removal of hydrogen atoms. PubMed:18688235 OxyRes A protein modification that effectively replaces a hydrogen atom with an hydroxyl group. X HyRes Hydroxylation (of delta C of Lysine, beta C of Tryptophan, C3 or C4 of Proline, beta C of Aspartate) PSI-MOD MOD:00677 From DeltaMass: Average Mass: 16 hydroxylated residue A protein modification that effectively replaces a hydrogen atom with an hydroxyl group. DeltaMass:0 HyRes Hydroxylation (of delta C of Lysine, beta C of Tryptophan, C3 or C4 of Proline, beta C of Aspartate) A protein modification that effectively converts an L-proline residue to an hydroxylated L-proline. P HyPro PSI-MOD MOD:00678 hydroxylated proline A protein modification that effectively converts an L-proline residue to an hydroxylated L-proline. PubMed:18688235 HyPro A protein modification that effectively adds oxygen atoms to a carbon atom of a residue and removes hydrogen atoms. COxyRes PSI-MOD MOD:00679 carbon oxygenated residue A protein modification that effectively adds oxygen atoms to a carbon atom of a residue and removes hydrogen atoms. PubMed:18688235 COxyRes A protein modification that effectively adds oxygen atoms to a sulfur atom of a residue without removing hydrogen atoms. SOxyRes PSI-MOD MOD:00680 sulfur oxygenated residue A protein modification that effectively adds oxygen atoms to a sulfur atom of a residue without removing hydrogen atoms. PubMed:18688235 SOxyRes A protein modification that effectively converts an L-lysine residue to a hydroxylated L-lysine. K HyLys PSI-MOD MOD:00681 hydroxylated lysine A protein modification that effectively converts an L-lysine residue to a hydroxylated L-lysine. PubMed:18688235 HyLys A protein modification that effectively converts an L-arginine residue to a hydroxylated L-arginine. R uniprot.ptm:PTM-0498 HyArg PSI-MOD MOD:00682 hydroxylated arginine A protein modification that effectively converts an L-arginine residue to a hydroxylated L-arginine. PubMed:18688235 HyArg A protein modification that effectively removes neutral hydrogen atoms (proton and electron) from a residue. X dHRes PSI-MOD MOD:00683 dehydrogenated residue A protein modification that effectively removes neutral hydrogen atoms (proton and electron) from a residue. PubMed:18688235 dHRes A protein modification that effectively converts an L-asparagine residue to L-aspartic acid. 0.98 C 0 H -1 N -1 O 1 0.984016 C 4 H 5 N 1 O 3 115.09 115.02694 N natural Unimod:7 uniprot.ptm:PTM-0116 (2S)-2-aminobutanedioic acid 2-azanylbutanedioic acid L-aspartic acid MOD_RES Deamidated asparagine aminosuccinic acid dNAsn PSI-MOD MOD:00684 incidental to RESID:AA0059 deamidated L-asparagine A protein modification that effectively converts an L-asparagine residue to L-aspartic acid. PubMed:1097438 PubMed:339692 PubMed:4399050 PubMed:5764436 PubMed:6692818 PubMed:8089117 PubMed:9521123 PubMed:9582379 RESID:AA0004#ASN Unimod:7#N (2S)-2-aminobutanedioic acid 2-azanylbutanedioic acid L-aspartic acid MOD_RES Deamidated asparagine aminosuccinic acid dNAsn A protein modification that effectively converts an L-glutamine residue to L-glutamic acid. 0.98 C 0 H -1 N -1 O 1 0.984016 C 5 H 7 N 1 O 3 129.12 129.04259 Q natural Unimod:7 uniprot.ptm:PTM-0117 (2S)-2-aminopentanedioic acid 1-aminopropane-1,3-dicarboxylic acid 2-aminoglutaric acid 2-azanylpentanedioic acid L-glutamic acid MOD_RES Deamidated glutamine alpha-aminoglutaric acid dNGln glutaminic acid PSI-MOD MOD:00685 deamidated L-glutamine A protein modification that effectively converts an L-glutamine residue to L-glutamic acid. PubMed:1881881 PubMed:4565668 PubMed:4922541 PubMed:6692818 PubMed:9192900 PubMed:957425 RESID:AA0006#GLN Unimod:7#Q (2S)-2-aminopentanedioic acid 1-aminopropane-1,3-dicarboxylic acid 2-aminoglutaric acid 2-azanylpentanedioic acid L-glutamic acid MOD_RES Deamidated glutamine alpha-aminoglutaric acid dNGln glutaminic acid A protein modification that effectively converts an L-cysteine residue to L-selenocysteine (not known as a natural, post-translational modification process). 46.91 C 0 H 0 N 0 O 0 S -1 Se 1 47.94445 C 3 H 5 N 1 O 1 Se 1 150.05 150.95363 C artifact Unimod:162 (2R)-2-amino-3-selanylpropanoic acid 2-azanyl-3-selanylpropanoic acid 3-selenylalanine L-selenocysteine NON_STD Selenocysteine SeCys Sec(Cys) selenium cysteine PSI-MOD MOD:00686 This entry is for the artifactual formation of L-selenocysteine from cysteine. For encoded L-selenocysteine, use MOD:00031 [JSG]. L-selenocysteine (Cys) A protein modification that effectively converts an L-cysteine residue to L-selenocysteine (not known as a natural, post-translational modification process). PubMed:10523135 PubMed:2037562 PubMed:2963330 PubMed:6217842 PubMed:6714945 RESID:AA0022#CYS Unimod:162#C (2R)-2-amino-3-selanylpropanoic acid 2-azanyl-3-selanylpropanoic acid 3-selenylalanine L-selenocysteine NON_STD Selenocysteine SeCys Sec(Cys) selenium cysteine A protein modification that crosslinks two residues by formation of a thioether bond between a cysteine thiol and either an alkyl C as in lanthionine, or an aryl C as 2'-(S-cysteinyl)-L-histidine. PSI-MOD MOD:00687 thioether crosslinked residues A protein modification that crosslinks two residues by formation of a thioether bond between a cysteine thiol and either an alkyl C as in lanthionine, or an aryl C as 2'-(S-cysteinyl)-L-histidine. PubMed:18688235 A protein modification that crosslinks two residues with an amide bond where either the donor amino or carboxyl is not an alpha group. PSI-MOD MOD:00688 isopeptide crosslinked residues A protein modification that crosslinks two residues with an amide bond where either the donor amino or carboxyl is not an alpha group. PubMed:18688235 A protein modification that crosslinks two cysteine residues by formation of a disulfide bond. PSI-MOD MOD:00689 disulfide crosslinked residues A protein modification that crosslinks two cysteine residues by formation of a disulfide bond. PubMed:18688235 A protein modification that crosslinks two residues by formation of an oxazole or thiazole ring. PSI-MOD MOD:00690 oxazole/thiazole ring crosslinked residues A protein modification that crosslinks two residues by formation of an oxazole or thiazole ring. PubMed:18688235 A protein modification that crosslinks two residues by formation of an 5-imidazolinone ring. PSI-MOD MOD:00691 5-imidazolinone ring crosslinked residues A protein modification that crosslinks two residues by formation of an 5-imidazolinone ring. PubMed:18688235 A protein crosslink modification that is not chemically categorized. PSI-MOD MOD:00692 uncategorized crosslinked residues A protein crosslink modification that is not chemically categorized. PubMed:18688235 A protein modification that effectively replaces a hydrogen atom with an carbohydrate-like group through a glycosidic bond. natural GlycoRes PSI-MOD MOD:00693 glycosylated residue A protein modification that effectively replaces a hydrogen atom with an carbohydrate-like group through a glycosidic bond. PubMed:18688235 GlycoRes A protein modification that effectively substitutes a halogen atom for a hydrogen atom. HalRes halogenated residue PSI-MOD MOD:00694 halogen containing residue A protein modification that effectively substitutes a halogen atom for a hydrogen atom. PubMed:18688235 HalRes halogenated residue A protein modification that effectively substitutes a sulfonyl group for the hydrogen atom of a hydroxyl or sulfanyl group. 80.06 O 3 S 1 79.95682 X natural Unimod:40 SulfRes Sulphonation (SO3H) (of PMC group) PSI-MOD O-Sulfonation Sulfo MOD:00695 From DeltaMass: Average Mass: 80. sulfated residue A protein modification that effectively substitutes a sulfonyl group for the hydrogen atom of a hydroxyl or sulfanyl group. DeltaMass:0 PubMed:14752058 Unimod:40 SulfRes Sulphonation (SO3H) (of PMC group) O-Sulfonation Sulfo A protein modification that effectively replaces a hydrogen atom with a phosphono group (H2PO3 or 'phosphate'). 79.98 H 1 O 3 P 1 79.96633 X Unimod:21 PhosRes Phosphorylation (O of Serine, Threonine, Tyrosine and Aspartate, N epsilon of Lysine) PSI-MOD Phospho Phosphorylation MOD:00696 From DeltaMass: Average Mass: 80. phosphorylated residue A protein modification that effectively replaces a hydrogen atom with a phosphono group (H2PO3 or 'phosphate'). DeltaMass:0 Unimod:21 PhosRes Phosphorylation (O of Serine, Threonine, Tyrosine and Aspartate, N epsilon of Lysine) Phospho Phosphorylation A protein modification that effectively results from forming an adduct with a compound containing a flavin group. X natural FlavRes PSI-MOD FAD Flavin adenine dinucleotide MOD:00697 flavin modified residue FlavRes FAD Flavin adenine dinucleotide A protein modification that effectively substitutes a metal atom or a metal cluster for hydrogen atoms, or coordinates a metal ion. MetalRes PSI-MOD MOD:00698 metal or metal cluster containing modified residue A protein modification that effectively substitutes a metal atom or a metal cluster for hydrogen atoms, or coordinates a metal ion. PubMed:18688235 MetalRes A protein modification that effectively results from forming an adduct with a compound containing a porphyrin group. PorphRes PSI-MOD MOD:00699 porphyrin modified residue A protein modification that effectively results from forming an adduct with a compound containing a porphyrin group. PubMed:18688235 PorphRes A protein modification that effectively results from forming an adduct with a compound containing a tetrapyrrole group. TetrapyrRes PSI-MOD MOD:00700 tetrapyrrole modified residue A protein modification that effectively results from forming an adduct with a compound containing a tetrapyrrole group. PubMed:18688235 TetrapyrRes A protein modification that effectively results from forming an adduct with a compound containing a nucleotide or a polynucleotide through formation of either a phosphodiester bond, a phosphoramide ester bond, or a glycosidic bond. NucRes PSI-MOD MOD:00701 nucleotide or nucleic acid modified residue A protein modification that effectively results from forming an adduct with a compound containing a nucleotide or a polynucleotide through formation of either a phosphodiester bond, a phosphoramide ester bond, or a glycosidic bond. PubMed:18688235 NucRes A protein modification that effectively substitutes atoms of particular common isotopes with atoms or groups containing isotopes that are not the most common. IsoTagRes SILAC PSI-MOD MOD:00702 In SILAC (stable isotope labelling of amino acids in cell culture), the label may be introduced either through labeling of an incorporated residue or labeling of the substrates in a metabolic modification. For isotope labeling introduced through a modification reagent see MOD:01426. isotope labeled residue A protein modification that effectively substitutes atoms of particular common isotopes with atoms or groups containing isotopes that are not the most common. PubMed:18688235 IsoTagRes SILAC A protein modification that effectively replaces a hydrogen atom with a group derived from an isoprene polymer, such as a geranyl (C10), farnesyl (C15) or geranylgeranyl (C20) group. IpRes PSI-MOD MOD:00703 isoprenylated residue A protein modification that effectively replaces a hydrogen atom with a group derived from an isoprene polymer, such as a geranyl (C10), farnesyl (C15) or geranylgeranyl (C20) group. PubMed:18688235 IpRes A protein modification that effectively forms a double bond by removing a molecule of water from a residue. -18.02 C 0 H -2 N 0 O -1 -18.010565 X natural Unimod:23 PSI-MOD Dehydrated Dehydration MOD:00704 dehydrated residue A protein modification that effectively forms a double bond by removing a molecule of water from a residue. DeltaMass:0 Unimod:23 Dehydrated Dehydration A protein modification that effectively converts an L-valine residue to D-valine. 0.0 C 0 H 0 N 0 O 0 0.0 C 5 H 9 N 1 O 1 99.13 99.06841 V natural uniprot.ptm:PTM-0124 (R)-2-amino-3-methylbutanoic acid D-Val D-valine MOD_RES D-valine alpha-amino-beta-methylbutyric acid alpha-aminoisovaleric acid PSI-MOD MOD:00705 D-valine A protein modification that effectively converts an L-valine residue to D-valine. ChEBI:30016 PubMed:15853325 RESID:AA0200 (R)-2-amino-3-methylbutanoic acid D-Val D-valine MOD_RES D-valine alpha-amino-beta-methylbutyric acid alpha-aminoisovaleric acid A protein modification that effectively converts L-tyrosine to 2,3-didehydrotyrosine. -2.02 C 0 H -2 N 0 O 0 -2.01565 C 9 H 7 N 1 O 2 161.16 161.04768 Y natural Unimod:401 uniprot.ptm:PTM-0008 MOD_RES 2,3-didehydrotyrosine dHTyr PSI-MOD MOD:00706 dehydrogenated tyrosine A protein modification that effectively converts L-tyrosine to 2,3-didehydrotyrosine. Unimod:401#Y MOD_RES 2,3-didehydrotyrosine dHTyr a protein modification that effectively converts an L-tyrosine residue to a multihydroxylated L-phenylalanine Y natural HyTyr PSI-MOD MOD:00707 hydroxylated tyrosine a protein modification that effectively converts an L-tyrosine residue to a multihydroxylated L-phenylalanine PubMed:18688235 HyTyr A protein modification that effectively adds oxygen atoms to a sulfur atom of L-cysteine residue without removing hydrogen atoms. C artifact SOxyCys PSI-MOD MOD:00708 sulfur oxygenated L-cysteine A protein modification that effectively adds oxygen atoms to a sulfur atom of L-cysteine residue without removing hydrogen atoms. PubMed:18688235 SOxyCys A protein modification that effectively adds oxygen atoms to a sulfur atom of L-methionine residue without removing hydrogen atoms. M artifact SOxyMet PSI-MOD MOD:00709 sulfur oxygenated L-methionine A protein modification that effectively adds oxygen atoms to a sulfur atom of L-methionine residue without removing hydrogen atoms. PubMed:18688235 SOxyMet A protein modification that effectively adds a proton and replaces two hydrogen atoms with two methyl groups. Me2+Res PSI-MOD MOD:00710 For N-terminal proline residues, dimethylation can effectively only be accomplished with a protonated imino group. This process accounts for both protonation and dimethylation. The alternative Me2Res process accounts only for dimethylation and not protonation. protonated-dimethylated residue A protein modification that effectively adds a proton and replaces two hydrogen atoms with two methyl groups. PubMed:18688235 Me2+Res A protein modification that effectively replaces three hydrogen atoms with three methyl groups, after a proton has been added to form an aminium group. 43.09 C 3 H 7 N 0 O 0 S 0 43.054226 1+ X natural Me3+Res PSI-MOD MOD:00711 For amino acids residues, amine trimethylation can effectively only be accomplished with a protonated primary amino group. This process accounts for both protonation and trimethylation. The alternative Me3Res process accounts only for trimethylation and not protonation. trimethylated protonated-residue A protein modification that effectively replaces three hydrogen atoms with three methyl groups, after a proton has been added to form an aminium group. PubMed:18688235 Me3+Res A protein modification that effectively converts an L-proline residue to a methylated proline, such as N,N-dimethylproline. P natural MePro PSI-MOD MOD:00712 methylated proline A protein modification that effectively converts an L-proline residue to a methylated proline, such as N,N-dimethylproline. PubMed:18688235 MePro A protein modification that effectively converts an L-glutamic acid residue to a methylated glutamic acid, such as L-glutamate 5-methyl ester. X natural MeGlu PSI-MOD MOD:00713 methylated glutamic acid A protein modification that effectively converts an L-glutamic acid residue to a methylated glutamic acid, such as L-glutamate 5-methyl ester. PubMed:18688235 MeGlu A protein modification that effectively converts a glycine residue to a methylated glycine, such as N-methylglycine. G natural MeGly PSI-MOD MOD:00714 methylated glycine A protein modification that effectively converts a glycine residue to a methylated glycine, such as N-methylglycine. PubMed:18688235 MeGly A protein modification that effectively converts an L-isoleucine residue to a methylated isoleucine residue, such as N-methyl-L-isoleucine. I natural MeIle PSI-MOD MOD:00715 methylated isoleucine A protein modification that effectively converts an L-isoleucine residue to a methylated isoleucine residue, such as N-methyl-L-isoleucine. PubMed:18688235 MeIle A protein modification that effectively converts an L-methionine residue to a methylated methionine, such as N-methyl-L-methionine. M natural N-term MeMet PSI-MOD MOD:00716 methylated methionine A protein modification that effectively converts an L-methionine residue to a methylated methionine, such as N-methyl-L-methionine. PubMed:18688235 MeMet A protein modification that effectively converts an L-phenylalanine residue to a methylated phenylalanine, such as N-methyl-L-phenylalanine. F natural MePhe PSI-MOD MOD:00717 methylated phenylalanine A protein modification that effectively converts an L-phenylalanine residue to a methylated phenylalanine, such as N-methyl-L-phenylalanine. PubMed:18688235 MePhe A protein modification that effectively converts an L-tyrosine residue to a methylated tyrosine, such as N-methyl-L-tyrosine. Y natural N-term MeTyr PSI-MOD MOD:00718 methylated tyrosine A protein modification that effectively converts an L-tyrosine residue to a methylated tyrosine, such as N-methyl-L-tyrosine. PubMed:18688235 MeTyr A protein modification that oxygenates an L-methionine residue to one of the diastereomeric L-methionine sulfoxide residues. 16.0 C 0 H 0 N 0 O 1 S 0 15.994915 C 5 H 9 N 1 O 2 S 1 147.19 147.0354 M artifact Unimod:35 uniprot.ptm:PTM-0469 (2S)-2-amino-4-[(R)-methylsulfinyl]butanoic acid L-methionine (R)-S-oxide L-methionine (R)-sulfoxide L-methionine S-oxide L-methionine sulfoxide MOD_RES Methionine sulfoxide MetO Methionyl Sulfoxide oxym PSI-MOD Oxidation MOD:00719 From DeltaMass: Average Mass: 147 Formula:C5H9O1N2S Monoisotopic Mass Change:147.035 Average Mass Change:147.195 (formula incorrect, N and O reversed) References:PE Sciex. L-methionine sulfoxide A protein modification that oxygenates an L-methionine residue to one of the diastereomeric L-methionine sulfoxide residues. DeltaMass:177 OMSSA:1 PubMed:21406390 PubMed:22116028 RESID:AA0581 Unimod:35#M (2S)-2-amino-4-[(R)-methylsulfinyl]butanoic acid L-methionine (R)-S-oxide L-methionine (R)-sulfoxide L-methionine S-oxide L-methionine sulfoxide MOD_RES Methionine sulfoxide MetO Methionyl Sulfoxide oxym Oxidation A protein modification that effectively oxygenates an L-methionine residue to L-methionine sulfoxide R-diastereomer. 16.0 C 0 H 0 N 0 O 1 S 0 15.994915 C 5 H 9 N 1 O 2 S 1 147.19 147.0354 M natural uniprot.ptm:PTM-0480 (2S)-2-amino-4-[(R)-methylsulfinyl]butanoic acid L-methionine (R)-S-oxide L-methionine (R)-sulfoxide MOD_RES Methionine (R)-sulfoxide R-MetO PSI-MOD MOD:00720 L-methionine (R)-sulfoxide A protein modification that effectively oxygenates an L-methionine residue to L-methionine sulfoxide R-diastereomer. ChEBI:45764 PubMed:21406390 PubMed:22116028 PubMed:23911929 RESID:AA0581 (2S)-2-amino-4-[(R)-methylsulfinyl]butanoic acid L-methionine (R)-S-oxide L-methionine (R)-sulfoxide MOD_RES Methionine (R)-sulfoxide R-MetO A protein modification that effectively oxygenates an L-methionine residue to L-methionine sulfoxide S-diastereomer. 16.0 C 0 H 0 N 0 O 1 S 0 15.994915 C 5 H 9 N 1 O 2 S 1 147.19 147.0354 M artifact uniprot.ptm:PTM-0481 MOD_RES Methionine (S)-sulfoxide S-MetO PSI-MOD MOD:00721 L-methionine (S)-sulfoxide A protein modification that effectively oxygenates an L-methionine residue to L-methionine sulfoxide S-diastereomer. PubMed:18688235 MOD_RES Methionine (S)-sulfoxide S-MetO A protein modification that effectively replaces one hydrogen atom of an L-glutamine residue with one methyl group. 14.03 C 1 H 2 N 0 O 0 14.01565 C 6 H 10 N 2 O 2 142.16 142.07423 Q natural Unimod:34 Me1Gln methylq PSI-MOD MOD:00722 monomethylated L-glutamine A protein modification that effectively replaces one hydrogen atom of an L-glutamine residue with one methyl group. OMSSA:14 Unimod:34#Q Me1Gln methylq A protein modification that effectively converts an L-lysine residue to either N2-acetyl-L-lysine, or N6-acetyl-L-lysine. 42.04 C 2 H 2 N 0 O 1 42.010567 C 8 H 15 N 2 O 2 171.22 171.11336 K natural NAcLys PSI-MOD MOD:00723 N-acetylated L-lysine A protein modification that effectively converts an L-lysine residue to either N2-acetyl-L-lysine, or N6-acetyl-L-lysine. PubMed:18688235 NAcLys A protein modification that effectively replaces one hydrogen atom on a nitrogen of an L-histidine residue with one methyl group. 