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The oxidation of the terminal amino-methylene groups of peptidyl-L-lysine or peptidyl-5-hydroxy-L-lysine to aldehyde groups to form allysine or hydroxyallysine residues, respectively; these are intermediates in the formation of covalent cross-links between adjacent polypeptide chains in proteins such as collagens. The linkage of protein to heme P460 via heme P460-bis-L-cysteine-L-lysine. The modification of peptidyl-lysine. The lipoylation of peptidyl-lysine to form peptidyl-N6-lipoyl-L-lysine. null The covalent modification of peptidyl-lysine by biotin to form peptidyl-N6-biotinyl-L-lysine. The posttranslation modification of peptidyl-lysine to form N6-pyridoxal phosphate-L-lysine. The posttranslation modification of peptidyl-lysine to form N6-retinal-L-lysine. The posttranslational modification of peptidyl-lysine and peptidyl-serine to form a (2Xi,9S)-L-lysinoalanine cross-link. The alteration of an amino acid residue in a peptide. The formation of an isopeptide cross-link between peptidyl-lysine and peptidyl-glutamine to produce N6-(L-isoglutamyl)-L-lysine. The modification of peptidyl-lysine to form peptidyl-N6-formyl-L-lysine. The formation of an isopeptide cross-link between peptidyl-lysine and peptidyl-glycine to produce N6-glycyl-L-lysine. This is distinct from the formation of the thiolester intermediate, which occurs during ubiquitination. The methylation of peptidyl-lysine to form either the mono-, di- or trimethylated derivative. The oxidation of allysine to 2-aminoadipic acid. The formation of a C-terminal peptidyl-lysine amide by hydrolysis and oxidation of an interior Lys-Gly peptide in a secreted protein. The removal of an acetyl group from an acetylated lysine residue in a peptide or protein. The posttranslational modification of peptidyl-lysine to form hypusine, N6-(4-amino-2-hydroxybutyl)-L-lysine. The palmitoylation of peptidyl-lysine to form peptidyl-N6-palmitoyl-L-lysine. The posttranslational modification of peptidyl-lysine to form peptidyl-N6-carboxy-L-lysine. The myristoylation of peptidyl-lysine to form peptidyl-N6-myristoyl-L-lysine. The posttranslational modification of peptidyl-lysine to form peptidyl-N6-1-carboxyethyl-L-lysine. The formation of a 2-tetrahydropyridinyl-5-imidazolinone protein chromophore cross-link from the alpha-carboxyl carbon of residue n, a lysine, 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. In addition, the residue N lysine undergoes cyclization. The alpha-amino nitrogen is replaced by the epsilon-amino nitrogen, the peptide chain is broken, residue N-1 is released as an amide, and a double bond is formed between the alpha-carbon and the nitrogen so that a tetrahydropyridine ring results. This modification is found in the GFP-like fluorescent chromoprotein FP538 from the sea anemone Zoanthus species. The acetylation of peptidyl-lysine. The formation of a fluorescent protein chromophore cross-link from the alpha-carboxyl carbon of residue n, a lysine, 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 cross-linking of the epsilon-amino group of a peptidyl-lysine with peptidyl-topaquinone, a modified tyrosine residue. The chemical reactions and pathways resulting in the formation of peptidyl-L-lysine methyl ester. The modification of peptidyl-lysine by the addition of an N6-propylamino and of propylmethylamino units, forming N6-(propylamino-poly(propylmethylamino)-propyldimethylamine)-L-lysine, typical of the silicate binding protein silaffin. The posttranslational guanylylation of peptidyl-lysine to form peptidyl-N6-(phospho-5'-guanosine)-L-lysine. The posttranslational glycosylation of protein via the O5 atom of peptidyl-hydroxylysine, forming O5-glycosyl-L-hydroxylysine; the most common form is galactosyl hydroxylysine. The posttranslation modification of peptidyl-lysine to form N6-3,4-didehydroretinylidene-L-lysine. The formation of isopeptide bonds by ligation of peptidyl-lysine and peptidyl-asparagine residues. The adenylylation of peptidyl-lysine to form peptidyl-N6-(phospho-5'-adenosine)-L-lysine. The process of linking a protein to peptidoglycan via the epsilon amino group of lysine to the diaminopimelic acid of the peptidoglycan. The chemical reactions and pathways resulting in the formation of a peptidyl cysteine-peptidyl lysine cross-link by the condensation of a cysteine thiol with the carbonyl of the preceding residue and alpha-beta dehydrogenation. The hydroxylation of peptidyl-lysine to form peptidyl-hydroxylysine. 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-lysine modification
Acc: GO:0018205
Aspect: Biological Process
Desc: The modification of peptidyl-lysine.
Proteins in PDR annotated with:
   This term: 9 [Search]
   Term or descendants: 73 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0018205 - peptidyl-lysine modification (interactive image map)
YRC Informatics Platform - Version 3.0
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