Splicing factor, proline- and glutamine-rich

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Q8VIJ6 (SFPQ_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 110. History...

Clusters with 100%, 90%, 50% identity |

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Splicing factor, proline- and glutamine-rich

Alternative name(s):
DNA-binding p52/p100 complex, 100 kDa subunit
Polypyrimidine tract-binding protein-associated-splicing factor
Short name=PSF
Short name=PTB-associated-splicing factor

Gene names

Name:

Sfpq

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

Protein attributes

Sequence length	699 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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 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.
Subunit structure	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
Subcellular location	Nucleus matrix By similarity. Cytoplasm By similarity. Note: Predominantly in nuclear matrix By similarity.
Post-translational modification	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.
Sequence similarities	Contains 2 RRM (RNA recognition motif) domains.

Ontologies

Keywords
Biological process	DNA damage DNA repair Transcription Transcription regulation mRNA processing mRNA splicing
Cellular component	Cytoplasm Nucleus
Domain	Repeat
Ligand	DNA-binding RNA-binding
Molecular function	Activator Repressor
PTM	Acetylation Methylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW alternative mRNA splicing, via spliceosome Inferred from electronic annotation. Source: Compara regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear matrix Inferred from electronic annotation. Source: UniProtKB-SubCell paraspeckles Inferred from electronic annotation. Source: Compara
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 699

699

Splicing factor, proline- and glutamine-rich

PRO_0000081910

Regions

Repeat

Repeat

Repeat

Domain

RRM 1

Domain

363 – 444

RRM 2

Region

9 – 27

3 X 3 AA repeats of R-G-G

Compositional bias

10 – 258

249

Gln/Glu/Pro-rich

Compositional bias

10 – 15

Poly-Gly

Compositional bias

20 – 27

Poly-Gly

Compositional bias

54 – 63

Poly-Pro

Compositional bias

65 – 69

Poly-Gln

Compositional bias

96 – 100

Poly-Pro

Compositional bias

158 – 161

Poly-Pro

Compositional bias

178 – 182

Poly-Pro

Compositional bias

563 – 566

Poly-Arg

Compositional bias

605 – 608

Poly-Gly

Compositional bias

627 – 633

Poly-Gly

Amino acid modifications

Modified residue

Omega-N-methylated arginine By similarity

Modified residue

Phosphoserine; by MKNK2 By similarity

Modified residue

Omega-N-methylated arginine By similarity

Modified residue

Omega-N-methylated arginine By similarity

Modified residue

Omega-N-methylated arginine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

265

Phosphoserine By similarity

Modified residue

275

Phosphoserine; by MKNK2 By similarity

Modified residue

285

Phosphotyrosine; by ALK By similarity

Modified residue

306

N6,N6-dimethyllysine By similarity

Modified residue

311

N6-acetyllysine By similarity

Modified residue

330

N6-acetyllysine By similarity

Modified residue

371

Phosphoserine By similarity

Modified residue

413

N6-acetyllysine By similarity

Modified residue

464

N6-acetyllysine By similarity

Modified residue

563

Dimethylated arginine By similarity

Modified residue

618

Phosphoserine By similarity

Modified residue

673

Omega-N-methylarginine By similarity

Modified residue

679

Phosphothreonine By similarity

Modified residue

685

Dimethylated arginine By similarity

Experimental info

Sequence conflict

M → Q AA sequence Ref.4

Sequence conflict

546

S → N in AAG17365. Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

Q8VIJ6 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 714F786264C63AA0
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FASTA

699

75,442

        10         20         30         40         50         60 
MSRDRFRSRG GGGGGFHRRG GGGGRGGLHD FRSPPPGMGL NQNRGPMGPG PGGPKPPLPP 

        70         80         90        100        110        120 
PPPHQQQQQP PPQQPPPQQP PPHQQPPPHQ PPHQQPPPPP QESKPVVPQG PGSAPGVSSA 

       130        140        150        160        170        180 
PPPAVSAPPA NPPTTGAPPG PGPTPTPPPA VPSTAPGPPP PSTPSSGVST TPPQTGGPPP 