14.03 C 1 H 2 N 0 O 0 14.01565 C 7 H 9 N 3 O 1 151.17 151.07455 H natural Unimod:34 NMeHis methylh PSI-MOD Methyl MOD:00724 N-methylated L-histidine A protein modification that effectively replaces one hydrogen atom on a nitrogen of an L-histidine residue with one methyl group. OMSSA:74 Unimod:34#H NMeHis methylh Methyl A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a carbohydrate-like group linked through a glycosidic bond. PSI-MOD MOD:00725 complex glycosylation A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a carbohydrate-like group linked through a glycosidic bond. PubMed:18688235 A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a glucose group through a glycosidic bond. MOD:00433 X natural Glc PSI-MOD MOD:00726 glucosylated residue A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a glucose group through a glycosidic bond. PubMed:18688235 Glc A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a mannose group through a glycosidic bond, X natural Man PSI-MOD MOD:00727 mannosylated residue A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a mannose group through a glycosidic bond, PubMed:18688235 Man A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a galactose group through a glycosidic bond. X natural Gal PSI-MOD MOD:00728 galactosylated residue A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a galactose group through a glycosidic bond. PubMed:18688235 Gal a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a pentose sugar group through a glycosidic bond 132.12 C 5 H 8 O 4 132.04225 X natural Pent Pentoses (Ara, Rib, Xyl) Pentosyl PSI-MOD MOD:00729 for Pentoses DeltaMass gives mass 132, for Pentosyl DeltaMass gives formula C 6 H 10 N4 with mass 146 pentosylated residue a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a pentose sugar group through a glycosidic bond DeltaMass:172 Pent Pentoses (Ara, Rib, Xyl) Pentosyl a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a arabinose sugar group through a glycosidic bond 132.12 C 5 H 8 O 4 132.04225 X natural Ara PSI-MOD MOD:00730 arabinosylated residue a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a arabinose sugar group through a glycosidic bond PubMed:18688235 Ara a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a ribose sugar group through a glycosidic bond 132.12 C 5 H 8 O 4 132.04225 X natural Rib PSI-MOD MOD:00731 ribosylated residue a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a ribose sugar group through a glycosidic bond PubMed:18688235 Rib a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a xylose sugar group through a glycosidic bond 132.12 C 5 H 8 O 4 132.04225 X natural Xyl PSI-MOD MOD:00732 xylosylated residue a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a xylose sugar group through a glycosidic bond PubMed:18688235 Xyl A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with an N-acetylglucosamine group through a glycosidic bond. 203.19 C 8 H 13 N 1 O 5 203.07938 X GlcNAc PSI-MOD MOD:00733 N-acetylaminoglucosylated residue A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with an N-acetylglucosamine group through a glycosidic bond. PubMed:18688235 GlcNAc A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with an N-acetylgalactosamine group through a glycosidic bond. 203.19 C 8 H 13 N 1 O 5 203.07938 X GalNAc N-acetylhexosamines (GalNAc, GlcNAc) PSI-MOD MOD:00734 From DeltaMass: Average Mass: 203 Formula:C8H13O5N1 Monoisotopic Mass Change:203.079 Average Mass Change:203.196 References:PE Sciex N-acetylaminogalactosylated residue A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with an N-acetylgalactosamine group through a glycosidic bond. DeltaMass:247 GalNAc N-acetylhexosamines (GalNAc, GlcNAc) A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a hexosuronic acid group through a glycosidic bond. 176.12 C 6 H 8 O 6 176.03209 X natural HexA PSI-MOD MOD:00735 hexosuronylated residue A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a hexosuronic acid group through a glycosidic bond. PubMed:18688235 HexA a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a deoxyhexose group through a glycosidic bond 146.14 C 6 H 10 O 4 146.0579 X natural GNO:G02438LG Deoxyhexoses (Fuc, Rha) dHex PSI-MOD MOD:00736 From DeltaMass: Average Mass: 146 deoxyhexosylated residue a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a deoxyhexose group through a glycosidic bond DeltaMass:0 Deoxyhexoses (Fuc, Rha) dHex A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with an N-acetylneuraminic acid (sialic acid) group through a glycosidic bond. 291.26 C 11 H 17 N 1 O 8 291.09543 X natural GNO:G76685HR N-acetylneuraminic acid (Sialic acid, NeuAc, NANA, SA) NeuNAc PSI-MOD MOD:00737 From DeltaMass: Average Mass: 291 N-acetylneuraminylated residue A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with an N-acetylneuraminic acid (sialic acid) group through a glycosidic bond. DeltaMass:0 N-acetylneuraminic acid (Sialic acid, NeuAc, NANA, SA) NeuNAc A protein modification that effectively substitutes an iron atom or a cluster containing iron for hydrogen atoms, or that coordinates an iron ion. FeRes PSI-MOD MOD:00738 iron containing modified residue A protein modification that effectively substitutes an iron atom or a cluster containing iron for hydrogen atoms, or that coordinates an iron ion. PubMed:18688235 FeRes A protein modification that effectively substitutes a cluster of iron and sulfur atoms for hydrogen atoms. FeSRes PSI-MOD MOD:00739 iron-sulfur cluster containing modification A protein modification that effectively substitutes a cluster of iron and sulfur atoms for hydrogen atoms. PubMed:18688235 FeSRes A protein modification that effectively substitutes a manganese atom or a cluster containing manganese for hydrogen atoms, or that coordinates a manganese ion. MnRes PSI-MOD MOD:00740 manganese containing modified residue A protein modification that effectively substitutes a manganese atom or a cluster containing manganese for hydrogen atoms, or that coordinates a manganese ion. PubMed:18688235 MnRes A protein modification that effectively substitutes a nickel atom or a cluster containing nickel for hydrogen atoms, or that coordinates a nickel ion. NiRes PSI-MOD MOD:00741 nickel containing modified residue A protein modification that effectively substitutes a nickel atom or a cluster containing nickel for hydrogen atoms, or that coordinates a nickel ion. PubMed:18688235 NiRes A protein modification that effectively substitutes a copper atom or a cluster containing copper for hydrogen atoms, or that coordinates a copper ion. CuRes PSI-MOD MOD:00742 copper containing modified residue A protein modification that effectively substitutes a copper atom or a cluster containing copper for hydrogen atoms, or that coordinates a copper ion. PubMed:18688235 CuRes A protein modification that effectively substitutes a molybdenum atom or a cluster containing molybdenum for hydrogen atoms, or that coordinates a molybdenum ion. MoRes PSI-MOD MOD:00743 molybdenum containing modified residue A protein modification that effectively substitutes a molybdenum atom or a cluster containing molybdenum for hydrogen atoms, or that coordinates a molybdenum ion. PubMed:18688235 MoRes A protein modification containing a molybdenum atom in a pterin ring system. MoPterRes PSI-MOD MOD:00744 molybdenum pterin containing modification A protein modification containing a molybdenum atom in a pterin ring system. PubMed:18688235 MoPterRes A protein modification that effectively substitutes a selenium atom or a cluster containing selenium for hydrogen atoms. SeRes PSI-MOD MOD:00745 selenium containing residue A protein modification that effectively substitutes a selenium atom or a cluster containing selenium for hydrogen atoms. PubMed:18688235 SeRes A protein modification that effectively substitutes a tungsten atom or a cluster containing tungsten for hydrogen atoms, or that coordinates a tungsten ion. WRes PSI-MOD MOD:00746 tungsten containing modified residue A protein modification that effectively substitutes a tungsten atom or a cluster containing tungsten for hydrogen atoms, or that coordinates a tungsten ion. PubMed:18688235 WRes A protein modification that effectively substitutes a sodium atom for a hydrogen atom. NaRes PSI-MOD MOD:00747 sodium containing modified residue A protein modification that effectively substitutes a sodium atom for a hydrogen atom. PubMed:18688235 NaRes A protein modification that effectively results from forming an adduct with a compound containing a pterin group. PterRes PSI-MOD MOD:00748 pterin modified residue A protein modification that effectively results from forming an adduct with a compound containing a pterin group. PubMed:18688235 PterRes A protein modification that effectively substitutes a sulfur atom for an oxygen atom. S(O)Res PSI-MOD MOD:00749 sulfur substitution for oxygen A protein modification that effectively substitutes a sulfur atom for an oxygen atom. PubMed:18688235 S(O)Res A protein modification that effectively crosslinks an amino acid residue and the 3'- or 5'-end of DNA through a phosphodiester bond. DNARes PSI-MOD MOD:00750 deoxyribonucleic acid linked residue A protein modification that effectively crosslinks an amino acid residue and the 3'- or 5'-end of DNA through a phosphodiester bond. PubMed:18688235 DNARes a protein modification RNARes PSI-MOD MOD:00751 ribonucleic acid linked residue a protein modification PubMed:18688235 RNARes A protein modification that effectively results from forming an adduct with one ADP-ribose through formation of a glycosidic bond. 541.3 C 15 H 21 N 5 O 13 P 2 541.0611 X natural ADP-rybosylation (from NAD) ADPRib1Res PSI-MOD MOD:00752 From DeltaMass: Average Mass: 541. monoadenosine diphosphoribosyl (ADP-ribosyl) modified residue A protein modification that effectively results from forming an adduct with one ADP-ribose through formation of a glycosidic bond. DeltaMass:0 ADP-rybosylation (from NAD) ADPRib1Res A protein modification that effectively substitutes a chlorine atom for a hydrogen atom. X ClRes PSI-MOD MOD:00753 chlorinated residue A protein modification that effectively substitutes a chlorine atom for a hydrogen atom. PubMed:18688235 ClRes A protein modification that effectively substitutes a bromine atom for a hydrogen atom. X BrRes PSI-MOD MOD:00754 brominated residue A protein modification that effectively substitutes a bromine atom for a hydrogen atom. PubMed:18688235 BrRes A protein modification that effectively substitutes an iodine atom of a residue for a hydrogen atom. X IRes PSI-MOD MOD:00755 iodinated residue A protein modification that effectively substitutes an iodine atom of a residue for a hydrogen atom. PubMed:18688235 IRes A protein modification that effectively converts an L-valine residue to 4-hydroxy-D-valine. 16.0 C 0 H 0 N 0 O 1 15.994915 C 5 H 9 N 1 O 2 115.13 115.06333 V natural uniprot.ptm:PTM-0111 (2R,3Xi)-2-amino-4-hydroxy-3-methylbutanoic acid 4-hydroxy-D-valine D-4HyVal D-gamma-hydroxyvaline MOD_RES D-4-hydroxyvaline PSI-MOD MOD:00756 4-hydroxy-D-valine A protein modification that effectively converts an L-valine residue to 4-hydroxy-D-valine. PubMed:15853325 RESID:AA0388 (2R,3Xi)-2-amino-4-hydroxy-3-methylbutanoic acid 4-hydroxy-D-valine D-4HyVal D-gamma-hydroxyvaline MOD_RES D-4-hydroxyvaline A protein modification that effectively converts an L-proline residue to O4-galactosyl-L-hydroxyproline. 178.14 C 6 H 10 N 0 O 6 178.04774 C 11 H 17 N 1 O 7 275.26 275.1005 P natural uniprot.ptm:PTM-0558 (2S,4R)-4-(beta-D-galactopyranosyloxy)pyrrolidine-2-carboxylic acid 4-(beta-D-galactopyranosyloxy)proline 4-(galactosyloxy)proline CARBOHYD O-linked (Gal) hydroxyproline O4-galactosyl-L-hydroxyproline O4-glycosyl-hydroxyproline beta-galactopyranosyl-4-hydroxyproline PSI-MOD MOD:00757 secondary to RESID:AA0030 O4-galactosyl-L-hydroxyproline A protein modification that effectively converts an L-proline residue to O4-galactosyl-L-hydroxyproline. RESID:AA0389 (2S,4R)-4-(beta-D-galactopyranosyloxy)pyrrolidine-2-carboxylic acid 4-(beta-D-galactopyranosyloxy)proline 4-(galactosyloxy)proline CARBOHYD O-linked (Gal) hydroxyproline O4-galactosyl-L-hydroxyproline O4-glycosyl-hydroxyproline beta-galactopyranosyl-4-hydroxyproline A protein modification that effectively converts an L-proline residue to O4-(N-acetylamino)glucosyl-L-hydroxyproline. 219.19 C 8 H 13 N 1 O 6 219.07428 C 13 H 20 N 2 O 7 316.31 316.12704 P natural uniprot.ptm:PTM-0578 (2S,4R)-4-[2-acetamido-2-deoxy-alpha-D-glucopyranosyloxy]pyrrolidine-2-carboxylic acid 4-(N-acetylglucosaminyloxy)proline 4-[(2-N-acetylamino)-alpha-D-glucopyranosyl]oxyproline CARBOHYD O-linked (GlcNAc) hydroxyproline O4-(N-acetylamino)glucosyl-L-hydroxyproline O4-glycosyl-hydroxyproline O4GlcNAcHyPro alpha-2-(N-acetylamino)glucopyranosyl-4-hydroxyproline PSI-MOD HexNAc MOD:00758 secondary to RESID:AA0030 O4-(N-acetylamino)glucosyl-L-hydroxyproline A protein modification that effectively converts an L-proline residue to O4-(N-acetylamino)glucosyl-L-hydroxyproline. PubMed:15238247 PubMed:9660787 RESID:AA0390 (2S,4R)-4-[2-acetamido-2-deoxy-alpha-D-glucopyranosyloxy]pyrrolidine-2-carboxylic acid 4-(N-acetylglucosaminyloxy)proline 4-[(2-N-acetylamino)-alpha-D-glucopyranosyl]oxyproline CARBOHYD O-linked (GlcNAc) hydroxyproline O4-(N-acetylamino)glucosyl-L-hydroxyproline O4-glycosyl-hydroxyproline O4GlcNAcHyPro alpha-2-(N-acetylamino)glucopyranosyl-4-hydroxyproline HexNAc modification from Unimod N-linked glycosylation 1607.48 C 62 H 102 N 4 O 44 1606.5867 C 66 H 108 N 6 O 46 1721.59 1720.6296 N natural GNO:G59937CP Unimod:307 PSI-MOD Fucosylated biantennary (-1 galactose) dHex(1)Hex(4)HexNAc(4) MOD:00759 fucosylated biantennary (-1 galactose) N4-glycosylated asparagine modification from Unimod N-linked glycosylation Unimod:307 Fucosylated biantennary (-1 galactose) dHex(1)Hex(4)HexNAc(4) modification from Unimod N-linked glycosylation - missing ref 1623.48 C 62 H 102 N 4 O 45 1622.5817 C 66 H 108 N 6 O 47 1737.59 1736.6245 N natural GNO:G10486CT Unimod:311 PSI-MOD Biantennary Hex(5)HexNAc(4) MOD:00760 biantennary N4-glycosylated asparagine modification from Unimod N-linked glycosylation - missing ref Unimod:311 Biantennary Hex(5)HexNAc(4) A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with one hexose sugar group through a glycosidic bond. 162.14 C 6 H 10 O 5 162.05283 X natural GNO:G81399MY Hex1 PSI-MOD MOD:00761 monohexosylated residue A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with one hexose sugar group through a glycosidic bond. PubMed:18688235 Hex1 modification from Unimod N-linked glycosylation - missing ref 1299.2 C 50 H 82 N 4 O 35 1298.476 C 54 H 88 N 6 O 37 1413.3 1412.5189 N natural GNO:G35029YA Unimod:309 PSI-MOD Biantennary (-2 galactose) Hex(3)HexNAc(4) MOD:00762 biantennary (-2 galactose) N4-glycosylated asparagine modification from Unimod N-linked glycosylation - missing ref Unimod:309 Biantennary (-2 galactose) Hex(3)HexNAc(4) modification from Unimod N-linked glycosylation - missing ref 1461.34 C 56 H 92 N 4 O 40 1460.5288 C 60 H 98 N 6 O 42 1575.44 1574.5717 N natural GNO:G72787SB Unimod:310 PSI-MOD Biantennary (-1 galactose) Hex(4)HexNAc(4) MOD:00763 biantennary (-1 galactose) N4-glycosylated asparagine modification from Unimod N-linked glycosylation - missing ref Unimod:310 Biantennary (-1 galactose) Hex(4)HexNAc(4) A protein modification that effectively results from forming an adduct with a carbohydrate-like group either through enzymatic formation of a glycosidic bond, or through non-enzymatic glycation formation of a Schiff-base or an Amadori ketosamine residue adduct. PSI-MOD MOD:00764 glycoconjugated residue A protein modification that effectively results from forming an adduct with a carbohydrate-like group either through enzymatic formation of a glycosidic bond, or through non-enzymatic glycation formation of a Schiff-base or an Amadori ketosamine residue adduct. PubMed:18688235 PubMed:3743566 A protein modification that effectively converts an L-cysteine residue to S-(L-cysteinyl)-L-cysteine, forming a disulfide bond with free cysteine. 119.14 C 3 H 5 N 1 O 2 S 1 119.0041 C 6 H 10 N 2 O 3 S 2 222.28 222.01329 C natural Unimod:312 uniprot.ptm:PTM-0415 (2R,2'R)-3,3'-disulfane-1,2-diylbis(2-aminopropanoic acid) 3,3'-disulfane-1,2-diylbis(2-azanylpropanoic acid) 3,3'-dithiobis(2-aminopropanoic acid) 3,3'-dithiobisalanine 3,3'-dithiodialanine Cysteinylation L-cystine MOD_RES S-cysteinyl cysteine S-cystenyl cystenyl SCysCys beta,beta'-diamino-beta,beta'-dicarboxydiethyldisulfide beta,beta'-dithiodialanine bis(alpha-aminopropionic acid)-beta-disulfide bis(beta-amino-beta-carboxyethyl)disulfide dicysteine PSI-MOD 2-amino-3-(2-amino-2-carboxy-ethyl)disulfanyl-propanoic acid MOD:00765 This entry is for formation of a disulfide bond between a peptide cysteine and a free cysteine. For the cystine cross-link, see MOD:00234. From DeltaMass: (name misspelled and formula incorrect, N and O reversed) Formula: C6H10O2N3S2 Monoisotopic Mass Change: 222.013 Average Mass Change: 222.283 cysteinylation (disulfide with free L-cysteine) A protein modification that effectively converts an L-cysteine residue to S-(L-cysteinyl)-L-cysteine, forming a disulfide bond with free cysteine. DeltaMass:260 PubMed:1988019 PubMed:2001356 PubMed:2076469 PubMed:3083866 PubMed:366603 PubMed:7918467 PubMed:8344916 RESID:AA0025#CYS1 Unimod:312 (2R,2'R)-3,3'-disulfane-1,2-diylbis(2-aminopropanoic acid) 3,3'-disulfane-1,2-diylbis(2-azanylpropanoic acid) 3,3'-dithiobis(2-aminopropanoic acid) 3,3'-dithiobisalanine 3,3'-dithiodialanine Cysteinylation L-cystine MOD_RES S-cysteinyl cysteine S-cystenyl cystenyl SCysCys beta,beta'-diamino-beta,beta'-dicarboxydiethyldisulfide beta,beta'-dithiodialanine bis(alpha-aminopropionic acid)-beta-disulfide bis(beta-amino-beta-carboxyethyl)disulfide dicysteine 2-amino-3-(2-amino-2-carboxy-ethyl)disulfanyl-propanoic acid modification from Unimod Post-translational - C-terminal loss of lysine OBSOLETE because the idenical to MOD:01642. Remap to MOD:01642 MOD:01642 -128.18 C -6 H -12 N -2 O -1 -128.09496 X C-term Unimod:313 PSI-MOD Loss of C-terminal K from Heavy Chain of MAb Lys-loss MOD:00766 C terminal -K from HC of MAb true modification from Unimod Post-translational - C-terminal loss of lysine OBSOLETE because the idenical to MOD:01642. Remap to MOD:01642 PubMed:16078144 Unimod:313 Loss of C-terminal K from Heavy Chain of MAb Lys-loss A modification produced in a non-enzymatic reaction between a carbohydrate carbonyl group (C1 of aldohexose or C2 of fructose) and a protein amino group to form a Schiff-base or an Amadori ketosamine residue adduct. artifact PSI-MOD MOD:00767 glycated residue A modification produced in a non-enzymatic reaction between a carbohydrate carbonyl group (C1 of aldohexose or C2 of fructose) and a protein amino group to form a Schiff-base or an Amadori ketosamine residue adduct. PubMed:18688235 Oxidation of methionine to methionine sulfone with neutral loss of CH3SO2H. -80.1 C -1 H -4 N 0 O -2 S -1 -79.9932 C 4 H 5 N 1 O 1 S 0 83.09 83.03712 M artifact PSI-MOD MOD:00768 Originally created from Unimod:508 that was later deleted. methionine oxidation with neutral loss of 80 Da Oxidation of methionine to methionine sulfone with neutral loss of CH3SO2H. PubMed:18688235 PubMed:9004526 Natural or modified residues with a mass of 71.0-71.1 Da. PSI-MOD MOD:00769 residues isobaric at 71.0-71.1 Da Natural or modified residues with a mass of 71.0-71.1 Da. PubMed:18688235 Natural or modified residues that are isobaric at a resolution below 0.01 Da. PSI-MOD MOD:00770 residues isobaric at a resolution below 0.01 Da Natural or modified residues that are isobaric at a resolution below 0.01 Da. PubMed:18688235 Natural or modified residues with a mass of 166.98-167.00 Da. PSI-MOD MOD:00771 residues isobaric at 166.98-167.00 Da Natural or modified residues with a mass of 166.98-167.00 Da. PubMed:18688235 A protein modification that effectively substitutes a vanadium atom or a cluster containing vanadium for hydrogen atoms, or that coordinates a vanadium ion. VRes PSI-MOD MOD:00772 vanadium containing modified residue A protein modification that effectively substitutes a vanadium atom or a cluster containing vanadium for hydrogen atoms, or that coordinates a vanadium ion. PubMed:18688235 VRes Natural or modified residues with a mass of 181.00-181.02 Da. PSI-MOD MOD:00773 residues isobaric at 181.00-181.02 Da Natural or modified residues with a mass of 181.00-181.02 Da. PubMed:18688235 Natural or modified residues with a mass of 243.02-243.03 Da. PSI-MOD MOD:00774 residues isobaric at 243.02-243.03 Da Natural or modified residues with a mass of 243.02-243.03 Da. PubMed:18688235 An artifactual protein modification that converts an L-histidine residue to L-asparagine by oxidative degradation. -23.04 C -2 H -1 N -1 O 1 -23.015984 C 4 H 6 N 2 O 2 114.1 114.04293 H artifact Unimod:348 his2asnh PSI-MOD His->Asn histidine oxidation to aspargine MOD:00775 L-asparagine (His) An artifactual protein modification that converts an L-histidine residue to L-asparagine by oxidative degradation. OMSSA:54 PubMed:9252331 Unimod:348 his2asnh His->Asn histidine oxidation to aspargine An artifactual protein modification that converts an L-histidine residue to L-aspartic acid by oxidative degradation. -22.05 C -2 H -2 N -2 O 2 -22.03197 C 4 H 5 N 1 O 3 115.09 115.02694 H artifact Unimod:349 his2asph PSI-MOD His->Asp histidine oxidation to aspartic acid MOD:00776 From OMSSA: desc="oxidation of H to D" monomass= -23.015984 (this is the same mass difference as OMSSA:54, his2asnh) [JSG]. L-aspartic acid (His) An artifactual protein modification that converts an L-histidine residue to L-aspartic acid by oxidative degradation. OMSSA:55 PubMed:9252331 Unimod:349 his2asph His->Asp histidine oxidation to aspartic acid Natural or modified residues with a mass of 182.96-182.98 Da. PSI-MOD MOD:00777 residues isobaric at 182.96-182.98 Da Natural or modified residues with a mass of 182.96-182.98 Da. PubMed:18688235 Natural or modified residues with a mass of 182.9-183.0 Da. PSI-MOD MOD:00778 residues isobaric at 182.9-183.0 Da Natural or modified residues with a mass of 182.9-183.0 Da. PubMed:18688235 OBSOLETE because redundant with MOD:00130. Remap to MOD:00130. MOD:00130 -1.03 H -3 N -1 O 1 -1.031634 K natural Unimod:352 Oxidation of lysine (to aminoadipic semialdehyde) PSI-MOD MOD:00779 From DeltaMass: Average Mass: -1 Average Mass Change:-1 References:Amici A, Levine, RL, Tsai, L, and Stadtman, ER: Conversion of amino acid residues in proteins and amino acid homopolymers to carbonyl derivatives by metal-catalyzed oxidation reactions. Journal of Biological Chemistry 264: 3341-3346 1989.Requena JR, Chao CC, Levine RL, and Stadtman ER: Glutamic and aminoadipic semialdehydes are the main carbonyl products of metal-catalyzed oxidation of proteins. Proceedings of the National Academy of Sciences USA 98: 69-74 2001. lysine oxidation to aminoadipic semialdehyde true OBSOLETE because redundant with MOD:00130. Remap to MOD:00130. DeltaMass:352 PubMed:11332453 PubMed:358196 PubMed:5337886 PubMed:5529814 Unimod:352 Oxidation of lysine (to aminoadipic semialdehyde) A protein modification that effectively converts an L-asparagine residue to N-acetyl-L-asparagine. 