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The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y, as carried out by individual cells. The chemical reactions and pathways resulting in the formation of glycoproteins, any protein that contains covalently bound glycose (i.e. monosaccharide) residues other than as a moiety of nucleic acid; the glycose occurs most commonly as oligosaccharide or fairly small polysaccharide but occasionally as monosaccharide. The posttranslational glycosylation of protein via peptidyl-arginine, omega-N-glycosyl-L-arginine. The conversion of N-linked glycan structures from the initially transferred oligosaccharide to a mature form, by the actions of glycosidases and glycosyltransferases. The early processing steps are conserved and play roles in glycoprotein folding and trafficking. A protein modification process that results in the addition of a sugar unit to a protein amino acid, e.g. the addition of glycan chains to proteins. The posttranslational glycosylation of protein via peptidyl-tryptophan, 1'-glycosyl-L-tryptophan; it is uncertain whether this is an N-glycoside linkage (as indicated), and which particular hexose is involved. The glycosylation of a nitrogen atom of a free alpha amino terminal of a peptide. The covalent attachment of a glycosyl residue to one or more monomeric units in a polypeptide, polynucleotide, polysaccharide, or other biological macromolecule. A protein amino acid glycosylation process in which a sugar unit is added to a protein via the N4 atom of peptidyl-asparagine, the omega-N of arginine, or the N1' atom peptidyl-tryptophan. The chemical reactions and pathways resulting in the formation of dolichol-linked oligosaccharide, usually by a stepwise addition of glycosyl chains to endoplasmic reticulum membrane-bound dolichol-P. 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.

View Gene Ontology (GO) Term

GO TERM SUMMARY

Name: protein amino acid N-linked glycosylation
Acc: GO:0006487
Aspect: Biological Process
Desc: A protein amino acid glycosylation process in which a sugar unit is added to a protein via the N4 atom of peptidyl-asparagine, the omega-N of arginine, or the N1' atom peptidyl-tryptophan.
Synonyms:
  • N-glycan metabolism
  • N-glycan biosynthesis
Proteins in PDR annotated with:
   This term: 163 [Search]
   Term or descendants: 250 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0006487 - protein amino acid N-linked glycosylation (interactive image map)

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