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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Alpha-1,3/1,6-mannosyltransferase ALG2

UniprotKB/SwissProt ID: Q9H553 (Q9H553)

Gene Name: ALG2

Organism: Homo sapiens (Human)

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 (PubMed:12684507, PubMed:35136180). 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 (PubMed:35136180)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Endoplasmic reticulum membrane

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR027054 ALG2
IPR001296 Glyco_trans_1
IPR028098 Glyco_trans_4-like_N

The S-nitrosylation sites of Q9H553

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 70 FAESRELPVR C AGDWLPRGLG