Term IRI Term label Parent term IRI Parent term label Alternative term Definition http://purl.obolibrary.org/obo/MOD_00493 formylated residue http://purl.obolibrary.org/obo/MOD_00649 acylated residue A protein modification that effectively replaces a hydrogen atom with a formyl group. http://purl.obolibrary.org/obo/MOD_01204 prompt loss of methanethiol from oxidixed methionine http://purl.obolibrary.org/obo/MOD_00913 modified L-methionine residue modification from Unimod Artifact - http://purl.obolibrary.org/obo/MOD_01733 TMT6plex-127 reporter+balance reagent O3-acylated serine http://purl.obolibrary.org/obo/MOD_02003 O3-acylated L-serine A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-127 reporter+balance group. http://purl.obolibrary.org/obo/MOD_02081 alpha-amino succinylated residue http://purl.obolibrary.org/obo/MOD_01696 alpha-amino acylated residue A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a succinyl group. http://purl.obolibrary.org/obo/MOD_02082 didehydrogenated and dehydrated residue http://purl.obolibrary.org/obo/MOD_00683 dehydrogenated residue A protein modification that effectively removes two neutral hydrogen atoms (proton and electron) and a water moiety from a residue. http://purl.obolibrary.org/obo/MOD_02083 4alpha-FMN modified residue http://purl.obolibrary.org/obo/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 through the 4-alpha position of FMN. http://purl.obolibrary.org/obo/MOD_02084 6-FMN modified residue http://purl.obolibrary.org/obo/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 through the 6 position of FMN. http://purl.obolibrary.org/obo/MOD_02085 8alpha-FMN modified residue http://purl.obolibrary.org/obo/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 through the 8-alpha position of FMN. http://purl.obolibrary.org/obo/MOD_02086 brominated phenylalanine http://purl.obolibrary.org/obo/MOD_00754 brominated residue A protein modification that effectively substitutes a hydrogen atom of an L-phenylalanine residue with a bromine atom. http://purl.obolibrary.org/obo/MOD_02087 adenosine diphosphoribosyl (ADP-ribosyl) modified residue http://purl.obolibrary.org/obo/MOD_00701 nucleotide or nucleic acid modified residue A protein modification that effectively results from forming an adduct with one or more ADP-ribose moieties or to modified residues through formation of a glycosidic bond. http://purl.obolibrary.org/obo/MOD_02089 O-(phospho-5'-uridine)-L-serine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively crosslinks an L-serine residue and 5'-phosphouridine through a phosphodiester bond to form O-(phospho-5'-uridine)-L-serine. http://purl.obolibrary.org/obo/MOD_02090 O-(phospho-5'-uridine)-L-threonine http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue A protein modification that effectively modifies an L-threonine residue with 5'-phosphouridine through a phosphodiester bond to form O-(phospho-5'-uridine)-L-threonine. http://purl.obolibrary.org/obo/MOD_02091 O-(phospho-5'-adenosine)-L-serine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively modifies an L-serine residue with 5'-phosphoadenosine through a phosphodiester bond to form O-(phospho-5'-adenosine)-L-serine. http://purl.obolibrary.org/obo/MOD_02092 S-methylbutanedioic acid-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to form S-methylbutanedioic acid-L-cysteine by alkylation with itaconate through a thioether bond. http://purl.obolibrary.org/obo/MOD_02093 N6-(2-hydroxyisobutanoyl)-L-lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively converts an L-lysine residue to N6-(2-hydroxyisobutanoyl)-L-lysine. http://purl.obolibrary.org/obo/MOD_02094 N6-((3R)-3-hydroxybutanoyl)-L-lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively converts an L-lysine residue to N6-((3R)-3-hydroxybutanoyl)-L-lysine. http://purl.obolibrary.org/obo/MOD_02095 N6-glutaryl-L-lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively converts an L-lysine residue to N6-glutaryl-L-lysine. http://purl.obolibrary.org/obo/MOD_02096 N4-methyl-D-asparagine http://purl.obolibrary.org/obo/MOD_00599 monomethylated residue A protein modification that effectively converts a D-asparagine residue to N4-methyl-D-asparagine. http://purl.obolibrary.org/obo/MOD_02097 modified D-asparagine residue http://purl.obolibrary.org/obo/MOD_00203 D-asparagine A protein modification that modifies a D-asparagine residue. http://purl.obolibrary.org/obo/MOD_00001 alkylated residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process A protein modification that effectively replaces a hydrogen atom with an alkyl group. http://purl.obolibrary.org/obo/MOD_00002 O-glycosyl-L-serine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to O3-glycosylserine. http://purl.obolibrary.org/obo/MOD_00003 Unimod http://purl.obolibrary.org/obo/MOD_00032 uncategorized protein modification Entry from Unimod. http://purl.obolibrary.org/obo/MOD_00005 O-glycosyl-L-threonine http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue A protein modification that effectively converts an L-threonine residue to O3-glycosylthreonine. http://purl.obolibrary.org/obo/MOD_00007 selenium substitution for sulfur http://purl.obolibrary.org/obo/MOD_00745 selenium containing residue A protein modification that effectively substitutes a selenium atom for a sulfur atom. http://purl.obolibrary.org/obo/MOD_00009 natural residue http://purl.obolibrary.org/obo/MOD_01157 protein modification categorized by amino acid modified A protein modification that removes a residue, or inserts or replaces a residue with a natural, standard or nonstandard, encoded residue. http://purl.obolibrary.org/obo/MOD_00010 L-alanine residue http://purl.obolibrary.org/obo/MOD_01441 natural, standard, encoded residue A protein modification that effectively converts a source amino acid residue to an L-alanine. http://purl.obolibrary.org/obo/MOD_00011 L-arginine residue http://purl.obolibrary.org/obo/MOD_01441 natural, standard, encoded residue A protein modification that effectively converts a source amino acid residue to an L-arginine. http://purl.obolibrary.org/obo/MOD_00012 L-asparagine residue http://purl.obolibrary.org/obo/MOD_01441 natural, standard, encoded residue A protein modification that effectively converts a source amino acid residue to an L-asparagine. http://purl.obolibrary.org/obo/MOD_00013 L-aspartic acid residue http://purl.obolibrary.org/obo/MOD_01441 natural, standard, encoded residue A protein modification that effectively converts a source amino acid residue to an L-aspartic acid. http://purl.obolibrary.org/obo/MOD_00014 L-cysteine residue http://purl.obolibrary.org/obo/MOD_01441 natural, standard, encoded residue A protein modification that effectively converts a source amino acid residue to an L-cysteine. http://purl.obolibrary.org/obo/MOD_00015 L-glutamic acid residue http://purl.obolibrary.org/obo/MOD_01441 natural, standard, encoded residue A protein modification that effectively converts a source amino acid residue to an L-glutamic acid. http://purl.obolibrary.org/obo/MOD_00016 L-glutamine residue http://purl.obolibrary.org/obo/MOD_01441 natural, standard, encoded residue A protein modification that effectively converts a source amino acid residue to an L-glutamine. http://purl.obolibrary.org/obo/MOD_00017 glycine residue http://purl.obolibrary.org/obo/MOD_01441 natural, standard, encoded residue A protein modification that effectively converts a source amino acid residue to a glycine. http://purl.obolibrary.org/obo/MOD_00018 L-histidine residue http://purl.obolibrary.org/obo/MOD_01441 natural, standard, encoded residue A protein modification that effectively converts a source amino acid residue to an L-histidine. http://purl.obolibrary.org/obo/MOD_00019 L-isoleucine residue http://purl.obolibrary.org/obo/MOD_01441 natural, standard, encoded residue A protein modification that effectively converts a source amino acid residue to an L-isoleucine. http://purl.obolibrary.org/obo/MOD_00020 L-leucine residue http://purl.obolibrary.org/obo/MOD_01441 natural, standard, encoded residue A protein modification that effectively converts a source amino acid residue to an L-leucine. http://purl.obolibrary.org/obo/MOD_00021 L-lysine residue http://purl.obolibrary.org/obo/MOD_01441 natural, standard, encoded residue A protein modification that effectively converts a source amino acid residue to L-lysine. http://purl.obolibrary.org/obo/MOD_00022 L-methionine residue http://purl.obolibrary.org/obo/MOD_01441 natural, standard, encoded residue A protein modification that effectively converts a source amino acid residue to L-methionine. http://purl.obolibrary.org/obo/MOD_00023 L-phenylalanine residue http://purl.obolibrary.org/obo/MOD_01441 natural, standard, encoded residue A protein modification that effectively converts a source amino acid residue to L-phenylalanine. http://purl.obolibrary.org/obo/MOD_00024 L-proline residue http://purl.obolibrary.org/obo/MOD_01441 natural, standard, encoded residue A protein modification that effectively converts a source amino acid residue to L-proline. http://purl.obolibrary.org/obo/MOD_00025 L-serine residue http://purl.obolibrary.org/obo/MOD_01441 natural, standard, encoded residue A protein modification that effectively converts a source amino acid residue to L-serine. http://purl.obolibrary.org/obo/MOD_00026 L-threonine residue http://purl.obolibrary.org/obo/MOD_01441 natural, standard, encoded residue A protein modification that effectively converts a source amino acid residue to L-threonine. http://purl.obolibrary.org/obo/MOD_00027 L-tryptophan residue http://purl.obolibrary.org/obo/MOD_01441 natural, standard, encoded residue A protein modification that effectively converts a source amino acid residue to L-tryptophan. http://purl.obolibrary.org/obo/MOD_00028 L-tyrosine residue http://purl.obolibrary.org/obo/MOD_01441 natural, standard, encoded residue A protein modification that effectively converts a source amino acid residue to L-tyrosine. http://purl.obolibrary.org/obo/MOD_00029 L-valine residue http://purl.obolibrary.org/obo/MOD_01441 natural, standard, encoded residue A protein modification that effectively converts a source amino acid residue to an L-valine. http://purl.obolibrary.org/obo/MOD_00032 uncategorized protein modification http://purl.obolibrary.org/obo/MOD_00000 protein modification A protein modification that is not chemically categorized. http://purl.obolibrary.org/obo/MOD_00034 L-cystine (cross-link) http://purl.obolibrary.org/obo/MOD_00689 disulfide crosslinked residues A protein modification that effectively cross-links two L-cysteine residues to form L-cystine. http://purl.obolibrary.org/obo/MOD_00035 (2S,3R)-3-hydroxyasparagine http://purl.obolibrary.org/obo/MOD_01688 3-hydroxy-L-asparagine A protein modification that effectively converts an L-asparagine residue to (2S,3R)-3-hydroxyasparagine. http://purl.obolibrary.org/obo/MOD_00043 S-phospho-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-phospho-L-cysteine. http://purl.obolibrary.org/obo/MOD_00044 1'-phospho-L-histidine http://purl.obolibrary.org/obo/MOD_00890 phosphorylated 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). http://purl.obolibrary.org/obo/MOD_00049 2'-[3-carboxamido-3-(trimethylammonio)propyl]-L-histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively converts an L-histidine residue to diphthamide. http://purl.obolibrary.org/obo/MOD_00051 N-acetyl-L-aspartic acid http://purl.obolibrary.org/obo/MOD_00904 modified L-aspartic acid residue A protein modification that effectively converts an L-aspartic acid residue to N-acetyl-L-aspartic acid. http://purl.obolibrary.org/obo/MOD_00052 N-acetyl-L-cysteine http://purl.obolibrary.org/obo/MOD_01458 alpha-amino acetylated residue A protein modification that effectively converts an L-cysteine residue to N-acetyl-L-cysteine. http://purl.obolibrary.org/obo/MOD_00054 N-acetyl-L-glutamine http://purl.obolibrary.org/obo/MOD_00907 modified L-glutamine residue A protein modification that effectively converts an L-glutamine residue to N-acetyl-L-glutamine. http://purl.obolibrary.org/obo/MOD_00056 N-acetyl-L-isoleucine http://purl.obolibrary.org/obo/MOD_00910 modified L-isoleucine residue A protein modification that effectively converts an L-isoleucine residue to N-acetyl-L-isoleucine. http://purl.obolibrary.org/obo/MOD_00057 N2-acetyl-L-lysine http://purl.obolibrary.org/obo/MOD_00723 N-acetylated L-lysine A protein modification that effectively converts an L-lysine residue to N2-acetyl-L-lysine. http://purl.obolibrary.org/obo/MOD_00059 N-acetyl-L-proline http://purl.obolibrary.org/obo/MOD_00915 modified L-proline residue A protein modification that effectively converts an L-proline residue to N-acetyl-L-proline. http://purl.obolibrary.org/obo/MOD_00061 N-acetyl-L-threonine http://purl.obolibrary.org/obo/MOD_01458 alpha-amino acetylated residue A protein modification that effectively converts an L-threonine residue to N-acetyl-L-threonine. http://purl.obolibrary.org/obo/MOD_00062 N-acetyl-L-tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively converts an L-tyrosine residue to N-acetyl-L-tyrosine. http://purl.obolibrary.org/obo/MOD_00063 N-acetyl-L-valine http://purl.obolibrary.org/obo/MOD_00920 modified L-valine residue A protein modification that effectively converts an L-valine residue to N-acetyl-L-valine. http://purl.obolibrary.org/obo/MOD_00065 S-acetyl-L-cysteine http://purl.obolibrary.org/obo/MOD_00646 monoacetylated L-cysteine A protein modification that effectively converts an L-cysteine residue to S-acetyl-L-cysteine. http://purl.obolibrary.org/obo/MOD_00066 N-formylglycine http://purl.obolibrary.org/obo/MOD_00908 modified glycine residue A protein modification that effectively converts a glycine residue to N-formylglycine. http://purl.obolibrary.org/obo/MOD_00067 N-D-glucuronoylglycine http://purl.obolibrary.org/obo/MOD_00908 modified glycine residue A protein modification that effectively converts a glycine residue to N-D-glucuronoylglycine. http://purl.obolibrary.org/obo/MOD_00070 N-methyl-L-alanine http://purl.obolibrary.org/obo/MOD_01680 alpha-amino monomethylated residue A protein modification that effectively converts an L-alanine residue to N-methyl-L-alanine. http://purl.obolibrary.org/obo/MOD_00071 N,N,N-trimethyl-L-alanine http://purl.obolibrary.org/obo/MOD_01698 alpha-amino trimethylated protonated-residue A protein modification that effectively converts an L-alanine residue to N,N,N-trimethyl-L-alanine. http://purl.obolibrary.org/obo/MOD_00072 N-methylglycine http://purl.obolibrary.org/obo/MOD_01680 alpha-amino monomethylated residue A protein modification that effectively converts a glycine residue to N-methylglycine. http://purl.obolibrary.org/obo/MOD_00073 N-methyl-L-methionine http://purl.obolibrary.org/obo/MOD_01680 alpha-amino monomethylated residue A protein modification that effectively converts an L-methionine residue to N-methyl-L-methionine. http://purl.obolibrary.org/obo/MOD_00074 N-methyl-L-phenylalanine http://purl.obolibrary.org/obo/MOD_01680 alpha-amino monomethylated residue A protein modification that effectively converts an L-phenylalanine residue to N-methyl-L-phenylalanine. http://purl.obolibrary.org/obo/MOD_00075 N,N-dimethyl-L-proline http://purl.obolibrary.org/obo/MOD_01462 N-methylated proline A protein modification that effectively converts an L-proline residue to N,N-dimethyl-L-proline. http://purl.obolibrary.org/obo/MOD_00079 N4-methyl-L-asparagine http://purl.obolibrary.org/obo/MOD_00599 monomethylated residue A protein modification that effectively converts an L-asparagine residue to N4-methyl-L-asparagine. http://purl.obolibrary.org/obo/MOD_00080 N5-methyl-L-glutamine http://purl.obolibrary.org/obo/MOD_00722 monomethylated L-glutamine A protein modification that effectively converts an L-glutamine residue to N5-methyl-L-glutamine. http://purl.obolibrary.org/obo/MOD_00081 L-glutamic acid 5-methyl ester (Glu) http://purl.obolibrary.org/obo/MOD_01453 L-glutamic acid 5-methyl ester A protein modification that effectively converts an L-glutamic acid residue to L-glutamate 5-methyl ester. http://purl.obolibrary.org/obo/MOD_00082 3'-methyl-L-histidine http://purl.obolibrary.org/obo/MOD_02038 monomethylated 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). http://purl.obolibrary.org/obo/MOD_00086 N6-palmitoyl-L-lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively converts an L-lysine residue to N6-palmitoyl-L-lysine. http://purl.obolibrary.org/obo/MOD_00088 O-palmitoyl-L-threonine http://purl.obolibrary.org/obo/MOD_02004 O3-acylated L-threonine A protein modification that effectively converts an L-threonine residue to O-palmitoyl-L-threonine. http://purl.obolibrary.org/obo/MOD_00089 O-palmitoyl-L-serine http://purl.obolibrary.org/obo/MOD_02003 O3-acylated L-serine A protein modification that effectively converts an L-serine residue to O-palmitoyl-L-serine. http://purl.obolibrary.org/obo/MOD_00090 L-alanine amide http://purl.obolibrary.org/obo/MOD_00901 modified L-alanine residue A protein modification that effectively converts an L-alanine residue to L-alanine amide. http://purl.obolibrary.org/obo/MOD_00091 L-arginine amide http://purl.obolibrary.org/obo/MOD_00902 modified L-arginine residue A protein modification that effectively converts an L-arginine residue to L-arginine amide. http://purl.obolibrary.org/obo/MOD_00092 L-asparagine amide http://purl.obolibrary.org/obo/MOD_00903 modified L-asparagine residue A protein modification that effectively converts an L-asparagine residue to L-asparagine amide. http://purl.obolibrary.org/obo/MOD_00093 L-aspartic acid 1-amide http://purl.obolibrary.org/obo/MOD_00904 modified L-aspartic acid residue A protein modification that effectively converts an L-aspartic acid residue to L-aspartic acid 1-amide. http://purl.obolibrary.org/obo/MOD_00094 L-cysteine amide http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to L-cysteine amide. http://purl.obolibrary.org/obo/MOD_00095 L-glutamine amide http://purl.obolibrary.org/obo/MOD_00907 modified L-glutamine residue A protein modification that effectively converts an L-glutamine residue to L-glutamine amide. http://purl.obolibrary.org/obo/MOD_00096 L-glutamic acid 1-amide http://purl.obolibrary.org/obo/MOD_00906 modified L-glutamic acid residue A protein modification that effectively converts an L-glutamic acid residue to L-glutamic acid 1-amide. http://purl.obolibrary.org/obo/MOD_00097 glycine amide http://purl.obolibrary.org/obo/MOD_00908 modified glycine residue A protein modification that effectively converts a glycine residue to glycine amide. http://purl.obolibrary.org/obo/MOD_00098 L-histidine amide http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively converts an L-histidine residue to L-histidine amide. http://purl.obolibrary.org/obo/MOD_00099 L-isoleucine amide http://purl.obolibrary.org/obo/MOD_00910 modified L-isoleucine residue A protein modification that effectively converts an L-isoleucine residue to L-isoleucine amide. http://purl.obolibrary.org/obo/MOD_00100 L-leucine amide http://purl.obolibrary.org/obo/MOD_00911 modified L-leucine residue A protein modification that effectively converts an L-leucine residue to L-leucine amide. http://purl.obolibrary.org/obo/MOD_00101 L-lysine amide http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively converts an L-lysine residue to L-lysine amide. http://purl.obolibrary.org/obo/MOD_00102 L-methionine amide http://purl.obolibrary.org/obo/MOD_00913 modified L-methionine residue A protein modification that effectively converts an L-methionine residue to L-methionine amide. http://purl.obolibrary.org/obo/MOD_00103 L-phenylalanine amide http://purl.obolibrary.org/obo/MOD_00914 modified L-phenylalanine residue A protein modification that effectively converts an L-phenylalanine residue to L-phenylalanine amide. http://purl.obolibrary.org/obo/MOD_00104 L-proline amide http://purl.obolibrary.org/obo/MOD_00915 modified L-proline residue A protein modification that effectively converts an L-proline residue to L-proline amide. http://purl.obolibrary.org/obo/MOD_00105 L-serine amide http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to L-serine amide. http://purl.obolibrary.org/obo/MOD_00106 L-threonine amide http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue A protein modification that effectively converts an L-threonine residue to L-threonine amide. http://purl.obolibrary.org/obo/MOD_00107 L-tryptophan amide http://purl.obolibrary.org/obo/MOD_00918 modified L-tryptophan residue A protein modification that effectively converts an L-tryptophan residue to L-tryptophan amide. http://purl.obolibrary.org/obo/MOD_00108 L-tyrosine amide http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively converts an L-tyrosine residue to L-tyrosine amide. http://purl.obolibrary.org/obo/MOD_00109 L-valine amide http://purl.obolibrary.org/obo/MOD_00920 modified L-valine residue A protein modification that effectively converts an L-valine residue to L-valine amide. http://purl.obolibrary.org/obo/MOD_00110 L-cysteine methyl disulfide http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to L-cysteine methyl disulfide. http://purl.obolibrary.org/obo/MOD_00112 S-12-hydroxyfarnesyl-L-cysteine http://purl.obolibrary.org/obo/MOD_01110 isoprenylated cysteine A protein modification that effectively converts an L-cysteine residue to S-12-hydroxyfarnesyl-L-cysteine. http://purl.obolibrary.org/obo/MOD_00116 S-diacylglycerol-L-cysteine http://purl.obolibrary.org/obo/MOD_01155 lipoconjugated residue A protein modification that effectively converts an L-cysteine residue to S-diacylglycerol-L-cysteine. http://purl.obolibrary.org/obo/MOD_00117 S-(L-isoglutamyl)-L-cysteine http://purl.obolibrary.org/obo/MOD_02046 crosslinked L-glutamine residue 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. http://purl.obolibrary.org/obo/MOD_00118 2'-(S-L-cysteinyl)-L-histidine http://purl.obolibrary.org/obo/MOD_02048 crosslinked L-histidine residue 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. http://purl.obolibrary.org/obo/MOD_00119 L-lanthionine (Cys-Ser) http://purl.obolibrary.org/obo/MOD_02055 crosslinked L-serine residue A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form L-lanthionine. http://purl.obolibrary.org/obo/MOD_00120 meso-lanthionine http://purl.obolibrary.org/obo/MOD_02055 crosslinked L-serine residue A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form meso-lanthionine. http://purl.obolibrary.org/obo/MOD_00121 (2S,3S,2'R)-3-methyllanthionine http://purl.obolibrary.org/obo/MOD_01981 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. http://purl.obolibrary.org/obo/MOD_00122 3'-(S-L-cysteinyl)-L-tyrosine http://purl.obolibrary.org/obo/MOD_02058 crosslinked L-tyrosine residue 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. http://purl.obolibrary.org/obo/MOD_00123 N6-carboxy-L-lysine http://purl.obolibrary.org/obo/MOD_01152 carboxylated residue A protein modification that effectively converts an L-lysine residue to N6-carboxy-L-lysine. http://purl.obolibrary.org/obo/MOD_00124 N6-1-carboxyethyl-L-lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively converts an L-lysine residue to N6-1-carboxyethyl-L-lysine. http://purl.obolibrary.org/obo/MOD_00125 hypusine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively converts an L-lysine residue to hypusine, N6-(4-amino-2-hydroxybutyl)-L-lysine. http://purl.obolibrary.org/obo/MOD_00129 N6-retinylidene-L-lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively converts an L-lysine residue to N6-retinylidene-L-lysine, the adduct of retinal. http://purl.obolibrary.org/obo/MOD_00130 L-allysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively converts an L-lysine residue to L-allysine. http://purl.obolibrary.org/obo/MOD_00131 L-2-aminoadipic acid http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively converts an L-lysine residue to L-2-aminoadipic acid. http://purl.obolibrary.org/obo/MOD_00132 L-lysinoalanine (Lys-Ser) http://purl.obolibrary.org/obo/MOD_02055 crosslinked L-serine residue 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. http://purl.obolibrary.org/obo/MOD_00134 N6-glycyl-L-lysine http://purl.obolibrary.org/obo/MOD_02051 crosslinked L-lysine residue A protein modification that effectively crosslinks an L-lysine residue and a glycine residue by an isopeptide bond to form N6-glycyl-L-lysine. http://purl.obolibrary.org/obo/MOD_00135 N-(L-isoaspartyl)-glycine (Asn) http://purl.obolibrary.org/obo/MOD_02042 crosslinked L-asparagine residue 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. http://purl.obolibrary.org/obo/MOD_00136 pyruvic acid (Cys) http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to pyruvic acid. http://purl.obolibrary.org/obo/MOD_00137 L-3-phenyllactic acid http://purl.obolibrary.org/obo/MOD_00914 modified L-phenylalanine residue A protein modification that effectively converts an L-phenylalanine residue into L-3-phenyllactic acid. http://purl.obolibrary.org/obo/MOD_00138 2-oxobutanoic acid http://purl.obolibrary.org/obo/MOD_01160 deaminated residue A protein modification that effectively converts an L-threonine residue into 2-oxobutanoic acid. http://purl.obolibrary.org/obo/MOD_00139 N2-succinyl-L-tryptophan http://purl.obolibrary.org/obo/MOD_00918 modified L-tryptophan residue A protein modification that effectively converts an L-tryptophan residue to N2-succinyl-L-tryptophan. http://purl.obolibrary.org/obo/MOD_00140 S-phycocyanobilin-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycocyanobilin. http://purl.obolibrary.org/obo/MOD_00141 S-phycoerythrobilin-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycoerythrobilin. http://purl.obolibrary.org/obo/MOD_00142 S-phytochromobilin-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phytochromobilin. http://purl.obolibrary.org/obo/MOD_00143 heme-bis-L-cysteine http://purl.obolibrary.org/obo/MOD_02067 metal or metal cluster coordinated L-cysteine residue 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. http://purl.obolibrary.org/obo/MOD_00144 heme-L-cysteine http://purl.obolibrary.org/obo/MOD_02067 metal or metal cluster coordinated L-cysteine residue 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. http://purl.obolibrary.org/obo/MOD_00145 tetrakis-L-cysteinyl iron http://purl.obolibrary.org/obo/MOD_02067 metal or metal cluster coordinated L-cysteine residue A protein modification that effectively converts four L-cysteine residues iron atom to tetrakis-L-cysteinyl iron. http://purl.obolibrary.org/obo/MOD_00146 tetrakis-L-cysteinyl diiron disulfide http://purl.obolibrary.org/obo/MOD_02067 metal or metal cluster coordinated L-cysteine residue A protein modification that effectively converts four L-cysteine residues and a two-iron two-sulfur cluster to tetrakis-L-cysteinyl diiron disulfide. http://purl.obolibrary.org/obo/MOD_00147 hexakis-L-cysteinyl triiron trisulfide http://purl.obolibrary.org/obo/MOD_02067 metal or metal cluster coordinated L-cysteine residue A protein modification that effectively converts six L-cysteine residues and a three-iron three-sulfur cluster to hexakis-L-cysteinyl triiron trisulfide. http://purl.obolibrary.org/obo/MOD_00148 tris-L-cysteinyl triiron tetrasulfide http://purl.obolibrary.org/obo/MOD_02067 metal or metal cluster coordinated L-cysteine residue A protein modification that effectively converts three L-cysteine residues and a three-iron four-sulfur cluster to tris-L-cysteinyl triiron tetrasulfide. http://purl.obolibrary.org/obo/MOD_00149 tetrakis-L-cysteinyl tetrairon tetrasulfide http://purl.obolibrary.org/obo/MOD_02067 metal or metal cluster coordinated L-cysteine residue A protein modification that effectively converts four L-cysteine residues and a four-iron four-sulfur cluster to tetrakis-L-cysteinyl tetrairon tetrasulfide. http://purl.obolibrary.org/obo/MOD_00150 L-cysteinyl-L-histidino-homocitryl molybdenum heptairon nonasulfide http://purl.obolibrary.org/obo/MOD_02070 metal or metal cluster coordinated L-histidine residue 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. http://purl.obolibrary.org/obo/MOD_00151 L-cysteinyl molybdopterin http://purl.obolibrary.org/obo/MOD_02067 metal or metal cluster coordinated L-cysteine residue A protein modification that effectively converts an L-cysteine residue to L-cysteinyl molybdopterin. http://purl.obolibrary.org/obo/MOD_00152 S-(8alpha-FAD)-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S'-(8alpha-FAD)-L-cystine. http://purl.obolibrary.org/obo/MOD_00153 3'-(8alpha-FAD)-L-histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively converts an L-histidine residue to 3'-(8alpha-FAD)-L-histidine. http://purl.obolibrary.org/obo/MOD_00154 O4'-(8alpha-FAD)-L-tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively converts an L-tyrosine residue to O4'-(8alpha-FAD)-L-tyrosine. http://purl.obolibrary.org/obo/MOD_00155 L-3',4'-dihydroxyphenylalanine http://purl.obolibrary.org/obo/MOD_00707 hydroxylated tyrosine A protein modification that effectively converts an L-tyrosine residue to L-3',4'-dihydroxyphenylalanine. http://purl.obolibrary.org/obo/MOD_00156 L-2',4',5'-topaquinone http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively converts an L-tyrosine residue to an L-2',4',5'-topaquinone. http://purl.obolibrary.org/obo/MOD_00157 L-tryptophyl quinone http://purl.obolibrary.org/obo/MOD_00918 modified L-tryptophan residue A protein modification that effectively converts an L-tryptophan residue to an L-tryptophan quinone. http://purl.obolibrary.org/obo/MOD_00158 4'-(L-tryptophan)-L-tryptophyl quinone http://purl.obolibrary.org/obo/MOD_02057 crosslinked L-tryptophan residue A protein modification that effectively cross-links two L-tryptophan residues by a carbon-carbon bond to form 4'-(L-tryptophan)-L-tryptophyl quinone. http://purl.obolibrary.org/obo/MOD_00161 S-glucosyl-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-glucosylated L-cysteine. http://purl.obolibrary.org/obo/MOD_00162 O5-glucosylgalactosyl-L-hydroxylysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively converts an L-lysine residue to O5-glucosylgalactosyl-L-hydroxylysine. http://purl.obolibrary.org/obo/MOD_00163 O-(N-acetylamino)galactosyl-L-serine http://purl.obolibrary.org/obo/MOD_01675 O-(N-acetylamino)hexosyl-L-serine A protein modification that effectively converts an L-serine residue to O-(N-acetylaminogalactosyl)-L-serine. http://purl.obolibrary.org/obo/MOD_00165 1'-mannosyl-L-tryptophan http://purl.obolibrary.org/obo/MOD_00918 modified L-tryptophan residue A protein modification that effectively converts an L-tryptophan residue to 1'-mannosyl-L-tryptophan. http://purl.obolibrary.org/obo/MOD_00166 O4'-glucosyl-L-tyrosine http://purl.obolibrary.org/obo/MOD_01927 O-glycosyl-L-tyrosine A protein modification that effectively converts an L-tyrosine residue to O4'-glucosyl-tyrosine. http://purl.obolibrary.org/obo/MOD_00168 N-aspartyl-glycosylphosphatidylinositolethanolamine http://purl.obolibrary.org/obo/MOD_00904 modified L-aspartic acid residue A protein modification that effectively converts an L-aspartic acid residue to N-(aspart-1-yl)-glycosylphosphatidylinositolethanolamine. http://purl.obolibrary.org/obo/MOD_00169 N-cysteinyl-glycosylphosphatidylinositolethanolamine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to N-cysteinyl-glycosylphosphatidylinositolethanolamine. http://purl.obolibrary.org/obo/MOD_00170 N-glycyl-glycosylphosphatidylinositolethanolamine http://purl.obolibrary.org/obo/MOD_00908 modified glycine residue A protein modification that effectively converts a glycine residue to N-glycyl-glycosylphosphatidylinositolethanolamine. http://purl.obolibrary.org/obo/MOD_00171 N-seryl-glycosylphosphatidylinositolethanolamine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to N-seryl-glycosylphosphatidylinositolethanolamine. http://purl.obolibrary.org/obo/MOD_00172 N-alanyl-glycosylphosphatidylinositolethanolamine http://purl.obolibrary.org/obo/MOD_00901 modified L-alanine residue A protein modification that effectively converts an L-alanine residue to N-alanyl-glycosylphosphatidylinositolethanolamine. http://purl.obolibrary.org/obo/MOD_00173 N-threonyl-glycosylphosphatidylinositolethanolamine http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue A protein modification that effectively converts an L-threonine residue to N-threonyl-glycosylphosphatidylinositolethanolamine. http://purl.obolibrary.org/obo/MOD_00174 N-glycyl-glycosylsphingolipidinositolethanolamine http://purl.obolibrary.org/obo/MOD_00908 modified glycine residue A protein modification that effectively converts a glycine residue to N-glycyl-glycosylsphingolipidinositolethanolamine. http://purl.obolibrary.org/obo/MOD_00175 N-seryl-glycosylsphingolipidinositolethanolamine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to N-seryl-glycosylsphingolipidinositolethanolamine. http://purl.obolibrary.org/obo/MOD_00176 O-(phosphoribosyl dephospho-coenzyme A)-L-serine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to O-(phosphoribosyl dephospho-coenzyme A)-L-serine. http://purl.obolibrary.org/obo/MOD_00177 omega-N-(ADP-ribosyl)-L-arginine http://purl.obolibrary.org/obo/MOD_00902 modified L-arginine residue A protein modification that effectively converts an L-argininine residue to omega-N-(ADP-ribosyl)-L-arginine. http://purl.obolibrary.org/obo/MOD_00178 S-(ADP-ribosyl)-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-(ADP-ribosyl)-L-cysteine. http://purl.obolibrary.org/obo/MOD_00179 L-glutamyl 5-glycerylphosphorylethanolamine http://purl.obolibrary.org/obo/MOD_00906 modified L-glutamic acid residue A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl 5-glycerylphosphorylethanolamine. http://purl.obolibrary.org/obo/MOD_00180 S-sulfo-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-sulfo-L-cysteine. http://purl.obolibrary.org/obo/MOD_00181 O4'-sulfo-L-tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively converts an L-tyrosine residue to O4'-sulfo-L-tyrosine. http://purl.obolibrary.org/obo/MOD_00182 L-bromohistidine http://purl.obolibrary.org/obo/MOD_01912 monobrominated residue A protein modification that effectively converts an L-histidine residue to L-bromohistidine. http://purl.obolibrary.org/obo/MOD_00183 L-2'-bromophenylalanine http://purl.obolibrary.org/obo/MOD_00972 monobrominated L-phenylalanine A protein modification that effectively converts an L-phenylalanine residue to L-2'-bromophenylalanine. http://purl.obolibrary.org/obo/MOD_00184 L-3'-bromophenylalanine http://purl.obolibrary.org/obo/MOD_00972 monobrominated L-phenylalanine A protein modification that effectively converts an L-phenylalanine residue to L-3'-bromophenylalanine. http://purl.obolibrary.org/obo/MOD_00185 L-4'-bromophenylalanine http://purl.obolibrary.org/obo/MOD_00972 monobrominated L-phenylalanine A protein modification that effectively converts an L-phenylalanine residue to L-4'-bromophenylalanine. http://purl.obolibrary.org/obo/MOD_00186 3,3',5-triiodo-L-thyronine http://purl.obolibrary.org/obo/MOD_00998 iodinated tyrosine A protein modification that effectively substitutes an L-tyrosine residue with 3,3',5-triiodo-L-thyronine. http://purl.obolibrary.org/obo/MOD_00187 L-thyroxine http://purl.obolibrary.org/obo/MOD_00998 iodinated tyrosine A protein modification that effectively substitutes an L-tyrosine residue with L-thyroxine. http://purl.obolibrary.org/obo/MOD_00188 6'-bromo-L-tryptophan http://purl.obolibrary.org/obo/MOD_01912 monobrominated residue A protein modification that effectively converts an L-tryptophan residue to 6'-bromo-L-tryptophan. http://purl.obolibrary.org/obo/MOD_00189 dehydroalanine (Ser) http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to dehydroalanine. http://purl.obolibrary.org/obo/MOD_00190 dehydrobutyrine (Thr) http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue A protein modification that effectively converts an L-threonine residue to dehydrobutyrine. http://purl.obolibrary.org/obo/MOD_00191 (Z)-2,3-didehydrotyrosine http://purl.obolibrary.org/obo/MOD_00706 dehydrogenated tyrosine A protein modification that effectively converts L-tyrosine to (Z)-2,3-didehydrotyrosine. http://purl.obolibrary.org/obo/MOD_00192 L-serine 5-imidazolinone glycine http://purl.obolibrary.org/obo/MOD_02055 crosslinked L-serine residue A protein modification that effectively crosslinks an L-serine residue and a glycine residue to form L-serine 5-imidazolinone glycine. http://purl.obolibrary.org/obo/MOD_00193 L-3-oxoalanine (Cys) http://purl.obolibrary.org/obo/MOD_01169 L-3-oxoalanine A protein modification that effectively converts an L-cysteine residue to L-oxoalanine. http://purl.obolibrary.org/obo/MOD_00194 lactic acid http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to an amino-terminal lactic acid. http://purl.obolibrary.org/obo/MOD_00195 L-alanine 5-imidazolinone glycine http://purl.obolibrary.org/obo/MOD_02047 crosslinked glycine residue A protein modification that effectively crosslinks an L-alanine residue and a glycine residue to form L-alanine 5-imidazolinone glycine. http://purl.obolibrary.org/obo/MOD_00196 L-cysteine 5-imidazolinone glycine http://purl.obolibrary.org/obo/MOD_02047 crosslinked glycine residue A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue to form L-cysteine 5-imidazolinone glycine. http://purl.obolibrary.org/obo/MOD_00197 2-imino-glutamine 5-imidazolinone glycine http://purl.obolibrary.org/obo/MOD_02047 crosslinked glycine residue A protein modification that effectively crosslinks an L-glutamine residue and a glycine residue to form 2-imino-glutamine 5-imidazolinone glycine. http://purl.obolibrary.org/obo/MOD_00198 D-alanine (Ala) http://purl.obolibrary.org/obo/MOD_00901 modified L-alanine residue A protein modification that effectively converts an L-alanine residue to D-alanine. http://purl.obolibrary.org/obo/MOD_00199 D-allo-isoleucine http://purl.obolibrary.org/obo/MOD_00910 modified L-isoleucine residue A protein modification that effectively converts an L-isoleucine residue to a D-allo-isoleucine. http://purl.obolibrary.org/obo/MOD_00200 D-methionine http://purl.obolibrary.org/obo/MOD_00913 modified L-methionine residue A protein modification that effectively converts an L-methionine residue to D-methionine. http://purl.obolibrary.org/obo/MOD_00201 D-phenylalanine http://purl.obolibrary.org/obo/MOD_00914 modified L-phenylalanine residue A protein modification that effectively converts an L-phenylalanine residue to D-phenylalanine. http://purl.obolibrary.org/obo/MOD_00202 D-serine (Ser) http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to D-serine. http://purl.obolibrary.org/obo/MOD_00203 D-asparagine http://purl.obolibrary.org/obo/MOD_00903 modified L-asparagine residue A protein modification that effectively converts an L-asparagine residue to D-asparagine. http://purl.obolibrary.org/obo/MOD_00204 D-leucine http://purl.obolibrary.org/obo/MOD_00911 modified L-leucine residue A protein modification that effectively converts an L-leucine residue to D-leucine. http://purl.obolibrary.org/obo/MOD_00205 D-tryptophan http://purl.obolibrary.org/obo/MOD_00918 modified L-tryptophan residue A protein modification that effectively converts an L-tryptophan residue to D-tryptophan. http://purl.obolibrary.org/obo/MOD_00206 L-isoglutamyl-polyglycine http://purl.obolibrary.org/obo/MOD_00906 modified L-glutamic acid residue A protein modification that effectively converts an L-glutamic acid residue to L-isoglutamyl-polyglycine. http://purl.obolibrary.org/obo/MOD_00207 L-isoglutamyl-polyglutamic acid http://purl.obolibrary.org/obo/MOD_00906 modified L-glutamic acid residue A protein modification that effectively converts an L-glutamic acid residue to isoglutamyl-polyglutamic acid, forming an isopeptide bond with a polyglutamic acid. http://purl.obolibrary.org/obo/MOD_00208 O4'-(phospho-5'-adenosine)-L-tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue 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. http://purl.obolibrary.org/obo/MOD_00209 S-(2-aminovinyl)-D-cysteine (Cys-Ser) http://purl.obolibrary.org/obo/MOD_02055 crosslinked L-serine residue 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. http://purl.obolibrary.org/obo/MOD_00210 L-cysteine sulfenic acid http://purl.obolibrary.org/obo/MOD_01854 sulfur monooxygenated residue A protein modification that effectively monooxygenates an L-cysteine residue to L-cysteine sulfenic acid. http://purl.obolibrary.org/obo/MOD_00211 S-(glycyl)-L-cysteine (Cys-Gly) http://purl.obolibrary.org/obo/MOD_02047 crosslinked glycine residue A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue by a thioester bond to form S-glycyl-L-cysteine. http://purl.obolibrary.org/obo/MOD_00212 S-4-hydroxycinnamyl-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-4-hydroxycinnamyl-L-cysteine. http://purl.obolibrary.org/obo/MOD_00214 dermatan 4-sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine http://purl.obolibrary.org/obo/MOD_00002 O-glycosyl-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. http://purl.obolibrary.org/obo/MOD_00216 N6-formyl-L-lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively converts an L-lysine residue to N6-formyl-L-lysine. http://purl.obolibrary.org/obo/MOD_00217 O4-arabinosyl-L-hydroxyproline http://purl.obolibrary.org/obo/MOD_00915 modified L-proline residue A protein modification that effectively converts an L-proline residue to O4-arabinosyl-L-hydroxyproline. http://purl.obolibrary.org/obo/MOD_00218 O-(phospho-5'-RNA)-L-serine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue 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. http://purl.obolibrary.org/obo/MOD_00220 4-hydroxy-L-arginine http://purl.obolibrary.org/obo/MOD_00682 hydroxylated arginine A protein modification that effectively converts an L-arginine residue to a 4-hydroxy-L-arginine. http://purl.obolibrary.org/obo/MOD_00221 N-(L-isoaspartyl)-L-cysteine http://purl.obolibrary.org/obo/MOD_02044 crosslinked L-cysteine residue A protein modification that effectively crosslinks L-aspartic acid and L-cysteine residues via an isopeptide bond to form N-(L-isoaspartyl)-L-cysteine. http://purl.obolibrary.org/obo/MOD_00223 N6-mureinyl-L-lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively converts an L-lysine residue to N6-mureinyl-L-lysine. http://purl.obolibrary.org/obo/MOD_00224 1-chondroitin sulfate-L-aspartic acid ester http://purl.obolibrary.org/obo/MOD_00904 modified L-aspartic acid residue A protein modification that effectively converts an L-aspartic acid residue to 1-chondroitin sulfate-L-aspartic acid ester http://purl.obolibrary.org/obo/MOD_00225 S-(6-FMN)-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-(6-FMN)-L-cysteine. http://purl.obolibrary.org/obo/MOD_00226 1'-(8alpha-FAD)-L-histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively converts an L-histidine residue to 1'-(8alpha-FAD)-L-histidine. http://purl.obolibrary.org/obo/MOD_00227 omega-N-phospho-L-arginine http://purl.obolibrary.org/obo/MOD_00902 modified L-arginine residue A protein modification that effectively converts an L-arginine residue to omega-N-phospho-L-arginine. http://purl.obolibrary.org/obo/MOD_00228 S-diphytanylglycerol diether-L-cysteine http://purl.obolibrary.org/obo/MOD_01155 lipoconjugated residue A protein modification that effectively converts an L-cysteine residue to S-diphytanylglycerol diether-L-cysteine. http://purl.obolibrary.org/obo/MOD_00229 alpha-1-microglobulin-Ig alpha complex chromophore http://purl.obolibrary.org/obo/MOD_02044 crosslinked L-cysteine residue A protein modification that effectively converts two L-cysteine residues to form alpha-1-microglobulin-Ig alpha complex chromophore. http://purl.obolibrary.org/obo/MOD_00230 bis-L-cysteinyl bis-L-histidino diiron disulfide http://purl.obolibrary.org/obo/MOD_02070 metal or metal cluster coordinated L-histidine residue 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. http://purl.obolibrary.org/obo/MOD_00231 hexakis-L-cysteinyl hexairon hexasulfide http://purl.obolibrary.org/obo/MOD_02067 metal or metal cluster coordinated L-cysteine residue A protein modification that effectively converts six L-cysteine residues and a six-iron six-sulfur cluster to hexakis-L-cysteinyl hexairon hexasulfide. http://purl.obolibrary.org/obo/MOD_00232 N6-(phospho-5'-adenosine)-L-lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue 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. http://purl.obolibrary.org/obo/MOD_00233 N6-(phospho-5'-guanosine)-L-lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue 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. http://purl.obolibrary.org/obo/MOD_00234 L-cysteine glutathione disulfide http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-glutathionyl-L-cysteine. http://purl.obolibrary.org/obo/MOD_00236 N4-(ADP-ribosyl)-L-asparagine http://purl.obolibrary.org/obo/MOD_00903 modified L-asparagine residue A protein modification that effectively converts an L-asparagine residue to N4-(ADP-ribosyl)-L-asparagine. http://purl.obolibrary.org/obo/MOD_00238 5'-(N6-L-lysine)-L-topaquinone http://purl.obolibrary.org/obo/MOD_02058 crosslinked L-tyrosine residue 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. http://purl.obolibrary.org/obo/MOD_00239 S-methyl-L-cysteine http://purl.obolibrary.org/obo/MOD_01682 monomethylated L-cysteine A protein modification that effectively converts an L-cysteine residue to S-methyl-L-cysteine. http://purl.obolibrary.org/obo/MOD_00240 4-hydroxy-L-lysine http://purl.obolibrary.org/obo/MOD_01047 monohydroxylated lysine A protein modification that effectively converts an L-lysine residue to 4-hydroxy-L-lysine. http://purl.obolibrary.org/obo/MOD_00241 N4-hydroxymethyl-L-asparagine http://purl.obolibrary.org/obo/MOD_00903 modified L-asparagine residue A protein modification that effectively converts an L-asparagine residue to N4-hydroxymethyl-L-asparagine. http://purl.obolibrary.org/obo/MOD_00242 O-(ADP-ribosyl)-L-serine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to O-(ADP-ribosyl)-L-serine. http://purl.obolibrary.org/obo/MOD_00243 L-cysteine oxazole-4-carboxylic acid http://purl.obolibrary.org/obo/MOD_02044 crosslinked L-cysteine residue A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-cysteine oxazole-4-carboxylic acid. http://purl.obolibrary.org/obo/MOD_00244 L-cysteine oxazoline-4-carboxylic acid http://purl.obolibrary.org/obo/MOD_02044 crosslinked L-cysteine residue A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-cysteine oxazoline-4-carboxylic acid. http://purl.obolibrary.org/obo/MOD_00245 glycine oxazole-4-carboxylic acid http://purl.obolibrary.org/obo/MOD_02047 crosslinked glycine residue A protein modification that effectively crosslinks a glycine residue and an L-serine residue to form glycine oxazole-4-carboxylic acid. http://purl.obolibrary.org/obo/MOD_00246 glycine thiazole-4-carboxylic acid http://purl.obolibrary.org/obo/MOD_02047 crosslinked glycine residue A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue to form glycine thiazole-4-carboxylic acid. http://purl.obolibrary.org/obo/MOD_00247 L-serine thiazole-4-carboxylic acid http://purl.obolibrary.org/obo/MOD_02055 crosslinked L-serine residue A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-serine thiazole-4-carboxylic acid. http://purl.obolibrary.org/obo/MOD_00248 L-phenylalanine thiazole-4-carboxylic acid http://purl.obolibrary.org/obo/MOD_02053 crosslinked L-phenylalanine residue A protein modification that effectively crosslinks an L-cysteine residue and an L-phenylalanine residue to form L-phenylalanine thiazole-4-carboxylic acid. http://purl.obolibrary.org/obo/MOD_00249 L-cysteine thiazole-4-carboxylic acid http://purl.obolibrary.org/obo/MOD_01420 thiazole/thiazoline ring crosslinked residues A protein modification that effectively crosslinks two L-cysteine residues to form L-cysteine thiazole-4-carboxylic acid. http://purl.obolibrary.org/obo/MOD_00250 L-lysine thiazole-4-carboxylic acid http://purl.obolibrary.org/obo/MOD_02051 crosslinked L-lysine residue A protein modification that effectively crosslinks an L-cysteine residue and an L-lysine residue to form L-lysine thiazole-4-carboxylic acid. http://purl.obolibrary.org/obo/MOD_00251 O-(phospho-5'-DNA)-L-serine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue 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. http://purl.obolibrary.org/obo/MOD_00252 keratan sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-threonine http://purl.obolibrary.org/obo/MOD_00005 O-glycosyl-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. http://purl.obolibrary.org/obo/MOD_00253 L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide) (Sec) http://purl.obolibrary.org/obo/MOD_01158 modified L-selenocysteine residue A protein modification that effectively converts an L-selenocysteine residue to L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide). http://purl.obolibrary.org/obo/MOD_00254 O4'-(phospho-5'-RNA)-L-tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue 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. http://purl.obolibrary.org/obo/MOD_00255 3-(3'-L-histidyl)-L-tyrosine http://purl.obolibrary.org/obo/MOD_02058 crosslinked L-tyrosine residue 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. http://purl.obolibrary.org/obo/MOD_00256 L-methionine sulfone http://purl.obolibrary.org/obo/MOD_01855 sulfur dioxygenated residue A protein modification that dioxygenates an L-methionine residue to L-methionine sulfone. http://purl.obolibrary.org/obo/MOD_00257 dipyrrolylmethanemethyl-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to dipyrrolylmethanemethyl-L-cysteine. http://purl.obolibrary.org/obo/MOD_00258 S-(2-aminovinyl)-3-methyl-D-cysteine http://purl.obolibrary.org/obo/MOD_02056 crosslinked L-threonine residue 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. http://purl.obolibrary.org/obo/MOD_00259 O4'-(phospho-5'-DNA)-L-tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue 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. http://purl.obolibrary.org/obo/MOD_00260 O-(phospho-5'-DNA)-L-threonine http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue 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. http://purl.obolibrary.org/obo/MOD_00261 O4'-(phospho-5'-uridine)-L-tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue 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. http://purl.obolibrary.org/obo/MOD_00262 N-(L-glutamyl)-L-tyrosine http://purl.obolibrary.org/obo/MOD_02045 crosslinked L-glutamic acid residue A protein modification that effectively forms a peptide bond between a C-terminal L-glutamic acid residue and a free L-tyrosine. http://purl.obolibrary.org/obo/MOD_00263 S-phycoviolobilin-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycoviolobilin. http://purl.obolibrary.org/obo/MOD_00264 phycoerythrobilin-bis-L-cysteine http://purl.obolibrary.org/obo/MOD_02044 crosslinked L-cysteine residue A protein modification that effectively results from forming an adduct between two cysteine residues and the tetrapyrrole compound phycoerythrobilin. http://purl.obolibrary.org/obo/MOD_00265 phycourobilin-bis-L-cysteine http://purl.obolibrary.org/obo/MOD_02044 crosslinked L-cysteine residue A protein modification that effectively results from forming an adduct between two cysteine residues and the tetrapyrrole compound phycourobilin. http://purl.obolibrary.org/obo/MOD_00266 N-L-glutamyl-poly-L-glutamic acid http://purl.obolibrary.org/obo/MOD_00906 modified L-glutamic acid residue 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. http://purl.obolibrary.org/obo/MOD_00267 L-cysteine sulfinic acid http://purl.obolibrary.org/obo/MOD_01855 sulfur dioxygenated residue A protein modification that effectively dioxygenates an L-cysteine residue to L-cysteine sulfinic acid. http://purl.obolibrary.org/obo/MOD_00268 L-3',4',5'-trihydroxyphenylalanine http://purl.obolibrary.org/obo/MOD_00707 hydroxylated tyrosine A protein modification that effectively converts an L-tyrosine residue to L-3',4',5'-trihydroxyphenylalanine. http://purl.obolibrary.org/obo/MOD_00269 O-(sn-1-glycerophosphoryl)-L-serine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to O-(sn-1-glycerophosphoryl)-L-serine. http://purl.obolibrary.org/obo/MOD_00270 1-thioglycine (internal) http://purl.obolibrary.org/obo/MOD_01625 1-thioglycine A protein modification that effectively converts a glycine residue to an internal 1-thioglycine. http://purl.obolibrary.org/obo/MOD_00271 heme P460-bis-L-cysteine-L-tyrosine http://purl.obolibrary.org/obo/MOD_02075 metal or metal cluster coordinated L-tyrosine residue 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. http://purl.obolibrary.org/obo/MOD_00272 O-(phospho-5'-adenosine)-L-threonine http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue 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. http://purl.obolibrary.org/obo/MOD_00273 tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino tetrairon disulfide trioxide http://purl.obolibrary.org/obo/MOD_02070 metal or metal cluster coordinated L-histidine residue 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. http://purl.obolibrary.org/obo/MOD_00274 L-cysteine persulfide http://purl.obolibrary.org/obo/MOD_01886 thiolated residue 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. http://purl.obolibrary.org/obo/MOD_00275 3'-(1'-L-histidyl)-L-tyrosine http://purl.obolibrary.org/obo/MOD_02058 crosslinked L-tyrosine residue 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. http://purl.obolibrary.org/obo/MOD_00276 heme P460-bis-L-cysteine-L-lysine http://purl.obolibrary.org/obo/MOD_02074 metal or metal cluster coordinated L-lysine residue 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. http://purl.obolibrary.org/obo/MOD_00277 5-methyl-L-arginine http://purl.obolibrary.org/obo/MOD_00414 monomethylated L-arginine A protein modification that effectively converts an L-arginine residue to 5-methyl-L-arginine. http://purl.obolibrary.org/obo/MOD_00278 2-methyl-L-glutamine http://purl.obolibrary.org/obo/MOD_00722 monomethylated L-glutamine A protein modification that effectively converts an L-glutamine residue to 2-methyl-L-glutamine. http://purl.obolibrary.org/obo/MOD_00279 N-pyruvic acid 2-iminyl-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to N-pyruvic acid 2-iminyl-L-cysteine. http://purl.obolibrary.org/obo/MOD_00280 N-pyruvic acid 2-iminyl-L-valine http://purl.obolibrary.org/obo/MOD_00920 modified L-valine residue A protein modification that effectively converts an L-valine residue to N-pyruvic acid 2-iminyl-L-valine. http://purl.obolibrary.org/obo/MOD_00281 3'-heme-L-histidine http://purl.obolibrary.org/obo/MOD_02070 metal or metal cluster coordinated L-histidine residue 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. http://purl.obolibrary.org/obo/MOD_00282 S-selenyl-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-selenyl-L-cysteine. http://purl.obolibrary.org/obo/MOD_00283 N6-propylamino-poly(propylmethylamino)-propyldimethylamine-L-lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively converts an L-lysine residue to an N6-propylamino-poly(propylmethylamino)-propyldimethylamine-L-lysine. http://purl.obolibrary.org/obo/MOD_00284 dihydroxyheme-L-aspartate ester-L-glutamate ester http://purl.obolibrary.org/obo/MOD_02068 metal or metal cluster coordinated L-glutamic acid residue 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. http://purl.obolibrary.org/obo/MOD_00285 dihydroxyheme-L-aspartate ester-L-glutamate ester-L-methionine sulfonium http://purl.obolibrary.org/obo/MOD_02071 metal or metal cluster coordinated L-methionine residue 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. http://purl.obolibrary.org/obo/MOD_00286 L-cysteinyl molybdenum bis(molybdopterin guanine dinucleotide) http://purl.obolibrary.org/obo/MOD_02067 metal or metal cluster coordinated L-cysteine residue A protein modification that effectively converts an L-cysteine residue to L-cysteinyl molybdenum bis(molybdopterin guanine dinucleotide). http://purl.obolibrary.org/obo/MOD_00287 (2S,3R,4S)-3,4-dihydroxyproline http://purl.obolibrary.org/obo/MOD_00866 dihydroxylated proline A protein modification that effectively converts an L-proline residue to a (2S,3R,4S)-3,4-dihydroxyproline. http://purl.obolibrary.org/obo/MOD_00288 pyrroloquinoline quinone http://purl.obolibrary.org/obo/MOD_02058 crosslinked L-tyrosine residue 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. http://purl.obolibrary.org/obo/MOD_00289 tris-L-cysteinyl L-N1'-histidino tetrairon tetrasulfide http://purl.obolibrary.org/obo/MOD_02070 metal or metal cluster coordinated L-histidine residue 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. http://purl.obolibrary.org/obo/MOD_00290 tris-L-cysteinyl L-N3'-histidino tetrairon tetrasulfide http://purl.obolibrary.org/obo/MOD_02070 metal or metal cluster coordinated L-histidine residue 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. http://purl.obolibrary.org/obo/MOD_00291 tris-L-cysteinyl L-aspartato tetrairon tetrasulfide http://purl.obolibrary.org/obo/MOD_02067 metal or metal cluster coordinated L-cysteine residue 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. http://purl.obolibrary.org/obo/MOD_00292 N6-pyruvic acid 2-iminyl-L-lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively converts an L-lysine residue to N6-pyruvic acid 2-iminyl-L-lysine. http://purl.obolibrary.org/obo/MOD_00293 tris-L-cysteinyl L-serinyl tetrairon tetrasulfide http://purl.obolibrary.org/obo/MOD_02072 metal or metal cluster coordinated L-serine residue 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. http://purl.obolibrary.org/obo/MOD_00294 bis-L-cysteinyl L-N3'-histidino L-serinyl tetrairon tetrasulfide http://purl.obolibrary.org/obo/MOD_02072 metal or metal cluster coordinated L-serine residue 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. http://purl.obolibrary.org/obo/MOD_00296 