Mouse Anti-SFPQ (AA 269-362) Recombinant Antibody (CBXS-3608) (CBMAB-S0893-CQ)

splicing factor proline/glutamine-rich (polypyrimidine tract binding protein associated)

SFPQ (Splicing Factor Proline And Glutamine Rich) is a Protein Coding gene. Diseases associated with SFPQ include Renal Cell Carcinoma, Xp11-Associated and Adrenal Neuroblastoma. Among its related pathways are mRNA Splicing - Major Pathway and Signaling by PTK6. Gene Ontology (GO) annotations related to this gene include nucleic acid binding and nucleotide binding. An important paralog of this gene is PSPC1.

Splicing Factor Proline And Glutamine Rich; Polypyrimidine Tract Binding Protein Associated; Protein Phosphatase 1, Regulatory Subunit 140; DNA-Binding P52/P100 Complex, 100 KDa Subunit; Splicing Factor Proline/Glutamine-Rich; 100 KDa DNA-Pairing Protein; PSF; Splicing Factor Proline/Glutamine Rich (Polypyrimidine Tract-Binding Protein-Associated); Splicing Factor Proline/Glutamine Rich (Polypyrimidine Tract Binding Protein Associated);

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. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45, a phosphorylated form is sequestered by THRAP3 from the pre-mRNA in resting T-cells; T-cell activation and subsequent reduced phosphorylation is proposed to lead to release from THRAP3 allowing binding to pre-mRNA splicing regulatotry elements which represses exon inclusion. 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 binds DNA (PubMed:25765647).
The SFPQ-NONO heteromer may be involved in DNA non-homologous 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. Functions as transcriptional activator (PubMed:25765647).
Transcriptional repression is mediated by an interaction of SFPQ with SIN3A and subsequent recruitment of histone deacetylases (HDACs). The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional activity. 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. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation (By similarity).
Required for the assembly of nuclear speckles (PubMed:25765647).
Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728).

Biological Process activation of innate immune responseManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process alternative mRNA splicing, via spliceosomeManual Assertion Based On ExperimentIMP:BHF-UCL
Biological Process chromosome organizationIEA:Ensembl
Biological Process dendritic transport of messenger ribonucleoprotein complexIEA:Ensembl
Biological Process double-strand break repair via homologous recombinationManual Assertion Based On ExperimentIMP:MGI
Biological Process histone H3 deacetylationISS:UniProtKB
Biological Process innate immune responseIEA:UniProtKB-KW
Biological Process mRNA processingManual Assertion Based On ExperimentTAS:ProtInc
Biological Process negative regulation of circadian rhythmISS:UniProtKB
Biological Process negative regulation of DNA-templated transcriptionISS:UniProtKB
Biological Process negative regulation of transcription by RNA polymerase IIManual Assertion Based On ExperimentIDA:ParkinsonsUK-UCL
Biological Process positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathwayManual Assertion Based On ExperimentIDA:ParkinsonsUK-UCL
Biological Process positive regulation of sister chromatid cohesionIEA:Ensembl
Biological Process positive regulation of transcription by RNA polymerase IIManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process regulation of circadian rhythmISS:UniProtKB
Biological Process regulation of DNA-templated transcriptionManual Assertion Based On ExperimentIBA:GO_Central
Biological Process rhythmic processIEA:UniProtKB-KW
Biological Process RNA splicingManual Assertion Based On ExperimentTAS:ProtInc

Nucleus speckle
Nucleus matrix
Cytoplasm
Predominantly in nuclear matrix.

A chromosomal aberration involving SFPQ may be a cause of papillary renal cell carcinoma (PRCC). Translocation t(X;1)(p11.2;p34) with TFE3.

The N-terminus is blocked.
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. In resting T-cells is phosphorylated at Thr-687 by GSK3B which is proposed to promote association with THRAP and to prevent binding to PTPRC/CD45 pre-mRNA; T-cell activation leads to reduced phosphorylation at Thr-687.