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.
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 an 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.
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Cited for: NUCLEOTIDE SEQUENCE [MRNA];PARTIAL PROTEIN SEQUENCE;ALTERNATIVE SPLICING;FUNCTION
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Cited for: PROTEIN SEQUENCE OF 33-44; 218-236; 246-267; 272-286; 299-315; 320-330; 350-358; 364-407; 414-425; 431-462; 480-493; 517-536; 549-559; 567-572; 575-581; 600-606; 612-630 AND 667-695;METHYLATION AT LYS-314; ARG-571; ARG-681 AND ARG-693;IDENTIFICATION BY MASS SPECTROMETRY
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Cited for: PROTEIN SEQUENCE OF 48-68 AND 213-246;BLOCKAGE OF N-TERMINUS;DNA-BINDING;SUBUNIT
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Cited for: PROTEIN SEQUENCE OF 292-311; 415-421 AND 503-510;IDENTIFICATION IN U5/4/6 SNRNP COMPLEXES
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Cited for: PROTEIN SEQUENCE OF 299-314 AND 480-493;IDENTIFICATION BY MASS SPECTROMETRY
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Cited for: PROTEIN SEQUENCE OF 414-421 AND 427-448;SUBCELLULAR LOCATION;INTERACTION WITH SNRPA;IDENTIFICATION IN A SNRNP-FREE COMPLEX WITH SNRPA
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Cited for: PROTEIN SEQUENCE OF 600-606 AND 667-677;INTERACTION WITH PTBP1;SUBCELLULAR LOCATION
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Cited for: FUNCTION;INTERACTION WITH PRE-MRNA;IDENTIFICATION IN SPLICEOSOME COMPLEX
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Cited for: INTERACTION WITH TOP1;IDENTIFICATION IN A COMPLEX WITH NONO AND TOP1
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Cited for: FUNCTION IN TRANSCRIPTION REGULATION;IDENTIFICATION BY MASS SPECTROMETRY
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Cited for: FUNCTION IN HOMOLOGOUS DNA PAIRING;PHOSPHORYLATION
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Cited for: FUNCTION IN NUCLEAR RETENTION OF A-TO-I EDITED RNAS;IDENTIFICATION IN A COMPLEX WITH NONO AND MATR3
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Cited for: FUNCTION IN TRANSCRIPTION REGULATION;INTERACTION WITH RXRA; THRA AND SIN3A
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Cited for: FUNCTION IN TRANSCRIPTION REGULATION;INTERACTION WITH NR5A1 AND SIN3A;IDENTIFICATION IN A COMPLEX WITH NONO AND NR5A1
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Cited for: INTERACTION WITH NONO AND U5 SNRNA;IDENTIFICATION IN IN U5/4/6 SNRNP SND SPLICEOSOME COMPLEXES
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Cited for: FUNCTION IN DNA REPAIR;IDENTIFICATION BY MASS SPECTROMETRY;DNA-BINDING;SUBUNIT
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-687;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273 AND THR-687;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: PHOSPHORYLATION;INTERACTION WITH PTK6;SUBCELLULAR LOCATION
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-319; LYS-338; LYS-421 AND LYS-472;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: FUNCTION;PHOSPHORYLATION AT THR-687;INTERACTION WITH THRAP3;MUTAGENESIS OF THR-687
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND SER-626;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33; SER-273 AND SER-283;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]