SFPQ
entrez
6421
canonical
uniprot
P23246
canonical
ensembl
ENSG00000116560
resolver
ensp
ENSP00000349748
resolver
genesymbol
SFPQ
resolver
genesymbol_syn
PSF
resolver
hgnc
HGNC:10774
resolver
uniprot
A0A384N5Z8
resolver
uniprot
P30808
resolver
uniprot
Q5SZ71
resolver
uniprot
Q86VG2
resolver
uniprot_entry
A0A384N5Z8_HUMAN
resolver
uniprot_entry
Q86VG2_HUMAN
resolver
uniprot_entry
SFPQ_HUMAN
resolver
uniprot_sec
P30808
resolver
uniprot_sec
Q5SZ71
resolver
amino_acid_sequence
MSRDRFRSRGGGGGGFHRRGGGGGRGGLHDFRSPPPGMGLNQNRGPMGPGPGQSGPKPPIPPPPPHQQQQQPPPQQPPPQQPPPHQPPPHPQPHQQQQPPPPPQDSSKPVVAQGPGPAPGVGSAPPASSSAPPATPPTSGAPPGSGPGPTPTPPPAVTSAPPGAPPPTPPSSGVPTTPPQAGGPPPPPAAVPGPGPGPKQGPGPGGPKGGKMPGGPKPGGGPGLSTPGGHPKPPHRGGGEPRGGRQHHPPYHQQHHQGPPPGGPGGRSEEKISDSEGFKANLSLLRRPGEKTYTQRCRLFVGNLPADITEDEFKRLFAKYGEPGEVFINKGKGFGFIKLESRALAEIAKAELDDTPMRGRQLRVRFATHAAALSVRNLSPYVSNELLEEAFSQFGPIERAVVIVDDRGRSTGKGIVEFASKPAARKAFERCSEGVFLLTTTPRPVIVEPLEQLDDEDGLPEKLAQKNPMYQKERETPPRFAQHGTFEYEYSQRWKSLDEMEKQQREQVEKNMKDAKDKLESEMEDAYHEHQANLLRQDLMRRQEELRRMEELHNQEMQKRKEMQLRQEEERRRREEEMMIRQREMEEQMRRQREESYSRMGYMDPRERDMRMGGGGAMNMGDPYGSGGQKFPPLGGGGGIGYEANPGVPPATMSGSMMGSDMRTERFGQGGAGPVGGQGPRGMGPGTPAGYGRGREEYEGPNKKPRF
uniprot
proteins
disease_involvement
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.
uniprot
proteins
function
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. 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 a 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 a 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 IGF1-stimulated transcriptional activity. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-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). {ECO:0000250|UniProtKB:Q8VIJ6, ECO:0000269|PubMed:10847580, ECO:0000269|PubMed:10858305, ECO:0000269|PubMed:10931916, ECO:0000269|PubMed:11259580, ECO:0000269|PubMed:11525732, ECO:0000269|PubMed:11897684, ECO:0000269|PubMed:15590677, ECO:0000269|PubMed:20932480, ECO:0000269|PubMed:25765647, ECO:0000269|PubMed:28712728, ECO:0000269|PubMed:8045264, ECO:0000269|PubMed:8449401}.
uniprot
proteins
mass_dalton
76149
uniprot
proteins
mutagenesis
MUTAGEN 535; /note="L->A: Impairs DNA binding and ability to mediate transcriptional activation; when associated with A-539; A-546 and A-549."; /evidence="ECO:0000269|PubMed:25765647"; MUTAGEN 539; /note="L->A: Impairs DNA binding and ability to mediate transcriptional activation; when associated with A-535; A-546 and A-549."; /evidence="ECO:0000269|PubMed:25765647"; MUTAGEN 546; /note="L->A: Impairs DNA binding and ability to mediate transcriptional activation; when associated with A-535; A-539 and A-549."; /evidence="ECO:0000269|PubMed:25765647"; MUTAGEN 549; /note="M->A: Impairs DNA binding and ability to mediate transcriptional activation; when associated with A-535; A-539 and A-546."; /evidence="ECO:0000269|PubMed:25765647"; MUTAGEN 687; /note="T->A: Abolishes phosphorylation by GSK3B. Impairs interaction with THRAP3."; /evidence="ECO:0000269|PubMed:20932480"; MUTAGEN 687; /note="T->D: No effect on interaction with THRAP3 (phosphomimetic)."; /evidence="ECO:0000269|PubMed:20932480
uniprot
proteins
post_translational_modification
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. 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. {ECO:0000269|PubMed:10931916, ECO:0000269|PubMed:11514619, ECO:0000269|PubMed:17537995, ECO:0000269|PubMed:17965020, ECO:0000269|PubMed:19439179, ECO:0000269|PubMed:20932480}.
uniprot
proteins
pubmed
10653975
uniprot
proteins
pubmed
10847580
uniprot
proteins
pubmed
10858305
uniprot
proteins
pubmed
10931916
uniprot
proteins
pubmed
11259580
uniprot
proteins
pubmed
11514619
uniprot
proteins
pubmed
11525732
uniprot
proteins
pubmed
11897684
uniprot
proteins
pubmed
12403470
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
15590677
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
16767080
uniprot
proteins
pubmed
17537995
uniprot
proteins
pubmed
17965020
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18655028
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19439179
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20454556
uniprot
proteins
pubmed
20932480
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21933836
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
2480877
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
25765647
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26030138
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28712728
uniprot
proteins
pubmed
8045264
uniprot
proteins
pubmed
8439294
uniprot
proteins
pubmed
8449401
uniprot
proteins
pubmed
9393982
uniprot
proteins
pubmed
9409622
uniprot
proteins
pubmed
9756848
uniprot
proteins
pubmed
9848648
uniprot
proteins
sequence_length
707
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:25765647}. Nucleus matrix {ECO:0000269|PubMed:10653975, ECO:0000269|PubMed:19439179, ECO:0000269|PubMed:9848648}. Cytoplasm {ECO:0000269|PubMed:19439179}. Note=Predominantly in nuclear matrix. {ECO:0000269|PubMed:19439179}.
uniprot
proteins