FUSIP1
FUS-interacting serine-arginine-rich protein 1 is a protein that in humans is encoded by the SFRS13A gene.[1][2][3]
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.[3]
Interactions
FUSIP1 has been shown to interact with FUS.[4]
References
- ↑ 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.
- ↑ 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.
- ↑ 3.0 3.1 "Entrez Gene: FUSIP1 FUS interacting protein (serine/arginine-rich) 1".
- ↑ 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 et al. (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. Vancouver style error (help)
- Andersen JS, Lyon CE, Fox AH, Leung AK, Lam YW, Steen H et al. (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 et al. (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. Vancouver style error (help)
- Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S et al. (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 et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.