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Gene Review

SEP15  -  15 kDa selenoprotein

Homo sapiens

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Disease relevance of SEP15


High impact information on SEP15

  • This, together with genetic data indicating loss of heterozygosity at the Sep15 locus in certain human tumor types, suggests that Sep15 may be involved in cancer development, risk, or both [3].
  • Here, we demonstrate significant differences in Sep15 allele frequencies by ethnicity and that the identity of the nucleotides at the polymorphic sites influences SECIS function in a selenium-dependent manner [3].
  • These data reveal that Sep15 and SelM are structural homologs that establish a new thioredoxin-like protein family [4].
  • In mammals, Sep15 expression is regulated by dietary selenium, and either decreased or increased expression of this selenoprotein alters redox homeostasis [4].
  • Association between the 15-kDa selenoprotein and UDP-glucose:glycoprotein glucosyltransferase in the endoplasmic reticulum of mammalian cells [5].

Biological context of SEP15

  • Since previous studies have implicated a potential role of the trace element selenium as a chemopreventive agent in animal models and in several types of human cancer, we investigated the effect of selenium on MM cells and its dependence on SEP15 genotype [1].
  • The 51-kilobase pair gene for the 15-kDa selenoprotein consisted of five exons and four introns and was localized on chromosome 1p31, a genetic locus commonly mutated or deleted in human cancers [6].
  • Selenoprotein P, selenoprotein W, a 15-kDa selenoprotein, an 18-kDa selenoprotein, and several selenoproteins identified in silico from nucleotide sequence databases were found to contain selenocysteine but their functions are not known [7].
  • Recently, a selenocysteine-containing oxidoreductase, Sep15, has been implicated in disulfide bond assisted protein folding, and a role in quality control for this selenoprotein has been proposed [8].
  • In contrast with other members of the Sep15 family, which contain a putative active site composed of Sec and cysteine, Fep15 has only Sec [9].

Anatomical context of SEP15

  • A gene, SEP15, encoding a 15-kDa selenium-containing protein was isolated using this approach and was subsequently shown to be downregulated in approximately 60% of MM cell lines and tumor specimens [1].


  1. Growth inhibition and induction of apoptosis in mesothelioma cells by selenium and dependence on selenoprotein SEP15 genotype. Apostolou, S., Klein, J.O., Mitsuuchi, Y., Shetler, J.N., Poulikakos, P.I., Jhanwar, S.C., Kruger, W.D., Testa, J.R. Oncogene (2004) [Pubmed]
  2. Multiple levels of regulation of selenoprotein biosynthesis revealed from the analysis of human glioma cell lines. Mansur, D.B., Hao, H., Gladyshev, V.N., Korotkov, K.V., Hu, Y., Moustafa, M.E., El-Saadani, M.A., Carlson, B.A., Hatfield, D.L., Diamond, A.M. Biochem. Pharmacol. (2000) [Pubmed]
  3. Distribution and functional consequences of nucleotide polymorphisms in the 3'-untranslated region of the human Sep15 gene. Hu, Y.J., Korotkov, K.V., Mehta, R., Hatfield, D.L., Rotimi, C.N., Luke, A., Prewitt, T.E., Cooper, R.S., Stock, W., Vokes, E.E., Dolan, M.E., Gladyshev, V.N., Diamond, A.M. Cancer Res. (2001) [Pubmed]
  4. NMR structures of the selenoproteins Sep15 and SelM reveal redox activity of a new thioredoxin-like family. Ferguson, A.D., Labunskyy, V.M., Fomenko, D.E., Araç, D., Chelliah, Y., Amezcua, C.A., Rizo, J., Gladyshev, V.N., Deisenhofer, J. J. Biol. Chem. (2006) [Pubmed]
  5. Association between the 15-kDa selenoprotein and UDP-glucose:glycoprotein glucosyltransferase in the endoplasmic reticulum of mammalian cells. Korotkov, K.V., Kumaraswamy, E., Zhou, Y., Hatfield, D.L., Gladyshev, V.N. J. Biol. Chem. (2001) [Pubmed]
  6. Structure-expression relationships of the 15-kDa selenoprotein gene. Possible role of the protein in cancer etiology. Kumaraswamy, E., Malykh, A., Korotkov, K.V., Kozyavkin, S., Hu, Y., Kwon, S.Y., Moustafa, M.E., Carlson, B.A., Berry, M.J., Lee, B.J., Hatfield, D.L., Diamond, A.M., Gladyshev, V.N. J. Biol. Chem. (2000) [Pubmed]
  7. Mammalian selenium-containing proteins. Behne, D., Kyriakopoulos, A. Annu. Rev. Nutr. (2001) [Pubmed]
  8. The Sep15 protein family: roles in disulfide bond formation and quality control in the endoplasmic reticulum. Labunskyy, V.M., Hatfield, D.L., Gladyshev, V.N. IUBMB Life (2007) [Pubmed]
  9. Identification and characterization of Fep15, a new selenocysteine-containing member of the Sep15 protein family. Novoselov, S.V., Hua, D., Lobanov, A.V., Gladyshev, V.N. Biochem. J. (2006) [Pubmed]
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