Protein Name:
Dolichyl-phosphate beta-glucosyltransferase
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UniprotKB/SwissProt ID: Q9Y673 (Q9Y673)
Gene Name:
ALG5
Organism: Homo sapiens (Human)
Function: Dolichyl-phosphate beta-glucosyltransferase 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. Dolichyl-phosphate beta-glucosyltransferase produces dolichyl beta-D-glucosyl phosphate/Dol-P-Glc, the glucose donor substrate used sequentially by ALG6, ALG8 and ALG10 to add glucose residues on top of the Man(9)GlcNAc(2)-PP-Dol structure. These are the three last steps in the biosynthetic pathway of dolichol-linked oligosaccharides to produce Glc(3)Man(9)GlcNAc(2)-PP-Dol. The enzyme is most probably active on the cytoplasmic side of the endoplasmic reticulum while its product Dol-P-Glc is the substrate for ALG6, ALG8 and ALG11 in the lumen of the endoplasmic reticulum
Other Modifications: View all modification sites in dbPTM
Protein Subcellular Localization: Endoplasmic reticulum membrane
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Graphical Visualization of S-nitrosylation Sites:
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The S-nitrosylation sites of Q9Y673
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| No. |
Position |
S-nitrosylated Peptide |
Secondary Structure of S-nitrosylated Peptide |
Solvent Accessibility of nitrosylated Site |
PubMed ID |
| 1 |
194 |
QPWPNQMAIA C GSRAHLEKES |
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| 2 |
236 |
LCVKGIRDTQ C GFKLFTREAA |
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