42.04 C 2 H 2 N 0 O 1 42.010567 C 6 H 8 N 2 O 3 156.14 156.0535 N artifact N-term AcAsn PSI-MOD MOD:00780 This modification has not been observed to occur naturally. N-acetyl-L-asparagine A protein modification that effectively converts an L-asparagine residue to N-acetyl-L-asparagine. PubMed:18688235 AcAsn A protein modification that effectively converts an L-histidine residue to N2-acetyl-L-histidine. 42.04 C 2 H 2 N 0 O 1 42.010567 C 8 H 9 N 3 O 2 179.18 179.06947 H artifact N-term AcHis PSI-MOD MOD:00781 This modification has not been observed to occur naturally. N2-acetyl-L-histidine A protein modification that effectively converts an L-histidine residue to N2-acetyl-L-histidine. PubMed:18688235 AcHis A protein modification that effectively converts an L-leucine residue to N-acetyl-L-leucine. 42.04 C 2 H 2 N 0 O 1 42.010567 C 8 H 14 N 1 O 2 156.2 156.10245 L artifact N-term AcLeu PSI-MOD MOD:00782 This modification has not been observed to occur naturally. N-acetyl-L-leucine A protein modification that effectively converts an L-leucine residue to N-acetyl-L-leucine. PubMed:18688235 AcLeu A protein modification that effectively replaces two hydrogen atoms of an L-arginine residue with two methyl groups. 28.05 C 2 H 4 N 0 O 0 28.0313 C 8 H 16 N 4 O 1 184.24 184.13242 R natural Unimod:36 uniprot.ptm:PTM-0341 NNMe2Arg dimethylr PSI-MOD Dimethyl MOD:00783 dimethylated L-arginine A protein modification that effectively replaces two hydrogen atoms of an L-arginine residue with two methyl groups. OMSSA:37 Unimod:36#R NNMe2Arg dimethylr Dimethyl A protein modification that effectively converts an L-phenylalanine residue to N-acetyl-L-phenylalanine. 42.04 C 2 H 2 N 0 O 1 42.010567 C 11 H 11 N 1 O 2 189.21 189.07898 F artifact N-term AcPhe PSI-MOD MOD:00784 This modification has not been observed to occur naturally. N-acetyl-L-phenylalanine A protein modification that effectively converts an L-phenylalanine residue to N-acetyl-L-phenylalanine. PubMed:18688235 AcPhe A protein modification that effectively converts an L-tryptophan residue to N2-acetyl-L-tryptophan. 42.04 C 2 H 2 N 0 O 1 42.010567 C 13 H 12 N 2 O 2 228.25 228.08987 W artifact N-term AcTrp PSI-MOD MOD:00785 This modification has not been observed to occur naturally. N2-acetyl-L-tryptophan A protein modification that effectively converts an L-tryptophan residue to N2-acetyl-L-tryptophan. PubMed:18688235 AcTrp A protein modification that effectively substitutes one or more (2)H deuterium atoms for (1)H protium atoms. D(H)Res PSI-MOD MOD:00786 deuterium substituted residue A protein modification that effectively substitutes one or more (2)H deuterium atoms for (1)H protium atoms. PubMed:18688235 D(H)Res modification from Unimod - label for the active site serine of the serine esterase/protease family also shown to label tyrosine in serum albumin 164.14 C 6 H 13 O 3 P 1 164.06023 C 9 H 18 N 1 O 5 P 1 251.22 251.09225 S artifact Unimod:362 PSI-MOD Diisopropylphosphate O-Diisopropylphosphorylation MOD:00787 diisopropylphosphoserine modification from Unimod - label for the active site serine of the serine esterase/protease family also shown to label tyrosine in serum albumin Unimod:362 Diisopropylphosphate O-Diisopropylphosphorylation modification from Unimod 122.06 C 3 H 7 O 3 P 1 122.01328 C 12 H 16 N 1 O 5 P 1 285.24 285.0766 Y artifact Unimod:363 PSI-MOD Isopropylphospho O-Isopropylphosphorylation MOD:00788 isopropylphosphotyrosine modification from Unimod Unimod:363 Isopropylphospho O-Isopropylphosphorylation modification from Unimod - isotopic label ICPL method - The paper describes an H/D labeling strategy whereas the commercial product follows a C/13C labeling strategy. The digest is typically applied AFTER ICPL_light/heavy labeling, only Protein N-term labeling and Lys-specific labeling is applied. 111.04 (13)C 6 H 3 N 1 O 1 111.041595 X artifact Unimod:364 PSI-MOD Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, heavy form ICPL:13C(6) MOD:00789 Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, heavy form modification from Unimod - isotopic label ICPL method - The paper describes an H/D labeling strategy whereas the commercial product follows a C/13C labeling strategy. The digest is typically applied AFTER ICPL_light/heavy labeling, only Protein N-term labeling and Lys-specific labeling is applied. PubMed:15602776 URL:http://www.serva.de/products/sheets/39230-E.pdf Unimod:364 Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, heavy form ICPL:13C(6) modification from Unimod - isotopic label ICPL method - The paper describes an H/D labeling strategy whereas the commercial product follows a C/13C labeling strategy. The digest is typically applied AFTER ICPL_light/heavy labeling, only Protein N-term labeling and Lys-specific labeling is applied. 105.02 (12)C 6 H 3 N 1 O 1 105.02146 X artifact Unimod:365 PSI-MOD Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, light form ICPL MOD:00790 Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, light form modification from Unimod - isotopic label ICPL method - The paper describes an H/D labeling strategy whereas the commercial product follows a C/13C labeling strategy. The digest is typically applied AFTER ICPL_light/heavy labeling, only Protein N-term labeling and Lys-specific labeling is applied. PubMed:15602776 URL:http://www.serva.de/products/sheets/39230-E.pdf Unimod:365 Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, light form ICPL A protein modification that effectively converts an L-glutamine residue to L-glutamic acid with one (18)O. 2.99 H -1 N -1 (18)O 1 2.988262 C 5 H 7 N 1 (16)O 2 (18)O 1 131.05 131.04684 Q artifact Unimod:366 PSI-MOD Deamidated:18O(1) Deamidation in presence of O18 MOD:00791 1x(18)O labeled deamidated L-glutamine A protein modification that effectively converts an L-glutamine residue to L-glutamic acid with one (18)O. PubMed:8382902 Unimod:366#Q Deamidated:18O(1) Deamidation in presence of O18 A protein modification that effectively substitutes one (2)H deuterium atom for one (1)H protium atom. D(H)1Res PSI-MOD MOD:00792 deuterium monosubstituted residue A protein modification that effectively substitutes one (2)H deuterium atom for one (1)H protium atom. PubMed:18688235 D(H)1Res A protein modification that effectively converts an L-cysteine residue to dehydroalanine. -34.08 C 0 H -2 N 0 O 0 S -1 -33.98772 C 3 H 3 N 1 O 1 69.06 69.02146 C natural Unimod:368 uniprot.ptm:PTM-0468 2,3-didehydroalanine 2-aminoacrylic acid 2-aminopropenoic acid 4-methylidene-imidazole-5-one (MIO) active site Dehydroalanine (from Cysteine) Dha MOD_RES 2,3-didehydroalanine (Cys) anhydroserine dHAla(Cys) dehydroalanine PSI-MOD Cys->Dha Dehydroalanine (from Cysteine) MOD:00793 From DeltaMass: In an attempt to clarfiy the difference between the modification of cysteine to lanthionine and cysteine to dehydroalanine, the following contributions from the ABRF email forum are presented:Structurally speaking lanthionine is like cystine but lacks one S atom. I imagine one can think of it as a condensation of cysteine and dehydroalanine but I do not know how it is made biologically. Dehydroalanine could be derived from either serine or cysteine. If I recall Biochem 101 correctly lanthionine was first found in wool.-Lowell Ericsson (ERICSSONLH@U.WASHINGTON.EDU)As far as I know, the structure of lanthionine is two Ala's joined by a single sulphur with the loss of two hydrogens from the methyl group of the Ala.Stephen Bayne (sbay@novo.dk)Regarding the structure of lanthionine and dehydroalanine: dehydroalanine is formed by the loss of one sulfur atom and two hydrogen atoms from ONE cysteine residue. lanthionine is formed from TWO cysteines, is a thioether, and contains one sulfur atom less than the amino acid cystine. Dan McCormick (MCCORMICK@rcf.mayo.edu) [DeltaMass]. Most bacterially produced lanthionine crosslinks are made by dehydration of L-serine to dehydroalanine, and then reaction with L-cysteine so as to produce chiral inversion at the alpha-carbon of the original L-serine; the lanthionine is a meso-diastereomer with L-configuration of the original cysteine alpha-carbon and D-configuration of the original L-serine alpha-carbon. In cypemycin dehydroalanine has been shown to be produced by loss of hydrogen sulfide from cysteine. Beta-elimination of hydrogen sulfide does occur during treatment with performic acid [JSG]. dehydroalanine (Cys) A protein modification that effectively converts an L-cysteine residue to dehydroalanine. ChEBI:17123 DeltaMass:8 PubMed:10220322 PubMed:11212008 PubMed:1547888 PubMed:15799070 PubMed:1815586 PubMed:20805503 PubMed:2914619 PubMed:7947813 PubMed:8239649 RESID:AA0181#CYS Unimod:368 2,3-didehydroalanine 2-aminoacrylic acid 2-aminopropenoic acid 4-methylidene-imidazole-5-one (MIO) active site Dehydroalanine (from Cysteine) Dha MOD_RES 2,3-didehydroalanine (Cys) anhydroserine dHAla(Cys) dehydroalanine Cys->Dha Dehydroalanine (from Cysteine) OBSOLETE because redundant and identical to MOD:00477. Remap to MOD:00477. MOD:00477 -28.01 C -1 O -1 -27.994915 C 4 H 7 N 1 O 0 69.11 69.057846 P artifact Unimod:369 PSI-MOD Pro->Pyrrolidone Pyrrolidone from Proline MOD:00794 This Unimod entry appears to have come from the same description in PubMed:9252331 as Unimod:360. This entry was not annotated as being approved. Neither difference formula corresponds to the result described in the original citation PubMed:2161657. pyrrolidone from proline true OBSOLETE because redundant and identical to MOD:00477. Remap to MOD:00477. PubMed:9252331 Unimod:369 Pro->Pyrrolidone Pyrrolidone from Proline modification from Unimod 86.09 C 4 H 6 O 2 86.03678 C 7 H 11 N 1 O 3 S 1 189.23 189.04596 C artifact Unimod:371 PSI-MOD HMVK Michael addition of hydroxymethylvinyl ketone to cysteine MOD:00795 Michael addition of hydroxymethylvinyl ketone to cysteine modification from Unimod PubMed:11743741 Unimod:371 HMVK Michael addition of hydroxymethylvinyl ketone to cysteine A protein modification that effectively converts an L-arginine residue to L-ornithine. -42.04 C -1 H -2 N -2 -42.021797 C 5 H 10 N 2 O 1 114.15 114.079315 R artifact Unimod:372 Ornithine (from Arginine) Ornithyl arg2orn PSI-MOD Arg->Orn Ornithine from Arginine MOD:00796 L-ornithine (Arg) A protein modification that effectively converts an L-arginine residue to L-ornithine. DeltaMass:129 OMSSA:163 PubMed:15489230 Unimod:372 Ornithine (from Arginine) Ornithyl arg2orn Arg->Orn Ornithine from Arginine a protein modification that effectively converts an L-cysteine residue to the PEP adduct, 2-(S-L-cysteinyl)pyruvic acid O-phosphothioketal 168.04 C 3 H 5 N 0 O 6 P 1 S 0 167.98238 C 6 H 10 N 1 O 7 P 1 S 1 271.18 270.99155 C natural uniprot.ptm:PTM-0424 (2R)-2-amino-3-[1-carboxy-1-(phosphonooxy)ethyl]sulfanylpropanoic acid 2-(S-L-cysteinyl)pyruvic acid O-phosphothioketal 2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-2-(phosphonooxy)propanoic acid 2-([(2R)-2-azanyl-2-carboxyethyl]sulfanyl)-2-(phosphonooxy)propanoic acid MOD_RES 2-(S-cysteinyl)pyruvic acid O-phosphothioketal S-[1-carboxy-1-(phosphonooxy)ethyl]cysteine SPEPCys cysteinyl pyruvate O-phosphothioketal phosphoenolpyruvate cysteine adduct phospholactoyl cysteine adduct PSI-MOD MOD:00797 2-(S-L-cysteinyl)pyruvic acid O-phosphothioketal a protein modification that effectively converts an L-cysteine residue to the PEP adduct, 2-(S-L-cysteinyl)pyruvic acid O-phosphothioketal ChEBI:149496 PubMed:4696757 PubMed:7999765 PubMed:8664284 RESID:AA0391 (2R)-2-amino-3-[1-carboxy-1-(phosphonooxy)ethyl]sulfanylpropanoic acid 2-(S-L-cysteinyl)pyruvic acid O-phosphothioketal 2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-2-(phosphonooxy)propanoic acid 2-([(2R)-2-azanyl-2-carboxyethyl]sulfanyl)-2-(phosphonooxy)propanoic acid MOD_RES 2-(S-cysteinyl)pyruvic acid O-phosphothioketal S-[1-carboxy-1-(phosphonooxy)ethyl]cysteine SPEPCys cysteinyl pyruvate O-phosphothioketal phosphoenolpyruvate cysteine adduct phospholactoyl cysteine adduct A protein modification that can be regarded as effectively either one half of a cystine cross-link, or a cysteine residue with one hydrogen atom or proton removed. -1.01 C 0 H -1 N 0 O 0 S 0 -1.007825 C 3 H 4 N 1 O 1 S 1 102.13 102.00136 C Unimod:374 PSI-MOD Dehydro Half of a disulfide bridge MOD:00798 half cystine A protein modification that can be regarded as effectively either one half of a cystine cross-link, or a cysteine residue with one hydrogen atom or proton removed. PubMed:1988019 PubMed:2001356 PubMed:2076469 PubMed:3083866 PubMed:366603 PubMed:7918467 PubMed:8344916 Unimod:374 Dehydro Half of a disulfide bridge A protein modification that effectively converts an L-cysteine residue to S-galactosyl-L-cysteine. 162.14 C 6 H 10 N 0 O 5 S 0 162.05283 C 9 H 15 N 1 O 6 S 1 265.28 265.062 C artifact uniprot.ptm:PTM-0624 (2R)-2-amino-3-(D-galactopyranosylsulfanyl)propanoic acid CARBOHYD S-linked (Gal) cysteine S-(beta-D-galactopyranosyl)cysteine S-galactosyl-L-cysteine S-glycosyl-cysteine SGalCys PSI-MOD MOD:00799 The reported peptide has not been isolated or characterized in subsequent work, and the peptide sequence has not been found in the human proteome. This is a deprecated entry in RESID. It probably does not occur naturally [JSG]. S-galactosyl-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-galactosyl-L-cysteine. PubMed:11945907 RESID:AA0392 (2R)-2-amino-3-(D-galactopyranosylsulfanyl)propanoic acid CARBOHYD S-linked (Gal) cysteine S-(beta-D-galactopyranosyl)cysteine S-galactosyl-L-cysteine S-glycosyl-cysteine SGalCys A protein modification that effectively converts an L-cysteine residue, an L-histidine residue, homocitric acid and a one-vanadium seven-iron nine-sulfur cluster to L-cysteinyl-L-histidino-homocitryl vanadium heptairon nonasulfide. 932.51 C 7 Fe 7 H 6 N 0 O 7 S 9 V 1 932.24854 C 16 Fe 7 H 18 N 4 O 9 S 10 V 1 1172.8 1172.3167 C, H hypothetical CysHis-[V7Fe9S] L-cysteinyl-L-histidino-homocitryl vanadium heptairon nonasulfide carbide nitrogenase iron-vanadium cofactor PSI-MOD MOD:00800 Cross-link 2; incidental to RESID:AA0300. L-cysteinyl-L-histidino-homocitryl vanadium heptairon nonasulfide A protein modification that effectively converts an L-cysteine residue, an L-histidine residue, homocitric acid and a one-vanadium seven-iron nine-sulfur cluster to L-cysteinyl-L-histidino-homocitryl vanadium heptairon nonasulfide. PubMed:2345152 RESID:AA0393 CysHis-[V7Fe9S] L-cysteinyl-L-histidino-homocitryl vanadium heptairon nonasulfide carbide nitrogenase iron-vanadium cofactor A protein modification that effectively converts an L-cysteine residue, an L-histidine residue, homocitric acid and an eight-iron nine-sulfur cluster to L-cysteinyl-L-histidino-homocitryl octairon nonasulfide. 937.42 C 7 Fe 8 H 6 N 0 O 7 S 9 937.2406 2- C 16 Fe 8 H 18 N 4 O 9 S 10 1177.7 1177.3087 C, H hypothetical CysHis-[8Fe9S] L-cysteinyl-L-histidino-homocitryl octairon nonasulfide carbide nitrogenase iron-iron cofactor PSI-MOD MOD:00801 Cross-link 2; incidental to RESID:AA0300. L-cysteinyl-L-histidino-homocitryl octairon nonasulfide A protein modification that effectively converts an L-cysteine residue, an L-histidine residue, homocitric acid and an eight-iron nine-sulfur cluster to L-cysteinyl-L-histidino-homocitryl octairon nonasulfide. PubMed:8392330 RESID:AA0394 CysHis-[8Fe9S] L-cysteinyl-L-histidino-homocitryl octairon nonasulfide carbide nitrogenase iron-iron cofactor a protein modification that effectively converts an L-histidine residue to L-histidino vanadium tetraoxide 116.95 C 0 H 2 N 0 O 4 V 1 116.93927 C 6 H 9 N 3 O 5 V 1 254.1 253.99818 H natural (4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl) (dihydroxy)dioxovanadium 1'-vanadato-L-histidine L-histidino vanadium tetraoxide N(tau)-vanadatohistidine NtauH2VO4His bromoperoxidase vanadium cofactor chloroperoxidase vanadium cofactor dihydrogen (4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl) (tetraoxido)vanadate haloperoxidase vanadium cofactor histidine-1-vanadate histidine-N(epsilon)-vanadate histidine-N1'-vanadate tele-vanadatohistidine PSI-MOD MOD:00802 L-histidino vanadium tetraoxide a protein modification that effectively converts an L-histidine residue to L-histidino vanadium tetraoxide PubMed:10543953 PubMed:16494433 PubMed:8552646 RESID:AA0395 (4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl) (dihydroxy)dioxovanadium 1'-vanadato-L-histidine L-histidino vanadium tetraoxide N(tau)-vanadatohistidine NtauH2VO4His bromoperoxidase vanadium cofactor chloroperoxidase vanadium cofactor dihydrogen (4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl) (tetraoxido)vanadate haloperoxidase vanadium cofactor histidine-1-vanadate histidine-N(epsilon)-vanadate histidine-N1'-vanadate tele-vanadatohistidine A protein modification that effectively cross-links an L-cysteine residue and an L-tyrosine residue by a thioether bond to form 3-(S-L-cysteinyl)-L-tyrosine. -2.02 C 0 H -2 N 0 O 0 S 0 -2.01565 C 12 H 12 N 2 O 3 S 1 264.3 264.05685 C, Y natural uniprot.ptm:PTM-0020 (2S,3R)-2-amino-3-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-3-(4-hydroxyphenyl)propanoic acid 2-amino-3-(2-amino-2-carboxyethylthio)-3-(4-hydroxyphenyl)propanoic acid 3-(L-cystein-S-yl)-L-tyrosine CROSSLNK 3-(S-cysteinyl)-tyrosine (Cys-Tyr) S-(tyros-3'-yl)cysteine XLNKSCys3Tyr PSI-MOD MOD:00803 Cross-link 2. 3-(S-L-cysteinyl)-L-tyrosine A protein modification that effectively cross-links an L-cysteine residue and an L-tyrosine residue by a thioether bond to form 3-(S-L-cysteinyl)-L-tyrosine. PubMed:15342250 RESID:AA0396 (2S,3R)-2-amino-3-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-3-(4-hydroxyphenyl)propanoic acid 2-amino-3-(2-amino-2-carboxyethylthio)-3-(4-hydroxyphenyl)propanoic acid 3-(L-cystein-S-yl)-L-tyrosine CROSSLNK 3-(S-cysteinyl)-tyrosine (Cys-Tyr) S-(tyros-3'-yl)cysteine XLNKSCys3Tyr A protein modification that effectively converts an L-serine residue to O3-beta-glucosylated L-serine. 162.14 C 6 H 10 N 0 O 5 162.05283 C 9 H 15 N 1 O 7 249.22 249.08485 S natural uniprot.ptm:PTM-0573 (2S)-2-amino-3-(beta-D-glucopyranosyloxy)propanoic acid CARBOHYD O-linked (Glc) serine CARBOHYD O-linked (Hex) O-glucosyl-L-serine O-glycosylserine O3-glucosylserine OGlcSer PSI-MOD MOD:00804 O-glucosyl-L-serine A protein modification that effectively converts an L-serine residue to O3-beta-glucosylated L-serine. PubMed:10734111 PubMed:2105311 PubMed:2511201 RESID:AA0397 (2S)-2-amino-3-(beta-D-glucopyranosyloxy)propanoic acid CARBOHYD O-linked (Glc) serine CARBOHYD O-linked (Hex) O-glucosyl-L-serine O-glycosylserine O3-glucosylserine OGlcSer A protein modification that effectively converts an L-serine residue to O3-(N-acetylaminoglucosyl)-L-serine. 203.19 C 8 H 13 N 1 O 5 203.07938 C 11 H 18 N 2 O 7 290.27 290.1114 S natural uniprot.ptm:PTM-0580 (2S)-2-amino-3-(2-acetamido-2-deoxy-beta-D-glucopyranosyloxy)propanoic acid CARBOHYD O-linked (GlcNAc) serine CARBOHYD O-linked (HexNAc) O-(2-acetylamino-2-deoxy-beta-D-glucopyranosyl)-L-serine O-(N-acetylamino)glucosyl-L-serine O-(N-acetylglucosaminyl)serine O-glycosylserine O-seryl-beta-N-acetylglucosaminide O3-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-L-serine O3-(N-acetylglucosaminyl)serine OGlcNAcSer PSI-MOD HexNAc MOD:00805 O-(N-acetylamino)glucosyl-L-serine A protein modification that effectively converts an L-serine residue to O3-(N-acetylaminoglucosyl)-L-serine. PubMed:3086323 PubMed:8404891 RESID:AA0398 (2S)-2-amino-3-(2-acetamido-2-deoxy-beta-D-glucopyranosyloxy)propanoic acid CARBOHYD O-linked (GlcNAc) serine CARBOHYD O-linked (HexNAc) O-(2-acetylamino-2-deoxy-beta-D-glucopyranosyl)-L-serine O-(N-acetylamino)glucosyl-L-serine O-(N-acetylglucosaminyl)serine O-glycosylserine O-seryl-beta-N-acetylglucosaminide O3-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-L-serine O3-(N-acetylglucosaminyl)serine OGlcNAcSer HexNAc A protein modification that effectively converts an L-threonine residue to O3-(N-acetylaminoglucosyl)-L-threonine. 203.19 C 8 H 13 N 1 O 5 203.07938 C 12 H 20 N 2 O 7 304.3 304.12704 T natural uniprot.ptm:PTM-0582 (2S,3R)-2-amino-3-(2-acetamido-2-deoxy-beta-D-glucopyranosyloxy)butanoic acid CARBOHYD O-linked (GlcNAc) threonine CARBOHYD O-linked (HexNAc) O-(2-acetylamino-2-deoxy-beta-D-glucopyranosyl)-L-threonine O-(N-acetylamino)glucosyl-L-threonine O-(N-acetylglucosaminyl)-L-threonine O-glycosylthreonine O-threonyl-beta-N-acetylglucosaminide O3-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-L-threonine O3-(N-acetylglucosaminyl)threonine OGlcNAcThr PSI-MOD HexNAc MOD:00806 O-(N-acetylamino)glucosyl-L-threonine A protein modification that effectively converts an L-threonine residue to O3-(N-acetylaminoglucosyl)-L-threonine. PubMed:3086323 PubMed:8404891 RESID:AA0399 (2S,3R)-2-amino-3-(2-acetamido-2-deoxy-beta-D-glucopyranosyloxy)butanoic acid CARBOHYD O-linked (GlcNAc) threonine CARBOHYD O-linked (HexNAc) O-(2-acetylamino-2-deoxy-beta-D-glucopyranosyl)-L-threonine O-(N-acetylamino)glucosyl-L-threonine O-(N-acetylglucosaminyl)-L-threonine O-glycosylthreonine O-threonyl-beta-N-acetylglucosaminide O3-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-L-threonine O3-(N-acetylglucosaminyl)threonine OGlcNAcThr HexNAc A protein modification that effectively converts an L-serine residue to pyruvic acid. -17.03 C 0 H -3 N -1 O 0 -17.026548 C 3 H 3 O 2 71.06 71.013306 S natural N-term Unimod:385 uniprot.ptm:PTM-0266 2-oxopropanoic acid MOD_RES Pyruvic acid (Ser) Pyruvate Pyruvoyl- (Serine) pyruvic acid PSI-MOD MOD:00807 DeltaMass gives mass 70 and difference mass -16 with no formula pyruvic acid (Ser) A protein modification that effectively converts an L-serine residue to pyruvic acid. DeltaMass:23 PubMed:10085076 PubMed:3042771 PubMed:8464063 RESID:AA0127#SER Unimod:385#S 2-oxopropanoic acid MOD_RES Pyruvic acid (Ser) Pyruvate Pyruvoyl- (Serine) pyruvic acid A protein modification that effectively converts an L-serine residue to O3-galactosylserine. 