| Function | Mannosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. Catalyzes, on the cytoplasmic face of the endoplasmic reticulum, the addition of the second and third mannose residues to the dolichol-linked oligosaccharide chain, to produce Man3GlcNAc(2)-PP-dolichol core oligosaccharide. Man3GlcNAc(2)-PP-dolichol is a substrate for ALG11, the following enzyme in the biosynthetic pathway. While both alpha 1,3 and alpha 1,6 linkages are possible, the sequential addition of alpha 1,3 followed by alpha 1,6 is probably the preferred route. |
| Protein Name | Alpha-1 -3/1 -6-Mannosyltransferase Alg2Asparagine-Linked Glycosylation Protein 2 HomologGdp-Man -Man(1glcnac(2-Pp-Dol Alpha-1 -3-MannosyltransferaseGdp-Man -Man(1glcnac(2-Pp-Dolichol MannosyltransferaseGdp-Man -Man(2glcnac(2-Pp-Dol Alpha-1 -6-Mannosyltransferase |
| Database Links | Reactome: R-HSA-446193Reactome: R-HSA-4549349 |
| Cellular Localisation | Endoplasmic Reticulum MembraneSingle-Pass Membrane ProteinActive On Cytoplasmic Side Of Endoplasmic Reticulum Membrane |
| Alternative Antibody Names | Anti-Alpha-1 -3/1 -6-Mannosyltransferase Alg2 antibodyAnti-Asparagine-Linked Glycosylation Protein 2 Homolog antibodyAnti-Gdp-Man -Man(1glcnac(2-Pp-Dol Alpha-1 -3-Mannosyltransferase antibodyAnti-Gdp-Man -Man(1glcnac(2-Pp-Dolichol Mannosyltransferase antibodyAnti-Gdp-Man -Man(2glcnac(2-Pp-Dol Alpha-1 -6-Mannosyltransferase antibodyAnti-ALG2 antibodyAnti-UNQ666 antibodyAnti-PRO1298 antibody |
Information sourced from Uniprot.org