O-D-glucuronosyl-L-serine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to O-D-glucuronosyl-L-serine. http://purl.obolibrary.org/obo/MOD_00297 tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino nickel triiron disulfide trioxide http://purl.obolibrary.org/obo/MOD_02070 metal or metal cluster coordinated L-histidine residue 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. http://purl.obolibrary.org/obo/MOD_00298 tris-L-cysteinyl L-cysteine persulfido L-glutamato L-histidino L-serinyl nickel triiron disulfide trioxide http://purl.obolibrary.org/obo/MOD_02072 metal or metal cluster coordinated L-serine residue 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. http://purl.obolibrary.org/obo/MOD_00299 N6-(L-isoaspartyl)-L-lysine (Asn) http://purl.obolibrary.org/obo/MOD_02042 crosslinked L-asparagine residue 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. http://purl.obolibrary.org/obo/MOD_00301 O-(N-acetylglucosamine-1-phosphoryl)-L-serine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to O-(N-acetylglucosamine-1-phosphoryl)-L-serine. http://purl.obolibrary.org/obo/MOD_00302 O-(phosphoglycosyl-D-mannose-1-phosphoryl)-L-serine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to O-(phosphoglycosyl-D-mannose-1-phosphoryl)-L-serine. http://purl.obolibrary.org/obo/MOD_00303 heptakis-L-histidino tetracopper mu4-sulfide hydroxide http://purl.obolibrary.org/obo/MOD_02070 metal or metal cluster coordinated L-histidine residue 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. http://purl.obolibrary.org/obo/MOD_00304 L-leucine methyl ester http://purl.obolibrary.org/obo/MOD_00599 monomethylated residue A protein modification that effectively converts an L-leucine residue to L-leucine methyl ester. http://purl.obolibrary.org/obo/MOD_00305 hexakis-L-cysteinyl L-serinyl octairon heptasulfide http://purl.obolibrary.org/obo/MOD_02072 metal or metal cluster coordinated L-serine residue 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. http://purl.obolibrary.org/obo/MOD_00306 residues isobaric at 113.084064 Da http://purl.obolibrary.org/obo/MOD_00624 residues isobaric at 113.0-113.1 Da Natural or modified residues with a mass of 113.084064 Da. http://purl.obolibrary.org/obo/MOD_00307 L-aspartimide http://purl.obolibrary.org/obo/MOD_00903 modified L-asparagine residue A protein modification that effectively cyclizes an L-asparagine residue to form a carboxyl-terminal L-aspartimide. http://purl.obolibrary.org/obo/MOD_00308 L-glutamimide http://purl.obolibrary.org/obo/MOD_00907 modified L-glutamine residue A protein modification that effectively cyclizes an L-glutamine residue to form a carboxyl-terminal L-glutamimide. http://purl.obolibrary.org/obo/MOD_00309 L-beta-carboxyaspartic acid http://purl.obolibrary.org/obo/MOD_01152 carboxylated residue A protein modification that effectively converts an L-aspartic acid residue to L-beta-carboxyaspartic acid. http://purl.obolibrary.org/obo/MOD_00310 N5-methyl-L-arginine http://purl.obolibrary.org/obo/MOD_00414 monomethylated L-arginine A protein modification that effectively converts an L-arginine residue to N5-methyl-L-arginine. http://purl.obolibrary.org/obo/MOD_00311 L-cysteine coenzyme A disulfide http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to L-cysteine coenzyme A disulfide. http://purl.obolibrary.org/obo/MOD_00312 S-myristoyl-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-myristoyl-L-cysteine. http://purl.obolibrary.org/obo/MOD_00313 S-palmitoleyl-L-cysteine http://purl.obolibrary.org/obo/MOD_02002 S-palmitoleylated residue A protein modification that effectively converts an L-cysteine residue to S-palmitoleyl-L-cysteine. http://purl.obolibrary.org/obo/MOD_00315 pentakis-L-cysteinyl L-histidino nickel tetrairon pentasulfide http://purl.obolibrary.org/obo/MOD_02070 metal or metal cluster coordinated L-histidine residue 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. http://purl.obolibrary.org/obo/MOD_00316 N4,N4-dimethyl-L-asparagine http://purl.obolibrary.org/obo/MOD_00673 methylated asparagine A protein modification that effectively converts an L-asparagine residue to N4,N4-dimethyl-L-asparagine. http://purl.obolibrary.org/obo/MOD_00317 N6-3,4-didehydroretinylidene-L-lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively converts an L-lysine residue to N6-3,4-didehydroretinylidene-L-lysine. http://purl.obolibrary.org/obo/MOD_00318 4'-(S-L-cysteinyl)-L-tryptophyl quinone http://purl.obolibrary.org/obo/MOD_02057 crosslinked L-tryptophan residue 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. http://purl.obolibrary.org/obo/MOD_00319 3-(S-L-cysteinyl)-L-aspartic acid http://purl.obolibrary.org/obo/MOD_02043 crosslinked L-aspartic acid residue 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. http://purl.obolibrary.org/obo/MOD_00320 4-(S-L-cysteinyl)-L-glutamic acid http://purl.obolibrary.org/obo/MOD_02045 crosslinked L-glutamic acid residue 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. http://purl.obolibrary.org/obo/MOD_00321 cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid L-aspartate ester http://purl.obolibrary.org/obo/MOD_01155 lipoconjugated residue A protein modification that effectively converts an L-aspartic acid residue to cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid L-aspartate ester. http://purl.obolibrary.org/obo/MOD_00322 1'-methyl-L-histidine http://purl.obolibrary.org/obo/MOD_02038 monomethylated L-histidine A protein modification that effectively converts an L-histidine residue to tele-methyl-L-histidine. http://purl.obolibrary.org/obo/MOD_00323 L-lysine methyl ester http://purl.obolibrary.org/obo/MOD_01683 monomethylated L-lysine A protein modification that effectively converts an L-lysine residue to L-lysine methyl ester. http://purl.obolibrary.org/obo/MOD_00324 L-serinyl molybdenum bis(molybdopterin guanine dinucleotide) http://purl.obolibrary.org/obo/MOD_02072 metal or metal cluster coordinated L-serine residue A protein modification that effectively converts an L-serine residue to L-serinyl molybdenum bis(molybdopterin guanine dinucleotide). http://purl.obolibrary.org/obo/MOD_00325 L-beta-methylthioasparagine http://purl.obolibrary.org/obo/MOD_00903 modified L-asparagine residue A protein modification that effectively converts an L-asparagine residue to L-beta-methylthioasparagine. http://purl.obolibrary.org/obo/MOD_00326 L-pyrrolysine (Lys) http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively converts an L-lysine residue to L-pyrrolysine (not known as a natural, post-translational modification process). http://purl.obolibrary.org/obo/MOD_00327 3-hydroxy-L-tryptophan http://purl.obolibrary.org/obo/MOD_01622 monohydroxylated tryptophan A protein modification that effectively converts an L-tryptophan residue to a 3-hydroxy-L-tryptophan. http://purl.obolibrary.org/obo/MOD_00328 O4'-(phospho-3'-DNA)-L-tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue 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. http://purl.obolibrary.org/obo/MOD_00329 hydroxyheme-L-glutamate ester http://purl.obolibrary.org/obo/MOD_02068 metal or metal cluster coordinated L-glutamic acid residue 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. http://purl.obolibrary.org/obo/MOD_00330 (phospho-5'-guanosine)-L-histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively converts an L-histidine residue to a (phospho-5'-guanosine)-L-histidine. http://purl.obolibrary.org/obo/MOD_00331 tetrakis-L-cysteinyl triiron tetrasulfide http://purl.obolibrary.org/obo/MOD_02067 metal or metal cluster coordinated L-cysteine residue A protein modification that effectively converts four L-cysteine residues and a three-iron four-sulfur cluster to tetrakis-L-cysteinyl triiron tetrasulfide. http://purl.obolibrary.org/obo/MOD_00332 omega-N-glucosyl-L-arginine http://purl.obolibrary.org/obo/MOD_01980 omega-N-glycosyl-L-arginine A protein modification that effectively converts an L-arginine residue to N4-glucosyl-arginine. http://purl.obolibrary.org/obo/MOD_00333 (3-aminopropyl)(L-aspartyl-1-amino)phosphoryl-5'-adenosine http://purl.obolibrary.org/obo/MOD_00903 modified L-asparagine residue A protein modification that effectively converts an L-asparagine residue to (3-aminopropyl)(L-aspartyl-1-amino)phosphoryl-5'-adenosine. http://purl.obolibrary.org/obo/MOD_00334 1'-heme-L-histidine http://purl.obolibrary.org/obo/MOD_02070 metal or metal cluster coordinated L-histidine residue 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. http://purl.obolibrary.org/obo/MOD_00335 (2S,3S,2'R)-3-methyllanthionine sulfoxide http://purl.obolibrary.org/obo/MOD_02056 crosslinked L-threonine residue 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. http://purl.obolibrary.org/obo/MOD_00336 tris-L-cysteinyl L-aspartato diiron disulfide http://purl.obolibrary.org/obo/MOD_02067 metal or metal cluster coordinated L-cysteine residue 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. http://purl.obolibrary.org/obo/MOD_00337 S-carbamoyl-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-carbamoyl-L-cysteine. http://purl.obolibrary.org/obo/MOD_00338 S-cyano-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-cyano-L-cysteine. http://purl.obolibrary.org/obo/MOD_00339 L-cysteinyl hydrogenase diiron subcluster http://purl.obolibrary.org/obo/MOD_02067 metal or metal cluster coordinated L-cysteine residue A protein modification that effectively converts an L-cysteine residue to L-cysteinyl hydrogenase diiron subcluster. http://purl.obolibrary.org/obo/MOD_00340 S-amidino-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-amidino-L-cysteine. http://purl.obolibrary.org/obo/MOD_00341 N-methyl-L-isoleucine http://purl.obolibrary.org/obo/MOD_01680 alpha-amino monomethylated residue A protein modification that effectively converts an L-isoleucine residue to N-methyl-L-isoleucine. http://purl.obolibrary.org/obo/MOD_00342 N-methyl-L-leucine http://purl.obolibrary.org/obo/MOD_01808 N-methylated leucine A protein modification that effectively converts an L-leucine residue to N-methyl-L-leucine. http://purl.obolibrary.org/obo/MOD_00343 N-methyl-L-tyrosine http://purl.obolibrary.org/obo/MOD_01680 alpha-amino monomethylated residue A protein modification that effectively converts an L-tyrosine residue to N-methyl-L-tyrosine. http://purl.obolibrary.org/obo/MOD_00344 N-palmitoylglycine http://purl.obolibrary.org/obo/MOD_00908 modified glycine residue A protein modification that effectively converts a glycine residue to N-palmitoylglycine. http://purl.obolibrary.org/obo/MOD_00345 2-(S-L-cysteinyl)-L-phenylalanine http://purl.obolibrary.org/obo/MOD_02053 crosslinked L-phenylalanine residue 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. http://purl.obolibrary.org/obo/MOD_00346 2-(S-L-cysteinyl)-D-phenylalanine http://purl.obolibrary.org/obo/MOD_02053 crosslinked L-phenylalanine residue 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. http://purl.obolibrary.org/obo/MOD_00347 2-(S-L-cysteinyl)-D-allo-threonine http://purl.obolibrary.org/obo/MOD_02056 crosslinked L-threonine residue 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. http://purl.obolibrary.org/obo/MOD_00348 N-carbamoyl-L-alanine http://purl.obolibrary.org/obo/MOD_00901 modified L-alanine residue A protein modification that effectively converts an L-alanine residue to N-carbamoyl-L-alanine. http://purl.obolibrary.org/obo/MOD_00349 4-amino-3-isothiazolidinone-L-serine http://purl.obolibrary.org/obo/MOD_02055 crosslinked L-serine residue A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form 4-amino-3-isothiazolidinone-L-serine. http://purl.obolibrary.org/obo/MOD_00350 L-threonyl-pentaglycyl-murein peptidoglycan http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue A protein modification that effectively attaches an L-threonine residue to murein peptidoglycan by a pentaglycine linker peptide. http://purl.obolibrary.org/obo/MOD_00351 N-glycyl-1-(phosphatidyl)ethanolamine http://purl.obolibrary.org/obo/MOD_01155 lipoconjugated residue A protein modification that effectively converts a glycine residue to N-glycyl-1-(phosphatidyl)ethanolamine. http://purl.obolibrary.org/obo/MOD_00352 L-glutamyl 5-omega-hydroxyceramide ester http://purl.obolibrary.org/obo/MOD_01155 lipoconjugated residue A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl 5-omega-hydroxyceramide ester. http://purl.obolibrary.org/obo/MOD_00353 S-[5'-(L-tryptoph-6'-yl)-L-tyrosin-3'-yl]-L-methionin-S-ium http://purl.obolibrary.org/obo/MOD_02058 crosslinked L-tyrosine residue 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. http://purl.obolibrary.org/obo/MOD_00354 O-(riboflavin phosphoryl)-L-threonine http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue A protein modification that effectively converts an L-threonine residue to O-(riboflavin phosphoryl)-L-threonine. http://purl.obolibrary.org/obo/MOD_00355 O-(riboflavin phosphoryl)-L-serine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to O-(riboflavin phosphoryl)-L-serine. http://purl.obolibrary.org/obo/MOD_00356 S-(4alpha-FMN)-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-(4a-FMN)-L-cysteine. http://purl.obolibrary.org/obo/MOD_00357 1'-(8alpha-FMN)-L-histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively converts an L-histidine residue to 1'-(8alpha-FMN)-L-histidine. http://purl.obolibrary.org/obo/MOD_00358 3'-(8alpha-FMN)-L-histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively converts an L-histidine residue to 3'-(8alpha-FMN)-L-histidine. http://purl.obolibrary.org/obo/MOD_00359 N2-acetyl-L-arginine http://purl.obolibrary.org/obo/MOD_00902 modified L-arginine residue A protein modification that effectively converts an L-arginine residue to N2-acetyl-L-arginine. http://purl.obolibrary.org/obo/MOD_00360 L-cysteinyl copper sulfido molybdopterin cytosine dinuncleotide http://purl.obolibrary.org/obo/MOD_02067 metal or metal cluster coordinated L-cysteine residue A protein modification that effectively converts an L-cysteine residue to L-cysteinyl copper sulfido molybdopterin cytosine dinuncleotide. http://purl.obolibrary.org/obo/MOD_00361 tris-L-cysteinyl S-adenosylmethion-N,O-diyl tetrairon tetrasulfide http://purl.obolibrary.org/obo/MOD_02067 metal or metal cluster coordinated L-cysteine residue 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. http://purl.obolibrary.org/obo/MOD_00362 tris-L-cysteinyl L-arginyl diiron disulfide http://purl.obolibrary.org/obo/MOD_02076 metal or metal cluster coordinated L-arginine residue 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. http://purl.obolibrary.org/obo/MOD_00363 L-cysteinyl-L-selenocysteine (Cys-Sec) http://purl.obolibrary.org/obo/MOD_02061 crosslinked L-selenocysteine residue A protein modification that effectively cross-links an L-cysteine residue and an L-selenocysteine residues to form L-cysteinyl-L-selenocystine. http://purl.obolibrary.org/obo/MOD_00364 5-hydroxy-N6,N6,N6-trimethyl-L-lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively converts an L-lysine residue to 5-hydroxy-N6,N6,N6-trimethyl-L-lysine. http://purl.obolibrary.org/obo/MOD_00365 N-(L-isoglutamyl)-glycine http://purl.obolibrary.org/obo/MOD_02047 crosslinked glycine residue 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. http://purl.obolibrary.org/obo/MOD_00366 O-sulfo-L-serine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to O-sulfo-L-serine. http://purl.obolibrary.org/obo/MOD_00367 O-sulfo-L-threonine http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue A protein modification that effectively converts an L-threonine residue to O-sulfo-L-threonine. http://purl.obolibrary.org/obo/MOD_00368 N-carboxy-L-methionine http://purl.obolibrary.org/obo/MOD_01152 carboxylated residue A protein modification that effectively converts an L-methionine residue to N-carboxy-L-methionine. http://purl.obolibrary.org/obo/MOD_00369 O-acetyl-L-serine http://purl.obolibrary.org/obo/MOD_02003 O3-acylated L-serine A protein modification that effectively converts an L-serine residue to O-acetyl-L-serine. http://purl.obolibrary.org/obo/MOD_00370 (E)-2,3-didehydrotyrosine http://purl.obolibrary.org/obo/MOD_00706 dehydrogenated tyrosine A protein modification that effectively converts an L-tyrosine residue to (E)-2,3-didehydrotyrosine. http://purl.obolibrary.org/obo/MOD_00371 bis-L-aspartato tris-L-glutamato L-histidino calcium tetramanganese tetroxide http://purl.obolibrary.org/obo/MOD_02070 metal or metal cluster coordinated L-histidine residue 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. http://purl.obolibrary.org/obo/MOD_00372 3'-(3'-L-tyrosinyl)-L-tyrosine http://purl.obolibrary.org/obo/MOD_02058 crosslinked L-tyrosine residue A protein modification that effectively cross-links two L-tyrosine residues with a carbon-carbon bond to form 3'-(3'-L-tyrosinyl)-L-tyrosine. http://purl.obolibrary.org/obo/MOD_00373 3'-(O4'-L-tyrosinyl)-L-tyrosine http://purl.obolibrary.org/obo/MOD_02058 crosslinked L-tyrosine residue A protein modification that effectively cross-links L-tyrosine residues with an ether bond to form 3'-(O4'-L-tyrosinyl)-L-tyrosine. http://purl.obolibrary.org/obo/MOD_00374 3,4-dihydroxy-L-arginine http://purl.obolibrary.org/obo/MOD_00682 hydroxylated arginine A protein modification that effectively converts an L-arginine residue to 3,4-dihydroxy-L-arginine. http://purl.obolibrary.org/obo/MOD_00375 4,5-dihydroxy-L-lysine http://purl.obolibrary.org/obo/MOD_00681 hydroxylated lysine A protein modification that effectively converts an L-lysine residue to 4,5-dihydroxy-L-lysine. http://purl.obolibrary.org/obo/MOD_00376 1'-(phospho-5'-adenosine)-L-histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue 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. http://purl.obolibrary.org/obo/MOD_00377 1'-(phospho-5'-uridine)-L-histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue 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. http://purl.obolibrary.org/obo/MOD_00378 L-aspartyl semialdehyde http://purl.obolibrary.org/obo/MOD_00904 modified L-aspartic acid residue A protein modification that effectively converts an L-aspartic acid residue to L-aspartyl semialdehyde. http://purl.obolibrary.org/obo/MOD_00379 L-serine microcin E492 siderophore ester http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to L-serine microcin E492 siderophore ester. http://purl.obolibrary.org/obo/MOD_00380 L-aspartyl molybdenum bis(molybdopterin guanine dinucleotide) http://purl.obolibrary.org/obo/MOD_02066 metal or metal cluster coordinated L-aspartic acid residue A protein modification that effectively converts an L-aspartic acid residue to L-aspartyl molybdenum bis(molybdopterin guanine dinucleotide). http://purl.obolibrary.org/obo/MOD_00381 L-selenocysteinyl tungsten bis(molybdopterin guanine dinucleotide) (Sec) http://purl.obolibrary.org/obo/MOD_02073 metal or metal cluster coordinated L-selenocysteine residue A protein modification that effectively converts an L-selenocysteine residue to L-selenocysteinyl tungsten bis(molybdopterin guanine dinucleotide). http://purl.obolibrary.org/obo/MOD_00382 3-(2-methylthio)ethyl-6-(4-hydroxybenzylidene)-5-iminopiperazin-2-one http://purl.obolibrary.org/obo/MOD_02058 crosslinked L-tyrosine residue 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. http://purl.obolibrary.org/obo/MOD_00383 2-imino-glutamic acid 5-imidazolinone glycine http://purl.obolibrary.org/obo/MOD_02047 crosslinked glycine residue A protein modification that effectively crosslinks an L-glutamic acid residue and a glycine residue to form 2-imino-glutamic acid 5-imidazolinone glycine. http://purl.obolibrary.org/obo/MOD_00384 2-imino-methionine 5-imidazolinone glycine http://purl.obolibrary.org/obo/MOD_02052 crosslinked L-methionine residue A protein modification that effectively crosslinks an L-methionine residue and a glycine residue to form 2-imino-methionine 5-imidazolinone glycine. http://purl.obolibrary.org/obo/MOD_00385 L-asparagine 5-imidazolinone glycine http://purl.obolibrary.org/obo/MOD_02047 crosslinked glycine residue A protein modification that effectively crosslinks an L-asparagine residue and a glycine residue to form L-asparagine 5-imidazolinone glycine. http://purl.obolibrary.org/obo/MOD_00386 L-lysine 5-imidazolinone glycine http://purl.obolibrary.org/obo/MOD_02051 crosslinked L-lysine residue A protein modification that effectively crosslinks an L-lysine residue and a glycine residue to form L-lysine 5-imidazolinone glycine. http://purl.obolibrary.org/obo/MOD_00387 2-tetrahydropyridinyl-5-imidazolinone glycine http://purl.obolibrary.org/obo/MOD_02051 crosslinked L-lysine residue A protein modification that effectively crosslinks an L-lysine residue and a glycine residue to form 2-tetrahydropyridinyl-5-imidazolinone glycine. http://purl.obolibrary.org/obo/MOD_00388 L-alanyl-pentaglycyl-murein peptidoglycan http://purl.obolibrary.org/obo/MOD_00901 modified L-alanine residue A protein modification that effectively attaches an L-alanine residue to murein peptidoglycan by a pentaglycine linker peptide. http://purl.obolibrary.org/obo/MOD_00389 N-formyl-L-proline http://purl.obolibrary.org/obo/MOD_00915 modified L-proline residue A protein modification that effectively converts an L-proline residue to N-formyl-L-proline. http://purl.obolibrary.org/obo/MOD_00390 O-decanoyl-L-serine http://purl.obolibrary.org/obo/MOD_02003 O3-acylated L-serine A protein modification that effectively converts an L-serine residue to O-decanoyl-L-serine. http://purl.obolibrary.org/obo/MOD_00391 O-octanoyl-L-threonine http://purl.obolibrary.org/obo/MOD_02004 O3-acylated L-threonine A protein modification that effectively converts an L-threonine residue to O-octanoyl-L-threonine. http://purl.obolibrary.org/obo/MOD_00392 O-decanoyl-L-threonine http://purl.obolibrary.org/obo/MOD_02004 O3-acylated L-threonine A protein modification that effectively converts an L-threonine residue to O-decanoyl-L-threonine. http://purl.obolibrary.org/obo/MOD_00393 O-methylated residue http://purl.obolibrary.org/obo/MOD_00427 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. http://purl.obolibrary.org/obo/MOD_00395 thioester crosslinked residues http://purl.obolibrary.org/obo/MOD_02044 crosslinked L-cysteine residue 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. http://purl.obolibrary.org/obo/MOD_00397 iodoacetamide derivatized residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue A protein modification that is produced by reaction with iodoacetamide, usually replacement of a reactive hydrogen with a methylcarboxamido group. http://purl.obolibrary.org/obo/MOD_00398 carbamoylated residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process A protein modification that effectively replaces a hydrogen atom with a carbamoyl (carboxamido) group. Replacement of an amino hydrogen produces a ureido group. http://purl.obolibrary.org/obo/MOD_00399 iodoacetic acid derivatized residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue A protein modification that is produced by reaction with iodoacetic acid, usually replacement of a reactive hydrogen with a methylcarboxy group. http://purl.obolibrary.org/obo/MOD_00400 deamidated residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process 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. http://purl.obolibrary.org/obo/MOD_00402 Gygi ICAT(TM) d8 modified cysteine http://purl.obolibrary.org/obo/MOD_01820 isotope tagged sufhydryl reagent 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. http://purl.obolibrary.org/obo/MOD_00403 homoserine http://purl.obolibrary.org/obo/MOD_00913 modified L-methionine residue A protein modification that effectively converts an L-methionine residue to homoserine. http://purl.obolibrary.org/obo/MOD_00404 homoserine lactone http://purl.obolibrary.org/obo/MOD_00913 modified L-methionine residue A protein modification that effectively converts an L-methionine residue to homoserine lactone. http://purl.obolibrary.org/obo/MOD_00405 Applied Biosystems original ICAT(TM) d8 modified cysteine http://purl.obolibrary.org/obo/MOD_01820 isotope tagged sufhydryl reagent 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. http://purl.obolibrary.org/obo/MOD_00406 Applied Biosystems original ICAT(TM) d0 modified cysteine http://purl.obolibrary.org/obo/MOD_01820 isotope tagged sufhydryl reagent 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. http://purl.obolibrary.org/obo/MOD_00408 mono N-acetylated residue http://purl.obolibrary.org/obo/MOD_00670 N-acylated residue A protein modification that effectively replaces a residue amino or imino hydrogen with an acetyl group. http://purl.obolibrary.org/obo/MOD_00409 N-formylated residue http://purl.obolibrary.org/obo/MOD_00670 N-acylated residue A protein modification that effectively replaces a residue amino group with a formamido group. http://purl.obolibrary.org/obo/MOD_00410 S-(N-isopropylcarboxamidomethyl)-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-(N-isopropylcarboxamidomethyl)-L-cysteine. http://purl.obolibrary.org/obo/MOD_00413 biotinyl-iodoacetamidyl-3,6-dioxaoctanediamine derivatized cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that is produced by reaction of a cysteine residue with biotinyl-iodoacetamidyl-3,6-dioxaoctanediamine. http://purl.obolibrary.org/obo/MOD_00416 phosphorylation of an hydroxyl amino acid with prompt loss of phosphate http://purl.obolibrary.org/obo/MOD_00704 dehydrated residue 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. http://purl.obolibrary.org/obo/MOD_00417 S-carboxamidoethyl-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-carboxamidoethyl-L-cysteine. http://purl.obolibrary.org/obo/MOD_00418 pyridylacetylated residue http://purl.obolibrary.org/obo/MOD_00649 acylated residue A protein modification that effectively replaces a hydrogen atom with an (pyridin-3-yl)acetyl group. http://purl.obolibrary.org/obo/MOD_00419 (R)-5-oxo-1,4-tetrahydrothiazine-3-carboxylic acid http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to (R)-5-oxo-1,4-tetrahydrothiazine-3-carboxylic acid. http://purl.obolibrary.org/obo/MOD_00420 2-pyrrolidone-5-carboxylic acid (Glu) http://purl.obolibrary.org/obo/MOD_01048 2-pyrrolidone-5-carboxylic acid A protein modification that effectively converts an L-glutamic acid residue to 2-pyrrolidone-5-carboxylic acid. http://purl.obolibrary.org/obo/MOD_00421 C-glycosylated residue http://purl.obolibrary.org/obo/MOD_00693 glycosylated residue A protein modification that effectively replaces a residue hydrogen atom on a carbon with a carbohydrate-like group through a glycosidic bond. http://purl.obolibrary.org/obo/MOD_00422 alpha-amino morpholine-2-acetylated residue http://purl.obolibrary.org/obo/MOD_01813 morpholine-2-acetylated residue A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a morpholine-2-acetyl group. http://purl.obolibrary.org/obo/MOD_00423 monosodium salt http://purl.obolibrary.org/obo/MOD_00747 sodium containing modified residue A protein modification that effectively substitutes one sodium atom for one hydrogen atom. http://purl.obolibrary.org/obo/MOD_00424 S-pyridylethyl-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-pyridylethyl-L-cysteine. http://purl.obolibrary.org/obo/MOD_00425 monohydroxylated residue http://purl.obolibrary.org/obo/MOD_00677 hydroxylated residue A protein modification that effectively replaces one hydrogen atom with a hydroxyl group. http://purl.obolibrary.org/obo/MOD_00426 S-glycosylated residue http://purl.obolibrary.org/obo/MOD_00693 glycosylated residue A protein modification that effectively replaces a residue hydrogen atom on a sulfur with a carbohydrate-like group through a glycosidic bond. http://purl.obolibrary.org/obo/MOD_00428 dihydroxylated residue http://purl.obolibrary.org/obo/MOD_00677 hydroxylated residue A protein modification that effectively replaces two hydrogen atoms with two hydroxyl groups. http://purl.obolibrary.org/obo/MOD_00429 dimethylated residue http://purl.obolibrary.org/obo/MOD_00427 methylated residue A protein modification that effectively replaces two hydrogen atoms with two methyl groups. http://purl.obolibrary.org/obo/MOD_00430 trimethylated residue http://purl.obolibrary.org/obo/MOD_00427 methylated residue A protein modification that effectively replaces three hydrogen atoms with three methyl groups. http://purl.obolibrary.org/obo/MOD_00431 modified residue with a secondary neutral loss http://purl.obolibrary.org/obo/MOD_01157 protein modification categorized by amino acid modified 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. http://purl.obolibrary.org/obo/MOD_00432 modified residue with neutral loss of phosphate http://purl.obolibrary.org/obo/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 trihydrogen phosphate molecular fragment. http://purl.obolibrary.org/obo/MOD_00433 monoglucosylated residue http://purl.obolibrary.org/obo/MOD_00761 monohexosylated residue A protein modification that effectively replaces a hydrogen atom with an glucose group through a glycosidic bond. http://purl.obolibrary.org/obo/MOD_00434 hexosylated residue http://purl.obolibrary.org/obo/MOD_00693 glycosylated 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. http://purl.obolibrary.org/obo/MOD_00435 O-phospho-L-serine with neutral loss of phosphate http://purl.obolibrary.org/obo/MOD_01151 phosphorylated residue 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. http://purl.obolibrary.org/obo/MOD_00436 N-acetylhexosaminylated residue http://purl.obolibrary.org/obo/MOD_00693 glycosylated 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. http://purl.obolibrary.org/obo/MOD_00439 O-phospho-L-threonine with neutral loss of phosphate http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue Covalent modification of a peptide or protein amino acid phosphorylated threonine with a secondary loss of a neutral trihydrogen phosphate molecular fragment. http://purl.obolibrary.org/obo/MOD_00441 geranylgeranylated residue http://purl.obolibrary.org/obo/MOD_00703 isoprenylated residue A protein modification that effectively replaces a hydrogen atom with a geranylgeranyl group. http://purl.obolibrary.org/obo/MOD_00442 protonated omega-N,omega-N'-dimethylated L-arginine with secondary neutral loss of N,N'-carbodiimide http://purl.obolibrary.org/obo/MOD_00902 modified L-arginine residue 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. http://purl.obolibrary.org/obo/MOD_00443 protonated omega-N,omega-N-dimethlyated L-arginine with secondary neutral loss of N,N-dimethylamine http://purl.obolibrary.org/obo/MOD_00902 modified L-arginine residue 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. http://purl.obolibrary.org/obo/MOD_00444 N-palmitoyl-S-(sn-1-2,3-dipalmitoyl-glycerol)cysteine http://purl.obolibrary.org/obo/MOD_00899 N-palmitoyl-S-diacylglycerol-L-cysteine A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-S-(sn-1-2,3-dipalmitoyl-glycerol)cysteine. http://purl.obolibrary.org/obo/MOD_00445 L-homoarginine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively converts an L-lysine residue to L-homoarginine, such as reaction with O-methylisourea. http://purl.obolibrary.org/obo/MOD_00446 4-hydroxynonenal adduct http://purl.obolibrary.org/obo/MOD_01155 lipoconjugated residue A protein modification produced by formation of an adduct of a residue with 4-hydroxynonenal. http://purl.obolibrary.org/obo/MOD_00447 N-glucuronylated residue http://purl.obolibrary.org/obo/MOD_00764 glycoconjugated 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. http://purl.obolibrary.org/obo/MOD_00449 acetate labeling reagent (N-term) (heavy form, +3amu) http://purl.obolibrary.org/obo/MOD_01431 (2)H deuterium tagged reagent modification from Unimod Isotopic label http://purl.obolibrary.org/obo/MOD_00451 alpha-amino propanoylated residue http://purl.obolibrary.org/obo/MOD_01894 propanoylated residue A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a propanoyl group. http://purl.obolibrary.org/obo/MOD_00452 alpha-amino 3x(13)C-labeled propanoylated residue http://purl.obolibrary.org/obo/MOD_01428 (13)C isotope tagged reagent A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a 3x(13)C-labeled propanoyl group. http://purl.obolibrary.org/obo/MOD_00453 quaternary amine labeling reagent light form (N-term & K) http://purl.obolibrary.org/obo/MOD_01426 isotope tagged reagent derivatized residue A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent light form group. http://purl.obolibrary.org/obo/MOD_00454 quaternary amine labeling reagent heavy form (+3amu) (N-term & K) http://purl.obolibrary.org/obo/MOD_01426 isotope tagged reagent derivatized residue A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent heavy (+3amu) form group. http://purl.obolibrary.org/obo/MOD_00455 quaternary amine labeling reagent heavy form (+6amu) (N-term & K) http://purl.obolibrary.org/obo/MOD_01426 isotope tagged reagent derivatized residue A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent heavy (+6amu) form group. http://purl.obolibrary.org/obo/MOD_00456 quaternary amine labeling reagent heavy form (+9amu) (N-term & K) http://purl.obolibrary.org/obo/MOD_01426 isotope tagged reagent derivatized residue A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent heavy (+9amu) form group. http://purl.obolibrary.org/obo/MOD_00457 4x(12)C, 4x(1)H labeled alpha-amino succinylated residue http://purl.obolibrary.org/obo/MOD_01696 alpha-amino acylated residue A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a light succinyl group. http://purl.obolibrary.org/obo/MOD_00458 4x(2)H labeled alpha-amino succinylated residue http://purl.obolibrary.org/obo/MOD_01696 alpha-amino acylated residue A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a 4x(2)H labeled succinyl group. http://purl.obolibrary.org/obo/MOD_00459 4x(13)C labeled alpha-amino succinylated residue http://purl.obolibrary.org/obo/MOD_01696 alpha-amino acylated residue A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a 4x(13)C labeled succinyl group. http://purl.obolibrary.org/obo/MOD_00460 L-cysteic acid (L-cysteine sulfonic acid) http://purl.obolibrary.org/obo/MOD_00708 sulfur oxygenated L-cysteine A protein modification that effectively trioxygenates an L-cysteine residue to L-cysteine sulfonic acid. http://purl.obolibrary.org/obo/MOD_00461 nitrated residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue A protein modification that effectively substitutes a nitrite (NO2) group for a hydrogen atom. http://purl.obolibrary.org/obo/MOD_00462 L-kynurenine http://purl.obolibrary.org/obo/MOD_00918 modified L-tryptophan residue A protein modification that effectively converts an L-tryptophan residue to L-kynurenine. http://purl.obolibrary.org/obo/MOD_00463 3'-hydroxy-L-kynurenine http://purl.obolibrary.org/obo/MOD_00918 modified L-tryptophan residue A protein modification that effectively converts an L-tryptophan residue to 3'-hydroxy-L-kynurenine. http://purl.obolibrary.org/obo/MOD_00464 N'-formyl-L-kynurenine http://purl.obolibrary.org/obo/MOD_00918 modified L-tryptophan residue A protein modification that effectively converts an L-tryptophan residue to N'-formyl-L-kynurenine. http://purl.obolibrary.org/obo/MOD_00465 dihydroxyphenylalanine (Phe) http://purl.obolibrary.org/obo/MOD_00914 modified L-phenylalanine residue A protein modification that effectively converts an L-phenylalanine residue to a dihydroxyphenylalanine. http://purl.obolibrary.org/obo/MOD_00466 glycosylsphingolipidinositolated residue http://purl.obolibrary.org/obo/MOD_01155 lipoconjugated residue A protein modification that effectively converts a residue to a glycosylsphingolipidinositolethanolamidated. http://purl.obolibrary.org/obo/MOD_00467 iminobiotinyl modified residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue A protein modification that effectively substitutes an iminobiotinyl group for a hydrogen atom. http://purl.obolibrary.org/obo/MOD_00468 ESP-Tag light d0 http://purl.obolibrary.org/obo/MOD_01426 isotope tagged reagent derivatized residue modification from Unimod Isotopic label http://purl.obolibrary.org/obo/MOD_00469 ESP-Tag heavy d10 http://purl.obolibrary.org/obo/MOD_01431 (2)H deuterium tagged reagent modification from Unimod Isotopic label http://purl.obolibrary.org/obo/MOD_00470 NHS-LC-Biotin http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00471 EDT-maleimide-PEO-biotin http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00472 IMID d0 http://purl.obolibrary.org/obo/MOD_01426 isotope tagged reagent derivatized residue modification from Unimod Isotopic label http://purl.obolibrary.org/obo/MOD_00473 IMID d4 http://purl.obolibrary.org/obo/MOD_01426 isotope tagged reagent derivatized residue modification from Unimod Isotopic label http://purl.obolibrary.org/obo/MOD_00474 S-([1,1,2-(2)H3]-carboxamidoethyl)-L-cysteine http://purl.obolibrary.org/obo/MOD_01426 isotope tagged reagent derivatized residue A protein modification that effectively converts an L-cysteine residue to S-(1,1,2-(2)H3)-propanamide-L-cysteine. http://purl.obolibrary.org/obo/MOD_00475 2-amino-L-tyrosine http://purl.obolibrary.org/obo/MOD_02039 aminated residue A protein modification that effectively converts an L-tyrosine residue to 2-amino-L-tyrosine. http://purl.obolibrary.org/obo/MOD_00476 monogalactosylated residue http://purl.obolibrary.org/obo/MOD_00761 monohexosylated residue A protein modification that effectively replaces a hydrogen atom with an galactose group through a glycosidic bond. http://purl.obolibrary.org/obo/MOD_00477 2-pyrrolidone http://purl.obolibrary.org/obo/MOD_00915 modified L-proline residue A protein modification that effectively converts, by oxidative decarboxylation, an L-proline residue to 2-pyrrolidone with breakage of the peptide chain. http://purl.obolibrary.org/obo/MOD_00478 glutamyl semialdehyde (Pro) http://purl.obolibrary.org/obo/MOD_00915 modified L-proline residue A protein modification that effectively converts an L-proline residue to L-glutamyl semialdehyde. http://purl.obolibrary.org/obo/MOD_00479 glutamyl semialdehyde (Arg) http://purl.obolibrary.org/obo/MOD_00902 modified L-arginine residue A protein modification that effectively converts an L-arginine residue to L-glutamyl semialdehyde. http://purl.obolibrary.org/obo/MOD_00480 Applied Biosystems cleavable ICAT(TM) light http://purl.obolibrary.org/obo/MOD_01426 isotope tagged reagent derivatized residue modification from Unimod Isotopic label http://purl.obolibrary.org/obo/MOD_00481 Applied Biosystems cleavable ICAT(TM) heavy http://purl.obolibrary.org/obo/MOD_01428 (13)C isotope tagged reagent modification from Unimod Isotopic label http://purl.obolibrary.org/obo/MOD_00482 N-formyl-L-methionine (Met) http://purl.obolibrary.org/obo/MOD_00913 modified L-methionine residue A protein modification that effectively converts an L-methionine residue to N-formyl-L-methionine (not known as a natural, post-translational modification process). http://purl.obolibrary.org/obo/MOD_00483 N-ethylmaleimide derivatized cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that is produced by reaction with N-ethylmaleimide. http://purl.obolibrary.org/obo/MOD_00484 oxidized lysine biotinylated with biotin-LC-hydrazide, reduced http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00485 oxidized lysine biotinylated with biotin-LC-hydrazide http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00486 oxidized proline biotinylated with biotin-LC-hydrazide, reduced http://purl.obolibrary.org/obo/MOD_00915 modified L-proline residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00487 oxidized proline biotinylated with biotin-LC-hydrazide http://purl.obolibrary.org/obo/MOD_00915 modified L-proline residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00488 oxidized arginine biotinylated with biotin-LC-hydrazide http://purl.obolibrary.org/obo/MOD_00902 modified L-arginine residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00489 oxidized arginine biotinylated with biotin-LC-hydrazide, reduced http://purl.obolibrary.org/obo/MOD_00902 modified L-arginine residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00490 EDT-iodo-PEO-biotin http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00491 thio ether formation - BTP Adduct http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00492 ubiquitination signature dipeptidyl lysine http://purl.obolibrary.org/obo/MOD_02051 crosslinked L-lysine residue 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. http://purl.obolibrary.org/obo/MOD_00494 N-iodoacetyl, p-chlorobenzyl-12C6-glucamine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue modification from Unimod Isotopic label http://purl.obolibrary.org/obo/MOD_00495 N-iodoacetyl, p-chlorobenzyl-13C6-glucamine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue modification from Unimod Isotopic label http://purl.obolibrary.org/obo/MOD_00497 3-sulfanylpropanoyl (N-term and Lys) http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue modification from Unimod [(35)S]dithiobis(succinimidyl propionate) crosslinking http://purl.obolibrary.org/obo/MOD_00498 fluorinated residue http://purl.obolibrary.org/obo/MOD_00694 halogen containing residue A protein modification that effectively substitutes a hydrogen of a residue with a fluorine atom. http://purl.obolibrary.org/obo/MOD_00499 5-iodoacetamidofluorescein http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00500 monoiodinated residue http://purl.obolibrary.org/obo/MOD_00755 iodinated residue A protein modification that effectively substitutes one hydrogen atom of a residue with one iodine atom. http://purl.obolibrary.org/obo/MOD_00501 diiodinated residue http://purl.obolibrary.org/obo/MOD_00755 iodinated residue A protein modification that effectively substitutes two hydrogen atoms of a residue with two iodine atoms. http://purl.obolibrary.org/obo/MOD_00502 triiodinated residue http://purl.obolibrary.org/obo/MOD_00755 iodinated residue A protein modification that effectively substitutes three hydrogen atoms of a residue with three iodine atoms. http://purl.obolibrary.org/obo/MOD_00503 N-(cis-delta 5)-tetradecaenoylglycine http://purl.obolibrary.org/obo/MOD_00908 modified glycine residue A protein modification that effectively converts a glycine residue to N-(cis-delta 5)-tetradecaenoylglycine. http://purl.obolibrary.org/obo/MOD_00504 N-(cis,cis-delta 5,delta 8)-tetradecadienoylglycine http://purl.obolibrary.org/obo/MOD_00908 modified glycine residue A protein modification that effectively converts a glycine residue to N-(cis,cis-delta 5,delta 8)-tetradecadienoylglycine. http://purl.obolibrary.org/obo/MOD_00505 benzoyl labeling reagent light form (N-term and K) http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from Unimod Isotopic label http://purl.obolibrary.org/obo/MOD_00506 N-linked glycan core N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine modification from Unimod N-linked glycosylation, Hex(5) HexNAc(2) http://purl.obolibrary.org/obo/MOD_00509 amidination of lysines or N-terminal amines with methyl acetimidate http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00510 HexNAc1dHex1 N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine modification from Unimod N-linked glycosylation, dHex HexNAc http://purl.obolibrary.org/obo/MOD_00511 HexNAc2 N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine modification from Unimod N-linked glycosylation, HexNAc(2) http://purl.obolibrary.org/obo/MOD_00512 Hex3 N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine modification from Unimod N-linked glycosylation, Hex3 http://purl.obolibrary.org/obo/MOD_00513 HexNAc1dHex2 N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine modification from Unimod N-linked glycosylation, dHex(2) HexNAc http://purl.obolibrary.org/obo/MOD_00514 Hex1HexNAc1dHex1 N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine modification from Unimod N-linked glycosylation, dHex Hex HexNAc http://purl.obolibrary.org/obo/MOD_00515 HexNAc2dHex1 N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine modification from Unimod N-linked glycosylation, dHex HexNAc(2) http://purl.obolibrary.org/obo/MOD_00516 Hex1HexNAc2 N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine modification from Unimod N-linked glycosylation http://purl.obolibrary.org/obo/MOD_00517 Hex1HexNAc1NeuAc1 glycosylated residue http://purl.obolibrary.org/obo/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 composed of Hex1HexNAc1NeuAc1 linked through a glycosidic bond. http://purl.obolibrary.org/obo/MOD_00518 HexNAc2dHex2 N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine modification from Unimod N-linked glycosylation http://purl.obolibrary.org/obo/MOD_00519 Hex1HexNAc2Pent1 N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine modification from Unimod N-linked glycosylation http://purl.obolibrary.org/obo/MOD_00520 Hex1HexNAc2dHex1 N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine modification from Unimod N-linked glycosylation http://purl.obolibrary.org/obo/MOD_00521 Hex2HexNAc2 N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine modification from Unimod N-linked glycosylation http://purl.obolibrary.org/obo/MOD_00522 Hex3HexNAc1Pent1 N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine modification from Unimod N-linked glycosylation http://purl.obolibrary.org/obo/MOD_00523 Hex1HexNAc2dHex1Pent1 N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine modification from Unimod N-linked glycosylation http://purl.obolibrary.org/obo/MOD_00524 Hex1HexNAc2dHex2 N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine modification from Unimod N-linked glycosylation http://purl.obolibrary.org/obo/MOD_00525 Hex2HexNAc2Pent1 N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine modification from Unimod N-linked glycosylation http://purl.obolibrary.org/obo/MOD_00526 Hex2HexNAc2dHex1 N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine modification from Unimod N-linked glycosylation http://purl.obolibrary.org/obo/MOD_00527 Hex3HexNAc2 N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine modification from Unimod N-linked glycosylation http://purl.obolibrary.org/obo/MOD_00528 Hex1HexNAc1NeuAc2 glycosylated residue http://purl.obolibrary.org/obo/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 composed of Hex1HexNAc1NeuAc2 linked through a glycosidic bond. http://purl.obolibrary.org/obo/MOD_00529 Hex3HexNAc2P1 N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine modification from Unimod N-linked glycosylation http://purl.obolibrary.org/obo/MOD_00530 L-selenomethionine http://purl.obolibrary.org/obo/MOD_00913 modified L-methionine residue A protein modification that effectively converts an L-methionine residue to L-selenomethionine. http://purl.obolibrary.org/obo/MOD_00531 (18)O labeled deglycosylated asparagine http://purl.obolibrary.org/obo/MOD_01293 1x(18)O labeled deamidated L-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. http://purl.obolibrary.org/obo/MOD_00532 Shimadzu 13CNBS http://purl.obolibrary.org/obo/MOD_01426 isotope tagged reagent derivatized residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00533 Shimadzu 12CNBS http://purl.obolibrary.org/obo/MOD_01426 isotope tagged reagent derivatized residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00534 Michael addition of BHT quinone methide to cysteine and lysine http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from Unimod Post-translational http://purl.obolibrary.org/obo/MOD_00535 phosphorylation to amine thiol http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00537 L-alanine residue (Thr) http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue A protein modification that effectively converts an L-threonine residue to L-alanine. http://purl.obolibrary.org/obo/MOD_00538 protein modification categorized by isobaric sets http://purl.obolibrary.org/obo/MOD_00000 protein modification Modified amino acid residues groups into isobaric sets at particular mass resolution cut-offs. http://purl.obolibrary.org/obo/MOD_00540 9x(13)C labeled residue http://purl.obolibrary.org/obo/MOD_00842 (13)C labeled residue A protein modification that effectively converts a residue containing common isotopes to a 9x(13)C labeled residue. http://purl.obolibrary.org/obo/MOD_00541 9x(13)C labeled L-phosphotyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively converts an L-tyrosine residue to 9x(13)C labeled L-phosphotyrosine. http://purl.obolibrary.org/obo/MOD_00542 hydroxyphenylglyoxal arginine http://purl.obolibrary.org/obo/MOD_00902 modified L-arginine residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00543 bis(hydroxyphenylglyoxal) arginine http://purl.obolibrary.org/obo/MOD_00902 modified L-arginine residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00544 6x(13)C labeled residue http://purl.obolibrary.org/obo/MOD_00842 (13)C labeled residue A protein modification that effectively converts a residue containing common isotopes to a 6x(13)C labeled residue. http://purl.obolibrary.org/obo/MOD_00546 (18)O label at both C-terminal oxygens http://purl.obolibrary.org/obo/MOD_00847 (18)O disubstituted residue A protein modification that effectively substitutes two (18)O atom for the two (16)O atoms of an alpha-carboxyl (1-carboxyl) group. http://purl.obolibrary.org/obo/MOD_00547 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from Unimod Chemical derivative used for amino acid analysis http://purl.obolibrary.org/obo/MOD_00548 APTA http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00549 APTA d3 http://purl.obolibrary.org/obo/MOD_01431 (2)H deuterium tagged reagent modification from Unimod Isotopic label http://purl.obolibrary.org/obo/MOD_00550 EAPTA d0 http://purl.obolibrary.org/obo/MOD_01426 isotope tagged reagent derivatized residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00551 EAPTA d5 http://purl.obolibrary.org/obo/MOD_01431 (2)H deuterium tagged reagent modification from Unimod Isotopic label http://purl.obolibrary.org/obo/MOD_00552 4x(2)H labeled dimethylated residue http://purl.obolibrary.org/obo/MOD_00839 (2)H deuterium labeled residue A protein modification that effectively converts a residue containing common isotopes to a 4x(2)H labeled dimethylated residue. http://purl.obolibrary.org/obo/MOD_00553 1,2-ethanedithiol modified residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue A protein modification that effectively substitutes a (2-sulfanylethyl)sulfanyl (or thioethylthiol) group for a hydroxy group. http://purl.obolibrary.org/obo/MOD_00561 N-ethyl iodoacetamide- http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from Unimod Isotopic label http://purl.obolibrary.org/obo/MOD_00562 N-ethyl iodoacetamide-d5 http://purl.obolibrary.org/obo/MOD_01431 (2)H deuterium tagged reagent modification from Unimod Isotopic label http://purl.obolibrary.org/obo/MOD_00563 mono-N-acetylaminogalactosylated residue http://purl.obolibrary.org/obo/MOD_01673 N-acetylaminohexosylated residue A protein modification that effectively replaces a hydrogen atom with an N-acetylaminogalactose group through a glycosidic bond. http://purl.obolibrary.org/obo/MOD_00565 deglycosylated asparagine http://purl.obolibrary.org/obo/MOD_00903 modified L-asparagine residue modification from Unimod N-linked glycosylation http://purl.obolibrary.org/obo/MOD_00566 label cysteine with IGBP reagent http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00569 residues isobaric at a resolution below 0.000001 Da http://purl.obolibrary.org/obo/MOD_00770 residues isobaric at a resolution below 0.01 Da Natural or modified residues that are isobaric at a resolution below 0.000001 Da. http://purl.obolibrary.org/obo/MOD_00570 residues isobaric at 71.037114 Da http://purl.obolibrary.org/obo/MOD_00769 residues isobaric at 71.0-71.1 Da Natural or modified residues with a mass of 71.037114 Da. http://purl.obolibrary.org/obo/MOD_00571 2-pyrrolidone-5-carboxylic acid (Pro) http://purl.obolibrary.org/obo/MOD_01048 2-pyrrolidone-5-carboxylic acid A modification that effectively oxygenates C5 of an L-proline residue to form a 2-pyrrolidone-5-carboxylic acid, pyroglutamic acid. http://purl.obolibrary.org/obo/MOD_00572 oxidized arginine biotinylated with biotin hydrazide http://purl.obolibrary.org/obo/MOD_00902 modified L-arginine residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00573 oxidized lysine biotinylated with biotin hydrazide http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00574 oxidized proline biotinylated with biotin hydrazide http://purl.obolibrary.org/obo/MOD_00915 modified L-proline residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00575 oxidized threonine biotinylated with biotin hydrazide http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00576 crotonylated residue http://purl.obolibrary.org/obo/MOD_00649 acylated residue modification from Unimod Other http://purl.obolibrary.org/obo/MOD_00577 acetaldehyde crosslinked penta-L-lysine http://purl.obolibrary.org/obo/MOD_02051 crosslinked L-lysine residue modification occurs as a Schiff base in the presence of pentalysine http://purl.obolibrary.org/obo/MOD_00581 (18)O monosubstituted residue http://purl.obolibrary.org/obo/MOD_00845 (18)O substituted residue A protein modification that effectively substitutes one (18)O atom for one (16)O atom. http://purl.obolibrary.org/obo/MOD_00582 6x(13)C,2x(15)N labeled L-lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively converts an L-lysine residue to 6x(13)C,2x(15)N labeled L-lysine. http://purl.obolibrary.org/obo/MOD_00583 thiophosphorylated residue http://purl.obolibrary.org/obo/MOD_00861 phosphorus containing modified residue A protein modification that effectively replaces a hydrogen atom with a thiophosphono group (H2PO2S, 'thiophosphate'). http://purl.obolibrary.org/obo/MOD_00584 4-sulfophenyl isothiocyanate derivatized residue http://purl.obolibrary.org/obo/MOD_00841 isothiocyanate reagent derivatized residue A protein modification produced by formation of an adduct with 4-sulfophenyl isothiocyanate. http://purl.obolibrary.org/obo/MOD_00585 deuterium trisubstituted residue http://purl.obolibrary.org/obo/MOD_00786 deuterium substituted residue A protein modification that effectively substitutes three (2)H deuterium atoms for three (1)H protium atoms. http://purl.obolibrary.org/obo/MOD_00586 pyridyl thiol modified residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00587 6x(13)C,4x(15)N labeled L-arginine http://purl.obolibrary.org/obo/MOD_00902 modified L-arginine residue A protein modification that effectively converts an L-arginine residue to 6x(13)C, 4x(15)N labeled L-arginine. http://purl.obolibrary.org/obo/MOD_00588 5x(13)C,1x(15)N labeled L-valine http://purl.obolibrary.org/obo/MOD_00920 modified L-valine residue A protein modification that effectively converts an L-valine residue to 5x(13)C,1x(15)N labeled L-valine. http://purl.obolibrary.org/obo/MOD_00589 9x(13)C,1x(15)N labeled L-phenylalanine http://purl.obolibrary.org/obo/MOD_00914 modified L-phenylalanine residue A protein modification that effectively converts an L-phenylalanine residue to (13)C,(15)N labeled L-phenylalanine. http://purl.obolibrary.org/obo/MOD_00592 sulfonation of N-terminal http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00594 residues isobaric at 113.047678 Da http://purl.obolibrary.org/obo/MOD_00624 residues isobaric at 113.0-113.1 Da Natural or modified resiues with a mass of 113.047678 Da. http://purl.obolibrary.org/obo/MOD_00595 monomannosylated residue http://purl.obolibrary.org/obo/MOD_00761 monohexosylated residue A protein modification that effectively replaces a hydrogen atom with an manose group through a glycosidic bond http://purl.obolibrary.org/obo/MOD_00596 4-(2-aminoethyl)benzenesulfonyl fluoride derivatized residue http://purl.obolibrary.org/obo/MOD_01652 sulfonyl halide reagent derivatized residue A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS. http://purl.obolibrary.org/obo/MOD_00598 S-(2-hydroxyethyl)cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-(2-hydroxyethyl)cysteine http://purl.obolibrary.org/obo/MOD_00600 L-glutamic acid 5-ethyl ester http://purl.obolibrary.org/obo/MOD_00906 modified L-glutamic acid residue A protein modification that effectively converts an L-glutamic acid residue to L-glutamate 5-ethyl ester. http://purl.obolibrary.org/obo/MOD_00602 N-methylated residue http://purl.obolibrary.org/obo/MOD_00427 methylated residue A protein modification that effectively replaces a hydrogen atom of a residue amino or imino group with an methyl group. http://purl.obolibrary.org/obo/MOD_00604 2x(2)H monomethylated L-lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively converts an L-lysine residue to 2x(2)H labeled monomethylated L-lysine. http://purl.obolibrary.org/obo/MOD_00605 Sulfanilic Acid (SA), light C12 http://purl.obolibrary.org/obo/MOD_01426 isotope tagged reagent derivatized residue modification from Unimod Chemical derivative, C-Terminal/Glutamate/Aspartate sulfonation http://purl.obolibrary.org/obo/MOD_00606 Sulfanilic Acid (SA), heavy C13 http://purl.obolibrary.org/obo/MOD_01428 (13)C isotope tagged reagent modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00607 dioxoindolealanine lactone http://purl.obolibrary.org/obo/MOD_00918 modified L-tryptophan residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00608 biotin polyethyleneoxide amine http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00609 Pierce EZ-Link Biotin-HPDP modified L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00610 cysteinyl mercury http://purl.obolibrary.org/obo/MOD_02067 metal or metal cluster coordinated L-cysteine residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00611 iodouridine monophosphate derivatized residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue A protein modification that is produced by reaction of iodouridine monophosphate with a residue. http://purl.obolibrary.org/obo/MOD_00612 3-(carboxamidomethylthio)propanoylated