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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 stepwise addition of sugar residues to the initially added O-linked sugar (usually GalNAc) to form a core O-glycan structure. The transfer of mannose from dolichyl activated mannose to the hydroxyl group of a seryl or threonyl residue of a protein acceptor molecule, to form an O-linked protein-sugar linkage. 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. A protein amino acid glycosylation process in which a sugar unit is added to a protein via the hydroxyl group of peptidyl-serine, peptidyl-threonine, peptidyl-hydroxylysine, or peptidyl-hydroxyproline, or via the phenol group of peptidyl-tyrosine, forming an O-glycan. 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 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. The posttranslational glycosylation of protein via the O4' atom of peptidyl-tyrosine, O4'-glycosyl-L-tyrosine; the carbohydrate is glucose, the origin for glycogen. 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 the O3 atom of peptidyl-threonine, forming O3-glycosyl-L-threonine; the most common forms are N-acetylgalactosaminyl, mannosyl, and galactosyl threonine. The covalent attachment of a glycosyl residue to one or more monomeric units in a polypeptide, polynucleotide, polysaccharide, or other biological macromolecule. The posttranslational glycosylation of proteins via 04 atom of hydroxyproline to form O4-glycosyl-L-hydroxyproline; the most common form is arabinofuranosyl-4-proline. 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: protein amino acid O-linked glycosylation
Acc: GO:0006493
Aspect: Biological Process
Desc: A protein amino acid glycosylation process in which a sugar unit is added to a protein via the hydroxyl group of peptidyl-serine, peptidyl-threonine, peptidyl-hydroxylysine, or peptidyl-hydroxyproline, or via the phenol group of peptidyl-tyrosine, forming an O-glycan.
Proteins in PDR annotated with:
   This term: 63 [Search]
   Term or descendants: 78 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0006493 - protein amino acid O-linked glycosylation (interactive image map)
YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle