FUSIP1

FUS-interacting serine-arginine-rich protein 1 is a protein that in humans is encoded by the SFRS13A gene.[5][6][7]

SRSF10
Identifiers
Aliases	SRSF10, FUSIP1, FUSIP2, NSSR, PPP1R149, SFRS13, SFRS13A, SRp38, SRrp40, TASR, TASR1, TASR2, serine/arginine-rich splicing factor 10, serine and arginine rich splicing factor 10
External IDs	OMIM: 605221 MGI: 1333805 HomoloGene: 134051 GeneCards: SRSF10
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1p36.11 Start 23,964,347 bp[1] End 23,980,927 bp[1]
Gene location (Mouse) Chr. Chromosome 4 (mouse)[2] Band 4|4 D3 Start 135,855,747 bp[2] End 135,869,908 bp[2]
Gene ontology Molecular function • unfolded protein binding • RS domain binding • GO:0001948 protein binding • nucleic acid binding • RNA binding Cellular component • cytoplasm • cell nucleus • nucleoplasm • cytosol • nuclear speck Biological process • RNA splicing, via transesterification reactions • mRNA splicing, via spliceosome • mRNA processing • spliceosomal tri-snRNP complex assembly • regulation of transcription, DNA-templated • negative regulation of mRNA splicing, via spliceosome • mRNA splice site selection • mRNA export from nucleus • RNA splicing • regulation of mRNA splicing, via spliceosome • cytosolic transport • regulation of RNA splicing • regulation of alternative mRNA splicing, via spliceosome • mRNA 5'-splice site recognition • mRNA cis splicing, via spliceosome Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	10772	14105
Ensembl	ENSG00000188529	ENSMUSG00000028676
UniProt	O75494 Q5JRI1	Q9R0U0
RefSeq (mRNA)	NM_001191005 NM_001191006 NM_001191007 NM_001191009 NM_001300936 NM_001300937 NM_006625 NM_054016	NM_001080387 NM_001284195 NM_001284196 NM_010178
RefSeq (protein)	NP_001177934 NP_001177935 NP_001177936 NP_001177938 NP_001287865 NP_001287866 NP_006616 NP_473357 NP_001287865.1	NP_001073856 NP_001271124 NP_001271125 NP_034308
Location (UCSC)	Chr 1: 23.96 – 23.98 Mb	Chr 4: 135.86 – 135.87 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

This gene product is a member of the serine-arginine (SR) family of proteins, which is involved in constitutive and regulated RNA splicing. Members of this family are characterized by N-terminal RNP1 and RNP2 motifs, which are required for binding to RNA, and multiple C-terminal SR/RS repeats, which are important in mediating association with other cellular proteins. This protein can influence splice site selection of adenovirus E1A pre-mRNA. It interacts with the oncoprotein TLS, and abrogates the influence of TLS on E1A pre-mRNA splicing. Alternative splicing of this gene results in at least two transcript variants encoding different isoforms. In addition, transcript variants utilizing alternative polyA sites exist.[7]

Interactions

FUSIP1 has been shown to interact with FUS.[8]

References

1. GRCh38: Ensembl release 89: ENSG00000188529 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000028676 - 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. Yang L, Embree LJ, Tsai S, Hickstein DD (November 1998). "Oncoprotein TLS interacts with serine-arginine proteins involved in RNA splicing". J. Biol. Chem. 273 (43): 27761–4. doi:10.1074/jbc.273.43.27761. PMID 9774382.
6. Clinton JM, Chansky HA, Odell DD, Zielinska-Kwiatkowska A, Hickstein DD, Yang L (March 2002). "Characterization and expression of the human gene encoding two translocation liposarcoma protein-associated serine-arginine (TASR) proteins". Gene. 284 (1–2): 141–7. doi:10.1016/S0378-1119(02)00382-7. PMID 11891055.
7. "Entrez Gene: FUSIP1 FUS interacting protein (serine/arginine-rich) 1".
8. Yang L, Embree LJ, Hickstein DD (May 2000). "TLS-ERG leukemia fusion protein inhibits RNA splicing mediated by serine-arginine proteins". Mol. Cell. Biol. 20 (10): 3345–54. doi:10.1128/MCB.20.10.3345-3354.2000. PMC 85627. PMID 10779324.

Further reading

• 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. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
• Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Yang L, Embree LJ, Hickstein DD (2000). "TLS-ERG leukemia fusion protein inhibits RNA splicing mediated by serine-arginine proteins". Mol. Cell. Biol. 20 (10): 3345–54. doi:10.1128/MCB.20.10.3345-3354.2000. PMC 85627. PMID 10779324.
• Cowper AE, Cáceres JF, Mayeda A, Screaton GR (2001). "Serine-arginine (SR) protein-like factors that antagonize authentic SR proteins and regulate alternative splicing". J. Biol. Chem. 276 (52): 48908–14. doi:10.1074/jbc.M103967200. PMID 11684676.
• Andersen JS, Lyon CE, Fox AH, Leung AK, Lam YW, Steen H, Mann M, Lamond AI (2002). "Directed proteomic analysis of the human nucleolus". Curr. Biol. 12 (1): 1–11. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298.
• Shin C, Manley JL (2002). "The SR protein SRp38 represses splicing in M phase cells". Cell. 111 (3): 407–17. doi:10.1016/S0092-8674(02)01038-3. PMID 12419250.
• Li J, Hawkins IC, Harvey CD, Jennings JL, Link AJ, Patton JG (2003). "Regulation of alternative splicing by SRrp86 and its interacting proteins". Mol. Cell. Biol. 23 (21): 7437–47. doi:10.1128/MCB.23.21.7437-7447.2003. PMC 207616. PMID 14559993.
• Shin C, Feng Y, Manley JL (2004). "Dephosphorylated SRp38 acts as a splicing repressor in response to heat shock". Nature. 427 (6974): 553–8. doi:10.1038/nature02288. PMID 14765198.
• Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
• Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S, Metalnikov P, O'Donnell P, Taylor P, Taylor L, Zougman A, Woodgett JR, Langeberg LK, Scott JD, Pawson T (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.
• Benzinger A, Muster N, Koch HB, Yates JR, Hermeking H (2005). "Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer". Mol. Cell. Proteomics. 4 (6): 785–95. doi:10.1074/mcp.M500021-MCP200. PMID 15778465.
• Shin C, Kleiman FE, Manley JL (2005). "Multiple properties of the splicing repressor SRp38 distinguish it from typical SR proteins". Mol. Cell. Biol. 25 (18): 8334–43. doi:10.1128/MCB.25.18.8334-8343.2005. PMC 1234314. PMID 16135820.
• 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 (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.