residue http://purl.obolibrary.org/obo/MOD_00649 acylated 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. http://purl.obolibrary.org/obo/MOD_00613 biotinoyl-iodoacetyl-ethylenediamine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00614 fucosylated residue http://purl.obolibrary.org/obo/MOD_00736 deoxyhexosylated 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. http://purl.obolibrary.org/obo/MOD_00616 residues isobaric at a resolution below 0.1 Da http://purl.obolibrary.org/obo/MOD_00538 protein modification categorized by isobaric sets Natural or modified residues that are isobaric at a resolution below 0.1 Da. http://purl.obolibrary.org/obo/MOD_00617 3x(2)H residue methyl ester http://purl.obolibrary.org/obo/MOD_00839 (2)H deuterium labeled residue A protein modification that effectively converts a residue containing common isotopes to a 3x(2)H labeled residue methyl ester. http://purl.obolibrary.org/obo/MOD_00618 tryptophan carboxylation http://purl.obolibrary.org/obo/MOD_01152 carboxylated residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00620 cysteine monobromobimane derivative http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00621 menadione quinone derivative http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00622 cysteine mercaptoethanol http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00623 fucosylated biantennary (-2 galactose) N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine modification from Unimod N-linked glycosylation http://purl.obolibrary.org/obo/MOD_00624 residues isobaric at 113.0-113.1 Da http://purl.obolibrary.org/obo/MOD_00616 residues isobaric at a resolution below 0.1 Da Natural or modified residues with a mass of 113.0-113.1 Da. http://purl.obolibrary.org/obo/MOD_00625 N-methylmaleimide derivatized residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00626 fluorescein-5-thiosemicarbazide modified residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00627 2,5-dimethylpyrrole lysine from 2,5-hexanedione adduct http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00628 Hex2 http://purl.obolibrary.org/obo/MOD_00725 complex glycosylation 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 http://purl.obolibrary.org/obo/MOD_00629 MDA adduct +62 http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00630 C3-H2-O adduct (+54 amu) of malondialdehyde with lysine or methylglyoxal with arginine. http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00631 hydrolyzed N-ethylmaleimide adduct http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00633 bis-N-I-sulfonerahodamine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00634 dimethyl 3,3'-dithiobispropionimidate http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00635 10-fluoroethoxyphosphinyl-N-(biotinamidopentyl)decanamide http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00636 S-ethylcysteine (Ser) http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to S-ethylcysteine. http://purl.obolibrary.org/obo/MOD_00637 1x(13)C,3x(2)H labeled monomethylated L-arginine http://purl.obolibrary.org/obo/MOD_00902 modified L-arginine residue 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. http://purl.obolibrary.org/obo/MOD_00638 2x(13)C,6x(2)H labeled dimethylated L-arginine http://purl.obolibrary.org/obo/MOD_00902 modified L-arginine residue 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. http://purl.obolibrary.org/obo/MOD_00639 thiophosphate labeled with biotin-HPDP http://purl.obolibrary.org/obo/MOD_00861 phosphorus containing modified residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00640 6-N-biotinylaminohexyl isopropyl phosphorofluoridate http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00642 reduced 4-hydroxynonenal adduct http://purl.obolibrary.org/obo/MOD_01155 lipoconjugated residue A protein modification produced by formation of an adduct of a residue with 4-hydroxynonenal artificially reduced by a reagent such as NaBH4. http://purl.obolibrary.org/obo/MOD_00643 methylamine Michael addition derivatized residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from Unimod Artifact http://purl.obolibrary.org/obo/MOD_00644 mono O-acetylated residue http://purl.obolibrary.org/obo/MOD_00394 monoacetylated residue A protein modification that effectively replaces a residue hydroxyl group with an acetoxy group. http://purl.obolibrary.org/obo/MOD_00645 mono S-acetylated residue http://purl.obolibrary.org/obo/MOD_00394 monoacetylated residue A protein modification that effectively replaces a residue sulfanyl group with an acetylsulfanyl group. http://purl.obolibrary.org/obo/MOD_00646 monoacetylated L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to either N-acetyl-L-cysteine or S-acetyl-L-cysteine. http://purl.obolibrary.org/obo/MOD_00647 monoacetylated L-serine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue 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. http://purl.obolibrary.org/obo/MOD_00648 N,O-diacetylated L-serine http://purl.obolibrary.org/obo/MOD_02080 diacetylated L-serine A protein modification that effectively converts an L-serine residue to N,O-diacetyl-L-serine. http://purl.obolibrary.org/obo/MOD_00650 N-myristoylated residue http://purl.obolibrary.org/obo/MOD_00670 N-acylated residue A protein modification that effectively replaces a residue amino group with a myristoylamino group. http://purl.obolibrary.org/obo/MOD_00651 N-palmitoylated residue http://purl.obolibrary.org/obo/MOD_00670 N-acylated residue A protein modification that effectively replaces a residue amino group with a palmitoylamino group. http://purl.obolibrary.org/obo/MOD_00652 O-palmitoylated residue http://purl.obolibrary.org/obo/MOD_00440 palmitoylated residue A protein modification that effectively replaces a residue hydroxyl group with a palmitoyloxy group. http://purl.obolibrary.org/obo/MOD_00653 S-palmitoylated residue http://purl.obolibrary.org/obo/MOD_00440 palmitoylated residue A protein modification that effectively replaces a residue sulfanyl group with an palmitoylsulfanyl group. http://purl.obolibrary.org/obo/MOD_00654 S-methylated residue http://purl.obolibrary.org/obo/MOD_00427 methylated residue a protein modification that effectively replaces a sulfanyl group with a methylsulfanyl group http://purl.obolibrary.org/obo/MOD_00655 S-myristoylated residue http://purl.obolibrary.org/obo/MOD_00438 myristoylated residue A protein modification that effectively replaces a residue sulfanyl group with an myristoylsulfanyl group. http://purl.obolibrary.org/obo/MOD_00656 C-methylated residue http://purl.obolibrary.org/obo/MOD_00427 methylated residue A protein modification that effectively replaces a residue hydrocarbyl hydrogen with an methyl group. http://purl.obolibrary.org/obo/MOD_00657 L-glutamic acid 5-methyl ester (Gln) http://purl.obolibrary.org/obo/MOD_01453 L-glutamic acid 5-methyl ester A protein modification that effectively converts an L-glutamine residue to L-glutamate 5-methyl ester. http://purl.obolibrary.org/obo/MOD_00658 methylated arginine http://purl.obolibrary.org/obo/MOD_00902 modified L-arginine residue 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. http://purl.obolibrary.org/obo/MOD_00660 methylated cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to a methylated cysteine, either S-methylcysteine, or cysteine methyl ester. http://purl.obolibrary.org/obo/MOD_00661 methylated histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively converts an L-histidine residue to a methylated histidine, such as pros-methylhistidine, or tele-methylhistidine. http://purl.obolibrary.org/obo/MOD_00662 methylated leucine http://purl.obolibrary.org/obo/MOD_00911 modified L-leucine residue A protein modification that effectively converts an L-leucine residue to a methylated leucine, either N-methylleucine, or leucine methyl ester. http://purl.obolibrary.org/obo/MOD_00664 stereoisomerized residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process A protein modification that effectively replaces a residue L-enantiomer (stereoisomer) with a D-enantiomer or with a different diastereomeric isomer. http://purl.obolibrary.org/obo/MOD_00665 methylated alanine http://purl.obolibrary.org/obo/MOD_00901 modified L-alanine residue 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. http://purl.obolibrary.org/obo/MOD_00667 decanoylated residue http://purl.obolibrary.org/obo/MOD_01155 lipoconjugated residue A protein modification that effectively replaces a hydrogen atom with a decanoyl group. http://purl.obolibrary.org/obo/MOD_00668 O-decanoylated residue http://purl.obolibrary.org/obo/MOD_00671 O-acylated residue A protein modification that effectively replaces a residue hydroxyl group with a decanoyloxy group. http://purl.obolibrary.org/obo/MOD_00669 O-octanoylated residue http://purl.obolibrary.org/obo/MOD_00666 octanoylated residue A protein modification that effectively replaces a residue hydroxyl group with a octanoyloxy group. http://purl.obolibrary.org/obo/MOD_00671 O-acylated residue http://purl.obolibrary.org/obo/MOD_00649 acylated residue A protein modification that effectively replaces a residue hydroxyl group with a acyloxy group. http://purl.obolibrary.org/obo/MOD_00672 S-acylated residue http://purl.obolibrary.org/obo/MOD_00649 acylated residue A protein modification that effectively replaces a residue sulfanyl group with an acylsulfanyl group. http://purl.obolibrary.org/obo/MOD_00673 methylated asparagine http://purl.obolibrary.org/obo/MOD_00903 modified L-asparagine residue 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. http://purl.obolibrary.org/obo/MOD_00674 amidated residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process A protein modification that effectively replaces a carboxyl group with a carboxamido group. http://purl.obolibrary.org/obo/MOD_00675 oxidized residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process 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. http://purl.obolibrary.org/obo/MOD_00676 oxygenated residue http://purl.obolibrary.org/obo/MOD_00675 oxidized residue A protein modification that effectively adds oxygen atoms to a residue with or without the removal of hydrogen atoms. http://purl.obolibrary.org/obo/MOD_00678 hydroxylated proline http://purl.obolibrary.org/obo/MOD_00915 modified L-proline residue A protein modification that effectively converts an L-proline residue to an hydroxylated L-proline. http://purl.obolibrary.org/obo/MOD_00679 carbon oxygenated residue http://purl.obolibrary.org/obo/MOD_00676 oxygenated residue A protein modification that effectively adds oxygen atoms to a carbon atom of a residue and removes hydrogen atoms. http://purl.obolibrary.org/obo/MOD_00680 sulfur oxygenated residue http://purl.obolibrary.org/obo/MOD_00676 oxygenated residue A protein modification that effectively adds oxygen atoms to a sulfur atom of a residue without removing hydrogen atoms. http://purl.obolibrary.org/obo/MOD_00681 hydroxylated lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively converts an L-lysine residue to a hydroxylated L-lysine. http://purl.obolibrary.org/obo/MOD_00682 hydroxylated arginine http://purl.obolibrary.org/obo/MOD_00902 modified L-arginine residue A protein modification that effectively converts an L-arginine residue to a hydroxylated L-arginine. http://purl.obolibrary.org/obo/MOD_00683 dehydrogenated residue http://purl.obolibrary.org/obo/MOD_00675 oxidized residue A protein modification that effectively removes neutral hydrogen atoms (proton and electron) from a residue. http://purl.obolibrary.org/obo/MOD_00684 deamidated L-asparagine http://purl.obolibrary.org/obo/MOD_00903 modified L-asparagine residue A protein modification that effectively converts an L-asparagine residue to L-aspartic acid. http://purl.obolibrary.org/obo/MOD_00685 deamidated L-glutamine http://purl.obolibrary.org/obo/MOD_00907 modified L-glutamine residue A protein modification that effectively converts an L-glutamine residue to L-glutamic acid. http://purl.obolibrary.org/obo/MOD_00686 L-selenocysteine (Cys) http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to L-selenocysteine (not known as a natural, post-translational modification process). http://purl.obolibrary.org/obo/MOD_00687 thioether crosslinked residues http://purl.obolibrary.org/obo/MOD_02044 crosslinked L-cysteine residue 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. http://purl.obolibrary.org/obo/MOD_00688 isopeptide crosslinked residues http://purl.obolibrary.org/obo/MOD_00033 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. http://purl.obolibrary.org/obo/MOD_00689 disulfide crosslinked residues http://purl.obolibrary.org/obo/MOD_01619 multisulfide crosslinked residues A protein modification that crosslinks two cysteine residues by formation of a disulfide bond. http://purl.obolibrary.org/obo/MOD_00690 oxazole/thiazole ring crosslinked residues http://purl.obolibrary.org/obo/MOD_00033 crosslinked residues A protein modification that crosslinks two residues by formation of an oxazole or thiazole ring. http://purl.obolibrary.org/obo/MOD_00691 5-imidazolinone ring crosslinked residues http://purl.obolibrary.org/obo/MOD_00033 crosslinked residues A protein modification that crosslinks two residues by formation of an 5-imidazolinone ring. http://purl.obolibrary.org/obo/MOD_00692 uncategorized crosslinked residues http://purl.obolibrary.org/obo/MOD_00033 crosslinked residues A protein crosslink modification that is not chemically categorized. http://purl.obolibrary.org/obo/MOD_00694 halogen containing residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process A protein modification that effectively substitutes a halogen atom for a hydrogen atom. http://purl.obolibrary.org/obo/MOD_00695 sulfated residue http://purl.obolibrary.org/obo/MOD_00860 sulfur containing modified residue A protein modification that effectively substitutes a sulfonyl group for the hydrogen atom of a hydroxyl or sulfanyl group. http://purl.obolibrary.org/obo/MOD_00697 flavin modified residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process A protein modification that effectively results from forming an adduct with a compound containing a flavin group. http://purl.obolibrary.org/obo/MOD_00698 metal or metal cluster containing modified residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process A protein modification that effectively substitutes a metal atom or a metal cluster for hydrogen atoms, or coordinates a metal ion. http://purl.obolibrary.org/obo/MOD_00699 porphyrin modified residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process A protein modification that effectively results from forming an adduct with a compound containing a porphyrin group. http://purl.obolibrary.org/obo/MOD_00700 tetrapyrrole modified residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process A protein modification that effectively results from forming an adduct with a compound containing a tetrapyrrole group. http://purl.obolibrary.org/obo/MOD_00702 isotope labeled residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process A protein modification that effectively substitutes atoms of particular common isotopes with atoms or groups containing isotopes that are not the most common. http://purl.obolibrary.org/obo/MOD_00704 dehydrated residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process A protein modification that effectively forms a double bond by removing a molecule of water from a residue. http://purl.obolibrary.org/obo/MOD_00705 D-valine http://purl.obolibrary.org/obo/MOD_00664 stereoisomerized residue A protein modification that effectively converts an L-valine residue to D-valine. http://purl.obolibrary.org/obo/MOD_00706 dehydrogenated tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively converts L-tyrosine to 2,3-didehydrotyrosine. http://purl.obolibrary.org/obo/MOD_00707 hydroxylated tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue a protein modification that effectively converts an L-tyrosine residue to a multihydroxylated L-phenylalanine http://purl.obolibrary.org/obo/MOD_00708 sulfur oxygenated L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively adds oxygen atoms to a sulfur atom of L-cysteine residue without removing hydrogen atoms. http://purl.obolibrary.org/obo/MOD_00709 sulfur oxygenated L-methionine http://purl.obolibrary.org/obo/MOD_00913 modified L-methionine residue A protein modification that effectively adds oxygen atoms to a sulfur atom of L-methionine residue without removing hydrogen atoms. http://purl.obolibrary.org/obo/MOD_00710 protonated-dimethylated residue http://purl.obolibrary.org/obo/MOD_00429 dimethylated residue A protein modification that effectively adds a proton and replaces two hydrogen atoms with two methyl groups. http://purl.obolibrary.org/obo/MOD_00711 trimethylated protonated-residue http://purl.obolibrary.org/obo/MOD_00427 methylated 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. http://purl.obolibrary.org/obo/MOD_00712 methylated proline http://purl.obolibrary.org/obo/MOD_00915 modified L-proline residue A protein modification that effectively converts an L-proline residue to a methylated proline, such as N,N-dimethylproline. http://purl.obolibrary.org/obo/MOD_00713 methylated glutamic acid http://purl.obolibrary.org/obo/MOD_00906 modified L-glutamic acid residue A protein modification that effectively converts an L-glutamic acid residue to a methylated glutamic acid, such as L-glutamate 5-methyl ester. http://purl.obolibrary.org/obo/MOD_00714 methylated glycine http://purl.obolibrary.org/obo/MOD_00908 modified glycine residue A protein modification that effectively converts a glycine residue to a methylated glycine, such as N-methylglycine. http://purl.obolibrary.org/obo/MOD_00715 methylated isoleucine http://purl.obolibrary.org/obo/MOD_00910 modified L-isoleucine residue A protein modification that effectively converts an L-isoleucine residue to a methylated isoleucine residue, such as N-methyl-L-isoleucine. http://purl.obolibrary.org/obo/MOD_00716 methylated methionine http://purl.obolibrary.org/obo/MOD_00913 modified L-methionine residue A protein modification that effectively converts an L-methionine residue to a methylated methionine, such as N-methyl-L-methionine. http://purl.obolibrary.org/obo/MOD_00717 methylated phenylalanine http://purl.obolibrary.org/obo/MOD_00914 modified L-phenylalanine residue A protein modification that effectively converts an L-phenylalanine residue to a methylated phenylalanine, such as N-methyl-L-phenylalanine. http://purl.obolibrary.org/obo/MOD_00718 methylated tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively converts an L-tyrosine residue to a methylated tyrosine, such as N-methyl-L-tyrosine. http://purl.obolibrary.org/obo/MOD_00719 L-methionine sulfoxide http://purl.obolibrary.org/obo/MOD_01854 sulfur monooxygenated residue A protein modification that oxygenates an L-methionine residue to one of the diastereomeric L-methionine sulfoxide residues. http://purl.obolibrary.org/obo/MOD_00720 L-methionine (R)-sulfoxide http://purl.obolibrary.org/obo/MOD_00719 L-methionine sulfoxide A protein modification that effectively oxygenates an L-methionine residue to L-methionine sulfoxide R-diastereomer. http://purl.obolibrary.org/obo/MOD_00721 L-methionine (S)-sulfoxide http://purl.obolibrary.org/obo/MOD_00719 L-methionine sulfoxide A protein modification that effectively oxygenates an L-methionine residue to L-methionine sulfoxide S-diastereomer. http://purl.obolibrary.org/obo/MOD_00722 monomethylated L-glutamine http://purl.obolibrary.org/obo/MOD_00599 monomethylated residue A protein modification that effectively replaces one hydrogen atom of an L-glutamine residue with one methyl group. http://purl.obolibrary.org/obo/MOD_00724 N-methylated L-histidine http://purl.obolibrary.org/obo/MOD_00599 monomethylated residue A protein modification that effectively replaces one hydrogen atom on a nitrogen of an L-histidine residue with one methyl group. http://purl.obolibrary.org/obo/MOD_00725 complex glycosylation http://purl.obolibrary.org/obo/MOD_00693 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 linked through a glycosidic bond. http://purl.obolibrary.org/obo/MOD_00726 glucosylated residue http://purl.obolibrary.org/obo/MOD_00693 glycosylated 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. http://purl.obolibrary.org/obo/MOD_00727 mannosylated residue http://purl.obolibrary.org/obo/MOD_00693 glycosylated 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, http://purl.obolibrary.org/obo/MOD_00728 galactosylated residue http://purl.obolibrary.org/obo/MOD_00693 glycosylated 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. http://purl.obolibrary.org/obo/MOD_00729 pentosylated residue http://purl.obolibrary.org/obo/MOD_00693 glycosylated 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 http://purl.obolibrary.org/obo/MOD_00730 arabinosylated residue http://purl.obolibrary.org/obo/MOD_00729 pentosylated 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 http://purl.obolibrary.org/obo/MOD_00731 ribosylated residue http://purl.obolibrary.org/obo/MOD_00729 pentosylated 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 http://purl.obolibrary.org/obo/MOD_00732 xylosylated residue http://purl.obolibrary.org/obo/MOD_00729 pentosylated 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 http://purl.obolibrary.org/obo/MOD_00733 N-acetylaminoglucosylated residue http://purl.obolibrary.org/obo/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-acetylglucosamine group through a glycosidic bond. http://purl.obolibrary.org/obo/MOD_00734 N-acetylaminogalactosylated residue http://purl.obolibrary.org/obo/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-acetylgalactosamine group through a glycosidic bond. http://purl.obolibrary.org/obo/MOD_00735 hexosuronylated residue http://purl.obolibrary.org/obo/MOD_00693 glycosylated 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. http://purl.obolibrary.org/obo/MOD_00736 deoxyhexosylated residue http://purl.obolibrary.org/obo/MOD_00693 glycosylated 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 http://purl.obolibrary.org/obo/MOD_00737 N-acetylneuraminylated residue http://purl.obolibrary.org/obo/MOD_00693 glycosylated 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. http://purl.obolibrary.org/obo/MOD_00738 iron containing modified residue http://purl.obolibrary.org/obo/MOD_00698 metal or metal cluster 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. http://purl.obolibrary.org/obo/MOD_00739 iron-sulfur cluster containing modification http://purl.obolibrary.org/obo/MOD_00860 sulfur containing modified residue A protein modification that effectively substitutes a cluster of iron and sulfur atoms for hydrogen atoms. http://purl.obolibrary.org/obo/MOD_00740 manganese containing modified residue http://purl.obolibrary.org/obo/MOD_00698 metal or metal cluster 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. http://purl.obolibrary.org/obo/MOD_00741 nickel containing modified residue http://purl.obolibrary.org/obo/MOD_00698 metal or metal cluster 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. http://purl.obolibrary.org/obo/MOD_00742 copper containing modified residue http://purl.obolibrary.org/obo/MOD_00698 metal or metal cluster 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. http://purl.obolibrary.org/obo/MOD_00743 molybdenum containing modified residue http://purl.obolibrary.org/obo/MOD_00698 metal or metal cluster 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. http://purl.obolibrary.org/obo/MOD_00744 molybdenum pterin containing modification http://purl.obolibrary.org/obo/MOD_00748 pterin modified residue A protein modification containing a molybdenum atom in a pterin ring system. http://purl.obolibrary.org/obo/MOD_00745 selenium containing residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process A protein modification that effectively substitutes a selenium atom or a cluster containing selenium for hydrogen atoms. http://purl.obolibrary.org/obo/MOD_00746 tungsten containing modified residue http://purl.obolibrary.org/obo/MOD_00698 metal or metal cluster 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. http://purl.obolibrary.org/obo/MOD_00747 sodium containing modified residue http://purl.obolibrary.org/obo/MOD_00698 metal or metal cluster containing modified residue A protein modification that effectively substitutes a sodium atom for a hydrogen atom. http://purl.obolibrary.org/obo/MOD_00748 pterin modified residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process A protein modification that effectively results from forming an adduct with a compound containing a pterin group. http://purl.obolibrary.org/obo/MOD_00749 sulfur substitution for oxygen http://purl.obolibrary.org/obo/MOD_00860 sulfur containing modified residue A protein modification that effectively substitutes a sulfur atom for an oxygen atom. http://purl.obolibrary.org/obo/MOD_00750 deoxyribonucleic acid linked residue http://purl.obolibrary.org/obo/MOD_00701 nucleotide or nucleic acid modified residue A protein modification that effectively crosslinks an amino acid residue and the 3'- or 5'-end of DNA through a phosphodiester bond. http://purl.obolibrary.org/obo/MOD_00751 ribonucleic acid linked residue http://purl.obolibrary.org/obo/MOD_00701 nucleotide or nucleic acid modified residue a protein modification http://purl.obolibrary.org/obo/MOD_00753 chlorinated residue http://purl.obolibrary.org/obo/MOD_00694 halogen containing residue A protein modification that effectively substitutes a chlorine atom for a hydrogen atom. http://purl.obolibrary.org/obo/MOD_00755 iodinated residue http://purl.obolibrary.org/obo/MOD_00694 halogen containing residue A protein modification that effectively substitutes an iodine atom of a residue for a hydrogen atom. http://purl.obolibrary.org/obo/MOD_00756 4-hydroxy-D-valine http://purl.obolibrary.org/obo/MOD_00664 stereoisomerized residue A protein modification that effectively converts an L-valine residue to 4-hydroxy-D-valine. http://purl.obolibrary.org/obo/MOD_00757 O4-galactosyl-L-hydroxyproline http://purl.obolibrary.org/obo/MOD_00915 modified L-proline residue A protein modification that effectively converts an L-proline residue to O4-galactosyl-L-hydroxyproline. http://purl.obolibrary.org/obo/MOD_00758 O4-(N-acetylamino)glucosyl-L-hydroxyproline http://purl.obolibrary.org/obo/MOD_01677 O4-(N-acetylamino)hexosyl-L-hydroxyproline A protein modification that effectively converts an L-proline residue to O4-(N-acetylamino)glucosyl-L-hydroxyproline. http://purl.obolibrary.org/obo/MOD_00759 fucosylated biantennary (-1 galactose) N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine modification from Unimod N-linked glycosylation http://purl.obolibrary.org/obo/MOD_00760 biantennary N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine modification from Unimod N-linked glycosylation - missing ref http://purl.obolibrary.org/obo/MOD_00761 monohexosylated residue http://purl.obolibrary.org/obo/MOD_00434 hexosylated 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. http://purl.obolibrary.org/obo/MOD_00762 biantennary (-2 galactose) N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine modification from Unimod N-linked glycosylation - missing ref http://purl.obolibrary.org/obo/MOD_00763 biantennary (-1 galactose) N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine modification from Unimod N-linked glycosylation - missing ref http://purl.obolibrary.org/obo/MOD_00765 cysteinylation (disulfide with free L-cysteine) http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-(L-cysteinyl)-L-cysteine, forming a disulfide bond with free cysteine. http://purl.obolibrary.org/obo/MOD_00767 glycated residue http://purl.obolibrary.org/obo/MOD_00764 glycoconjugated 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. http://purl.obolibrary.org/obo/MOD_00768 methionine oxidation with neutral loss of 80 Da http://purl.obolibrary.org/obo/MOD_00431 modified residue with a secondary neutral loss Oxidation of methionine to methionine sulfone with neutral loss of CH3SO2H. http://purl.obolibrary.org/obo/MOD_00769 residues isobaric at 71.0-71.1 Da http://purl.obolibrary.org/obo/MOD_00616 residues isobaric at a resolution below 0.1 Da Natural or modified residues with a mass of 71.0-71.1 Da. http://purl.obolibrary.org/obo/MOD_00770 residues isobaric at a resolution below 0.01 Da http://purl.obolibrary.org/obo/MOD_00616 residues isobaric at a resolution below 0.1 Da Natural or modified residues that are isobaric at a resolution below 0.01 Da. http://purl.obolibrary.org/obo/MOD_00771 residues isobaric at 166.98-167.00 Da http://purl.obolibrary.org/obo/MOD_00770 residues isobaric at a resolution below 0.01 Da Natural or modified residues with a mass of 166.98-167.00 Da. http://purl.obolibrary.org/obo/MOD_00772 vanadium containing modified residue http://purl.obolibrary.org/obo/MOD_00698 metal or metal cluster 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. http://purl.obolibrary.org/obo/MOD_00773 residues isobaric at 181.00-181.02 Da http://purl.obolibrary.org/obo/MOD_00770 residues isobaric at a resolution below 0.01 Da Natural or modified residues with a mass of 181.00-181.02 Da. http://purl.obolibrary.org/obo/MOD_00774 residues isobaric at 243.02-243.03 Da http://purl.obolibrary.org/obo/MOD_00770 residues isobaric at a resolution below 0.01 Da Natural or modified residues with a mass of 243.02-243.03 Da. http://purl.obolibrary.org/obo/MOD_00775 L-asparagine (His) http://purl.obolibrary.org/obo/MOD_02088 natural, standard, encoded residue substitution An artifactual protein modification that converts an L-histidine residue to L-asparagine by oxidative degradation. http://purl.obolibrary.org/obo/MOD_00776 L-aspartic acid (His) http://purl.obolibrary.org/obo/MOD_02088 natural, standard, encoded residue substitution An artifactual protein modification that converts an L-histidine residue to L-aspartic acid by oxidative degradation. http://purl.obolibrary.org/obo/MOD_00777 residues isobaric at 182.96-182.98 Da http://purl.obolibrary.org/obo/MOD_00778 residues isobaric at 182.9-183.0 Da Natural or modified residues with a mass of 182.96-182.98 Da. http://purl.obolibrary.org/obo/MOD_00778 residues isobaric at 182.9-183.0 Da http://purl.obolibrary.org/obo/MOD_00616 residues isobaric at a resolution below 0.1 Da Natural or modified residues with a mass of 182.9-183.0 Da. http://purl.obolibrary.org/obo/MOD_00780 N-acetyl-L-asparagine http://purl.obolibrary.org/obo/MOD_00903 modified L-asparagine residue A protein modification that effectively converts an L-asparagine residue to N-acetyl-L-asparagine. http://purl.obolibrary.org/obo/MOD_00781 N2-acetyl-L-histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively converts an L-histidine residue to N2-acetyl-L-histidine. http://purl.obolibrary.org/obo/MOD_00782 N-acetyl-L-leucine http://purl.obolibrary.org/obo/MOD_00911 modified L-leucine residue A protein modification that effectively converts an L-leucine residue to N-acetyl-L-leucine. http://purl.obolibrary.org/obo/MOD_00784 N-acetyl-L-phenylalanine http://purl.obolibrary.org/obo/MOD_00914 modified L-phenylalanine residue A protein modification that effectively converts an L-phenylalanine residue to N-acetyl-L-phenylalanine. http://purl.obolibrary.org/obo/MOD_00785 N2-acetyl-L-tryptophan http://purl.obolibrary.org/obo/MOD_00918 modified L-tryptophan residue A protein modification that effectively converts an L-tryptophan residue to N2-acetyl-L-tryptophan. http://purl.obolibrary.org/obo/MOD_00786 deuterium substituted residue http://purl.obolibrary.org/obo/MOD_00839 (2)H deuterium labeled residue A protein modification that effectively substitutes one or more (2)H deuterium atoms for (1)H protium atoms. http://purl.obolibrary.org/obo/MOD_00787 diisopropylphosphoserine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue modification from Unimod - label for the active site serine of the serine esterase/protease family also shown to label tyrosine in serum albumin http://purl.obolibrary.org/obo/MOD_00788 isopropylphosphotyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue modification from Unimod http://purl.obolibrary.org/obo/MOD_00789 Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, heavy form http://purl.obolibrary.org/obo/MOD_01428 (13)C isotope tagged reagent 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. http://purl.obolibrary.org/obo/MOD_00790 Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, light form http://purl.obolibrary.org/obo/MOD_01426 isotope tagged reagent derivatized residue 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. http://purl.obolibrary.org/obo/MOD_00791 1x(18)O labeled deamidated L-glutamine http://purl.obolibrary.org/obo/MOD_00852 1x(18)O labeled deamidated residue A protein modification that effectively converts an L-glutamine residue to L-glutamic acid with one (18)O. http://purl.obolibrary.org/obo/MOD_00792 deuterium monosubstituted residue http://purl.obolibrary.org/obo/MOD_00786 deuterium substituted residue A protein modification that effectively substitutes one (2)H deuterium atom for one (1)H protium atom. http://purl.obolibrary.org/obo/MOD_00793 dehydroalanine (Cys) http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to dehydroalanine. http://purl.obolibrary.org/obo/MOD_00795 Michael addition of hydroxymethylvinyl ketone to cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue modification from Unimod http://purl.obolibrary.org/obo/MOD_00796 L-ornithine (Arg) http://purl.obolibrary.org/obo/MOD_00902 modified L-arginine residue A protein modification that effectively converts an L-arginine residue to L-ornithine. http://purl.obolibrary.org/obo/MOD_00797 2-(S-L-cysteinyl)pyruvic acid O-phosphothioketal http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue a protein modification that effectively converts an L-cysteine residue to the PEP adduct, 2-(S-L-cysteinyl)pyruvic acid O-phosphothioketal http://purl.obolibrary.org/obo/MOD_00798 half cystine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue 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. http://purl.obolibrary.org/obo/MOD_00799 S-galactosyl-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-galactosyl-L-cysteine. http://purl.obolibrary.org/obo/MOD_00800 L-cysteinyl-L-histidino-homocitryl vanadium heptairon nonasulfide http://purl.obolibrary.org/obo/MOD_02070 metal or metal cluster coordinated L-histidine residue 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. http://purl.obolibrary.org/obo/MOD_00801 L-cysteinyl-L-histidino-homocitryl octairon nonasulfide http://purl.obolibrary.org/obo/MOD_02070 metal or metal cluster coordinated L-histidine residue 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. http://purl.obolibrary.org/obo/MOD_00802 L-histidino vanadium tetraoxide http://purl.obolibrary.org/obo/MOD_02070 metal or metal cluster coordinated L-histidine residue a protein modification that effectively converts an L-histidine residue to L-histidino vanadium tetraoxide http://purl.obolibrary.org/obo/MOD_00803 3-(S-L-cysteinyl)-L-tyrosine http://purl.obolibrary.org/obo/MOD_02058 crosslinked L-tyrosine residue 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. http://purl.obolibrary.org/obo/MOD_00804 O-glucosyl-L-serine http://purl.obolibrary.org/obo/MOD_00433 monoglucosylated residue A protein modification that effectively converts an L-serine residue to O3-beta-glucosylated L-serine. http://purl.obolibrary.org/obo/MOD_00807 pyruvic acid (Ser) http://purl.obolibrary.org/obo/MOD_01160 deaminated residue A protein modification that effectively converts an L-serine residue to pyruvic acid. http://purl.obolibrary.org/obo/MOD_00808 O-galactosyl-L-serine http://purl.obolibrary.org/obo/MOD_00476 monogalactosylated residue A protein modification that effectively converts an L-serine residue to O3-galactosylserine. http://purl.obolibrary.org/obo/MOD_00809 O-galactosyl-L-threonine http://purl.obolibrary.org/obo/MOD_01348 O-hexosylated threonine A protein modification that effectively converts an L-threonine residue to O3-galactosylthreonine. http://purl.obolibrary.org/obo/MOD_00810 O-mannosyl-L-serine http://purl.obolibrary.org/obo/MOD_00595 monomannosylated residue A protein modification that effectively converts an L-serine residue to O3-mannosylserine. http://purl.obolibrary.org/obo/MOD_00811 O-mannosyl-L-threonine http://purl.obolibrary.org/obo/MOD_01348 O-hexosylated threonine a protein modification that effectively forms a O3-mannosylthreonine http://purl.obolibrary.org/obo/MOD_00816 S-stearoyl-L-cysteine http://purl.obolibrary.org/obo/MOD_02006 S-stearoylated residue A protein modification that effectively converts an L-cysteine residue to S-stearoyl-L-cysteine. http://purl.obolibrary.org/obo/MOD_00817 3'-geranyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan http://purl.obolibrary.org/obo/MOD_00601 cyclized residue A protein modification that effectively converts an L-tryptophan residue to 3'-geranyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan. http://purl.obolibrary.org/obo/MOD_00819 L-2-aminobutanoic acid (Glu) http://purl.obolibrary.org/obo/MOD_00906 modified L-glutamic acid residue A protein modification that effectively converts an L-glutamic acid residue to L-2-aminobutanoic acid. http://purl.obolibrary.org/obo/MOD_00820 2-imino-alanine 5-imidazolinone glycine http://purl.obolibrary.org/obo/MOD_02047 crosslinked glycine residue A protein modification that effectively crosslinks an L-aspartic acid residue and a glycine residue to form 2-imino-alanine 5-imidazolinone glycine. http://purl.obolibrary.org/obo/MOD_00821 S-(L-alanyl)-L-cysteine http://purl.obolibrary.org/obo/MOD_02040 crosslinked L-alanine residue 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. http://purl.obolibrary.org/obo/MOD_00822 S-(L-leucyl)-L-cysteine http://purl.obolibrary.org/obo/MOD_02050 crosslinked L-leucine residue 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. http://purl.obolibrary.org/obo/MOD_00823 S-(L-methionyl)-L-cysteine http://purl.obolibrary.org/obo/MOD_02052 crosslinked L-methionine residue 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. http://purl.obolibrary.org/obo/MOD_00824 dehydroalanine (Tyr) http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively converts an L-tyrosine residue to dehydroalanine. http://purl.obolibrary.org/obo/MOD_00825 S-(L-phenylalanyl)-L-cysteine http://purl.obolibrary.org/obo/MOD_02053 crosslinked L-phenylalanine residue 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. http://purl.obolibrary.org/obo/MOD_00826 S-(L-threonyl)-L-cysteine http://purl.obolibrary.org/obo/MOD_02056 crosslinked L-threonine residue 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. http://purl.obolibrary.org/obo/MOD_00827 S-(L-tyrosyl)-L-cysteine http://purl.obolibrary.org/obo/MOD_02058 crosslinked L-tyrosine residue 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. http://purl.obolibrary.org/obo/MOD_00828 S-(L-tryptophanyl)-L-cysteine http://purl.obolibrary.org/obo/MOD_02057 crosslinked L-tryptophan residue 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. http://purl.obolibrary.org/obo/MOD_00829 O-(L-phenylalanyl)-L-serine http://purl.obolibrary.org/obo/MOD_02055 crosslinked L-serine residue 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. http://purl.obolibrary.org/obo/MOD_00830 N-methyl-L-proline http://purl.obolibrary.org/obo/MOD_01680 alpha-amino monomethylated residue A protein modification that effectively converts an L-proline residue to an N-methyl-L-proline. http://purl.obolibrary.org/obo/MOD_00832 N4-(N-acetylamino)galactosyl-L-asparagine http://purl.obolibrary.org/obo/MOD_01674 N4-(N-acetylamino)hexosyl-L-asparagine A protein modification that effectively converts an L-asparagine residue to N4-(N-acetaminogalactosyl)-L-asparagine. http://purl.obolibrary.org/obo/MOD_00833 N4-glucosyl-L-asparagine http://purl.obolibrary.org/obo/MOD_01346 N4-hexosylated asparagine A protein modification that effectively converts an L-asparagine residue to N4-glucosyl-asparagine. http://purl.obolibrary.org/obo/MOD_00834 O-(N-acetylamino)fucosyl-L-serine http://purl.obolibrary.org/obo/MOD_00002 O-glycosyl-L-serine A protein modification that effectively converts an L-serine residue to O3-(N-acetamino)fucosylserine. http://purl.obolibrary.org/obo/MOD_00835 L-3-oxoalanine (Ser) http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to L-oxoalanine. http://purl.obolibrary.org/obo/MOD_00836 deuterium disubstituted residue http://purl.obolibrary.org/obo/MOD_00786 deuterium substituted residue A protein modification that effectively substitutes two (2)H deuterium atoms for two (1)H protium atoms. http://purl.obolibrary.org/obo/MOD_00837 deuterium tetrasubstituted residue http://purl.obolibrary.org/obo/MOD_00786 deuterium substituted residue A protein modification that effectively substitutes four (2)H deuterium atoms for four (1)H protium atoms. http://purl.obolibrary.org/obo/MOD_00838 3x(2)H labeled L-leucine http://purl.obolibrary.org/obo/MOD_00911 modified L-leucine residue 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. http://purl.obolibrary.org/obo/MOD_00839 (2)H deuterium labeled residue http://purl.obolibrary.org/obo/MOD_00702 isotope labeled residue A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing deuteriumm, (2)H. http://purl.obolibrary.org/obo/MOD_00840 isocyanate reagent derivatized residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue A protein modification produced by formation of an adduct with an isocyanate compound. http://purl.obolibrary.org/obo/MOD_00841 isothiocyanate reagent derivatized residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue A protein modification produced by formation of an adduct with an isothiocyanate compound. http://purl.obolibrary.org/obo/MOD_00842 (13)C labeled residue http://purl.obolibrary.org/obo/MOD_00702 isotope labeled residue A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing (13)C. http://purl.obolibrary.org/obo/MOD_00843 (15)N labeled residue http://purl.obolibrary.org/obo/MOD_00702 isotope labeled residue A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing (15)N. http://purl.obolibrary.org/obo/MOD_00844 (18)O labeled residue http://purl.obolibrary.org/obo/MOD_00702 isotope labeled residue A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing (18)O. http://purl.obolibrary.org/obo/MOD_00845 (18)O substituted residue http://purl.obolibrary.org/obo/MOD_00844 (18)O labeled residue A protein modification that effectively substitutes one or more (18)O atoms for (16)O atoms. http://purl.obolibrary.org/obo/MOD_00846 levuglandinyl (prostaglandin H2) adduct http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue stub http://purl.obolibrary.org/obo/MOD_00847 (18)O disubstituted residue http://purl.obolibrary.org/obo/MOD_00845 (18)O substituted residue A protein modification that effectively substitutes two (18)O atom for two (16)O atoms. http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process A protein modification that is produced by formation of an adduct with a particular compound used as a reagent. http://purl.obolibrary.org/obo/MOD_00849 potassium containing modified residue http://purl.obolibrary.org/obo/MOD_00698 metal or metal cluster containing modified residue A protein modification that effectively substitutes a potassium atom for a hydrogen atom. http://purl.obolibrary.org/obo/MOD_00850 unnatural residue http://purl.obolibrary.org/obo/MOD_01157 protein modification categorized by amino acid modified 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. http://purl.obolibrary.org/obo/MOD_00851 (18)O labeled deamidated residue http://purl.obolibrary.org/obo/MOD_00844 (18)O labeled residue A protein modification that effectively replaces a carboxamido group with a carboxyl group labeled with (18)O. http://purl.obolibrary.org/obo/MOD_00852 1x(18)O labeled deamidated residue http://purl.obolibrary.org/obo/MOD_00851 (18)O labeled deamidated residue A protein modification that effectively replaces a carboxamido group with a carboxyl group labeled with one (18)O. http://purl.obolibrary.org/obo/MOD_00853 2x(18)O labeled deamidated residue http://purl.obolibrary.org/obo/MOD_00851 (18)O labeled deamidated residue A protein modification that effectively replaces a carboxamido group with a carboxyl group labeled with two (18)O. http://purl.obolibrary.org/obo/MOD_00854 protonated L-lysine (L-lysinium) residue http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively converts an L-lysine to L-lysinium (protonated L-lysine). http://purl.obolibrary.org/obo/MOD_00855 N6,N6,N6-trimethyl-L-lysine (from L-lysinium residue) http://purl.obolibrary.org/obo/MOD_00430 trimethylated residue A protein modification that effectively converts an L-lysinium (N6-protonated L-lysine) residue to an N6,N6,N6-trimethyl-L-lysine. http://purl.obolibrary.org/obo/MOD_00856 protonated L-alanine (L-alaninium) residue http://purl.obolibrary.org/obo/MOD_00901 modified L-alanine residue A protein modification that effectively converts an L-alanine residue to an L-alaninium (protonated L-alanine). http://purl.obolibrary.org/obo/MOD_00857 N,N,N-trimethyl-L-alanine (from L-alaninium) http://purl.obolibrary.org/obo/MOD_01687 alpha-amino trimethylated residue A protein modification that effectively converts an L-alaninium (protonated L-alanine) residue to an N,N,N-trimethyl-L-alanine. http://purl.obolibrary.org/obo/MOD_00858 D-alanine (Ser) http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to D-alanine. http://purl.obolibrary.org/obo/MOD_00859 modified residue that can arise from different natural residues http://purl.obolibrary.org/obo/MOD_01157 protein modification categorized by amino acid modified A protein modification that can be derived from different natural residues by different chemical processes. http://purl.obolibrary.org/obo/MOD_00860 sulfur containing modified residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process A protein modification that produces an amino acid residue containing an exogenous sulfur atom. http://purl.obolibrary.org/obo/MOD_00861 phosphorus containing modified residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process A protein modification that produces an amino acid residue containing a phosphorus atom. http://purl.obolibrary.org/obo/MOD_00862 D-alanine http://purl.obolibrary.org/obo/MOD_00859 modified residue that can arise from different natural residues A protein modification that effectively converts a source amino acid residue to D-alanine. http://purl.obolibrary.org/obo/MOD_00863 D-allo-threonine http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue A protein modification that effectively converts an L-threonine residue to D-allo-threonine. http://purl.obolibrary.org/obo/MOD_00864 tris-L-cysteinyl L-histidino diiron disulfide http://purl.obolibrary.org/obo/MOD_02070 metal or metal cluster coordinated L-histidine residue 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. http://purl.obolibrary.org/obo/MOD_00865 N-aspartyl-glycosylsphingolipidinositolethanolamine http://purl.obolibrary.org/obo/MOD_00904 modified L-aspartic acid residue A protein modification that effectively converts an L-aspartic acid residue to N-aspartyl-glycosylsphingolipidinositolethanolamine. http://purl.obolibrary.org/obo/MOD_00866 dihydroxylated proline http://purl.obolibrary.org/obo/MOD_00678 hydroxylated 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. http://purl.obolibrary.org/obo/MOD_00867 L-cysteinyl-L-selenocysteine (Cys-Cys) http://purl.obolibrary.org/obo/MOD_01627 L-cysteinyl-L-selenocysteine 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. http://purl.obolibrary.org/obo/MOD_00868 natural, non-standard encoded residue http://purl.obolibrary.org/obo/MOD_00009 natural 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. http://purl.obolibrary.org/obo/MOD_00869 L-alanine residue (Asp) http://purl.obolibrary.org/obo/MOD_02088 natural, standard, encoded residue substitution A protein modification that effectively converts an L-aspartic acid residue to L-alanine. http://purl.obolibrary.org/obo/MOD_00870 phenyl isocyanate derivatized residue http://purl.obolibrary.org/obo/MOD_00840 isocyanate reagent derivatized residue A protein modification produced by formation of an adduct with phenyl isocyanate. http://purl.obolibrary.org/obo/MOD_00871 (2)H5-phenyl isocyanate derivatized residue http://purl.obolibrary.org/obo/MOD_01431 (2)H deuterium tagged reagent A protein modification produced by formation of an adduct with (2)H5-phenyl isocyanate. http://purl.obolibrary.org/obo/MOD_00873 L-isoglutamyl diglutamic acid http://purl.obolibrary.org/obo/MOD_00207 L-isoglutamyl-polyglutamic 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. http://purl.obolibrary.org/obo/MOD_00874 L-isoglutamyl triglutamic acid http://purl.obolibrary.org/obo/MOD_00207 L-isoglutamyl-polyglutamic 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. http://purl.obolibrary.org/obo/MOD_00875 L-isoglutamyl tetraglutamic acid http://purl.obolibrary.org/obo/MOD_00207 L-isoglutamyl-polyglutamic 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. http://purl.obolibrary.org/obo/MOD_00876 hexosaminylated residue http://purl.obolibrary.org/obo/MOD_00693 glycosylated 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. http://purl.obolibrary.org/obo/MOD_00877 imidoester crosslink dimethyl pimelimidate singly attached http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue dimethyl pimelimidate modification from Unimod http://purl.obolibrary.org/obo/MOD_00878 imidoester crosslink dimethyl pimelimidate doubly attached http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue dimethyl pimelimidate modification from Unimod - Mechanism of the reaction of imidoesters with amines http://purl.obolibrary.org/obo/MOD_00879 naphthalene-2,3-dicarboxaldehyde http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from Unimod http://purl.obolibrary.org/obo/MOD_00880 6x(13)C labeled 4-sulfophenyl isothiocyanate derivatized residue http://purl.obolibrary.org/obo/MOD_01428 (13)C isotope tagged reagent A protein modification produced by formation of an adduct with 6x(13)C labeled 4-sulfophenyl isothiocyanate. http://purl.obolibrary.org/obo/MOD_00882 S-(2-aminoethyl)cysteine (Ser) http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to S-(2-aminoethyl)cysteine. http://purl.obolibrary.org/obo/MOD_00883 C1-amidated residue http://purl.obolibrary.org/obo/MOD_00674 amidated residue A protein modification that effectively replaces a 1-carboxyl group (usually referred to as the alpha-carboxyl) with a carboxamido group. http://purl.obolibrary.org/obo/MOD_00884 S-aminoethylcysteine (Cys) http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-2-aminoethylcysteine. http://purl.obolibrary.org/obo/MOD_00885 ester crosslinked residues http://purl.obolibrary.org/obo/MOD_00033 crosslinked residues A protein modification that crosslinks two residues by formation of an ester bond. http://purl.obolibrary.org/obo/MOD_00886 6'-chloro-L-tryptophan http://purl.obolibrary.org/obo/MOD_01913 monochlorinated L-tryptophan A protein modification that effectively converts an L-tryptophan residue to 6'-chloro-L-tryptophan. http://purl.obolibrary.org/obo/MOD_00887 methylated aspartic acid http://purl.obolibrary.org/obo/MOD_00904 modified L-aspartic acid residue A protein modification that effectively converts an L-aspartic acid residue to a methylated aspartic acid, such as aspartic acid 4-methyl ester. http://purl.obolibrary.org/obo/MOD_00888 protonated L-proline (L-prolinium) residue http://purl.obolibrary.org/obo/MOD_00915 modified L-proline residue A protein modification that effectively converts an L-proline to an L-prolinium (protonated L-proline). http://purl.obolibrary.org/obo/MOD_00889 N,N-dimethyl-L-proline (from L-prolinium) http://purl.obolibrary.org/obo/MOD_01686 alpha-amino dimethylated residue A protein modification that effectively converts an L-prolinium (charged L-proline) residue to N,N-dimethyl-L-proline. http://purl.obolibrary.org/obo/MOD_00890 phosphorylated L-histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively converts an L-histidine residue to a phosphorylated L-histidine, such as pros-phosphohistidine, or tele-phosphohistidine. http://purl.obolibrary.org/obo/MOD_00891 D-serine http://purl.obolibrary.org/obo/MOD_00859 modified residue that can arise from different natural residues A protein modification that effectively converts a source amino acid residue to D-serine. http://purl.obolibrary.org/obo/MOD_00892 D-serine (Cys) http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to D-serine. http://purl.obolibrary.org/obo/MOD_00893 residues isobaric at 128.0-128.1 http://purl.obolibrary.org/obo/MOD_00616 residues isobaric at a resolution below 0.1 Da Natural or modified residues with a mass of 128.0-128.1 Da. http://purl.obolibrary.org/obo/MOD_00894 residues isobaric at 128.058578 Da http://purl.obolibrary.org/obo/MOD_00893 residues isobaric at 128.0-128.1 Natural or modified resiues with a mass of 128.058578 Da. http://purl.obolibrary.org/obo/MOD_00895 FAD modified residue http://purl.obolibrary.org/obo/MOD_00861 phosphorus containing modified residue A protein modification that effectively results from forming an adduct with a compound containing a flavin adenine dinucleotide (FAD) group. http://purl.obolibrary.org/obo/MOD_00896 FMN modified residue http://purl.obolibrary.org/obo/MOD_00861 phosphorus containing modified residue A protein modification that effectively results from forming an adduct with a compound containing a riboflavin phosphate (flavin mononucleotide, FMN) group. http://purl.obolibrary.org/obo/MOD_00897 N-acetyl-S-archeol-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to N-acetyl-S-archeol-L-cysteine. http://purl.obolibrary.org/obo/MOD_00898 S-(sn-1-2-oleoyl-3-palmitoyl-glycerol)cysteine http://purl.obolibrary.org/obo/MOD_00116 S-diacylglycerol-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-(sn-1-2-oleoyl-3-palmitoyl-glycerol)cysteine. http://purl.obolibrary.org/obo/MOD_00899 N-palmitoyl-S-diacylglycerol-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-S-diacylglycerol-L-cysteine. http://purl.obolibrary.org/obo/MOD_00900 N-palmitoyl-S-(sn-1-2-oleoyl-3-palmitoyl-glycerol)cysteine http://purl.obolibrary.org/obo/MOD_00899 N-palmitoyl-S-diacylglycerol-L-cysteine A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-S-(sn-1-2-oleoyl-3-palmitoyl-glycerol)cysteine. http://purl.obolibrary.org/obo/MOD_00922 Cy3 CyDye DIGE Fluor saturation dye http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00923 Cy5 CyDye DIGE Fluor saturation dye http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00924 N6-(L-threonyl)-L-lysine http://purl.obolibrary.org/obo/MOD_02056 crosslinked L-threonine residue 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. http://purl.obolibrary.org/obo/MOD_00925 heptosylated residue http://purl.obolibrary.org/obo/MOD_00693 glycosylated 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. http://purl.obolibrary.org/obo/MOD_00927 2x(13)C,4x(2)H labeled dimethylated residue http://purl.obolibrary.org/obo/MOD_00842 (13)C labeled 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. http://purl.obolibrary.org/obo/MOD_00928 [3-(2,5)-dioxopyrrolidin-1-yloxycarbonyl)-propyl]dimethyloctylammonium http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00929 lactose glycated lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue 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. http://purl.obolibrary.org/obo/MOD_00930 propyl-NAG tyrosine adduct http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue tyrosine adduct with substrate analog inhibitor 1,2-dideoxy-2'-methyl-alpha-D-glucopyranoso-[2,1-d]-Delta2'-thiazoline. http://purl.obolibrary.org/obo/MOD_00931 Michael addition of t-butyl hydroxylated BHT (BHTOH) to C, H or K http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue 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 http://purl.obolibrary.org/obo/MOD_00932 IDBEST tag for quantitation http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue modification from Unimod Isotopic label http://purl.obolibrary.org/obo/MOD_00933 methylglyoxal arginine adduct (+54 amu) http://purl.obolibrary.org/obo/MOD_00902 modified L-arginine residue modification from Unimod Chemical derivative - 5-hydro-5-methylimidazol-4-one, arginine methylglyoxal arginine adduct (+54 amu) http://purl.obolibrary.org/obo/MOD_00934 Levuglandinyl - arginine hydroxylactam adduct http://purl.obolibrary.org/obo/MOD_00902 modified L-arginine residue modification from Unimod Post-translational http://purl.obolibrary.org/obo/MOD_00935 methionine oxidation with neutral loss of 64 Da http://purl.obolibrary.org/obo/MOD_00913 modified L-methionine residue Oxidation of methionine to methionine sulfoxide with neutral loss of CH3SOH. http://purl.obolibrary.org/obo/MOD_00936 Levuglandinyl - hydroxylactam adduct, K and N-term http://purl.obolibrary.org/obo/MOD_00846 levuglandinyl (prostaglandin H2) adduct modification from Unimod Post-translational http://purl.obolibrary.org/obo/MOD_00937 Levuglandinyl - arginine lactam adduct http://purl.obolibrary.org/obo/MOD_00902 modified L-arginine residue modification from Unimod Post-translational http://purl.obolibrary.org/obo/MOD_00938 Levuglandinyl - lactam adduct, K and N-term http://purl.obolibrary.org/obo/MOD_00846 levuglandinyl (prostaglandin H2) adduct modification from Unimod Post-translational http://purl.obolibrary.org/obo/MOD_00939 hydrolyzed N-methylmaleimide cysteine adduct http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00940 3-methyl-2-pyridyl isocyanate derivatized residue http://purl.obolibrary.org/obo/MOD_00840 isocyanate reagent derivatized residue A