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The oxidative deamination of N-terminal peptidyl-cysteine, or peptidyl-serine, to form pyruvic acid with an amide bond between its 1-carboxyl group and the N-terminal residue. The formation of a cross-link between peptide chains mediated by a chondroitin 4-sulfate glycosaminoglycan that originates from a typical O-glycosidic link to serine of one chain; the other chain is esterified, via the alpha-carbon of its C-terminal Asp, to C-6 of an internal N-acetylgalactosamine of the glycosaminoglycan chain. The palmitoylation of peptidyl-serine to form peptidyl-O-palmitoyl-L-threonine. The posttranslational phosphopantetheinylation of peptidyl-serine to form peptidyl-O-phosphopantetheine-L-serine. The posttranslational modification of peptidyl-serine to peptidyl-O-(sn-1-glycerophosphoryl)-L-serine. The incorporation of iron into a 4Fe-4S iron-sulfur cluster via tris-L-cysteinyl-L-serinyl tetrairon tetrasulfide. The chemical reactions and pathways resulting in the formation of a peptidyl serine-peptidyl cysteine cross-link by the condensation of a serine hydroxyl with the carbonyl of the preceding residue. The chemical reactions and pathways resulting in the formation of a peptidyl serine-peptidyl glycine cross-link by the condensation of a serine hydroxyl with the carbonyl of the preceding residue and alpha-beta dehydrogenation. The posttranslational modification of peptidyl-lysine and peptidyl-serine to form a (2Xi,9S)-L-lysinoalanine cross-link. The formation of peptidyl-dehydroalanine from either peptidyl-tyrosine by phenyl transfer, or from peptidyl-serine, which is coupled with the formation of 5-imidazolinone by the two neighboring residues, produces an 4-methylidene-imidazole-5-one active site of some amino acid ammonia-lyases; the 4-methylidene-imidazole-5-one, is formed autocatalytically by cyclization and dehydration of the sequence ASG. The formation of a protein-protein cross-link between peptidyl-serine and peptidyl-cysteine by the synthesis of sn-(2S,6R)-lanthionine (meso-lanthione). The posttranslational phosphorylation of peptidyl-serine to form peptidyl-O-phospho-L-serine. The O-glucuronidation of peptidyl-serine to form peptidyl-O3-D-glucuronyl-L-serine. The chemical reactions and pathways resulting in the formation of a peptidyl cysteine-peptidyl serine cross-link by the condensation of a cysteine thiol with the carbonyl of the preceding residue and alpha-beta dehydrogenation. The posttranslational octanoylation of peptidyl-serine to form peptidyl-O3-octanoyl-L-serine, typical of the protein ghrelin. The posttranslational synthesis of (S,Z)-S-(2-aminovinyl)cysteine forming an intra-polypeptide cross-link between serine and cysteine. The formation of the green fluorescent protein chromophore cross-link from the alpha-carboxyl carbon of residue n, a serine, to the alpha-amino nitrogen of residue n+2, a glycine, and a dehydration to form a double bond to the alpha-amino nitrogen of residue n+1. This cross-linking is coupled with a dehydrogenation of residue n+1 to form a double bond between the alpha and beta carbons. The alteration of an amino acid residue in a peptide. The posttranslational sulfation of peptidyl-serine to form peptidyl-O-sulfo-L-serine. The formation of a protein-protein cross-link between peptidyl-serine and peptidyl-cysteine by the synthesis of (2R,6R)-lanthionine (L-lanthionine). The acetylation of the N-terminal serine of proteins to form the derivative N-acetyl-L-serine. The formation of a covalent cross-link between RNA and a peptidyl-serine residue by the formation of O-(phospho-5'-5NA)-L-serine. The chemical reactions and pathways resulting in the formation of a peptidyl serine-peptidyl cysteine cross-link by the condensation of a serine hydroxyl with the carbonyl of the preceding residue and alpha-beta dehydrogenation. The