162.14 C 6 H 10 N 0 O 5 162.05283 C 9 H 15 N 1 O 7 249.22 249.08485 S natural uniprot.ptm:PTM-0560 (2S)-2-amino-3-(alpha-D-galactopyranosyloxy)propanoic acid CARBOHYD O-linked (Gal) serine CARBOHYD O-linked (Hex) O-galactosyl-L-serine O-glycosylserine O3-galactosylserine OGalSer PSI-MOD MOD:00808 O-galactosyl-L-serine A protein modification that effectively converts an L-serine residue to O3-galactosylserine. PubMed:666730 RESID:AA0400 (2S)-2-amino-3-(alpha-D-galactopyranosyloxy)propanoic acid CARBOHYD O-linked (Gal) serine CARBOHYD O-linked (Hex) O-galactosyl-L-serine O-glycosylserine O3-galactosylserine OGalSer A protein modification that effectively converts an L-threonine residue to O3-galactosylthreonine. 162.14 C 6 H 10 N 0 O 5 162.05283 C 10 H 17 N 1 O 7 263.25 263.1005 T natural uniprot.ptm:PTM-0562 (2S,3R)-2-amino-3-(alpha-D-galactopyranosyloxy)butanoic acid CARBOHYD O-linked (Gal) threonine CARBOHYD O-linked (Hex) O-galactosyl-L-threonine O-glycosylthreonine O3-galactosylthreonine OGalThr PSI-MOD MOD:00809 O-galactosyl-L-threonine A protein modification that effectively converts an L-threonine residue to O3-galactosylthreonine. PubMed:2673008 RESID:AA0401 (2S,3R)-2-amino-3-(alpha-D-galactopyranosyloxy)butanoic acid CARBOHYD O-linked (Gal) threonine CARBOHYD O-linked (Hex) O-galactosyl-L-threonine O-glycosylthreonine O3-galactosylthreonine OGalThr A protein modification that effectively converts an L-serine residue to O3-mannosylserine. 162.14 C 6 H 10 N 0 O 5 162.05283 C 9 H 15 N 1 O 7 249.22 249.08485 S natural uniprot.ptm:PTM-0588 (2S)-2-amino-3-(alpha-D-mannopyranosyloxy)propanoic acid CARBOHYD O-linked (Hex) CARBOHYD O-linked (Man) serine O-glycosylserine O-mannopyranosylserine O-mannosyl-L-serine O3-mannosylserine OManSer PSI-MOD MOD:00810 O-mannosyl-L-serine A protein modification that effectively converts an L-serine residue to O3-mannosylserine. PubMed:391559 RESID:AA0402 (2S)-2-amino-3-(alpha-D-mannopyranosyloxy)propanoic acid CARBOHYD O-linked (Hex) CARBOHYD O-linked (Man) serine O-glycosylserine O-mannopyranosylserine O-mannosyl-L-serine O3-mannosylserine OManSer a protein modification that effectively forms a O3-mannosylthreonine 162.14 C 6 H 10 N 0 O 5 162.05283 C 10 H 17 N 1 O 7 263.25 263.1005 T natural uniprot.ptm:PTM-0591 (2S,3R)-2-amino-3-(alpha-D-mannopyranosyloxy)butanoic acid CARBOHYD O-linked (Hex) CARBOHYD O-linked (Man) threonine O-glycosylthreonine O-mannosyl-L-threonine O3-mannosylthreonine OManThr PSI-MOD MOD:00811 O-mannosyl-L-threonine a protein modification that effectively forms a O3-mannosylthreonine PubMed:391559 RESID:AA0403 (2S,3R)-2-amino-3-(alpha-D-mannopyranosyloxy)butanoic acid CARBOHYD O-linked (Hex) CARBOHYD O-linked (Man) threonine O-glycosylthreonine O-mannosyl-L-threonine O3-mannosylthreonine OManThr A protein modification that effectively converts an L-serine residue to an O-fucosylserine. 146.14 C 6 H 10 N 0 O 4 146.0579 C 9 H 15 N 1 O 6 233.22 233.08994 S natural Unimod:295 uniprot.ptm:PTM-0550 (2S)-2-amino-3-(6-deoxy-alpha-D-galactopyranosyloxy)propanoic acid CARBOHYD O-linked (Fuc) CARBOHYD O-linked (Fuc) serine CARBOHYD O-linked (dHex) O-fucosyl-L-serine O-glycosylserine O3-fucosylserine OFucSer PSI-MOD Fucose dHex MOD:00812 O-fucosyl-L-serine A protein modification that effectively converts an L-serine residue to an O-fucosylserine. PubMed:10734111 PubMed:11067851 PubMed:11344537 PubMed:12096136 PubMed:1517205 PubMed:15189151 PubMed:1904059 PubMed:3311742 PubMed:3578767 RESID:AA0404 Unimod:295#S (2S)-2-amino-3-(6-deoxy-alpha-D-galactopyranosyloxy)propanoic acid CARBOHYD O-linked (Fuc) CARBOHYD O-linked (Fuc) serine CARBOHYD O-linked (dHex) O-fucosyl-L-serine O-glycosylserine O3-fucosylserine OFucSer Fucose dHex A protein modification that effectively converts an threonine residue to an O-fucosylthreonine. 146.14 C 6 H 10 N 0 O 4 146.0579 C 10 H 17 N 1 O 6 247.25 247.10559 T natural Unimod:295 uniprot.ptm:PTM-0552 (2S,3R)-2-amino-3-(6-deoxy-alpha-D-galactopyranosyloxy)butanoic acid CARBOHYD O-linked (Fuc) threonine CARBOHYD O-linked (dHex) O-fucosyl-L-threonine O-glycosylthreonine O3-fucosylthreonine OFucThr PSI-MOD Fucose dHex MOD:00813 O-fucosyl-L-threonine A protein modification that effectively converts an threonine residue to an O-fucosylthreonine. PubMed:11344537 PubMed:11857757 PubMed:15189151 PubMed:1740125 PubMed:1900431 RESID:AA0405 Unimod:295#T (2S,3R)-2-amino-3-(6-deoxy-alpha-D-galactopyranosyloxy)butanoic acid CARBOHYD O-linked (Fuc) threonine CARBOHYD O-linked (dHex) O-fucosyl-L-threonine O-glycosylthreonine O3-fucosylthreonine OFucThr Fucose dHex A protein modification that effectively converts an L-serine residue to O3-xylosylserine. 132.12 C 5 H 8 N 0 O 4 132.04225 C 8 H 13 N 1 O 6 219.19 219.07428 S artifact uniprot.ptm:PTM-0598 (2S)-2-amino-3-(alpha-D-xylopyranosyloxy)propanoic acid CARBOHYD O-linked (Xyl) serine O-(beta-D-xylopyranosyl)-L-serine O-glycosylserine O-xylosyl-L-serine O3-xylosylserine OXylSer PSI-MOD MOD:00814 One glycosylated serine with weak electron density was modeled as O3-alpha-xylosylserine, while O3-alpha-mannosyl serine and threonine were modeled at ten other positions. The authors do not discuss this exception or provide chemical evidence for it. Since an O3-xylosyl serine modification has not been reported in any other fungal proteins, the modification is probably also an O3-alpha-mannosyl serine, see MOD:00810 [JSG]. O-xylosyl-L-serine A protein modification that effectively converts an L-serine residue to O3-xylosylserine. PubMed:8747463 RESID:AA0406 (2S)-2-amino-3-(alpha-D-xylopyranosyloxy)propanoic acid CARBOHYD O-linked (Xyl) serine O-(beta-D-xylopyranosyl)-L-serine O-glycosylserine O-xylosyl-L-serine O3-xylosylserine OXylSer OBSOLETE because redundant with MOD:00151. Remap to MOD:00151. MOD:00151 520.27 C 10 H 11 Mo 1 N 5 O 8 P 1 S 2 521.8841 C natural PSI-MOD MOD:00815 molybdopterin true OBSOLETE because redundant with MOD:00151. Remap to MOD:00151. PubMed:14527393 PubMed:7878465 PubMed:9428520 A protein modification that effectively converts an L-cysteine residue to S-stearoyl-L-cysteine. 266.47 C 18 H 34 N 0 O 1 S 0 266.26096 C 21 H 39 N 1 O 2 S 1 369.61 369.27014 C natural uniprot.ptm:PTM-0283 (R)-2-amino-3-(octadecanoylsulfanyl)propanoic acid 2-amino-3-(octadecanoylthio)propanoic acid LIPID S-stearoyl cysteine S-stearoyl-L-cysteine SSteCys Stearoylation cysteine octadecanoate thioester cysteine stearate thioester PSI-MOD MOD:00816 From DeltaMass: Average Mass: 266 S-stearoyl-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-stearoyl-L-cysteine. DeltaMass:0 PubMed:2371783 PubMed:3143715 PubMed:8761467 RESID:AA0407 (R)-2-amino-3-(octadecanoylsulfanyl)propanoic acid 2-amino-3-(octadecanoylthio)propanoic acid LIPID S-stearoyl cysteine S-stearoyl-L-cysteine SSteCys Stearoylation cysteine octadecanoate thioester cysteine stearate thioester A protein modification that effectively converts an L-tryptophan residue to 3'-geranyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan. 136.24 C 10 H 16 N 0 O 0 136.1252 C 21 H 26 N 2 O 1 322.45 322.2045 W natural uniprot.ptm:PTM-0026 (2S,3R)-3-geranyl-2,3-dihydro-2,N(alpha)-cyclo-L-tryptophan (2S,3aR,8aS)-3a-[(2E)-3,7-dimethylocta-2,6-dien-1-yl]-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole-2-carboxylic acid 3'-geranyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan 3'Ger2'N2cycTrp LIPID 3'-geranyl-2',N2-cyclotryptophan PSI-MOD MOD:00817 3'-geranyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan A protein modification that effectively converts an L-tryptophan residue to 3'-geranyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan. ChEBI:35304 PubMed:16407988 PubMed:8168130 RESID:AA0408 (2S,3R)-3-geranyl-2,3-dihydro-2,N(alpha)-cyclo-L-tryptophan (2S,3aR,8aS)-3a-[(2E)-3,7-dimethylocta-2,6-dien-1-yl]-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole-2-carboxylic acid 3'-geranyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan 3'Ger2'N2cycTrp LIPID 3'-geranyl-2',N2-cyclotryptophan A protein modification that effectively converts a residue to a glycosylphosphatidylinositolethanolamidated. 123.05 C 2 H 6 N 1 O 3 P 1 123.00853 X natural C-term Unimod:394 uniprot.ptm:PTM-0139 GPIRes LIPID GPI-anchor amidated carboxyl end PSI-MOD GPIanchor glycosylphosphatidylinositol MOD:00818 glycosylphosphatidylinositolated residue A protein modification that effectively converts a residue to a glycosylphosphatidylinositolethanolamidated. PubMed:12643538 Unimod:394#C-term GPIRes LIPID GPI-anchor amidated carboxyl end GPIanchor glycosylphosphatidylinositol A protein modification that effectively converts an L-glutamic acid residue to L-2-aminobutanoic acid. -44.01 C -1 H 0 N 0 O -2 -43.98983 C 4 H 7 N 1 O 1 85.11 85.052765 E natural (S)-2-aminobutanoic acid Abu L-2-amino-n-butyric acid L-2-aminobutanoic acid L-2-aminobutyric acid L-alpha-amino-n-butyric acid L-alpha-aminobutyric acid L-butyrine alpha-amino-n-butyric acid alpha-aminobutyric acid butyrine dCbxGlu PSI-MOD MOD:00819 L-2-aminobutanoic acid (Glu) A protein modification that effectively converts an L-glutamic acid residue to L-2-aminobutanoic acid. ChEBI:35619 DeltaMass:0 PubMed:11740505 RESID:AA0409 (S)-2-aminobutanoic acid Abu Abu L-2-amino-n-butyric acid L-2-aminobutanoic acid L-2-aminobutyric acid L-alpha-amino-n-butyric acid L-alpha-aminobutyric acid L-butyrine alpha-amino-n-butyric acid alpha-aminobutyric acid butyrine dCbxGlu A protein modification that effectively crosslinks an L-aspartic acid residue and a glycine residue to form 2-imino-alanine 5-imidazolinone glycine. -64.04 C -1 H -4 N 0 O -3 -64.016045 C 5 H 4 N 2 O 1 108.1 108.032364 D, G natural (2-ethanimidoyl-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid 2,N-didehydroalanyl-5-imidazolinone glycine 2-(1-iminoethyl)-1-carboxymethyl-1-imidazolin-5-one 2-imino-alanine 5-imidazolinone glycine 2-imino-alanyl-5-imidazolinone glycine [2-(1-iminoethyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid alanyl-5-imidazolinone glycine para-hydroxybenzylidene-imidazolidinone chromophore red fluorescent protein zRFP574 chromophore PSI-MOD MOD:00820 Cross-link 2; carboxamidine. 2-imino-alanine 5-imidazolinone glycine A protein modification that effectively crosslinks an L-aspartic acid residue and a glycine residue to form 2-imino-alanine 5-imidazolinone glycine. PubMed:16627946 RESID:AA0410 (2-ethanimidoyl-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid 2,N-didehydroalanyl-5-imidazolinone glycine 2-(1-iminoethyl)-1-carboxymethyl-1-imidazolin-5-one 2-imino-alanine 5-imidazolinone glycine 2-imino-alanyl-5-imidazolinone glycine [2-(1-iminoethyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid alanyl-5-imidazolinone glycine para-hydroxybenzylidene-imidazolidinone chromophore red fluorescent protein zRFP574 chromophore A protein modification that effectively crosslinks an L-alanine residue and an L-cysteine residue by a thioester bond to form S-(L-alanyl)-L-cysteine. -18.02 C 0 H -2 N 0 O -1 S 0 -18.010565 C 6 H 9 N 2 O 2 S 1 173.21 173.03847 A, C hypothetical C-term (2R)-2-amino-3-([(2S)-2-aminopropanoyl]sulfanyl)propanoic acid CROSSLNK Alanyl cysteine thioester (Cys-Ala) S-(2-aminopropanoyl)cysteine S-(L-alanyl)-L-cysteine XLNK1AlaSCys alanine cysteine thioester PSI-MOD MOD:00821 Cross-link 2. S-(L-alanyl)-L-cysteine A protein modification that effectively crosslinks an L-alanine residue and an L-cysteine residue by a thioester bond to form S-(L-alanyl)-L-cysteine. PubMed:11807079 RESID:AA0411 (2R)-2-amino-3-([(2S)-2-aminopropanoyl]sulfanyl)propanoic acid CROSSLNK Alanyl cysteine thioester (Cys-Ala) S-(2-aminopropanoyl)cysteine S-(L-alanyl)-L-cysteine XLNK1AlaSCys alanine cysteine thioester A protein modification that effectively crosslinks an L-leucine residue and an L-cysteine residue by a thioester bond to form S-(L-leucyl)-L-cysteine. -18.02 C 0 H -2 N 0 O -1 S 0 -18.010565 C 9 H 15 N 2 O 2 S 1 215.29 215.08542 C, L natural C-term (2R)-2-amino-3-([(2S)-2-amino-4-methylpentanoyl]sulfanyl)propanoic acid CROSSLNK Leucyl cysteine thioester (Cys-Leu) S-(2-amino-4-methylpentanoyl)cysteine S-(L-leucyl)-L-cysteine XLNK1LeuSCys leucine cysteine thioester PSI-MOD MOD:00822 Cross-link 2. S-(L-leucyl)-L-cysteine A protein modification that effectively crosslinks an L-leucine residue and an L-cysteine residue by a thioester bond to form S-(L-leucyl)-L-cysteine. PubMed:12591958 RESID:AA0412 (2R)-2-amino-3-([(2S)-2-amino-4-methylpentanoyl]sulfanyl)propanoic acid CROSSLNK Leucyl cysteine thioester (Cys-Leu) S-(2-amino-4-methylpentanoyl)cysteine S-(L-leucyl)-L-cysteine XLNK1LeuSCys leucine cysteine thioester A protein modification that effectively crosslinks an L-methionine residue and an L-cysteine residue by a thioester bond to form S-(L-methionyl)-L-cysteine. -18.02 C 0 H -2 N 0 O -1 S 0 -18.010565 C 8 H 13 N 2 O 2 S 2 233.32 233.04184 C, M natural C-term (2R)-2-amino-3-([(2S)-2-amino-4-(methylsulfanyl)butanoyl]sulfanyl)propanoic acid CROSSLNK Methionyl cysteine thioester (Cys-Met) S-(2-amino-4-methylthiobutanoyl)cysteine S-(L-methionyl)-L-cysteine XLNK1MetSCys methionine cysteine thioester PSI-MOD MOD:00823 Cross-link 2. S-(L-methionyl)-L-cysteine A protein modification that effectively crosslinks an L-methionine residue and an L-cysteine residue by a thioester bond to form S-(L-methionyl)-L-cysteine. PubMed:12146974 RESID:AA0413 (2R)-2-amino-3-([(2S)-2-amino-4-(methylsulfanyl)butanoyl]sulfanyl)propanoic acid CROSSLNK Methionyl cysteine thioester (Cys-Met) S-(2-amino-4-methylthiobutanoyl)cysteine S-(L-methionyl)-L-cysteine XLNK1MetSCys methionine cysteine thioester A protein modification that effectively converts an L-tyrosine residue to dehydroalanine. -94.11 C -6 H -6 N 0 O -1 -94.04186 C 3 H 3 N 1 O 1 69.06 69.02146 Y natural Unimod:400 uniprot.ptm:PTM-0647 2,3-didehydroalanine 2-aminoacrylic acid 2-aminopropenoic acid 4-methylidene-imidazole-5-one (MIO) active site Dha anhydroserine dHAla(Tyr) dehydroalanine PSI-MOD MOD:00824 incidental to RESID:AA0178 dehydroalanine (Tyr) A protein modification that effectively converts an L-tyrosine residue to dehydroalanine. PubMed:10220322 PubMed:1547888 PubMed:1815586 PubMed:2914619 PubMed:6838602 PubMed:7947813 PubMed:8239649 RESID:AA0181#TYR Unimod:400 2,3-didehydroalanine 2-aminoacrylic acid 2-aminopropenoic acid 4-methylidene-imidazole-5-one (MIO) active site Dha anhydroserine dHAla(Tyr) dehydroalanine A protein modification that effectively crosslinks an L-phenylalanine residue and an L-cysteine residue by a thioester bond to form S-(L-phenylalaninyl)-L-cysteine. -18.02 C 0 H -2 N 0 O -1 S 0 -18.010565 C 12 H 13 N 2 O 2 S 1 249.31 249.06978 C, F natural C-term (2R)-2-amino-3-([(2S)-2-amino-3-phenylpropanoyl]sulfanyl)propanoic acid CROSSLNK Phenylalanyl cysteine thioester (Cys-Phe) S-(2-amino-3-phenylpropanoyl)cysteine S-(L-phenylalanyl)-L-cysteine XLNK1PheSCys phenylalanine cysteine thioester PSI-MOD MOD:00825 Cross-link 2. S-(L-phenylalanyl)-L-cysteine A protein modification that effectively crosslinks an L-phenylalanine residue and an L-cysteine residue by a thioester bond to form S-(L-phenylalaninyl)-L-cysteine. PubMed:12591958 RESID:AA0414 (2R)-2-amino-3-([(2S)-2-amino-3-phenylpropanoyl]sulfanyl)propanoic acid CROSSLNK Phenylalanyl cysteine thioester (Cys-Phe) S-(2-amino-3-phenylpropanoyl)cysteine S-(L-phenylalanyl)-L-cysteine XLNK1PheSCys phenylalanine cysteine thioester A protein modification that effectively crosslinks an L-threonine residue and an L-cysteine residue by a thioester bond to form S-(L-threonyl)-L-cysteine. -18.02 C 0 H -2 N 0 O -1 S 0 -18.010565 C 7 H 11 N 2 O 3 S 1 203.24 203.04904 C, T natural C-term (2R)-2-amino-3-([(2S,3R)-2-amino-3-hydroxybutanoyl]sulfanyl)propanoic acid CROSSLNK Threonyl cysteine thioester (Cys-Thr) S-(2-amino-3-hydroxybutanoyl)cysteine S-(L-threonyl)-L-cysteine XLNK1ThrSCys threonine cysteine thioester PSI-MOD MOD:00826 Cross-link 2. S-(L-threonyl)-L-cysteine A protein modification that effectively crosslinks an L-threonine residue and an L-cysteine residue by a thioester bond to form S-(L-threonyl)-L-cysteine. PubMed:15268951 RESID:AA0415 (2R)-2-amino-3-([(2S,3R)-2-amino-3-hydroxybutanoyl]sulfanyl)propanoic acid CROSSLNK Threonyl cysteine thioester (Cys-Thr) S-(2-amino-3-hydroxybutanoyl)cysteine S-(L-threonyl)-L-cysteine XLNK1ThrSCys threonine cysteine thioester A protein modification that effectively crosslinks an L-tyrosine residue and an L-cysteine residue by a thioester bond to form S-(L-tyrosyl)-L-cysteine. -18.02 C 0 H -2 N 0 O -1 S 0 -18.010565 C 12 H 13 N 2 O 3 S 1 265.31 265.0647 C, Y natural C-term (2R)-2-amino-3-([(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]sulfanyl)propanoic acid CROSSLNK Tyrosyl cysteine thioester (Cys-Tyr) S-(L-tyrosyl)-L-cysteine S-[2-amino-3-(4-hydoxyphenyl)propanoyl]cysteine XLNK1TyrSCys tyrosine cysteine thioester PSI-MOD MOD:00827 Cross-link 2. S-(L-tyrosyl)-L-cysteine A protein modification that effectively crosslinks an L-tyrosine residue and an L-cysteine residue by a thioester bond to form S-(L-tyrosyl)-L-cysteine. PubMed:11807079 RESID:AA0416 (2R)-2-amino-3-([(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]sulfanyl)propanoic acid CROSSLNK Tyrosyl cysteine thioester (Cys-Tyr) S-(L-tyrosyl)-L-cysteine S-[2-amino-3-(4-hydoxyphenyl)propanoyl]cysteine XLNK1TyrSCys tyrosine cysteine thioester A protein modification that effectively crosslinks an L-tryptophan residue and an L-cysteine residue by a thioester bond to form S-(L-tryptophanyl)-L-cysteine. -18.02 C 0 H -2 N 0 O -1 S 0 -18.010565 C 14 H 14 N 3 O 2 S 1 288.35 288.08066 C, W natural C-term (2R)-2-amino-3-([(2S)-2-amino-3-(1H-indol-3-yl)propanoyl]sulfanyl)propanoic acid CROSSLNK Tryptophanyl cysteine thioester (Cys-Trp) S-(L-tryptophanyl)-L-cysteine S-[2-amino-3-(1H-indol-3-yl)propanoyl]cysteine XLNK1TrpSCys tryptophan cysteine thioester PSI-MOD MOD:00828 Cross-link 2. S-(L-tryptophanyl)-L-cysteine A protein modification that effectively crosslinks an L-tryptophan residue and an L-cysteine residue by a thioester bond to form S-(L-tryptophanyl)-L-cysteine. PubMed:16030216 RESID:AA0417 (2R)-2-amino-3-([(2S)-2-amino-3-(1H-indol-3-yl)propanoyl]sulfanyl)propanoic acid CROSSLNK Tryptophanyl cysteine thioester (Cys-Trp) S-(L-tryptophanyl)-L-cysteine S-[2-amino-3-(1H-indol-3-yl)propanoyl]cysteine XLNK1TrpSCys tryptophan cysteine thioester A protein modification that effectively crosslinks an L-phenylalanine residue and an L-serine residue by an ester bond to form S-(L-phenylalaninyl)-L-serine. -18.02 C 0 H -2 N 0 O -1 S 0 -18.010565 C 12 H 13 N 2 O 3 233.25 233.09262 F, S natural C-term (2S)-2-amino-3-([(2S)-2-amino-3-phenylpropanoyl]oxy)propanoic acid CROSSLNK Phenylalanyl serine ester (Ser-Phe) O-(2-amino-3-phenylpropanoyl)serine O-(L-phenylalanyl)-L-serine XLNK1PheOSer phenylalanine serine ester PSI-MOD MOD:00829 Cross-link 2. O-(L-phenylalanyl)-L-serine A protein modification that effectively crosslinks an L-phenylalanine residue and an L-serine residue by an ester bond to form S-(L-phenylalaninyl)-L-serine. PubMed:12591958 RESID:AA0418 (2S)-2-amino-3-([(2S)-2-amino-3-phenylpropanoyl]oxy)propanoic acid CROSSLNK Phenylalanyl serine ester (Ser-Phe) O-(2-amino-3-phenylpropanoyl)serine O-(L-phenylalanyl)-L-serine XLNK1PheOSer phenylalanine serine ester A protein modification that effectively converts an L-proline residue to an N-methyl-L-proline. 14.03 C 1 H 2 N 0 O 0 14.01565 C 6 H 10 N 1 O 1 112.15 112.07624 P natural N-term uniprot.ptm:PTM-0219 (S)-1-methylpyrrolidine-2-carboxylic acid 1-methylpyrrolidine-2-carboxylic acid MOD_RES N-methylproline N-methyl-L-proline N-methylated L-proline NMePro hygric acid PSI-MOD MOD:00830 Polypeptides with monomethylated amino terminals can undergo premature cleavage during the coupling step of an Edman degradation. This can result in "preview" with both a residue and the following residue being seen from the first step on through a sequence [JSG]. N-methyl-L-proline A protein modification that effectively converts an L-proline residue to an N-methyl-L-proline. PubMed:3127388 RESID:AA0419 (S)-1-methylpyrrolidine-2-carboxylic acid 1-methylpyrrolidine-2-carboxylic acid MOD_RES N-methylproline N-methyl-L-proline N-methylated L-proline NMePro hygric acid A protein modification that effectively converts an L-asparagine residue to N4-(N-acetylaminoglucosyl)-L-asparagine. 203.19 C 8 H 13 N 1 O 5 203.07938 C 12 H 19 N 3 O 7 317.3 317.1223 N natural uniprot.ptm:PTM-0527 CARBOHYD N-linked (GlcNAc) asparagine N4GlcNAcAsn PSI-MOD HexNAc MOD:00831 N4-(N-acetylamino)glucosyl-L-asparagine A protein modification that effectively converts an L-asparagine residue to N4-(N-acetylaminoglucosyl)-L-asparagine. PubMed:111247 PubMed:1694179 PubMed:5490222 RESID:AA0151#var CARBOHYD N-linked (GlcNAc) asparagine N4GlcNAcAsn HexNAc A protein modification that effectively converts an L-asparagine residue to N4-(N-acetaminogalactosyl)-L-asparagine. 