SF1 (gene)

SF1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1K1G, 1O0P, 1OPI, 2M09, 4FXW, 4FXX
Identifiers
Aliases	SF1, BBP, D11S636, MBBP, ZCCHC25, ZFM1, ZNF162, splicing factor 1
External IDs	OMIM: 601516; MGI: 1095403; HomoloGene: 138518; GeneCards: SF1; OMA:SF1 - orthologs
Gene location (Human) Chr. Chromosome 11 (human)[1] Band 11q13.1 Start 64,764,606 bp[1] End 64,778,786 bp[1]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right uterine tube left ovary tibial nerve gastric mucosa right ovary right lobe of thyroid gland left uterine tube canal of the cervix right hemisphere of cerebellum left lobe of thyroid gland n/a More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transcription corepressor activity zinc ion binding metal ion binding protein binding nucleic acid binding identical protein binding pre-mRNA branch point binding RNA binding Cellular component ribosome spliceosomal complex nucleus nucleoplasm nuclear body Biological process negative regulation of smooth muscle cell proliferation regulation of transcription, DNA-templated Leydig cell differentiation mRNA processing regulation of steroid biosynthetic process male sex determination transcription, DNA-templated spliceosomal complex assembly mRNA 3'-splice site recognition RNA splicing negative regulation of nucleic acid-templated transcription mRNA splicing, via spliceosome nuclear body organization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 7536 22668 Ensembl ENSG00000168066 ENSMUSG00000024949 UniProt Q15637 Q64213 RefSeq (mRNA) NM_001178030 NM_001178031 NM_004630 NM_201995 NM_201997 NM_201998 NM_001346363 NM_001346364 NM_001346409 NM_001346410 NM_001378956 NM_001378957 NM_001110791 NM_011750 RefSeq (protein) NP_001171501 NP_001171502 NP_001333292 NP_001333293 NP_001333338 NP_001333339 NP_004621 NP_973724 NP_973726 NP_973727 NP_001365885 NP_001365886 NP_001104261 NP_035880 NP_001347322 NP_001390363 NP_001390364 NP_001390365 NP_001390368 NP_001390369 NP_001390370 NP_001390371 NP_001390372 NP_001390373 NP_001390374 NP_001390375 NP_001390376 NP_001390377 NP_001390378 Location (UCSC) Chr 11: 64.76 – 64.78 Mb n/a PubMed search [2] [3]
Wikidata
View/Edit Human View/Edit Mouse

Splicing factor 1 also known as zinc finger protein 162 (ZFM162) is a protein that in humans is encoded by the SF1 gene.[4][5][6]

Splicing factor SF1 is involved in the ATP-dependent formation of the spliceosome complex.[7] 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 Sertoli cells. In Sertoli 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,[8] U2AF2,[9][10][11] Testis determining factor,[12] and transcription elongation regulator 1.[13]

References

1. GRCh38: Ensembl release 89: ENSG00000168066 – Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. 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.
5. Kramer A, Quentin M, Mulhauser F (Jun 1998). "Diverse modes of alternative splicing of human splicing factor SF-1 deduced from the exon-intron structure of the gene". Gene. 211 (1): 29–37. doi:10.1016/S0378-1119(98)00058-4. PMID 9573336.
6. "Entrez Gene: SF1 splicing factor 1".
7. 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.
8. 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.
9. 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
10. 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.
11. 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. S2CID 18466775.
12. 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.
13. 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

• Krämer A (1992). "Purification of splicing factor SF1, a heat-stable protein that functions in the assembly of a presplicing complex". Mol. Cell. Biol. 12 (10): 4545–52. doi:10.1128/MCB.12.10.4545. PMC 360381. PMID 1406644.
• Naumovski L, Cleary ML (1996). "The p53-binding protein 53BP2 also interacts with Bc12 and impedes cell cycle progression at G2/M". Mol. Cell. Biol. 16 (7): 3884–92. doi:10.1128/MCB.16.7.3884. PMC 231385. PMID 8668206.
• Arning S, Grüter P, Bilbe G, Krämer A (1996). "Mammalian splicing factor SF1 is encoded by variant cDNAs and binds to RNA". RNA. 2 (8): 794–810. PMC 1369416. PMID 8752089.
• Abovich N, Rosbash M (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. S2CID 18466775.
• Caslini C, Spinelli O, Cazzaniga G, et al. (1997). "Identification of two novel isoforms of the ZNF162 gene: a growing family of signal transduction and activator of RNA proteins". Genomics. 42 (2): 268–77. doi:10.1006/geno.1997.4705. PMID 9192847.
• Zhang D, Childs G (1998). "Human ZFM1 protein is a transcriptional repressor that interacts with the transcription activation domain of stage-specific activator protein". J. Biol. Chem. 273 (12): 6868–77. doi:10.1074/jbc.273.12.6868. PMID 9506990.
• Berglund JA, Abovich N, Rosbash M (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.
• Zhang D, Paley AJ, Childs G (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.
• Neubauer G, King A, Rappsilber J, et al. (1998). "Mass spectrometry and EST-database searching allows characterization of the multi-protein spliceosome complex". Nat. Genet. 20 (1): 46–50. doi:10.1038/1700. PMID 9731529. S2CID 585778.
• Wang X, Bruderer S, Rafi Z, et al. (1999). "Phosphorylation of splicing factor SF1 on Ser20 by cGMP-dependent protein kinase regulates spliceosome assembly". EMBO J. 18 (16): 4549–59. doi:10.1093/emboj/18.16.4549. PMC 1171529. PMID 10449420.
• Lapteva N, Nieda M, Ando Y, et al. (2001). "Expression of renin-angiotensin system genes in immature and mature dendritic cells identified using human cDNA microarray". Biochem. Biophys. Res. Commun. 285 (4): 1059–65. doi:10.1006/bbrc.2001.5215. PMID 11467860.
• Goldstrohm AC, Albrecht TR, Suñé C, et al. (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.
• Liu Z, Luyten I, Bottomley MJ, et al. (2001). "Structural basis for recognition of the intron branch site RNA by splicing factor 1". Science. 294 (5544): 1098–102. Bibcode:2001Sci...294.1098L. doi:10.1126/science.1064719. PMID 11691992. S2CID 21402023.
• Rappsilber J, Ryder U, Lamond AI, Mann M (2002). "Large-scale proteomic analysis of the human spliceosome". Genome Res. 12 (8): 1231–45. doi:10.1101/gr.473902. PMC 186633. PMID 12176931.
• 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Selenko P, Gregorovic G, Sprangers R, et al. (2003). "Structural basis for the molecular recognition between human splicing factors U2AF65 and SF1/mBBP". Mol. Cell. 11 (4): 965–76. doi:10.1016/S1097-2765(03)00115-1. PMID 12718882.
• Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
• Lin KT, Lu RM, Tarn WY (2004). "The WW domain-containing proteins interact with the early spliceosome and participate in pre-mRNA splicing in vivo". Mol. Cell. Biol. 24 (20): 9176–85. doi:10.1128/MCB.24.20.9176-9185.2004. PMC 517884. PMID 15456888.