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STT3A
Identifiers
Aliases	STT3A, ITM1, STT3-A, TMC, catalytic subunit of the oligosaccharyltransferase complex, STT3 oligosaccharyltransferase complex catalytic subunit A, CDG1WAR, CDG1WAD
External IDs	OMIM: 601134; MGI: 105124; HomoloGene: 40617; GeneCards: STT3A; OMA:STT3A - orthologs
Gene location (Human) Chr. Chromosome 11 (human) Band 11q24.2 Start 125,591,712 bp End 125,625,215 bp
Gene location (Mouse) Chr. Chromosome 9 (mouse) Band 9 A4|9 20.67 cM Start 36,640,640 bp End 36,678,975 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in stromal cell of endometrium body of pancreas islet of Langerhans canal of the cervix rectum Achilles tendon right ovary epithelium of colon ventricular zone left ovary Top expressed in otic placode cumulus cell saccule lacrimal gland submandibular gland gastrula calvaria seminal vesicula yolk sac molar More reference expression data BioGPS n/a
Gene ontology Molecular function oligosaccharyl transferase activity glycosyltransferase activity 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 protein 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: 36.64 – 36.68 Mb PubMed search
Wikidata
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STT3A, catalytic subunit of the oligosaccharyltransferase complex is a protein that in humans is encoded by the STT3A gene.

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. .

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.

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