protein modification produced by formation of an adduct with 3-methyl-2-pyridyl isocyanate. http://purl.obolibrary.org/obo/MOD_00941 dehydropyrrolizidine alkaloid (dehydroretronecine) derivatized cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00942 (4,4,5,5-(2)H4)-L-lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue 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. http://purl.obolibrary.org/obo/MOD_00943 4-trimethylammoniumbutanoyl derivatized residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from Unimod Isotopic label http://purl.obolibrary.org/obo/MOD_00944 d9-4-trimethylammoniumbutanoyl derivatized residue http://purl.obolibrary.org/obo/MOD_01431 (2)H deuterium tagged reagent modification from Unimod Isotopic label http://purl.obolibrary.org/obo/MOD_00946 crosslinked residues with loss of ammonia http://purl.obolibrary.org/obo/MOD_00033 crosslinked residues A protein modification that crosslinks two residues with a covalent bond and the loss of ammonia. http://purl.obolibrary.org/obo/MOD_00947 DeltaMass http://purl.obolibrary.org/obo/MOD_00032 uncategorized protein modification Entries from DeltaMass see http://www.abrf.org/index.cfm/dm.home?AvgMass=all. http://purl.obolibrary.org/obo/MOD_00951 L-gamma-carboxyglutamic acid with neutral loss of carbon dioxide http://purl.obolibrary.org/obo/MOD_00906 modified L-glutamic acid residue 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. http://purl.obolibrary.org/obo/MOD_00952 (2-aminosuccinimidyl)acetic acid (Asp) http://purl.obolibrary.org/obo/MOD_02043 crosslinked L-aspartic acid residue 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. http://purl.obolibrary.org/obo/MOD_00953 O-(L-isoglutamyl)-L-serine (Glu-Ser) http://purl.obolibrary.org/obo/MOD_02045 crosslinked L-glutamic acid residue 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. http://purl.obolibrary.org/obo/MOD_00954 crosslinked residues with loss of water http://purl.obolibrary.org/obo/MOD_00033 crosslinked residues A protein modification that crosslinks two residues with a covalent bond and the loss of water. http://purl.obolibrary.org/obo/MOD_00955 alaninohistidine (serine crosslinked to tele or pros nitrogen of histidine) http://purl.obolibrary.org/obo/MOD_02055 crosslinked L-serine residue 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. http://purl.obolibrary.org/obo/MOD_00956 misincorporation of norleucine for methionine http://purl.obolibrary.org/obo/MOD_01026 norleucine residue (Nle) modification from DeltaMass http://purl.obolibrary.org/obo/MOD_00957 modified residue with neutral loss of carbon dioxide http://purl.obolibrary.org/obo/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 carbon dioxide molecular fragment. http://purl.obolibrary.org/obo/MOD_00958 crosslink between Arg and His sidechains http://purl.obolibrary.org/obo/MOD_00692 uncategorized crosslinked residues modification from DeltaMass http://purl.obolibrary.org/obo/MOD_00959 3,3',5,5'-TerTyr (Crosslink) http://purl.obolibrary.org/obo/MOD_00692 uncategorized crosslinked residues modification from DeltaMass http://purl.obolibrary.org/obo/MOD_00960 decarboxylated residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process A protein modification that effectively replaces a carboxylic acid group with a hydrogen atom. http://purl.obolibrary.org/obo/MOD_00961 reduction of disulfide crosslink in cystine to two cysteines http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively reduces the disulfide bond of cystine to form two cysteine residues. http://purl.obolibrary.org/obo/MOD_00962 2',3'-dihydrotryptophan http://purl.obolibrary.org/obo/MOD_00918 modified L-tryptophan residue A protein modification that by reducing the indole ring system of tryptophan to indoline effectively converts an L-tryptophan residue to 2',3'-dihydrotryptophan. http://purl.obolibrary.org/obo/MOD_00964 lysine epsilon amino to imine + 12 amu http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_00965 4-thiazolidinecarboxylic acid http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an N-terminal L-cysteine residue by a formadehyde adduct to 4-thiazolidinecarboxylic acid. http://purl.obolibrary.org/obo/MOD_00966 1,2,3,4-tetrahydro-beta-carboline-3-carboxylic acid http://purl.obolibrary.org/obo/MOD_00918 modified L-tryptophan residue 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. http://purl.obolibrary.org/obo/MOD_00967 syndesine http://purl.obolibrary.org/obo/MOD_02051 crosslinked L-lysine residue A protein modification that effectively cross-links two L-lysine residues to form syndesine, hydroxylysinohydroxynorleucine. http://purl.obolibrary.org/obo/MOD_00970 delta-hydroxy-allysine (Lys) http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_00971 2-Oxohistidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively converts an L-histidine residue to 2-oxohistidine. http://purl.obolibrary.org/obo/MOD_00972 monobrominated L-phenylalanine http://purl.obolibrary.org/obo/MOD_01912 monobrominated residue A protein modification that effectively converts an L-phenylalanine residue to a monobrominated L-phenylalanine, such as L-2'-bromophenylalanine. http://purl.obolibrary.org/obo/MOD_00973 Oxidation of proline (to glutamic acid) http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_00974 (35)Cl labeled 3'-chlorotyrosine http://purl.obolibrary.org/obo/MOD_00987 chlorinated tyrosine modification from DeltaMass http://purl.obolibrary.org/obo/MOD_00975 (37)Cl labeled 3'-chlorotyrosine http://purl.obolibrary.org/obo/MOD_00987 chlorinated tyrosine modification from DeltaMass http://purl.obolibrary.org/obo/MOD_00977 disodium salt http://purl.obolibrary.org/obo/MOD_00747 sodium containing modified residue modification from DeltaMass http://purl.obolibrary.org/obo/MOD_00978 piperidine adduct to C-terminal Cys http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_00979 t-butyl ester (OtBu) and t-butyl (tBu) http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_00981 sodium and potassium salt http://purl.obolibrary.org/obo/MOD_00849 potassium containing modified residue modification from DeltaMass http://purl.obolibrary.org/obo/MOD_00982 L-selenocysteine (Ser) http://purl.obolibrary.org/obo/MOD_02088 natural, standard, encoded residue substitution A protein modification that effectively converts an L-serine residue to L-selenocysteine (not known as a natural post-translational modification process). http://purl.obolibrary.org/obo/MOD_00983 Asp transamidation with piperidine http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_00984 (35)Cl labeled 3',5'-dichlorotyrosine http://purl.obolibrary.org/obo/MOD_00987 chlorinated tyrosine modification from DeltaMass http://purl.obolibrary.org/obo/MOD_00985 halogenated tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with a halogen atom. http://purl.obolibrary.org/obo/MOD_00986 (35)Cl and (37)Cl labeled 3',5'-dichlorotyrosine http://purl.obolibrary.org/obo/MOD_00987 chlorinated tyrosine modification from DeltaMass http://purl.obolibrary.org/obo/MOD_00987 chlorinated tyrosine http://purl.obolibrary.org/obo/MOD_00985 halogenated tyrosine A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with a chlorine atom. http://purl.obolibrary.org/obo/MOD_00988 brominated tyrosine http://purl.obolibrary.org/obo/MOD_00754 brominated residue A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with a bromine atom. http://purl.obolibrary.org/obo/MOD_00990 (37)Cl labeled 3',5'-dichlorotyrosine http://purl.obolibrary.org/obo/MOD_00987 chlorinated tyrosine modification from DeltaMass http://purl.obolibrary.org/obo/MOD_00991 S-(sn-1-glyceryl)-L-cysteine http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_00992 glutamate 5-glycerol ester http://purl.obolibrary.org/obo/MOD_00906 modified L-glutamic acid residue modification from DeltaMass http://purl.obolibrary.org/obo/MOD_00993 phenyl ester http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from DeltaMass http://purl.obolibrary.org/obo/MOD_00994 (79)Br labeled 3'-bromotyrosine http://purl.obolibrary.org/obo/MOD_01000 monobrominated tyrosine modification from DeltaMass http://purl.obolibrary.org/obo/MOD_00995 (81)Br labeled 2'-bromophenylalanine http://purl.obolibrary.org/obo/MOD_02086 brominated phenylalanine A protein modification that effectively converts an L-phenylalanine residue to (81)Br-L-2'-bromophenylalanine. http://purl.obolibrary.org/obo/MOD_00996 (81)Br labeled 3'-bromotyrosine http://purl.obolibrary.org/obo/MOD_01000 monobrominated tyrosine modification from DeltaMass http://purl.obolibrary.org/obo/MOD_00997 cyclohexyl ester http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from DeltaMass http://purl.obolibrary.org/obo/MOD_00998 iodinated tyrosine http://purl.obolibrary.org/obo/MOD_00985 halogenated tyrosine A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with an iodine atom. http://purl.obolibrary.org/obo/MOD_01000 monobrominated tyrosine http://purl.obolibrary.org/obo/MOD_00988 brominated tyrosine A protein modification that effectively substitutes one hydrogen atom of an L-tyrosine residue with one bromine atom. http://purl.obolibrary.org/obo/MOD_01001 2-aminoisobutyric acid residue (Aib) http://purl.obolibrary.org/obo/MOD_00850 unnatural residue A protein modification that inserts or replaces a residue with a 2-aminoisobutyric acid. http://purl.obolibrary.org/obo/MOD_01002 gamma-aminobutyryl http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01003 t-butyloxymethyl (Bum) http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01004 diaminopropionyl http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01005 t-butylsulfenyl http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01006 dibrominated tyrosine http://purl.obolibrary.org/obo/MOD_00988 brominated tyrosine A protein modification that effectively substitutes two hydrogen atoms of an L-tyrosine residue with two bromine atoms. http://purl.obolibrary.org/obo/MOD_01007 anisyl modified residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue A protein modification that effectively substitutes an anisyl (methoxyphenyl) group for a hydroxyl group, typically at the 4 or para position. http://purl.obolibrary.org/obo/MOD_01008 benzyl (Bzl) and benzyl ester (OBzl) modified residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue A protein modification that effectively substitutes a benzyl (phenylmethyl) group for a hydrogen atom. http://purl.obolibrary.org/obo/MOD_01009 dehydrogenated proline http://purl.obolibrary.org/obo/MOD_00915 modified L-proline residue modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01010 trifluoroacetylated residue http://purl.obolibrary.org/obo/MOD_00649 acylated residue A protein modification that effectively substitutes a trifluoroacetyl group for a hydrogen atom. http://purl.obolibrary.org/obo/MOD_01011 N-hydroxysuccinimide (ONSu, OSu) http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01012 oxidation of disulfide crosslink in cystine to two cysteic acids http://purl.obolibrary.org/obo/MOD_00675 oxidized residue A protein modification that effectively oxidizes the disulfide bond of a cystine crosslink to form two cysteic acid residues. http://purl.obolibrary.org/obo/MOD_01013 tetramethylguanidinium termination by-product on amine http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01014 phosphate/sulphate adduct of proteins http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01015 isovaline residue (Iva) http://purl.obolibrary.org/obo/MOD_00850 unnatural residue A protein modification that inserts or replaces a residue with an isovaline. http://purl.obolibrary.org/obo/MOD_01016 t-butyloxycarbonyl http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01018 4-methylbenzyl http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01019 hydroxymethylphenyl linker http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01020 thioanisyl http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01021 thiocresyl http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01022 2-piperidinecarboxylic acid http://purl.obolibrary.org/obo/MOD_01160 deaminated residue A protein modification that effectively converts an L-lysine residue to 2-piperidinecarboxylic acid. http://purl.obolibrary.org/obo/MOD_01023 3',5'-dibromo-L-tyrosine http://purl.obolibrary.org/obo/MOD_01006 dibrominated tyrosine A protein modification that effectively converts an L-tyrosine residue to 3',5'-dibromo-L-tyrosine. http://purl.obolibrary.org/obo/MOD_01024 monohydroxylated proline http://purl.obolibrary.org/obo/MOD_00678 hydroxylated 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. http://purl.obolibrary.org/obo/MOD_01025 3'-bromo-L-tyrosine http://purl.obolibrary.org/obo/MOD_01000 monobrominated tyrosine A protein modification that effectively converts an L-tyrosine residue to 3'-bromo-L-tyrosine. http://purl.obolibrary.org/obo/MOD_01026 norleucine residue (Nle) http://purl.obolibrary.org/obo/MOD_00850 unnatural residue A protein modification that inserts or replaces a residue with a norleucine. http://purl.obolibrary.org/obo/MOD_01027 t-amyloxycarbonyl http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01028 monochlorinated L-tyrosine http://purl.obolibrary.org/obo/MOD_01911 monochlorinated residue A protein modification that effectively substitutes one hydrogen atom of an L-tyrosine residue with one chlorine atom. http://purl.obolibrary.org/obo/MOD_01029 succinylated residue http://purl.obolibrary.org/obo/MOD_00649 acylated residue A protein modification that effectively replaces a hydrogen atom with a succinyl group linked through a carbonyl carbon. http://purl.obolibrary.org/obo/MOD_01030 hydroxybenzotriazole ester http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01031 dimethylbenzyl http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01032 benzyloxymethyl modified residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue A protein modification that effectively substitutes a benzyloxymethyl group for a hydrogen atom. http://purl.obolibrary.org/obo/MOD_01033 p-methoxybenzyl modified residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue A protein modification that effectively substitutes a p-methoxybenzyl group for a hydrogen atom. http://purl.obolibrary.org/obo/MOD_01034 4-nitrophenyl modified residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue A protein modification that effectively substitutes a 4-nitrophenyl group for a hydrogen atom. http://purl.obolibrary.org/obo/MOD_01035 chlorobenzyl http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01037 dichlorinated tyrosine http://purl.obolibrary.org/obo/MOD_00987 chlorinated tyrosine A protein modification that effectively substitutes two hydrogen atoms of an L-tyrosine residue with two chlorine atoms. http://purl.obolibrary.org/obo/MOD_01040 penicillamine residue http://purl.obolibrary.org/obo/MOD_00850 unnatural residue A protein modification that inserts or replaces a residue with a penicillamine. http://purl.obolibrary.org/obo/MOD_01041 benzyloxycarbonyl modified residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue A protein modification that effectively substitutes a benzyloxycarbonyl group for a hydrogen atom. http://purl.obolibrary.org/obo/MOD_01042 adamantyl modified residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue A protein modification that effectively substitutes a adamantyl group for a hydrogen atom. http://purl.obolibrary.org/obo/MOD_01043 p-nitrobenzyl ester modified residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue A protein modification that effectively substitutes a p-nitrobenzyl group for the hydrogen atom of a carboxyl group. http://purl.obolibrary.org/obo/MOD_01045 3',5'-dichloro-L-tyrosine http://purl.obolibrary.org/obo/MOD_01037 dichlorinated tyrosine A protein modification that effectively converts an L-tyrosine residue to 3',5'-dichloro-L-tyrosine. http://purl.obolibrary.org/obo/MOD_01046 3'-chloro-L-tyrosine http://purl.obolibrary.org/obo/MOD_01028 monochlorinated L-tyrosine A protein modification that effectively converts an L-tyrosine residue to 3'-chloro-L-tyrosine. http://purl.obolibrary.org/obo/MOD_01047 monohydroxylated lysine http://purl.obolibrary.org/obo/MOD_00681 hydroxylated lysine A protein modification that effectively converts an L-lysine residue to a monohydroxylated lysine. http://purl.obolibrary.org/obo/MOD_01049 halogenated histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively substitutes a hydrogen atom of an L-histidine residue with a halogen atom. http://purl.obolibrary.org/obo/MOD_01050 pyridyl alanyl http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01051 2-nitrobenzoyl http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01052 dimethoxybenzyl Trp http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01053 2-nitrophenylsulphenyl http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01054 4-toluenesulfonyl http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01055 3-nitro-2-pyridinesulfenyl http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01056 (79)Br labeled 3',5'-dibromotyrosine http://purl.obolibrary.org/obo/MOD_01006 dibrominated tyrosine modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01057 (79)Br and (81)Br labeled 3',5'-dibromotyrosine http://purl.obolibrary.org/obo/MOD_01006 dibrominated tyrosine modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01058 dichlorobenzyl http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01059 (81)Br labeled 3',5'-dibromotyrosine http://purl.obolibrary.org/obo/MOD_01006 dibrominated tyrosine modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01060 S-carboxamidomethyl-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-carboxamidomethyl-L-cysteine. http://purl.obolibrary.org/obo/MOD_01061 S-carboxymethyl-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-carboxymethyl-L-cysteine. http://purl.obolibrary.org/obo/MOD_01063 monomethylated phenylalanine http://purl.obolibrary.org/obo/MOD_00599 monomethylated residue A protein modification that effectively converts an L-phenylalanine residue to a monomethylated phenylalanine. http://purl.obolibrary.org/obo/MOD_01064 inositol http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01065 hexose glycated N-terminal http://purl.obolibrary.org/obo/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 N-terminal amino group to form a Schiff-base or an Amadori ketosamine (or aminoketose) residue adduct. http://purl.obolibrary.org/obo/MOD_01066 halogenated phenylalanine http://purl.obolibrary.org/obo/MOD_00914 modified L-phenylalanine residue A protein modification that effectively substitutes a hydrogen atom of an L-phenylalanine residue with a halogen atom. http://purl.obolibrary.org/obo/MOD_01067 linker attached to peptide in Fmoc peptide synthesis http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01068 halogenated tryptophan http://purl.obolibrary.org/obo/MOD_00918 modified L-tryptophan residue A protein modification that effectively substitutes a hydrogen atom of an L-tryptophan residue with a halogen atom. http://purl.obolibrary.org/obo/MOD_01069 2,4-dinitrophenyl modified residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue A protein modification that effectively substitutes a 2,4-dinitrophenyl group for a hydrogen atom. http://purl.obolibrary.org/obo/MOD_01070 pentafluorophenyl modified residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue A protein modification that effectively substitutes a pentafluorophenyl group for a hydrogen atom. http://purl.obolibrary.org/obo/MOD_01071 diphenylmethyl modified residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue A protein modification that effectively substitutes a diphenylmethyl group for a hydrogen atom. http://purl.obolibrary.org/obo/MOD_01072 monopotassium salt http://purl.obolibrary.org/obo/MOD_00849 potassium containing modified residue A protein modification that effectively substitutes one potassium atom for one hydrogen atom. http://purl.obolibrary.org/obo/MOD_01073 2-chlorobenzyloxycarbonyl modified residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue A protein modification that effectively substitutes a 2-chlorobenzyloxycarbonyl group for a hydrogen atom. http://purl.obolibrary.org/obo/MOD_01074 napthylacetyl modified residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue A protein modification that effectively substitutes a napthylacetyl group for a hydrogen atom. http://purl.obolibrary.org/obo/MOD_01075 mercury containing modified residue http://purl.obolibrary.org/obo/MOD_00698 metal or metal cluster containing modified residue A protein modification that effectively substitutes a mercury atom or a cluster containing mercury for hydrogen atoms, or that coordinates a mercury ion. http://purl.obolibrary.org/obo/MOD_01077 ethanedithiol/TFA cyclic adduct http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01078 S-(2-aminoethyl)-3-methylcysteine (Thr) http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue A protein modification that effectively converts an L-threonine residue to S-(2-aminoethyl)-3-methylcysteine. http://purl.obolibrary.org/obo/MOD_01079 S-(acetylamino)methyl-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-[(acetylamino)methyl]-L-cysteine. http://purl.obolibrary.org/obo/MOD_01081 delta-glycosyloxy- (of lysine) or beta-glycosyloxy- (of phenylalanine or tyrosine) http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01083 O-benzyl-L-serine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to O-benzyl-L-serine. http://purl.obolibrary.org/obo/MOD_01084 iodoacetic acid derivatized amino-terminal residue http://purl.obolibrary.org/obo/MOD_00399 iodoacetic acid derivatized residue A protein modification that by reaction of iodoacetic acid effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a carboxymethyl group. http://purl.obolibrary.org/obo/MOD_01085 alpha-N-gluconoylated L-histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively replaces the N-terminal hydrogen atom of a N-terminal histidine residue with a gluconoyl group linked through a glycosidic bond. modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01086 p-nitrobenzyloxycarbonyl http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01087 2,4,5-trichlorophenyl modified residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue A protein modification that effectively substitutes a 2,4,5-trichlorophenyl group for a hydrogen atom. http://purl.obolibrary.org/obo/MOD_01088 2,4,6-trimethyloxybenzyl modified residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue A protein modification that effectively substitutes a 2,4,6-trimethyloxybenzyl group for a hydrogen atom. http://purl.obolibrary.org/obo/MOD_01089 xanthyl http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01090 iodoacetamide derivatized amino-terminal residue http://purl.obolibrary.org/obo/MOD_00397 iodoacetamide derivatized residue A protein modification that by reaction of iodoacetamide effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a carboxamidomethyl group. http://purl.obolibrary.org/obo/MOD_01091 monochlorinated L-phenylalanine http://purl.obolibrary.org/obo/MOD_01911 monochlorinated residue A protein modification that effectively substitutes one hydrogen atom of an L-phenylalanine residue with one chlorine atom. http://purl.obolibrary.org/obo/MOD_01092 mesitylene-2-sulfonyl http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01093 isopropyl lysyl http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01094 N6-carboxymethyl-L-lysine http://purl.obolibrary.org/obo/MOD_00399 iodoacetic acid derivatized residue A protein modification that effectively converts an L-lysine residue to N6-carboxymethyl-L-lysine. http://purl.obolibrary.org/obo/MOD_01096 O-benzyl-L-threonine http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue A protein modification that effectively converts an L-threonine residue to O-benzyl-L-threonine. http://purl.obolibrary.org/obo/MOD_01097 S-benzyl-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-benzyl-L-cysteine. http://purl.obolibrary.org/obo/MOD_01098 naphthylalanine residue http://purl.obolibrary.org/obo/MOD_00850 unnatural residue A protein modification that inserts or replaces a residue with a naphthylalanine. http://purl.obolibrary.org/obo/MOD_01099 succinyl beta-aspartyl anhydride http://purl.obolibrary.org/obo/MOD_00904 modified L-aspartic acid residue A protein modification that effectively converts an L-aspartic acid residue to succinyl beta-aspartyl anhydride. http://purl.obolibrary.org/obo/MOD_01100 HMP (hydroxymethylphenyl)/TFA adduct http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01104 4-methoxy-2,3,6-trimethylbenzenesulfonyl http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01105 2-bromobenzyloxycarbonyl http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01106 N-formyl-L-tryptophan http://purl.obolibrary.org/obo/MOD_00918 modified L-tryptophan residue A protein modification that effectively converts an L-tryptophan residue to N-formyl-L-tryptophan. http://purl.obolibrary.org/obo/MOD_01107 O5-benzyl-L-glutamate http://purl.obolibrary.org/obo/MOD_00906 modified L-glutamic acid residue A protein modification that effectively converts an L-glutamic acid residue to O5-benzyl-L-glutamate. http://purl.obolibrary.org/obo/MOD_01108 2-amino-5-(4-methoxyphenyl)-5-oxopentanoic acid (Glu) http://purl.obolibrary.org/obo/MOD_00906 modified L-glutamic acid residue A protein modification that effectively converts an L-glutamic acid residue to 2-amino-5-(4-methoxyphenyl)-5-oxopentanoic acid, glutamtic acid anisole adduct. http://purl.obolibrary.org/obo/MOD_01111 dimethoxybenzhydryl modified residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue A protein modification that effectively substitutes a dimethoxybenzhydryl group for a hydrogen atom. http://purl.obolibrary.org/obo/MOD_01113 2-(p-biphenyl)isopropyl-oxycarbonyl http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01114 triphenylmethyl http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01115 isoprenylated tryptophan http://purl.obolibrary.org/obo/MOD_00918 modified L-tryptophan residue A protein modification that effectively replaces a hydrogen atom of an L-tryptophan residue with a group derived from an isoprene polymer, such as a geranyl (C10), farnesyl (C15) or geranylgeranyl (C20). http://purl.obolibrary.org/obo/MOD_01116 S-farnesyl-L-cysteine methyl ester http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-farnesyl-L-cysteine methyl ester. http://purl.obolibrary.org/obo/MOD_01117 pentamethyldihydrobenzofuransulfonyl http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01118 alpha-N-6-phosphogluconoylated L-histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively replaces the N-terminal hydrogen atom of a N-terminal histidine residue with a 6-phosphogluconoyl group linked through a glycosidic bond. modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01120 2,2,5,7,8-pentamethylchroman-6-sulfonyl chloride derivatized residue http://purl.obolibrary.org/obo/MOD_01652 sulfonyl halide reagent derivatized residue A protein modification that is produced by formation of an adduct with 2,2,5,7,8-pentamethylchroman-6-sulfonyl chloride, Pmc chloride. http://purl.obolibrary.org/obo/MOD_01121 monomethoxytrityl http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01124 aldohexosyl lysyl http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01128 N-glycolneuraminic acid http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01130 SucPhencarb Lysyl http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01133 S-12-hydroxyfarnesyl-L-cysteine methyl ester http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-12-hydroxyfarnesyl-L-cysteine methyl ester. http://purl.obolibrary.org/obo/MOD_01134 fluorescein labelling of peptide N-terminal using NHS ester http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01135 Hex-HexNAc http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01137 N6-(2,2,5,7,8-pentamethylchroman-6-sulfonyl)-L-lysine http://purl.obolibrary.org/obo/MOD_00902 modified L-arginine residue A protein modification that is produced by reaction of a lysine residue with 2,2,5,7,8-pentamethylchroman-6-sulfonyl chloride, Pmc chloride, to form N6-(2,2,5,7,8-pentamethylchroman-6-sulfonyl)-L-lysine. http://purl.obolibrary.org/obo/MOD_01140 diiodinated tyrosine http://purl.obolibrary.org/obo/MOD_00998 iodinated tyrosine A protein modification that effectively substitutes two hydrogen atoms of an L-tyrosine residue with two iodine atoms. http://purl.obolibrary.org/obo/MOD_01141 omega-N-(2,2,5,7,8-pentamethylchroman-6-sulfonyl)-L-arginine http://purl.obolibrary.org/obo/MOD_00902 modified L-arginine residue A protein modification that is produced by reaction with 2,2,5,7,8-pentamethylchroman-6-sulfonyl chloride, Pmc chloride, to form omega-N-(2,2,5,7,8-pentamethylchroman-6-sulfonyl)-L-arginine. http://purl.obolibrary.org/obo/MOD_01142 S-15,16-dihydrobiliverdin-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound 15,16-dihydrobiliverdin. http://purl.obolibrary.org/obo/MOD_01143 15,16-dihydrobiliverdin-bis-L-cysteine http://purl.obolibrary.org/obo/MOD_02044 crosslinked L-cysteine residue A protein modification that effectively results from forming an adduct between two cysteine residues and the tetrapyrrole compound 15,16-dihydrobiliverdin. http://purl.obolibrary.org/obo/MOD_01144 S-(sn-1-2,3-dipalmitoylglycerol)-L-cysteine http://purl.obolibrary.org/obo/MOD_00116 S-diacylglycerol-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-(sn-1-2,3-dipalmitoyl-glycerol)cysteine. http://purl.obolibrary.org/obo/MOD_01145 N-tau-(ADP-ribosyl)diphthamide http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively converts an L-histidine residue to N-tau-(ADP-ribosyl)diphthamide. http://purl.obolibrary.org/obo/MOD_01146 S-(6-FAD)-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-(6-FAD)-L-cystine. http://purl.obolibrary.org/obo/MOD_01147 dHex1Hex3HexNAc2 N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01151 phosphorylated residue with neutral loss of phosphate http://purl.obolibrary.org/obo/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 phosphorylated residue with a secondary loss of a neutral trihydrogen phosphate molecular fragment. http://purl.obolibrary.org/obo/MOD_01153 methylthiolated residue http://purl.obolibrary.org/obo/MOD_01886 thiolated residue A protein modification that effectively replaces a hydrogen atom with an methylsulfanyl group (thiomethyl group). http://purl.obolibrary.org/obo/MOD_01154 pyruvic acid http://purl.obolibrary.org/obo/MOD_00859 modified residue that can arise from different natural residues A protein modification that effectively converts a source amino acid to pyruvic acid. http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process http://purl.obolibrary.org/obo/MOD_00000 protein modification Modified amino acid residue derived from a natural amino acid by a real or hypothetical chemical process. http://purl.obolibrary.org/obo/MOD_01157 protein modification categorized by amino acid modified http://purl.obolibrary.org/obo/MOD_00000 protein modification A protein modification considered either as modified amino acid residues derived from natural amino acids, as a replacement by another natural amino acid, or as a replacement by an unnatural amino acid. http://purl.obolibrary.org/obo/MOD_01158 modified L-selenocysteine residue http://purl.obolibrary.org/obo/MOD_01157 protein modification categorized by amino acid modified A protein modification that modifies an L-selenocysteine residue. http://purl.obolibrary.org/obo/MOD_01159 peptidoglycanated residue http://purl.obolibrary.org/obo/MOD_00764 glycoconjugated residue A protein modification that effectively attaches a residue to murein peptidoglycan by either a pentaglycine linker peptide or a peptide-like L-alanyl-D-glutamyl-2,6-diaminopimelic acid linkage. http://purl.obolibrary.org/obo/MOD_01161 deoxygenated residue http://purl.obolibrary.org/obo/MOD_01472 reduced residue A protein modification that effectively removes oxygen atoms from a residue without the removal of hydrogen atoms. http://purl.obolibrary.org/obo/MOD_01162 fucosylated biantennary http://purl.obolibrary.org/obo/MOD_00725 complex glycosylation modification from Unimod N-linked glycosylation http://purl.obolibrary.org/obo/MOD_01163 guanylated residue http://purl.obolibrary.org/obo/MOD_00701 nucleotide or nucleic acid modified residue A protein modification that effectively crosslinks an amino acid residue and 5'-phosphoguanosine through either a phosphodiester or a phosphoramide bond. http://purl.obolibrary.org/obo/MOD_01164 riboflavin-phosphorylated residue http://purl.obolibrary.org/obo/MOD_00697 flavin modified residue A protein modification that effectively results from forming an adduct with a compound containing a riboflavin phosphate (flavin mononucleotide, FMN) group through a phosphodiester bond. http://purl.obolibrary.org/obo/MOD_01165 adenylated residue http://purl.obolibrary.org/obo/MOD_00701 nucleotide or nucleic acid modified residue A protein modification that effectively crosslinks an amino acid residue and 5'-phosphoadenosine through either a phosphodiester or a phosphoramide bond. http://purl.obolibrary.org/obo/MOD_01166 uridylated residue http://purl.obolibrary.org/obo/MOD_00701 nucleotide or nucleic acid modified residue A protein modification that effectively crosslinks an amino acid residue and 5'-phosphouridine through either a phosphodiester or a phosphoramide bond. http://purl.obolibrary.org/obo/MOD_01167 molybdopterin guanine dinucleotide http://purl.obolibrary.org/obo/MOD_00744 molybdenum pterin containing modification modification from Unimod http://purl.obolibrary.org/obo/MOD_01168 dehydroalanine http://purl.obolibrary.org/obo/MOD_00859 modified residue that can arise from different natural residues A protein modification that effectively converts a source amino acid residue to dehydroalanine. http://purl.obolibrary.org/obo/MOD_01169 L-3-oxoalanine http://purl.obolibrary.org/obo/MOD_00859 modified residue that can arise from different natural residues A protein modification that effectively converts a source amino acid residue to L-oxoalanine. http://purl.obolibrary.org/obo/MOD_01170 pyruvic acid iminylated residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process A protein modification that effectively forms a 2-ketoimine of pyruvicacid with a residue amino group. http://purl.obolibrary.org/obo/MOD_01171 O-acetyl-L-threonine http://purl.obolibrary.org/obo/MOD_01186 monoacetylated L-threonine A protein modification that effectively converts an L-threonine residue to O-acetyl-L-threonine. http://purl.obolibrary.org/obo/MOD_01172 N-alanyl-glycosylsphingolipidinositolethanolamine http://purl.obolibrary.org/obo/MOD_00901 modified L-alanine residue A protein modification that effectively converts an L-alanine residue to N-alanyl-glycosylsphingolipidinositolethanolamine. http://purl.obolibrary.org/obo/MOD_01173 N-asparaginyl-glycosylsphingolipidinositolethanolamine http://purl.obolibrary.org/obo/MOD_00903 modified L-asparagine residue A protein modification that effectively converts an L-asparagine residue to N-asparaginyl-glycosylsphingolipidinositolethanolamine. http://purl.obolibrary.org/obo/MOD_01174 S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)-L-cysteine http://purl.obolibrary.org/obo/MOD_01155 lipoconjugated residue A protein modification that effectively converts an L-cysteine residue to S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)-L-cysteine. http://purl.obolibrary.org/obo/MOD_01175 S-phycourobilin-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycourobilin. http://purl.obolibrary.org/obo/MOD_01176 L-dehydrolysinonorleucine http://purl.obolibrary.org/obo/MOD_02051 crosslinked L-lysine residue A protein modification that effectively cross-links an L-lysine residue and an L-lysine residue converted to allysine with a carbon-nitrogen bond to form L-dehydrolysinonorleucine. http://purl.obolibrary.org/obo/MOD_01177 1'-(1,2,3-trihydroxyprop-2-yl)-L-histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively converts an L-histidine residue to 1'-(1,2,3-trihydroxyprop-2-yl)-L-histidine. http://purl.obolibrary.org/obo/MOD_01178 S-(aspart-4-yloxy) thiocarbonate http://purl.obolibrary.org/obo/MOD_00904 modified L-aspartic acid residue A protein modification that effectively converts an L-aspartic acid residue to S-(aspart-4-yloxy) thiocarbonate. http://purl.obolibrary.org/obo/MOD_01179 N,N-dimethyl-L-alanine http://purl.obolibrary.org/obo/MOD_01686 alpha-amino dimethylated residue A protein modification that effectively converts an L-alanine residue to N,N-dimethyl-L-alanine. http://purl.obolibrary.org/obo/MOD_01180 2-hydroxyglycine observational artifact http://purl.obolibrary.org/obo/MOD_00908 modified glycine residue A protein modification that effectively converts a glycine residue to 2-hydroxyglycine. http://purl.obolibrary.org/obo/MOD_01181 L-aspartic acid 4-methyl ester http://purl.obolibrary.org/obo/MOD_01681 monomethylated L-aspartic acid A protein modification that effectively converts an L-aspartic acid residue to L-aspartate 4-methyl ester. http://purl.obolibrary.org/obo/MOD_01182 6-(S-L-cysteinyl)-8alpha-(-3'-L-histidino)-FAD http://purl.obolibrary.org/obo/MOD_02048 crosslinked L-histidine residue A protein modification that crosslinks a cysteine and a histidine residue by forming the adduct 6-(S-L-cysteinyl)-8alpha-(-3'-L-histidino)-FAD. http://purl.obolibrary.org/obo/MOD_01183 L-selenocystine (oxidized selenocysteine) (Sec-Sec) http://purl.obolibrary.org/obo/MOD_01158 modified L-selenocysteine residue A protein modification that effectively cross-links two L-selenocysteine residues to form L-selenocystine, http://purl.obolibrary.org/obo/MOD_01184 L-selenocystine (selenium disubstituted L-cystine) http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively substitutes two selenium atoms for two sulfur atoms in L-cystine to form L-selenocystine. http://purl.obolibrary.org/obo/MOD_01185 4-amidated L-aspartic acid http://purl.obolibrary.org/obo/MOD_00904 modified L-aspartic acid residue A protein modification that effectively converts an L-aspartic acid residue to L-asparagine. http://purl.obolibrary.org/obo/MOD_01186 monoacetylated L-threonine http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue A protein modification that effectively converts an L-threonine residue to either N-acetyl-L-threonne, or O-acetyl-Lthreonine. http://purl.obolibrary.org/obo/MOD_01187 L-pyrrolysine residue http://purl.obolibrary.org/obo/MOD_00868 natural, non-standard encoded residue A protein modification that inserts or replaces a residue with an L-pyrrolysine residue, a natural pretranslational modification. http://purl.obolibrary.org/obo/MOD_01188 N-ethyl iodoacetamide-d5 - site Y http://purl.obolibrary.org/obo/MOD_00562 N-ethyl iodoacetamide-d5 modification from Unimod Isotopic label - http://purl.obolibrary.org/obo/MOD_01189 N-ethyl iodoacetamide-d5 - site C http://purl.obolibrary.org/obo/MOD_00562 N-ethyl iodoacetamide-d5 modification from Unimod Isotopic label - http://purl.obolibrary.org/obo/MOD_01191 N-ethyl iodoacetamide-d0 - site C http://purl.obolibrary.org/obo/MOD_00561 N-ethyl iodoacetamide- modification from Unimod Isotopic label - http://purl.obolibrary.org/obo/MOD_01192 N-ethyl iodoacetamide-d0 - site Y http://purl.obolibrary.org/obo/MOD_00561 N-ethyl iodoacetamide- modification from Unimod Isotopic label - http://purl.obolibrary.org/obo/MOD_01193 pyridyl thiol modified L-threonine http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue modification from Unimod Chemical derivative - http://purl.obolibrary.org/obo/MOD_01194 pyridyl thiol modified L-serine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue modification from Unimod Chemical derivative - http://purl.obolibrary.org/obo/MOD_01195 benzoyl labeling reagent light form - site K http://purl.obolibrary.org/obo/MOD_00505 benzoyl labeling reagent light form (N-term and K) modification from Unimod Isotopic label - http://purl.obolibrary.org/obo/MOD_01197 N-heptosyl-L-glutamine http://purl.obolibrary.org/obo/MOD_00925 heptosylated residue A protein modification that effectively converts an L-glutamine residue to N-heptosyl-L-glutamine. http://purl.obolibrary.org/obo/MOD_01198 O-heptosyl-L-serine http://purl.obolibrary.org/obo/MOD_00925 heptosylated residue A protein modification that effectively converts an L-serine residue to O-heptosyl-L-serine. http://purl.obolibrary.org/obo/MOD_01199 N-heptosyl-L-arginine http://purl.obolibrary.org/obo/MOD_00925 heptosylated residue A protein modification that effectively converts an L-arginine residue to an N-heptosyl-L-arginine. http://purl.obolibrary.org/obo/MOD_01200 O-heptosyl-L-threonine http://purl.obolibrary.org/obo/MOD_00925 heptosylated residue A protein modification that effectively converts an L-threonine residue to O-heptosyl-L-threonine. http://purl.obolibrary.org/obo/MOD_01201 N6-heptosyl-L-lysine http://purl.obolibrary.org/obo/MOD_00925 heptosylated residue A protein modification that effectively converts an L-lysine residue to N6-heptosyl-L-lysine. http://purl.obolibrary.org/obo/MOD_01202 N-heptosyl-L-asparagine http://purl.obolibrary.org/obo/MOD_00925 heptosylated residue A protein modification that effectively converts an L-asparagine residue to N-heptosyl-L-asparagine. http://purl.obolibrary.org/obo/MOD_01203 N6-(pyridylacetyl)lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively converts an L-lysine residue to N6-[(pyrid-3-yl)acetyl]lysine. http://purl.obolibrary.org/obo/MOD_01205 Hex1HexNAc1NeuAc2 O-glycosylated serine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively replaces an O3 hydrogen atom of a serine residue with a carbohydrate-like group composed of Hex1HexNAc1NeuAc2 linked through a glycosidic bond. http://purl.obolibrary.org/obo/MOD_01206 Hex1HexNAc1NeuAc2 O-glycosylated threonine http://purl.obolibrary.org/obo/MOD_00528 Hex1HexNAc1NeuAc2 glycosylated residue A protein modification that effectively replaces an O3 hydrogen atom of a threonine residue with a carbohydrate-like group composed of Hex1HexNAc1NeuAc2 linked through a glycosidic bond. http://purl.obolibrary.org/obo/MOD_01207 Hex1HexNAc1NeuAc2 N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine A protein modification that effectively replaces an N4 hydrogen atom of an asparagine residue with a carbohydrate-like group composed of Hex1HexNAc1NeuAc2 linked through a glycosidic bond. http://purl.obolibrary.org/obo/MOD_01208 copper(1+) carboxylate C-terminal residue http://purl.obolibrary.org/obo/MOD_00742 copper containing modified residue A protein modification that effectively converts a C-terminal residue to the copper(1+) carboxylate salt. http://purl.obolibrary.org/obo/MOD_01209 copper(1+) L-aspartate http://purl.obolibrary.org/obo/MOD_02066 metal or metal cluster coordinated L-aspartic acid residue A protein modification that effectively converts an L-aspartic acid residue to the copper(1+) aspartate salt. http://purl.obolibrary.org/obo/MOD_01210 copper(1+) L-glutamate http://purl.obolibrary.org/obo/MOD_02068 metal or metal cluster coordinated L-glutamic acid residue A protein modification that effectively converts an L-glutamic acid residue to the copper(1+) glutamate salt. http://purl.obolibrary.org/obo/MOD_01211 N6-(morpholine-2-acetyl)-lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively converts an L-lysine residue to N6-(morpholine-2-acetyl)-lysine. http://purl.obolibrary.org/obo/MOD_01212 iodoacetamide N6-derivatized lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively converts an L-lysine residue to N6-(carboxamidomethyl)lysine. http://purl.obolibrary.org/obo/MOD_01213 iodoacetamide derivatized histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively converts an L-histidine residue to an iodoacetamide derivatized histidine, either 1'- or 3'-(carboxamidolmethyl)histidine. http://purl.obolibrary.org/obo/MOD_01215 iodoacetamide derivatized aspartic acid http://purl.obolibrary.org/obo/MOD_00904 modified L-aspartic acid residue A protein modification that effectively converts an L-aspartic acid residue to O4-(carboxamidomethyl)aspartate. http://purl.obolibrary.org/obo/MOD_01216 iodoacetamide derivatized glutamic acid http://purl.obolibrary.org/obo/MOD_00906 modified L-glutamic acid residue A protein modification that effectively converts an L-glutamic acid residue to O5-(carboxamidomethyl)glutamate. http://purl.obolibrary.org/obo/MOD_01217 Sulfanilic Acid (SA), light C12 - site D http://purl.obolibrary.org/obo/MOD_00605 Sulfanilic Acid (SA), light C12 modification from Unimod Isotopic label - http://purl.obolibrary.org/obo/MOD_01218 Sulfanilic Acid (SA), light C12 - site E http://purl.obolibrary.org/obo/MOD_00605 Sulfanilic Acid (SA), light C12 modification from Unimod Isotopic label - http://purl.obolibrary.org/obo/MOD_01219 Sulfanilic Acid (SA), heavy C13 - site D http://purl.obolibrary.org/obo/MOD_00606 Sulfanilic Acid (SA), heavy C13 modification from Unimod Chemical derivative - http://purl.obolibrary.org/obo/MOD_01220 Sulfanilic Acid (SA), heavy C13 - site E http://purl.obolibrary.org/obo/MOD_00606 Sulfanilic Acid (SA), heavy C13 modification from Unimod Chemical derivative - http://purl.obolibrary.org/obo/MOD_01221 O-formyl-L-threonine http://purl.obolibrary.org/obo/MOD_02004 O3-acylated L-threonine A protein modification that effectively converts an L-threonine residue to O-formyl-L-threonine. http://purl.obolibrary.org/obo/MOD_01222 O-formyl-L-serine http://purl.obolibrary.org/obo/MOD_02003 O3-acylated L-serine A protein modification that effectively converts an L-serine residue to O-formyl-L-serine. http://purl.obolibrary.org/obo/MOD_01223 thioacylation of primary amines - site N-term http://purl.obolibrary.org/obo/MOD_00497 3-sulfanylpropanoyl (N-term and Lys) modification from Unimod Other - http://purl.obolibrary.org/obo/MOD_01224 thioacylation of primary amines - site K http://purl.obolibrary.org/obo/MOD_00497 3-sulfanylpropanoyl (N-term and Lys) modification from Unimod Other - http://purl.obolibrary.org/obo/MOD_01225 monofluorinated L-tyrosine http://purl.obolibrary.org/obo/MOD_00985 halogenated tyrosine A protein modification that effectively converts an L-tyrosine residue into an L-fluorotyrosine. http://purl.obolibrary.org/obo/MOD_01226 monofluorinated L-tryptophan http://purl.obolibrary.org/obo/MOD_01068 halogenated tryptophan A protein modification that effectively converts an L-tryptophan residue to an L-fluorotryptophan. http://purl.obolibrary.org/obo/MOD_01227 monofluorinated L-phenylalanine http://purl.obolibrary.org/obo/MOD_01066 halogenated phenylalanine A protein modification that effectively converts an L-phenylalanine residue to an L-fluorophenylalanine. http://purl.obolibrary.org/obo/MOD_01228 monoiodinated tyrosine http://purl.obolibrary.org/obo/MOD_00998 iodinated tyrosine A protein modification that effectively substitutes one hydrogen atom of an L-tyrosine residue with one iodine atom. http://purl.obolibrary.org/obo/MOD_01229 L-iodohistidine http://purl.obolibrary.org/obo/MOD_01049 halogenated histidine A protein modification that effectively converts an L-histidine residue to an L-iodohistidine. http://purl.obolibrary.org/obo/MOD_01230 Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, light form - site K http://purl.obolibrary.org/obo/MOD_00790 Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, light form modification from Unimod Isotopic label - http://purl.obolibrary.org/obo/MOD_01231 3x(13)C labeled N6-propanoyl-L-lysine http://purl.obolibrary.org/obo/MOD_01428 (13)C isotope tagged reagent A protein modification that effectively converts an L-lysine residue to 3x(13)C labeled N6-propanoyl-L-lysine. http://purl.obolibrary.org/obo/MOD_01232 3x(12)C labeled N6-propanoyl-L-lysine http://purl.obolibrary.org/obo/MOD_01426 isotope tagged reagent derivatized residue A protein modification that effectively converts an L-lysine residue to 3x(12)C labeled N6-propanoyl-L-lysine. http://purl.obolibrary.org/obo/MOD_01233 3x(2)H labeled N6-acetyl-L-lysine http://purl.obolibrary.org/obo/MOD_00449 acetate labeling reagent (N-term) (heavy form, +3amu) A protein modification that effectively converts an L-lysine residue to 3x(2)H labeled N6-acetyl-L-lysine. http://purl.obolibrary.org/obo/MOD_01234 (18)O monosubstituted L-serine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue modification from Unimod Isotopic label - alkaline phosphatase to dephosphorylate http://purl.obolibrary.org/obo/MOD_01235 (18)O monosubstituted L-threonine http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue modification from Unimod Isotopic label - alkaline phosphatase to dephosphorylate http://purl.obolibrary.org/obo/MOD_01236 (18)O monosubstituted L-tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue modification from Unimod Isotopic label - alkaline phosphatase to dephosphorylate http://purl.obolibrary.org/obo/MOD_01237 cysteine 4-hydroxynonenal adduct http://purl.obolibrary.org/obo/MOD_00446 4-hydroxynonenal adduct A protein modification produced by formation of an adduct of an L-cysteine residue with 4-hydroxynonenal. http://purl.obolibrary.org/obo/MOD_01238 lysine 4-hydroxynonenal adduct http://purl.obolibrary.org/obo/MOD_00446 4-hydroxynonenal adduct A protein modification produced by formation of an adduct of an L-lysine residue with 4-hydroxynonenal. http://purl.obolibrary.org/obo/MOD_01239 histidine 4-hydroxynonenal adduct http://purl.obolibrary.org/obo/MOD_00446 4-hydroxynonenal adduct A protein modification produced by formation of an adduct of an L-histidine residue with 4-hydroxynonenal. http://purl.obolibrary.org/obo/MOD_01241 3x(2)H labeled L-aspartic acid 4-methyl ester http://purl.obolibrary.org/obo/MOD_00904 modified L-aspartic acid residue A protein modification that effectively converts an L-lysine residue to 3x(2)H labeled L-aspartic acid 4-methyl ester. http://purl.obolibrary.org/obo/MOD_01242 3x(2)H labeled L-glutamic acid 5-methyl ester http://purl.obolibrary.org/obo/MOD_00906 modified L-glutamic acid residue A protein modification that effectively converts an L-lysine residue to 3x(2)H labeled L-glutamic acid 5-methyl ester. http://purl.obolibrary.org/obo/MOD_01243 potassium carboxylate C-terminal residue http://purl.obolibrary.org/obo/MOD_01072 monopotassium salt A protein modification that effectively converts a C-terminal residue to the potassium carboxylate salt. http://purl.obolibrary.org/obo/MOD_01244 potassium L-glutamate http://purl.obolibrary.org/obo/MOD_00906 modified L-glutamic acid residue A protein modification that effectively converts an L-glutamioc acid residue to the potassium glutamate salt. http://purl.obolibrary.org/obo/MOD_01245 potassium L-aspartate http://purl.obolibrary.org/obo/MOD_00904 modified L-aspartic acid residue A protein modification that effectively converts an L-aspartic acid residue to the potassium aspartate salt. http://purl.obolibrary.org/obo/MOD_01248 iodouridine monophosphate derivatized tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that is produced by reaction of iodouridine monophosphate with an L-tyrosine residue to form an ether linkage. http://purl.obolibrary.org/obo/MOD_01249 iodouridine monophosphate derivatized tryptophan http://purl.obolibrary.org/obo/MOD_00918 modified L-tryptophan residue A protein modification that is produced by reaction of iodouridine monophosphate with an L-tryptophan residue. http://purl.obolibrary.org/obo/MOD_01250 iodouridine monophosphate derivatized phenylalanine http://purl.obolibrary.org/obo/MOD_00914 modified L-phenylalanine residue A protein modification that is produced by reaction of iodouridine monophosphate with an L-phenylalanine residue. http://purl.obolibrary.org/obo/MOD_01251 N6-[3-(carboxamidomethylthio)propanoyl]lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively converts an L-lysine residue to N6-[3-(carboxamidomethylthio)propanoyl]lysine. http://purl.obolibrary.org/obo/MOD_01253 malondialdehyde lysine adduct (+54 amu) http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue modification from Unimod Chemical derivative - Malondialdehyde (MDA) adduct http://purl.obolibrary.org/obo/MOD_01254 4x(2)H labeled dimethylated L-lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively converts an L-lysine residue to 4x(2)H labeled dimethylated L-lysine. http://purl.obolibrary.org/obo/MOD_01255 S-(2-sulfanylethyl)cysteine (Ser) http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to S-(2-sulfanylethyl)cysteine. http://purl.obolibrary.org/obo/MOD_01256 3-methyl-S-(2-sulfanylethyl)cysteine (Thr) http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue A protein modification that effectively converts an L-threonine residue to 3-methyl-S-(2-sulfanylethyl)cysteine. http://purl.obolibrary.org/obo/MOD_01257 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate - site K http://purl.obolibrary.org/obo/MOD_00547 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate modification from Unimod Chemical derivative - http://purl.obolibrary.org/obo/MOD_01258 N-methylmaleimide modified L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue modification from Unimod Chemical derivative - http://purl.obolibrary.org/obo/MOD_01259 N-methylmaleimide modified L-lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue modification from Unimod Chemical derivative - http://purl.obolibrary.org/obo/MOD_01272 iminobiotinylation - site K http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine modification from Unimod Chemical derivative - http://purl.obolibrary.org/obo/MOD_01273 O-[4-(2-aminoethyl)benzenesulfonyl] serine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS, and an L-serine residue. http://purl.obolibrary.org/obo/MOD_01274 N'-[4-(2-aminoethyl)benzenesulfonyl] derivatized histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS, and an L-histidine residue. http://purl.obolibrary.org/obo/MOD_01275 N6-[4-(2-aminoethyl)benzenesulfonyl]lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS, and an L-lysine residue. http://purl.obolibrary.org/obo/MOD_01276 O4'-[4-(2-aminoethyl)benzenesulfonyl]tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS, and an L-tyrosine residue. http://purl.obolibrary.org/obo/MOD_01277 crotonylated L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue modification from Unimod Other - http://purl.obolibrary.org/obo/MOD_01278 crotonylated L-lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue modification from Unimod Other - http://purl.obolibrary.org/obo/MOD_01279 crotonylated L-histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue modification from Unimod Other - http://purl.obolibrary.org/obo/MOD_01280 EDT-iodo-PEO-biotin - site T http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue modification from Unimod Chemical derivative - http://purl.obolibrary.org/obo/MOD_01281 EDT-iodo-PEO-biotin - site S http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue modification from Unimod Chemical derivative - http://purl.obolibrary.org/obo/MOD_01285 6x(13)C,1x(15)N labeled L-leucine http://purl.obolibrary.org/obo/MOD_00911 modified L-leucine residue A protein modification that effectively converts an L-leucine residue to 6x(13)C,1x(15)N isotope labeled L-leucine. http://purl.obolibrary.org/obo/MOD_01286 6x(13)C,1x(15)N labeled L-isoleucine http://purl.obolibrary.org/obo/MOD_00910 modified L-isoleucine residue A protein modification that effectively converts an L-isoleucine residue to 6x(13)C,1x(15)N isotope labeled L-isoleucine. http://purl.obolibrary.org/obo/MOD_01287 Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, heavy form - site K http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue modification from Unimod Isotopic label - http://purl.obolibrary.org/obo/MOD_01293 1x(18)O labeled deamidated L-asparagine http://purl.obolibrary.org/obo/MOD_00852 1x(18)O labeled deamidated residue A protein modification that effectively converts an L-asparagine residue to L-aspartic acid with one (18)O. http://purl.obolibrary.org/obo/MOD_01295 monosodium L-aspartate http://purl.obolibrary.org/obo/MOD_00904 modified L-aspartic acid residue A protein modification that effectively converts an L-aspartic acid residue to monosodium L-aspartate. http://purl.obolibrary.org/obo/MOD_01296 monosodium L-glutamate http://purl.obolibrary.org/obo/MOD_00906 modified L-glutamic acid residue A protein modification that effectively converts an L-glutamic acid residue to monosodium L-glutamate. http://purl.obolibrary.org/obo/MOD_01297 5x(13)C labeled L-proline http://purl.obolibrary.org/obo/MOD_00915 modified L-proline residue A protein modification that effectively converts an L-proline residue to 5x(13)C labeled L-proline. http://purl.obolibrary.org/obo/MOD_01298 reduced cysteine 4-hydroxynonenal adduct http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification produced by formation of an adduct of an L-cysteine residue with 4-hydroxynonenal artificially reduced by a reagent such as NaBH4. http://purl.obolibrary.org/obo/MOD_01299 reduced lysine 4-hydroxynonenal adduct http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification produced by formation of an adduct of an L-histidine residue with 4-hydroxynonenal artificially reduced by a reagent such as NaBH4. http://purl.obolibrary.org/obo/MOD_01300 reduced histidine 4-hydroxynonenal adduct http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification produced by formation of an adduct of an L-histidine residue with 4-hydroxynonenal artificially reduced by a reagent such as NaBH4. http://purl.obolibrary.org/obo/MOD_01301 methylamine Michael addition derivatized threonine http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue A protein modification that effectively converts an L-threonine residue to 2-amino-3-(methylamino)butanoic acid. http://purl.obolibrary.org/obo/MOD_01302 