UniProt Accession

 SFPQ_HUMAN; P23246; P30808; Q5SZ71 

Genbank Protein ID

 X70944; AL590434; CH471059; X16850 

Genbank Nucleotide ID

 CAA50283.1; CAI12467.1; EAX07426.1; CAA34747.1 

Protein Name

 Splicing factor, proline- and glutamine-rich 

Protein Synonyms/Alias

 100 kDa DNA-pairing protein; hPOMp100; DNA-binding p52/p100 complex, 100 kDa subunit; Polypyrimidine tract-binding protein-associated-splicing factor; PSF; PTB-associated-splicing factor 

Gene Name

 SFPQ 

Gene Synonyms/Alias

 PSF 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
279	ISDSEGFKANLSLLR	ubiquitination	[1]
330	PGEVFINKGKGFGFI	ubiquitination	[1]
338	GKGFGFIKLESRALA	ubiquitination	[1]
413	DRGRSTGKGIVEFAS	ubiquitination	[1]
466	LPEKLAQKNPMYQKE	ubiquitination	[1]

Reference

 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 

Functional Description

 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 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. 

Sequence Annotation

 REPEAT 9 11 1.
 REPEAT 19 21 2.
 REPEAT 25 27 3.
 DOMAIN 297 369 RRM 1.
 DOMAIN 371 452 RRM 2.
 REGION 9 27 3 X 3 AA repeats of R-G-G.
 MOD_RES 8 8 Phosphoserine; by MKNK2.
 MOD_RES 33 33 Phosphoserine.
 MOD_RES 273 273 Phosphoserine.
 MOD_RES 283 283 Phosphoserine; by MKNK2.
 MOD_RES 293 293 Phosphotyrosine; by ALK.
 MOD_RES 314 314 N6,N6-dimethyllysine.
 MOD_RES 319 319 N6-acetyllysine.
 MOD_RES 338 338 N6-acetyllysine.
 MOD_RES 379 379 Phosphoserine.
 MOD_RES 421 421 N6-acetyllysine.
 MOD_RES 472 472 N6-acetyllysine.
 MOD_RES 571 571 Dimethylated arginine.
 MOD_RES 626 626 Phosphoserine.
 MOD_RES 681 681 Omega-N-methylarginine.
 MOD_RES 687 687 Phosphothreonine.
 MOD_RES 693 693 Dimethylated arginine.  

Keyword

 Acetylation; Activator; Alternative splicing; Chromosomal rearrangement; Complete proteome; Cytoplasm; Direct protein sequencing; DNA damage; DNA recombination; DNA repair; DNA-binding; Methylation; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor; RNA-binding; Transcription; Transcription regulation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 707 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0016363; C:nuclear matrix; IDA:BHF-UCL.
 GO:0042382; C:paraspeckles; IDA:BHF-UCL.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0000380; P:alternative mRNA splicing, via spliceosome; IMP:BHF-UCL.
 GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
 GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 

Interpro

 IPR012975; NOPS.
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 

Pfam

 PF08075; NOPS
 PF00076; RRM_1 

SMART

 SM00360; RRM 

PROSITE

 PS50102; RRM 

PRINTS