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The methylation of peptidyl-asparagine to form peptidyl-N4-methyl-L-asparagine or peptidyl-N4,N4-dimethyl-L-asparagine. The posttranslation modification of peptidyl-asparagine to form peptidyl-L-beta-methylthioasparagine, typical of bacterial ribosomal protein S12. The posttranslational hydroxylation of peptidyl-asparagine to form peptidyl-hydroxyasparagine. The chemical reactions and pathways resulting in the formation of N4-hydroxymethyl-L-asparagine from other compounds, including peptidyl-asparagine. The racemization of peptidyl-asparagine. The formation of a C-terminal peptidyl-asparagine amide by hydrolysis and oxidation of an interior Asn-Gly peptide in a secreted protein. The modification of peptidyl-asparagine. The formation of an isopeptide cross-link between peptidyl-asparagine and peptidyl-cysteine to produce N-(L-isoaspartyl)-L-cysteine. The formation of an isopeptide cross-link between peptidyl-asparagine and peptidyl-glycine to produce N-(L-isoaspartyl)-glycine. The transfer, from NAD, of ADP-ribose to peptidyl-asparagine to form peptidyl-N4-(ADP-ribosyl)-L-asparagine. The formation of isopeptide bonds by ligation of peptidyl-lysine and peptidyl-asparagine residues. The alteration of an amino acid residue in a peptide. The chemical reactions and pathways resulting in the formation of a C-terminal peptidyl-asparagine ethanolamide-linked glycosylphosphatidylinositol (GPI) anchor following hydrolysis of a asparaginyl-peptide bond in the carboxy-terminal region of a membrane-associated protein. The formation of the fluorescent protein FP506 chromophore cross-link from the alpha-carboxyl carbon of residue n, an asparagine, 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 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). The posttranslational glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine also occurs; this modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification. The modification of asparagine to (3-aminopropyl)(L-aspartyl-1-amino)phosphoryl-5'-adenosine as found in microcin C7 produced from the mccA gene in E. coli plasmid pMccC7.

View Gene Ontology (GO) Term

GO TERM SUMMARY
Name: peptidyl-asparagine modification
Acc: GO:0018196
Aspect: Biological Process
Desc: The modification of peptidyl-asparagine.
Proteins in PDR annotated with:
   This term: 0
   Term or descendants: 24 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0018196 - peptidyl-asparagine modification (interactive image map)
YRC Informatics Platform - Version 3.0
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