203.19 C 8 H 13 N 1 O 5 203.07938 C 12 H 19 N 3 O 7 317.3 317.1223 N natural uniprot.ptm:PTM-0512 (2S)-2-amino-4-(2-acetamido-2-deoxy-beta-D-galactopyranosyl)amino-4-oxobutanoic acid CARBOHYD N-linked (GalNAc) asparagine N4-(2-acetamido-2-deoxy-beta-D-galactopyranosyl)-L-asparagine N4-(2-acetylamino-2-deoxy-beta-D-galactopyranosyl)-L-asparagine N4-(N-acetylamino)galactosyl-L-asparagine N4-(N-acetylgalactosaminyl)asparagine N4-asparagine-beta-N-acetylgalactosaminide N4-glycosyl-L-asparagine N4-glycosylasparagine N4GalNAcAsn PSI-MOD HexNAc MOD:00832 N4-(N-acetylamino)galactosyl-L-asparagine A protein modification that effectively converts an L-asparagine residue to N4-(N-acetaminogalactosyl)-L-asparagine. PubMed:8262914 RESID:AA0420 (2S)-2-amino-4-(2-acetamido-2-deoxy-beta-D-galactopyranosyl)amino-4-oxobutanoic acid CARBOHYD N-linked (GalNAc) asparagine N4-(2-acetamido-2-deoxy-beta-D-galactopyranosyl)-L-asparagine N4-(2-acetylamino-2-deoxy-beta-D-galactopyranosyl)-L-asparagine N4-(N-acetylamino)galactosyl-L-asparagine N4-(N-acetylgalactosaminyl)asparagine N4-asparagine-beta-N-acetylgalactosaminide N4-glycosyl-L-asparagine N4-glycosylasparagine N4GalNAcAsn HexNAc A protein modification that effectively converts an L-asparagine residue to N4-glucosyl-asparagine. 162.14 C 6 H 10 N 0 O 5 162.05283 C 10 H 16 N 2 O 7 276.25 276.09576 N natural uniprot.ptm:PTM-0517 (2S)-2-amino-4-(D-glucopyranosyl)amino-4-oxobutanoic acid CARBOHYD N-linked (Glc) CARBOHYD N-linked (Glc) asparagine N4-(D-glucopyranosyl)-L-asparagine N4-asparagine-glucoside N4-glucosyl-L-asparagine N4-glucosylasparagine N4-glycosyl-L-asparagine N4-glycosylasparagine N4GlcAsn PSI-MOD MOD:00833 N4-glucosyl-L-asparagine A protein modification that effectively converts an L-asparagine residue to N4-glucosyl-asparagine. PubMed:1569073 PubMed:3410849 RESID:AA0421 (2S)-2-amino-4-(D-glucopyranosyl)amino-4-oxobutanoic acid CARBOHYD N-linked (Glc) CARBOHYD N-linked (Glc) asparagine N4-(D-glucopyranosyl)-L-asparagine N4-asparagine-glucoside N4-glucosyl-L-asparagine N4-glucosylasparagine N4-glycosyl-L-asparagine N4-glycosylasparagine N4GlcAsn A protein modification that effectively converts an L-serine residue to O3-(N-acetamino)fucosylserine. 187.19 C 8 H 13 N 1 O 4 187.08446 C 11 H 18 N 2 O 6 274.27 274.1165 S natural uniprot.ptm:PTM-0553 (2S)-2-amino-3-(2-acetamido-2-deoxy-beta-D-fucopyranosyloxy)propanoic acid CARBOHYD O-linked (FucNAc) serine O-(2-acetylamino-2-deoxy-beta-D-fucopyranosyl)-L-serine O-(N-acetylamino)fucosyl-L-serine O-(N-acetylfucosaminyl)serine O-seryl-beta-N-acetylfucosaminide O3-(2-acetamido-2-deoxy-beta-D-fucopyranosyl)-L-serine O3-(N-acetylfucosaminyl)serine OFucNAcSer PSI-MOD MOD:00834 O-(N-acetylamino)fucosyl-L-serine A protein modification that effectively converts an L-serine residue to O3-(N-acetamino)fucosylserine. PubMed:11342554 PubMed:12010970 RESID:AA0422 (2S)-2-amino-3-(2-acetamido-2-deoxy-beta-D-fucopyranosyloxy)propanoic acid CARBOHYD O-linked (FucNAc) serine O-(2-acetylamino-2-deoxy-beta-D-fucopyranosyl)-L-serine O-(N-acetylamino)fucosyl-L-serine O-(N-acetylfucosaminyl)serine O-seryl-beta-N-acetylfucosaminide O3-(2-acetamido-2-deoxy-beta-D-fucopyranosyl)-L-serine O3-(N-acetylfucosaminyl)serine OFucNAcSer A protein modification that effectively converts an L-serine residue to L-oxoalanine. -2.02 C 0 H -2 N 0 O 0 -2.01565 C 3 H 3 N 1 O 2 85.06 85.01638 S natural Unimod:401 (S)-2-amino-3-oxopropanoic acid 2-amino-3-oxopropionic acid L-3-oxoalanine L-amino-malonic acid semialdehyde L-aminomalonaldehydic acid MOD_RES 3-oxoalanine (Ser) formylglycine (from serine) PSI-MOD C(alpha)-formylglycine Didehydro L-serinesemialdehyde dehydrogenated serine residue formylglycine oxoalanine MOD:00835 L-3-oxoalanine (Ser) A protein modification that effectively converts an L-serine residue to L-oxoalanine. DeltaMass:349 PubMed:14563551 PubMed:7628016 PubMed:8681943 PubMed:9276974 PubMed:9478923 RESID:AA0185#SER Unimod:401#S (S)-2-amino-3-oxopropanoic acid 2-amino-3-oxopropionic acid L-3-oxoalanine L-amino-malonic acid semialdehyde L-aminomalonaldehydic acid MOD_RES 3-oxoalanine (Ser) formylglycine (from serine) C(alpha)-formylglycine Didehydro L-serinesemialdehyde dehydrogenated serine residue formylglycine oxoalanine A protein modification that effectively substitutes two (2)H deuterium atoms for two (1)H protium atoms. D(H)2Res PSI-MOD MOD:00836 deuterium disubstituted residue A protein modification that effectively substitutes two (2)H deuterium atoms for two (1)H protium atoms. PubMed:18688235 D(H)2Res A protein modification that effectively substitutes four (2)H deuterium atoms for four (1)H protium atoms. D(H)4Res PSI-MOD MOD:00837 deuterium tetrasubstituted residue A protein modification that effectively substitutes four (2)H deuterium atoms for four (1)H protium atoms. PubMed:18688235 D(H)4Res A protein modification that effectively substitutes three (1)H protium atoms with three (2)H deuterium atoms to produce 3x(2)H labeled L-leucine. 3.02 (1)H -3 (2)H 3 3.01883 C 6 (1)H 8 (2)H 3 N 1 O 1 116.1 116.1029 L artifact Unimod:262 D(H)3Leu PSI-MOD Label:2H(3) Trideuteration MOD:00838 3x(2)H labeled L-leucine A protein modification that effectively substitutes three (1)H protium atoms with three (2)H deuterium atoms to produce 3x(2)H labeled L-leucine. Unimod:262#L D(H)3Leu Label:2H(3) Trideuteration A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing deuteriumm, (2)H. PSI-MOD MOD:00839 (2)H deuterium labeled residue A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing deuteriumm, (2)H. PubMed:18688235 A protein modification produced by formation of an adduct with an isocyanate compound. PSI-MOD MOD:00840 isocyanate reagent derivatized residue A protein modification produced by formation of an adduct with an isocyanate compound. PubMed:18688235 A protein modification produced by formation of an adduct with an isothiocyanate compound. PSI-MOD MOD:00841 isothiocyanate reagent derivatized residue A protein modification produced by formation of an adduct with an isothiocyanate compound. PubMed:18688235 A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing (13)C. PSI-MOD MOD:00842 (13)C labeled residue A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing (13)C. PubMed:18688235 A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing (15)N. PSI-MOD MOD:00843 (15)N labeled residue A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing (15)N. PubMed:18688235 A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing (18)O. PSI-MOD MOD:00844 (18)O labeled residue A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing (18)O. PubMed:18688235 A protein modification that effectively substitutes one or more (18)O atoms for (16)O atoms. PSI-MOD MOD:00845 (18)O substituted residue A protein modification that effectively substitutes one or more (18)O atoms for (16)O atoms. PubMed:18688235 stub PSI-MOD MOD:00846 levuglandinyl (prostaglandin H2) adduct stub PubMed:18688235 A protein modification that effectively substitutes two (18)O atom for two (16)O atoms. PSI-MOD MOD:00847 (18)O disubstituted residue A protein modification that effectively substitutes two (18)O atom for two (16)O atoms. PubMed:18688235 A protein modification that is produced by formation of an adduct with a particular compound used as a reagent. PSI-MOD MOD:00848 reagent derivatized residue A protein modification that is produced by formation of an adduct with a particular compound used as a reagent. PubMed:18688235 A protein modification that effectively substitutes a potassium atom for a hydrogen atom. KRes PSI-MOD MOD:00849 potassium containing modified residue A protein modification that effectively substitutes a potassium atom for a hydrogen atom. PubMed:18688235 KRes A protein modification that inserts or replaces a residue with an unnatural residue that is not considered to be derived from a natural residue by some chemical process. PSI-MOD MOD:00850 unnatural residue A protein modification that inserts or replaces a residue with an unnatural residue that is not considered to be derived from a natural residue by some chemical process. PubMed:18688235 A protein modification that effectively replaces a carboxamido group with a carboxyl group labeled with (18)O. X artifact PSI-MOD MOD:00851 (18)O labeled deamidated residue A protein modification that effectively replaces a carboxamido group with a carboxyl group labeled with (18)O. PubMed:18688235 A protein modification that effectively replaces a carboxamido group with a carboxyl group labeled with one (18)O. 2.99 H -1 N -1 (18)O 1 2.988262 X artifact Unimod:366 PSI-MOD MOD:00852 1x(18)O labeled deamidated residue A protein modification that effectively replaces a carboxamido group with a carboxyl group labeled with one (18)O. PubMed:8382902 Unimod:366 A protein modification that effectively replaces a carboxamido group with a carboxyl group labeled with two (18)O. 4.99 H -1 N -1 (16)O -1 (18)O 2 4.992508 X artifact PSI-MOD MOD:00853 2x(18)O labeled deamidated residue A protein modification that effectively replaces a carboxamido group with a carboxyl group labeled with two (18)O. PubMed:18688235 A protein modification that effectively converts an L-lysine to L-lysinium (protonated L-lysine). 1.01 C 0 H 1 N 0 O 0 1.007276 1+ C 6 H 13 N 2 O 1 129.18 129.10223 K natural PSI-MOD MOD:00854 Some sources compute the difference formula for charged, quatenary modified lysine based on protonated lysine rather than neutral lysine residue. In such cases, a comparable difference formula can be calculated based on this derivative. protonated L-lysine (L-lysinium) residue A protein modification that effectively converts an L-lysine to L-lysinium (protonated L-lysine). PubMed:18688235 A protein modification that effectively converts an L-lysinium (N6-protonated L-lysine) residue to an N6,N6,N6-trimethyl-L-lysine. 42.08 C 3 H 6 N 0 O 0 42.046402 1+ C 9 H 19 N 2 O 1 171.26 171.14919 MOD:00854 natural Unimod:37 N6Me3Lys trimethylk PSI-MOD MOD:00855 For amino acids residues, amine trimethylation can effectively only be accomplished with an aminium, protonated primary amino, group. This process accounts only for trimethylation and not protonation. The alternative N6Me3+Lys process (MOD:00083) accounts for both protonation and trimethylation. N6,N6,N6-trimethyl-L-lysine (from L-lysinium residue) A protein modification that effectively converts an L-lysinium (N6-protonated L-lysine) residue to an N6,N6,N6-trimethyl-L-lysine. DeltaMass:0 OMSSA:15 PubMed:12590383 PubMed:3145979 PubMed:4304194 PubMed:6778808 PubMed:7093227 PubMed:8453381 Unimod:37#K N6Me3Lys trimethylk A protein modification that effectively converts an L-alanine residue to an L-alaninium (protonated L-alanine). 1.01 C 0 H 1 N 0 O 0 1.007276 1+ C 3 H 7 N 1 O 1 73.09 73.052216 A natural N-term PSI-MOD MOD:00856 protonated L-alanine (L-alaninium) residue A protein modification that effectively converts an L-alanine residue to an L-alaninium (protonated L-alanine). PubMed:18688235 A protein modification that effectively converts an L-alaninium (protonated L-alanine) residue to an N,N,N-trimethyl-L-alanine. 42.08 C 3 H 6 N 0 O 0 42.046402 1+ C 6 H 13 N 1 O 1 115.18 115.09917 MOD:00856 natural N-term Unimod:37 N2Me3Ala PSI-MOD MOD:00857 For amino acids residues, amine trimethylation can effectively only be accomplished with an aminium, protonated primary amino, group. This process accounts only for trimethylation and not protonation. The alternative N2Me3+Ala process (MOD:00071) accounts for both protonation and trimethylation. N,N,N-trimethyl-L-alanine (from L-alaninium) A protein modification that effectively converts an L-alaninium (protonated L-alanine) residue to an N,N,N-trimethyl-L-alanine. PubMed:12590383 PubMed:332162 PubMed:3979397 PubMed:6778808 PubMed:7715456 Unimod:37#A N2Me3Ala A protein modification that effectively converts an L-serine residue to D-alanine. -16.0 C 0 H 0 N 0 O -1 -15.994915 C 3 H 5 N 1 O 1 71.08 71.03712 S natural uniprot.ptm:PTM-0113 (R)-2-aminopropanoic acid D-Ala(Ser) D-alanine MOD_RES D-alanine (Ser) PSI-MOD MOD:00858 D-alanine (Ser) A protein modification that effectively converts an L-serine residue to D-alanine. PubMed:7961627 RESID:AA0191#SER (R)-2-aminopropanoic acid D-Ala(Ser) D-alanine MOD_RES D-alanine (Ser) A protein modification that can be derived from different natural residues by different chemical processes. X natural PSI-MOD MOD:00859 modified residue that can arise from different natural residues A protein modification that can be derived from different natural residues by different chemical processes. PubMed:18688235 A protein modification that produces an amino acid residue containing an exogenous sulfur atom. PSI-MOD MOD:00860 sulfur containing modified residue A protein modification that produces an amino acid residue containing an exogenous sulfur atom. PubMed:18688235 A protein modification that produces an amino acid residue containing a phosphorus atom. PSI-MOD MOD:00861 phosphorus containing modified residue A protein modification that produces an amino acid residue containing a phosphorus atom. PubMed:18688235 A protein modification that effectively converts a source amino acid residue to D-alanine. C 3 H 5 N 1 O 1 71.08 71.03712 X natural (R)-2-aminopropanoic acid D-alanine MOD_RES D-alanine (Ala) MOD_RES D-alanine (Ser) PSI-MOD MOD:00862 D-alanine A protein modification that effectively converts a source amino acid residue to D-alanine. ChEBI:29949 PubMed:7287302 PubMed:7961627 RESID:AA0191 (R)-2-aminopropanoic acid D-alanine MOD_RES D-alanine (Ala) MOD_RES D-alanine (Ser) A protein modification that effectively converts an L-threonine residue to D-allo-threonine. 0.0 C 0 H 0 N 0 O 0 0.0 C 4 H 7 N 1 O 2 101.1 101.047676 T natural uniprot.ptm:PTM-0310 (2R,3R)-2-amino-3-hydroxybutanoic acid D-Thr D-threonine MOD_RES D-threonine PSI-MOD MOD:00863 D-allo-threonine A protein modification that effectively converts an L-threonine residue to D-allo-threonine. ChEBI:32826 PubMed:18025465 PubMed:6893271 RESID:AA0199 (2R,3R)-2-amino-3-hydroxybutanoic acid D-Thr D-threonine MOD_RES D-threonine A protein modification that effectively converts three L-cysteine residues, an L-histidine residue and a two-iron two-sulfur cluster to tris-L-cysteinyl L-histidino diiron disulfide. 171.78 C 0 Fe 2 H -4 N 0 O 0 S 2 171.78381 2- C 15 Fe 2 H 18 N 6 O 4 S 5 618.34 617.8703 C, C, C, H natural CDGSH domain iron-sulfur cluster METAL Iron-sulfur (2Fe-2S) METAL Iron-sulfur (2Fe-2S); via pros nitrogen di-mu-sulfido(bis-S-cysteinyliron)(S-cysteinyl-N3'-histidinoiron) tris-L-cysteinyl L-histidino diiron disulfide PSI-MOD MOD:00864 Cross-link 4. tris-L-cysteinyl L-histidino diiron disulfide A protein modification that effectively converts three L-cysteine residues, an L-histidine residue and a two-iron two-sulfur cluster to tris-L-cysteinyl L-histidino diiron disulfide. PubMed:17766439 PubMed:17766440 RESID:AA0438 CDGSH domain iron-sulfur cluster METAL Iron-sulfur (2Fe-2S) METAL Iron-sulfur (2Fe-2S); via pros nitrogen di-mu-sulfido(bis-S-cysteinyliron)(S-cysteinyl-N3'-histidinoiron) tris-L-cysteinyl L-histidino diiron disulfide A protein modification that effectively converts an L-aspartic acid residue to N-aspartyl-glycosylsphingolipidinositolethanolamine. 123.05 C 2 H 6 N 1 O 3 P 1 123.00853 C 6 H 12 N 2 O 7 P 1 255.14 255.03821 D hypothetical C-term uniprot.ptm:PTM-0322 GSIAsp LIPID GPI-like-anchor amidated aspartate N-aspartyl-glycosylsphingolipidinositolethanolamine PSI-MOD MOD:00865 N-aspartyl-glycosylsphingolipidinositolethanolamine A protein modification that effectively converts an L-aspartic acid residue to N-aspartyl-glycosylsphingolipidinositolethanolamine. RESID:AA0439 GSIAsp LIPID GPI-like-anchor amidated aspartate N-aspartyl-glycosylsphingolipidinositolethanolamine A protein modification that effectively converts an L-proline residue to one of several dihydroxylated proline residues, such as (2S,3R,4R)-3,4-dihydroxyproline or (2S,3R,4S)-3,4-dihydroxyproline. 32.0 C 0 H 0 N 0 O 2 31.989828 C 5 H 7 N 1 O 3 129.12 129.04259 P natural uniprot.ptm:PTM-0024 Hy2Pro PSI-MOD MOD:00866 dihydroxylated proline A protein modification that effectively converts an L-proline residue to one of several dihydroxylated proline residues, such as (2S,3R,4R)-3,4-dihydroxyproline or (2S,3R,4S)-3,4-dihydroxyproline. PubMed:18688235 Hy2Pro A protein modification that effectively cross-links an L-cysteine residue and an L-cysteine converted to an L-selenocysteine residue to form L-cysteinyl-L-selenocystine. 44.9 C 0 H -2 N 0 O 0 S -1 Se 1 45.9288 C 6 H 8 N 2 O 2 S 1 Se 1 251.17 251.94717 C, C natural (R,R)-2-amino-3-[3-(2-aminopropanoic acid)sulfanyl]selanylpropanoic acid CROSSLNK Cysteinyl-selenocysteine (Cys-Sec) CROSSLNK Cysteinyl-selenocysteine (Sec-Cys) L-cysteinyl-L-selenocysteine PSI-MOD MOD:00867 Cross-link 2. L-cysteinyl-L-selenocysteine (Cys-Cys) A protein modification that effectively cross-links an L-cysteine residue and an L-cysteine converted to an L-selenocysteine residue to form L-cysteinyl-L-selenocystine. PubMed:10801974 PubMed:12911312 PubMed:17177418 RESID:AA0358#CYS (R,R)-2-amino-3-[3-(2-aminopropanoic acid)sulfanyl]selanylpropanoic acid CROSSLNK Cysteinyl-selenocysteine (Cys-Sec) CROSSLNK Cysteinyl-selenocysteine (Sec-Cys) L-cysteinyl-L-selenocysteine A protein modification that inserts or replaces a residue with a natural, non-standard encoded residue, such as N-formyl-L-methionine, L-selenocysteine, or L-pyrrolysine. X natural PSI-MOD MOD:00868 These are produced exclusively by modification of amino acids acylated to special tRNA before incorporation by ribosomes into proteins. For this reason, they have also been referred to as pre-translational modifications. natural, non-standard encoded residue A protein modification that inserts or replaces a residue with a natural, non-standard encoded residue, such as N-formyl-L-methionine, L-selenocysteine, or L-pyrrolysine. PubMed:18688235 A protein modification that effectively converts an L-aspartic acid residue to L-alanine. -44.01 C -1 H 0 N 0 O -2 -43.98983 C 3 H 5 N 1 O 1 71.08 71.03712 D natural uniprot.ptm:PTM-0314 (2S)-2-aminopropanoic acid 2-aminopropionic acid 2-azanylpropanoic acid Asp(Ala) L-alanine MOD_RES Beta-decarboxylated aspartate alpha-alanine alpha-aminopropionic acid PSI-MOD MOD:00869 This has been reported to occur by a natural process of beta-decarboxylation. L-alanine residue (Asp) A protein modification that effectively converts an L-aspartic acid residue to L-alanine. PubMed:17138938 RESID:AA0001#ASP (2S)-2-aminopropanoic acid 2-aminopropionic acid 2-azanylpropanoic acid Asp(Ala) L-alanine MOD_RES Beta-decarboxylated aspartate alpha-alanine alpha-aminopropionic acid A protein modification produced by formation of an adduct with phenyl isocyanate. 119.12 C 7 H 5 N 1 O 1 119.03712 X artifact N-term Unimod:411 PSI-MOD Phenylisocyanate phenyl isocyanate MOD:00870 From Unimod with no citation. phenyl isocyanate derivatized residue A protein modification produced by formation of an adduct with phenyl isocyanate. Unimod:411 Phenylisocyanate phenyl isocyanate A protein modification produced by formation of an adduct with (2)H5-phenyl isocyanate. 124.07 C 7 (2)H 5 N 1 O 1 124.0685 X artifact N-term Unimod:412 PSI-MOD Phenylisocyanate:2H(5) d5-phenyl isocyanate MOD:00871 From Unimod with no citation. (2)H5-phenyl isocyanate derivatized residue A protein modification produced by formation of an adduct with (2)H5-phenyl isocyanate. Unimod:412 Phenylisocyanate:2H(5) d5-phenyl isocyanate OBSOLETE because redundant and identical to MOD:01970. Remap to MOD:01970. MOD:01970 129.12 C 5 H 7 N 1 O 3 129.04259 C 10 H 14 N 2 O 6 258.23 258.08517 E natural Unimod:450 N alpha -(gamma-Glutamyl)-Glu PSI-MOD Glu monoglutamyl MOD:00872 L-isoglutamyl monoglutamic acid true OBSOLETE because redundant and identical to MOD:01970. Remap to MOD:01970. PubMed:10747868 PubMed:15525938 PubMed:1680872 RESID:AA0202#var Unimod:450 N alpha -(gamma-Glutamyl)-Glu Glu monoglutamyl A protein modification that effectively converts an L-glutamic acid residue to isoglutamyl glutamyl-glutamic acid, forming an isopeptide bond with a diglutamic acid. 258.23 C 10 H 14 N 2 O 6 258.08517 C 15 H 21 N 3 O 9 387.35 387.12778 E natural Unimod:451 PSI-MOD GluGlu diglutamyl MOD:00873 L-isoglutamyl diglutamic acid A protein modification that effectively converts an L-glutamic acid residue to isoglutamyl glutamyl-glutamic acid, forming an isopeptide bond with a diglutamic acid. DeltaMass:0 PubMed:10747868 PubMed:1680872 RESID:AA0202#var Unimod:451 GluGlu diglutamyl A protein modification that effectively converts an L-glutamic acid residue to isoglutamyl glutamyl-glutamyl-glutamic acid, forming an isopeptide bond with a triglutamic acid. 387.35 C 15 H 21 N 3 O 9 387.12778 C 20 H 28 N 4 O 12 516.46 516.17035 E natural Unimod:452 N alpha -(gamma-Glutamyl)-Glu3 PSI-MOD GluGluGlu triglutamyl MOD:00874 From DeltaMass: Average Mass: 388. L-isoglutamyl triglutamic acid A protein modification that effectively converts an L-glutamic acid residue to isoglutamyl glutamyl-glutamyl-glutamic acid, forming an isopeptide bond with a triglutamic acid. DeltaMass:0 PubMed:10747868 PubMed:1680872 RESID:AA0202#var Unimod:452 N alpha -(gamma-Glutamyl)-Glu3 GluGluGlu triglutamyl A protein modification that effectively converts an L-glutamic acid residue to isoglutamyl glutamyl-glutamyl-glutamyl-glutamic acid, forming an isopeptide bond with a tetraglutamic acid. 516.46 C 20 H 28 N 4 O 12 516.17035 C 25 H 35 N 5 O 15 645.57 645.21295 E natural Unimod:453 PSI-MOD GluGluGluGlu tetraglutamyl MOD:00875 L-isoglutamyl tetraglutamic acid A protein modification that effectively converts an L-glutamic acid residue to isoglutamyl glutamyl-glutamyl-glutamyl-glutamic acid, forming an isopeptide bond with a tetraglutamic acid. PubMed:10747868 PubMed:1680872 RESID:AA0202#var Unimod:453 GluGluGluGlu tetraglutamyl A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a hexosamine sugar group through a glycosidic bond. 161.16 C 6 H 11 N 1 O 4 161.0688 X natural Unimod:454 Hexosamines (GalN, GlcN) PSI-MOD HexN Hexosamine MOD:00876 hexosaminylated residue A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a hexosamine sugar group through a glycosidic bond. Unimod:454 Hexosamines (GalN, GlcN) HexN Hexosamine dimethyl pimelimidate modification from Unimod 154.21 C 8 H 14 N 2 O 1 154.11061 X artifact Unimod:455 PSI-MOD One end of crosslink attached, one end free Xlink:DMP-s MOD:00877 imidoester crosslink dimethyl pimelimidate singly attached dimethyl pimelimidate modification from Unimod URL:http://www.piercenet.com/files/0668ss5.pdf Unimod:455 One end of crosslink attached, one end free Xlink:DMP-s dimethyl pimelimidate modification from Unimod - Mechanism of the reaction of imidoesters with amines 122.17 C 7 H 10 N 2 122.0844 X artifact Unimod:456 PSI-MOD Both ends of crosslink attached to same peptide Xlink:DMP MOD:00878 imidoester crosslink dimethyl pimelimidate doubly attached dimethyl pimelimidate modification from Unimod - Mechanism of the reaction of imidoesters with amines PubMed:7171546 URL:http://dx.doi.org/10.1021/ja00877a017 Unimod:456 Both ends of crosslink attached to same peptide Xlink:DMP modification from Unimod 175.19 C 13 H 5 N 1 175.0422 X artifact Unimod:457 PSI-MOD NDA naphthalene-2,3-dicarboxaldehyde MOD:00879 naphthalene-2,3-dicarboxaldehyde modification from Unimod PubMed:2081203 Unimod:457 NDA naphthalene-2,3-dicarboxaldehyde A protein modification produced by formation of an adduct with 6x(13)C labeled 4-sulfophenyl isothiocyanate. 