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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: Oligosaccharyltransferase complex subunit OSTC

UniprotKB/SwissProt ID: Q9NRP0 (Q9NRP0)

Gene Name: OSTC

Organism: Homo sapiens (Human)

Function: Subunit of STT3A-containing oligosaccharyl transferase (OST-A) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (PubMed:28860277, PubMed:31831667, PubMed:39509507). N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER) (PubMed:28860277, PubMed:31831667, PubMed:39509507). Within the OST-A complex, acts as an adapter that anchors the OST-A complex to the Sec61 complex (PubMed:28860277). May be involved in N-glycosylation of APP (amyloid-beta precursor protein) (PubMed:21768116). Can modulate gamma-secretase cleavage of APP by enhancing endoprotelysis of PSEN1 (PubMed:21768116)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Endoplasmic reticulum. Membrane

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR021149 OligosaccharylTrfase_OST3/OST6
IPR042416 OSTC

The S-nitrosylation sites of Q9NRP0

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 14 LYRVPFLVLE C PNLKLKKPPW