Glycosylation is one of the most universal but at the same time complex protein modifications. Modification with sugar moeties can be both co- translational and post- translational, occurring in the endoplasmatic reticulum and golgi. Three different forms of glycosylation can be distinguished: N-linked oligosaccharides, O-linked oligosaccharides and glycosyl- phosphatidylinositol (GPI-) anchors. Glycosylation results in thousands of distinct, bioactive glycoproteins resident throughout the cell that strongly determine protein-protein, carbohydrate-protein, membrane, and adhesion properties. Diseases associated with glycosylation defects include Congenital disorders of glycosylation, (CDG), also known as carbohydrate deficient glycoprotein syndromes, and diseases associated with advanced aging.
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Protein Aliases: beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N--acetylglucosaminyltransferase; Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase; beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase (Core 2 branching enzyme) (Core2-GlcNAc-transferase) (C2GNT); beta-1,6-N-acetylglucosaminyltransferase; C2GNT; core 2 beta-1,6-N-acetylglucosaminyltransferase I; core 2 beta1,6 N-acetylglucosaminyltransferase-I; core 2 branching enzyme; core 2 GnT; Core 2-branching enzyme; Core2-GlcNAc-transferase; glucosaminyl (N-acetyl) transferase 1, core 2 (beta-1,6-N-acetylglucosaminyltransferase)
Gene Aliases: 5630400D21Rik; B130048E03; C2 GlcNAcT; C2GNT; C2GNT-L; C2GNT1; G6NT; GCNT1; IGnT; NACGT2; NAGCT2