220.99 (12)C 1 (13)C 6 H 5 N 1 O 3 S 2 220.99121 X artifact Unimod:464 PSI-MOD 4-sulfophenyl isothiocyanate (Heavy C13) SPITC:13C(6) MOD:00880 6x(13)C labeled 4-sulfophenyl isothiocyanate derivatized residue A protein modification produced by formation of an adduct with 6x(13)C labeled 4-sulfophenyl isothiocyanate. PubMed:15536630 PubMed:16526082 Unimod:464 4-sulfophenyl isothiocyanate (Heavy C13) SPITC:13C(6) OBSOLETE because Unimod entry 465 megerd with 199. Remap to MOD:00552 DiMethyl-CH2D. MOD:00552 32.06 C 2 (2)H 4 32.056408 X artifact Unimod:465 PSI-MOD MOD:00881 N-reductive amination-D true OBSOLETE because Unimod entry 465 megerd with 199. Remap to MOD:00552 DiMethyl-CH2D. PubMed:9252331 Unimod:465 A protein modification that effectively converts an L-serine residue to S-(2-aminoethyl)cysteine. 59.13 C 2 H 5 N 1 O -1 S 1 59.019356 C 5 H 10 N 2 O 1 S 1 146.21 146.05139 S artifact Unimod:472 Aminoethyl Cysteinyl (AECys) PSI-MOD AEC-MAEC aminoethylcysteine MOD:00882 From DeltaMass: Average Mass: 146 Abbreviation:-AECys_ Formula:C5H10O2N1S1 Monoisotopic Mass Change:146.051 Average Mass Change:146.214 References:PE Sciex. S-(2-aminoethyl)cysteine (Ser) A protein modification that effectively converts an L-serine residue to S-(2-aminoethyl)cysteine. DeltaMass:171 PubMed:12923550 Unimod:472#S Aminoethyl Cysteinyl (AECys) AEC-MAEC aminoethylcysteine A protein modification that effectively replaces a 1-carboxyl group (usually referred to as the alpha-carboxyl) with a carboxamido group. -0.98 C 0 H 1 N 1 O -1 -0.984016 X natural C-term Unimod:2 Amide formation (C terminus) ResN alpha-amidated residue ctermamide PSI-MOD Amidated Amidation MOD:00883 The normal biological process involves formation of an amide of an amino acid residue in a peptide sequence where it is followed by a glycine and two basic residues, either arginine or lysine, although in some taxa only one basic residue is required. The peptide is cleaved after the basic residues, glycine is oxidized to hydroxyglycine, which decomposes to release a carboxamide C-terminal [JSG]. C1-amidated residue A protein modification that effectively replaces a 1-carboxyl group (usually referred to as the alpha-carboxyl) with a carboxamido group. DeltaMass:0 OMSSA:25 Unimod:2 Amide formation (C terminus) ResN alpha-amidated residue ctermamide Amidated Amidation A protein modification that effectively converts an L-cysteine residue to S-2-aminoethylcysteine. 43.07 C 2 H 5 N 1 O 0 S 0 43.0422 C 5 H 10 N 2 O 1 S 1 146.21 146.05139 C artifact 4-thialysine L-cysteine aziridine adduct S-(2-aminoethyl)-L-cysteine PSI-MOD MOD:00884 This modified residue is a chemical isolog of L-lysine for trypsin hydolysis produced from L-cysteine by aziridine. S-aminoethylcysteine (Cys) A protein modification that effectively converts an L-cysteine residue to S-2-aminoethylcysteine. PubMed:1175632 PubMed:18688235 4-thialysine L-cysteine aziridine adduct S-(2-aminoethyl)-L-cysteine A protein modification that crosslinks two residues by formation of an ester bond. PSI-MOD MOD:00885 ester crosslinked residues A protein modification that crosslinks two residues by formation of an ester bond. PubMed:18688235 A protein modification that effectively converts an L-tryptophan residue to 6'-chloro-L-tryptophan. 34.44 C 0 Cl 1 H -1 N 0 O 0 33.96103 C 11 Cl 1 H 9 N 2 O 1 220.66 220.04034 W natural Unimod:936 uniprot.ptm:PTM-0052 (2S)-2-amino-3-(6-chloro-1H-indol-3-yl)propanoic acid 6'-ClTrp 6'-chloro-L-tryptophan MOD_RES 6'-chlorotryptophan PSI-MOD MOD:00886 The Unimod:340 cross-reference to RESID:AA0180 is incorrect. RESID:AA0180 should be cross-referenced by Unimod:936 [JSG]. 6'-chloro-L-tryptophan A protein modification that effectively converts an L-tryptophan residue to 6'-chloro-L-tryptophan. PubMed:9033387 RESID:AA0180 Unimod:936#W (2S)-2-amino-3-(6-chloro-1H-indol-3-yl)propanoic acid 6'-ClTrp 6'-chloro-L-tryptophan MOD_RES 6'-chlorotryptophan A protein modification that effectively converts an L-aspartic acid residue to a methylated aspartic acid, such as aspartic acid 4-methyl ester. PSI-MOD MOD:00887 methylated aspartic acid A protein modification that effectively converts an L-aspartic acid residue to a methylated aspartic acid, such as aspartic acid 4-methyl ester. PubMed:18688235 A protein modification that effectively converts an L-proline to an L-prolinium (protonated L-proline). 1.01 C 0 H 1 N 0 O 0 1.007276 1+ C 5 H 9 N 1 O 1 99.13 99.06786 P natural N-term PSI-MOD MOD:00888 protonated L-proline (L-prolinium) residue A protein modification that effectively converts an L-proline to an L-prolinium (protonated L-proline). PubMed:18688235 A protein modification that effectively converts an L-prolinium (charged L-proline) residue to N,N-dimethyl-L-proline. 28.05 C 2 H 4 N 0 O 0 28.030752 1+ C 7 H 13 N 1 O 1 127.19 127.09917 MOD:00888 natural N-term Unimod:36 PSI-MOD MOD:00889 N,N-dimethyl-L-proline (from L-prolinium) A protein modification that effectively converts an L-prolinium (charged L-proline) residue to N,N-dimethyl-L-proline. Unimod:36#P A protein modification that effectively converts an L-histidine residue to a phosphorylated L-histidine, such as pros-phosphohistidine, or tele-phosphohistidine. 79.98 C 0 H 1 N 0 O 3 P 1 79.96633 C 6 H 8 N 3 O 4 P 1 217.12 217.02524 H natural Unimod:21 uniprot.ptm:PTM-0252 NPhosHis mod192 phosphohistidine PSI-MOD Phospho MOD:00890 phosphorylated L-histidine A protein modification that effectively converts an L-histidine residue to a phosphorylated L-histidine, such as pros-phosphohistidine, or tele-phosphohistidine. OMSSA:192 Unimod:21#H NPhosHis mod192 phosphohistidine Phospho A protein modification that effectively converts a source amino acid residue to D-serine. C 3 H 5 N 1 O 2 87.08 87.03203 X natural (R)-2-amino-3-hydroxypropanoic acid D-Ser D-serine PSI-MOD MOD:00891 D-serine A protein modification that effectively converts a source amino acid residue to D-serine. ChEBI:29998 PubMed:6893271 PubMed:7973665 RESID:AA0195 (R)-2-amino-3-hydroxypropanoic acid D-Ser D-serine A protein modification that effectively converts an L-cysteine residue to D-serine. -16.06 C 0 H 0 N 0 O 1 S -1 -15.977156 C 3 H 5 N 1 O 2 87.08 87.03203 C natural uniprot.ptm:PTM-0309 (R)-2-amino-3-hydroxypropanoic acid D-serine MOD_RES D-serine (Cys) PSI-MOD MOD:00892 D-serine (Cys) A protein modification that effectively converts an L-cysteine residue to D-serine. PubMed:18025465 PubMed:6893271 RESID:AA0195#CYS (R)-2-amino-3-hydroxypropanoic acid D-serine MOD_RES D-serine (Cys) Natural or modified residues with a mass of 128.0-128.1 Da. PSI-MOD MOD:00893 residues isobaric at 128.0-128.1 Natural or modified residues with a mass of 128.0-128.1 Da. PubMed:18688235 Natural or modified resiues with a mass of 128.058578 Da. PSI-MOD MOD:00894 residues isobaric at 128.058578 Da Natural or modified resiues with a mass of 128.058578 Da. PubMed:18688235 A protein modification that effectively results from forming an adduct with a compound containing a flavin adenine dinucleotide (FAD) group. 783.54 C 27 H 31 N 9 O 15 P 2 783.1415 X natural FADRes PSI-MOD MOD:00895 FAD modified residue A protein modification that effectively results from forming an adduct with a compound containing a flavin adenine dinucleotide (FAD) group. PubMed:18688235 FADRes A protein modification that effectively results from forming an adduct with a compound containing a riboflavin phosphate (flavin mononucleotide, FMN) group. X natural FMNRes PSI-MOD MOD:00896 FMN modified residue A protein modification that effectively results from forming an adduct with a compound containing a riboflavin phosphate (flavin mononucleotide, FMN) group. PubMed:18688235 FMNRes A protein modification that effectively converts an L-cysteine residue to N-acetyl-S-archeol-L-cysteine. 677.2 C 45 H 88 N 0 O 3 S 0 676.67334 C 48 H 93 N 1 O 4 S 1 780.34 779.68256 C natural N-term PSI-MOD MOD:00897 N-acetyl-S-archeol-cysteine A protein modification that effectively converts an L-cysteine residue to N-acetyl-S-archeol-L-cysteine. RESID:AA0043#var RESID:AA0223#var A protein modification that effectively converts an L-cysteine residue to S-(sn-1-2-oleoyl-3-palmitoyl-glycerol)cysteine. 576.95 C 37 H 68 N 0 O 4 S 0 576.5118 C 40 H 73 N 1 O 5 S 1 680.09 679.52094 C natural Unimod:377 PSI-MOD Diacylglycerol diacylglycerol MOD:00898 Incidental to RESID:AA0060. S-(sn-1-2-oleoyl-3-palmitoyl-glycerol)cysteine A protein modification that effectively converts an L-cysteine residue to S-(sn-1-2-oleoyl-3-palmitoyl-glycerol)cysteine. PubMed:10896212 PubMed:4575979 PubMed:9056182 RESID:AA0107#var Unimod:377 Diacylglycerol diacylglycerol A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-S-diacylglycerol-L-cysteine. C natural N-term PSI-MOD MOD:00899 N-palmitoyl-S-diacylglycerol-L-cysteine A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-S-diacylglycerol-L-cysteine. RESID:AA0069#var RESID:AA0107#var A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-S-(sn-1-2-oleoyl-3-palmitoyl-glycerol)cysteine. 815.36 C 53 H 98 N 0 O 5 S 0 814.74146 C 56 H 103 N 1 O 6 S 1 918.5 917.7506 C natural N-term (R)-2-hexadecanoylamino-3-[(S)-2-((Z)-9-octadecenoyloxy)-3-(hexadecanoyloxy)propyl]sulfanylpropanoic acid 2-hexadecanoylamino-3-[(S)-2-((Z)-9-octadecenoyloxy)-3-(hexadecanoyloxy)propyl]thiopropanoic acid PSI-MOD MOD:00900 N-palmitoyl-S-(sn-1-2-oleoyl-3-palmitoyl-glycerol)cysteine A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-S-(sn-1-2-oleoyl-3-palmitoyl-glycerol)cysteine. PubMed:18688235 (R)-2-hexadecanoylamino-3-[(S)-2-((Z)-9-octadecenoyloxy)-3-(hexadecanoyloxy)propyl]sulfanylpropanoic acid 2-hexadecanoylamino-3-[(S)-2-((Z)-9-octadecenoyloxy)-3-(hexadecanoyloxy)propyl]thiopropanoic acid A protein modification that modifies an L-alanine. A ModAla PSI-MOD MOD:00901 modified L-alanine residue A protein modification that modifies an L-alanine. PubMed:18688235 ModAla A protein modification that modifies an L-arginine residue. R ModArg PSI-MOD MOD:00902 modified L-arginine residue A protein modification that modifies an L-arginine residue. PubMed:18688235 ModArg A protein modification that modifies an L-asparagine residue. N ModAsn PSI-MOD MOD:00903 modified L-asparagine residue A protein modification that modifies an L-asparagine residue. PubMed:18688235 ModAsn A protein modification that modifies an L-aspartic acid residue. D ModAsp PSI-MOD MOD:00904 modified L-aspartic acid residue A protein modification that modifies an L-aspartic acid residue. PubMed:18688235 ModAsp A protein modification that modifies an L-cysteine residue. C ModCys PSI-MOD MOD:00905 modified L-cysteine residue A protein modification that modifies an L-cysteine residue. PubMed:18688235 ModCys A protein modification that modifies an L-glutamic acid residue. E ModGlu PSI-MOD MOD:00906 modified L-glutamic acid residue A protein modification that modifies an L-glutamic acid residue. PubMed:18688235 ModGlu A protein modification that modifies an L-glutamine residue. Q ModGln PSI-MOD MOD:00907 modified L-glutamine residue A protein modification that modifies an L-glutamine residue. PubMed:18688235 ModGln A protein modification that modifies a glycine residue. G ModGly PSI-MOD MOD:00908 modified glycine residue A protein modification that modifies a glycine residue. PubMed:18688235 ModGly A protein modification that modifies an L-histidine residue. H ModHis PSI-MOD MOD:00909 modified L-histidine residue A protein modification that modifies an L-histidine residue. PubMed:18688235 ModHis A protein modification that modifies an L-isoleucine residue. I ModIle PSI-MOD MOD:00910 modified L-isoleucine residue A protein modification that modifies an L-isoleucine residue. PubMed:18688235 ModIle A protein modification that modifies an L-leucine residue. L ModLeu PSI-MOD MOD:00911 modified L-leucine residue A protein modification that modifies an L-leucine residue. PubMed:18688235 ModLeu A protein modification that modifies an L-lysine residue. K ModLys PSI-MOD MOD:00912 modified L-lysine residue A protein modification that modifies an L-lysine residue. PubMed:18688235 ModLys A protein modification that modifies an L-methionine residue. M ModMet PSI-MOD MOD:00913 modified L-methionine residue A protein modification that modifies an L-methionine residue. PubMed:18688235 ModMet A protein modification that modifies an L-phenylalanine residue. F ModPhe PSI-MOD MOD:00914 modified L-phenylalanine residue A protein modification that modifies an L-phenylalanine residue. PubMed:18688235 ModPhe A protein modification that modifies an L-proline residue. P ModPro PSI-MOD MOD:00915 modified L-proline residue A protein modification that modifies an L-proline residue. PubMed:18688235 ModPro A protein modification that modifies an L-serine residue. S ModSer PSI-MOD MOD:00916 modified L-serine residue A protein modification that modifies an L-serine residue. PubMed:18688235 ModSer A protein modification that modifies an L-threonine residue. T ModThr PSI-MOD MOD:00917 modified L-threonine residue A protein modification that modifies an L-threonine residue. PubMed:18688235 ModThr A protein modification that modifies an L-tryptophan residue. W ModTrp PSI-MOD MOD:00918 modified L-tryptophan residue A protein modification that modifies an L-tryptophan residue. PubMed:18688235 ModTrp A protein modification that modifies an L-tyrosine residue. Y ModTyr PSI-MOD MOD:00919 modified L-tyrosine residue A protein modification that modifies an L-tyrosine residue. PubMed:18688235 ModTyr A protein modification that modifies an L-valine residue. V ModVal PSI-MOD MOD:00920 modified L-valine residue A protein modification that modifies an L-valine residue. PubMed:18688235 ModVal New uncategorized Unimod. OBSOLETE because organizational use is no longer required. PSI-MOD MOD:00921 new uncategorized Unimod entries true New uncategorized Unimod. OBSOLETE because organizational use is no longer required. PubMed:18688235 modification from Unimod Chemical derivative 672.84 C 37 H 44 N 4 O 6 S 1 672.29816 C 40 H 49 N 5 O 7 S 2 775.98 775.3073 C artifact Unimod:494 PSI-MOD Cy3 CyDye DIGE Fluor saturation dye CyDye-Cy3 MOD:00922 Cy3 CyDye DIGE Fluor saturation dye modification from Unimod Chemical derivative Unimod:494 Cy3 CyDye DIGE Fluor saturation dye CyDye-Cy3 modification from Unimod Chemical derivative 684.85 C 38 H 44 N 4 O 6 S 1 684.29816 C 41 H 49 N 5 O 7 S 2 787.99 787.3073 C artifact Unimod:495 PSI-MOD Cy5 CyDye DIGE Fluor saturation dye CyDye-Cy5 MOD:00923 Cy5 CyDye DIGE Fluor saturation dye modification from Unimod Chemical derivative Unimod:495 Cy5 CyDye DIGE Fluor saturation dye CyDye-Cy5 A protein modification that effectively crosslinks an L-lysine residue and an L-threonine residue by an isopeptide bond to form N6-(L-threonyl)-L-lysine. -18.02 C 0 H -2 N 0 O -1 -18.010565 C 10 H 18 N 3 O 3 228.27 228.13481 K, T natural C-term uniprot.ptm:PTM-0326 (2S)-2-amino-6-([(2S,3R)-2-amino-3-hydroxybutanoyl]amino)hexanoic acid N6-(L-threonyl)-L-lysine N6-threonyl-lysine PSI-MOD MOD:00924 Cross-link 2. N6-(L-threonyl)-L-lysine A protein modification that effectively crosslinks an L-lysine residue and an L-threonine residue by an isopeptide bond to form N6-(L-threonyl)-L-lysine. PubMed:18063774 RESID:AA0440 (2S)-2-amino-6-([(2S,3R)-2-amino-3-hydroxybutanoyl]amino)hexanoic acid N6-(L-threonyl)-L-lysine N6-threonyl-lysine A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a heptose sugar group through a glycosidic bond. 192.17 C 7 H 12 O 6 192.06339 X natural Unimod:490 PSI-MOD Hep Heptose MOD:00925 From Unimod with no citation [JSG]. heptosylated residue A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a heptose sugar group through a glycosidic bond. Unimod:490 Hep Heptose Modification from Unimod Non-standard residue. OBSOLETE because not an amino acid modification. From Unimod not an approved entry. 340.42 C 21 H 24 O 4 340.16745 X artifact Unimod:493 PSI-MOD BADGE Bisphenol A diglycidyl ether derivative MOD:00926 Bisphenol A diglycidyl ether derivative true Modification from Unimod Non-standard residue. OBSOLETE because not an amino acid modification. From Unimod not an approved entry. PubMed:11225353 Unimod:493 BADGE Bisphenol A diglycidyl ether derivative A protein modification that effectively replaces two hydrogen atoms of a residue containing common isotopes with two (13)C,3x(2)H labeled methyl groups to form a 2x(13)C,6x(2)H labeled dimethylated residue. 34.06 (13)C 2 (2)H 4 34.063118 X artifact Unimod:510 PSI-MOD DiMethyl-C13HD2 Dimethyl:2H(4)13C(2) MOD:00927 2x(13)C,4x(2)H labeled dimethylated residue A protein modification that effectively replaces two hydrogen atoms of a residue containing common isotopes with two (13)C,3x(2)H labeled methyl groups to form a 2x(13)C,6x(2)H labeled dimethylated residue. PubMed:16335955 PubMed:3802193 Unimod:510 DiMethyl-C13HD2 Dimethyl:2H(4)13C(2) modification from Unimod Chemical derivative 227.39 C 14 H 29 N 1 O 1 227.22491 X artifact Unimod:513 PSI-MOD C8-QAT [3-(2,5)-Dioxopyrrolidin-1-yloxycarbonyl)-propyl]dimethyloctylammonium MOD:00928 Should have children for K and X-N-term [JSG]. [3-(2,5)-dioxopyrrolidin-1-yloxycarbonyl)-propyl]dimethyloctylammonium modification from Unimod Chemical derivative PubMed:16771548 Unimod:513 C8-QAT [3-(2,5)-Dioxopyrrolidin-1-yloxycarbonyl)-propyl]dimethyloctylammonium A modification produced in a non-enzymatic reaction between a lactose carbonyl group and an L-lysine to form a Schiff-base or an Amadori ketosamine lysine adduct. 342.3 C 12 H 22 O 11 342.1162 C 18 H 34 N 2 O 12 470.47 470.21118 K natural Unimod:512 uniprot.ptm:PTM-0511 CARBOHYD N-linked (Lac) (glycation) lysine PSI-MOD Hex(2) Lactosylation MOD:00929 The term lactosylation used with this meaning is a misnomer [JSG]. lactose glycated lysine A modification produced in a non-enzymatic reaction between a lactose carbonyl group and an L-lysine to form a Schiff-base or an Amadori ketosamine lysine adduct. PubMed:9606156 Unimod:512 CARBOHYD N-linked (Lac) (glycation) lysine Hex(2) Lactosylation tyrosine adduct with substrate analog inhibitor 1,2-dideoxy-2'-methyl-alpha-D-glucopyranoso-[2,1-d]-Delta2'-thiazoline. 232.27 C 9 H 14 N 1 O 4 S 1 232.06436 C 18 H 23 N 2 O 6 S 1 395.45 395.1277 Y artifact Unimod:514 PSI-MOD MOD:00930 propyl-NAG tyrosine adduct tyrosine adduct with substrate analog inhibitor 1,2-dideoxy-2'-methyl-alpha-D-glucopyranoso-[2,1-d]-Delta2'-thiazoline. PubMed:15795231 Unimod:514 modification from Unimod Other - BHTOH is formed upon metabolism of BHT with P450 enzymes. The BHTOH is further metabolized to its quinone methide (electrophile) which reacts with -SH and -NH2 groups 234.34 C 15 H 22 O 2 234.16199 X artifact Unimod:498 PSI-MOD BHTOH Michael addition of t-butyl hydroxylated BHT (BHTOH) to C, H or K MOD:00931 Michael addition of t-butyl hydroxylated BHT (BHTOH) to C, H or K modification from Unimod Other - BHTOH is formed upon metabolism of BHT with P450 enzymes. The BHTOH is further metabolized to its quinone methide (electrophile) which reacts with -SH and -NH2 groups PubMed:11085420 Unimod:498 BHTOH Michael addition of t-butyl hydroxylated BHT (BHTOH) to C, H or K modification from Unimod Isotopic label 298.02 Br 1 (12)C 10 (13)C 2 H 13 N 2 O 2 298.02274 Br 1 (12)C 13 (13)C 2 H 18 N 3 O 3 S 1 401.03 401.03192 C artifact Unimod:499 PSI-MOD Heavy IDBEST tag for quantitation IGBP:13C(2) MOD:00932 IDBEST tag for quantitation modification from Unimod Isotopic label PubMed:11821862 Unimod:499 Heavy IDBEST tag for quantitation IGBP:13C(2) modification from Unimod Chemical derivative - 5-hydro-5-methylimidazol-4-one, arginine methylglyoxal arginine adduct (+54 amu) 54.05 C 3 H 2 O 1 54.010567 C 9 H 14 N 4 O 2 210.24 210.11168 R artifact Unimod:319 PSI-MOD Delta:H(2)C(3)O(1) MDA adduct +54 MOD:00933 Ref. Uchida K, Sakai K, Itakura K, Osawa T, Toyokuni S. 1977. Protein modification by lipid peroxidation products: formation of malondialdehyde-derived N(epsilon)-(2-propenol)lysine in proteins. Arch Biochem Biophys. 