methylamine Michael addition derivatized serine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to 2-amino-3-(methylamino)propanoic acid. http://purl.obolibrary.org/obo/MOD_01303 N4-hexosaminylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine A protein modification that effectively converts an L-asparagine residue to an N4-hexosaminyl-L-asparagine. http://purl.obolibrary.org/obo/MOD_01304 N6-hexosaminylated lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively converts an L-lysine residue to an N4-hexosaminyl-L-lysine, as a synthetic peptide protectting group. http://purl.obolibrary.org/obo/MOD_01305 N1'-hexosaminylated tryptophan http://purl.obolibrary.org/obo/MOD_00918 modified L-tryptophan residue A protein modification that effectively converts an L-tryptophan residue to N1'-hexosaminyl-L-tryptophan. http://purl.obolibrary.org/obo/MOD_01306 O-hexosaminylated threonine http://purl.obolibrary.org/obo/MOD_00876 hexosaminylated residue A protein modification that effectively converts an L-threonine residue to O-hexosaminyl-L-threonine. http://purl.obolibrary.org/obo/MOD_01307 thiophosphate labeled with biotin-HPDP -site S http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue modification from Unimod Chemical derivative - http://purl.obolibrary.org/obo/MOD_01308 thiophosphate labeled with biotin-HPDP -site T http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue modification from Unimod Chemical derivative - http://purl.obolibrary.org/obo/MOD_01309 thiophosphate labeled with biotin-HPDP - site Y http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue modification from Unimod Chemical derivative - http://purl.obolibrary.org/obo/MOD_01310 quaternary amine labeling reagent light form N6-L-lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively replaces a lysine N6-hydrogen with a quaternary amine reagent light form group. http://purl.obolibrary.org/obo/MOD_01311 quaternary amine labeling reagent heavy form (+3amu) N6-L-lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively replaces a lysine N6-hydrogen with a quaternary amine reagent heavy (+3amu) form group. http://purl.obolibrary.org/obo/MOD_01312 quaternary amine labeling reagent heavy form (+6amu) N6-L-lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively replaces a lysine N6-hydrogen with a quaternary amine reagent heavy (+6amu) form group. http://purl.obolibrary.org/obo/MOD_01313 quaternary amine labeling reagent heavy form (+9amu) N6-L-lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively replaces a lysine N6-hydrogen with a quaternary amine reagent heavy (+9amu) form group. http://purl.obolibrary.org/obo/MOD_01314 4x(1)H,4x(12)C-labeled N6-succinyl-L-lysine http://purl.obolibrary.org/obo/MOD_00670 N-acylated residue A protein modification that effectively converts an L-lysine residue to 4x(1)H,4x(12)C-labeled N6-succinyl-L-lysine. http://purl.obolibrary.org/obo/MOD_01315 4x(2)H labeled N6-succinyl-L-lysine http://purl.obolibrary.org/obo/MOD_00670 N-acylated residue A protein modification that effectively converts an L-lysine residue to 4x(2)H-labeled N6-succinyl-L-lysine. http://purl.obolibrary.org/obo/MOD_01316 4x(13)C labeled N6-succinyl-L-lysine http://purl.obolibrary.org/obo/MOD_00670 N-acylated residue A protein modification that effectively converts an L-lysine residue to 4x(13)C labeled N6-succinyl-L-lysine. http://purl.obolibrary.org/obo/MOD_01317 phosphorylation to amine thiol - site T http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue modification from Unimod Chemical derivative - http://purl.obolibrary.org/obo/MOD_01318 phosphorylation to amine thiol - site S http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue modification from Unimod Chemical derivative - http://purl.obolibrary.org/obo/MOD_01319 Michael addition of BHT quinone methide to histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue modification from Unimod Other http://purl.obolibrary.org/obo/MOD_01320 Michael addition of BHT quinone methide to lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue modification from Unimod Other http://purl.obolibrary.org/obo/MOD_01321 Michael addition of BHT quinone methide to cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue modification from Unimod Other http://purl.obolibrary.org/obo/MOD_01326 9x(13)C labeled L-tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively converts an L-tyrosine residue to 9x(13)C labeled L-tyrosine. http://purl.obolibrary.org/obo/MOD_01327 9x(13)C labeled L-phenylalanine http://purl.obolibrary.org/obo/MOD_00914 modified L-phenylalanine residue A protein modification that effectively converts an L-phenylalanine residue to 9x(13)C labeled L-phenylalanine. http://purl.obolibrary.org/obo/MOD_01328 iodoacetic acid - site W http://purl.obolibrary.org/obo/MOD_00918 modified L-tryptophan residue modification from Unimod Chemical derivative - hydroxylethanone http://purl.obolibrary.org/obo/MOD_01331 6x(13)C labeled L-arginine http://purl.obolibrary.org/obo/MOD_00544 6x(13)C labeled residue A protein modification that effectively converts an L-arginine residue to 6x(13)C labeled L-arginine. http://purl.obolibrary.org/obo/MOD_01332 6x(13)C labeled L-leucine http://purl.obolibrary.org/obo/MOD_00544 6x(13)C labeled residue A protein modification that effectively converts an L-leucine residue to 6x(13)C labeled L-leucine. http://purl.obolibrary.org/obo/MOD_01333 6x(13)C labeled L-isoleucine http://purl.obolibrary.org/obo/MOD_00544 6x(13)C labeled residue A protein modification that effectively converts an L-isoleucine residue to 6x(13)C labeled L-isoleucine. http://purl.obolibrary.org/obo/MOD_01334 6x(13)C labeled L-lysine http://purl.obolibrary.org/obo/MOD_00544 6x(13)C labeled residue A protein modification that effectively converts an L-lysine residue to 6x(13)C labeled L-lysine. http://purl.obolibrary.org/obo/MOD_01335 6x(13)C labeled 4-sulfophenyl isothiocyanate derivatized lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue modification from Unimod Chemical derivative - http://purl.obolibrary.org/obo/MOD_01337 deamidated 4-methyl esterified asparagine http://purl.obolibrary.org/obo/MOD_01369 deamidated and methyl esterified residue A protein modification that effectively converts an L-asparagine residue to L-aspartate 4-methyl ester. http://purl.obolibrary.org/obo/MOD_01338 N6-ethyl-L-lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively converts an L-lysine residue to N6-ethyl-L-lysine. http://purl.obolibrary.org/obo/MOD_01339 ethylated residue http://purl.obolibrary.org/obo/MOD_00001 alkylated residue A protein modification that effectively replaces a hydrogen atom with an ethyl group. http://purl.obolibrary.org/obo/MOD_01340 ESP-Tag heavy d10 - site K http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue modification from Unimod Isotopic label - http://purl.obolibrary.org/obo/MOD_01341 ESP-Tag light d0 - site K http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue modification from Unimod Isotopic label - http://purl.obolibrary.org/obo/MOD_01345 2-amino-3-oxobutanoic acid http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue A protein modification that effectively converts an L-threonine residue to 2-amino-3-oxobutanoic acid. http://purl.obolibrary.org/obo/MOD_01346 N4-hexosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine A protein modification that effectively converts an L-asparagine residue to an N4-hexosyl-L-asparagine. http://purl.obolibrary.org/obo/MOD_01347 hexose glycated L-lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A modification produced in a non-enzymatic reaction between a carbohydrate carbonyl group (C1 of aldohexose or C2 of fructose) and an L-lysine residue to form a Schiff-base or an Amadori ketosamine lysine adduct. http://purl.obolibrary.org/obo/MOD_01348 O-hexosylated threonine http://purl.obolibrary.org/obo/MOD_00434 hexosylated residue A protein modification that effectively converts an L-threonine residue to an O-hexosyl-L-threonine. http://purl.obolibrary.org/obo/MOD_01349 hydrolyzed N-ethylmaleimide cysteine adduct http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue modification from Unimod Chemical derivative - http://purl.obolibrary.org/obo/MOD_01350 hydrolyzed N-ethylmaleimide lysine adduct http://purl.obolibrary.org/obo/MOD_00631 hydrolyzed N-ethylmaleimide adduct modification from Unimod Chemical derivative - http://purl.obolibrary.org/obo/MOD_01351 nitrated L-tryptophan http://purl.obolibrary.org/obo/MOD_00918 modified L-tryptophan residue A protein modification that effectively converts an L-tryptophan residue to a nitrated L-tryptophan. http://purl.obolibrary.org/obo/MOD_01353 amidination of lysines or N-terminal amines with methyl acetimidate - site K http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue modification from Unimod Chemical derivative - http://purl.obolibrary.org/obo/MOD_01354 Hex1HexNAc1NeuAc1 N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine A protein modification that effectively replaces an N4 hydrogen atom of an asparagine residue with a carbohydrate-like group composed of Hex1HexNAc1NeuAc1 linked through a glycosidic bond. http://purl.obolibrary.org/obo/MOD_01355 Hex1HexNAc1NeuAc1 O-glycosylated threonine http://purl.obolibrary.org/obo/MOD_00517 Hex1HexNAc1NeuAc1 glycosylated residue A protein modification that effectively replaces an O3 hydrogen atom of a threonine residue with a carbohydrate-like group composed of Hex1HexNAc1NeuAc1 linked through a glycosidic bond. http://purl.obolibrary.org/obo/MOD_01356 Hex1HexNAc1NeuAc1 O-glycosylated serine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively replaces an O3 hydrogen atom of a serine residue with a carbohydrate-like group composed of Hex1HexNAc1NeuAc1 linked through a glycosidic bond. http://purl.obolibrary.org/obo/MOD_01357 2x(13)C,4x(2)H labeled dimethylated L-lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively replaces two hydrogen atoms of an L-lysine 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 L-lysine. http://purl.obolibrary.org/obo/MOD_01358 Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, medium form - site N-term http://purl.obolibrary.org/obo/MOD_01426 isotope tagged reagent derivatized residue modification from Unimod Isotopic label - Use when labelling post-digest http://purl.obolibrary.org/obo/MOD_01359 Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, medium form - site K http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue modification from Unimod Isotopic label - Use when labelling post-digest http://purl.obolibrary.org/obo/MOD_01360 4-sulfophenyl isothiocyanate N6-derivatized lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively converts an L-lysine residue to the 4-sulfophenyl isothiocyanate adduct, N6-[(4-sulfophenyl)carbamothioyl]lysine. http://purl.obolibrary.org/obo/MOD_01361 O-thiophospho-L-threonine http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue A protein modification that effectively converts an L-threonine residue to O-thiophospho-L-threonine. http://purl.obolibrary.org/obo/MOD_01362 O-thiophospho-L-serine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to O-thiophospho-L-serine. http://purl.obolibrary.org/obo/MOD_01363 O4'-thiophospho-L-tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively converts an L-tyrosine residue to O4'-thiophospho-L-tyrosine. http://purl.obolibrary.org/obo/MOD_01364 fluorescein-5-thiosemicarbazide - site S http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue modification from Unimod Chemical derivative - http://purl.obolibrary.org/obo/MOD_01365 fluorescein-5-thiosemicarbazide - site C http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue modification from Unimod Chemical derivative - http://purl.obolibrary.org/obo/MOD_01366 fluorescein-5-thiosemicarbazide - site K http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue modification from Unimod Chemical derivative - http://purl.obolibrary.org/obo/MOD_01367 fluorescein-5-thiosemicarbazide - site P http://purl.obolibrary.org/obo/MOD_00915 modified L-proline residue modification from Unimod Chemical derivative - http://purl.obolibrary.org/obo/MOD_01368 fluorescein-5-thiosemicarbazide - site R http://purl.obolibrary.org/obo/MOD_00902 modified L-arginine residue modification from Unimod Chemical derivative - http://purl.obolibrary.org/obo/MOD_01369 deamidated and methyl esterified residue http://purl.obolibrary.org/obo/MOD_00393 O-methylated residue A protein modification that effectively replaces a carboxamido group with a carboxyl methyl ester group. http://purl.obolibrary.org/obo/MOD_01370 6x(13)C,1x(15)N labeled residue http://purl.obolibrary.org/obo/MOD_00843 (15)N labeled residue A protein modification that effectively converts a residue containing common isotopes to a 6x(13)C,1x(15)N labeled residue. http://purl.obolibrary.org/obo/MOD_01372 (2S)-4-hydroxyleucine http://purl.obolibrary.org/obo/MOD_01411 monohydroxylated leucine A protein modification that effectively converts an L-leucine residue to a (2S)-4-hydroxyleucine. http://purl.obolibrary.org/obo/MOD_01373 (2S,4R)-5-hydroxyleucine http://purl.obolibrary.org/obo/MOD_01411 monohydroxylated leucine A protein modification that effectively converts an L-leucine residue to a (2S,4R)-5-hydroxyleucine. http://purl.obolibrary.org/obo/MOD_01374 (2S,4R)-5-oxoleucine http://purl.obolibrary.org/obo/MOD_00911 modified L-leucine residue A modification that effectively oxygenates C5 of an L-leucine residue to form a (2S,4R)-5-oxoleucine. http://purl.obolibrary.org/obo/MOD_01375 (2S,4R)-4,5-dihydroxyleucine http://purl.obolibrary.org/obo/MOD_01412 dihydroxylated leucine A protein modification that effectively converts an L-leucine residue to a (2S,4R)-4,5-dihydroxyleucine. http://purl.obolibrary.org/obo/MOD_01376 (2S,3S,4R)-3,4-dihydroxyisoleucine http://purl.obolibrary.org/obo/MOD_01416 dihydroxylated isoleucine A protein modification that effectively converts an L-isoleucine residue to a (2S,3S,4R)-3,4-dihydroxyisoleucine. http://purl.obolibrary.org/obo/MOD_01377 (2S,3R,4S)-4-hydroxyisoleucine http://purl.obolibrary.org/obo/MOD_01415 monohydroxylated isoleucine A protein modification that effectively converts an L-isoleucine residue to a (2S,3R,4S)-4-hydroxyisoleucine. http://purl.obolibrary.org/obo/MOD_01378 (2S,3R,4R)-4,5-dihydroxyisoleucine http://purl.obolibrary.org/obo/MOD_01416 dihydroxylated isoleucine A protein modification that effectively converts an L-isoleucine residue to a (2S,3R,4R)-4,5-dihydroxyisoleucine. http://purl.obolibrary.org/obo/MOD_01379 2'-methylsulfonyl-L-tryptophan http://purl.obolibrary.org/obo/MOD_00918 modified L-tryptophan residue A protein modification that effectively converts an L-tryptophan residue to 2'-methylsulfonyl-L-tryptophan. http://purl.obolibrary.org/obo/MOD_01380 2'-(S-L-cysteinyl)-6'-hydroxy-L-tryptophan sulfoxide http://purl.obolibrary.org/obo/MOD_02057 crosslinked L-tryptophan residue A protein modification that effectively cross-links an L-cysteine residue and an L-tryptophan residue by a thioether bond to form 2'-(S-L-cysteinyl)-6'-hydroxy-L-tryptophan sulfoxide. http://purl.obolibrary.org/obo/MOD_01381 O-palmitoleyl-L-serine http://purl.obolibrary.org/obo/MOD_02003 O3-acylated L-serine A protein modification that effectively converts an L-serine residue to O-palmitoleyl-L-serine. http://purl.obolibrary.org/obo/MOD_01382 N,N,N-trimethyl-L-methionine http://purl.obolibrary.org/obo/MOD_01698 alpha-amino trimethylated protonated-residue A protein modification that effectively converts an L-methionine residue to N,N,N-trimethyl-L-methionine. http://purl.obolibrary.org/obo/MOD_01383 L-cystine S-oxide http://purl.obolibrary.org/obo/MOD_02044 crosslinked L-cysteine residue A protein modification that effectively cross-links two L-cysteine residues and oxidizes a sulfur to form L-cystine S-oxide. http://purl.obolibrary.org/obo/MOD_01384 aminomalonic acid (Ser) http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to an aminomalonic acid. http://purl.obolibrary.org/obo/MOD_01385 3-hydroxy-L-phenylalanine http://purl.obolibrary.org/obo/MOD_00914 modified L-phenylalanine residue A protein modification that effectively converts an L-phenylalanine residue to 3-hydroxy-L-phenylalanine. http://purl.obolibrary.org/obo/MOD_01386 3-hydroxy-L-valine http://purl.obolibrary.org/obo/MOD_00920 modified L-valine residue A protein modification that effectively converts an L-valine residue to 3-hydroxy-L-valine. http://purl.obolibrary.org/obo/MOD_01387 O-methyl-L-threonine http://purl.obolibrary.org/obo/MOD_01803 O-methylated threonine A protein modification that effectively converts an L-threonine residue to O-methyl-L-threonine. http://purl.obolibrary.org/obo/MOD_01388 1-amino-2-propanol http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue A protein modification that effectively converts an L-threonine residue into 1-amino-2-propanol. http://purl.obolibrary.org/obo/MOD_01389 L-isoleucine thiazole-4-carboxylic acid http://purl.obolibrary.org/obo/MOD_02049 crosslinked L-isoleucine residue A protein modification that effectively crosslinks an L-cysteine residue and an L-isoleucine residue to form L-isoleucine thiazole-4-carboxylic acid. http://purl.obolibrary.org/obo/MOD_01390 L-valine thiazole-4-carboxylic acid http://purl.obolibrary.org/obo/MOD_02059 crosslinked L-valine residue A protein modification that effectively crosslinks an L-cysteine residue and an L-valine residue to form L-valine thiazole-4-carboxylic acid. http://purl.obolibrary.org/obo/MOD_01391 L-valine 5-(methoxymethyl)thiazole-4-carboxylic acid http://purl.obolibrary.org/obo/MOD_02059 crosslinked L-valine residue A protein modification that effectively crosslinks an L-cysteine residue and an L-valine residue, and C-5 methoxymethylates to form L-valine 5-(methoxymethyl)thiazole-4-carboxylic acid. http://purl.obolibrary.org/obo/MOD_01392 L-asparagine 5-methylthiazole-4-carboxylic acid http://purl.obolibrary.org/obo/MOD_02042 crosslinked L-asparagine residue A protein modification that effectively crosslinks an L-cysteine residue and an L-asparagine residue, and C-4 methylates to form L-asparagine 5-methylthiazole-4-carboxylic acid. http://purl.obolibrary.org/obo/MOD_01393 L-cysteine pyridine-2,5-dicarboxylic acid http://purl.obolibrary.org/obo/MOD_02055 crosslinked L-serine residue A protein modification that crosslinks two serine residues and a cysteine residue by formation of a pyridine-2,5-dicarboxylic acid. http://purl.obolibrary.org/obo/MOD_01394 L-cysteine 5-amino-3,4,5,6-tetrahydropyridine-2,5-dicarboxylic acid http://purl.obolibrary.org/obo/MOD_02055 crosslinked L-serine residue A protein modification that crosslinks two serine residues and a cysteine residue by formation of a 5-amino-3,4,5,6-tetrahydropyridine-2,5-dicarboxylic acid. http://purl.obolibrary.org/obo/MOD_01395 4-(1-hydroxyethyl)-7-isoleucino-2-(threonin-O3-ylcarbonyl)-7,8-dihydroquinolin-8-ol http://purl.obolibrary.org/obo/MOD_02056 crosslinked L-threonine residue A protein modification that effectively results from forming an adduct between an isoleucine residue, a threonine residue and the quinaldate compound 2-carboxy-4-(1-hydroxyethyl)--7,8-dihydroquinolin-8-ol. http://purl.obolibrary.org/obo/MOD_01396 5-hydroxy-3-methyl-L-proline (Pro) http://purl.obolibrary.org/obo/MOD_00915 modified L-proline residue A protein modification that effectively converts an L-proline residue to a 5-hydroxy-3-methyl-L-proline. http://purl.obolibrary.org/obo/MOD_01397 L-serine 5-methyloxazole-4-carboxylic acid http://purl.obolibrary.org/obo/MOD_02055 crosslinked L-serine residue A protein modification that effectively crosslinks an L-serine residue and an L-threonine residue to form L-serine 5-methyloxazole-4-carboxylic acid. http://purl.obolibrary.org/obo/MOD_01398 N6-propanoyl-L-lysine http://purl.obolibrary.org/obo/MOD_01155 lipoconjugated residue A protein modification that effectively converts an L-lysine residue to N6-propanoyl-L-lysine. http://purl.obolibrary.org/obo/MOD_01400 L-lysyl-poly(ADP-ribose) http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively converts an L-lysine residue to an L-lysyl-poly(ADP-ribose). http://purl.obolibrary.org/obo/MOD_01401 (2S,3S)-3-hydroxyasparagine http://purl.obolibrary.org/obo/MOD_01688 3-hydroxy-L-asparagine A protein modification that effectively converts an L-asparagine residue to a (2S,3S)-3-hydroxyasparagine. http://purl.obolibrary.org/obo/MOD_01402 (2S,3R,4R)-3,4-dihydroxyproline http://purl.obolibrary.org/obo/MOD_00866 dihydroxylated proline A protein modification that effectively converts an L-proline residue to a (2S,3R,4R)-3,4-dihydroxyproline. http://purl.obolibrary.org/obo/MOD_01403 (2S)-4,5,5'-trihydroxyleucine http://purl.obolibrary.org/obo/MOD_01413 trihydroxylated leucine A protein modification that effectively converts an L-leucine residue to a (2S)-4,5,5'-trihydroxyleucine. http://purl.obolibrary.org/obo/MOD_01404 L-asparagine thiazole-4-carboxylic acid http://purl.obolibrary.org/obo/MOD_02042 crosslinked L-asparagine residue A protein modification that effectively crosslinks an L-cysteine residue and an L-asparagine residue to form L-asparagine thiazole-4-carboxylic acid. http://purl.obolibrary.org/obo/MOD_01405 L-proline thiazole-4-carboxylic acid http://purl.obolibrary.org/obo/MOD_02054 crosslinked L-proline residue A protein modification that effectively crosslinks an L-cysteine residue and an L-proline residue to form L-proline thiazole-4-carboxylic acid. http://purl.obolibrary.org/obo/MOD_01406 L-threonine thiazole-4-carboxylic acid http://purl.obolibrary.org/obo/MOD_02056 crosslinked L-threonine residue A protein modification that effectively crosslinks an L-cysteine residue and an L-threonine residue to form L-threonine thiazole-4-carboxylic acid. http://purl.obolibrary.org/obo/MOD_01407 L-phenylalanine thiazoline-4-carboxylic acid http://purl.obolibrary.org/obo/MOD_02053 crosslinked L-phenylalanine residue A protein modification that effectively crosslinks an L-cysteine residue and an L-phenylalanine residue to form L-phenylalanine thiazoline-4-carboxylic acid. http://purl.obolibrary.org/obo/MOD_01408 L-threonine thiazoline-4-carboxylic acid http://purl.obolibrary.org/obo/MOD_02056 crosslinked L-threonine residue A protein modification that effectively crosslinks an L-cysteine residue and an L-threonine residue to form L-threonine thiazoline-4-carboxylic acid. http://purl.obolibrary.org/obo/MOD_01409 trihydroxylated residue http://purl.obolibrary.org/obo/MOD_00677 hydroxylated residue A protein modification that effectively replaces three hydrogen atoms with three hydroxyl groups. http://purl.obolibrary.org/obo/MOD_01410 hydroxylated leucine http://purl.obolibrary.org/obo/MOD_00911 modified L-leucine residue A protein modification that effectively converts an L-leucine residue to an hydroxylated leucine. http://purl.obolibrary.org/obo/MOD_01411 monohydroxylated leucine http://purl.obolibrary.org/obo/MOD_01410 hydroxylated leucine A protein modification that effectively converts an L-leucine residue to a monohydroxylated leucine. http://purl.obolibrary.org/obo/MOD_01412 dihydroxylated leucine http://purl.obolibrary.org/obo/MOD_01410 hydroxylated leucine A protein modification that effectively converts an L-leucine residue to a dihydroxylated leucine. http://purl.obolibrary.org/obo/MOD_01413 trihydroxylated leucine http://purl.obolibrary.org/obo/MOD_01410 hydroxylated leucine A protein modification that effectively converts an L-leucine residue to a trihydroxylated leucine. http://purl.obolibrary.org/obo/MOD_01414 hydroxylated isoleucine http://purl.obolibrary.org/obo/MOD_00910 modified L-isoleucine residue A protein modification that effectively converts an L-isoleucine residue to an hydroxylated isoleucine. http://purl.obolibrary.org/obo/MOD_01415 monohydroxylated isoleucine http://purl.obolibrary.org/obo/MOD_01414 hydroxylated isoleucine A protein modification that effectively converts an L-isoleucine residue to a monohydroxylated isoleucine. http://purl.obolibrary.org/obo/MOD_01416 dihydroxylated isoleucine http://purl.obolibrary.org/obo/MOD_01414 hydroxylated isoleucine A protein modification that effectively converts an L-isoleucine residue to a dihydroxylated isoleucine. http://purl.obolibrary.org/obo/MOD_01417 monomethylated proline http://purl.obolibrary.org/obo/MOD_00599 monomethylated residue A protein modification that effectively converts an L-proline residue to a monomethylated proline. http://purl.obolibrary.org/obo/MOD_01418 methylated threonine http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue A protein modification that effectively converts an L-threonine residue to a methylated threonine, such as O-methyl-L-threonine. http://purl.obolibrary.org/obo/MOD_01419 oxazole/oxazoline ring crosslinked residues http://purl.obolibrary.org/obo/MOD_00690 oxazole/thiazole ring crosslinked residues A protein modification that crosslinks two residues by condensation of a serine or threonine hydroxyl with the carbonyl of the preceding residue to form an oxazole or oxazoline ring, or by rearrangement and condensation of a cysteine with the carbonyl of the preceding residue to form a 1,3-oxazole-4-carbothionic acid. http://purl.obolibrary.org/obo/MOD_01420 thiazole/thiazoline ring crosslinked residues http://purl.obolibrary.org/obo/MOD_00690 oxazole/thiazole ring crosslinked residues A protein modification that crosslinks two residues by condensation of a cysteine thiol with the carbonyl of the preceding residue to form a thiazole or thiazoline ring. http://purl.obolibrary.org/obo/MOD_01421 oxazole/oxazoline ring crosslinked residues (Ser) http://purl.obolibrary.org/obo/MOD_02055 crosslinked L-serine residue A protein modification that crosslinks two residues by condensation of a serine hydroxyl with the carbonyl of the preceding residue to form an oxazole or oxazoline ring. http://purl.obolibrary.org/obo/MOD_01422 oxazole/oxazoline ring crosslinked residues (Thr) http://purl.obolibrary.org/obo/MOD_02056 crosslinked L-threonine residue A protein modification that crosslinks two residues by condensation of a threonine hydroxyl with the carbonyl of the preceding residue to form a 5-methyloxazole or 5-methyloxazoline ring. http://purl.obolibrary.org/obo/MOD_01423 palmitoleylated residue http://purl.obolibrary.org/obo/MOD_01155 lipoconjugated residue A protein modification that effectively replaces a hydrogen atom with a palmitoleyl group. http://purl.obolibrary.org/obo/MOD_01424 quinaldate modified residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process A protein modification that effectively results from forming an adduct with a compound containing a quinaldate, kynurenate, or xanthurenate group. http://purl.obolibrary.org/obo/MOD_01425 pyridinyl ring crosslinked residues http://purl.obolibrary.org/obo/MOD_00033 crosslinked residues A protein modification that crosslinks three residues by formation of a pyridinyl ring, such as pyridine-2,5-dicarboxylic acid or 5-aminopiperideine-2,5-dicarboxylic acid. http://purl.obolibrary.org/obo/MOD_01426 isotope tagged reagent derivatized residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue A protein modification that forms an adduct with a particular isotope labeled compound used as a reagent. http://purl.obolibrary.org/obo/MOD_01428 (13)C isotope tagged reagent http://purl.obolibrary.org/obo/MOD_01426 isotope tagged reagent derivatized residue A protein modification that forms an adduct with a (13)C labeled compound used as a reagent. http://purl.obolibrary.org/obo/MOD_01429 (15)N isotope tagged reagent http://purl.obolibrary.org/obo/MOD_01426 isotope tagged reagent derivatized residue A protein modification that forms an adduct with a (15)N labeled compound used as a reagent. http://purl.obolibrary.org/obo/MOD_01430 (18)O isotope tagged reagent http://purl.obolibrary.org/obo/MOD_01426 isotope tagged reagent derivatized residue A protein modification that forms an adduct with a (13)C labeled compound used as a reagent. http://purl.obolibrary.org/obo/MOD_01431 (2)H deuterium tagged reagent http://purl.obolibrary.org/obo/MOD_01426 isotope tagged reagent derivatized residue A protein modification that forms an adduct with a (2)H labeled compound used as a reagent. http://purl.obolibrary.org/obo/MOD_01432 (2S,4S)-4,5-dihydroxyleucine http://purl.obolibrary.org/obo/MOD_01412 dihydroxylated leucine A protein modification that effectively converts an L-leucine residue to a (2S,4S)-4,5-dihydroxyleucine. http://purl.obolibrary.org/obo/MOD_01433 1-amino-2-propanone http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue A protein modification that effectively converts an L-threonine residue into 1-amino-2-propanone. http://purl.obolibrary.org/obo/MOD_01434 4-hydroxy-L-glutamic acid http://purl.obolibrary.org/obo/MOD_00906 modified L-glutamic acid residue A protein modification that effectively converts an L-glutamic acid residue to a 4-hydroxy-L-glutamic acid. http://purl.obolibrary.org/obo/MOD_01435 2-(cystein-S-ylcarbonyl)-3-methyl-4-(glutam-5-yloxy)methylindole http://purl.obolibrary.org/obo/MOD_02045 crosslinked L-glutamic acid residue A protein modification that effectively results from forming an adduct between a cysteine residue, a glutamic acid residue and the indole compound 2-carboxy-3-methyl-4-hydroxymethyl--indole. http://purl.obolibrary.org/obo/MOD_01436 cyclo[(prolylserin)-O-yl] cysteinate (Cys) http://purl.obolibrary.org/obo/MOD_01629 cyclo[(prolylserin)-O-yl] cysteinate A protein modification that effectively converts an L-cysteine residue to cyclo[(prolylserin)-O-yl] cysteinate. http://purl.obolibrary.org/obo/MOD_01437 cyclo[(prolylserin)-O-yl] cysteinate (Cys-Pro-Ser cross-link) http://purl.obolibrary.org/obo/MOD_02055 crosslinked L-serine residue A protein modification that effectively converts an L-cysteine residue, an L-proline residue, and an L-serine residue to cyclo[(prolylserin)-O-yl] cysteinate. http://purl.obolibrary.org/obo/MOD_01438 S-[2-(pyridin-2-yl)ethyl]-L-cysteine http://purl.obolibrary.org/obo/MOD_00424 S-pyridylethyl-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-[2-(pyridin-2-yl)ethyl]-L-cysteine. http://purl.obolibrary.org/obo/MOD_01439 S-[2-(pyridin-4-yl)ethyl]-L-cysteine http://purl.obolibrary.org/obo/MOD_00424 S-pyridylethyl-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-[2-(pyridin-4-yl)ethyl]-L-cysteine. http://purl.obolibrary.org/obo/MOD_01440 glutamyl semialdehyde http://purl.obolibrary.org/obo/MOD_00859 modified residue that can arise from different natural residues A protein modification that effectively converts a source amino acid residue to an L-glutamyl semialdehyde. http://purl.obolibrary.org/obo/MOD_01441 natural, standard, encoded residue http://purl.obolibrary.org/obo/MOD_00009 natural residue A protein modification that inserts or replaces a residue with a natural, standard, encoded residue. http://purl.obolibrary.org/obo/MOD_01442 3-(O4'-L-tyrosyl)-L-valine http://purl.obolibrary.org/obo/MOD_02059 crosslinked L-valine residue A protein modification that effectively cross-links an L-valine residue and an L-tyrosine residue by an ether bond to form 3-(O4'-L-tyrosyl)-L-valine. http://purl.obolibrary.org/obo/MOD_01443 tetrakis-L-glutamato bis-L-N1'-histidino lipid carboxylato manganese iron oxide http://purl.obolibrary.org/obo/MOD_02070 metal or metal cluster coordinated L-histidine residue A protein modification that effectively converts four L-glutamic acid residues and two L-histidine residues to tetrakis-L-glutamato bis-L-N1'-histidino lipid carboxylato manganese iron oxide. http://purl.obolibrary.org/obo/MOD_01444 L-3,3-dihydroxyoalanine (Cys) http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to L-3,3-dihydroxyoalanine. http://purl.obolibrary.org/obo/MOD_01445 L-3,3-dihydroxyoalanine (Ser) http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to L-3,3-dihydroxyoalanine. http://purl.obolibrary.org/obo/MOD_01446 N-(dihydroxymethyl)-L-methionine (fMet) http://purl.obolibrary.org/obo/MOD_01450 modified N-formyl-L-methionine residue A protein modification that effectively converts an N-formyl-Lmethionine residue to N-(dihydroxymethyl)-L-methionine. http://purl.obolibrary.org/obo/MOD_01447 N-(dihydroxymethyl)-L-methionine (Met) http://purl.obolibrary.org/obo/MOD_00913 modified L-methionine residue A protein modification that effectively converts an L-methionine residue to N-(dihydroxymethyl)-L-methionine (not known as a natural, post-translational modification process). http://purl.obolibrary.org/obo/MOD_01448 L-3,3-dihydroxyoalanine http://purl.obolibrary.org/obo/MOD_00859 modified residue that can arise from different natural residues A protein modification that effectively converts a source amino acid residue to L-3,3-dihydroxyoalanine. http://purl.obolibrary.org/obo/MOD_01449 L-3,3-dihydroxyoalanine (Oxoalanine) http://purl.obolibrary.org/obo/MOD_01448 L-3,3-dihydroxyoalanine A protein modification that effectively converts an L-3-oxoalanine residue to L-3,3-dihydroxyoalanine. http://purl.obolibrary.org/obo/MOD_01450 modified N-formyl-L-methionine residue http://purl.obolibrary.org/obo/MOD_01157 protein modification categorized by amino acid modified A protein modification that modifies an N-formyl-L-methionine residue. http://purl.obolibrary.org/obo/MOD_01451 O-phospho-L-serine arising from O-phosphopantetheine-L-serine after neutral loss of pantetheine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that converts an L-serine residue to O-phosphopantetheine-L-serine with secondary neutral loss of pantetheine resulting in O-phospho-L-serine. http://purl.obolibrary.org/obo/MOD_01452 O-phosphopantetheine-L-serine with neutral loss of pantetheine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue Covalent modification of a peptide or protein amino acid O-phosphopantetheine-L-serine with secondary neutral loss of pantetheine resulting in O-phospho-L-serine. http://purl.obolibrary.org/obo/MOD_01453 L-glutamic acid 5-methyl ester http://purl.obolibrary.org/obo/MOD_00599 monomethylated residue A protein modification that effectively converts a source amino acid residue to L-glutamate 5-methyl ester. http://purl.obolibrary.org/obo/MOD_01454 N-(DNA-1',2'-dideoxyribos-1'-ylidene)-L-prolinium http://purl.obolibrary.org/obo/MOD_00915 modified L-proline residue A protein modification that effectively crosslinks an N-terminal L-proline residue and a strand of DNA at the C-1 of a ribose, freeing the nucleotide base and forming N-(DNA-1',2'-dideoxyribos-1'-ylidene)-L-prolinium. http://purl.obolibrary.org/obo/MOD_01455 O-phosphorylated residue http://purl.obolibrary.org/obo/MOD_00696 phosphorylated residue A protein modification that effectively replaces a residue hydroxyl or carboxyl hydrogen with a phosphono group (H2PO3 or 'phosphate'). http://purl.obolibrary.org/obo/MOD_01456 N-phosphorylated residue http://purl.obolibrary.org/obo/MOD_00696 phosphorylated residue A protein modification that effectively replaces a hydrogen atom of a residue amino or imino group with a phosphono group (H2PO3 or 'phosphate'). http://purl.obolibrary.org/obo/MOD_01457 L-cysteine (Ser) http://purl.obolibrary.org/obo/MOD_02088 natural, standard, encoded residue substitution A protein modification that effectively converts an L-serine residue to L-cysteine (not known as a natural, post-translational modification process). http://purl.obolibrary.org/obo/MOD_01458 alpha-amino acetylated residue http://purl.obolibrary.org/obo/MOD_01696 alpha-amino acylated residue A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an acetyl group. http://purl.obolibrary.org/obo/MOD_01459 4x(2)H labeled alpha-dimethylamino N-terminal residue http://purl.obolibrary.org/obo/MOD_00552 4x(2)H labeled dimethylated residue A protein modification that effectively converts an N-terminal residue to an 4x(2)H labeled alpha-dimethylamino N-terminal residue. http://purl.obolibrary.org/obo/MOD_01460 alpha-amino methylated residue http://purl.obolibrary.org/obo/MOD_00602 N-methylated residue A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a methyl group. http://purl.obolibrary.org/obo/MOD_01461 N-methylated alanine http://purl.obolibrary.org/obo/MOD_01460 alpha-amino methylated residue A protein modification that effectively replaces an L-alanine alpha amino hydrogen with a methyl group. http://purl.obolibrary.org/obo/MOD_01462 N-methylated proline http://purl.obolibrary.org/obo/MOD_01460 alpha-amino methylated residue A protein modification that effectively replaces an L-proline alpha imino hydrogen with a methyl group. http://purl.obolibrary.org/obo/MOD_01463 N-methylated methionine http://purl.obolibrary.org/obo/MOD_01460 alpha-amino methylated residue A protein modification that effectively replaces an L-methionine alpha amino hydrogen with a methyl group. http://purl.obolibrary.org/obo/MOD_01464 protonated L-methionine (L-methioninium) residue http://purl.obolibrary.org/obo/MOD_00913 modified L-methionine residue A protein modification that effectively converts an L-methionine residue to an L-methioninium (protonated L-methionine). http://purl.obolibrary.org/obo/MOD_01465 N,N,N-trimethyl-L-methionine (from L-methioninium) http://purl.obolibrary.org/obo/MOD_01687 alpha-amino trimethylated residue A protein modification that effectively converts an L-methioninium (protonated L-methionine) residue to an N6,N6,N6-trimethyl-L-methionine. http://purl.obolibrary.org/obo/MOD_01466 menadione quinone derivative - site C http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_01467 menadione quinone derivative - site K http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_01468 L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide) (Cys) http://purl.obolibrary.org/obo/MOD_02073 metal or metal cluster coordinated L-selenocysteine residue A protein modification that effectively converts an L-cysteine residue to L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide) (not known as a natural, post-translational modification process). http://purl.obolibrary.org/obo/MOD_01469 L-selenocysteinyl tungsten bis(molybdopterin guanine dinucleotide) (Cys) http://purl.obolibrary.org/obo/MOD_02073 metal or metal cluster coordinated L-selenocysteine residue A protein modification that effectively converts an L-cysteine residue to L-selenocysteinyl tungsten bis(molybdopterin guanine dinucleotide) (not known as a natural, post-translational modification process). http://purl.obolibrary.org/obo/MOD_01470 (E)-dehydrobutyrine (Thr) http://purl.obolibrary.org/obo/MOD_00190 dehydrobutyrine (Thr) A protein modification that effectively converts an L-threonine residue to (E)-dehydrobutyrine. http://purl.obolibrary.org/obo/MOD_01471 (Z)-dehydrobutyrine (Thr) http://purl.obolibrary.org/obo/MOD_00190 dehydrobutyrine (Thr) A protein modification that effectively converts an L-threonine residue to (Z)-dehydrobutyrine. http://purl.obolibrary.org/obo/MOD_01472 reduced residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process A protein modification that effectively either adds neutral hydrogen atoms (proton and electron), or removes oxygen atoms from a residue with or without the addition of hydrogen atoms. http://purl.obolibrary.org/obo/MOD_01473 hydrogenated residue http://purl.obolibrary.org/obo/MOD_01472 reduced residue A protein modification that effectively adds neutral hydrogen atoms (proton and electron) to a residue. http://purl.obolibrary.org/obo/MOD_01474 O-[S-(carboxymethyl)phosphopantetheine]-L-serine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to O-[S-(carboxymethyl)phosphopantetheine]-L-serine. http://purl.obolibrary.org/obo/MOD_01475 O-[S-(carboxamidomethyl)phosphopantetheine]-L-serine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to O-[S-(carboxamidomethyl)phosphopantetheine]-L-serine. http://purl.obolibrary.org/obo/MOD_01476 2'-fluoro-L-phenylalanine http://purl.obolibrary.org/obo/MOD_01227 monofluorinated L-phenylalanine A protein modification that effectively converts an L-phenylalanine residue to an 2'-fluoro-L-fluorophenylalanine. http://purl.obolibrary.org/obo/MOD_01477 3'-fluoro-L-phenylalanine http://purl.obolibrary.org/obo/MOD_01227 monofluorinated L-phenylalanine A protein modification that effectively converts an L-phenylalanine residue to an 3'-fluoro-L-fluorophenylalanine. http://purl.obolibrary.org/obo/MOD_01478 4'-fluoro-L-phenylalanine http://purl.obolibrary.org/obo/MOD_01227 monofluorinated L-phenylalanine A protein modification that effectively converts an L-phenylalanine residue into an 4'-fluoro-L-fluorophenylalanine. http://purl.obolibrary.org/obo/MOD_01479 4'-fluoro-L-tryptophan http://purl.obolibrary.org/obo/MOD_01226 monofluorinated L-tryptophan A protein modification that effectively converts an L-tryptophan residue into an 4'-fluoro-L-tryptophan. http://purl.obolibrary.org/obo/MOD_01480 5'-fluoro-L-tryptophan http://purl.obolibrary.org/obo/MOD_01226 monofluorinated L-tryptophan A protein modification that effectively converts an L-tryptophan residue into an 5'-fluoro-L-tryptophan. http://purl.obolibrary.org/obo/MOD_01481 6'-fluoro-L-tryptophan http://purl.obolibrary.org/obo/MOD_01226 monofluorinated L-tryptophan A protein modification that effectively converts an L-tryptophan residue into an 6'-fluoro-L-tryptophan. http://purl.obolibrary.org/obo/MOD_01482 calcium containing modified residue http://purl.obolibrary.org/obo/MOD_00698 metal or metal cluster containing modified residue A protein modification that effectively substitutes a calcium atom or a cluster containing calcium for hydrogen atoms, or that coordinates a calcium ion. http://purl.obolibrary.org/obo/MOD_01483 O-formylated residue http://purl.obolibrary.org/obo/MOD_00671 O-acylated residue A protein modification that effectively replaces a residue hydroxyl group with a formyloxy group. http://purl.obolibrary.org/obo/MOD_01484 N6-(L-isoglutamyl)-L-lysine (Glu) http://purl.obolibrary.org/obo/MOD_02045 crosslinked L-glutamic acid residue A protein modification that effectively crosslinks an L-glutamic acid residue and an L-lysine residue by an isopeptide bond to form N6-(L-isoglutamyl)-L-lysine and the release of water. http://purl.obolibrary.org/obo/MOD_01485 iTRAQ4plex-114 reporter+balance reagent acylated residue http://purl.obolibrary.org/obo/MOD_01518 iTRAQ4plex reporter+balance reagent acylated residue A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01486 iTRAQ4plex-114 reporter+balance reagent acylated N-terminal http://purl.obolibrary.org/obo/MOD_01711 iTRAQ4plex reporter+balance reagent acylated N-terminal A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ4plex-114 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01487 iTRAQ4plex-114 reporter+balance reagent N6-acylated lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01488 iTRAQ4plex-114 reporter+balance reagent O4'-acylated tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01489 iTRAQ4plex-114 reporter+balance reagent N'-acylated histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01490 iTRAQ4plex-114 reporter+balance reagent O3-acylated serine http://purl.obolibrary.org/obo/MOD_02003 O3-acylated L-serine A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01491 iTRAQ4plex-114 reporter+balance reagent O3-acylated threonine http://purl.obolibrary.org/obo/MOD_02004 O3-acylated L-threonine A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01492 iTRAQ4plex-115 reporter+balance reagent acylated residue http://purl.obolibrary.org/obo/MOD_01518 iTRAQ4plex reporter+balance reagent acylated residue A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01493 iTRAQ4plex-115 reporter+balance reagent acylated N-terminal http://purl.obolibrary.org/obo/MOD_01711 iTRAQ4plex reporter+balance reagent acylated N-terminal A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ4plex-115 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01494 iTRAQ4plex-115 reporter+balance reagent N6-acylated lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01495 iTRAQ4plex-115 reporter+balance reagent O4'-acylated tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01496 iTRAQ4plex-115 reporter+balance reagent N'-acylated histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01497 iTRAQ4plex-115 reporter+balance reagent O3-acylated serine http://purl.obolibrary.org/obo/MOD_02003 O3-acylated L-serine A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01498 iTRAQ4plex-115 reporter+balance reagent O3-acylated threonine http://purl.obolibrary.org/obo/MOD_02004 O3-acylated L-threonine A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01499 iTRAQ4plex-116 reporter+balance reagent acylated residue http://purl.obolibrary.org/obo/MOD_01518 iTRAQ4plex reporter+balance reagent acylated residue A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01500 iTRAQ4plex-116 reporter+balance reagent acylated N-terminal http://purl.obolibrary.org/obo/MOD_01711 iTRAQ4plex reporter+balance reagent acylated N-terminal A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ4plex-116 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01501 iTRAQ4plex-116 reporter+balance reagent N6-acylated lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01502 iTRAQ4plex-116 reporter+balance reagent O4'-acylated tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01503 iTRAQ4plex-116 reporter+balance reagent N'-acylated histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01504 iTRAQ4plex-116 reporter+balance reagent O3-acylated serine http://purl.obolibrary.org/obo/MOD_02003 O3-acylated L-serine A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01505 iTRAQ4plex-116 reporter+balance reagent O3-acylated threonine http://purl.obolibrary.org/obo/MOD_02004 O3-acylated L-threonine A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01506 iTRAQ4plex-117, mTRAQ heavy, reporter+balance reagent acylated residue http://purl.obolibrary.org/obo/MOD_01863 mTRAQ reporter+balance reagent acylated residue A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01507 iTRAQ4plex-117, mTRAQ heavy, reporter+balance reagent acylated N-terminal http://purl.obolibrary.org/obo/MOD_01711 iTRAQ4plex reporter+balance reagent acylated N-terminal A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ4plex-117 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01508 iTRAQ4plex-117, mTRAQ heavy, reporter+balance reagent N6-acylated lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively replaces the N6-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01509 iTRAQ4plex-117, mTRAQ heavy, reporter+balance reagent O4'-acylated tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01510 iTRAQ4plex-117 reporter+balance reagent N'-acylated histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01511 iTRAQ4plex-117 reporter+balance reagent O3-acylated serine http://purl.obolibrary.org/obo/MOD_02003 O3-acylated L-serine A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01512 iTRAQ4plex-117 reporter+balance reagent O3-acylated threonine http://purl.obolibrary.org/obo/MOD_02004 O3-acylated L-threonine A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01513 modifications with monoisotopic mass differences that are nominally equal at a resolution below 0.1 Da http://purl.obolibrary.org/obo/MOD_00538 protein modification categorized by isobaric sets Modifications that have monoisotopic mass differences from their respective origins that are nominally equal (sometimes called isobaric) at a resolution below 0.1 Da. http://purl.obolibrary.org/obo/MOD_01514 modifications with monoisotopic mass differences that are nominally equal at a resolution below 0.01 Da http://purl.obolibrary.org/obo/MOD_01513 modifications with monoisotopic mass differences that are nominally equal at a resolution below 0.1 Da Modifications that have monoisotopic mass differences from their respective origins that are nominally equal (sometimes called isobaric) at a resolution below 0.01 Da. http://purl.obolibrary.org/obo/MOD_01515 modifications with monoisotopic mass differences that are nominally equal at a resolution below 0.000001 Da http://purl.obolibrary.org/obo/MOD_01514 modifications with monoisotopic mass differences that are nominally equal at a resolution below 0.01 Da Modifications that have monoisotopic mass differences from their respective origins that are nominally equal (sometimes called isobaric) at a resolution below 0.000001 Da. http://purl.obolibrary.org/obo/MOD_01516 modifications with monoisotopic mass diferences that are nominally equal at 144.099-144.106 Da. http://purl.obolibrary.org/obo/MOD_01514 modifications with monoisotopic mass differences that are nominally equal at a resolution below 0.01 Da Modifications that have monoisotopic mass differences from their respective origins of 144.099-144.106 Da. http://purl.obolibrary.org/obo/MOD_01517 modifications with monoisotopic mass differences that are nominally equal at 144.102062 Da http://purl.obolibrary.org/obo/MOD_01516 modifications with monoisotopic mass diferences that are nominally equal at 144.099-144.106 Da. Modifications that have monoisotopic mass differences from their respective origins of 144.102062 Da. http://purl.obolibrary.org/obo/MOD_01518 iTRAQ4plex reporter+balance reagent acylated residue http://purl.obolibrary.org/obo/MOD_01705 isotope tagged reagent acylated residue A protein modification that effectively replaces a hydrogen atom of a residue with one of the Applied Biosystems iTRAQ4plex reagent reporter+balance groups. http://purl.obolibrary.org/obo/MOD_01519 reporter fragment http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process A distinct molecular entity produced from a protein or a protein modification as the result of a fragmentation process. http://purl.obolibrary.org/obo/MOD_01520 modification reporter fragment http://purl.obolibrary.org/obo/MOD_01519 reporter fragment A distinct molecular entity produced as the result of a fragmentation process performed on a particular modified residue. http://purl.obolibrary.org/obo/MOD_01521 iTRAQ4plex reporter fragment http://purl.obolibrary.org/obo/MOD_01520 modification reporter fragment A protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex reagent derivatized residue. http://purl.obolibrary.org/obo/MOD_01522 iTRAQ4plex-114 reporter fragment http://purl.obolibrary.org/obo/MOD_01521 iTRAQ4plex reporter fragment The protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex 114 reagent derivatized residue. http://purl.obolibrary.org/obo/MOD_01523 iTRAQ4plex-115 reporter fragment http://purl.obolibrary.org/obo/MOD_01521 iTRAQ4plex reporter fragment The protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex 115 reagent derivatized residue. http://purl.obolibrary.org/obo/MOD_01524 iTRAQ4plex-116 reporter fragment http://purl.obolibrary.org/obo/MOD_01521 iTRAQ4plex reporter fragment The protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex 116 reagent derivatized residue. http://purl.obolibrary.org/obo/MOD_01525 iTRAQ4plex-117, mTRAQ heavy, reporter fragment http://purl.obolibrary.org/obo/MOD_01870 mTRAQ reporter fragment The protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex 117 reagent derivatized residue. http://purl.obolibrary.org/obo/MOD_01526 iTRAQ8plex reporter+balance reagent acylated residue http://purl.obolibrary.org/obo/MOD_01705 isotope tagged reagent acylated residue A protein modification that effectively replaces a hydrogen atom of a residue with one of the Applied Biosystems iTRAQ8plex reagent reporter+balance groups. http://purl.obolibrary.org/obo/MOD_01527 residue reporter fragment http://purl.obolibrary.org/obo/MOD_01519 reporter fragment A distinct molecular entity produced from a particular amino acid residue as the result of a fragmentation process. http://purl.obolibrary.org/obo/MOD_01528 iTRAQ8plex-113 reporter+balance reagent acylated residue http://purl.obolibrary.org/obo/MOD_01591 modifications with monoisotopic mass differences that are nominally equal at 304.205359 Da A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01529 iTRAQ8plex-113 reporter+balance reagent acylated N-terminal http://purl.obolibrary.org/obo/MOD_01712 iTRAQ8plex reporter+balance reagent acylated N-terminal A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-113 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01530 iTRAQ8plex-113 reporter+balance reagent N6-acylated lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01531 iTRAQ8plex-113 reporter+balance reagent O4'-acylated tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01532 iTRAQ8plex-113 reporter+balance reagent N'-acylated histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01533 iTRAQ8plex-113 reporter+balance reagent O3-acylated serine http://purl.obolibrary.org/obo/MOD_02003 O3-acylated L-serine A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01534 iTRAQ8plex-113 reporter+balance reagent O3-acylated threonine http://purl.obolibrary.org/obo/MOD_02004 O3-acylated L-threonine A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01535 iTRAQ8plex-114 reporter+balance reagent acylated residue http://purl.obolibrary.org/obo/MOD_01591 modifications with monoisotopic mass differences that are nominally equal at 304.205359 Da A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01536 iTRAQ8plex-114 reporter+balance reagent acylated N-terminal http://purl.obolibrary.org/obo/MOD_01712 iTRAQ8plex reporter+balance reagent acylated N-terminal A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-114 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01537 iTRAQ8plex-114 reporter+balance reagent N6-acylated lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01538 iTRAQ8plex-114 reporter+balance reagent O4'-acylated tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01539 iTRAQ8plex-114 reporter+balance reagent N'-acylated histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01540 iTRAQ8plex-114 reporter+balance reagent O3-acylated serine http://purl.obolibrary.org/obo/MOD_02003 O3-acylated L-serine A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01541 iTRAQ8plex-114 reporter+balance reagent O3-acylated threonine http://purl.obolibrary.org/obo/MOD_02004 O3-acylated L-threonine A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01542 iTRAQ8plex-115 reporter+balance reagent acylated residue http://purl.obolibrary.org/obo/MOD_01584 modifications with monoisotopic mass differences that are nominally equal at 304.199039 Da A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01543 iTRAQ8plex-115 reporter+balance reagent acylated N-terminal http://purl.obolibrary.org/obo/MOD_01712 iTRAQ8plex reporter+balance reagent acylated N-terminal A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-115 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01544 iTRAQ8plex-115 reporter+balance reagent N6-acylated lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01545 iTRAQ8plex-115 reporter+balance reagent O4'-acylated tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01546 iTRAQ8plex-115 reporter+balance reagent N'-derivatized histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01547 iTRAQ8plex-115 reporter+balance reagent O3-acylated serine http://purl.obolibrary.org/obo/MOD_02003 O3-acylated L-serine A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01548 iTRAQ8plex-115 reporter+balance reagent O3-acylated threonine http://purl.obolibrary.org/obo/MOD_02004 O3-acylated L-threonine A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01549 iTRAQ8plex-116 reporter+balance reagent acylated residue http://purl.obolibrary.org/obo/MOD_01591 modifications with monoisotopic mass differences that are nominally equal at 304.205359 Da A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01550 iTRAQ8plex-116 reporter+balance reagent acylated N-terminal http://purl.obolibrary.org/obo/MOD_01712 iTRAQ8plex reporter+balance reagent acylated N-terminal A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-116 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01551 iTRAQ8plex-116 reporter+balance reagent N6-acylated lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01552 iTRAQ8plex-116 reporter+balance reagent O4'-acylated tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01553 iTRAQ8plex-116 reporter+balance reagent N'-acylated histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01554 iTRAQ8plex-116 reporter+balance reagent O3-acylated serine http://purl.obolibrary.org/obo/MOD_02003 O3-acylated L-serine A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01555 iTRAQ8plex-116 reporter+balance reagent O3-acylated threonine http://purl.obolibrary.org/obo/MOD_02004 O3-acylated L-threonine A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01556 iTRAQ8plex-117 reporter+balance reagent acylated residue http://purl.obolibrary.org/obo/MOD_01591 modifications with monoisotopic mass differences that are nominally equal at 304.205359 Da A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01557 iTRAQ8plex-117 reporter+balance reagent acylated N-terminal http://purl.obolibrary.org/obo/MOD_01712 iTRAQ8plex reporter+balance reagent acylated N-terminal A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-117 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01558 iTRAQ8plex-117 reporter+balance reagent N6-acylated lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01559 iTRAQ8plex-117 reporter+balance reagent O4'-acylated tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01560 iTRAQ8plex-117 reporter+balance reagent N'-acylated histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01561 iTRAQ8plex-117 reporter+balance reagent O3-acylated serine http://purl.obolibrary.org/obo/MOD_02003 O3-acylated L-serine A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01562 iTRAQ8plex-117 reporter+balance reagent O3-acylated threonine http://purl.obolibrary.org/obo/MOD_02004 O3-acylated L-threonine A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01563 iTRAQ8plex-118 