SF1 (gene)

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
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RefSeq (mRNA)

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RefSeq (protein)

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Splicing factor 1 also known as zinc finger protein 162 (ZFM162) is a protein that in humans is encoded by the SF1 gene.[1][2][3]

Splicing factor SF1 is involved in the ATP-dependent formation of the spliceosome complex.[4]SF1 gene is necessary to make the bipotential gonad ; but while SF1 levels decline in the genital ridge of XX mouse embryos,the SF1 gene stays on the developing testes. SF 1 (transcription factor) appears to be active in masculining both the Leydig cells and Steroli cells. In Sterolic cells with the SOX9 protein it elevates the level of AMH transcription. In Leydig cells it activates the gene encoding the enzyme that make testosterone hormone.

Interactions

SF1 (gene) has been shown to interact with Ewing sarcoma breakpoint region 1,[5] U2AF2,[6][7][8] Testis determining factor,[9] and Transcription elongation regulator 1.[10]

References

  1. Toda T, Iida A, Miwa T, Nakamura Y, Imai T (Jul 1994). "Isolation and characterization of a novel gene encoding nuclear protein at a locus (D11S636) tightly linked to multiple endocrine neoplasia type 1 (MEN1)". Hum Mol Genet. 3 (3): 465–70. doi:10.1093/hmg/3.3.465. PMID 7912130.
  2. Kramer A, Quentin M, Mulhauser F (Jun 1998). "Diverse modes of alternative splicing of human splicing factor SF1 deduced from the exon-intron structure of the gene". Gene. 211 (1): 29–37. doi:10.1016/S0378-1119(98)00058-4. PMID 9573336.
  3. "Entrez Gene: SF1 splicing factor 1".
  4. Rino J, Desterro JM, Pacheco TR, Gadella TW, Carmo-Fonseca M (May 2008). "Splicing factors SF1 and U2AF associate in extraspliceosomal complexes". Mol. Cell. Biol. 28 (9): 3045–57. doi:10.1128/MCB.02015-07. PMC 2293075. PMID 18285458.
  5. Zhang D, Paley AJ, Childs G (July 1998). "The transcriptional repressor ZFM1 interacts with and modulates the ability of EWS to activate transcription". J. Biol. Chem. 273 (29): 18086–91. doi:10.1074/jbc.273.29.18086. PMID 9660765.
  6. Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
  7. Berglund JA, Abovich N, Rosbash M (March 1998). "A cooperative interaction between U2AF65 and mBBP/SF1 facilitates branchpoint region recognition". Genes Dev. 12 (6): 858–67. doi:10.1101/gad.12.6.858. PMC 316625. PMID 9512519.
  8. Abovich N, Rosbash M (May 1997). "Cross-intron bridging interactions in the yeast commitment complex are conserved in mammals". Cell. 89 (3): 403–12. doi:10.1016/S0092-8674(00)80221-4. PMID 9150140.
  9. Kashimada K, Koopman P (December 2010). "Sry: the master switch in mammalian sex determination". Development. 137 (23): 3921–30. doi:10.1242/dev.048983. PMID 21062860.
  10. Goldstrohm AC, Albrecht TR, Suñé C, Bedford MT, Garcia-Blanco MA (November 2001). "The transcription elongation factor CA150 interacts with RNA polymerase II and the pre-mRNA splicing factor SF1". Mol. Cell. Biol. 21 (22): 7617–28. doi:10.1128/MCB.21.22.7617-7628.2001. PMC 99933. PMID 11604498.

Further reading