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The chemical reactions and pathways involving 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 removal of sugar residues from a glycosylated protein. The chemical reactions and pathways resulting in the breakdown 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 covalent alteration of one or more monomeric units in a polypeptide, polynucleotide, polysaccharide, or other biological macromolecule, resulting in a change in its properties. The chemical reactions and pathways resulting in the breakdown of a macromolecule, any molecule of high relative molecular mass, the structure of which essentially comprises the multiple repetition of units derived, actually or conceptually, from molecules of low relative molecular mass. The chemical reactions and pathways involving a specific protein, rather than of proteins in general, occurring at the level of an individual cell. Includes protein modification. 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 deglycosylation
Acc: GO:0006517
Aspect: Biological Process
Desc: The removal of sugar residues from a glycosylated protein.
Synonyms:
  • glycoprotein deglycosylation
Proteins in PDR annotated with:
   This term: 8 [Search]
   Term or descendants: 8 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0006517 - protein deglycosylation (interactive image map)
YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle