FUS-interacting serine-arginine-rich protein 1 is a protein that in humans is encoded by the SFRS13Agene.
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.
^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". Gene284 (1–2): 141–7. doi:10.1016/S0378-1119(02)00382-7. PMID11891055.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID9373149.
Cowper AE, Cáceres JF, Mayeda A, Screaton GR (2002). "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. PMID11684676.
Jin J, Smith FD, Stark C 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. PMID15324660.
Benzinger A, Muster N, Koch HB et al. (2005). "Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer". Mol. Cell Proteomics4 (6): 785–95. doi:10.1074/mcp.M500021-MCP200. PMID15778465.