Human Gene SRSF5 (uc001xll.3) Description and Page Index
Description: Homo sapiens serine/arginine-rich splicing factor 5 (SRSF5), transcript variant 1, mRNA. RefSeq Summary (NM_006925): The protein encoded by this 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. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Feb 2016]. Transcript (Including UTRs) Position: hg19 chr14:70,193,619-70,238,722 Size: 45,104 Total Exon Count: 9 Strand: + Coding Region Position: hg19 chr14:70,234,874-70,238,178 Size: 3,305 Coding Exon Count: 7
ID:SRSF5_HUMAN DESCRIPTION: RecName: Full=Serine/arginine-rich splicing factor 5; AltName: Full=Delayed-early protein HRS; AltName: Full=Pre-mRNA-splicing factor SRP40; AltName: Full=Splicing factor, arginine/serine-rich 5; FUNCTION: Plays a role in constitutive splicing and can modulate the selection of alternative splice sites. SUBUNIT: Interacts (via RS domain) with PHF5A (via N-terminus) (By similarity). Found in a pre-mRNA splicing complex with SRSF4/SFRS4, SRSF5/SFRS5, SNRNP70, SNRPA1, SRRM1 and SRRM2. SUBCELLULAR LOCATION: Nucleus. PTM: Extensively phosphorylated on serine residues in the RS domain (By similarity). SIMILARITY: Belongs to the splicing factor SR family. SIMILARITY: Contains 2 RRM (RNA recognition motif) domains. SEQUENCE CAUTION: Sequence=AAC39543.1; Type=Frameshift; Positions=113, 140;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q13243
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.
Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.