| Gene Symbol |
STT3B
|
| Entrez Gene |
201595
|
| Alt Symbol |
CDG1X, SIMP, STT3-B
|
| Species |
Human
|
| Gene Type |
protein-coding
|
| Description |
STT3B, subunit of the oligosaccharyltransferase complex (catalytic)
|
| Other Description |
STT3, subunit of the oligosaccharyltransferase complex, homolog B|dolichyl-diphosphooligosaccharide protein glycotransferase|dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B|homolog of yeast STT3|oligosaccharyl transferase subunit STT3B|source of immunodominant MHC-associated peptides homolog
|
| Swissprots |
Q96JZ4 Q96KY7 Q8TCJ2
|
| Accessions |
CAF85831 EAW64415 EAW64416 Q8TCJ2 AI914841 AK027789 BAB55370 AK074587 AK075380 BAC11581 AK311488 AX799082 CAE48447 AY074880 AAL71884 BC015880 AAH15880 HY015137 HY039873 XM_011533465 XP_011531767 NM_178862 NP_849193
|
| Function |
Catalytic subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. 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). STT3B is present in a small subset of OST complexes and mediates both cotranslational and post-translational N-glycosylation of target proteins: STT3B-containing complexes are required for efficient cotranslational glycosylation and while they are less competent than STT3A-containing complexes for cotranslational glycosylation, they have the ability to mediate glycosylation of some nascent sites that are not accessible for STT3A. STT3B-containing complexes also act post-translationally and mediate modification of skip
|
| Subcellular Location |
Endoplasmic reticulum membrane; Multi-pass membrane protein.
|
| Tissue Specificity |
Expressed in heart, brain, placenta, lung, liver, muscle, kidney and pancreas. Expressed in skin fibroblasts (at protein level). {ECO:0000269|PubMed:12887896}.
|
| Top Pathways |
N-Glycan biosynthesis, Protein processing in endoplasmic reticulum
|