346(1):45-52. methylglyoxal arginine adduct (+54 amu) modification from Unimod Chemical derivative - 5-hydro-5-methylimidazol-4-one, arginine methylglyoxal arginine adduct (+54 amu) Unimod:319#R Delta:H(2)C(3)O(1) MDA adduct +54 modification from Unimod Post-translational 306.4 C 19 H 26 N -2 O 5 306.17188 C 25 H 38 N 2 O 6 462.59 462.27298 R natural Unimod:506 PSI-MOD LG-Hlactam-R Levuglandinyl - arginine hydroxylactam adduct MOD:00934 Levuglandinyl - arginine hydroxylactam adduct modification from Unimod Post-translational Unimod:506 LG-Hlactam-R Levuglandinyl - arginine hydroxylactam adduct Oxidation of methionine to methionine sulfoxide with neutral loss of CH3SOH. -64.1 C -1 H -4 N 0 O -1 S -1 -63.998287 C 4 H 5 N 1 O 1 S 0 83.09 83.03712 M artifact PSI-MOD MOD:00935 Originally created from Unimod:507 that was later deleted. methionine oxidation with neutral loss of 64 Da Oxidation of methionine to methionine sulfoxide with neutral loss of CH3SOH. PubMed:18688235 PubMed:9004526 modification from Unimod Post-translational 348.44 C 20 H 28 O 5 348.19366 X artifact Unimod:504 PSI-MOD LG-Hlactam-K Levuglandinyl - lysine hydroxylactam adduct MOD:00936 Levuglandinyl - hydroxylactam adduct, K and N-term modification from Unimod Post-translational Unimod:504 LG-Hlactam-K Levuglandinyl - lysine hydroxylactam adduct modification from Unimod Post-translational 290.4 C 19 H 26 N -2 O 4 290.17697 C 25 H 38 N 2 O 5 446.59 446.27808 R artifact Unimod:505 PSI-MOD LG-lactam-R Levuglandinyl - arginine lactam adduct MOD:00937 Levuglandinyl - arginine lactam adduct modification from Unimod Post-translational Unimod:505 LG-lactam-R Levuglandinyl - arginine lactam adduct modification from Unimod Post-translational 332.44 C 20 H 28 O 4 332.19876 X artifact Unimod:503 PSI-MOD LG-lactam-K Levuglandinyl - lysine lactam adduct MOD:00938 Levuglandinyl - lactam adduct, K and N-term modification from Unimod Post-translational PubMed:12590383 Unimod:503 LG-lactam-K Levuglandinyl - lysine lactam adduct modification from Unimod Chemical derivative 129.12 C 5 H 7 N 1 O 3 129.04259 C 8 H 12 N 2 O 4 S 1 232.25 232.05177 C artifact Unimod:500 PSI-MOD Nmethylmaleimide+water Nmethylmaleimidehydrolysis MOD:00939 hydrolyzed N-methylmaleimide cysteine adduct modification from Unimod Chemical derivative Unimod:500 Nmethylmaleimide+water Nmethylmaleimidehydrolysis A protein modification produced by formation of an adduct with 3-methyl-2-pyridyl isocyanate. 134.14 C 7 H 6 N 2 O 1 134.04802 X artifact N-term Unimod:501 PSI-MOD 3-methyl-2-pyridyl isocyanate PyMIC MOD:00940 3-methyl-2-pyridyl isocyanate derivatized residue A protein modification produced by formation of an adduct with 3-methyl-2-pyridyl isocyanate. PubMed:11078590 Unimod:501 3-methyl-2-pyridyl isocyanate PyMIC modification from Unimod Chemical derivative 118.16 C 8 H 8 N 1 118.065674 C 11 H 13 N 2 S 1 205.3 205.07994 C artifact Unimod:488 PSI-MOD DHP Dehydropyrrolizidine alkaloid (dehydroretronecine) on cysteines MOD:00941 dehydropyrrolizidine alkaloid (dehydroretronecine) derivatized cysteine modification from Unimod Chemical derivative PubMed:12175151 Unimod:488 DHP Dehydropyrrolizidine alkaloid (dehydroretronecine) on cysteines A protein modification that effectively substitutes four (1)H protium atoms with four (2)H deuterium atoms to produce (4,4,5,5-(2)H4)-L-lysine. 4.03 (1)H -4 (2)H 4 4.025107 C 6 (1)H 8 (2)H 4 N 2 O 1 132.12 132.12007 K artifact Unimod:481 4,4,5,5-tetradeuterolysine lys-2H4 PSI-MOD 4,4,5,5-D4 Lysine Label:2H(4) MOD:00942 For SILAC experiments. (4,4,5,5-(2)H4)-L-lysine A protein modification that effectively substitutes four (1)H protium atoms with four (2)H deuterium atoms to produce (4,4,5,5-(2)H4)-L-lysine. OMSSA:180 Unimod:481 4,4,5,5-tetradeuterolysine lys-2H4 4,4,5,5-D4 Lysine Label:2H(4) modification from Unimod Isotopic label 128.19 C 7 H 14 N 1 O 1 128.10754 X artifact Unimod:476 PSI-MOD 4-trimethyllammoniumbutyryl- TMAB MOD:00943 4-trimethylammoniumbutanoyl derivatized residue modification from Unimod Isotopic label PubMed:12643539 Unimod:476 4-trimethyllammoniumbutyryl- TMAB modification from Unimod Isotopic label 137.16 C 7 (1)H 5 (2)H 9 N 1 O 1 137.16403 X artifact Unimod:477 PSI-MOD TMAB:2H(9) d9-4-trimethyllammoniumbutyryl- MOD:00944 d9-4-trimethylammoniumbutanoyl derivatized residue modification from Unimod Isotopic label Unimod:477 TMAB:2H(9) d9-4-trimethyllammoniumbutyryl- OBSOLETE because redundant and identical to MOD:00626. Remap to MOD:00626. MOD:00626 421.43 C 21 H 15 N 3 O 5 S 1 421.07324 S artifact PSI-MOD MOD:00945 fluorescein-5-thiosemicarbazide adduct true OBSOLETE because redundant and identical to MOD:00626. Remap to MOD:00626. PubMed:18688235 A protein modification that crosslinks two residues with a covalent bond and the loss of ammonia. PSI-MOD MOD:00946 crosslinked residues with loss of ammonia A protein modification that crosslinks two residues with a covalent bond and the loss of ammonia. PubMed:18688235 Entries from DeltaMass see http://www.abrf.org/index.cfm/dm.home?AvgMass=all. PSI-MOD MOD:00947 DeltaMass Entries from DeltaMass see http://www.abrf.org/index.cfm/dm.home?AvgMass=all. PubMed:18688235 OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass X PSI-MOD MOD:00948 From DeltaMass: Average Mass: -79 5'-dephospho true OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass DeltaMass:0 OBSOLETE because redundant and identical to MOD:01933. Remap to MOD:01933. MOD:01933 K PSI-MOD MOD:00949 From DeltaMass: Average Mass: -58 desmosine true OBSOLETE because redundant and identical to MOD:01933. Remap to MOD:01933. DeltaMass:0 OBSOLETE because this modification has not been seen/reported on since this original publication in 1994 and carboxymethylation of proteins is common enough for this mass shift to have been seen in the intervening 25+ years. modification from DeltaMass M PSI-MOD MOD:00950 From DeltaMass: Average Mass: -48 Average Mass Change:-48 References:Anal. Biochem. Vol 216 No.1 p141 decomposed carboxymethylated methionine true OBSOLETE because this modification has not been seen/reported on since this original publication in 1994 and carboxymethylation of proteins is common enough for this mass shift to have been seen in the intervening 25+ years. modification from DeltaMass DeltaMass:3 Covalent modification of a peptide or protein L-glutamic acid residue to gamma-carboxyglutamic acid with secondary loss of a neutral carbon dioxide molecular fragment. -44.01 C -1 H 0 N 0 O -2 -43.98983 C 5 H 7 N 1 O 3 129.12 129.04259 E artifact d4CbxGlu PSI-MOD MOD:00951 From DeltaMass: Average Mass: -44 Formula:CO2 Average Mass Change:-44 References:Nakamura T, Yu Z, Fainzilber M, Burlingame AL. Protein Sci (1996) 5, 524-530 Mass spectrometric-based revision of the structure of a cysteine-rich peptide toxin with gamma-carboxyglutamic acid, TxVIIA, from the sea snail, Conus textile. Notes: The elimination of CO2 will regenerate glutamate as if there was no modification. However, peaks appearing with an interval of 44 is quite characteristic. It would be noteworthy to remind that loss of 44 from a gamma-carboxyglutamate-containing peptide may be observed not only as a result of spontaneous decarboxylation but also as an artifact under some ionization conditions such as negative ion mode MALDI. L-gamma-carboxyglutamic acid with neutral loss of carbon dioxide Covalent modification of a peptide or protein L-glutamic acid residue to gamma-carboxyglutamic acid with secondary loss of a neutral carbon dioxide molecular fragment. DeltaMass:58 d4CbxGlu A protein modification that crosslinks an aspartic acid and the following glycine residue with the formation of (2-aminosuccinimidyl)acetic acid and the loss of a water molecule. -18.02 C 0 H -2 N 0 O -1 -18.010565 C 6 H 6 N 2 O 3 154.13 154.03784 D, G hypothetical uniprot.ptm:PTM-0312 (2-aminosuccinimidyl)acetic acid (3-amino-2,5-dioxo-1-pyrrolidinyl)acetic acid CROSSLNK (2-aminosuccinimidyl)acetic acid (Asp-Gly) N-(2-aminosuccinyl)glycine [(3S)-3-amino-2,5-dioxopyrrolidin-1-yl]acetic acid anhydroaspartyl glycine aspartimide glycine PSI-MOD MOD:00952 Cross-link 2; this cross-link is formed by the condensation of an aspartic acid residue with the alpha-amido of the following residue. (2-aminosuccinimidyl)acetic acid (Asp) A protein modification that crosslinks an aspartic acid and the following glycine residue with the formation of (2-aminosuccinimidyl)acetic acid and the loss of a water molecule. PubMed:10801322 RESID:AA0441#ASP (2-aminosuccinimidyl)acetic acid (3-amino-2,5-dioxo-1-pyrrolidinyl)acetic acid CROSSLNK (2-aminosuccinimidyl)acetic acid (Asp-Gly) N-(2-aminosuccinyl)glycine [(3S)-3-amino-2,5-dioxopyrrolidin-1-yl]acetic acid anhydroaspartyl glycine aspartimide glycine A protein modification that effectively crosslinks an L-glutamic acid residue and an L-serine residue by an ester bond and releasing water to form O-(L-isoglutamyl)-L-serine. -18.02 C 0 H -2 N 0 O -1 -18.010565 C 8 H 10 N 2 O 4 198.18 198.06406 E, S artifact (2S)-2-amino-5-[(2S)-2-amino-2-carboxyethoxy]-5-oxopentanoic acid CROSSLNK isoglutamyl serine ester (Ser-Glu) O(beta)-(gamma-glutamyl)serine O-(L-isoglutamyl)-L-serine O-gamma-Glutamyl- (Crosslink to Serine) O3-(isoglutamyl)-serine PSI-MOD MOD:00953 Cross-link 2; From DeltaMass: with no citation. O-(L-isoglutamyl)-L-serine (Glu-Ser) A protein modification that effectively crosslinks an L-glutamic acid residue and an L-serine residue by an ester bond and releasing water to form O-(L-isoglutamyl)-L-serine. DeltaMass:0 PubMed:19035375 RESID:AA0597#ESX (2S)-2-amino-5-[(2S)-2-amino-2-carboxyethoxy]-5-oxopentanoic acid CROSSLNK isoglutamyl serine ester (Ser-Glu) O(beta)-(gamma-glutamyl)serine O-(L-isoglutamyl)-L-serine O-gamma-Glutamyl- (Crosslink to Serine) O3-(isoglutamyl)-serine A protein modification that crosslinks two residues with a covalent bond and the loss of water. PSI-MOD MOD:00954 crosslinked residues with loss of water A protein modification that crosslinks two residues with a covalent bond and the loss of water. PubMed:18688235 A protein modification that effectively crosslinks an L-serine residue and an L-histidine residue to release water and form tele- or pros-(2-amino-2-carboxyethyl)histidine. -18.02 C 0 H -2 N 0 O -1 -18.010565 C 9 H 10 N 4 O 2 206.2 206.08038 H, S artifact beta-alaninohistidine PSI-MOD MOD:00955 Cross-link 2; From DeltaMass with no citation or formula: Average Mass: -18. The DeltaMass description "Serine crosslinked to theta or pi carbon of Histidine" is incorrect. The histidine ring nitrogens (not carbons) are designated tele or N-tau (not theta), and pros or N-pi [JSG]. alaninohistidine (serine crosslinked to tele or pros nitrogen of histidine) A protein modification that effectively crosslinks an L-serine residue and an L-histidine residue to release water and form tele- or pros-(2-amino-2-carboxyethyl)histidine. DeltaMass:0 beta-alaninohistidine modification from DeltaMass -18.03 C 1 H 2 N 0 O 0 S -1 -17.95642 C 6 H 11 N 1 O 1 113.16 113.08406 M PSI-MOD MOD:00956 From DeltaMass: Average Mass: -18 Average Mass Change:-18 Notes: It has the same mass as leucine or isoleucine and can be charged on the methionyl t-RNA. This often happens in minimal media-prepared fermentations that are not supplemented with enough free methionine. It gives a mass change of -18 and can often be confused with dehydration. misincorporation of norleucine for methionine modification from DeltaMass DeltaMass:10 Covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid residue with a secondary loss of a neutral carbon dioxide molecular fragment. -44.01 C -1 H 0 N 0 O -2 -43.98983 X artifact dCO2ModRes PSI-MOD MOD:00957 modified residue with neutral loss of carbon dioxide Covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid residue with a secondary loss of a neutral carbon dioxide molecular fragment. PubMed:18688235 dCO2ModRes modification from DeltaMass H, R PSI-MOD MOD:00958 Cross-link 2; From DeltaMass: Average Mass: -5 crosslink between Arg and His sidechains modification from DeltaMass DeltaMass:0 modification from DeltaMass Y, Y, Y, Y PSI-MOD MOD:00959 Cross-link 4; From DeltaMass: Average Mass: -4 3,3',5,5'-TerTyr (Crosslink) modification from DeltaMass DeltaMass:0 A protein modification that effectively replaces a carboxylic acid group with a hydrogen atom. -44.01 C -1 H 0 N 0 O -2 -43.98983 X artifact PSI-MOD MOD:00960 decarboxylated residue A protein modification that effectively replaces a carboxylic acid group with a hydrogen atom. PubMed:18688235 A protein modification that effectively reduces the disulfide bond of cystine to form two cysteine residues. 2.02 C 0 H 2 N 0 O 0 S 0 2.01565 C 6 H 10 N 2 O 2 S 2 206.28 206.01837 MOD:00034 PSI-MOD MOD:00961 Cross-link 2; this modification destroys the cross-link. From DeltaMass: Treatment of cystine (cys-cys) by reducing agents such as dithiothreitol (DTT) or triscarboxyethylphosphine (TCEP) results in cleavage of the disulphide bond and reduction of the sulphur atom of each molecule to create cysteine. reduction of disulfide crosslink in cystine to two cysteines A protein modification that effectively reduces the disulfide bond of cystine to form two cysteine residues. DeltaMass:333 A protein modification that by reducing the indole ring system of tryptophan to indoline effectively converts an L-tryptophan residue to 2',3'-dihydrotryptophan. 2.02 C 0 H 2 N 0 O 0 S 0 2.01565 C 11 H 12 N 2 O 1 188.23 188.09496 W artifact PSI-MOD MOD:00962 From DeltaMass: References:1. Pearson,D.A., Blanchette,M., Baker,M.L. and Guindon,C.A. (1989) Trialkylsilanes as scavengers for the trifluoroacetic acid deblocking ofprotecting groups in peptide synthesis. Tetrahedron Lett., 30(21), 2739-2742 Notes: Reduction of indole double bond of Trp which occurs when triethylsilane (TES) is used as a scavenger and Trp is incorporated without protection of indole nitrogen [1]. This side reaction is likely to be accompanied by oxidation of indoline ring with formation of intensively colored peptide by-products. Triisopropylsilane (TIPS) does not give this side reaction. See structure at http://www.abrf.org/images/misc/dmass2.gif. [However, the pictured indoline structure is incorrect - JSG]. 2',3'-dihydrotryptophan A protein modification that by reducing the indole ring system of tryptophan to indoline effectively converts an L-tryptophan residue to 2',3'-dihydrotryptophan. DeltaMass:343 URL:http://dx.doi.org/10.1016/S0040-4039(00)99113-5 Modification from DeltaMass. OBSOLETE because redundant and identical to MOD:00462. Remap to MOD:00462. MOD:00462 W artifact PSI-MOD MOD:00963 From DeltaMass: Average Mass: 4 Monoisotopic Mass Change:3.995 Average Mass Change:3.989 References:Ruoppolo M, Amoresano A, Pucci P, Pascarella S, Polticelli F, Trovato M,Menegatti E, Ascenzi P.Characterization of five new low-molecular-mass trypsin inhibitors fromwhite mustard (Sinapis alba L.) seed.Eur J Biochem. 2000 267:6486-92. Notes: See structure at http://www.abrf.org/images/misc/dmass32.jpg. Oxidation of Trp to kynurenine true Modification from DeltaMass. OBSOLETE because redundant and identical to MOD:00462. Remap to MOD:00462. DeltaMass:357 modification from DeltaMass 12.01 C 1 H 0 N 0 O 0 12.0 C 7 H 12 N 2 O 1 140.19 140.09496 K artifact N6-(methylidene)-lysine PSI-MOD MOD:00964 From DeltaMass: Average Mass: 12 Average Mass Change: 12 References: Mathews, W. Rodney; Runge, Thomas A.; Haroldsen, Peter E.; Gaskell, Simon J. (1989) Characterization of impurities in a synthetic renin substrate peptide by fast-atom bombardment mass spectrometry and hybrid tandem mass spectrometry. Rapid Commun. Mass Spectrom. 3(9), 314-19 Notes: Fast-atom bombardment mass spectrometry of a synthetic renin substrate decapeptide (Pro-His-Pro-Phe-His-Leu-Val-Ile-His-D-Lys) indicated the presence of several side products, including a component 12 Da higher in mass. Low-energy collisionally activated ***decompn*** analyses were performed using a hybrid tandem instrument and demonstrated that the heavier side product had two components, in which the structural modification was either at the N- or the C-terminus. Addnl. analyses of the N-acetyl deriv. indicated that for each component the structural modification blocked a site of N-acetylation. It is suggested that the formation of these side products is attributable to the generation of formaldehyde, during removal of the histidine protecting group (benzyloxymethyl), which reacts with the N-terminus of the peptide to give an imidazolidinone structure or with the D- ***lysine***.epsilon.-amine group to yield an ***imine*** . While the precise genesis of the side-products remains speculative, it is clear that the combined strategy of derivatization and tandem mass spectrometry has allowed structural conclusions concerning individual components of an isobaric mixt. lysine epsilon amino to imine + 12 amu modification from DeltaMass DeltaMass:34 N6-(methylidene)-lysine A protein modification that effectively converts an N-terminal L-cysteine residue by a formadehyde adduct to 4-thiazolidinecarboxylic acid. 12.01 C 1 H 0 N 0 O 0 S 0 12.0 C 4 H 6 N 1 O 1 S 1 116.16 116.01701 C artifact N-term thioproline PSI-MOD MOD:00965 From DeltaMass: References: Mitchell, M.A., Runge, T.A., Mathews, W.R., Ichhpurani, A.K., Harn, N.K., Dobrowolski, P.J. and Eckenrrrode, F.M. Problems associated with use of the benzylozymethyl protecting group for histidines. Formaldehyde adducts formed during cleavage by hydrogen fluoride. Int. J. Pept. Protein Res. 1990, 36(4), 350-355. Gesquiere, J.-C., Diesis, E. and Tartar, A. Conversion of N-terminal cysteine to thiazolidine carboxylic acid during hydrogen fluoride deprotection of peptides containing pi-N-Bom protected histidine. J. Chem. Soc. Chem. Commun. 1990, (20), 1402-1403. Kumagaye, K.Y., Inui, T., Nakajima, K., Kimura,T. and Sakakibara, S. Suppression of a side reaction associated with Nim-benzyloxymethyl group during synthesis of peptides containing cysteinyl residue at the N-terminus. Pept. Res. 1991, 4(2), 84-87. Colombo, R., Colombo, F. and Jones, J.H. Acid-labile histidine side-chain protection. The N(pi)-t-butoxymethyl group. J. Chem. Soc. Chem. Commun. 1984, (5), 292-293. Notes: Conversion of N-term Cys to thiazolidine during HF deprotection of His(Bom)-containing peptides [1-3]. See structure at http://www.abrf.org/images/misc/dmass12b.gif; modification in red. This modification cannot be excluded during final deprotection/cleavage in Fmoc-chemistry in cases when His(Bum) was employed [4]. For formation of free imino acid see PubMed:1527501. 4-thiazolidinecarboxylic acid A protein modification that effectively converts an N-terminal L-cysteine residue by a formadehyde adduct to 4-thiazolidinecarboxylic acid. DeltaMass:342 thioproline A protein modification that effectively converts an N-terminal L-tryptophan residue by a formadehyde adduct to 1,2,3,4-tetrahydro-beta-carboline-3-carboxylic acid. 12.01 C 1 H 0 N 0 O 0 S 0 12.0 C 12 H 10 N 2 O 1 198.22 198.07932 W artifact PSI-MOD MOD:00966 From DeltaMass: Average Mass: 12 Average Mass Change: 12 References: Lippke, K. P., W. G. Schunack, W. Wenning, W. E. Mueller. 1983..beta.-Carbolines as benzodiazepine receptor ligands. 1. Synthesis andbenzodiazepine receptor interaction of esters of.beta.-carboline-3-carboxylic acid. J. Med. Chem.26: 499-503 Cain, M., R. W. Weber, F. Guzman, J. M. Cook, S. A. Barker, K. C.Rice, J. N. Crawley, S. M. Paul, P. Skolnick. 1982. .beta.-Carbolines:synthesis and neurochemical and pharmacological actions on brainbenzodiazepine receptors.J. Med. Chem. 25: 1081-91 Notes: +12 Da modification corresponds to formaldehyde adduct of Trp having beta-carboline structure (methylene bridge links carbon-2 of indole ring and alfa-N. See structure at http://www.abrf.org/images/misc/dmass12a.gif; modification in red. 1,2,3,4-tetrahydro-beta-carboline-3-carboxylic acid A protein modification that effectively converts an N-terminal L-tryptophan residue by a formadehyde adduct to 1,2,3,4-tetrahydro-beta-carboline-3-carboxylic acid. DeltaMass:339 A protein modification that effectively cross-links two L-lysine residues to form syndesine, hydroxylysinohydroxynorleucine. 16.96 C 0 H -3 N -2 O 3 16.95512 C 12 H 21 N 2 O 5 273.31 273.14505 K, K hydroxylysinohydroxynorleucine PSI-MOD MOD:00967 Cross-link 2; From DeltaMass: Average Mass: 13 Average Mass Change: 13 (incorrect) [JSG]. syndesine A protein modification that effectively cross-links two L-lysine residues to form syndesine, hydroxylysinohydroxynorleucine. DeltaMass:35 PubMed:75151974 hydroxylysinohydroxynorleucine OBSOLETE because this isn't a protein modification, but rather the difference between two known modifications. modification from DeltaMass C artifact PSI-MOD MOD:00968 From DeltaMass: Average Mass: 13 Formula:C2H2O2 vs C3H5ON Monoisotopic Mass Change:13.03 Average Mass Change:13.05 Notes:Residual acrylamide in SDS gels can partly label cysteine residues in proteins (propionamido-Cys, PAM-Cys, DeltaMass +71Da; see entry). Subsequent alkylation of protein bands with iodoacetic acid e.g. in preparation for proteomic analysis, will convert remaining free cysteines into carboxymethyl-Cys (CM-Cys, DeltaMass +58Da; see entry). Peptide mass fingerprinting may therefore potentially reveal the same cysteine-containing peptide in two forms, differing in mass by 13Da. The relative ratios of the peaks will depend on the initial degree of labelling with acrylamide. Use of high quality, deionised acrylamide in the SDS gel will minimise modification of cysteine through this route. Where it remains a problem, deliberate alkylation using acrylamide instead of iodoacetamide will ensure chemical homogeneity of the final product. CM-Cys vs PAM-Cys true OBSOLETE because this isn't a protein modification, but rather the difference between two known modifications. modification from DeltaMass DeltaMass:347 OBSOLETE because this isn't a protein modification, but rather the difference between two known modifications. modification from DeltaMass C artifact PSI-MOD MOD:00969 From DeltaMass: Average Mass: 14 Formula:CH2 Monoisotopic Mass Change:14.016 Average Mass Change:14.027 Notes: Residual acrylamide in SDS gels can partly label cysteine residues in proteins (propionamido-Cys, PAM-Cys, DeltaMass +71Da; see entry). Subsequent alkylation of protein bands with iodoacetamide e.g. in preparation for proteomic analysis, will convert remaining free cysteines into carboxamidomethyl-Cys (CAM-Cys, DeltaMass +57Da; see entry). Peptide mass fingerprinting may therefore potentially reveal the same cysteine-containing peptide in two forms, differing in mass by 14Da. The relative ratios of the peaks will depend on the initial degree of labelling with acrylamide. Use of high quality, deionised acrylamide in the SDS gel will minimise modification of cysteine through this route. Where it remains a problem, deliberate alkylation using acrylamide instead of iodoacetamide will ensure chemical homogeneity of the final product. CAM-Cys vs PAM-Cys true OBSOLETE because this isn't a protein modification, but rather the difference between two known modifications. modification from DeltaMass DeltaMass:346 modification from DeltaMass K natural PSI-MOD MOD:00970 From DeltaMass: Average Mass: 15 Average Mass Change:15 Notes:In going from Lys to hydroxy-allysine, two separate reactions are involved:1. the oxidative deamination converting Lys to allysine (-CH2NH2 being converted to -CHO) with a net mass change of -1;2.conversion of allysine to delta-hydroxy-allysine (-CH2-CHO being converted to -CH(OH)-CHO) with a mass change of +16. The net change from Lys to hydroxyallysine thus is +15. delta-hydroxy-allysine (Lys) modification from DeltaMass DeltaMass:37 A protein modification that effectively converts an L-histidine residue to 2-oxohistidine. 