       190        200        210        220        230        240 
PPAGGAGPGP KPGPGPGGPK GGKMPGGPKP GGGPGMGAPG GHPKPPHRGG GEPRGGRQHH 

       250        260        270        280        290        300 
APYHQQHHQG PPPGGPGPRT EEKISDSEGF KANLSLLRRP GEKTYTQRCR LFVGNLPADI 

       310        320        330        340        350        360 
TEDEFKRLFA KYGEPGEVFI NKGKGFGFIK LESRALAEIA KAELDDTPMR GRQLRVRFAT 

       370        380        390        400        410        420 
HAAALSVRNL SPYVSNELLE EAFSQFGPIE RAVVIVDDRG RSTGKGIVEF ASKPAARKAF 

       430        440        450        460        470        480 
ERCSEGVFLL TTTPRPVIVE PLEQLDDEDG LPEKLAQKNP MYQKERETPP RFAQHGTFEY 

       490        500        510        520        530        540 
EYSQRWKSLD EMEKQQREQV EKNMKDAKDK LESEMEDAYH EHQANLLRQD LMRRQEELRR 

       550        560        570        580        590        600 
MEELHSQEMQ KRKEMQLRQE EERRRREEEM MIRQREMEEQ MRRQREESYS RMGYMDPRER 

       610        620        630        640        650        660 
DMRMGGGGTM NMGDPYGSGG QKFPPLGGGG GIGYEANPGV PPATMSGSMM GSDMRTERFG 

       670        680        690 
QGGAGPVGGQ GPRGMGPGTP AGYGRGREEY EGPNKKPRF

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"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]. Strain: C57BL/6J.
[3]	"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]. Strain: C57BL/6. Tissue: Brain.
[4]	"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.
[5]	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. Strain: OF1. Tissue: Hippocampus.
[6]	"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.
[7]	"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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY034062 mRNA. Translation: AAK60397.1. AL606985 Genomic DNA. Translation: CAM15587.1. BC089305 mRNA. Translation: AAH89305.1. AF272847 mRNA. Translation: AAG17365.1.
IPI	IPI00129430.
RefSeq	NP_076092.1. NM_023603.3.
UniGene	Mm.257276. Mm.482296.
3D structure databases
ProteinModelPortal	Q8VIJ6.
SMR	Q8VIJ6. Positions 279-527.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8VIJ6. 1 interaction.
MINT	MINT-4120373.
PTM databases
PhosphoSite	Q8VIJ6.
2D gel databases
REPRODUCTION-2DPAGE	Q8VIJ6.
Proteomic databases
PaxDb	Q8VIJ6.
PRIDE	Q8VIJ6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000030623; ENSMUSP00000030623; ENSMUSG00000028820.
GeneID	71514.
KEGG	mmu:71514.
UCSC	uc008utz.2. mouse.
Organism-specific databases
CTD	6421.
MGI	MGI:1918764. Sfpq.
Phylogenomic databases
eggNOG	NOG298586.
GeneTree	ENSGT00390000005004.
HOGENOM	HOG000231095.
HOVERGEN	HBG009801.
InParanoid	A2A7U6.
KO	K13219.
OMA	APGGHPK.
OrthoDB	EOG4RNB8S.
Gene expression databases
ArrayExpress	Q8VIJ6.
Bgee	Q8VIJ6.
Genevestigator	Q8VIJ6.
GermOnline	ENSMUSG00000028820. Mus musculus.
Family and domain databases
Gene3D	3.30.70.330. 2 hits.
InterPro	IPR012975. NOPS. IPR012677. Nucleotide-bd_a/b_plait. IPR000504. RRM_dom. [Graphical view]
Pfam	PF08075. NOPS. 1 hit. PF00076. RRM_1. 2 hits. [Graphical view]
SMART	SM00360. RRM. 2 hits. [Graphical view]
PROSITE	PS50102. RRM. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SFPQ. mouse.
NextBio	333919.
SOURCE	Search...

Entry information

Entry name

SFPQ_MOUSE

Accession

Primary (citable) accession number: Q8VIJ6
Secondary accession number(s): A2A7U6, Q9ERW2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	March 1, 2002
Last modified:	May 29, 2013
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents