SELS (gene)

Selenoprotein S, also known as SELS, is a human gene.[5]

SELENOS
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesSELENOS, ADO15, SBBI8, SELS, SEPS1, AD-015, VIMP, VCP interacting membrane selenoprotein, selenoprotein S
External IDsOMIM: 607918 MGI: 95994 HomoloGene: 10200 GeneCards: SELENOS
Gene location (Human)
Chr.Chromosome 15 (human)[1]
Band15q26.3Start101,270,817 bp[1]
End101,277,500 bp[1]
Orthologs
SpeciesHumanMouse
Entrez

55829

109815

Ensembl

ENSG00000131871

ENSMUSG00000075701

UniProt

Q9BQE4

Q9BCZ4

RefSeq (mRNA)

NM_203472
NM_018445

NM_024439
NM_001348246

RefSeq (protein)

NP_060915
NP_982298

NP_001335175
NP_077759

Location (UCSC)Chr 15: 101.27 – 101.28 MbChr 7: 66.08 – 66.09 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

This gene encodes a selenoprotein, which contains a selenocysteine (Sec) residue at its active site. The selenocysteine is encoded by the UGA codon that normally signals translation termination. The 3' UTR of selenoprotein genes have a common stem-loop structure, the sec insertion sequence (SECIS), that is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. Studies suggest that this protein may regulate cytokine production, and thus play a key role in the control of the inflammatory response. Two alternatively spliced transcript variants encoding the same protein have been found for this gene.[5]

Interactions

SELS (gene) has been shown to interact with Valosin-containing protein.[6][7]

References

  1. GRCh38: Ensembl release 89: ENSG00000131871 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000075701 - 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: SELS selenoprotein S".
  6. Ye, Yihong; Shibata Yoko; Yun Chi; Ron David; Rapoport Tom A (Jun 2004). "A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol". Nature. 429 (6994): 841–847. doi:10.1038/nature02656. PMID 15215856.
  7. Wang, Qiuyan; Li Lianyun; Ye Yihong (Mar 2008). "Inhibition of p97-dependent Protein Degradation by Eeyarestatin I". J. Biol. Chem. 283 (12): 7445–7454. doi:10.1074/jbc.M708347200. ISSN 0021-9258. PMC 2276333. PMID 18199748.

Further reading

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