reporter+balance reagent acylated residue http://purl.obolibrary.org/obo/MOD_01584 modifications with monoisotopic mass differences that are nominally equal at 304.199039 Da A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01564 iTRAQ8plex-118 reporter+balance reagent acylated N-terminal http://purl.obolibrary.org/obo/MOD_01712 iTRAQ8plex reporter+balance reagent acylated N-terminal A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-118 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01565 iTRAQ8plex-118 reporter+balance reagent N6-acylated lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01566 iTRAQ8plex-118 reporter+balance reagent O4'-acylated tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01567 iTRAQ8plex-118 reporter+balance reagent N'-acylated histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01568 iTRAQ8plex-118 reporter+balance reagent O3-acylated serine http://purl.obolibrary.org/obo/MOD_02003 O3-acylated L-serine A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01569 iTRAQ8plex-118 reporter+balance reagent O3-acylated threonine http://purl.obolibrary.org/obo/MOD_02004 O3-acylated L-threonine A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01570 iTRAQ8plex-119 reporter+balance reagent acylated residue http://purl.obolibrary.org/obo/MOD_01584 modifications with monoisotopic mass differences that are nominally equal at 304.199039 Da A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01571 iTRAQ8plex-119 reporter+balance reagent acylated N-terminal http://purl.obolibrary.org/obo/MOD_01712 iTRAQ8plex reporter+balance reagent acylated N-terminal A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-119 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01572 iTRAQ8plex-119 reporter+balance reagent N6-acylated lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01573 iTRAQ8plex-119 reporter+balance reagent O4'-acylated tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01574 iTRAQ8plex-119 reporter+balance reagent N'-acylated histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01575 iTRAQ8plex-119 reporter+balance reagent O3-acylated serine http://purl.obolibrary.org/obo/MOD_02003 O3-acylated L-serine A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01576 iTRAQ8plex-119 reporter+balance reagent O3-acylated threonine http://purl.obolibrary.org/obo/MOD_02004 O3-acylated L-threonine A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01577 iTRAQ8plex-121 reporter+balance reagent acylated residue http://purl.obolibrary.org/obo/MOD_01584 modifications with monoisotopic mass differences that are nominally equal at 304.199039 Da A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01578 iTRAQ8plex-121 reporter+balance reagent acylated N-terminal http://purl.obolibrary.org/obo/MOD_01712 iTRAQ8plex reporter+balance reagent acylated N-terminal A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-121 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01579 iTRAQ8plex-121 reporter+balance reagent N6-acylated lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01580 iTRAQ8plex-121 reporter+balance reagent O4'-acylated tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01581 iTRAQ8plex-121 reporter+balance reagent N'-acylated histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01582 iTRAQ8plex-121 reporter+balance reagent O3-acylated serine http://purl.obolibrary.org/obo/MOD_02003 O3-acylated L-serine A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01583 iTRAQ8plex-121 reporter+balance reagent O3-acylated threonine http://purl.obolibrary.org/obo/MOD_02004 O3-acylated L-threonine A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01584 modifications with monoisotopic mass differences that are nominally equal at 304.199039 Da http://purl.obolibrary.org/obo/MOD_01592 modifications with monoisotopic mass differences that are nominally equal at 304.199-304.206 Da Modifications that have monoisotopic mass differences from their respective origins of 304.199039 Da. http://purl.obolibrary.org/obo/MOD_01585 O-glycyl-L-serine http://purl.obolibrary.org/obo/MOD_02055 crosslinked L-serine residue A protein modification that effectively crosslinks an L-serine residue and a glycine residue by an ester bond to form O-glycyl-L-serine. http://purl.obolibrary.org/obo/MOD_01586 O-glycyl-L-threonine http://purl.obolibrary.org/obo/MOD_02047 crosslinked glycine residue A protein modification that effectively crosslinks an L-threonine residue and a glycine residue by an ester bond to form O-glycyl-L-threonine. http://purl.obolibrary.org/obo/MOD_01587 O-(2-aminoethylphosphoryl)-L-serine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to O-(2-aminoethylphosphoryl)-L-serine. http://purl.obolibrary.org/obo/MOD_01588 O-cholinephosphoryl-L-serine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to O-cholinephosphoryl-L-serine. http://purl.obolibrary.org/obo/MOD_01589 O-(2,4-diacetamido-2,4-dideoxyglucosyl)-L-serine http://purl.obolibrary.org/obo/MOD_00002 O-glycosyl-L-serine A protein modification that effectively converts an L-serine residue to O-(2,4-diacetamido-2,4-dideoxyglucosyl)-L-serine. http://purl.obolibrary.org/obo/MOD_01590 3'-farnesyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan http://purl.obolibrary.org/obo/MOD_00601 cyclized residue A protein modification that effectively converts an L-tryptophan residue to 3'-farnesyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan. http://purl.obolibrary.org/obo/MOD_01591 modifications with monoisotopic mass differences that are nominally equal at 304.205359 Da http://purl.obolibrary.org/obo/MOD_01592 modifications with monoisotopic mass differences that are nominally equal at 304.199-304.206 Da Modifications that have monoisotopic mass differences from their respective origins of 304.205359 Da. http://purl.obolibrary.org/obo/MOD_01592 modifications with monoisotopic mass differences that are nominally equal at 304.199-304.206 Da http://purl.obolibrary.org/obo/MOD_01514 modifications with monoisotopic mass differences that are nominally equal at a resolution below 0.01 Da Modifications that have monoisotopic mass differences from their respective origins of 304.199-304.206 Da. http://purl.obolibrary.org/obo/MOD_01593 iTRAQ8plex reporter fragment http://purl.obolibrary.org/obo/MOD_01520 modification reporter fragment A protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex reagent derivatized residue. http://purl.obolibrary.org/obo/MOD_01594 iTRAQ8plex-113 reporter fragment http://purl.obolibrary.org/obo/MOD_01593 iTRAQ8plex reporter fragment The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-113 reagent derivatized residue. http://purl.obolibrary.org/obo/MOD_01595 iTRAQ8plex-114 reporter fragment http://purl.obolibrary.org/obo/MOD_01593 iTRAQ8plex reporter fragment The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-114 reagent derivatized residue. http://purl.obolibrary.org/obo/MOD_01596 iTRAQ8plex-115 reporter fragment http://purl.obolibrary.org/obo/MOD_01593 iTRAQ8plex reporter fragment The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-115 reagent derivatized residue. http://purl.obolibrary.org/obo/MOD_01597 iTRAQ8plex-116 reporter fragment http://purl.obolibrary.org/obo/MOD_01593 iTRAQ8plex reporter fragment The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-116 reagent derivatized residue. http://purl.obolibrary.org/obo/MOD_01598 iTRAQ8plex-117 reporter fragment http://purl.obolibrary.org/obo/MOD_01593 iTRAQ8plex reporter fragment The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-117 reagent derivatized residue. http://purl.obolibrary.org/obo/MOD_01599 iTRAQ8plex-118 reporter fragment http://purl.obolibrary.org/obo/MOD_01593 iTRAQ8plex reporter fragment The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-118 reagent derivatized residue. http://purl.obolibrary.org/obo/MOD_01600 iTRAQ8plex-119 reporter fragment http://purl.obolibrary.org/obo/MOD_01593 iTRAQ8plex reporter fragment The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-119 reagent derivatized residue. http://purl.obolibrary.org/obo/MOD_01601 iTRAQ8plex-121 reporter fragment http://purl.obolibrary.org/obo/MOD_01593 iTRAQ8plex reporter fragment The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-121 reagent derivatized residue. http://purl.obolibrary.org/obo/MOD_01602 S-(L-lysyl)-L-methionine sulfilimine http://purl.obolibrary.org/obo/MOD_02052 crosslinked L-methionine residue A protein modification that effectively converts an L-lysine residue, and an L-methionine residue to S-(L-lysyl)-L-methionine sulfilimine. http://purl.obolibrary.org/obo/MOD_01603 2x(15)N labeled L-lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively converts an L-lysine residue to 2x(15)N labeled L-lysine. http://purl.obolibrary.org/obo/MOD_01604 4x(15)N labeled L-arginine http://purl.obolibrary.org/obo/MOD_00902 modified L-arginine residue A protein modification that effectively converts an L-arginine residue to 4x(15)N labeled L-arginine. http://purl.obolibrary.org/obo/MOD_01605 5-glutamyl 2-aminoadipic acid http://purl.obolibrary.org/obo/MOD_00906 modified L-glutamic acid residue A protein modification that effectively converts an L-glutamic acid residue to 5-glutamyl 2-aminoadipic acid. http://purl.obolibrary.org/obo/MOD_01606 5-glutamyl 2-aminoadipic 6-phosphoric anhydride http://purl.obolibrary.org/obo/MOD_00906 modified L-glutamic acid residue A protein modification that effectively converts an L-glutamic acid residue to 5-glutamyl 2-aminoadipic 6-phosphoric anhydride. http://purl.obolibrary.org/obo/MOD_01607 5-glutamyl allysine http://purl.obolibrary.org/obo/MOD_00906 modified L-glutamic acid residue A protein modification that effectively converts an L-glutamic acid residue to 5-glutamyl allysine. http://purl.obolibrary.org/obo/MOD_01608 N2-(L-isoglutamyl)-L-lysine http://purl.obolibrary.org/obo/MOD_00906 modified L-glutamic acid residue A protein modification that effectively converts an L-glutamic acid residue to N2-(L-isoglutamyl)-L-lysine. This is not an isopeptide cross-link. http://purl.obolibrary.org/obo/MOD_01609 7'-hydroxy-2'-alpha-mannosyl-L-tryptophan http://purl.obolibrary.org/obo/MOD_00918 modified L-tryptophan residue A protein modification that effectively converts an L-tryptophan residue to 7'-hydroxy-2'-alpha-mannosyl-L-tryptophan. http://purl.obolibrary.org/obo/MOD_01610 L-threonine methyl ester http://purl.obolibrary.org/obo/MOD_01803 O-methylated threonine A protein modification that effectively converts an L-threonine residue to L-threonine methyl ester. http://purl.obolibrary.org/obo/MOD_01611 6-(S-L-cysteinyl)-8alpha-(-3'-L-histidino)-FMN http://purl.obolibrary.org/obo/MOD_02048 crosslinked L-histidine residue A protein modification that crosslinks a cysteine and a histidine residue by forming the adduct 6-(S-L-cysteinyl)-8alpha-(-3'-L-histidino)-FMN. http://purl.obolibrary.org/obo/MOD_01612 3'-iodo-L-tyrosine http://purl.obolibrary.org/obo/MOD_01228 monoiodinated tyrosine A protein modification that effectively converts an L-tyrosine residue to 3'-iodo-L-tyrosine. http://purl.obolibrary.org/obo/MOD_01613 3',5'-diiodo-L-tyrosine http://purl.obolibrary.org/obo/MOD_01140 diiodinated tyrosine A protein modification that effectively converts an L-tyrosine residue to 3',5'-diiodo-L-tyrosine. http://purl.obolibrary.org/obo/MOD_01614 glycyl phospho-5'-adenosine http://purl.obolibrary.org/obo/MOD_00908 modified glycine residue A protein modification that effectively converts a glycine residue to glycyl phospho-5'-adenosine. http://purl.obolibrary.org/obo/MOD_01615 glycyl cysteine dithioester http://purl.obolibrary.org/obo/MOD_02047 crosslinked glycine residue A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue by a dithioester bond to form glycyl cysteine dithioester. http://purl.obolibrary.org/obo/MOD_01616 trithiocystine http://purl.obolibrary.org/obo/MOD_01620 polysulfide crosslinked residues A protein modification that effectively cross-links two L-cysteine residues and adds three sulfur atoms to form trithiocystine. http://purl.obolibrary.org/obo/MOD_01617 O-(6-phosphomannosyl)-L-threonine http://purl.obolibrary.org/obo/MOD_01804 glycosylphosphorylated residue A protein modification that effectively converts an L-threonine residue to O-(6-phosphomannosyl)-L-threonine. http://purl.obolibrary.org/obo/MOD_01618 L-alanyl-L-isoaspartyl cyclopeptide http://purl.obolibrary.org/obo/MOD_02042 crosslinked L-asparagine residue A protein modification that effectively converts an L-alaine residue and an L-asparagine residue to L-alanyl-L-isoaspartyl cyclopeptide. http://purl.obolibrary.org/obo/MOD_01619 multisulfide crosslinked residues http://purl.obolibrary.org/obo/MOD_02044 crosslinked L-cysteine residue A protein modification that crosslinks two cysteine residues by formation of a chain of two or more bonded sulfur atoms. http://purl.obolibrary.org/obo/MOD_01620 polysulfide crosslinked residues http://purl.obolibrary.org/obo/MOD_01619 multisulfide crosslinked residues A protein modification that crosslinks two cysteine residues by formation of a chain of three or more bonded sulfur atoms. http://purl.obolibrary.org/obo/MOD_01621 flavin crosslinked residues http://purl.obolibrary.org/obo/MOD_00033 crosslinked residues A protein modification that crosslinks two or more amino acid residues by forming an adduct with a compound containing a flavin group. http://purl.obolibrary.org/obo/MOD_01622 monohydroxylated tryptophan http://purl.obolibrary.org/obo/MOD_00918 modified L-tryptophan residue A protein modification that effectively converts an L-tryptophan residue to one of several monohydroxylated tryptophan residues, including 3-hydroxy-L-tryptophan and 7'-hydroxy-L-tryptophan. http://purl.obolibrary.org/obo/MOD_01623 1-thioglycine (C-terminal) http://purl.obolibrary.org/obo/MOD_01625 1-thioglycine A protein modification that effectively converts a glycine residue to a C-terminal 1-thioglycine. http://purl.obolibrary.org/obo/MOD_01624 (2-aminosuccinimidyl)acetic acid (Asn) http://purl.obolibrary.org/obo/MOD_02042 crosslinked L-asparagine residue A protein modification that crosslinks an asparagine and the following glycine residue with the formation of (2-aminosuccinimidyl)acetic acid and the release of ammonia. http://purl.obolibrary.org/obo/MOD_01625 1-thioglycine http://purl.obolibrary.org/obo/MOD_00908 modified glycine residue A protein modification that effectively converts a glycine residue to 1-thioglycine. http://purl.obolibrary.org/obo/MOD_01626 L-cystine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that forms L-cystine by forming a disulfide bond that either cross-links two peptidyl L-cysteine residues, or modifies a peptidyl cysteine with a free cysteine. http://purl.obolibrary.org/obo/MOD_01627 L-cysteinyl-L-selenocysteine http://purl.obolibrary.org/obo/MOD_02044 crosslinked L-cysteine residue A protein modification that forms L-cysteinyl-L-selenocysteine either by the natural process of cross-linking an L-cysteine residue and an L-selenocysteine residue, or by the hypothetical process of substituting a selenium for a sulfur atom in cystine. http://purl.obolibrary.org/obo/MOD_01628 (2-aminosuccinimidyl)acetic acid http://purl.obolibrary.org/obo/MOD_02047 crosslinked glycine residue A protein modification that forms (2-aminosuccinimidyl)acetic acid by crosslinking either an aspartic acid residue or an asparagine residue with the following glycine residue. http://purl.obolibrary.org/obo/MOD_01629 cyclo[(prolylserin)-O-yl] cysteinate http://purl.obolibrary.org/obo/MOD_02044 crosslinked L-cysteine residue A protein modification that forms cyclo[(prolylserin)-O-yl] cysteinate by the natural process of cross-linking an L-cysteine residue an L-proline residue, and an L-serine residue, or by effectively modifying a cysteine residue. http://purl.obolibrary.org/obo/MOD_01630 N6-(L-isoglutamyl)-L-lysine http://purl.obolibrary.org/obo/MOD_02051 crosslinked L-lysine residue A protein modification that effectively crosslinks either an L-glutamine residue or an L-glutamic acid residue with an L-lysine residue by an isopeptide bond to form N6-(L-isoglutamyl)-L-lysine . http://purl.obolibrary.org/obo/MOD_01631 L-alanine removal http://purl.obolibrary.org/obo/MOD_00901 modified L-alanine residue A protein modification that effectively removes or replaces an L-alanine. http://purl.obolibrary.org/obo/MOD_01632 L-arginine removal http://purl.obolibrary.org/obo/MOD_00902 modified L-arginine residue A protein modification that effectively removes or replaces an L-arginine. http://purl.obolibrary.org/obo/MOD_01633 L-asparagine removal http://purl.obolibrary.org/obo/MOD_00903 modified L-asparagine residue A protein modification that effectively removes or replaces an L-asparagine. http://purl.obolibrary.org/obo/MOD_01634 L-aspartic acid removal http://purl.obolibrary.org/obo/MOD_00904 modified L-aspartic acid residue A protein modification that effectively removes or replaces an L-aspartic acid. http://purl.obolibrary.org/obo/MOD_01635 L-cysteine removal http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively removes or replaces an L-cysteine. http://purl.obolibrary.org/obo/MOD_01636 L-glutamic acid removal http://purl.obolibrary.org/obo/MOD_00906 modified L-glutamic acid residue A protein modification that effectively removes or replaces an L-glutamic acid. http://purl.obolibrary.org/obo/MOD_01637 L-glutamine removal http://purl.obolibrary.org/obo/MOD_00907 modified L-glutamine residue A protein modification that effectively removes or replaces an L-glutamine. http://purl.obolibrary.org/obo/MOD_01638 glycine removal http://purl.obolibrary.org/obo/MOD_00908 modified glycine residue A protein modification that effectively removes or replaces a glycine. http://purl.obolibrary.org/obo/MOD_01639 L-histidine removal http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively removes or replaces an L-histidine. http://purl.obolibrary.org/obo/MOD_01640 L-isoleucine removal http://purl.obolibrary.org/obo/MOD_00910 modified L-isoleucine residue A protein modification that effectively removes or replaces an L-isoleucine. http://purl.obolibrary.org/obo/MOD_01641 L-leucine removal http://purl.obolibrary.org/obo/MOD_00911 modified L-leucine residue A protein modification that effectively removes or replaces an L-leucine. http://purl.obolibrary.org/obo/MOD_01642 L-lysine removal http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively removes or replaces an L-lysine. http://purl.obolibrary.org/obo/MOD_01643 L-methionine removal http://purl.obolibrary.org/obo/MOD_00913 modified L-methionine residue A protein modification that effectively removes or replaces an L-methionine. http://purl.obolibrary.org/obo/MOD_01644 L-phenylalanine removal http://purl.obolibrary.org/obo/MOD_00914 modified L-phenylalanine residue A protein modification that effectively removes or replaces an L-phenylalanine. http://purl.obolibrary.org/obo/MOD_01645 L-proline removal http://purl.obolibrary.org/obo/MOD_00915 modified L-proline residue A protein modification that effectively removes or replaces an L-proline. http://purl.obolibrary.org/obo/MOD_01646 L-serine removal http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively removes or replaces an L-serine. http://purl.obolibrary.org/obo/MOD_01647 L-threonine removal http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue A protein modification that effectively removes or replaces an L-threonine. http://purl.obolibrary.org/obo/MOD_01648 L-tryptophan removal http://purl.obolibrary.org/obo/MOD_00918 modified L-tryptophan residue A protein modification that effectively removes or replaces an L-tryptophan. http://purl.obolibrary.org/obo/MOD_01649 L-tyrosine removal http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively removes or replaces an L-tyrosine. http://purl.obolibrary.org/obo/MOD_01650 L-valine removal http://purl.obolibrary.org/obo/MOD_00920 modified L-valine residue A protein modification that effectively removes or replaces an L-valine. http://purl.obolibrary.org/obo/MOD_01651 natural, standard, encoded residue removal http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process A protein modification that effectively removes a natural, standard, encoded residue. http://purl.obolibrary.org/obo/MOD_01652 sulfonyl halide reagent derivatized residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue A protein modification that is produced by formation of an adduct with a sulfonyl halide compound used as a reagent. http://purl.obolibrary.org/obo/MOD_01653 dansyl chloride derivatized residue http://purl.obolibrary.org/obo/MOD_01652 sulfonyl halide reagent derivatized residue A protein modification that is produced by formation of an adduct with 5-dimethylaminonaphthalene-1-sulfonyl chloride, dansyl chloride. http://purl.obolibrary.org/obo/MOD_01654 N6-Dansyl derivatized lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that is produced by reaction with 5-dimethylaminonaphthalene-1-sulfonyl chloride, dansyl chloride, to form N6-Dansyl-lysine. http://purl.obolibrary.org/obo/MOD_01655 alpha-amino-Dansyl derivatized residue http://purl.obolibrary.org/obo/MOD_01653 dansyl chloride derivatized residue A protein modification that is produced by reaction with 5-dimethylaminonaphthalene-1-sulfonyl chloride, dansyl chloride, to form an alpha-amino-Dansyl-derivatized residue. http://purl.obolibrary.org/obo/MOD_01656 Dabsyl chloride derivatized residue http://purl.obolibrary.org/obo/MOD_01652 sulfonyl halide reagent derivatized residue A protein modification that is produced by formation of an adduct with 4-(4-dimethylaminophenylazo)benzenesulfonyl chloride, Dabsyl chloride. http://purl.obolibrary.org/obo/MOD_01657 N6-Dabsyl derivatized lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that is produced by reaction with 4-(4-dimethylaminophenylazo)benzenesulfonyl chloride, dabsyl chloride, to form N6-Dabsyl-lysine. http://purl.obolibrary.org/obo/MOD_01658 alpha-amino-Dabsyl derivatized residue http://purl.obolibrary.org/obo/MOD_01656 Dabsyl chloride derivatized residue A protein modification that is produced by reaction with 4-(4-dimethylaminophenylazo)benzenesulfonyl chloride, dabsyl chloride, to form an alpha-amino-Dabsyl-derivatized residue. http://purl.obolibrary.org/obo/MOD_01659 Uniblue A derivatized residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue A protein modification that is produced by formation of an adduct with 1-amino-4-{[3-(ethenylsulfonyl)phenyl]amino}-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate, Uniblue A. http://purl.obolibrary.org/obo/MOD_01660 Uniblue A derivatized cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that is produced by reaction with 1-amino-4-{[3-(ethenylsulfonyl)phenyl]amino}-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate, Uniblue A, to form Uniblue A cysteine adduct. http://purl.obolibrary.org/obo/MOD_01661 pyruvic acid (Tyr) http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively converts an L-tyrosine residue to pyruvic acid. http://purl.obolibrary.org/obo/MOD_01662 N5-(ADP-ribosyl)-L-glutamine http://purl.obolibrary.org/obo/MOD_00907 modified L-glutamine residue A protein modification that effectively converts an L-glutamine residue to N5-(ADP-ribosyl)-L-glutamine. http://purl.obolibrary.org/obo/MOD_01663 O-(ADP-ribosyl)-L-threonine http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue A protein modification that effectively converts an L-threonine residue to O-(ADP-ribosyl)-L-threonine. http://purl.obolibrary.org/obo/MOD_01664 7'-hydroxy-L-tryptophan http://purl.obolibrary.org/obo/MOD_01622 monohydroxylated tryptophan A protein modification that effectively converts an L-tryptophan residue to a 7'-hydroxy-L-tryptophan. http://purl.obolibrary.org/obo/MOD_01665 N-(DNA-1',2'-dideoxyribos-1'-ylidene)-L-valine http://purl.obolibrary.org/obo/MOD_00920 modified L-valine residue A protein modification that effectively crosslinks an N-terminal L-valine residue and a strand of DNA at the C-1 of a ribose, freeing the nucleotide base and forming N-(DNA-1',2'-dideoxyribos-1'-ylidene)-L-valine. http://purl.obolibrary.org/obo/MOD_01666 epicocconone derivatized residue http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue A protein modification that is produced by formation of an adduct with epicocconone. http://purl.obolibrary.org/obo/MOD_01667 N6-epicoccononyl lysine adduct http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that is produced by formation of an adduct with epicocconone. http://purl.obolibrary.org/obo/MOD_01668 O4-(8alpha-FAD)-L-aspartate http://purl.obolibrary.org/obo/MOD_00904 modified L-aspartic acid residue A protein modification that effectively converts an L-aspartic acid residue to O4-(8alpha-FAD)-L-aspartate. http://purl.obolibrary.org/obo/MOD_01669 trimethyl-L-arginine http://purl.obolibrary.org/obo/MOD_00658 methylated arginine A protein modification that effectively converts an L-arginine residue to N(omega),N(omega),N'(omega)-trimethyl-L-arginine. http://purl.obolibrary.org/obo/MOD_01670 N6-chloro-L-lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively converts an L-lysine residue to N6-methyl-L-lysine. http://purl.obolibrary.org/obo/MOD_01671 O-(L-isoaspartyl)-L-threonine (active site intermediate) http://purl.obolibrary.org/obo/MOD_01978 O-(L-isoaspartyl)-L-threonine A protein modification that effectively converts an L-threonine residue to O-(L-isoaspartyl)-L-threonine, using free L-asparagine and releasing ammonia. http://purl.obolibrary.org/obo/MOD_01672 halogenated lysine http://purl.obolibrary.org/obo/MOD_00694 halogen containing residue A protein modification that effectively substitutes a hydrogen atom of an L-lysine residue with a halogen atom. http://purl.obolibrary.org/obo/MOD_01673 N-acetylaminohexosylated residue http://purl.obolibrary.org/obo/MOD_00436 N-acetylhexosaminylated residue A protein modification that effectively replaces a hydrogen atom with an N-acetylaminohexose group through a glycosidic bond. http://purl.obolibrary.org/obo/MOD_01674 N4-(N-acetylamino)hexosyl-L-asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine A protein modification that effectively converts an L-asparagine residue to N4-(N-acetaminohexosyl)-L-asparagine. http://purl.obolibrary.org/obo/MOD_01675 O-(N-acetylamino)hexosyl-L-serine http://purl.obolibrary.org/obo/MOD_01673 N-acetylaminohexosylated residue A protein modification that effectively converts an L-serine residue to O3-(N-acetylaminohexosyl)-L-serine. http://purl.obolibrary.org/obo/MOD_01676 O-(N-acetylamino)hexosyl-L-threonine http://purl.obolibrary.org/obo/MOD_01673 N-acetylaminohexosylated residue A protein modification that effectively converts an L-threonine residue to O3-(N-acetylaminohexosyl)-L-threonine. http://purl.obolibrary.org/obo/MOD_01677 O4-(N-acetylamino)hexosyl-L-hydroxyproline http://purl.obolibrary.org/obo/MOD_00915 modified L-proline residue A protein modification that effectively converts an L-proline residue to O4-(N-acetylamino)hexosyl-L-hydroxyproline. http://purl.obolibrary.org/obo/MOD_01678 N6-carbamoyl-L-lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively coverts L-lysine to N6-carbamoyl-L-lysine. http://purl.obolibrary.org/obo/MOD_01679 alpha-aminocarbamoylated residue http://purl.obolibrary.org/obo/MOD_00398 carbamoylated residue A protein modification that effectively replaces a residue alpha amino or imino hydrogen with a carbamoyl group. http://purl.obolibrary.org/obo/MOD_01680 alpha-amino monomethylated residue http://purl.obolibrary.org/obo/MOD_00599 monomethylated residue A protein modification that effectively replaces one residue alpha amino or imino hydrogen with one methyl group. http://purl.obolibrary.org/obo/MOD_01681 monomethylated L-aspartic acid http://purl.obolibrary.org/obo/MOD_00599 monomethylated residue A protein modification that effectively replaces one hydrogen atom of an L-aspartic acid residue with one methyl group. http://purl.obolibrary.org/obo/MOD_01682 monomethylated L-cysteine http://purl.obolibrary.org/obo/MOD_00599 monomethylated residue A protein modification that effectively replaces one hydrogen atom of an L-cysteine residue with one methyl group. http://purl.obolibrary.org/obo/MOD_01684 palmitoylated-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to a palmitoylated-L-cysteine, such as N-palmitoyl-L-cysteine or S-palmitoyl-L-cysteine. http://purl.obolibrary.org/obo/MOD_01685 alpha-amino palmitoylated residue http://purl.obolibrary.org/obo/MOD_01696 alpha-amino acylated residue A protein modification that effectively replaces a residue alpha-amino group with a alpha-palmitoylamino group. http://purl.obolibrary.org/obo/MOD_01686 alpha-amino dimethylated residue http://purl.obolibrary.org/obo/MOD_01460 alpha-amino methylated residue A protein modification that effectively replaces two alpha amino hydrogen atoms with two methyl group. http://purl.obolibrary.org/obo/MOD_01687 alpha-amino trimethylated residue http://purl.obolibrary.org/obo/MOD_01460 alpha-amino methylated residue A protein modification that effectively replaces an alpha-aminium group with a trimethylaminium group. http://purl.obolibrary.org/obo/MOD_01688 3-hydroxy-L-asparagine http://purl.obolibrary.org/obo/MOD_00903 modified L-asparagine residue A protein modification that effectively converts an L-asparagine residue to one of the diastereomeric 3-hydroxy-L-asparagine residues. http://purl.obolibrary.org/obo/MOD_01689 alpha-carboxyl methylated residue http://purl.obolibrary.org/obo/MOD_00393 O-methylated residue A protein modification that effectively converts a carboxyl-terminal residue to an alpha-carboxyl (1-carboxyl) methyl ester. http://purl.obolibrary.org/obo/MOD_01690 N-[(12R)-12-hydroxymyristoyl]-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to N-[(12R)-12-hydroxymyristoyl]-L-cysteine. http://purl.obolibrary.org/obo/MOD_01691 N-(12-ketomyristoyl)-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to N-(12-ketomyristoyl)-L-cysteine. http://purl.obolibrary.org/obo/MOD_01692 glutamyl semialdehyde (Glu) http://purl.obolibrary.org/obo/MOD_00906 modified L-glutamic acid residue A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl semialdehyde. http://purl.obolibrary.org/obo/MOD_01693 alpha-amino pyridylacetylated residue http://purl.obolibrary.org/obo/MOD_01696 alpha-amino acylated residue A protein modification that effectively replaces a residue alpha amino or imino hydrogen with a (pyrid-3-yl)acetyl group. http://purl.obolibrary.org/obo/MOD_01694 S-(coelenterazin-3a-yl)-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively results from forming an adduct between an L-cysteine residue and the bioluminescent compound didehydrocoelenterazine to form S-(coelenterazin-3a-yl)-L-cysteine. http://purl.obolibrary.org/obo/MOD_01695 alpha-amino 3-(carboxamidomethylthio)propanoylated residue http://purl.obolibrary.org/obo/MOD_01696 alpha-amino acylated residue A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an 3-(carboxamidomethylthio)propanoyl group. http://purl.obolibrary.org/obo/MOD_01696 alpha-amino acylated residue http://purl.obolibrary.org/obo/MOD_00670 N-acylated residue A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an acyl group. http://purl.obolibrary.org/obo/MOD_01697 alpha-amino 4-(2-aminoethyl)benzenesulfonylated residue http://purl.obolibrary.org/obo/MOD_00596 4-(2-aminoethyl)benzenesulfonyl fluoride derivatized residue A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an 4-(2-aminoethyl)benzenesulfonyl group. http://purl.obolibrary.org/obo/MOD_01698 alpha-amino trimethylated protonated-residue http://purl.obolibrary.org/obo/MOD_01460 alpha-amino methylated residue A protein modification that effectively replaces an amino group with a trimethylaminium group. http://purl.obolibrary.org/obo/MOD_01699 protonated residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process A protein modification that effectively adds a hydrogen cation, a proton, forming a cationic residue. http://purl.obolibrary.org/obo/MOD_01700 alpha-amino protonated residue http://purl.obolibrary.org/obo/MOD_01699 protonated residue A protein modification that effectively adds a proton to a residue alpha-amnino or alpha-imino group forming an alpha-aminium or alpha-iminium group, respectively. http://purl.obolibrary.org/obo/MOD_01701 deprotonated residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process A protein modification that effectively removes a hydrogen cation, a proton, forming an anionic residue. http://purl.obolibrary.org/obo/MOD_01702 alpha-carboxyl deprotonated residue http://purl.obolibrary.org/obo/MOD_01701 deprotonated residue A protein modification that effectively removes a proton from a residue 1-carboxyl group (referred to as the alpha-carboxyl), forming a carboxylate anion. http://purl.obolibrary.org/obo/MOD_01703 dehydrobutyrine http://purl.obolibrary.org/obo/MOD_00859 modified residue that can arise from different natural residues A protein modification that effectively converts a source amino acid residue to dehydrobutyrine. http://purl.obolibrary.org/obo/MOD_01704 dehydrobutyrine (Met) http://purl.obolibrary.org/obo/MOD_00913 modified L-methionine residue A protein modification that effectively converts an L-methionine residue to dehydrobutyrine, by neutral loss of methyl sulfide. http://purl.obolibrary.org/obo/MOD_01705 isotope tagged reagent acylated residue http://purl.obolibrary.org/obo/MOD_00649 acylated residue A protein modification that effectively replaces a residue hydrogen with an isotope tagged reagent acyl group. http://purl.obolibrary.org/obo/MOD_01706 isotope tagged reagent N-acylated residue http://purl.obolibrary.org/obo/MOD_00670 N-acylated residue A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an isotope tagged reagent acyl group. http://purl.obolibrary.org/obo/MOD_01707 isotope tagged reagent O-acylated residue http://purl.obolibrary.org/obo/MOD_00671 O-acylated residue A protein modification that effectively replaces a residue hydroxyl group with an isotope tagged reagent acyloxy group. http://purl.obolibrary.org/obo/MOD_01708 isotope tagged reagent alpha-amino acylated residue http://purl.obolibrary.org/obo/MOD_01706 isotope tagged reagent N-acylated residue A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an isotope tagged reagent acyl group. http://purl.obolibrary.org/obo/MOD_01709 iTRAQ4plex reporter+balance reagent N-acylated residue http://purl.obolibrary.org/obo/MOD_01706 isotope tagged reagent N-acylated residue A protein modification that effectively replaces a residue amino- or imino-hydrogen with one of the Applied Biosystems iTRAQ4plex reagent reporter+balance groups. http://purl.obolibrary.org/obo/MOD_01710 iTRAQ8plex reporter+balance reagent N-acylated residue http://purl.obolibrary.org/obo/MOD_01706 isotope tagged reagent N-acylated residue A protein modification that effectively replaces a residue amino- or imino-hydrogen with one of the Applied Biosystems iTRAQ8plex reagent reporter+balance groups. http://purl.obolibrary.org/obo/MOD_01711 iTRAQ4plex reporter+balance reagent acylated N-terminal http://purl.obolibrary.org/obo/MOD_01709 iTRAQ4plex reporter+balance reagent N-acylated residue A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with one of the Applied Biosystems iTRAQ4plex reagent reporter+balance groups. http://purl.obolibrary.org/obo/MOD_01712 iTRAQ8plex reporter+balance reagent acylated N-terminal http://purl.obolibrary.org/obo/MOD_01710 iTRAQ8plex reporter+balance reagent N-acylated residue A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with one of the Applied Biosystems iTRAQ8plex reagent reporter+balance groups. http://purl.obolibrary.org/obo/MOD_01713 iTRAQ4plex reporter+balance reagent O-acylated residue http://purl.obolibrary.org/obo/MOD_01707 isotope tagged reagent O-acylated residue A protein modification that effectively replaces a residue hydroxyl with one of the Applied Biosystems iTRAQ4plex reagent reporter+balance acyloxy groups. http://purl.obolibrary.org/obo/MOD_01714 iTRAQ8plex reporter+balance reagent O-acylated residue http://purl.obolibrary.org/obo/MOD_01707 isotope tagged reagent O-acylated residue A protein modification that effectively replaces a residue hydroxyl with one of the Applied Biosystems iTRAQ8plex reagent reporter+balance acyloxy groups. http://purl.obolibrary.org/obo/MOD_01715 TMT6plex reporter+balance reagent acylated residue http://purl.obolibrary.org/obo/MOD_01705 isotope tagged reagent acylated residue A protein modification that effectively replaces a hydrogen atom of a residue with a Proteome Sciences TMT6plex reporter+balance group. http://purl.obolibrary.org/obo/MOD_01716 TMT6plex reporter fragment http://purl.obolibrary.org/obo/MOD_01520 modification reporter fragment The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-126 reagent acylated residue. http://purl.obolibrary.org/obo/MOD_01717 TMT6plex reporter+balance reagent N-acylated residue http://purl.obolibrary.org/obo/MOD_01706 isotope tagged reagent N-acylated residue A protein modification that effectively replaces a residue amino- or imino-hydrogen with a Proteome Sciences TMT6plex reporter+balance group. http://purl.obolibrary.org/obo/MOD_01718 TMT6plex reporter+balance reagent acylated N-terminal http://purl.obolibrary.org/obo/MOD_01717 TMT6plex reporter+balance reagent N-acylated residue A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a Proteome Sciences TMT6plex reporter+balance group. http://purl.obolibrary.org/obo/MOD_01719 TMT6plex reporter+balance reagent O-acylated residue http://purl.obolibrary.org/obo/MOD_01707 isotope tagged reagent O-acylated residue A protein modification that effectively replaces a residue hydroxyl with one of the Proteome Sciences TMT6plex reagent reporter+balance acyloxy groups. http://purl.obolibrary.org/obo/MOD_01720 TMT6plex-126 reporter+balance reagent acylated residue http://purl.obolibrary.org/obo/MOD_01715 TMT6plex reporter+balance reagent acylated residue A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-126 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01721 TMT6plex-126 reporter+balance reagent acylated N-terminal http://purl.obolibrary.org/obo/MOD_01720 TMT6plex-126 reporter+balance reagent acylated residue A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-126 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01722 TMT6plex-126 reporter+balance reagent N6-acylated lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-126 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01723 TMT6plex-126 reporter+balance reagent O4'-acylated tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-126 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01724 TMT6plex-126 reporter+balance reagent N'-acylated histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-126 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01725 TMT6plex-126 reporter+balance reagent O3-acylated serine http://purl.obolibrary.org/obo/MOD_02003 O3-acylated L-serine A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-126 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01726 TMT6plex-126 reporter+balance reagent O3-acylated threonine http://purl.obolibrary.org/obo/MOD_02004 O3-acylated L-threonine A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-126 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01727 TMT6plex-126 reporter fragment http://purl.obolibrary.org/obo/MOD_01716 TMT6plex reporter fragment The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-126 reagent acylated residue. http://purl.obolibrary.org/obo/MOD_01728 TMT6plex-127 reporter+balance reagent acylated residue http://purl.obolibrary.org/obo/MOD_01715 TMT6plex reporter+balance reagent acylated residue A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-127 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01729 TMT6plex-127 reporter+balance reagent acylated N-terminal http://purl.obolibrary.org/obo/MOD_01728 TMT6plex-127 reporter+balance reagent acylated residue A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-127 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01730 TMT6plex-127 reporter+balance reagent N6-acylated lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-127 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01731 TMT6plex-127 reporter+balance reagent O4'-acylated tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-127 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01732 TMT6plex-127 reporter+balance reagent N'-acylated histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-127 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01734 TMT6plex-127 reporter+balance reagent O3-acylated threonine http://purl.obolibrary.org/obo/MOD_02004 O3-acylated L-threonine A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-127 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01735 TMT6plex-127 reporter fragment http://purl.obolibrary.org/obo/MOD_01716 TMT6plex reporter fragment The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-127 reagent acylated residue. http://purl.obolibrary.org/obo/MOD_01736 TMT6plex-128 reporter+balance reagent acylated residue http://purl.obolibrary.org/obo/MOD_01715 TMT6plex reporter+balance reagent acylated residue A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-128 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01737 TMT6plex-128 reporter+balance reagent acylated N-terminal http://purl.obolibrary.org/obo/MOD_01736 TMT6plex-128 reporter+balance reagent acylated residue A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-128 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01738 TMT6plex-128 reporter+balance reagent N6-acylated lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-128 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01739 TMT6plex-128 reporter+balance reagent O4'-acylated tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-128 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01740 TMT6plex-128 reporter+balance reagent N'-acylated histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-128 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01741 TMT6plex-128 reporter+balance reagent O3-acylated serine http://purl.obolibrary.org/obo/MOD_02003 O3-acylated L-serine A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-128 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01742 TMT6plex-128 reporter+balance reagent O3-acylated threonine http://purl.obolibrary.org/obo/MOD_02004 O3-acylated L-threonine A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-128 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01743 TMT6plex-128 reporter fragment http://purl.obolibrary.org/obo/MOD_01716 TMT6plex reporter fragment The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-128 reagent acylated residue. http://purl.obolibrary.org/obo/MOD_01744 TMT6plex-129 reporter+balance reagent acylated residue http://purl.obolibrary.org/obo/MOD_01715 TMT6plex reporter+balance reagent acylated residue A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-129 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01745 TMT6plex-129 reporter+balance reagent acylated N-terminal http://purl.obolibrary.org/obo/MOD_01744 TMT6plex-129 reporter+balance reagent acylated residue A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-129 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01746 TMT6plex-129 reporter+balance reagent N6-acylated lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-129 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01747 TMT6plex-129 reporter+balance reagent O4'-acylated tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-129 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01748 TMT6plex-129 reporter+balance reagent N'-acylated histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-129 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01749 TMT6plex-129 reporter+balance reagent O3-acylated serine http://purl.obolibrary.org/obo/MOD_02003 O3-acylated L-serine A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-129 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01750 TMT6plex-129 reporter+balance reagent O3-acylated threonine http://purl.obolibrary.org/obo/MOD_02004 O3-acylated L-threonine A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-129 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01751 TMT6plex-129 reporter fragment http://purl.obolibrary.org/obo/MOD_01716 TMT6plex reporter fragment The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-129 reagent acylated residue. http://purl.obolibrary.org/obo/MOD_01752 TMT6plex-130 reporter+balance reagent acylated residue http://purl.obolibrary.org/obo/MOD_01715 TMT6plex reporter+balance reagent acylated residue A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-130 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01753 TMT6plex-130 reporter+balance reagent acylated N-terminal http://purl.obolibrary.org/obo/MOD_01752 TMT6plex-130 reporter+balance reagent acylated residue A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-130 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01754 TMT6plex-130 reporter+balance reagent N6-acylated lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-130 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01755 TMT6plex-130 reporter+balance reagent O4'-acylated tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-130 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01756 TMT6plex-130 reporter+balance reagent N'-acylated histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-130 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01757 TMT6plex-130 reporter+balance reagent O3-acylated serine http://purl.obolibrary.org/obo/MOD_02003 O3-acylated L-serine A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-130 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01758 TMT6plex-130 reporter+balance reagent O3-acylated threonine http://purl.obolibrary.org/obo/MOD_02004 O3-acylated L-threonine A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-130 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01759 TMT6plex-130 reporter fragment http://purl.obolibrary.org/obo/MOD_01716 TMT6plex reporter fragment The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-130 reagent acylated residue. http://purl.obolibrary.org/obo/MOD_01760 TMT6plex-131 reporter+balance reagent acylated residue http://purl.obolibrary.org/obo/MOD_01715 TMT6plex reporter+balance reagent acylated residue A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-131 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01761 TMT6plex-131 reporter+balance reagent acylated N-terminal http://purl.obolibrary.org/obo/MOD_01760 TMT6plex-131 reporter+balance reagent acylated residue A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-131 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01762 TMT6plex-131 reporter+balance reagent N6-acylated lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-131 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01763 TMT6plex-131 reporter+balance reagent O4'-acylated tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-131 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01764 TMT6plex-131 reporter+balance reagent N'-acylated histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-131 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01765 TMT6plex-131 reporter+balance reagent O3-acylated serine http://purl.obolibrary.org/obo/MOD_02003 O3-acylated L-serine A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-131 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01766 TMT6plex-131 reporter+balance reagent O3-acylated threonine http://purl.obolibrary.org/obo/MOD_02004 O3-acylated L-threonine A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-131 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01767 TMT6plex-131 reporter fragment http://purl.obolibrary.org/obo/MOD_01716 TMT6plex reporter fragment The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-131 reagent acylated residue. http://purl.obolibrary.org/obo/MOD_01768 O-palmitoleylated residue http://purl.obolibrary.org/obo/MOD_01423 palmitoleylated residue A protein modification that effectively replaces a residue hydroxyl group with a palmitoleyloxy group. http://purl.obolibrary.org/obo/MOD_01769 O-palmitoleyl-L-threonine http://purl.obolibrary.org/obo/MOD_02004 O3-acylated L-threonine A protein modification that effectively converts an L-threonine residue to O-palmitoleyl-L-threonine. http://purl.obolibrary.org/obo/MOD_01770 O-palmitoyl-L-threonine amide http://purl.obolibrary.org/obo/MOD_02004 O3-acylated L-threonine A protein modification that effectively converts an L-threonine residue to O-palmitoyl-L-threonine amide. http://purl.obolibrary.org/obo/MOD_01771 farnesyl reporter fragment http://purl.obolibrary.org/obo/MOD_01520 modification reporter fragment The farnesyl cation protein modification reporter fragment produced by fragmentation of some farnesyl modified residues. http://purl.obolibrary.org/obo/MOD_01772 palmityl reporter fragment http://purl.obolibrary.org/obo/MOD_01520 modification reporter fragment The palmityl cation protein modification reporter fragment produced by fragmentation of some palmitoyl modified residues. http://purl.obolibrary.org/obo/MOD_01773 N6,N6,N6-trimethyl-L-lysine with neutral loss of trimethylamine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue Covalent modification of a trimethyllysine residue with secondary loss of a neutral trimethylamine molecular fragment. http://purl.obolibrary.org/obo/MOD_01774 N6-octanoyl-L-lysine http://purl.obolibrary.org/obo/MOD_00666 octanoylated residue A protein modification that effectively converts an L-lysine residue to N6-octanoyl-L-lysine. http://purl.obolibrary.org/obo/MOD_01775 5-glutamyl serotonin http://purl.obolibrary.org/obo/MOD_00907 modified L-glutamine residue A protein modification that effectively converts an L-glutamine residue to 5-glutamyl serotonin. http://purl.obolibrary.org/obo/MOD_01776 S-methylthiocarbonylaminoethylcysteine (Cys) http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-methylthiocarbonylaminoethylcysteine. http://purl.obolibrary.org/obo/MOD_01777 S-(glycyl)-L-cysteine (Gly) http://purl.obolibrary.org/obo/MOD_00908 modified glycine residue A protein modification that effectively converts a C-terminal glycine residue to S-(glycyl)-L-cysteine by forming a thioester bond with a free L-cysteine. http://purl.obolibrary.org/obo/MOD_01778 N-(glycyl)-L-cysteine http://purl.obolibrary.org/obo/MOD_00908 modified glycine residue A protein modification that effectively converts a C-terminal glycine residue to N-(glycyl)-L-cysteine by forming a peptide bond with a free L-cysteine. http://purl.obolibrary.org/obo/MOD_01779 N6-(L-lysyl)-L-lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively converts an L-lysine residue to N6-(L-lysyl)-L-lysine by formation of an isopeptide bond between the carboxyl group of a free lysine and the N6-amino group of the peptidyl L-lysine. http://purl.obolibrary.org/obo/MOD_01780 N6-(beta-lysyl)-L-5-hydroxylysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively converts an L-lysine residue to N6-(beta-lysyl)-L-5-hydroxylysine by formation of an isopeptide bond between the carboxyl group of a free beta-lysine and the N6-amino group of a peptidyl L-lysine. http://purl.obolibrary.org/obo/MOD_01781 N6-butanoyl-L-lysine http://purl.obolibrary.org/obo/MOD_01997 N-butanoylated residue A protein modification that effectively converts an L-lysine residue to N6-butanoyl-L-lysine. http://purl.obolibrary.org/obo/MOD_01782 N-methyl-L-serine http://purl.obolibrary.org/obo/MOD_01800 N-methylated serine A protein modification that effectively converts an L-serine residue to N-methyl-L-serine. http://purl.obolibrary.org/obo/MOD_01783 N,N-dimethyl-L-serine http://purl.obolibrary.org/obo/MOD_01800 N-methylated serine A protein modification that effectively converts an L-serine residue to N,N-dimethyl-L-serine. http://purl.obolibrary.org/obo/MOD_01784 N,N,N-trimethyl-L-serine http://purl.obolibrary.org/obo/MOD_01800 N-methylated serine A protein modification that effectively converts an L-serine residue to N,N,N-trimethyl-L-serine. http://purl.obolibrary.org/obo/MOD_01785 O-(L-isoglutamyl)-L-threonine (active site intermediate) http://purl.obolibrary.org/obo/MOD_01979 O-(L-isoglutamyl)-L-threonine A protein modification that effectively converts an L-threonine residue to O-(L-isoglutamyl)-L-threonine, using free L-glutamine and releasing ammonia. http://purl.obolibrary.org/obo/MOD_01787 5'-(L-tyros-5'-yl)amino-L-tyrosine http://purl.obolibrary.org/obo/MOD_02058 crosslinked L-tyrosine residue A protein modification that effectively cross-links two L-tyrosine residues through their 5' positions by amine nitrogen to form 5'-(L-tyros-5'-yl)amino-L-tyrosine. http://purl.obolibrary.org/obo/MOD_01788 histidine immonium ion http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively converts an N-terminal L-histidine residue to histidine immonium ion. http://purl.obolibrary.org/obo/MOD_01789 phenylalanine immonium ion http://purl.obolibrary.org/obo/MOD_00914 modified L-phenylalanine residue A protein modification that effectively converts an N-terminal L-phenylalanine residue to phenylalanine immonium ion. http://purl.obolibrary.org/obo/MOD_01790 tyrosine immonium ion http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively converts an an N-terminal L-tyrosine residue to tyrosine immonium ion. http://purl.obolibrary.org/obo/MOD_01791 phosphohistidine immonium ion http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively converts an N-terminal phosphohistidine residue to phosphohistidine immonium ion. http://purl.obolibrary.org/obo/MOD_01792 phosphotyrosine immonium ion http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively converts an N-terminal O4'-phospho-L-tyrosine residue to tyrosine immonium ion. http://purl.obolibrary.org/obo/MOD_01793 S-carboxamidomethyl-L-cysteine sulfoxide http://purl.obolibrary.org/obo/MOD_01854 sulfur monooxygenated residue A protein modification that effectively converts an L-cysteine residue to S-carboxamidomethyl-L-cysteine sulfoxide. http://purl.obolibrary.org/obo/MOD_01794 1x(13)C,3x(2)H labeled monomethylated residue http://purl.obolibrary.org/obo/MOD_00842 (13)C labeled residue A protein modification that effectively replaces the methyl group of a residue containing common isotopes with a 1x(13)C,3x(2)H labeled monomethylated residue. http://purl.obolibrary.org/obo/MOD_01795 1x(13)C,3x(2)H C(6)-labeled L-methionine http://purl.obolibrary.org/obo/MOD_00913 modified L-methionine residue A protein modification that effectively converts an L-methionine residue containing common isotopes to 1x(13)C,3x(2)H C(6)-labeled L-methionine. http://purl.obolibrary.org/obo/MOD_01796 1x(13)C,3x(2)H C(6)-labeled L-methionine sulfoxide http://purl.obolibrary.org/obo/MOD_00913 modified L-methionine residue A protein modification that effectively converts an L-methionine residue containing common isotopes to 1x(13)C,3x(2)H C(6)-labeled L-methionine sulfoxide. http://purl.obolibrary.org/obo/MOD_01797 1'-phosphohistidine immonium ion http://purl.obolibrary.org/obo/MOD_01791 phosphohistidine immonium ion A protein modification that effectively converts an N-terminal 1'-phosphohistidine residue to 1'-phosphohistidine immonium ion. http://purl.obolibrary.org/obo/MOD_01798 3'-phosphohistidine immonium ion http://purl.obolibrary.org/obo/MOD_01791 phosphohistidine immonium ion A protein modification that effectively converts an N-terminal 3'-phosphohistidine residue to 3'-phosphohistidine immonium ion. http://purl.obolibrary.org/obo/MOD_01799 methylated serine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-alanine residue to a methylated serine, such as N-methylserine, N,N-dimethylserine, or N,N,N-trimethylserine. http://purl.obolibrary.org/obo/MOD_01800 N-methylated serine http://purl.obolibrary.org/obo/MOD_01799 methylated serine A protein modification that effectively replaces an L-serine alpha amino hydrogen with a methyl group. http://purl.obolibrary.org/obo/MOD_01801 protonated L-serine (L-serinium) residue http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to an L-serinium (protonated L-serine). http://purl.obolibrary.org/obo/MOD_01802 N,N,N-trimethyl-L-serine (from L-serinium) http://purl.obolibrary.org/obo/MOD_01687 alpha-amino trimethylated residue A protein modification that effectively converts an L-serinium (protonated L-serine) residue to an N,N,N-trimethyl-L-serine. http://purl.obolibrary.org/obo/MOD_01803 O-methylated threonine http://purl.obolibrary.org/obo/MOD_01418 methylated threonine A protein modification that effectively converts an L-threonine residue to a methylated threonine, such as O-methyl-L-threonine or L-threonine methyl ester. http://purl.obolibrary.org/obo/MOD_01804 glycosylphosphorylated residue http://purl.obolibrary.org/obo/MOD_00764 glycoconjugated residue A protein modification that effectively results from forming an adduct with a glycosylphosphate through a phosphodiester bond. http://purl.obolibrary.org/obo/MOD_01805 N-(L-isoaspartyl)-glycine (Asp) http://purl.obolibrary.org/obo/MOD_02043 crosslinked L-aspartic acid residue A protein modification that effectively crosslinks an L-aspartic acid residue and a glycine residue by an isopeptide bond with formation of N-(L-isoaspartyl)-glycine and the release of water. http://purl.obolibrary.org/obo/MOD_01806 N,N-dimethyl-L-leucine http://purl.obolibrary.org/obo/MOD_01808 N-methylated leucine A protein modification that effectively converts an L-leucine residue to N,N-dimethyl-L-leucine. http://purl.obolibrary.org/obo/MOD_01807 N-formyl-L-glutamic acid http://purl.obolibrary.org/obo/MOD_00906 modified L-glutamic acid residue A protein modification that effectively converts an L-glutamic acid residue to N-formyl-L-glutamic