ID:SFPQ_HUMAN DESCRIPTION: RecName: Full=Splicing factor, proline- and glutamine-rich; AltName: Full=100 kDa DNA-pairing protein; Short=hPOMp100; AltName: Full=DNA-binding p52/p100 complex, 100 kDa subunit; AltName: Full=Polypyrimidine tract-binding protein-associated-splicing factor; Short=PSF; Short=PTB-associated-splicing factor; FUNCTION: DNA- and RNA binding protein, involved in several nuclear processes. Essential pre-mRNA splicing factor required early in spliceosome formation and for splicing catalytic step II, probably as a heteromer with NONO. Binds to pre-mRNA in spliceosome C complex, and specifically binds to intronic polypyrimidine tracts. Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b. May be involved in a pre-mRNA coupled splicing and polyadenylation process as component of a snRNP-free complex with SNRPA/U1A. The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs. SFPQ may be involved in homologous DNA pairing; in vitro, promotes the invasion of ssDNA between a duplex DNA and produces a D-loop formation. The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1; in vitro, stimulates dissociation of TOP1 from DNA after cleavage and enhances its jumping between separate DNA helices. The SFPQ-NONO heteromer may be involved in DNA nonhomologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends; in vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex. SFPQ is involved in transcriptional regulation. Transcriptional repression is probably mediated by an interaction of SFPQ with SIN3A and subsequent recruitment of histone deacetylases (HDACs). The SFPQ-NONO/SF-1 complex binds to the CYP17 promoter and regulates basal and cAMP- dependent transcriptional avtivity. SFPQ isoform Long binds to the DNA binding domains (DBD) of nuclear hormone receptors, like RXRA and probably THRA, and acts as transcriptional corepressor in absence of hormone ligands. Binds the DNA sequence 5'-CTGAGTC-3' in the insulin-like growth factor response element (IGFRE) and inhibits IGF-I-stimulated transcriptional activity. SUBUNIT: Interacts with PSPC1 (By similarity). Monomer and component of the SFPQ-NONO complex, which is probably a heterotetramer of two 52 kDa (NONO) and two 100 kDa (SFPQ) subunits. SFPQ is a component of spliceosome and U5.4/6 snRNP complexes. Interacts with SNRPA/U1A. Component of a snRNP-free complex with SNRPA/U1A. Part of complex consisting of SFPQ, NONO and MATR3. Interacts with polypyrimidine tract-binding protein 1/PTB. Part of a complex consisting of SFPQ, NONO and NR5A1. Interacts with RXRA, probably THRA, and SIN3A. Interacts with TOP1. Part of a complex consisting of SFPQ, NONO and TOP1. Interacts with SNRNP70 in apoptotic cells (By similarity). Interacts with RNF43. Interacts with PITX3 and NR4A2/NURR1 (By similarity). Interacts with PTK6. INTERACTION: P26599:PTBP1; NbExp=2; IntAct=EBI-355453, EBI-350540; P28700:Rxra (xeno); NbExp=3; IntAct=EBI-355463, EBI-346715; Q96ST3:SIN3A; NbExp=2; IntAct=EBI-355453, EBI-347218; P09012:SNRPA; NbExp=4; IntAct=EBI-355453, EBI-607085; P04625:THRA (xeno); NbExp=2; IntAct=EBI-355463, EBI-286261; SUBCELLULAR LOCATION: Nucleus matrix. Cytoplasm. Note=Predominantly in nuclear matrix. PTM: The N-terminus is blocked. PTM: Phosphorylated on multiple serine and threonine residues during apoptosis. In vitro phosphorylated by PKC. Phosphorylation stimulates binding to DNA and D-loop formation, but inhibits binding to RNA. Phosphorylation of C-terminal tyrosines promotes its cytoplasmic localization, impaired its binding to polypyrimidine RNA and led to cell cycle arrest. PTM: Arg-7, Arg-9, Arg-19 and Arg-25 are dimethylated, probably to asymmetric dimethylarginine. DISEASE: Note=A chromosomal aberration involving SFPQ may be a cause of papillary renal cell carcinoma (PRCC). Translocation t(X;1)(p11.2;p34) with TFE3. SIMILARITY: Contains 2 RRM (RNA recognition motif) domains. CAUTION: Was originally (PubMed:2480877) thought to be myoblast cell surface antigen 24.1D5 and a possible membrane-bound protein ectokinase. WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/PSFID167.html";
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 P23246
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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.
US Server
Sequence and Links to Tools and Databases 
Common Gene Haplotype Alleles 