incorporation of molybdenum into a protein via L-serinyl molybdopterin guanine dinucleotide. The modification of serine to N-[5-(6-O-seryl-beta-glucosyl)-2,3-dihydroxybenzoyl]-O-[N-(2,3-dihydroxybenzoyl)-O-[N-(2,3-dihydroxybenzoyl)seryl]seryl]serine as found in microcin E492 produced from the mceA gene in plasmid pJAM229 of the E. coli VCS257 strain and the K. pneumoniae RYC492 strain. The formation of a C-terminal peptidyl-serine amide by hydrolysis and oxidation of an interior Ser-Gly peptide in a secreted protein. The posttranslational decanoylation of peptidyl-serine to form peptidyl-O3-decanoyl-L-serine, typical of the protein ghrelin. The transfer, from NAD, of ADP-ribose to peptidyl-serine to form peptidyl-O-(ADP-ribosyl)-L-serine. The incorporation of iron into a 3Fe-2S cluster by tris-L-cysteinyl L-cysteine persulfido L-glutamato L-histidino L-serinyl nickel triiron disulfide trioxide. The posttranslational modification of peptidyl-cysteine or peptidyl-serine to peptidyl-L-3-oxoalanine; characteristic of the active sites of arylsulfatases. The incorporation of iron into a 4Fe-4S iron-sulfur cluster via bis-L-cysteinyl-L-N3'-histidino-L-serinyl tetrairon tetrasulfide. The modification of N-terminal peptidyl-serine to lactic acid. Heparan sulfate components are covalently linked to a core glycoprotein via O-glycosidic linkages between xylose and serine residues. The modification of peptidyl-serine. Dermatan sulfate components are covalently linked to a core glycoprotein via O-glycosidic linkages between xylose and serine residues. The posttranslational glycosylation of protein via the O3 atom of peptidyl-serine, forming O3-glycosyl-L-serine; the most common forms are N-acetylgalactosaminyl, mannosyl, galactosyl, and xylosyl serine. Chondroitin sulfate components are covalently linked to a core glycoprotein via O-glycosidic linkages between xylose and serine residues. The formation of a covalent cross-link between DNA and a peptidyl-serine residue by the formation of O-(phospho-5'-DNA)-L-serine. The chemical reactions and pathways resulting in the formation of a peptidyl cysteine-peptidyl serine cross-link through a process of forming first an intermediate cysteine sulfenic acid by peroxide oxidation, followed by condensation with the alpha-amido of the following serine residue and the release of water. The formation of a C-terminal peptidyl-serine ethanolamide-linked glycosylsphingolipidinositol (GSI) anchor following hydrolysis of a seryl-peptide bond in the carboxy-terminal region of a membrane-associated protein. The incorporation of iron into a 8Fe-7S iron-sulfur cluster via hexakis-L-cysteinyl L-serinyl octairon heptasulfide, found in nitrogenase. The chemical reactions and pathways resulting in the formation of a C-terminal peptidyl-serine ethanolamide-linked glycosylphosphatidylinositol (GPI) anchor following hydrolysis of a seryl-peptide bond in the carboxy-terminal region of a membrane-associated protein. The acetylation of peptidyl-serine to form peptidyl-O-acetyl-L-serine. The linkage of phosphoribosyl dephospho-coenzyme A to protein via peptidyl-serine, to form O-(phosphoribosyl dephospho-coenzyme A)-L-serine; it is uncertain whether the phosphoribosyl glycosidic attachment to the dephospho-coenzyme A is alpha or beta, and through the 2' or the 3' position. The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications). Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification).

View Gene Ontology (GO) Term

GO TERM SUMMARY
Name: peptidyl-serine modification
Acc: GO:0018209
Aspect: Biological Process
Desc: The modification of peptidyl-serine.
Proteins in PDR annotated with:
   This term: 1 [Search]
   Term or descendants: 137 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0018209 - peptidyl-serine modification (interactive image map)
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