Q8VIJ6 (SFPQ_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified May 29, 2013. Version 110. History...
Names and origin
|Protein names||Recommended name:|
Splicing factor, proline- and glutamine-rich
DNA-binding p52/p100 complex, 100 kDa subunit
Polypyrimidine tract-binding protein-associated-splicing factor
Short name=PTB-associated-splicing factor
|Organism||Mus musculus (Mouse) [Reference proteome]|
|Taxonomic identifier||10090 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus|
|Sequence length||699 AA.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
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-NR5A1 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 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. Interacts with PSPC1. Interacts with RNF43. Interacts with PITX3 and NR4A2/NURR1. Interacts with PTK6. Interacts with THRAP3; the interaction is dependent on SFPQ phosphorylation at 'Thr-679' and inhibits binding of SFPQ to a ESS1 exonic splicing silencer element-containing RNA. Ref.6 Ref.7
Phosphorylated on multiple serine and threonine residues during apoptosis By similarity. Phosphorylation of C-terminal tyrosines promotes its cytoplasmic localization, impaired its binding to polypyrimidine RNA and led to cell cycle arrest By similarity. In resting T-cells is phosphorylated at Thr-679 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-679.
Contains 2 RRM (RNA recognition motif) domains.
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 699||699||Splicing factor, proline- and glutamine-rich||PRO_0000081910|
|Repeat||9 – 11||3||1|
|Repeat||19 – 21||3||2|
|Repeat||25 – 27||3||3|
|Domain||289 – 361||73||RRM 1|
|Domain||363 – 444||82||RRM 2|
|Region||9 – 27||19||3 X 3 AA repeats of R-G-G|
|Compositional bias||10 – 258||249||Gln/Glu/Pro-rich|
|Compositional bias||10 – 15||6||Poly-Gly|
|Compositional bias||20 – 27||8||Poly-Gly|
|Compositional bias||54 – 63||10||Poly-Pro|
|Compositional bias||65 – 69||5||Poly-Gln|
|Compositional bias||96 – 100||5||Poly-Pro|
|Compositional bias||158 – 161||4||Poly-Pro|
|Compositional bias||178 – 182||5||Poly-Pro|
|Compositional bias||563 – 566||4||Poly-Arg|
|Compositional bias||605 – 608||4||Poly-Gly|
|Compositional bias||627 – 633||7||Poly-Gly|
Amino acid modifications
|Modified residue||7||1||Omega-N-methylated arginine By similarity|
|Modified residue||8||1||Phosphoserine; by MKNK2 By similarity|
|Modified residue||9||1||Omega-N-methylated arginine By similarity|
|Modified residue||19||1||Omega-N-methylated arginine By similarity|
|Modified residue||25||1||Omega-N-methylated arginine By similarity|
|Modified residue||33||1||Phosphoserine By similarity|
|Modified residue||265||1||Phosphoserine By similarity|
|Modified residue||275||1||Phosphoserine; by MKNK2 By similarity|
|Modified residue||285||1||Phosphotyrosine; by ALK By similarity|
|Modified residue||306||1||N6,N6-dimethyllysine By similarity|
|Modified residue||311||1||N6-acetyllysine By similarity|
|Modified residue||330||1||N6-acetyllysine By similarity|
|Modified residue||371||1||Phosphoserine By similarity|
|Modified residue||413||1||N6-acetyllysine By similarity|
|Modified residue||464||1||N6-acetyllysine By similarity|
|Modified residue||563||1||Dimethylated arginine By similarity|
|Modified residue||618||1||Phosphoserine By similarity|
|Modified residue||673||1||Omega-N-methylarginine By similarity|
|Modified residue||679||1||Phosphothreonine By similarity|
|Modified residue||685||1||Dimethylated arginine By similarity|
|Sequence conflict||47||1||M → Q AA sequence Ref.4|
|Sequence conflict||546||1||S → N in AAG17365. Ref.4|
|||"Nuclear relocalization of the pre-mRNA splicing factor PSF during apoptosis involves hyperphosphorylation, masking of antigenic epitopes, and changes in protein interactions."|
Shav-Tal Y., Cohen M., Lapter S., Dye B., Patton J.G., Vandekerckhove J., Zipori D.
Mol. Biol. Cell 12:2328-2340(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Bone marrow.
|||"Lineage-specific biology revealed by a finished genome assembly of the mouse."|
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
|||"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."|
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
|||"Enhanced proteolysis of pre-mRNA splicing factors in myeloid cells."|
Shav-Tal Y., Lee B., Bar-Haim S., Vandekerckhove J., Zipori D.
Exp. Hematol. 28:1029-1038(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 198-580, PROTEIN SEQUENCE OF 20-30; 47-55 AND 210-238.
Tissue: Bone marrow.
|||Lubec G., Sunyer B., Chen W.-Q.|
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 291-306; 312-322; 358-368 AND 472-485, MASS SPECTROMETRY.
|||"Expression and functional significance of mouse paraspeckle protein 1 on spermatogenesis."|
Myojin R., Kuwahara S., Yasaki T., Matsunaga T., Sakurai T., Kimura M., Uesugi S., Kurihara Y.
Biol. Reprod. 71:926-932(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PSPC1.
|||"Pitx3 potentiates Nurr1 in dopamine neuron terminal differentiation through release of SMRT-mediated repression."|
Jacobs F.M., van Erp S., van der Linden A.J., von Oerthel L., Burbach J.P., Smidt M.P.
Development 136:531-540(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PITX3 AND NR4A2.
|+||Additional computationally mapped references.|
|AY034062 mRNA. Translation: AAK60397.1.|
AL606985 Genomic DNA. Translation: CAM15587.1.
BC089305 mRNA. Translation: AAH89305.1.
AF272847 mRNA. Translation: AAG17365.1.
|RefSeq||NP_076092.1. NM_023603.3. |
3D structure databases
|SMR||Q8VIJ6. Positions 279-527. |
Protein-protein interaction databases
|IntAct||Q8VIJ6. 1 interaction.|
2D gel databases
Protocols and materials databases
Genome annotation databases
|Ensembl||ENSMUST00000030623; ENSMUSP00000030623; ENSMUSG00000028820. |
|UCSC||uc008utz.2. mouse. |
|MGI||MGI:1918764. Sfpq. |
Gene expression databases
|GermOnline||ENSMUSG00000028820. Mus musculus. |
Family and domain databases
|Gene3D||18.104.22.1680. 2 hits. |
|InterPro||IPR012975. NOPS. |
|Pfam||PF08075. NOPS. 1 hit. |
PF00076. RRM_1. 2 hits.
|SMART||SM00360. RRM. 2 hits. |
|PROSITE||PS50102. RRM. 2 hits. |
|ChiTaRS||SFPQ. mouse. |
|Accession||Primary (citable) accession number: Q8VIJ6|
Secondary accession number(s): A2A7U6, Q9ERW2
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|