acid. http://purl.obolibrary.org/obo/MOD_01808 N-methylated leucine http://purl.obolibrary.org/obo/MOD_01460 alpha-amino methylated residue A protein modification that effectively replaces an L-leucine alpha amino hydrogen with a methyl group. http://purl.obolibrary.org/obo/MOD_01809 5x(13)C,1x(15)N labeled residue http://purl.obolibrary.org/obo/MOD_00843 (15)N labeled residue A protein modification that effectively converts a residue containing common isotopes to a 5x(13)C,1x(15)N labeled residue. http://purl.obolibrary.org/obo/MOD_01810 5x(13)C,1x(15)N labeled L-proline http://purl.obolibrary.org/obo/MOD_00915 modified L-proline residue A protein modification that effectively converts an L-proline residue to 5x(13)C,1x(15)N labeled L-proline. http://purl.obolibrary.org/obo/MOD_01811 5x(13)C,1x(15)N labeled L-methionine http://purl.obolibrary.org/obo/MOD_00913 modified L-methionine residue A protein modification that effectively converts an L-methionine residue to 5x(13)C,1x(15)N labeled L-methionine. http://purl.obolibrary.org/obo/MOD_01812 5x(13)C,1x(15)N labeled L-methionine sulfoxide http://purl.obolibrary.org/obo/MOD_01809 5x(13)C,1x(15)N labeled residue A protein modification that effectively converts an L-methionine residue to 5x(13)C,1x(15)N labeled L-methionine sulfoxide. http://purl.obolibrary.org/obo/MOD_01813 morpholine-2-acetylated residue http://purl.obolibrary.org/obo/MOD_00649 acylated residue A protein modification that effectively substitutes a morpholine-2-acetyl group for a hydrogen atom. http://purl.obolibrary.org/obo/MOD_01814 L-cysteine 3-hydroxy-2,5-pyridinedicarboxylic acid http://purl.obolibrary.org/obo/MOD_02055 crosslinked L-serine residue A protein modification that effectively cross-links a cysteine and two serine residues to form L-cysteine 3-hydroxy-2,5-pyridinedicarboxylic acid. http://purl.obolibrary.org/obo/MOD_01815 L-glutamate thiazole-4-carboxylic acid http://purl.obolibrary.org/obo/MOD_02045 crosslinked L-glutamic acid residue A protein modification that effectively crosslinks an L-cysteine residue and an L-glutamic acid residue to form L-glutamate thiazole-4-carboxylic acid. http://purl.obolibrary.org/obo/MOD_01816 2'-hydroxy-L-tryptophan http://purl.obolibrary.org/obo/MOD_01622 monohydroxylated tryptophan A protein modification that effectively converts an L-tryptophan residue to a 2'-hydroxy-L-tryptophan. http://purl.obolibrary.org/obo/MOD_01817 2'-oxo-L-tryptophan http://purl.obolibrary.org/obo/MOD_00918 modified L-tryptophan residue A protein modification that effectively converts an L-tryptophan residue to a 2'-oxo-L-tryptophan. http://purl.obolibrary.org/obo/MOD_01818 1'-(L-tryptophan-3'-yl)-L-tryptophan http://purl.obolibrary.org/obo/MOD_02057 crosslinked L-tryptophan residue A protein modification that effectively cross-links two tryptophan residues to form 1'-(L-tryptophan-3'-yl)-L-tryptophan. http://purl.obolibrary.org/obo/MOD_01819 N6-succinyl-L-lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively converts an L-lysine residue to N6-succinyl-L-lysine. http://purl.obolibrary.org/obo/MOD_01820 isotope tagged sufhydryl reagent modified cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively replaces a cysteine sulhydryl hydrogen with an isotope tagged sulfhydryl reagent group. http://purl.obolibrary.org/obo/MOD_01821 cysTMT6plex reporter+balance reagent cysteine disulfide http://purl.obolibrary.org/obo/MOD_01820 isotope tagged sufhydryl reagent modified cysteine A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex reporter+balance group. http://purl.obolibrary.org/obo/MOD_01822 cysTMT6plex-zero reporter+balance reagent cysteine disulfide http://purl.obolibrary.org/obo/MOD_01821 cysTMT6plex reporter+balance reagent cysteine disulfide A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-zero reporter+balance group. http://purl.obolibrary.org/obo/MOD_01823 cysTMT6plex-126 reporter+balance reagent cysteine disulfide http://purl.obolibrary.org/obo/MOD_01821 cysTMT6plex reporter+balance reagent cysteine disulfide A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-126 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01824 cysTMT6plex-127 reporter+balance reagent cysteine disulfide http://purl.obolibrary.org/obo/MOD_01821 cysTMT6plex reporter+balance reagent cysteine disulfide A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-127 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01825 cysTMT6plex-128 reporter+balance reagent cysteine disulfide http://purl.obolibrary.org/obo/MOD_01821 cysTMT6plex reporter+balance reagent cysteine disulfide A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-128 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01826 cysTMT6plex-129 reporter+balance reagent cysteine disulfide http://purl.obolibrary.org/obo/MOD_01821 cysTMT6plex reporter+balance reagent cysteine disulfide A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-129 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01827 cysTMT6plex-130 reporter+balance reagent cysteine disulfide http://purl.obolibrary.org/obo/MOD_01821 cysTMT6plex reporter+balance reagent cysteine disulfide A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-130 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01828 cysTMT6plex-131 reporter+balance reagent cysteine disulfide http://purl.obolibrary.org/obo/MOD_01821 cysTMT6plex reporter+balance reagent cysteine disulfide A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-131 reporter+balance group. http://purl.obolibrary.org/obo/MOD_01829 S-carboxymethyl-L-cysteine sulfoxide http://purl.obolibrary.org/obo/MOD_01854 sulfur monooxygenated residue A protein modification that effectively converts an L-cysteine residue to S-carboxymethyl-L-cysteine sulfoxide. http://purl.obolibrary.org/obo/MOD_01830 S-carboxymethyl-L-cysteine sulfone http://purl.obolibrary.org/obo/MOD_01855 sulfur dioxygenated residue A protein modification that effectively converts an L-cysteine residue to S-carboxymethyl-L-cysteine sulfone. http://purl.obolibrary.org/obo/MOD_01831 S-carboxamidomethyl-L-cysteine sulfone http://purl.obolibrary.org/obo/MOD_01855 sulfur dioxygenated residue A protein modification that effectively converts an L-cysteine residue to S-carboxamidomethyl-L-cysteine sulfone. http://purl.obolibrary.org/obo/MOD_01832 5x(13)C-labeled residue http://purl.obolibrary.org/obo/MOD_00842 (13)C labeled residue A protein modification that effectively converts a residue containing common isotopes to a 5x(13)C-labeled residue. http://purl.obolibrary.org/obo/MOD_01833 5x(13)C-labeled L-methionine http://purl.obolibrary.org/obo/MOD_00913 modified L-methionine residue A protein modification that effectively converts an L-methionine residue containing common isotopes to 5x(13)C-labeled L-methionine. http://purl.obolibrary.org/obo/MOD_01834 5x(13)C-labeled L-methionine sulfoxide http://purl.obolibrary.org/obo/MOD_01832 5x(13)C-labeled residue A protein modification that effectively converts an L-methionine residue containing common isotopes to 5x(13)C-labeled L-methionine sulfoxide. http://purl.obolibrary.org/obo/MOD_01835 5x(13)C-labeled L-methionine sulfone http://purl.obolibrary.org/obo/MOD_01832 5x(13)C-labeled residue A protein modification that effectively converts an L-methionine residue containing common isotopes to 5x(13)C-labeled L-methionine sulfone. http://purl.obolibrary.org/obo/MOD_01836 N6-[([1-(6-nitro-2H-1,3-benzodioxol-5-yl)ethoxy]carbonyl]lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively converts an L-lysine residue to N6-[([1-(6-nitro-2H-1,3-benzodioxol-5-yl)ethoxy]carbonyl]lysine. http://purl.obolibrary.org/obo/MOD_01837 L-lanthionine (Cys-Cys) http://purl.obolibrary.org/obo/MOD_00687 thioether crosslinked residues A protein modification that effectively cross-links two L-cysteine residues with a thioether bond to form L-lanthionine. http://purl.obolibrary.org/obo/MOD_01838 L-lysinoalanine (Lys) http://purl.obolibrary.org/obo/MOD_01853 L-lysinoalanine A protein modification that effectively converts an L-lysine residue to L-lysinoalanine. http://purl.obolibrary.org/obo/MOD_01839 L-lanthionine http://purl.obolibrary.org/obo/MOD_01841 lanthionine A protein modification that effectively cross-links either two L-cysteine residues, or an L-cysteine residue and an L-serine residue by a thioether bond to form L-lanthionine. http://purl.obolibrary.org/obo/MOD_01840 L-allo-isoleucine http://purl.obolibrary.org/obo/MOD_00910 modified L-isoleucine residue A protein modification that effectively converts an L-isoleucine residue to L-allo-isoleucine. http://purl.obolibrary.org/obo/MOD_01841 lanthionine http://purl.obolibrary.org/obo/MOD_01993 beta-carbon thioether crosslinked residues A protein modification that effectively cross-links either two or an L-cysteine residue and an L-serine residue by a thioether bond to form a lanthionine, either D- or L- or meso-lanthionine. http://purl.obolibrary.org/obo/MOD_01842 S-(2-aminovinyl)-L-cysteine http://purl.obolibrary.org/obo/MOD_01851 S-(2-aminovinyl)-cysteine A protein modification that effectively converts two L-cysteine residues to S-(2-aminovinyl)-L-cysteine. http://purl.obolibrary.org/obo/MOD_01843 5'-chloro-L-tryptophan http://purl.obolibrary.org/obo/MOD_01913 monochlorinated L-tryptophan A protein modification that effectively converts an L-tryptophan residue to 5'-chloro-L-tryptophan. http://purl.obolibrary.org/obo/MOD_01844 2-(3-methylbutanoyl)-5-hydroxyoxazole-4-carbothionic acid http://purl.obolibrary.org/obo/MOD_02050 crosslinked L-leucine residue A protein modification that effectively converts an L-cysteine residue and an L-leucine residue to 2-(3-methylbutanoyl)-5-hydroxyoxazole-4-carbothionic acid. http://purl.obolibrary.org/obo/MOD_01845 L-proline 5-hydroxyoxazole-4-carbothionic acid http://purl.obolibrary.org/obo/MOD_02054 crosslinked L-proline residue A protein modification that effectively converts an L-cysteine residue and an L-proline residue to L-proline 5-hydroxyoxazole-4-carbothionic acid. http://purl.obolibrary.org/obo/MOD_01846 methanobactin OB3b copper complex http://purl.obolibrary.org/obo/MOD_02067 metal or metal cluster coordinated L-cysteine residue A protein modification that effectively converts two L-cysteine residues, and a copper atom to the methanobactin OB3b copper complex. http://purl.obolibrary.org/obo/MOD_01847 L-cysteine sulfinyl phosphate http://purl.obolibrary.org/obo/MOD_00861 phosphorus containing modified residue A protein modification that effectively converts an L-cysteine residue to L-cysteine sulfinyl phosphate. http://purl.obolibrary.org/obo/MOD_01848 S-(spermidinoglutathion-S-yl)-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-(spermidinoglutathion-S-yl)-L-cysteine. http://purl.obolibrary.org/obo/MOD_01849 S-(2-aminovinyl)-D-cysteine (Cys-Cys) http://purl.obolibrary.org/obo/MOD_01850 S-(2-aminovinyl)-D-cysteine A protein modification that effectively cross-links two L-cysteine residues by a thioether bond to form S-(2-aminovinyl)-D-cysteine. http://purl.obolibrary.org/obo/MOD_01850 S-(2-aminovinyl)-D-cysteine http://purl.obolibrary.org/obo/MOD_01851 S-(2-aminovinyl)-cysteine A protein modification that effectively cross-links either two L-cysteine residues, or an L-cysteine residue and an L-serine residue by a thioether bond to form S-(2-aminovinyl)-D-cysteine. http://purl.obolibrary.org/obo/MOD_01851 S-(2-aminovinyl)-cysteine http://purl.obolibrary.org/obo/MOD_00859 modified residue that can arise from different natural residues A protein modification that effectively cross-links either two L-cysteine residues, or an L-cysteine residue and an L-serine residue by a thioether bond to form S-(2-aminovinyl)-cysteine. http://purl.obolibrary.org/obo/MOD_01852 L-lysinoalanine (Lys-Cys) http://purl.obolibrary.org/obo/MOD_02051 crosslinked L-lysine residue A protein modification that effectively crosslinks an L-cysteine residue and an L-lysine residue to release hydrogen sulfide and form 2-amino-6-(2-amino-2-carboxyethylamino)hexanoic acid. http://purl.obolibrary.org/obo/MOD_01853 L-lysinoalanine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively converts an L-lysine residue to L-lysinoalanine either by forming a cross-link with peptidyl-cysteine or peptidyl-serine, or by condensation with free serine. http://purl.obolibrary.org/obo/MOD_01854 sulfur monooxygenated residue http://purl.obolibrary.org/obo/MOD_00680 sulfur oxygenated residue A protein modification that effectively adds one oxygen atom to a sulfur atom of a residue without removing hydrogen atoms. http://purl.obolibrary.org/obo/MOD_01855 sulfur dioxygenated residue http://purl.obolibrary.org/obo/MOD_00680 sulfur oxygenated residue A protein modification that effectively adds two oxygen atoms to a sulfur atom of a residue without removing hydrogen atoms. http://purl.obolibrary.org/obo/MOD_01856 oxazole/oxazoline ring crosslinked residues (Cys) http://purl.obolibrary.org/obo/MOD_01419 oxazole/oxazoline ring crosslinked residues A protein modification that crosslinks two residues by rearrangement and condensation of a cysteine with the carbonyl of the preceding residue to form a 1,3-oxazole-4-carbothionic acid. http://purl.obolibrary.org/obo/MOD_01857 2-(L-cystein-S-yl)-methionine http://purl.obolibrary.org/obo/MOD_02052 crosslinked L-methionine residue A protein modification that effectively cross-links an L-cysteine residue and an L-methionine residue by a thioether bond to form 2-(L-cystein-S-yl)-methionine. http://purl.obolibrary.org/obo/MOD_01858 S-(N-acetylamino)glucosyl-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-(N-acetylamino)glucosyl-L-cysteine. http://purl.obolibrary.org/obo/MOD_01859 4-amino-3-isothiazolidinone-L-phenylalanine http://purl.obolibrary.org/obo/MOD_02053 crosslinked L-phenylalanine residue A protein modification that effectively crosslinks an L-cysteine residue and an L-phenylalanine residue to form 4-amino-3-isothiazolidinone-L-phenylalanine. http://purl.obolibrary.org/obo/MOD_01860 L-cysteine bacillithiol disulfide http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to L-cysteine bacillithiol disulfide. http://purl.obolibrary.org/obo/MOD_01861 isothiazolidinone ring crosslinked residues http://purl.obolibrary.org/obo/MOD_00033 crosslinked residues A protein modification that crosslinks two residues by condensation of a cysteine thiol with the amido nitrogen of the following residue to form an isothiazolidinone ring. http://purl.obolibrary.org/obo/MOD_01862 disulfide conjugated residue http://purl.obolibrary.org/obo/MOD_01886 thiolated residue A protein modification that effectively replaces the hydrogen atom of a cysteine sulfanyl group with a substituted sulfanyl group, forming a disulfide bond that does not cross-link two encoded peptide chains. http://purl.obolibrary.org/obo/MOD_01863 mTRAQ reporter+balance reagent acylated residue http://purl.obolibrary.org/obo/MOD_01705 isotope tagged reagent acylated residue A protein modification that effectively replaces a hydrogen atom of a residue with one of the Applied Biosystems mTRAQ reagent reporter+balance groups. http://purl.obolibrary.org/obo/MOD_01864 mTRAQ light reporter+balance reagent acylated residue http://purl.obolibrary.org/obo/MOD_01868 modifications with monoisotopic mass differences that are nominally equal at 140.094963 Da A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems mTRAQ light reporter+balance group. http://purl.obolibrary.org/obo/MOD_01865 mTRAQ light reporter+balance reagent acylated N-terminal http://purl.obolibrary.org/obo/MOD_01864 mTRAQ light reporter+balance reagent acylated residue A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems mTRAQ light reporter+balance group. http://purl.obolibrary.org/obo/MOD_01866 mTRAQ light reporter+balance reagent N6-acylated lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively replaces the N6-amino hydrogen atom of a lysine residue with the Applied Biosystems mTRAQ light reporter+balance group. http://purl.obolibrary.org/obo/MOD_01867 mTRAQ light reporter+balance reagent O4'-acylated tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems mTRAQ light reporter+balance group. http://purl.obolibrary.org/obo/MOD_01868 modifications with monoisotopic mass differences that are nominally equal at 140.094963 Da http://purl.obolibrary.org/obo/MOD_01515 modifications with monoisotopic mass differences that are nominally equal at a resolution below 0.000001 Da Modifications that have monoisotopic mass differences from their respective origins of 140.094963 Da. http://purl.obolibrary.org/obo/MOD_01869 mTRAQ light reporter fragment http://purl.obolibrary.org/obo/MOD_01870 mTRAQ reporter fragment The protein modification reporter fragment produced by an Applied Biosystems mTRAQ light reagent derivatized residue. http://purl.obolibrary.org/obo/MOD_01870 mTRAQ reporter fragment http://purl.obolibrary.org/obo/MOD_01520 modification reporter fragment A protein modification reporter fragment produced by an Applied Biosystems mTRAQ reagent derivatized residue. http://purl.obolibrary.org/obo/MOD_01871 cyclized N-terminal S-carboxamidomethyl-L-cysteine http://purl.obolibrary.org/obo/MOD_01160 deaminated residue A protein modification that effectively cyclizes an S-carboxamidomethyl-L-cysteine residue to (R)-5-oxo-1,4-tetrahydrothiazine-3-carboxylic acid with the loss of ammonia. http://purl.obolibrary.org/obo/MOD_01872 cyclized N-terminal S-carboxymethyl-L-cysteine http://purl.obolibrary.org/obo/MOD_00704 dehydrated residue A protein modification that effectively cyclizes an S-carboxymethyl-L-cysteine residue to (R)-5-oxo-1,4-tetrahydrothiazine-3-carboxylic acid with the loss of water. http://purl.obolibrary.org/obo/MOD_01873 N-carboxy-L-alanine http://purl.obolibrary.org/obo/MOD_01152 carboxylated residue A protein modification that effectively converts an L-alanine residue to N-carboxy-L-alanine. http://purl.obolibrary.org/obo/MOD_01874 N-carboxy-L-valine http://purl.obolibrary.org/obo/MOD_01152 carboxylated residue A protein modification that effectively converts an L-alanine residue to N-carboxy-L-valine. http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively replaces an N6-amino hydrogen atom of L-lysine with an acyl group. http://purl.obolibrary.org/obo/MOD_01877 2-(4-guanidinobutanoyl)-5-hydroxyimidazole-4-carbothionic acid http://purl.obolibrary.org/obo/MOD_02044 crosslinked L-cysteine residue A protein modification that effectively converts an L-cysteine residue and an L-arginine residue to 2-(4-guanidinobutanoyl)-5-hydroxyimidazole-4-carbothionic acid. http://purl.obolibrary.org/obo/MOD_01878 L-threonine 5-hydroxyoxazole-4-carbonthionic acid http://purl.obolibrary.org/obo/MOD_02056 crosslinked L-threonine residue A protein modification that effectively converts an L-cysteine residue and an L-threonine residue to L-threonine 5-hydroxyoxazole-4-carbothionic acid. http://purl.obolibrary.org/obo/MOD_01879 methanobactin SB2 copper complex http://purl.obolibrary.org/obo/MOD_02067 metal or metal cluster coordinated L-cysteine residue A protein modification that effectively converts two L-cysteine residues, an L-arginine residue, an L-threonine residue and a copper atom to the methanobactin SB2 copper complex. http://purl.obolibrary.org/obo/MOD_01880 L-deoxyhypusine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue modification from RESID http://purl.obolibrary.org/obo/MOD_01881 3-(L-phenylalan-2'-yl)-L-valine http://purl.obolibrary.org/obo/MOD_02059 crosslinked L-valine residue A protein modification that effectively crosslinks an L-phenylalanine residue and an L-valine residue by a free radical process effectively releasing a hydrogen molecule and forming 3-(L-phenylalan-2'-yl)-L-valine. http://purl.obolibrary.org/obo/MOD_01882 5-imidazolinone ring crosslinked residues (Gly) http://purl.obolibrary.org/obo/MOD_00691 5-imidazolinone ring crosslinked residues A protein modification that effectively crosslinks the carbonyl of an amino acid residue at position n with the alpha amino of a glycine residue at position n+2 to form a 5-imidazolinone ring. http://purl.obolibrary.org/obo/MOD_01883 5-imidazolinone ring crosslinked residues (Cys) http://purl.obolibrary.org/obo/MOD_00691 5-imidazolinone ring crosslinked residues A protein modification that crosslinks two residues by rearrangement and condensation of a cysteine with the carbonyl of the preceding residue to form a 5-imidazolinone ring. http://purl.obolibrary.org/obo/MOD_01884 4-aminobutylated residue http://purl.obolibrary.org/obo/MOD_00001 alkylated residue A protein modification that effectively replaces a hydrogen atom with a 4-aminobutyl group, usually derived from spermidine. http://purl.obolibrary.org/obo/MOD_01887 Uniblue A derivatized lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that is produced by reaction with 1-amino-4-{[3-(ethenylsulfonyl)phenyl]amino}-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate, Uniblue A, to form Uniblue A lysine adduct. http://purl.obolibrary.org/obo/MOD_01888 didehydrogenated residue http://purl.obolibrary.org/obo/MOD_00683 dehydrogenated residue A protein modification that effectively removes two neutral hydrogen atoms (proton and electron) from a residue. http://purl.obolibrary.org/obo/MOD_01889 S-(2-succinyl)-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-(2-succinyl)-L-cysteine, by addition of either fumaric acid or maleic acid. http://purl.obolibrary.org/obo/MOD_01890 N-[(L-histidin-1'-yl)methyl]-L-methionine (fMet) http://purl.obolibrary.org/obo/MOD_02062 crosslinked N-formyl-L-methionine residue A protein modification that effectively crosslinks an N-formyl-L-methionine residue and an L-histidine residue to form N-[(L-histidin-1'-yl)methyl]-L-methionine. http://purl.obolibrary.org/obo/MOD_01891 N-[(L-histidin-1'-yl)methyl]-L-methionine (Met) http://purl.obolibrary.org/obo/MOD_02052 crosslinked L-methionine residue A protein modification that effectively crosslinks an L-methionine residue and an L-histidine residue to form N-[(L-histidin-1'-yl)methyl]-L-methionine. http://purl.obolibrary.org/obo/MOD_01892 N6-crotonyl-L-lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively converts an L-lysine residue to N6-crotonyl-L-lysine. http://purl.obolibrary.org/obo/MOD_01893 N6-malonyl-L-lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively converts an L-lysine residue to N6-malonyl-L-lysine. http://purl.obolibrary.org/obo/MOD_01894 propanoylated residue http://purl.obolibrary.org/obo/MOD_00649 acylated residue A protein modification that effectively replaces a hydrogen atom with an propanoyl group. http://purl.obolibrary.org/obo/MOD_01895 alpha-amino 3x(12)C-labeled propanoylated residue http://purl.obolibrary.org/obo/MOD_01426 isotope tagged reagent derivatized residue A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a 3x(12)C-labeled propanoyl group. http://purl.obolibrary.org/obo/MOD_01896 trifluoroacetic acid adduct http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue A protein modification produced by trifluoroacetic acid forming an adduct, either a salt or a hydrogen bonded carboxylic acid dimer, with an amino acid residue. http://purl.obolibrary.org/obo/MOD_01897 5-hydroxy-3-methyl-L-proline (Ile) http://purl.obolibrary.org/obo/MOD_00910 modified L-isoleucine residue A protein modification that effectively converts an L-isoleucine residue to 5-hydroxy-3-methyl-L-proline. http://purl.obolibrary.org/obo/MOD_01898 N2,N2-dimethyl-L-arginine http://purl.obolibrary.org/obo/MOD_00783 dimethylated L-arginine modification from RESID http://purl.obolibrary.org/obo/MOD_01899 L-arginine thiazole-4-carboxylic acid http://purl.obolibrary.org/obo/MOD_02041 crosslinked L-arginine residue A protein modification that effectively crosslinks an L-arginine residue and an L-cysteine residue to form arginine thiazole-4-carboxylic acid. http://purl.obolibrary.org/obo/MOD_01900 L-cysteine 5-methyloxazole-4-carboxylic acid http://purl.obolibrary.org/obo/MOD_02044 crosslinked L-cysteine residue A protein modification that effectively crosslinks an L-cysteine residue and an L-threonine residue to form L-cysteine 5-methyloxazole-4-carboxylic acid. http://purl.obolibrary.org/obo/MOD_01901 L-threonine 5-methyloxazole-4-carboxylic acid http://purl.obolibrary.org/obo/MOD_01422 oxazole/oxazoline ring crosslinked residues (Thr) A protein modification that effectively crosslinks two L-threonine residues to form L-threonine 5-methyloxazole-4-carboxylic acid. http://purl.obolibrary.org/obo/MOD_01902 L-isoleucine oxazole-4-carboxylic acid http://purl.obolibrary.org/obo/MOD_02049 crosslinked L-isoleucine residue A protein modification that effectively crosslinks an L-isoleucine residue and an L-serine residue to form L-cysteine oxazole-4-carboxylic acid. http://purl.obolibrary.org/obo/MOD_01903 L-serine oxazole-4-carboxylic acid http://purl.obolibrary.org/obo/MOD_01421 oxazole/oxazoline ring crosslinked residues (Ser) A protein modification that effectively crosslinks two L-serine residues to form serine oxazole-4-carboxylic acid. http://purl.obolibrary.org/obo/MOD_01904 L-serine 5-methyloxazoline-4-carboxylic acid http://purl.obolibrary.org/obo/MOD_02055 crosslinked L-serine residue A protein modification that effectively crosslinks an L-serine residue and an L-threonine residue to form L-serine 5-methyloxazoline-4-carboxylic acid. http://purl.obolibrary.org/obo/MOD_01905 5-hydroxy-3-methyl-L-proline http://purl.obolibrary.org/obo/MOD_00859 modified residue that can arise from different natural residues A protein modification that effectively converts a source amino acid residue to 5-hydroxy-3-methyl-L-proline. http://purl.obolibrary.org/obo/MOD_01906 dehydromethionine http://purl.obolibrary.org/obo/MOD_00913 modified L-methionine residue A protein modification that effectively converts an L-methionine residue to dehydromethionine. http://purl.obolibrary.org/obo/MOD_01907 dehydromethionine (from L-methioninium) http://purl.obolibrary.org/obo/MOD_00913 modified L-methionine residue A protein modification that effectively converts an L-methioninium (protonated L-methionine) residue to dehydromethionine. http://purl.obolibrary.org/obo/MOD_01908 4-sulfophenyl isothiocyanate alpha-amino derivatized residue http://purl.obolibrary.org/obo/MOD_00584 4-sulfophenyl isothiocyanate derivatized residue A protein modification that effectively converts a residue to the 4-sulfophenyl isothiocyanate adduct, alpha-amino-[(4-sulfophenyl)carbamothioyl] residue. http://purl.obolibrary.org/obo/MOD_01909 6x(13)C labeled 4-sulfophenyl isothiocyanate alpha-amino derivatized residue http://purl.obolibrary.org/obo/MOD_00880 6x(13)C labeled 4-sulfophenyl isothiocyanate derivatized residue A protein modification that effectively converts a residue to the 6x(13)C labeled 4-sulfophenyl isothiocyanate adduct, alpha-amino-[(4-sulfophenyl)carbamothioyl] residue. http://purl.obolibrary.org/obo/MOD_01910 monofluorinated residue http://purl.obolibrary.org/obo/MOD_00498 fluorinated residue A protein modification that effectively substitutes one hydrogen atom of a residue with one fluorine atom. http://purl.obolibrary.org/obo/MOD_01911 monochlorinated residue http://purl.obolibrary.org/obo/MOD_00753 chlorinated residue A protein modification that effectively substitutes one hydrogen atom of a residue with one chlorine atom. http://purl.obolibrary.org/obo/MOD_01912 monobrominated residue http://purl.obolibrary.org/obo/MOD_00754 brominated residue A protein modification that effectively substitutes one hydrogen atom of a residue with one bromine atom. http://purl.obolibrary.org/obo/MOD_01913 monochlorinated L-tryptophan http://purl.obolibrary.org/obo/MOD_01911 monochlorinated residue A protein modification that effectively substitutes one hydrogen atom of an L-tryptophan residue with one chlorine atom. http://purl.obolibrary.org/obo/MOD_01914 O5-galactosyl-L-hydroxylysine http://purl.obolibrary.org/obo/MOD_00396 O-glycosylated residue A protein modification that effectively converts a 5-hydroxy-L-lysine residue to O5-galactosyl-L-hydroxylysine. http://purl.obolibrary.org/obo/MOD_01915 N-formyl-L-alanine http://purl.obolibrary.org/obo/MOD_00901 modified L-alanine residue A protein modification that effectively converts an L-alanine residue to N-formyl-L-alanine. http://purl.obolibrary.org/obo/MOD_01916 O4'-(N-acetylamino)galactosyl-L-tyrosine http://purl.obolibrary.org/obo/MOD_01927 O-glycosyl-L-tyrosine A protein modification that effectively converts an L-tyrosine residue to O4'-(N-acetylamino)galactosyl-L-tyrosine. http://purl.obolibrary.org/obo/MOD_01917 N6-(L-isoaspartyl)-L-lysine (Asp) http://purl.obolibrary.org/obo/MOD_02043 crosslinked L-aspartic acid residue A protein modification that effectively crosslinks an L-aspartic acid residue and an L-lysine residue by an isopeptide bond with the formation of N6-(L-isoaspartyl)-L-lysine and the release of water. http://purl.obolibrary.org/obo/MOD_01918 (2S,5S)-5-hydroxylysine http://purl.obolibrary.org/obo/MOD_00037 5-hydroxy-L-lysine A protein modification that effectively converts an L-lysine residue to (2S,5S)-5-hydroxylysine. http://purl.obolibrary.org/obo/MOD_01919 (2S,3S)-3-hydroxyaspartic acid http://purl.obolibrary.org/obo/MOD_01926 3-hydroxy-L-aspartic acid A protein modification that effectively converts an L-aspartic acid residue to (2S,3S)-3-hydroxyaspartic acid. http://purl.obolibrary.org/obo/MOD_01920 3-hydroxy-L-histidine http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that effectively converts an L-histidine residue to 3-hydroxy-L-histidine. http://purl.obolibrary.org/obo/MOD_01921 D-aspartic acid (Asp) http://purl.obolibrary.org/obo/MOD_00904 modified L-aspartic acid residue A protein modification that effectively converts an L-aspartic acid residue to D-aspartic acid. http://purl.obolibrary.org/obo/MOD_01922 3-methoxydehydroalanine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to 3-methoxydehydroalanine. http://purl.obolibrary.org/obo/MOD_01923 N6-(L-aspartyl)-L-lysine http://purl.obolibrary.org/obo/MOD_02043 crosslinked L-aspartic acid residue A protein modification that effectively crosslinks an L-aspartic acid residue and an L-lysine residue by an isopeptide bond to form N6-(L-aspartyl)-L-lysine and the release of water. http://purl.obolibrary.org/obo/MOD_01924 S-octanoyl-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-octanoyl-L-cysteine. http://purl.obolibrary.org/obo/MOD_01925 (2S,5R)-5-hydroxylysine http://purl.obolibrary.org/obo/MOD_00037 5-hydroxy-L-lysine A protein modification that effectively converts an L-lysine residue to (2S,5R)-5-hydroxylysine. http://purl.obolibrary.org/obo/MOD_01926 3-hydroxy-L-aspartic acid http://purl.obolibrary.org/obo/MOD_00904 modified L-aspartic acid residue A protein modification that effectively converts an L-aspartic acid residue to one of the diastereomeric 3-hydroxy-L-aspartic acid residues. http://purl.obolibrary.org/obo/MOD_01927 O-glycosyl-L-tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively converts an L-tyrosine residue to O4'-glycosyltyrosine. http://purl.obolibrary.org/obo/MOD_01928 N-(L-isoaspartyl)-glycine http://purl.obolibrary.org/obo/MOD_02047 crosslinked glycine residue A protein modification that effectively crosslinks either an L-asparagine residue or an L-aspartic acid residue with a glycine residue by an isopeptide bond with formation of N-(L-isoaspartyl)glycine. http://purl.obolibrary.org/obo/MOD_01929 N6-(L-isoaspartyl)-L-lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively crosslinks an either an L-asparagine residue or an L-aspartic acid residue with an L-lysine residue by an isopeptide bond with the formation of N6-(L-isoaspartyl)-L-lysine. http://purl.obolibrary.org/obo/MOD_01930 D-aspartic acid (Asn) http://purl.obolibrary.org/obo/MOD_00903 modified L-asparagine residue A protein modification that effectively converts an L-asparagine residue to D-aspartic acid. http://purl.obolibrary.org/obo/MOD_01931 N6-phospho-L-lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively converts an L-lysine residue to N6-phospho-L-lysine. http://purl.obolibrary.org/obo/MOD_01932 L-lysinonorleucine http://purl.obolibrary.org/obo/MOD_02051 crosslinked L-lysine residue A protein modification that effectively cross-links two lysine residues with a carbon-nitrogen bond to form L-lysinonorleucine.. http://purl.obolibrary.org/obo/MOD_01933 desmosine http://purl.obolibrary.org/obo/MOD_02051 crosslinked L-lysine residue A protein modification that effectively cross-links four L-lysine residues to form desmosine. http://purl.obolibrary.org/obo/MOD_01934 isodesmosine http://purl.obolibrary.org/obo/MOD_02051 crosslinked L-lysine residue A protein modification that effectively cross-links four L-lysine residues to form isodesmosine. http://purl.obolibrary.org/obo/MOD_01935 O-glucosyl-L-hydroxylysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue modification from RESID http://purl.obolibrary.org/obo/MOD_01936 N6-oleoyl-L-lysine http://purl.obolibrary.org/obo/MOD_02011 N-oleoylated residue A protein modification that effectively converts an L-lysine residue to N6-oleoyl-L-lysine. http://purl.obolibrary.org/obo/MOD_01937 N-palmitoyl-L-methionine http://purl.obolibrary.org/obo/MOD_00913 modified L-methionine residue A protein modification that effectively converts an L-methionine residue to N-palmitoyl-L-methionine. http://purl.obolibrary.org/obo/MOD_01938 2-(2-aminosuccinimidyl)-3-sulfanylpropanoic acid (Asn) http://purl.obolibrary.org/obo/MOD_02042 crosslinked L-asparagine residue A protein modification that crosslinks an asparagine and the following cysteine residue with the formation of (2-aminosuccinimidyl)-3-sulfanylpropanoic acid and the release of ammonia. http://purl.obolibrary.org/obo/MOD_01939 2-(2-aminosuccinimidyl)-3-sulfanylpropanoic acid (Asp) http://purl.obolibrary.org/obo/MOD_02043 crosslinked L-aspartic acid residue A protein modification that crosslinks an aspartic acid and the following cysteine residue with the formation of (2-aminosuccinimidyl)-3-sulfanylpropanoic acid and the loss of a water molecule. http://purl.obolibrary.org/obo/MOD_01940 2-(2-aminosuccinimidyl)pentanedioic acid (Asn) http://purl.obolibrary.org/obo/MOD_02042 crosslinked L-asparagine residue A protein modification that crosslinks an asparagine and the following glutamic acid residue with the formation of (2-aminosuccinimidyl)pentanedioic acid and the release of ammonia. http://purl.obolibrary.org/obo/MOD_01941 2-(2-aminosuccinimidyl)pentanedioic acid (Asp) http://purl.obolibrary.org/obo/MOD_02043 crosslinked L-aspartic acid residue A protein modification that crosslinks an aspartic acid and the following glycine residue with the formation of (2-aminosuccinimidyl)pentanedioic acid and the loss of a water molecule. http://purl.obolibrary.org/obo/MOD_01942 D-aspartic acid http://purl.obolibrary.org/obo/MOD_00859 modified residue that can arise from different natural residues A protein modification that effectively converts a source amino acid residue to D-aspartic acid. http://purl.obolibrary.org/obo/MOD_01943 pyrrolidione ring crosslinked residues http://purl.obolibrary.org/obo/MOD_00033 crosslinked residues A protein modification that crosslinks two adjacent residues by formation of a pyrrolidione ring. http://purl.obolibrary.org/obo/MOD_01944 2-aminosuccinimide ring crosslinked residues http://purl.obolibrary.org/obo/MOD_00033 crosslinked residues A protein modification that forms (2-aminosuccinimidyl)acetic acid by crosslinking either an aspartic acid residue or an asparagine residue with the following residue. http://purl.obolibrary.org/obo/MOD_01945 2-(2-aminosuccinimidyl)-3-sulfanylpropanoic acid http://purl.obolibrary.org/obo/MOD_02044 crosslinked L-cysteine residue A protein modification that forms (2-aminosuccinimidyl)-3-sulfanylpropanoic acid by crosslinking either an aspartic acid residue or an asparagine residue with the following cysteine residue. http://purl.obolibrary.org/obo/MOD_01946 2-(2-aminosuccinimidyl)pentanedioic acid http://purl.obolibrary.org/obo/MOD_02045 crosslinked L-glutamic acid residue A protein modification that forms (2-aminosuccinimidyl)pentanedioicacid by crosslinking either an aspartic acid residue or an asparagine residue with the following glutamic acid residue. http://purl.obolibrary.org/obo/MOD_01947 O-(L-isoaspartyl)-L-threonine (cross-link) http://purl.obolibrary.org/obo/MOD_02043 crosslinked L-aspartic acid residue A protein modification that effectively cross-links an L-threonine residue and an L-aspartic acid residue with an ester bond to form O-(L-isoaspartyl)-L-threonine. http://purl.obolibrary.org/obo/MOD_01948 labionin http://purl.obolibrary.org/obo/MOD_02055 crosslinked L-serine residue A protein modification that effectively cross-links an L-cysteine residue and two L-serine residues by a thioether bond and a carbon-carbon bond to form labionin. http://purl.obolibrary.org/obo/MOD_01949 coelenterazine http://purl.obolibrary.org/obo/MOD_02058 crosslinked L-tyrosine residue A protein modification that effectively cross-links a phenylalanine and two tyrosine residues to form coelenterazine. http://purl.obolibrary.org/obo/MOD_01950 L-isoglutamyl histamine http://purl.obolibrary.org/obo/MOD_00907 modified L-glutamine residue A protein modification that effectively converts an L-glutamine residue to L-isoglutamyl histamine. http://purl.obolibrary.org/obo/MOD_01951 O-(L-isoglutamyl)-L-serine (Gln-Ser) http://purl.obolibrary.org/obo/MOD_02046 crosslinked L-glutamine residue A protein modification that effectively crosslinks an L-glutamine residue and an L-serine residue by an ester bond and releasing ammonia to form O-(L-isoglutamyl)-L-serine. http://purl.obolibrary.org/obo/MOD_01952 O-(L-isoglutamyl)-L-threonine (Gln-Thr) http://purl.obolibrary.org/obo/MOD_02056 crosslinked L-threonine residue A protein modification that effectively cross-links an L-threonine residue and an L-glutamine residue with an ester bond releasing ammonia to form O-(L-isoglutamyl)-L-threonine. http://purl.obolibrary.org/obo/MOD_01953 tetrakis-L-cysteinyl tetrairon octanitrosyl http://purl.obolibrary.org/obo/MOD_02067 metal or metal cluster coordinated L-cysteine residue A protein modification that effectively converts four L-cysteine residues and a four-iron cluster to tetrakis-L-cysteinyl tetrairon octanitrosyl. http://purl.obolibrary.org/obo/MOD_01954 dehydroalanine (Sec) http://purl.obolibrary.org/obo/MOD_01168 dehydroalanine A protein modification that effectively converts an L-selenocysteine residue to dehydroalanine. http://purl.obolibrary.org/obo/MOD_01955 L-alaninato bis-L-aspartato tris-L-glutamato L-histidino calcium tetramanganese pentoxide http://purl.obolibrary.org/obo/MOD_02065 metal or metal cluster coordinated L-alanine residue modification from RESID http://purl.obolibrary.org/obo/MOD_01956 (3R)-3-hydroxy-L-arginine http://purl.obolibrary.org/obo/MOD_00682 hydroxylated arginine A protein modification that effectively converts an L-arginine residue to (3R)-3-hydroxy-L-arginine. http://purl.obolibrary.org/obo/MOD_01957 2-hydroxyproline http://purl.obolibrary.org/obo/MOD_01024 monohydroxylated proline A protein modification that effectively converts an L-proline residue to 2-hydroxyproline. http://purl.obolibrary.org/obo/MOD_01958 bis-L-cysteinyl bisglutathion-S-yl diiron disulfide http://purl.obolibrary.org/obo/MOD_02067 metal or metal cluster coordinated L-cysteine residue A protein modification that effectively converts four L-cysteine residues and a two-iron two-sulfur cluster to bis-L-cysteinyl bisglutathion-S-yl diiron disulfide. http://purl.obolibrary.org/obo/MOD_01959 tris-L-cysteinyl L-glutamato tetrairon tetrasulfide http://purl.obolibrary.org/obo/MOD_02068 metal or metal cluster coordinated L-glutamic acid residue A protein modification that effectively converts three L-cysteine residues, an L-glutamic acid and a four-iron four-sulfur cluster to tris-L-cysteinyl L-glutamato tetrairon tetrasulfide. http://purl.obolibrary.org/obo/MOD_01960 tris-L-cysteinyl L-glutamin-O6-yl tetrairon tetrasulfide http://purl.obolibrary.org/obo/MOD_02069 metal or metal cluster coordinated L-glutamine residue A protein modification that effectively converts three L-cysteine residues, an L-glutamine residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-glutamin-O6-yl tetrairon tetrasulfide. http://purl.obolibrary.org/obo/MOD_01962 N4-(2,4-diacetamido-2,4,6-trideoxy-D-glucosyl)-L-asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine A protein modification that effectively converts an L-asparagine residue to N4-(2,4-diacetamido-2,4,6-trideoxy-D-glucosyl)-L-asparagine. http://purl.obolibrary.org/obo/MOD_01963 O-(2,4-diacetamido-2,4,6-trideoxy-D-glucosyl)-L-serine http://purl.obolibrary.org/obo/MOD_00002 O-glycosyl-L-serine A protein modification that effectively converts an L-serine residue to O-(2,4-diacetamido-2,4,6-trideoxy-D-glucosyl)-L-serine. http://purl.obolibrary.org/obo/MOD_01964 O-(2-acetamido-4-glyceramido-2,4,6-trideoxy-D-glucosyl)-L-serine http://purl.obolibrary.org/obo/MOD_00002 O-glycosyl-L-serine A protein modification that effectively converts an L-serine residue to O-(2-acetamido-4-glyceramido-2,4,6-trideoxy-D-glucosyl)-L-serine. http://purl.obolibrary.org/obo/MOD_01965 2xC(13),3x(2)H labeled N6-acetyl-L-lysine http://purl.obolibrary.org/obo/MOD_01431 (2)H deuterium tagged reagent A protein modification that effectively converts an L-lysine residue to 2xC(13),3x(2)H labeled N6-acetyl-L-lysine. http://purl.obolibrary.org/obo/MOD_01967 omega-N-(N-acetylamino)glucosyl-L-arginine http://purl.obolibrary.org/obo/MOD_00448 mono-N-acetylaminoglucosylated residue A protein modification that effectively converts an L-arginine residue to omega-N-(N-acetylamino)glucosyl-L-arginine. http://purl.obolibrary.org/obo/MOD_01968 (2R,3R,2'R)-3-methyllanthionine http://purl.obolibrary.org/obo/MOD_01981 3-methyllanthionine A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form (2R,3R,2'R)-3-methyllanthionine. http://purl.obolibrary.org/obo/MOD_01969 S-(gamma-glutamyl-cysteinyl-glycyl)-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-(gamma-glutamyl-cysteinyl-glycyl)-cysteine. http://purl.obolibrary.org/obo/MOD_01970 5-glutamyl glutamic acid http://purl.obolibrary.org/obo/MOD_00207 L-isoglutamyl-polyglutamic acid A protein modification that effectively converts an L-glutamic acid residue to 5-glutamyl glutamic acid, forming an isopeptide bond with a free glutamic acid. http://purl.obolibrary.org/obo/MOD_01971 5-glutamyl N2-ornithine http://purl.obolibrary.org/obo/MOD_00906 modified L-glutamic acid residue A protein modification that effectively converts an L-glutamic acid residue to N2-ornithine. http://purl.obolibrary.org/obo/MOD_01972 5-glutamyl coenzyme A thioester http://purl.obolibrary.org/obo/MOD_00906 modified L-glutamic acid residue A protein modification that effectively converts an L-glutamic acid residue to 5-glutamyl coenzyme A thioester. http://purl.obolibrary.org/obo/MOD_01973 N6-(3-phosphoglyceryl)-L-lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively converts an L-lysine residue to N6-(3-phosphoglyceryl)-L-lysine. http://purl.obolibrary.org/obo/MOD_01974 S-methyl-L-methionine http://purl.obolibrary.org/obo/MOD_00716 methylated methionine A protein modification that effectively converts an L-methionine residue to S-methyl-L-methionine. http://purl.obolibrary.org/obo/MOD_01975 S-poly(3-hydroxybutyrate)-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-(poly-3-hydroxybutyrate)-L-cysteine. http://purl.obolibrary.org/obo/MOD_01976 O3-(poly-3-hydroxybutyrate)-L-serine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to O3-(poly-3-hydroxybutyrate)-L-serine. http://purl.obolibrary.org/obo/MOD_01977 O-(L-isoglutamyl)-L-serine http://purl.obolibrary.org/obo/MOD_02055 crosslinked L-serine residue A protein modification that effectively crosslinks either an L-glutamine residue or an L-glutamic acid residue with an L-serine residue by an ester bond to form O-(L-isoglutamyl)-L-serine. http://purl.obolibrary.org/obo/MOD_01978 O-(L-isoaspartyl)-L-threonine http://purl.obolibrary.org/obo/MOD_02056 crosslinked L-threonine residue A protein modification that effectively converts an L-threonine residue to O-(L-isoaspartyl)-L-threonine, using either free L-asparagine and releasing ammonia or using a peptidyl L-aspartic acid residue and releasing water. http://purl.obolibrary.org/obo/MOD_01979 O-(L-isoglutamyl)-L-threonine http://purl.obolibrary.org/obo/MOD_02056 crosslinked L-threonine residue A protein modification that effectively converts an L-threonine residue to O-(L-isoglutamyl)-L-threonine, using free L-glutamine and releasing ammonia, or using a peptidyl L-glutamine and releasing ammonia. http://purl.obolibrary.org/obo/MOD_01980 omega-N-glycosyl-L-arginine http://purl.obolibrary.org/obo/MOD_00902 modified L-arginine residue A protein modification that effectively converts an L-arginine residue to N4-glycosyl-arginine. http://purl.obolibrary.org/obo/MOD_01981 3-methyllanthionine http://purl.obolibrary.org/obo/MOD_02056 crosslinked L-threonine residue A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form 3-methyllanthionine with unresolved stereospecificity. http://purl.obolibrary.org/obo/MOD_01982 N,N,N-trimethylglycine http://purl.obolibrary.org/obo/MOD_01698 alpha-amino trimethylated protonated-residue modification from RESID http://purl.obolibrary.org/obo/MOD_01983 N,N-dimethylglycine http://purl.obolibrary.org/obo/MOD_01686 alpha-amino dimethylated residue A protein modification that effectively converts a glycine residue to N,N-dimethyllglycine. http://purl.obolibrary.org/obo/MOD_01984 2-(L-cystein-S-yl)-L-alanine http://purl.obolibrary.org/obo/MOD_02040 crosslinked L-alanine residue A protein modification that effectively cross-links an L-cysteine residue and an L-alanine residue by a thioether bond to form 2-(S-L-cysteinyl)-L-alanine. http://purl.obolibrary.org/obo/MOD_01985 2-(L-cystein-S-yl)-D-asparagine http://purl.obolibrary.org/obo/MOD_02060 crosslinked D-asparagine residue A protein modification that effectively cross-links an L-cysteine residue and an L-asparagine residue by a thioether bond to form 2-(S-L-cysteinyl)-D-asparagine. http://purl.obolibrary.org/obo/MOD_01986 2-(L-cystein-S-yl)-L-serine http://purl.obolibrary.org/obo/MOD_02055 crosslinked L-serine residue A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form 2-(S-L-cysteinyl)-L-serine. http://purl.obolibrary.org/obo/MOD_01987 2-(L-cystein-S-yl)-D-serine http://purl.obolibrary.org/obo/MOD_02064 crosslinked D-serine residue A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form 2-(S-L-cysteinyl)-D-serine. http://purl.obolibrary.org/obo/MOD_01988 2-(L-cystein-S-yl)-L-threonine http://purl.obolibrary.org/obo/MOD_02056 crosslinked L-threonine residue 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)-L-threonine. http://purl.obolibrary.org/obo/MOD_01989 2-(L-cystein-S-yl)-D-tyrosine http://purl.obolibrary.org/obo/MOD_02058 crosslinked L-tyrosine residue 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)-D-tyrosine. http://purl.obolibrary.org/obo/MOD_01990 protonated glycine (glycinium) residue http://purl.obolibrary.org/obo/MOD_00908 modified glycine residue A protein modification that effectively converts a glycine residue to a glycinium (protonated glycine). http://purl.obolibrary.org/obo/MOD_01991 N,N,N-trimethylglycine (from glycinium) http://purl.obolibrary.org/obo/MOD_01687 alpha-amino trimethylated residue A protein modification that effectively converts a glycinium (protonated glycine) residue to an N,N,N-trimethylglycine. http://purl.obolibrary.org/obo/MOD_01992 alpha-carbon thioether crosslinked residues http://purl.obolibrary.org/obo/MOD_00687 thioether crosslinked residues A protein modification that crosslinks two residues by formation of a thioether bond between a cysteine thiol and the alpha-carbon of another amino acid residue. http://purl.obolibrary.org/obo/MOD_01993 beta-carbon thioether crosslinked residues http://purl.obolibrary.org/obo/MOD_00687 thioether crosslinked residues A protein modification that crosslinks two residues by formation of a thioether bond between a cysteine thiol and the beta-carbon of another amino acid residue. http://purl.obolibrary.org/obo/MOD_01994 N1'-formyl-L-tryptophan http://purl.obolibrary.org/obo/MOD_01106 N-formyl-L-tryptophan A protein modification that effectively converts an L-tryptophan residue to N1'-formyl-L-tryptophan. http://purl.obolibrary.org/obo/MOD_01995 N2-formyl-L-tryptophan http://purl.obolibrary.org/obo/MOD_01106 N-formyl-L-tryptophan A protein modification that effectively converts an L-tryptophan residue to N2-formyl-L-tryptophan. http://purl.obolibrary.org/obo/MOD_01996 butanoylated residue http://purl.obolibrary.org/obo/MOD_00649 acylated residue A protein modification that effectively replaces a hydrogen atom with an butanoyl group. http://purl.obolibrary.org/obo/MOD_01997 N-butanoylated residue http://purl.obolibrary.org/obo/MOD_01996 butanoylated residue A protein modification that effectively replaces a residue amino or imino hydrogen with a butanoyl group. http://purl.obolibrary.org/obo/MOD_01998 alpha-amino butanoylated residue http://purl.obolibrary.org/obo/MOD_01997 N-butanoylated residue A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a butanoyl group. http://purl.obolibrary.org/obo/MOD_01999 N6-(11-cis)-retinylidene-L-lysine http://purl.obolibrary.org/obo/MOD_02000 N6-retinylidene-L-lysine (unspecified geometric isomer) A protein modification that effectively converts an L-lysine residue to N6-retinylidene-(11-cis)-L-lysine. http://purl.obolibrary.org/obo/MOD_02000 N6-retinylidene-L-lysine (unspecified geometric isomer) http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively converts an L-lysine residue to N6-retinylidene-L-lysine (unspecified geometric isomer). http://purl.obolibrary.org/obo/MOD_02077 nitrosylated residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process A protein modification that effectively replaces a hydrogen atom with an nitrosyl (NO) group. http://purl.obolibrary.org/obo/MOD_02078 acetylated residue http://purl.obolibrary.org/obo/MOD_00649 acylated residue A protein modification that effectively replaces one or more hydrogen atoms with one or more acetyl groups. http://purl.obolibrary.org/obo/MOD_02079 diacetylated residue http://purl.obolibrary.org/obo/MOD_02078 acetylated residue A protein modification that effectively replaces one hydrogen atom with one acetyl group. http://purl.obolibrary.org/obo/MOD_02080 diacetylated L-serine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue 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. http://purl.obolibrary.org/obo/MOD_01112 nicotinoyl lysine http://purl.obolibrary.org/obo/MOD_00947 DeltaMass modification from DeltaMass http://purl.obolibrary.org/obo/MOD_00401 Gygi ICAT(TM) d0 modified cysteine http://purl.obolibrary.org/obo/MOD_01820 isotope tagged sufhydryl reagent 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. http://purl.obolibrary.org/obo/MOD_00659 methylated glutamine http://purl.obolibrary.org/obo/MOD_00907 modified L-glutamine residue 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. http://purl.obolibrary.org/obo/MOD_00006 N-glycosylated residue http://purl.obolibrary.org/obo/MOD_00693 glycosylated residue A protein modification that effectively replaces a residue hydrogen atom on a nitrogen with a carbohydrate-like group through a glycosidic bond. http://purl.obolibrary.org/obo/MOD_00030 N-formyl-L-methionine residue http://purl.obolibrary.org/obo/MOD_00868 natural, non-standard encoded residue A protein modification that effectively converts a source amino acid residue to an N-formyl-L-methionine, a natural pretranslational modification. http://purl.obolibrary.org/obo/MOD_00031 L-selenocysteine residue http://purl.obolibrary.org/obo/MOD_00868 natural, non-standard encoded residue A protein modification that effectively converts a source amino acid residue to an L-selenocysteine, a natural pretranslational modification. http://purl.obolibrary.org/obo/MOD_00033 crosslinked residues http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process A protein modification that crosslinks two or more amino acid residues with covalent bonds. http://purl.obolibrary.org/obo/MOD_00036 (2S,3R)-3-hydroxyaspartic acid http://purl.obolibrary.org/obo/MOD_01926 3-hydroxy-L-aspartic acid A protein modification that effectively converts an L-aspartic acid residue to (2S,3R)-3-hydroxyaspartic acid. http://purl.obolibrary.org/obo/MOD_00037 5-hydroxy-L-lysine http://purl.obolibrary.org/obo/MOD_01047 monohydroxylated lysine A protein modification that effectively converts an L-lysine residue to one of the diastereomeric 5-hydroxy-L-lysine residues. http://purl.obolibrary.org/obo/MOD_00038 3-hydroxy-L-proline http://purl.obolibrary.org/obo/MOD_01024 monohydroxylated proline A protein modification that effectively converts an L-proline residue to 3-hydroxy-L-proline. http://purl.obolibrary.org/obo/MOD_00039 4-hydroxy-L-proline http://purl.obolibrary.org/obo/MOD_01024 monohydroxylated proline A protein modification that effectively converts an L-proline residue to 4-hydroxy-L-proline http://purl.obolibrary.org/obo/MOD_00040 2-pyrrolidone-5-carboxylic acid (Gln) http://purl.obolibrary.org/obo/MOD_01160 deaminated residue A protein modification that effectively converts an L-glutamine residue to 2-pyrrolidone-5-carboxylic acid. http://purl.obolibrary.org/obo/MOD_00041 L-gamma-carboxyglutamic acid http://purl.obolibrary.org/obo/MOD_01152 carboxylated residue A protein modification that effectively converts an L-glutamic acid residue to L-gamma-carboxyglutamic acid. http://purl.obolibrary.org/obo/MOD_00042 L-aspartic 4-phosphoric anhydride http://purl.obolibrary.org/obo/MOD_00904 modified L-aspartic acid residue A protein modification that effectively converts an L-aspartic acid residue to L-aspartic 4-phosphoric anhydride. http://purl.obolibrary.org/obo/MOD_00045 3'-phospho-L-histidine http://purl.obolibrary.org/obo/MOD_00890 phosphorylated 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). http://purl.obolibrary.org/obo/MOD_00046 O-phospho-L-serine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to O-phospho-L-serine. http://purl.obolibrary.org/obo/MOD_00047 O-phospho-L-threonine http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue A protein modification that effectively converts an L-threonine residue to O-phospho-L-threonine. http://purl.obolibrary.org/obo/MOD_00048 O4'-phospho-L-tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively converts an L-tyrosine residue to O4'-phospho-L-tyrosine. http://purl.obolibrary.org/obo/MOD_00050 N-acetyl-L-alanine http://purl.obolibrary.org/obo/MOD_00901 modified L-alanine residue A protein modification that effectively converts an L-alanine residue to N-acetyl-L-alanine. http://purl.obolibrary.org/obo/MOD_00053 N-acetyl-L-glutamic acid http://purl.obolibrary.org/obo/MOD_00906 modified L-glutamic acid residue A protein modification that effectively converts an L-glutamic acid residue to N-acetyl-L-glutamic acid. http://purl.obolibrary.org/obo/MOD_00055 N-acetylglycine http://purl.obolibrary.org/obo/MOD_00908 modified glycine residue A protein modification that effectively converts a glycine residue to N-acetylglycine. http://purl.obolibrary.org/obo/MOD_00058 N-acetyl-L-methionine http://purl.obolibrary.org/obo/MOD_00913 modified L-methionine residue A protein modification that effectively converts an L-methionine to N-acetyl-L-methionine. http://purl.obolibrary.org/obo/MOD_00060 N-acetyl-L-serine http://purl.obolibrary.org/obo/MOD_01458 alpha-amino acetylated residue A protein modification that effectively converts an L-serine residue to N-acetyl-L-serine. http://purl.obolibrary.org/obo/MOD_00064 N6-acetyl-L-lysine http://purl.obolibrary.org/obo/MOD_00723 N-acetylated L-lysine A protein modification that effectively converts an L-lysine residue to N6-acetyl-L-lysine. http://purl.obolibrary.org/obo/MOD_00068 N-myristoylglycine http://purl.obolibrary.org/obo/MOD_00908 modified glycine residue A protein modification that effectively converts a glycine residue to N-myristoylglycine. http://purl.obolibrary.org/obo/MOD_00069 N-palmitoyl-L-cysteine http://purl.obolibrary.org/obo/MOD_01685 alpha-amino palmitoylated residue A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-L-cysteine. http://purl.obolibrary.org/obo/MOD_00076 symmetric dimethyl-L-arginine http://purl.obolibrary.org/obo/MOD_00783 dimethylated L-arginine A protein modification that effectively converts an L-arginine residue to symmetric dimethylarginine, N(omega),N'(omega)-dimethyl-L-arginine. http://purl.obolibrary.org/obo/MOD_00077 asymmetric dimethyl-L-arginine http://purl.obolibrary.org/obo/MOD_00783 dimethylated L-arginine A protein modification that effectively converts an L-arginine residue to asymmetric dimethylarginine, N(omega),N(omega)-dimethyl-L-arginine. http://purl.obolibrary.org/obo/MOD_00078 omega-N-methyl-L-arginine http://purl.obolibrary.org/obo/MOD_00414 monomethylated L-arginine A protein modification that effectively converts an L-arginine residue to N(omega)-methyl-L-arginine. http://purl.obolibrary.org/obo/MOD_00083 N6,N6,N6-trimethyl-L-lysine http://purl.obolibrary.org/obo/MOD_00663 methylated lysine A protein modification that effectively converts an L-lysine residue to N6,N6,N6-trimethyl-L-lysine. http://purl.obolibrary.org/obo/MOD_00084 N6,N6-dimethyl-L-lysine http://purl.obolibrary.org/obo/MOD_00663 methylated lysine A protein modification that effectively converts an L-lysine residue to N6,N6-dimethyl-L-lysine. http://purl.obolibrary.org/obo/MOD_00085 N6-methyl-L-lysine http://purl.obolibrary.org/obo/MOD_01683 monomethylated L-lysine A protein modification that effectively converts an L-lysine residue to N6-methyl-L-lysine. http://purl.obolibrary.org/obo/MOD_00087 