Srsf2 - serine and arginine-rich splicing factor 2 (house mouse)
Gene
Symbol
Taxonomy
Dates
- Create:2016-09-14
- Modify:2025-01-18
Description
The protein encoded by the Srsf2 gene is a member of the serine/arginine (SR)-rich family of pre-mRNA splicing factors, which constitute part of the spliceosome. Each of these factors contains an RNA recognition motif (RRM) for binding RNA and an RS domain for binding other proteins. The RS domain is rich in serine and arginine residues and facilitates interaction between different SR splicing factors. In addition to being critical for mRNA splicing, the SR proteins have also been shown to be involved in mRNA export from the nucleus and in translation. [provided by RefSeq, Sep 2010]
Enables pre-mRNA binding activity. Acts upstream of or within regulation of alternative mRNA splicing, via spliceosome. Located in nuclear speck. Part of spliceosomal complex. Is expressed in several structures, including central nervous system; early conceptus; hemolymphoid system gland; reproductive system; and retina. Used to study myelodysplastic syndrome. Human ortholog(s) of this gene implicated in acute myeloid leukemia; congestive heart failure; hepatocellular carcinoma; and myelodysplastic syndrome. Orthologous to human SRSF2 (serine and arginine rich splicing factor 2).
- D11Wsu175e
- MRF-1
- Pr264
- SC35
- Sfrs10
- Sfrs2
- serine/arginine-rich splicing factor 2
- myelin regulatory factor 1
- putative myelin regulatory factor 1
- splicing component, 35 kDa
- splicing factor Sc35
- splicing factor, arginine/serine-rich 2 (SC-35)
Necessary for the splicing of pre-mRNA. It is required for formation of the earliest ATP-dependent splicing complex and interacts with spliceosomal components bound to both the 5'- and 3'-splice sites during spliceosome assembly. It also is required for ATP-dependent interactions of both U1 and U2 snRNPs with pre-mRNA (By similarity). Can bind to the myelin basic protein (MBP) gene MB3 regulatory region and increase transcription of the mbp promoter in cells derived from the CNS. The phosphorylated form (by SRPK2) is required for cellular apoptosis in response to cisplatin treatment (By similarity).
Highly accurate protein structure prediction with AlphaFold. Nature. 2021 Aug;596(7873):583-589. DOI:10.1038/s41586-021-03819-2. PMID:34265844; PMCID:PMC8371605
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