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The posttranslational iodination of peptidyl-thyronine, formed from tyrosine. The formation of a 2-keto-5-iminopiperazine protein chromophore cross-link from the alpha-amino nitrogen of residue n, a methionine, to the alpha-carboxyl carbon of residue n+1, a tyrosine, and a dehydration to form a double bond to the alpha-amino nitrogen of residue n+2. This cross-linking is coupled with a dehydrogenation of residue n+1 to form a double bond between the alpha and beta carbons. The posttranslation modification of two peptidyl-tyrosines to form a 3'-(O4'-L-tyrosinyl)-L-tyrosine protein cross-link. The formation of peptidyl-thyronine from peptidyl-tyrosine in thyroglobulin by phenyl transfer coupled with the formation of peptidyl-dehydroalanine. The formation of a C-terminal peptidyl-tyrosine amide by hydrolysis and oxidation of an interior Tyr-Gly peptide in a secreted protein. The posttranslational cross-linking of a tyrosine residue to a tryptophan residue and a methionine residue to form S-[5'-(L-tryptoph-6'-yl)-L-tyrosin-3'-yl]-L-methionin-S-ium. The, presumably, posttranslational modification of protein tyrosine to peptidyl-L-3',4',5'-dihydroxyphenylalanine. 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 oxidation of the C alpha-C beta bond of peptidyl-tyrosine to form peptidyl-dehydrotyrosine coupled with cyclization of neighboring residues. The formation of a covalent cross-link between DNA and a peptidyl-tyrosine residue. The alteration of an amino acid residue in a peptide. The posttranslational adenylylation of peptidyl-tyrosine to form peptidyl-O4'-(phospho-5'-adenosine)-L-tyrosine. The posttranslation modification of peptidyl-histidine and peptidyl-tyrosine to form a protein cross-link. The posttranslational sulfation of peptidyl-tyrosine residues to form peptidyl-O4'-sulfo-L-tyrosine. The formation of a protein-FAD linkage via O4'-(8-alpha-FAD)-L-tyrosine. The acetylation of the N-terminal tyrosine of proteins to form the derivative N-acetyl-L-tyrosine. The linkage of protein to heme P460 via heme P460-bis-L-cysteine-L-tyrosine. The posttranslational modification of protein tyrosine to L-2',4',5'-topaquinone, characteristic of the active site of copper amine oxidases. The posttranslational modification of protein tyrosine to peptidyl-L-3',4'-dihydroxyphenylalanine (DOPA). The posttranslational thioether cross-linking of a cysteine residue to a tyrosine residue to form 3'-(S-L-cysteinyl)-L-tyrosine, found in galactose oxidase. The posttranslational phosphorylation of peptidyl-tyrosine to form peptidyl-O4'-phospho-L-tyrosine. The methylation of the N-terminal tyrosine of proteins to form the derivative N-methyl-L-tyrosine. The modification of peptidyl-tyrosine. The posttranslation modification of two peptidyl-tyrosines to form a 3'-(3'-L-tyrosinyl)-L-tyrosine protein cross-link. The cross-linking of the epsilon-amino group of a peptidyl-lysine with peptidyl-topaquinone, a modified tyrosine residue. The formation of a covalent cross-link between RNA and a peptidyl-tyrosine residue by the formation of O4'-(phospho-5'-RNA)-L-tyrosine. The uridylylation of peptidyl-tyrosine to form peptidyl-O4'-(phospho-5'-uridine)-L-tyrosine, found in glutamine synthetase. The posttranslational glycosylation of protein via the O4' atom of peptidyl-tyrosine, O4'-glycosyl-L-tyrosine; the carbohydrate is glucose, the origin for glycogen. The ATP-dependent posttranslational addition of a tyrosine residue to the C-terminus of a protein; typically the addition of tyrosine to the C-terminus of detyrosinated alpha-tubulin by the enzyme tubulin-tyrosine ligase. The chemical reactions and pathways resulting in the formation of the cofactor pyrroloquinoline quinone (PQQ); it is synthesized from a small peptide containing tyrosine and glutamic acid; these amino acids in the peptide are multiply cross-linked and the rest of the peptide is removed. 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


Name: peptidyl-tyrosine modification
Acc: GO:0018212
Aspect: Biological Process
Desc: The modification of peptidyl-tyrosine.
Proteins in PDR annotated with:
   This term: 0
   Term or descendants: 323 [Search]


GO:0018212 - peptidyl-tyrosine modification (interactive image map)

YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle