SELS (gene)

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Selenoprotein S
File:PBB Protein SELS image.jpg
PDB rendering based on 2q2f.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols SELS ; AD-015; ADO15; MGC104346; MGC2553; SBBI8; SEPS1; VIMP
External IDs Template:OMIM5 Template:MGI HomoloGene10200
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Selenoprotein S, also known as SELS, is a human gene.[1]

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.[1]

References

  1. 1.0 1.1 "Entrez Gene: SELS selenoprotein S".

Further reading

  • Robertson NG, Khetarpal U, Gutiérrez-Espeleta GA; et al. (1995). "Isolation of novel and known genes from a human fetal cochlear cDNA library using subtractive hybridization and differential screening". Genomics. 23 (1): 42–50. doi:10.1006/geno.1994.1457. PMID 7829101.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. PMID 8125298.
  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. PMID 8889548.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K; et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. PMID 9373149.
  • Hu RM, Han ZG, Song HD; et al. (2000). "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning". Proc. Natl. Acad. Sci. U.S.A. 97 (17): 9543–8. doi:10.1073/pnas.160270997. PMID 10931946.
  • Walder K, Kantham L, McMillan JS; et al. (2002). "Tanis: a link between type 2 diabetes and inflammation?". Diabetes. 51 (6): 1859–66. PMID 12031974.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Gao Y, Walder K, Sunderland T; et al. (2003). "Elevation in Tanis expression alters glucose metabolism and insulin sensitivity in H4IIE cells". Diabetes. 52 (4): 929–34. PMID 12663463.
  • Kryukov GV, Castellano S, Novoselov SV; et al. (2003). "Characterization of mammalian selenoproteomes". Science. 300 (5624): 1439–43. doi:10.1126/science.1083516. PMID 12775843.
  • Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Gao Y, Feng HC, Walder K; et al. (2004). "Regulation of the selenoprotein SelS by glucose deprivation and endoplasmic reticulum stress - SelS is a novel glucose-regulated protein". FEBS Lett. 563 (1–3): 185–90. doi:10.1016/S0014-5793(04)00296-0. PMID 15063746.
  • Karlsson HK, Tsuchida H, Lake S; et al. (2004). "Relationship between serum amyloid A level and Tanis/SelS mRNA expression in skeletal muscle and adipose tissue from healthy and type 2 diabetic subjects". Diabetes. 53 (6): 1424–8. PMID 15161744.
  • Ye Y, Shibata Y, Yun C; et al. (2004). "A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol". Nature. 429 (6994): 841–7. doi:10.1038/nature02656. PMID 15215856.
  • Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
  • Lilley BN, Ploegh HL (2006). "Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane". Proc. Natl. Acad. Sci. U.S.A. 102 (40): 14296–301. doi:10.1073/pnas.0505014102. PMID 16186509.
  • Ye Y, Shibata Y, Kikkert M; et al. (2006). "Inaugural Article: Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane". Proc. Natl. Acad. Sci. U.S.A. 102 (40): 14132–8. doi:10.1073/pnas.0505006102. PMID 16186510.
  • Curran JE, Jowett JB, Elliott KS; et al. (2006). "Genetic variation in selenoprotein S influences inflammatory response". Nat. Genet. 37 (11): 1234–41. doi:10.1038/ng1655. PMID 16227999.
  • Gao Y, Hannan NR, Wanyonyi S; et al. (2006). "Activation of the selenoprotein SEPS1 gene expression by pro-inflammatory cytokines in HepG2 cells". Cytokine. 33 (5): 246–51. doi:10.1016/j.cyto.2006.02.005. PMID 16574427.
  • Gao Y, Pagnon J, Feng HC; et al. (2007). "Secretion of the glucose-regulated selenoprotein SEPS1 from hepatoma cells". Biochem. Biophys. Res. Commun. 356 (3): 636–41. doi:10.1016/j.bbrc.2007.03.018. PMID 17374524.
  • Seiderer J, Dambacher J, Kühnlein B; et al. (2007). "The role of the selenoprotein S (SELS) gene -105G>A promoter polymorphism in inflammatory bowel disease and regulation of SELS gene expression in intestinal inflammation". Tissue Antigens. 70 (3): 238–46. doi:10.1111/j.1399-0039.2007.00888.x. PMID 17661913.

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