Stt3a, catalytic subunit of the oligosaccharyltransferase complex

STT3A
Identifiers
AliasesSTT3A, ITM1, STT3-A, TMC, catalytic subunit of the oligosaccharyltransferase complex
External IDsMGI: 105124 HomoloGene: 40617 GeneCards: STT3A
Gene location (Human)
Chr.Chromosome 11 (human)[1]
Band11q24.2Start125,591,712 bp[1]
End125,625,215 bp[1]
Orthologs
SpeciesHumanMouse
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 MbChr 9: 36.73 – 36.77 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

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

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000134910 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000032116 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  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.
  • 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". J. Child Neurol. 32 (6): 560–565. doi:10.1177/0883073817696816. PMID 28424003.


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