16.0 C 0 H 0 N 0 O 1 15.994915 C 6 H 7 N 3 O 2 153.14 153.05383 H natural PSI-MOD MOD:00971 From DeltaMass: Average Mass: 16 Average Mass Change:16 References:Lewisch, S. A. and Levine, R. L. (1995) Anal. Biochem. 231, 440-446. Determination of 2-oxo-histidine by amino acid analysis Notes:Rod LevineNIHBldg 3, Room 106 MSC 0320Bethesda, MD 20892-0320email: rlevine@nih.govvoice: 1 (301) 496-2310fax: 1 (301) 496-0599 2-Oxohistidine A protein modification that effectively converts an L-histidine residue to 2-oxohistidine. DeltaMass:38 PubMed:8405458 A protein modification that effectively converts an L-phenylalanine residue to a monobrominated L-phenylalanine, such as L-2'-bromophenylalanine. 78.9 Br 1 C 0 H -1 N 0 O 0 77.910515 Br 1 C 9 H 8 N 1 O 1 226.07 224.97893 F natural Unimod:340 Br1Phe PSI-MOD Bromo bromination MOD:00972 From DeltaMass: Average Mass: 78 Average Mass Change:78 References:Yoshino,K et.al. Biochemistry Vol. 30 pg 6203-9 (1991) Identifidation of a novel amino acid, o-bromo-L-phenylananine, in egg-associated peptides that activate spermatozoa monobrominated L-phenylalanine A protein modification that effectively converts an L-phenylalanine residue to a monobrominated L-phenylalanine, such as L-2'-bromophenylalanine. Unimod:340#F Br1Phe Bromo bromination modification from DeltaMass P artifact PSI-MOD MOD:00973 From DeltaMass: Average Mass: 32 Monoisotopic Mass Change:31.99 Average Mass Change:32 References:Amici A, Levine, RL, Tsai, L, and Stadtman, ER: Conversion of amino acid residues in proteins and amino acid homopolymers to carbonyl derivatives by metal-catalyzed oxidation reactions. Journal of Biological Chemistry 264: 3341-3346 1989.Rod Levine (unpublished) Oxidation of proline (to glutamic acid) modification from DeltaMass DeltaMass:355 modification from DeltaMass 33.96 (35)Cl 1 H -1 33.96103 C 9 (35)Cl 1 H 8 N 1 O 2 197.02 197.02435 Y artifact PSI-MOD MOD:00974 From DeltaMass: Average Mass: 34 (35)Cl labeled 3'-chlorotyrosine modification from DeltaMass DeltaMass:0 modification from DeltaMass 35.96 (37)Cl 1 H -1 35.958076 C 9 (37)Cl 1 H 8 N 1 O 2 199.02 199.02141 Y artifact PSI-MOD MOD:00975 From DeltaMass: Average Mass: 36 (37)Cl labeled 3'-chlorotyrosine modification from DeltaMass DeltaMass:0 modification from DeltaMass - OBSOLETE because redundant and identical to MOD:01072. Remap to MOD:01072. MOD:01072 38.09 H -1 K 1 37.955883 X PSI-MOD MOD:00976 From DeltaMass: Average Mass: 38 potassium salt true modification from DeltaMass - OBSOLETE because redundant and identical to MOD:01072. Remap to MOD:01072. DeltaMass:0 modification from DeltaMass 43.96 H -2 Na 2 43.963886 X PSI-MOD MOD:00977 From DeltaMass: Average Mass: 44 disodium salt modification from DeltaMass DeltaMass:0 modification from DeltaMass C artifact PSI-MOD MOD:00978 From DeltaMass: Average Mass: 51 Average Mass Change: 51 References:Lukszo, Patterson, Albericio, and Kates, Letters in Peptide Science 3, 157-166(1996) Notes:The side reaction can be very significant, and the level to which it occurs depends on how the C-terminal Cys is anchored and what the side-chain protecting group is. The mechanism involves piperidine-mediated beta-elimination of sulfur (with the protecting group on), followed by addition of piperidine across the C-terminaldehydroalanine. Since this last-mentioned step creates a chiral center, a mixture of diastereomers is formed which in special cases can be separatedby HPLC. Another problem with C-terminal Cys is racemization; some references in the review article by Andreu, Albericio, Sole, Munson, Ferrer, and Barany in Pennington-Dunn Peptide Synthesis and Purification Protocols, vol 35, 1994, pp. 91-169. piperidine adduct to C-terminal Cys modification from DeltaMass DeltaMass:345 modification from DeltaMass X artifact PSI-MOD MOD:00979 From DeltaMass: Average Mass: 56 t-butyl ester (OtBu) and t-butyl (tBu) modification from DeltaMass DeltaMass:0 modification from DeltaMass - OBSOLETE because redundant, the difference component of MOD:01060. Remap to MOD:01060. MOD:01060 C artifact PSI-MOD MOD:00980 From DeltaMass: Average Mass: 57 Abbreviation:CamCys Formula:C2H3NO Monoisotopic Mass Change:57.021 Average Mass Change:57.051 Notes:Cysteine reacts with iodoacetamide to produce carboxamidomethyl cysteine. Alternative names are often used, such as amidocarboxymethylcysteine and carbamoylmethylcysteine Carboxamidomethyl (on Cysteine) true modification from DeltaMass - OBSOLETE because redundant, the difference component of MOD:01060. Remap to MOD:01060. DeltaMass:337 modification from DeltaMass 60.07 H -2 K 1 Na 1 59.937824 X PSI-MOD MOD:00981 From DeltaMass: Average Mass: 60 sodium and potassium salt modification from DeltaMass DeltaMass:0 A protein modification that effectively converts an L-serine residue to L-selenocysteine (not known as a natural post-translational modification process). 62.97 C 0 H 0 N 0 O -1 Se 1 63.921608 C 3 H 5 N 1 O 1 Se 1 150.05 150.95363 S artifact Sec(Ser) Selenocysteine (from Serine) PSI-MOD MOD:00982 [From DeltaMass: Average Mass: 64.] Although selenocysteine-charged tRNA(Sec) is biosynthesized from serine-charged tRNA(Sec), in peptide work selenocysteine is usually considered as either a natural residue or as a modified cysteine residue. This entry is for the artifactual formation of L-selenocysteine from serine. For encoded L-selenocysteine, use MOD:00031 [JSG]. L-selenocysteine (Ser) A protein modification that effectively converts an L-serine residue to L-selenocysteine (not known as a natural post-translational modification process). DeltaMass:0 Sec(Ser) Selenocysteine (from Serine) modification from DeltaMass D artifact PSI-MOD MOD:00983 From DeltaMass: Average Mass: 67 Average Mass Change:67 References:http://www.abrf.org/archives/hmail/0008/0007.html Notes:1.) Get rid of the DBU. It can cause piperidine amides at Asp residues. The tbu ester side chain comes off during synthesis and the residue is trans-amidated with piperidine (+67Da by MS). If you haven't yet seen this, you will. Even "normal" 20% pip/DMF (NMP) will cause this, but less frequently. Literature exists for this; I don't remember the exact reference. David H. Singleton Scientist Pfizer Central Research PO Box 8118-101 Eastern Point Road Groton, CT 06340 (860)441-4404. Asp transamidation with piperidine modification from DeltaMass DeltaMass:67 modification from DeltaMass 67.92 (35)Cl 2 H -2 67.92206 C 9 (35)Cl 2 H 7 N 1 O 2 230.99 230.98538 Y artifact PSI-MOD MOD:00984 From DeltaMass: Average Mass: 68 (35)Cl labeled 3',5'-dichlorotyrosine modification from DeltaMass DeltaMass:0 A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with a halogen atom. Y HalTyr PSI-MOD MOD:00985 halogenated tyrosine A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with a halogen atom. PubMed:18688235 HalTyr modification from DeltaMass 69.92 (35)Cl 1 (37)Cl 1 H -2 69.919106 C 9 (35)Cl 1 (37)Cl 1 H 7 N 1 O 2 232.98 232.98244 Y artifact PSI-MOD MOD:00986 From DeltaMass: Average Mass: 70. (35)Cl and (37)Cl labeled 3',5'-dichlorotyrosine modification from DeltaMass DeltaMass:0 A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with a chlorine atom. Y ClTyr PSI-MOD MOD:00987 chlorinated tyrosine A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with a chlorine atom. PubMed:18688235 ClTyr A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with a bromine atom. Y BrTyr PSI-MOD MOD:00988 brominated tyrosine A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with a bromine atom. PubMed:18688235 BrTyr OBSOLETE because redundant, the difference component of MOD:01079. Remap to MOD:01079. MOD:01079 C artifact PSI-MOD MOD:00989 From DeltaMass with no citation or formula. acetamidomethyl (Acm) true OBSOLETE because redundant, the difference component of MOD:01079. Remap to MOD:01079. DeltaMass:0 modification from DeltaMass 71.92 (37)Cl 2 H -2 71.91615 C 9 (37)Cl 2 H 7 N 1 O 2 234.98 234.97948 Y artifact PSI-MOD MOD:00990 From DeltaMass: Average Mass: 72 (37)Cl labeled 3',5'-dichlorotyrosine modification from DeltaMass DeltaMass:0 modification from DeltaMass 74.08 C 3 H 6 O 2 74.03678 C 6 H 11 N 1 O 3 S 1 177.22 177.04596 C artifact PSI-MOD MOD:00991 From DeltaMass: Average Mass: 74 with no citation. S-(sn-1-glyceryl)-L-cysteine modification from DeltaMass DeltaMass:0 modification from DeltaMass 74.08 C 3 H 6 O 2 74.03678 C 8 H 13 N 1 O 5 203.19 203.07938 E artifact PSI-MOD MOD:00992 From DeltaMass: Average Mass: 74 Average Mass Change: 74 References: Anal. Biochem. 1993 Vol 208 No. 2 382-386, PubMed:8452236. [DeltaMass] This article only suggests this as a possible modification and does no characterization. Isolation and stuctural evidence for artifactual modification are found in PubMed:18767873 [JSG]. glutamate 5-glycerol ester modification from DeltaMass DeltaMass:78 PubMed:18767873 modification from DeltaMass 76.1 C 6 H 4 76.0313 X artifact OPh PSI-MOD MOD:00993 From DeltaMass: Average Mass: 76, on acidic amino acids phenyl ester modification from DeltaMass DeltaMass:0 OPh modification from DeltaMass 77.91 (79)Br 1 H -1 77.910515 (79)Br 1 C 9 H 8 N 1 O 2 240.97 240.97385 Y artifact PSI-MOD MOD:00994 From DeltaMass: Average Mass: 78 (79)Br labeled 3'-bromotyrosine modification from DeltaMass DeltaMass:0 A protein modification that effectively converts an L-phenylalanine residue to (81)Br-L-2'-bromophenylalanine. 79.91 (81)Br 1 H -1 79.90846 (81)Br 1 C 9 H 8 N 1 O 1 226.98 226.97688 F artifact PSI-MOD MOD:00995 From DeltaMass: Average Mass: 80 (81)Br labeled 2'-bromophenylalanine A protein modification that effectively converts an L-phenylalanine residue to (81)Br-L-2'-bromophenylalanine. DeltaMass:0 modification from DeltaMass 79.91 (81)Br 1 H -1 79.90846 (81)Br 1 C 9 H 8 N 1 O 2 242.97 242.97179 Y artifact PSI-MOD MOD:00996 From DeltaMass: Average Mass: 80 (81)Br labeled 3'-bromotyrosine modification from DeltaMass DeltaMass:0 modification from DeltaMass 82.15 C 6 H 10 82.07825 X artifact OcHex PSI-MOD MOD:00997 From DeltaMass: Average Mass: 82 cyclohexyl ester modification from DeltaMass DeltaMass:0 OcHex A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with an iodine atom. Y ITyr PSI-MOD MOD:00998 iodinated tyrosine A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with an iodine atom. PubMed:18688235 ITyr OBSOLETE because redundant and identical to MOD:00404. Remap to MOD:00404. MOD:00404 M artifact PSI-MOD MOD:00999 From DeltaMass: Average Mass: 83 Formula:C4H5O1N1 Monoisotopic Mass Change:83.037 Average Mass Change:83.09 homoseryl lactone true OBSOLETE because redundant and identical to MOD:00404. Remap to MOD:00404. DeltaMass:90 A protein modification that effectively substitutes one hydrogen atom of an L-tyrosine residue with one bromine atom. Y Br1Tyr PSI-MOD MOD:01000 monobrominated tyrosine A protein modification that effectively substitutes one hydrogen atom of an L-tyrosine residue with one bromine atom. PubMed:18688235 Br1Tyr A protein modification that inserts or replaces a residue with a 2-aminoisobutyric acid. C 4 H 7 N 1 O 1 85.11 85.052765 X artifact 2-amino-2-methylpropanoic acid 2-amino-2-methylpropionic acid 2-methylalanine Aib alpha,alpha-dimethylglycine alpha-aminoisobutyric acid alpha-methylalanine PSI-MOD MOD:01001 Modification from DeltaMass: Average Mass: 85. 2-aminoisobutyric acid residue (Aib) A protein modification that inserts or replaces a residue with a 2-aminoisobutyric acid. DeltaMass:0 2-amino-2-methylpropanoic acid 2-amino-2-methylpropionic acid 2-methylalanine Aib alpha,alpha-dimethylglycine alpha-aminoisobutyric acid alpha-methylalanine modification from DeltaMass 85.11 C 4 H 7 N 1 O 1 85.052765 X artifact PSI-MOD MOD:01002 From DeltaMass: Average Mass: 85 Formula: C 4 H 7 O 1 N 1 Monoisotopic Mass Change: 85.053 Average Mass Change: 85.106 gamma-aminobutyryl modification from DeltaMass DeltaMass:92 modification from DeltaMass X artifact PSI-MOD MOD:01003 From DeltaMass: Average Mass: 86 t-butyloxymethyl (Bum) modification from DeltaMass DeltaMass:0 modification from DeltaMass 86.09 C 3 H 6 N 2 O 1 86.04801 X artifact PSI-MOD MOD:01004 From DeltaMass: Average Mass: 86 Formula: C 3 H 6 O 2 N 1 Monoisotopic Mass Change: 86.048 Average Mass Change: 86.094 diaminopropionyl modification from DeltaMass DeltaMass:95 modification from DeltaMass X artifact StBu PSI-MOD MOD:01005 From DeltaMass: Average Mass: 88 t-butylsulfenyl modification from DeltaMass DeltaMass:0 StBu A protein modification that effectively substitutes two hydrogen atoms of an L-tyrosine residue with two bromine atoms. Y Unimod:534 Br2Tyr PSI-MOD Dibromo MOD:01006 dibrominated tyrosine A protein modification that effectively substitutes two hydrogen atoms of an L-tyrosine residue with two bromine atoms. Unimod:534 Br2Tyr Dibromo Dibromo A protein modification that effectively substitutes an anisyl (methoxyphenyl) group for a hydroxyl group, typically at the 4 or para position. 90.13 C 7 H 6 90.04695 X artifact PSI-MOD MOD:01007 From DeltaMass with no citation or formula: Average Mass: 90. anisyl modified residue A protein modification that effectively substitutes an anisyl (methoxyphenyl) group for a hydroxyl group, typically at the 4 or para position. DeltaMass:0 A protein modification that effectively substitutes a benzyl (phenylmethyl) group for a hydrogen atom. 90.13 C 7 H 6 90.04695 X artifact PSI-MOD MOD:01008 From DeltaMass with no citation or formula: Average Mass: 90 benzyl (Bzl) and benzyl ester (OBzl) modified residue A protein modification that effectively substitutes a benzyl (phenylmethyl) group for a hydrogen atom. DeltaMass:0 modification from DeltaMass -2.02 C 0 H -2 N 0 O 0 -2.01565 C 5 H 5 N 1 O 1 95.1 95.03712 P PSI-MOD MOD:01009 From DeltaMass with no citation. dehydrogenated proline modification from DeltaMass DeltaMass:0 A protein modification that effectively substitutes a trifluoroacetyl group for a hydrogen atom. 96.01 C 2 F 3 H -1 O 1 95.9823 X artifact TFA PSI-MOD MOD:01010 trifluoroacetylated residue A protein modification that effectively substitutes a trifluoroacetyl group for a hydrogen atom. DeltaMass:0 TFA modification from DeltaMass X artifact PSI-MOD MOD:01011 From DeltaMass: Average Mass: 97 N-hydroxysuccinimide (ONSu, OSu) modification from DeltaMass DeltaMass:0 A protein modification that effectively oxidizes the disulfide bond of a cystine crosslink to form two cysteic acid residues. 98.01 C 0 H 2 N 0 O 6 S 0 97.98514 C 6 H 10 N 2 O 8 S 2 302.27 301.98785 MOD:00034 artifact PSI-MOD MOD:01012 Cross-link 2. This modification destroys a cross-link. From DeltaMass: Average Mass: 98 Abbreviation: Cya Average Mass Change: 98 Notes: Treatment of cystine by strongly oxidising reagents such as performic acid results in the breakage of the disulphide bond and complete oxidation of the sulphur atoms on each molecule. Such treatment is often carried out prior to amino acid analysis as the resulting cysteic acid is then resistant to acid degradation during the hydrolysis procedure. oxidation of disulfide crosslink in cystine to two cysteic acids A protein modification that effectively oxidizes the disulfide bond of a cystine crosslink to form two cysteic acid residues. DeltaMass:335 modification from DeltaMass X PSI-MOD MOD:01013 From DeltaMass: Average Mass: 98 tetramethylguanidinium termination by-product on amine modification from DeltaMass DeltaMass:0 modification from DeltaMass X PSI-MOD MOD:01014 From DeltaMass: Average Mass: 98 Formula:H3PO4 or H2SO4 Monoisotopic Mass Change:97.97 Average Mass Change:98 Notes:Proteins may pick up non-covalent salt adducts during purification. Phosphate and sulphate salts are commonly used and may be observed as +98 amu adducts (or multiples thereof) forming ion pairs with basic residues. Monoisotopic masses H2SO4 97.967, H3PO4 97.977 phosphate/sulphate adduct of proteins modification from DeltaMass DeltaMass:358 A protein modification that inserts or replaces a residue with an isovaline. C 5 H 9 N 1 O 1 99.13 99.06841 X artifact 2-amino-2-methylbutanoic acid Isovalyl (-I-,-Iva-) Iva PSI-MOD MOD:01015 isovaline residue (Iva) A protein modification that inserts or replaces a residue with an isovaline. DeltaMass:110 2-amino-2-methylbutanoic acid Isovalyl (-I-,-Iva-) Iva modification from DeltaMass X artifact tBoc PSI-MOD MOD:01016 From DeltaMass: Average Mass: 100 t-butyloxycarbonyl modification from DeltaMass DeltaMass:0 tBoc OBSOLETE because redundant and identical to MOD:00403. Remap to MOD:00403. MOD:00403 M artifact PSI-MOD MOD:01017 From DeltaMass: Average Mass: 101 Abbreviation:-Hse- Formula:C4H7O2N Monoisotopic Mass Change:101.048 Average Mass Change:101.105 homoseryl (-Hse-) true OBSOLETE because redundant and identical to MOD:00403. Remap to MOD:00403. DeltaMass:113 modification from DeltaMass X artifact Meb PSI-MOD MOD:01018 From DeltaMass: Average Mass: 104 4-methylbenzyl modification from DeltaMass DeltaMass:0 Meb modification from DeltaMass X artifact HMP PSI-MOD MOD:01019 From DeltaMass: Average Mass: 106 hydroxymethylphenyl linker modification from DeltaMass DeltaMass:0 HMP modification from DeltaMass X artifact PSI-MOD MOD:01020 From DeltaMass: Average Mass: 106 thioanisyl modification from DeltaMass DeltaMass:0 modification from DeltaMass X artifact PSI-MOD MOD:01021 From DeltaMass: Average Mass: 106 thiocresyl modification from DeltaMass DeltaMass:0 A protein modification that effectively converts an L-lysine residue to 2-piperidinecarboxylic acid. -17.03 C 0 H -3 N -1 O 0 -17.026548 C 6 H 9 N 1 O 1 111.14 111.06841 K artifact Pip PSI-MOD MOD:01022 2-piperidinecarboxylic acid A protein modification that effectively converts an L-lysine residue to 2-piperidinecarboxylic acid. DeltaMass:0 Pip A protein modification that effectively converts an L-tyrosine residue to 3',5'-dibromo-L-tyrosine. 157.79 Br 2 C 0 H -2 N 0 O 0 155.82103 Br 2 C 9 H 7 N 1 O 2 320.97 318.88434 Y 3',5'-Br2Tyr PSI-MOD MOD:01023 3',5'-dibromo-L-tyrosine A protein modification that effectively converts an L-tyrosine residue to 3',5'-dibromo-L-tyrosine. DeltaMass:156 3',5'-Br2Tyr A protein modification that effectively converts an L-proline residue to one of several monohydroxylated proline residues, including 3-hydroxy-L-proline and 4-hydroxy-L-proline. 16.0 C 0 H 0 N 0 O 1 15.994915 C 5 H 7 N 1 O 2 113.12 113.047676 P natural Unimod:35 uniprot.ptm:PTM-0149 Hy1Pro Hydroxyproline Hyp hydroxylationp PSI-MOD Oxidation MOD:01024 From DeltaMass: Average Mass: 131. This is the mass of the free amino acid [JSG]. monohydroxylated proline A protein modification that effectively converts an L-proline residue to one of several monohydroxylated proline residues, including 3-hydroxy-L-proline and 4-hydroxy-L-proline. DeltaMass:0 OMSSA:62 Unimod:35#P Hy1Pro Hydroxyproline Hyp hydroxylationp Oxidation A protein modification that effectively converts an L-tyrosine residue to 3'-bromo-L-tyrosine. 78.9 Br 1 H -1 77.910515 Br 1 C 9 H 8 N 1 O 2 242.07 240.97385 Y 3'-BrTyr PSI-MOD MOD:01025 3'-bromo-L-tyrosine A protein modification that effectively converts an L-tyrosine residue to 3'-bromo-L-tyrosine. PubMed:18688235 3'-BrTyr A protein modification that inserts or replaces a residue with a norleucine. C 6 H 11 N 1 O 1 113.16 113.08406 X artifact Nle PSI-MOD MOD:01026 norleucine residue (Nle) A protein modification that inserts or replaces a residue with a norleucine. DeltaMass:126 Nle modification from DeltaMass X artifact Aoc PSI-MOD MOD:01027 From DeltaMass: Average Mass: 114 t-amyloxycarbonyl modification from DeltaMass DeltaMass:0 Aoc A protein modification that effectively substitutes one hydrogen atom of an L-tyrosine residue with one chlorine atom. 34.44 C 0 Cl 1 H -1 N 0 O 0 33.96103 C 9 Cl 1 H 8 N 1 O 2 197.62 197.02435 Y artifact Cl1Tyr PSI-MOD MOD:01028 monochlorinated L-tyrosine A protein modification that effectively substitutes one hydrogen atom of an L-tyrosine residue with one chlorine atom. PubMed:18688235 Cl1Tyr A protein modification that effectively replaces a hydrogen atom with a succinyl group linked through a carbonyl carbon. 100.07 C 4 H 4 O 3 100.016045 X Unimod:64 PSI-MOD Succinic anhydride labeling reagent light form (N-term & K) MOD:01029 From DeltaMass with no citation or formula, Average Mass: 117 [JSG]. succinylated residue A protein modification that effectively replaces a hydrogen atom with a succinyl group linked through a carbonyl carbon. DeltaMass:0 Unimod:64 Succinic anhydride labeling reagent light form (N-term & K)