Stt3a, catalytic subunit of the oligosaccharyltransferase complex

STT3A, catalytic subunit of the oligosaccharyltransferase complex is a protein that in humans is encoded by the STT3A gene. [5]

STT3A
Identifiers
Aliases	STT3A, ITM1, STT3-A, TMC, catalytic subunit of the oligosaccharyltransferase complex, STT3 oligosaccharyltransferase complex catalytic subunit A
External IDs	OMIM: 601134 MGI: 105124 HomoloGene: 40617 GeneCards: STT3A
Gene location (Human) Chr. Chromosome 11 (human)[1] Band 11q24.2 Start 125,591,712 bp[1] End 125,625,215 bp[1]
Gene location (Mouse) Chr. Chromosome 9 (mouse)[2] Band 9 A4|9 20.67 cM Start 36,729,344 bp[2] End 36,767,679 bp[2]
Gene ontology Molecular function • oligosaccharyl transferase activity • transferase activity, transferring glycosyl groups • GO:0001948 protein binding • transferase activity • dolichyl-diphosphooligosaccharide-protein glycotransferase activity • metal ion binding Cellular component • endoplasmic reticulum membrane • integral component of membrane • endoplasmic reticulum • oligosaccharyltransferase complex • membrane • oligosaccharyltransferase III complex Biological process • co-translational protein modification • protein glycosylation • protein N-linked glycosylation via asparagine • post-translational modification Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	3703	16430
Ensembl	ENSG00000134910	ENSMUSG00000032116
UniProt	P46977	P46978
RefSeq (mRNA)	NM_001278503 NM_001278504 NM_152713	NM_008408
RefSeq (protein)	NP_001265432 NP_001265433 NP_689926	NP_032434
Location (UCSC)	Chr 11: 125.59 – 125.63 Mb	Chr 9: 36.73 – 36.77 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

The protein encoded by this gene is a catalytic subunit of the N-oligosaccharyltransferase (OST) complex, which functions in the endoplasmic reticulum to transfer glycan chains to asparagine residues of target proteins. A separate complex containing a similar catalytic subunit with an overlapping function also exists. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Aug 2015].

See also

• Oligosaccharyltransferase

References

1. GRCh38: Ensembl release 89: ENSG00000134910 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000032116 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: STT3A, catalytic subunit of the oligosaccharyltransferase complex". Retrieved 2018-07-12.

Further reading

• Ruiz-Canada C, Kelleher DJ, Gilmore R (January 2009). "Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms". Cell. 136 (2): 272–83. doi:10.1016/j.cell.2008.11.047. PMC 2859625. PMID 19167329.
• Patel MR, Stadler ME, Deal AM, Kim HS, Shores CG, Zanation AM (May 2011). "STT3A, C1orf24, TFF3: putative markers for characterization of follicular thyroid neoplasms from fine-needle aspirates". Laryngoscope. 121 (5): 983–9. doi:10.1002/lary.21736. PMID 21520112. S2CID 206198313.
• Sigstad E, Paus E, Bjøro T, Berner A, Grøholt KK, Jørgensen LH, Sobrinho-Simões M, Holm R, Warren DJ (April 2012). "The new molecular markers DDIT3, STT3A, ARG2 and FAM129A are not useful in diagnosing thyroid follicular tumors". Mod. Pathol. 25 (4): 537–47. doi:10.1038/modpathol.2011.188. PMC 3318159. PMID 22157935.
• Shrimal S, Ng BG, Losfeld ME, Gilmore R, Freeze HH (November 2013). "Mutations in STT3A and STT3B cause two congenital disorders of glycosylation". Hum. Mol. Genet. 22 (22): 4638–45. doi:10.1093/hmg/ddt312. PMC 3888133. PMID 23842455.
• Malaby HL, Kobertz WR (August 2014). "The middle X residue influences cotranslational N-glycosylation consensus site skipping". Biochemistry. 53 (30): 4884–93. doi:10.1021/bi500681p. PMC 4372077. PMID 25029371.
• Ghosh A, Urquhart J, Daly S, Ferguson A, Scotcher D, Morris AA, Clayton-Smith J (May 2017). "Phenotypic Heterogeneity in a Congenital Disorder of Glycosylation Caused by Mutations in STT3A" (PDF). J. Child Neurol. 32 (6): 560–565. doi:10.1177/0883073817696816. PMID 28424003. S2CID 11435676.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.