N6-myristoyl-L-lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively converts an L-lysine residue to N6-myristoyl-L-lysine. http://purl.obolibrary.org/obo/MOD_00111 S-farnesyl-L-cysteine http://purl.obolibrary.org/obo/MOD_01110 isoprenylated cysteine A protein modification that effectively converts an L-cysteine residue to S-farnesyl-L-cysteine. http://purl.obolibrary.org/obo/MOD_00113 S-geranylgeranyl-L-cysteine http://purl.obolibrary.org/obo/MOD_01110 isoprenylated cysteine A protein modification that effectively converts an L-cysteine residue to S-geranylgeranyl-L-cysteine. http://purl.obolibrary.org/obo/MOD_00114 L-cysteine methyl ester http://purl.obolibrary.org/obo/MOD_01689 alpha-carboxyl methylated residue A protein modification that effectively converts an L-cysteine residue to L-cysteine methyl ester. http://purl.obolibrary.org/obo/MOD_00115 S-palmitoyl-L-cysteine http://purl.obolibrary.org/obo/MOD_01684 palmitoylated-L-cysteine A protein modification that effectively converts an L-cysteine residue to S-palmitoyl-L-cysteine. http://purl.obolibrary.org/obo/MOD_00126 N6-biotinyl-L-lysine http://purl.obolibrary.org/obo/MOD_01885 biotinylated residue A protein modification that effectively converts an L-lysine residue to N6-biotinyl-L-lysine. http://purl.obolibrary.org/obo/MOD_00127 N6-lipoyl-L-lysine http://purl.obolibrary.org/obo/MOD_01875 N6-acylated L-lysine A protein modification that effectively converts an L-lysine residue to N6-lipoyl-L-lysine. http://purl.obolibrary.org/obo/MOD_00128 N6-pyridoxal phosphate-L-lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively converts an L-lysine residue to N6-pyridoxal phosphate-L-lysine. http://purl.obolibrary.org/obo/MOD_00133 N6-(L-isoglutamyl)-L-lysine (Gln) http://purl.obolibrary.org/obo/MOD_02046 crosslinked L-glutamine residue 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. http://purl.obolibrary.org/obo/MOD_00159 O-phosphopantetheine-L-serine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively converts an L-serine residue to O-phosphopantetheine-L-serine. http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine http://purl.obolibrary.org/obo/MOD_00903 modified L-asparagine residue A protein modification that effectively converts an L-asparagine residue to an N4-glycosyl-L-asparagine. http://purl.obolibrary.org/obo/MOD_00164 O-(N-acetylamino)galactosyl-L-threonine http://purl.obolibrary.org/obo/MOD_01676 O-(N-acetylamino)hexosyl-L-threonine A protein modification that effectively converts an L-asparagine residue to O-(N-acetylaminogalactosyl)-L-threonine. http://purl.obolibrary.org/obo/MOD_00167 N-asparaginyl-glycosylphosphatidylinositolethanolamine http://purl.obolibrary.org/obo/MOD_00903 modified L-asparagine residue A protein modification that effectively converts an L-asparagine residue to N-asparaginyl-glycosylphosphatidylinositolethanolamine. http://purl.obolibrary.org/obo/MOD_00213 chondroitin sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine http://purl.obolibrary.org/obo/MOD_00002 O-glycosyl-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. http://purl.obolibrary.org/obo/MOD_00215 heparan sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine http://purl.obolibrary.org/obo/MOD_00002 O-glycosyl-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. http://purl.obolibrary.org/obo/MOD_00219 L-citrulline http://purl.obolibrary.org/obo/MOD_00902 modified L-arginine residue A protein modification that effectively converts an L-arginine residue to L-citrulline. http://purl.obolibrary.org/obo/MOD_00222 2'-alpha-mannosyl-L-tryptophan http://purl.obolibrary.org/obo/MOD_00918 modified L-tryptophan residue A protein modification that effectively converts an L-tryptophan residue to 2'-alpha-mannosyl-L-tryptophan. http://purl.obolibrary.org/obo/MOD_00235 S-nitrosyl-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-nitrosyl-L-cysteine. http://purl.obolibrary.org/obo/MOD_00237 L-beta-methylthioaspartic acid http://purl.obolibrary.org/obo/MOD_00904 modified L-aspartic acid residue A protein modification that effectively converts an L-aspartic acid residue to L-beta-methylthioaspartic acid. http://purl.obolibrary.org/obo/MOD_00295 O-octanoyl-L-serine http://purl.obolibrary.org/obo/MOD_02003 O3-acylated L-serine A protein modification that effectively converts an L-serine residue to O-octanoyl-L-serine. http://purl.obolibrary.org/obo/MOD_00300 L-glutamyl-5-poly(ADP-ribose) http://purl.obolibrary.org/obo/MOD_00906 modified L-glutamic acid residue A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl-5-poly(ADP-ribose). http://purl.obolibrary.org/obo/MOD_00314 glycine cholesterol ester http://purl.obolibrary.org/obo/MOD_01155 lipoconjugated residue A protein modification that effectively converts a glycine residue to glycine cholesterol ester. http://purl.obolibrary.org/obo/MOD_00394 monoacetylated residue http://purl.obolibrary.org/obo/MOD_02078 acetylated residue A protein modification that effectively replaces one hydrogen atom with one acetyl group. http://purl.obolibrary.org/obo/MOD_00396 O-glycosylated residue http://purl.obolibrary.org/obo/MOD_00693 glycosylated residue A protein modification that effectively replaces a residue hydrogen atom on an oxygen with a carbohydrate-like group through a glycosidic bond. http://purl.obolibrary.org/obo/MOD_00414 monomethylated L-arginine http://purl.obolibrary.org/obo/MOD_00599 monomethylated residue A protein modification that effectively replaces one hydrogen atom of an L-arginine residue with one methyl group. http://purl.obolibrary.org/obo/MOD_00427 methylated residue http://purl.obolibrary.org/obo/MOD_00001 alkylated residue A protein modification that effectively replaces a hydrogen atom with a methyl group. http://purl.obolibrary.org/obo/MOD_00437 farnesylated residue http://purl.obolibrary.org/obo/MOD_00703 isoprenylated residue A protein modification that effectively replaces a hydrogen atom with a farnesyl group. http://purl.obolibrary.org/obo/MOD_00438 myristoylated residue http://purl.obolibrary.org/obo/MOD_01155 lipoconjugated residue A protein modification that effectively replaces a hydrogen atom with a myristoyl group. http://purl.obolibrary.org/obo/MOD_00440 palmitoylated residue http://purl.obolibrary.org/obo/MOD_01155 lipoconjugated residue A protein modification that effectively replaces a hydrogen atom with a palmitoyl group. http://purl.obolibrary.org/obo/MOD_00448 mono-N-acetylaminoglucosylated residue http://purl.obolibrary.org/obo/MOD_01673 N-acetylaminohexosylated residue A protein modification that effectively replaces a hydrogen atom with an N-acetylaminoglucose group through a glycosidic bond. http://purl.obolibrary.org/obo/MOD_00599 monomethylated residue http://purl.obolibrary.org/obo/MOD_00427 methylated residue A protein modification that effectively replaces one hydrogen atom with one methyl group. http://purl.obolibrary.org/obo/MOD_00601 cyclized residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process 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. http://purl.obolibrary.org/obo/MOD_00649 acylated residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process A protein modification that effectively replaces a hydrogen atom with an acyl group. http://purl.obolibrary.org/obo/MOD_00663 methylated lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively converts an L-lysine residue to a methylated lysine. http://purl.obolibrary.org/obo/MOD_00666 octanoylated residue http://purl.obolibrary.org/obo/MOD_01155 lipoconjugated residue A protein modification that effectively replaces a hydrogen atom with an octanoyl group. http://purl.obolibrary.org/obo/MOD_00670 N-acylated residue http://purl.obolibrary.org/obo/MOD_00649 acylated residue A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an acyl group. http://purl.obolibrary.org/obo/MOD_00677 hydroxylated residue http://purl.obolibrary.org/obo/MOD_00679 carbon oxygenated residue A protein modification that effectively replaces a hydrogen atom with an hydroxyl group. http://purl.obolibrary.org/obo/MOD_00693 glycosylated residue http://purl.obolibrary.org/obo/MOD_00764 glycoconjugated residue A protein modification that effectively replaces a hydrogen atom with an carbohydrate-like group through a glycosidic bond. http://purl.obolibrary.org/obo/MOD_00696 phosphorylated residue http://purl.obolibrary.org/obo/MOD_00861 phosphorus containing modified residue A protein modification that effectively replaces a hydrogen atom with a phosphono group (H2PO3 or 'phosphate'). http://purl.obolibrary.org/obo/MOD_00701 nucleotide or nucleic acid modified residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process 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. http://purl.obolibrary.org/obo/MOD_00703 isoprenylated residue http://purl.obolibrary.org/obo/MOD_01155 lipoconjugated 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. http://purl.obolibrary.org/obo/MOD_00723 N-acetylated L-lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively converts an L-lysine residue to either N2-acetyl-L-lysine, or N6-acetyl-L-lysine. http://purl.obolibrary.org/obo/MOD_00752 monoadenosine diphosphoribosyl (ADP-ribosyl) modified residue http://purl.obolibrary.org/obo/MOD_02087 adenosine 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. http://purl.obolibrary.org/obo/MOD_00754 brominated residue http://purl.obolibrary.org/obo/MOD_00694 halogen containing residue A protein modification that effectively substitutes a bromine atom for a hydrogen atom. http://purl.obolibrary.org/obo/MOD_00764 glycoconjugated residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process 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. http://purl.obolibrary.org/obo/MOD_00783 dimethylated L-arginine http://purl.obolibrary.org/obo/MOD_00658 methylated arginine A protein modification that effectively replaces two hydrogen atoms of an L-arginine residue with two methyl groups. http://purl.obolibrary.org/obo/MOD_00805 O-(N-acetylamino)glucosyl-L-serine http://purl.obolibrary.org/obo/MOD_00448 mono-N-acetylaminoglucosylated residue A protein modification that effectively converts an L-serine residue to O3-(N-acetylaminoglucosyl)-L-serine. http://purl.obolibrary.org/obo/MOD_00806 O-(N-acetylamino)glucosyl-L-threonine http://purl.obolibrary.org/obo/MOD_00448 mono-N-acetylaminoglucosylated residue A protein modification that effectively converts an L-threonine residue to O3-(N-acetylaminoglucosyl)-L-threonine. http://purl.obolibrary.org/obo/MOD_00812 O-fucosyl-L-serine http://purl.obolibrary.org/obo/MOD_00614 fucosylated residue A protein modification that effectively converts an L-serine residue to an O-fucosylserine. http://purl.obolibrary.org/obo/MOD_00813 O-fucosyl-L-threonine http://purl.obolibrary.org/obo/MOD_00614 fucosylated residue A protein modification that effectively converts an threonine residue to an O-fucosylthreonine. http://purl.obolibrary.org/obo/MOD_00814 O-xylosyl-L-serine http://purl.obolibrary.org/obo/MOD_00002 O-glycosyl-L-serine A protein modification that effectively converts an L-serine residue to O3-xylosylserine. http://purl.obolibrary.org/obo/MOD_00818 glycosylphosphatidylinositolated residue http://purl.obolibrary.org/obo/MOD_01155 lipoconjugated residue A protein modification that effectively converts a residue to a glycosylphosphatidylinositolethanolamidated. http://purl.obolibrary.org/obo/MOD_00831 N4-(N-acetylamino)glucosyl-L-asparagine http://purl.obolibrary.org/obo/MOD_00448 mono-N-acetylaminoglucosylated residue A protein modification that effectively converts an L-asparagine residue to N4-(N-acetylaminoglucosyl)-L-asparagine. http://purl.obolibrary.org/obo/MOD_00901 modified L-alanine residue http://purl.obolibrary.org/obo/MOD_01157 protein modification categorized by amino acid modified A protein modification that modifies an L-alanine. http://purl.obolibrary.org/obo/MOD_00902 modified L-arginine residue http://purl.obolibrary.org/obo/MOD_01157 protein modification categorized by amino acid modified A protein modification that modifies an L-arginine residue. http://purl.obolibrary.org/obo/MOD_00903 modified L-asparagine residue http://purl.obolibrary.org/obo/MOD_01157 protein modification categorized by amino acid modified A protein modification that modifies an L-asparagine residue. http://purl.obolibrary.org/obo/MOD_00904 modified L-aspartic acid residue http://purl.obolibrary.org/obo/MOD_01157 protein modification categorized by amino acid modified A protein modification that modifies an L-aspartic acid residue. http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue http://purl.obolibrary.org/obo/MOD_01157 protein modification categorized by amino acid modified A protein modification that modifies an L-cysteine residue. http://purl.obolibrary.org/obo/MOD_00906 modified L-glutamic acid residue http://purl.obolibrary.org/obo/MOD_01157 protein modification categorized by amino acid modified A protein modification that modifies an L-glutamic acid residue. http://purl.obolibrary.org/obo/MOD_00907 modified L-glutamine residue http://purl.obolibrary.org/obo/MOD_01157 protein modification categorized by amino acid modified A protein modification that modifies an L-glutamine residue. http://purl.obolibrary.org/obo/MOD_00908 modified glycine residue http://purl.obolibrary.org/obo/MOD_01157 protein modification categorized by amino acid modified A protein modification that modifies a glycine residue. http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue http://purl.obolibrary.org/obo/MOD_01157 protein modification categorized by amino acid modified A protein modification that modifies an L-histidine residue. http://purl.obolibrary.org/obo/MOD_00910 modified L-isoleucine residue http://purl.obolibrary.org/obo/MOD_01157 protein modification categorized by amino acid modified A protein modification that modifies an L-isoleucine residue. http://purl.obolibrary.org/obo/MOD_00911 modified L-leucine residue http://purl.obolibrary.org/obo/MOD_01157 protein modification categorized by amino acid modified A protein modification that modifies an L-leucine residue. http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue http://purl.obolibrary.org/obo/MOD_01157 protein modification categorized by amino acid modified A protein modification that modifies an L-lysine residue. http://purl.obolibrary.org/obo/MOD_00913 modified L-methionine residue http://purl.obolibrary.org/obo/MOD_01157 protein modification categorized by amino acid modified A protein modification that modifies an L-methionine residue. http://purl.obolibrary.org/obo/MOD_00914 modified L-phenylalanine residue http://purl.obolibrary.org/obo/MOD_01157 protein modification categorized by amino acid modified A protein modification that modifies an L-phenylalanine residue. http://purl.obolibrary.org/obo/MOD_00915 modified L-proline residue http://purl.obolibrary.org/obo/MOD_01157 protein modification categorized by amino acid modified A protein modification that modifies an L-proline residue. http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue http://purl.obolibrary.org/obo/MOD_01157 protein modification categorized by amino acid modified A protein modification that modifies an L-serine residue. http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue http://purl.obolibrary.org/obo/MOD_01157 protein modification categorized by amino acid modified A protein modification that modifies an L-threonine residue. http://purl.obolibrary.org/obo/MOD_00918 modified L-tryptophan residue http://purl.obolibrary.org/obo/MOD_01157 protein modification categorized by amino acid modified A protein modification that modifies an L-tryptophan residue. http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue http://purl.obolibrary.org/obo/MOD_01157 protein modification categorized by amino acid modified A protein modification that modifies an L-tyrosine residue. http://purl.obolibrary.org/obo/MOD_00920 modified L-valine residue http://purl.obolibrary.org/obo/MOD_01157 protein modification categorized by amino acid modified A protein modification that modifies an L-valine residue. http://purl.obolibrary.org/obo/MOD_01048 2-pyrrolidone-5-carboxylic acid http://purl.obolibrary.org/obo/MOD_00601 cyclized residue A protein modification that effectively converts a source amino acid residue to 2-pyrrolidone-5-carboxylic acid. http://purl.obolibrary.org/obo/MOD_01110 isoprenylated cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively replaces a hydrogen atom of an L-cysteine residue with a group derived from an isoprene polymer, such as a geranyl (C10), farnesyl (C15) or geranylgeranyl (C20). http://purl.obolibrary.org/obo/MOD_01119 S-geranylgeranyl-L-cysteine methyl ester http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively converts an L-cysteine residue to S-geranylgeranyl-L-cysteine methyl ester. http://purl.obolibrary.org/obo/MOD_01148 ubiquitinylated lysine http://purl.obolibrary.org/obo/MOD_02051 crosslinked L-lysine residue A protein modification that effectively crosslinks the N6-amino of a peptidyl lysine with the carboxyl-terminal glycine of a ubiquitin. http://purl.obolibrary.org/obo/MOD_01149 sumoylated lysine http://purl.obolibrary.org/obo/MOD_02051 crosslinked L-lysine residue A protein modification that effectively crosslinks the N6-amino of a peptidyl lysine with the carboxyl-terminal glycine of a sumo (Small Ubiquitin-related MOdifier) protein. http://purl.obolibrary.org/obo/MOD_01150 neddylated lysine http://purl.obolibrary.org/obo/MOD_02051 crosslinked L-lysine residue A protein modification that effectively crosslinks the N6-amino of a peptidyl lysine with the carboxyl-terminal glycine of a nedd8 protein. http://purl.obolibrary.org/obo/MOD_01152 carboxylated residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process A protein modification that effectively replaces a hydrogen atom with a carboxylic acid group. http://purl.obolibrary.org/obo/MOD_01155 lipoconjugated residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process A protein modification that effectively results from forming an adduct with a compound containing a lipid-like group either through acylation, alkylation, or amidation. http://purl.obolibrary.org/obo/MOD_01160 deaminated residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process A protein modification that effectively results in the loss of an ammonia, usually by a process of vicinal dehydration, rearrangement, and rehydration with release of ammonia, resulting in a loss of nitrogen with no gain of oxygen. http://purl.obolibrary.org/obo/MOD_01240 ubiquitination signature tetrapeptidyl lysine http://purl.obolibrary.org/obo/MOD_02051 crosslinked L-lysine residue A protein modification that crosslinks the N6-amino of a peptidyl lysine with the carboxyl of leucyl-arginyl-glycyl-glycine, the C-terminal tetrapeptide of ubiquitin. http://purl.obolibrary.org/obo/MOD_01352 nitrated L-tyrosine http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that effectively converts an L-tyrosine residue to a nitrated L-tyrosine. http://purl.obolibrary.org/obo/MOD_01399 N6-(ADP-ribosyl)-L-lysine http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that effectively converts an L-lysine residue to an N6-(ADP-ribosyl)-L-lysine. http://purl.obolibrary.org/obo/MOD_01683 monomethylated L-lysine http://purl.obolibrary.org/obo/MOD_00663 methylated lysine A protein modification that effectively replaces one hydrogen atom of an L-lysine residue with one methyl group. http://purl.obolibrary.org/obo/MOD_01786 3'-nitro-L-tyrosine http://purl.obolibrary.org/obo/MOD_01352 nitrated L-tyrosine A protein modification that effectively converts an L-tyrosine residue to 3'-nitro-L-tyrosine. http://purl.obolibrary.org/obo/MOD_01885 biotinylated residue http://purl.obolibrary.org/obo/MOD_00649 acylated residue A protein modification that effectively replaces a hydrogen atom with a biotinyl group. http://purl.obolibrary.org/obo/MOD_01886 thiolated residue http://purl.obolibrary.org/obo/MOD_00860 sulfur containing modified residue A protein modification that effectively replaces a hydrogen atom with an sulfanyl or substituted sulfanyl group. http://purl.obolibrary.org/obo/MOD_02039 aminated residue http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process A protein modification that effectively replaces a hydrogen group with a amino group http://purl.obolibrary.org/obo/MOD_02040 crosslinked L-alanine residue http://purl.obolibrary.org/obo/MOD_00901 modified L-alanine residue A protein modification that contains an L-alanine residue crosslinked to one or more amino acid residues. http://purl.obolibrary.org/obo/MOD_02041 crosslinked L-arginine residue http://purl.obolibrary.org/obo/MOD_00902 modified L-arginine residue A protein modification that contains an L-arginine residue crosslinked to one or more amino acid residues. http://purl.obolibrary.org/obo/MOD_02042 crosslinked L-asparagine residue http://purl.obolibrary.org/obo/MOD_00903 modified L-asparagine residue A protein modification that contains an L-asparagine residue crosslinked to one or more amino acid residues. http://purl.obolibrary.org/obo/MOD_02043 crosslinked L-aspartic acid residue http://purl.obolibrary.org/obo/MOD_00904 modified L-aspartic acid residue A protein modification that contains an L-aspartic acid residue crosslinked to one or more amino acid residues. http://purl.obolibrary.org/obo/MOD_02044 crosslinked L-cysteine residue http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that contains an L-cysteine residue crosslinked to one or more amino acid residues. http://purl.obolibrary.org/obo/MOD_02045 crosslinked L-glutamic acid residue http://purl.obolibrary.org/obo/MOD_00906 modified L-glutamic acid residue A protein modification that contains an L-glutamic acid residue crosslinked to one or more amino acid residues. http://purl.obolibrary.org/obo/MOD_02046 crosslinked L-glutamine residue http://purl.obolibrary.org/obo/MOD_00907 modified L-glutamine residue A protein modification that contains an L-glutamine residue crosslinked to one or more amino acid residues. http://purl.obolibrary.org/obo/MOD_02047 crosslinked glycine residue http://purl.obolibrary.org/obo/MOD_00908 modified glycine residue A protein modification that contains a glycine residue crosslinked to one or more amino acid residues. http://purl.obolibrary.org/obo/MOD_02048 crosslinked L-histidine residue http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that contains an L-histidine residue crosslinked to one or more amino acid residues. http://purl.obolibrary.org/obo/MOD_02049 crosslinked L-isoleucine residue http://purl.obolibrary.org/obo/MOD_00910 modified L-isoleucine residue A protein modification that contains an L-isoleucine residue crosslinked to one or more amino acid residues. http://purl.obolibrary.org/obo/MOD_02050 crosslinked L-leucine residue http://purl.obolibrary.org/obo/MOD_00911 modified L-leucine residue A protein modification that contains an L-leucine residue crosslinked to one or more amino acid residues. http://purl.obolibrary.org/obo/MOD_02051 crosslinked L-lysine residue http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that contains an L-lysine residue crosslinked to one or more amino acid residues. http://purl.obolibrary.org/obo/MOD_02052 crosslinked L-methionine residue http://purl.obolibrary.org/obo/MOD_00913 modified L-methionine residue A protein modification that contains an L-methionine residue crosslinked to one or more amino acid residues. http://purl.obolibrary.org/obo/MOD_02053 crosslinked L-phenylalanine residue http://purl.obolibrary.org/obo/MOD_00914 modified L-phenylalanine residue A protein modification that contains an L-phenylalanine residue crosslinked to one or more amino acid residues. http://purl.obolibrary.org/obo/MOD_02054 crosslinked L-proline residue http://purl.obolibrary.org/obo/MOD_00915 modified L-proline residue A protein modification that contains an L-proline residue crosslinked to one or more amino acid residues. http://purl.obolibrary.org/obo/MOD_02055 crosslinked L-serine residue http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that contains an L-serine residue crosslinked to one or more amino acid residues. http://purl.obolibrary.org/obo/MOD_02056 crosslinked L-threonine residue http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue A protein modification that contains an L-threonine residue crosslinked to one or more amino acid residues. http://purl.obolibrary.org/obo/MOD_02057 crosslinked L-tryptophan residue http://purl.obolibrary.org/obo/MOD_00918 modified L-tryptophan residue A protein modification that contains an L-tryptophan residue crosslinked to one or more amino acid residues. http://purl.obolibrary.org/obo/MOD_02058 crosslinked L-tyrosine residue http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that contains an L-tyrosine residue crosslinked to one or more amino acid residues. http://purl.obolibrary.org/obo/MOD_02059 crosslinked L-valine residue http://purl.obolibrary.org/obo/MOD_00920 modified L-valine residue A protein modification that contains an L-valine residue crosslinked to one or more amino acid residues. http://purl.obolibrary.org/obo/MOD_02061 crosslinked L-selenocysteine residue http://purl.obolibrary.org/obo/MOD_01158 modified L-selenocysteine residue A protein modification that contains an L-selenocysteine residue crosslinked to one or more amino acid residues. http://purl.obolibrary.org/obo/MOD_02062 crosslinked N-formyl-L-methionine residue http://purl.obolibrary.org/obo/MOD_01450 modified N-formyl-L-methionine residue A protein modification that contains an N-formyl-L-methionine residue crosslinked to one or more amino acid residues. http://purl.obolibrary.org/obo/MOD_02066 metal or metal cluster coordinated L-aspartic acid residue http://purl.obolibrary.org/obo/MOD_00904 modified L-aspartic acid residue A protein modification that contains an L-aspartic acid residue coordinated to one or more metal atoms or metal clusters. http://purl.obolibrary.org/obo/MOD_02067 metal or metal cluster coordinated L-cysteine residue http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that contains an L-cysteine residue coordinated to one or more metal atoms or metal clusters. http://purl.obolibrary.org/obo/MOD_02068 metal or metal cluster coordinated L-glutamic acid residue http://purl.obolibrary.org/obo/MOD_00906 modified L-glutamic acid residue A protein modification that contains an L-glutamic acid residue coordinated to one or more metal atoms or metal clusters. http://purl.obolibrary.org/obo/MOD_02070 metal or metal cluster coordinated L-histidine residue http://purl.obolibrary.org/obo/MOD_00909 modified L-histidine residue A protein modification that contains an L-histidine residue coordinated to one or more metal atoms or metal clusters. http://purl.obolibrary.org/obo/MOD_02071 metal or metal cluster coordinated L-methionine residue http://purl.obolibrary.org/obo/MOD_00913 modified L-methionine residue A protein modification that contains an L-methionine residue coordinated to one or more metal atoms or metal clusters. http://purl.obolibrary.org/obo/MOD_02072 metal or metal cluster coordinated L-serine residue http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that contains an L-serine residue coordinated to one or more metal atoms or metal clusters. http://purl.obolibrary.org/obo/MOD_02073 metal or metal cluster coordinated L-selenocysteine residue http://purl.obolibrary.org/obo/MOD_01158 modified L-selenocysteine residue A protein modification that contains an L-selenocysteine residue coordinated to one or more metal atoms or metal clusters. http://purl.obolibrary.org/obo/MOD_02074 metal or metal cluster coordinated L-lysine residue http://purl.obolibrary.org/obo/MOD_00912 modified L-lysine residue A protein modification that contains an L-lysine residue coordinated to one or more metal atoms or metal clusters. http://purl.obolibrary.org/obo/MOD_02075 metal or metal cluster coordinated L-tyrosine residue http://purl.obolibrary.org/obo/MOD_00919 modified L-tyrosine residue A protein modification that contains an L-tyrosine residue coordinated to one or more metal atoms or metal clusters. http://purl.obolibrary.org/obo/MOD_02076 metal or metal cluster coordinated L-arginine residue http://purl.obolibrary.org/obo/MOD_00902 modified L-arginine residue A protein modification that contains an L-arginine residue coordinated to one or more metal atoms or metal clusters. http://purl.obolibrary.org/obo/MOD_02060 crosslinked D-asparagine residue http://purl.obolibrary.org/obo/MOD_02097 modified D-asparagine residue A protein modification that contains an D-asparagine residue crosslinked to one or more amino acid residues. http://purl.obolibrary.org/obo/MOD_02063 crosslinked D-phenylalanine residue http://purl.obolibrary.org/obo/MOD_00201 D-phenylalanine A protein modification that contains an D-phenylalanine residue crosslinked to one or more amino acid residues. http://purl.obolibrary.org/obo/MOD_02064 crosslinked D-serine residue http://purl.obolibrary.org/obo/MOD_00202 D-serine (Ser) A protein modification that contains an D-serine residue crosslinked to one or more amino acid residues. http://purl.obolibrary.org/obo/MOD_02065 metal or metal cluster coordinated L-alanine residue http://purl.obolibrary.org/obo/MOD_00901 modified L-alanine residue A protein modification that contains an L-alanine residue coordinated to one or more metal atoms or metal clusters. http://purl.obolibrary.org/obo/MOD_02069 metal or metal cluster coordinated L-glutamine residue http://purl.obolibrary.org/obo/MOD_00907 modified L-glutamine residue A protein modification that contains an L-glutamine residue coordinated to one or more metal atoms or metal clusters. http://purl.obolibrary.org/obo/MOD_01109 9-fluorenylmethyloxycarbonyl (Fmoc) http://purl.obolibrary.org/obo/MOD_00848 reagent derivatized residue modification from DeltaMass http://purl.obolibrary.org/obo/MOD_02088 natural, standard, encoded residue substitution http://purl.obolibrary.org/obo/MOD_01156 protein modification categorized by chemical process A protein modification that effectively replaces a natural, standard, encoded residue. http://purl.obolibrary.org/obo/MOD_02001 stearoylated residue http://purl.obolibrary.org/obo/MOD_01155 lipoconjugated residue A protein modification that effectively replaces a hydrogen atom with a stearoyl group. http://purl.obolibrary.org/obo/MOD_02002 S-palmitoleylated residue http://purl.obolibrary.org/obo/MOD_01423 palmitoleylated residue A protein modification that effectively replaces a residue sulfanyl group with a palmitoleylsulfanyl group. http://purl.obolibrary.org/obo/MOD_02003 O3-acylated L-serine http://purl.obolibrary.org/obo/MOD_00916 modified L-serine residue A protein modification that effectively replaces an O3-hydroxy hydrogen atom of L-serine with an acyl group. http://purl.obolibrary.org/obo/MOD_02004 O3-acylated L-threonine http://purl.obolibrary.org/obo/MOD_00917 modified L-threonine residue A protein modification that effectively replaces an O3-hydroxy hydrogen atom of L-threonine with an acyl group. http://purl.obolibrary.org/obo/MOD_02005 S-acylated L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively replaces an sulfanyl hydrogen atom of L-cysteine with an acyl group. http://purl.obolibrary.org/obo/MOD_02006 S-stearoylated residue http://purl.obolibrary.org/obo/MOD_02001 stearoylated residue A protein modification that effectively replaces a residue sulfanyl group with a stearoylsulfanyl group. http://purl.obolibrary.org/obo/MOD_02007 N6-palmitoleyl-L-lysine http://purl.obolibrary.org/obo/MOD_02008 N-palmitoleylated residue A protein modification that effectively converts an L-lysine residue to N6-palmitoleyl-L-lysine. http://purl.obolibrary.org/obo/MOD_02008 N-palmitoleylated residue http://purl.obolibrary.org/obo/MOD_00670 N-acylated residue A protein modification that effectively replaces a residue amino group with a palmitoleylamino group. http://purl.obolibrary.org/obo/MOD_02009 N6-stearoyl-L-lysine http://purl.obolibrary.org/obo/MOD_02010 N-stearoylated residue A protein modification that effectively converts an L-lysine residue to N6-stearoyl-L-lysine. http://purl.obolibrary.org/obo/MOD_02010 N-stearoylated residue http://purl.obolibrary.org/obo/MOD_02001 stearoylated residue A protein modification that effectively replaces a residue amino group with a stearoylamino group. http://purl.obolibrary.org/obo/MOD_02011 N-oleoylated residue http://purl.obolibrary.org/obo/MOD_02012 oleoylated residue A protein modification that effectively replaces a residue amino group with a oleoylamino group. http://purl.obolibrary.org/obo/MOD_02012 oleoylated residue http://purl.obolibrary.org/obo/MOD_01155 lipoconjugated residue A protein modification that effectively replaces a hydrogen atom with a oleoyl group. http://purl.obolibrary.org/obo/MOD_02013 N6-linoloyl-L-lysine http://purl.obolibrary.org/obo/MOD_02014 N-linoloylated residue A protein modification that effectively converts an L-lysine residue to N6-linoloyl-L-lysine. http://purl.obolibrary.org/obo/MOD_02014 N-linoloylated residue http://purl.obolibrary.org/obo/MOD_02015 linoloylated residue A protein modification that effectively replaces a residue amino group with a linoloylamino group. http://purl.obolibrary.org/obo/MOD_02015 linoloylated residue http://purl.obolibrary.org/obo/MOD_01155 lipoconjugated residue A protein modification that effectively replaces a hydrogen atom with a linoloyl group. http://purl.obolibrary.org/obo/MOD_02016 N6-arachidonoyl-L-lysine http://purl.obolibrary.org/obo/MOD_02017 N-arachidonoylated residue A protein modification that effectively converts an L-lysine residue to N6-arachidonoyl-L-lysine. http://purl.obolibrary.org/obo/MOD_02017 N-arachidonoylated residue http://purl.obolibrary.org/obo/MOD_02018 arachidonoylated residue A protein modification that effectively replaces a residue amino group with an arachidonoylamino group. http://purl.obolibrary.org/obo/MOD_02018 arachidonoylated residue http://purl.obolibrary.org/obo/MOD_01155 lipoconjugated residue A protein modification that effectively replaces a hydrogen atom with an arachidonoyl group. http://purl.obolibrary.org/obo/MOD_02019 N6-timnodonoyl-L-lysine http://purl.obolibrary.org/obo/MOD_02020 N-timnodonoylated residue A protein modification that effectively converts an L-lysine residue to N6-timnodonoyl-L-lysine. http://purl.obolibrary.org/obo/MOD_02020 N-timnodonoylated residue http://purl.obolibrary.org/obo/MOD_02021 timnodonoylated residue A protein modification that effectively replaces a residue amino group with a timnodonoylamino group. http://purl.obolibrary.org/obo/MOD_02021 timnodonoylated residue http://purl.obolibrary.org/obo/MOD_01155 lipoconjugated residue A protein modification that effectively replaces a hydrogen atom with a timnodonoyl group. http://purl.obolibrary.org/obo/MOD_02022 N6-cervonoyl-L-lysine http://purl.obolibrary.org/obo/MOD_02023 N-cervonoylated residue A protein modification that effectively converts an L-lysine residue to N6-cervonoyl-L-lysine. http://purl.obolibrary.org/obo/MOD_02023 N-cervonoylated residue http://purl.obolibrary.org/obo/MOD_02024 cervonoylated residue A protein modification that effectively replaces a residue amino group with a cervonoylamino group. http://purl.obolibrary.org/obo/MOD_02024 cervonoylated residue http://purl.obolibrary.org/obo/MOD_01155 lipoconjugated residue A protein modification that effectively replaces a hydrogen atom with a cervonoyl group. http://purl.obolibrary.org/obo/MOD_02025 5-glutaminyl glutamic acid http://purl.obolibrary.org/obo/MOD_00906 modified L-glutamic acid residue A protein modification that effectively converts the alpha amino group of a glutamine residue to glutaminyl glutamic acid by forming an isopeptide bond with the side chain carboxyl group of a free glutamic acid. http://purl.obolibrary.org/obo/MOD_02026 S-(cysteinyl-glycyl)-L-cysteine http://purl.obolibrary.org/obo/MOD_00905 modified L-cysteine residue A protein modification that effectively cross-links an L-cysteinyl-L-glycine dipeptide and an L-cysteine residue by a disulfide bond to form S-(cysteinyl-glycyl)-L-cysteine. http://purl.obolibrary.org/obo/MOD_02027 urmylated lysine http://purl.obolibrary.org/obo/MOD_02051 crosslinked L-lysine residue A protein modification that effectively crosslinks the N6-amino of a peptidyl lysine with the carboxyl-terminal glycine of a URM1 protein. http://purl.obolibrary.org/obo/MOD_02028 iTRAQ4plex reporter+balance reagent acylated residue, average mass modification http://purl.obolibrary.org/obo/MOD_01709 iTRAQ4plex reporter+balance reagent N-acylated residue A protein modification that effectively replaces a hydrogen atom of a residue with one of the Applied Biosystems iTRAQ4plex reagent reporter+balance groups. http://purl.obolibrary.org/obo/MOD_02029 cis-peptidyl-L-proline http://purl.obolibrary.org/obo/MOD_00915 modified L-proline residue A protein modification that effectively specifies the boundary conformation of two adjacent source amino acid residues, the second (C-term side) being a L-proline, where the carbonyl group of the amide bond of the N-side of the L-proline is positioned such that the organodiyl group is in the cis orientation (omega=0) http://purl.obolibrary.org/obo/MOD_02030 trans-peptidyl-L-proline http://purl.obolibrary.org/obo/MOD_00915 modified L-proline residue A protein modification that effectively specifies the boundary conformation of two adjacent source amino acid residues, the second (C-term side) being a L-proline, where the carbonyl group of the amide bond of the N-side of the L-proline is positioned such that the organodiyl group is in the trans orientation (omega=180) http://purl.obolibrary.org/obo/MOD_02031 dHex1Hex4HexNAc5 N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine modification from Unimod N-linked glycosylation, dHex Hex(4) HexNAc(5) http://purl.obolibrary.org/obo/MOD_02032 dHex2Hex4HexNAc5 N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine modification from Unimod N-linked glycosylation, dHex(2) Hex(4) HexNAc(5) http://purl.obolibrary.org/obo/MOD_02033 dHex1Hex5HexNAc3 N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine modification from Unimod N-linked glycosylation, dHex Hex(5) HexNAc(3) http://purl.obolibrary.org/obo/MOD_02034 dHex1Hex3HexNAc6 N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine modification from Unimod N-linked glycosylation, dHex Hex(3) HexNAc(6) http://purl.obolibrary.org/obo/MOD_02035 dHex1Hex6HexNAc3 N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine modification from Unimod N-linked glycosylation, dHex Hex(6) HexNAc(3) http://purl.obolibrary.org/obo/MOD_02036 Hex9HexNAc2 N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine modification from Unimod N-linked glycosylation, Hex(9)HexNAc(2) http://purl.obolibrary.org/obo/MOD_02037 Hex7HexNAc2 N4-glycosylated asparagine http://purl.obolibrary.org/obo/MOD_00160 N4-glycosyl-L-asparagine modification from Unimod N-linked glycosylation, Hex(7) HexNAc(2) http://purl.obolibrary.org/obo/MOD_02038 monomethylated L-histidine http://purl.obolibrary.org/obo/MOD_00599 monomethylated residue A protein modification that effectively replaces one hydrogen atom of an L-histidine residue with one methyl group. http://purl.obolibrary.org/obo/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. http://purl.obolibrary.org/obo/MOD_00004 artifact Artifact entry from Unimod - OBSOLETE because organizational use is no longer required. http://purl.obolibrary.org/obo/MOD_00008 common Entry from Unimod representing one or more entries in RESID. OBSOLETE because organizational use is no longer required. http://purl.obolibrary.org/obo/MOD_00407 residue methyl ester 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. http://purl.obolibrary.org/obo/MOD_00411 O18 label modification from Unimod Isotopic label. OBSOLETE because Unimod:18 is now merged with entry 258 remap to MOD:00581 'single 018 label' http://purl.obolibrary.org/obo/MOD_00412 oxidation modification from Unimod artifact. OBSOLETE because Unimod entry 19 is now merged with Unimod 35 remap to MOD:00425 'monohydroxylated residue'. http://purl.obolibrary.org/obo/MOD_00415 phosphorylation without neutral loss modification from Unimod - OBSOLETE because Unimod entry 22 is now merged with entry 21 remap to MOD:00696 'phosphorylated residue'. http://purl.obolibrary.org/obo/MOD_00450 acetate labeling reagent light form (K) OBSOLETE because this isotopic label from Unimod entry 57 is deprecated http://purl.obolibrary.org/obo/MOD_00496 reductive amination-D OBSOLETE because Unimod entry 125 is merged with entry 199, remap to id: MOD:00552 http://purl.obolibrary.org/obo/MOD_00507 5-dimethylaminonaphthalene-1-sulfonyl OBSOLETE because redundant, replaced by MOD:01653. Remap to MOD:01653. http://purl.obolibrary.org/obo/MOD_00508 ISD a-series (C-Term) 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 http://purl.obolibrary.org/obo/MOD_00536 L-serine to L-alanine replacement OBSOLETE because Unimod 179 merged with Unimod 447 remap to ??? a protein modification that replaces an L-serine residue with an L-alanine residue http://purl.obolibrary.org/obo/MOD_00539 threonine reduced to aminobutynate OBSOLETE because Unimod 179 merged wth Unimod 447 remap to ??? modification from Unimod O-linked glycosylation http://purl.obolibrary.org/obo/MOD_00545 deuterated dimethyl labeling (D) OBSOLETE because redundant with MOD:00927. Remap to MOD:00927. http://purl.obolibrary.org/obo/MOD_00554 APTA-d0 with no neutral loss OBSOLETE because Unimod entry 202 was merged with entry 195, remap to MOD:00548. modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00555 APTA-d0 with quaternary amine loss OBSOLETE because Unimod entry 202 was merged with entry 195, remap to MOD:00548. modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00556 acrolein addition +94 OBSOLETE because this modification not supported by any literature that I can find[PMT] http://purl.obolibrary.org/obo/MOD_00557 acrolein addition +56 OBSOLETE because this modification not supported by the papers listed or any other that I can find[PMT] http://purl.obolibrary.org/obo/MOD_00558 acrolein addition +38 OBSOLETE because this modification not supported by any literature that I can find[PMT] http://purl.obolibrary.org/obo/MOD_00559 acrolein addition +76 OBSOLETE because this modification not supported by any literature that I can find[PMT] http://purl.obolibrary.org/obo/MOD_00560 acrolein addition +112 OBSOLETE because this modification not supported by any literature that I can find[PMT] http://purl.obolibrary.org/obo/MOD_00564 Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry 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. http://purl.obolibrary.org/obo/MOD_00567 histidine oxidation to asparagine OBSOLETE because Unimod entry 244 is redundant with Unimod 348. Remap to MOD:00775. http://purl.obolibrary.org/obo/MOD_00568 histidine oxidation to aspartic acid OBSOLETE because Unimod entry 245 is redundant with Unimod 349. Remap to MOD:00776 http://purl.obolibrary.org/obo/MOD_00578 acetaldehyde +28 OBSOLETE because this modification not supported by any literature that I can find [PMT] http://purl.obolibrary.org/obo/MOD_00579 propionaldehyde +40 OBSOLETE because not supported by the linked literature [PMT]. modification from Unimod Other http://purl.obolibrary.org/obo/MOD_00580 propionaldehyde +42 OBSOLETE because entry removed from Unimod. Remap potentially to MOD:00579 propionaldehyde +40 http://purl.obolibrary.org/obo/MOD_00590 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 http://purl.obolibrary.org/obo/MOD_00591 nucleophilic addition to cytopiloyne+H2O 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 http://purl.obolibrary.org/obo/MOD_00593 covalent modification of lysine by omega-maleimido alkanoyl N-hydroxysuccinimido esters OBSOLETE because removed from Unimod. modification from Unimod Chemical derivative http://purl.obolibrary.org/obo/MOD_00597 methyl methanethiosulfonate OBSOLETE because Unimod entry 277 redundant with Unimod 39. Remap to MOD:00110. http://purl.obolibrary.org/obo/MOD_00603 N-ethylation OBSOLETE because Unimod entry 283 is redundant with Unimod 280. Remap to MOD:00600 http://purl.obolibrary.org/obo/MOD_00615 4-sulfophenyl isothiocyante modification to N-term R OBSOLETE because entry Unimod:261 site N-term R was abandoned. Remap to MOD:00584 http://purl.obolibrary.org/obo/MOD_00619 hydroxylethanone OBSOLETE because entry 300 is redundant with Unimod 6 remap to MOD:01328 http://purl.obolibrary.org/obo/MOD_00632 N-succinimide OBSOLETE because this chemical derivative modification from Unimod 321 is deprecated. http://purl.obolibrary.org/obo/MOD_00641 CAMthiopropanoyl of Lys OBSOLETE because Unimod entry 334 is merged with Unimod 293. Remap to MOD:00612 http://purl.obolibrary.org/obo/MOD_00766 C terminal -K from HC of MAb modification from Unimod Post-translational - C-terminal loss of lysine OBSOLETE because the idenical to MOD:01642. Remap to MOD:01642 http://purl.obolibrary.org/obo/MOD_00779 lysine oxidation to aminoadipic semialdehyde OBSOLETE because redundant with MOD:00130. Remap to MOD:00130. http://purl.obolibrary.org/obo/MOD_00794 pyrrolidone from proline OBSOLETE because redundant and identical to MOD:00477. Remap to MOD:00477. http://purl.obolibrary.org/obo/MOD_00815 molybdopterin OBSOLETE because redundant with MOD:00151. Remap to MOD:00151. http://purl.obolibrary.org/obo/MOD_00872 L-isoglutamyl monoglutamic acid OBSOLETE because redundant and identical to MOD:01970. Remap to MOD:01970. http://purl.obolibrary.org/obo/MOD_00881 N-reductive amination-D OBSOLETE because Unimod entry 465 megerd with 199. Remap to MOD:00552 DiMethyl-CH2D. http://purl.obolibrary.org/obo/MOD_00921 new uncategorized Unimod entries New uncategorized Unimod. OBSOLETE because organizational use is no longer required. http://purl.obolibrary.org/obo/MOD_00926 Bisphenol A diglycidyl ether derivative Modification from Unimod Non-standard residue. OBSOLETE because not an amino acid modification. From Unimod not an approved entry. http://purl.obolibrary.org/obo/MOD_00945 fluorescein-5-thiosemicarbazide adduct OBSOLETE because redundant and identical to MOD:00626. Remap to MOD:00626. http://purl.obolibrary.org/obo/MOD_00948 5'-dephospho OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass http://purl.obolibrary.org/obo/MOD_00949 desmosine OBSOLETE because redundant and identical to MOD:01933. Remap to MOD:01933. http://purl.obolibrary.org/obo/MOD_00950 decomposed carboxymethylated methionine 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 http://purl.obolibrary.org/obo/MOD_00963 Oxidation of Trp to kynurenine Modification from DeltaMass. OBSOLETE because redundant and identical to MOD:00462. Remap to MOD:00462. http://purl.obolibrary.org/obo/MOD_00968 CM-Cys vs PAM-Cys OBSOLETE because this isn't a protein modification, but rather the difference between two known modifications. modification from DeltaMass http://purl.obolibrary.org/obo/MOD_00969 CAM-Cys vs PAM-Cys OBSOLETE because this isn't a protein modification, but rather the difference between two known modifications. modification from DeltaMass http://purl.obolibrary.org/obo/MOD_00976 potassium salt modification from DeltaMass - OBSOLETE because redundant and identical to MOD:01072. Remap to MOD:01072. http://purl.obolibrary.org/obo/MOD_00980 Carboxamidomethyl (on Cysteine) modification from DeltaMass - OBSOLETE because redundant, the difference component of MOD:01060. Remap to MOD:01060. http://purl.obolibrary.org/obo/MOD_00989 acetamidomethyl (Acm) OBSOLETE because redundant, the difference component of MOD:01079. Remap to MOD:01079. http://purl.obolibrary.org/obo/MOD_00999 homoseryl lactone OBSOLETE because redundant and identical to MOD:00404. Remap to MOD:00404. http://purl.obolibrary.org/obo/MOD_01017 homoseryl (-Hse-) OBSOLETE because redundant and identical to MOD:00403. Remap to MOD:00403. http://purl.obolibrary.org/obo/MOD_01036 O-methyl aspartyl OBSOLETE because redundant and identical to MOD:01181. Remap to MOD:01181. http://purl.obolibrary.org/obo/MOD_01038 norleucine (Nle) OBSOLETE because this represents a free amino acid and the corresponding residue is MOD:01026. http://purl.obolibrary.org/obo/MOD_01039 hydroxy aspartyl OBSOLETE because redundant and identical to MOD:00036. Remap to MOD:00036. http://purl.obolibrary.org/obo/MOD_01044 N-methyl glutamyl OBSOLETE because redundant and identical to MOD:00080. Remap to MOD:00080. http://purl.obolibrary.org/obo/MOD_01062 carboxymethyl cysteinyl OBSOLETE because duplicate and redundant with MOD:01061. Remap to MOD:01061 http://purl.obolibrary.org/obo/MOD_01076 N-methyl arginyl modification from DeltaMass - OBSOLETE because redundant and identical to MOD:00414. Remap to MOD:00414. http://purl.obolibrary.org/obo/MOD_01080 acrylamidyl cysteinyl OBSOLETE because this is identical to MOD:00417. modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01082 4-glycosyloxy- (hexosyl, C6) (of proline) OBSOLETE because redundant with MOD:00757, remap. modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01095 Matrix alpha cyano MH+ Modification from DeltaMass. OBSOLETE because not an amino acid modification. http://purl.obolibrary.org/obo/MOD_01101 S-Farnesyl- OBSOLETE because erroneous and apparently redundant to MOD:00111. Remap to MOD:00111. http://purl.obolibrary.org/obo/MOD_01102 myristoylation-4H (two double bonds) OBSOLETE because redundant and identical to MOD:00504. Remap to MOD:00504. http://purl.obolibrary.org/obo/MOD_01103 myristoleylation (one double bond) OBSOLETE because redundant and identical to MOD:00503. Remap to MOD:00503. http://purl.obolibrary.org/obo/MOD_01122 5'phos dCytidinyl OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01123 monoiodated tyrosine OBSOLETE because redundant and identical to MOD:01123. Remap to MOD:01123. http://purl.obolibrary.org/obo/MOD_01125 5'phos dThymidinyl OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01126 5'phos Cytidinyl OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01127 5'phos Uridinyl OBSOLETE because redundant and identical to MOD:01166. Remap to MOD:01166. http://purl.obolibrary.org/obo/MOD_01129 5'phos dAdenosyl OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01131 5'phos dGuanosyl OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01132 5'phos Adenosinyl OBSOLETE because redundant and identical to MOD:01165. Remap to MOD:01165. http://purl.obolibrary.org/obo/MOD_01136 dioctyl phthalate OBSOLETE because this is a small molecule contaminant and not a modification to a polypeptide. modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01138 Aedans Cystenyl OBSOLETE because no evidence has been seen for this protein modification. modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01139 dioctyl phthalate sodium adduct OBSOLETE because this is a MS contaminant, not a known modification to a polypeptide. modification from DeltaMass http://purl.obolibrary.org/obo/MOD_01190 dibromo Modification from Unimod Chemical derivative. OBSOLETE because duplicate and redundant with MOD:01006. Remap to MOD:01006. http://purl.obolibrary.org/obo/MOD_01196 5-dimethylaminonaphthalene-1-sulfonyl - site K OBSOLETE because redundant, replaced with MOD:01654. Remap to MOD:01654. http://purl.obolibrary.org/obo/MOD_01214 iodoacetamide - site C modification from Unimod Chemical derivative - OBSOLETE because redundant, the difference component of MOD:01060. Remap to MOD:01060. http://purl.obolibrary.org/obo/MOD_01246 fucosylated -site S OBSOLETE because redundant and identical to MOD:00812 after formula correction. Remap to MOD:00812. http://purl.obolibrary.org/obo/MOD_01247 fucosylated -site T OBSOLETE because redundant and identical to MOD:00813 after formula correction. Remap to MOD:00813. http://purl.obolibrary.org/obo/MOD_01252 5-hydro-5-methylimidazol-4-one, methylglyoxal arginine adduct (+54 amu) OBSOLETE because redundant and identical to MOD:00933. Remap to MOD:00933. http://purl.obolibrary.org/obo/MOD_01260 nucleophilic addtion to cytopiloyne - site Y 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 - http://purl.obolibrary.org/obo/MOD_01261 nucleophilic addtion to cytopiloyne - site S 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 - http://purl.obolibrary.org/obo/MOD_01262 nucleophilic addition to cytopiloyne - site R 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 - http://purl.obolibrary.org/obo/MOD_01263 nucleophilic addtion to cytopiloyne - site K 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 - http://purl.obolibrary.org/obo/MOD_01264 nucleophilic addtion to cytopiloyne - site C 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 - http://purl.obolibrary.org/obo/MOD_01265 nucleophilic addtion to cytopiloyne - site P 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 - http://purl.obolibrary.org/obo/MOD_01266 nucleophilic addition to cytopiloyne+H2O - site C 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 - http://purl.obolibrary.org/obo/MOD_01267 nucleophilic addition to cytopiloyne+H2O - site K 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 - http://purl.obolibrary.org/obo/MOD_01268 nucleophilic addition to cytopiloyne+H2O - site T 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 - http://purl.obolibrary.org/obo/MOD_01269 nucleophilic addition to cytopiloyne+H2O - site R 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 - http://purl.obolibrary.org/obo/MOD_01270 nucleophilic addition to cytopiloyne+H2O - site S 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 - http://purl.obolibrary.org/obo/MOD_01271 nucleophilic addition to cytopiloyne+H2O - site Y 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 - http://purl.obolibrary.org/obo/MOD_01282 acrolein addition +56 - site H OBSOLETE because this modification is not supported by the linked literature [PMT] http://purl.obolibrary.org/obo/MOD_01283 acrolein addition +56 - site K OBSOLETE because this modification is not supported by the linked literature [PMT] http://purl.obolibrary.org/obo/MOD_01284 acrolein addition +56 - site C OBSOLETE because this modification is not supported by the linked literature [PMT] http://purl.obolibrary.org/obo/MOD_01288 acetaldehyde +28 - site H OBSOLETE because this is not supported by the literature [PMT] http://purl.obolibrary.org/obo/MOD_01289 acetaldehyde +28 - site K OBSOLETE because this is not supported by the literature [PMT] http://purl.obolibrary.org/obo/MOD_01290 dihydroxylated residue - site F OBSOLETE because redundant and identical to MOD:00465. Remap to MOD:00465. http://purl.obolibrary.org/obo/MOD_01291 dihydroxylated residue - site W OBSOLETE because redundant and identical to MOD:00464. Remap to MOD:00464. http://purl.obolibrary.org/obo/MOD_01292 dimethylation of proline residue OBSOLETE because redundant and identical to MOD:00075. Map to MOD:00075. http://purl.obolibrary.org/obo/MOD_01294 deamidation in presence of O18 -site Q OBSOLETE identical and redundant with MOD:00791. Remap to MOD:00791. http://purl.obolibrary.org/obo/MOD_01322 propionaldehyde +40 - site K OBSOLETE because not supported by the linked literature [PMT]. modification from Unimod Other - http://purl.obolibrary.org/obo/MOD_01323 propionaldehyde +40 - site H OBSOLETE because not supported by the linked literature [PMT]. modification from Unimod Other - http://purl.obolibrary.org/obo/MOD_01324 acetaldehyde +26 - site H OBSOLETE because this is not supported by the linked literature [PMT] http://purl.obolibrary.org/obo/MOD_01325 acetaldehyde +26 - site K OBSOLETE because this is not supported by the linked literature [PMT] http://purl.obolibrary.org/obo/MOD_01329 iodoacetic acid - site C OBSOLETE because duplicate and redundant with MOD:01061. Remap to MOD:01061 http://purl.obolibrary.org/obo/MOD_01330 iodoacetic acid -site K OBSOLETE because identical with MOD:01094. Remap to MOD:01094 http://purl.obolibrary.org/obo/MOD_01336 deamidation followed by a methylation -site Q OBSOLETE - identical and redundant with MOD:00657. Remap to MOD:00657. http://purl.obolibrary.org/obo/MOD_01342 selenium substitution for sulfur - site M OBSOLETE because redundant and identical to MOD:00530. Remap to MOD:00530. http://purl.obolibrary.org/obo/MOD_01343 selenium substitution for sulfur - site C OBSOLETE because redundant and identical to MOD:00686. Remap to MOD:00686. http://purl.obolibrary.org/obo/MOD_01344 dehydrogenated residue - site S OBSOLETE because redundant and identical with MOD:00835. Remap to MOD:00835. http://purl.obolibrary.org/obo/MOD_01371 deamidation in presence of O18 OBSOLETE bcecause identical and redundant with MOD:00851. Remap to MOD:00851. http://purl.obolibrary.org/obo/MOD_01427 2-aminobutanoic acid (Abu) OBSOLETE because redundant and identical to MOD:00819. Remap to MOD:00819. http://purl.obolibrary.org/obo/MOD_01876 4x(1)H,4x(12)C-labeled alpha-amino succinylated residue OBSOLETE because identical to MOD:00457 http://purl.obolibrary.org/obo/MOD_01961 O-(L-isoglutamyl)-L-threonine (THR) OBSOLETE because redundant and identical to MOD:01785. Remap to MOD:01785. http://purl.obolibrary.org/obo/MOD_01966 L-methionine (R)-sulfoxide OBSOLETE because redundant and identical to MOD:00720. Remap to MOD:00720. http://purl.obolibrary.org/obo/mod#contains contains 'Entity A' contains 'Entity B' implies that 'Entity B' is a part of the structure of 'Entity A'. http://purl.obolibrary.org/obo/mod#derives_from derives from 'Entity A' derives_from 'Entity B' implies that 'Entity A' is chemically derived from 'Entity B'. http://purl.obolibrary.org/obo/mod#has_functional_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. http://purl.obolibrary.org/obo/mod#part_of part of 'Entity A' part_of 'Entity B' implies that 'Entity A' is a part of the structure of 'Entity B'.