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UniProtKB - Q8VIJ6 (SFPQ_MOUSE)

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Protein

Splicing factor, proline- and glutamine-rich

Gene

Sfpq

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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. 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 transcriptional activator (By similarity). 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 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). Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation (PubMed:21680841, PubMed:22966205). Required for the assembly of nuclear speckles (By similarity). 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 (By similarity).By similarity2 Publications

GO - Molecular functioni

  • chromatin binding Source: BHF-UCL
  • DNA binding Source: MGI
  • E-box binding Source: UniProtKB
  • histone deacetylase binding Source: MGI
  • protein homodimerization activity Source: MGI
  • RNA binding Source: UniProtKB-KW
  • RNA polymerase II distal enhancer sequence-specific DNA binding Source: BHF-UCL
  • transcription regulatory region DNA binding Source: MGI
  • transcription regulatory region sequence-specific DNA binding Source: UniProtKB
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • activation of innate immune response Source: MGI
  • alternative mRNA splicing, via spliceosome Source: MGI
  • cellular response to DNA damage stimulus Source: MGI
  • chromosome organization Source: MGI
  • double-strand break repair via homologous recombination Source: MGI
  • histone H3 deacetylation Source: UniProtKB
  • innate immune response Source: UniProtKB-KW
  • negative regulation of circadian rhythm Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription by RNA polymerase II Source: MGI
  • positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: MGI
  • positive regulation of sister chromatid cohesion Source: MGI
  • positive regulation of transcription by RNA polymerase II Source: UniProtKB
  • regulation of cell cycle Source: MGI
  • regulation of circadian rhythm Source: UniProtKB
  • rhythmic process Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionActivator, DNA-binding, Repressor, RNA-binding
Biological processBiological rhythms, DNA damage, DNA repair, Immunity, Innate immunity, mRNA processing, mRNA splicing, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-MMU-8849468 PTK6 Regulates Proteins Involved in RNA Processing

Names & Taxonomyi

Protein namesi
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 namesi
Name:Sfpq
Synonyms:Psf
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1918764 Sfpq

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000819101 – 699Splicing factor, proline- and glutamine-richAdd BLAST699

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei7Omega-N-methylated arginineBy similarity1
Modified residuei8Phosphoserine; by MKNK2By similarity1
Modified residuei9Asymmetric dimethylarginine; alternateCombined sources1
Modified residuei9Omega-N-methylarginine; alternateCombined sources1
Modified residuei9Omega-N-methylated arginine; alternateBy similarity1
Modified residuei19Omega-N-methylated arginineBy similarity1
Modified residuei25Omega-N-methylated arginineBy similarity1
Modified residuei33PhosphoserineBy similarity1
Modified residuei200N6-acetyllysineCombined sources1
Modified residuei228Omega-N-methylarginineCombined sources1
Modified residuei234Omega-N-methylarginineCombined sources1
Modified residuei237Omega-N-methylarginineCombined sources1
Cross-linki263Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei265PhosphoserineBy similarity1
Cross-linki271Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei275Phosphoserine; by MKNK2By similarity1
Modified residuei285Phosphotyrosine; by ALKBy similarity1
Modified residuei306N6,N6-dimethyllysineBy similarity1
Modified residuei311N6-acetyllysineBy similarity1
Modified residuei330N6-acetyllysine; alternateBy similarity1
Cross-linki330Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei360PhosphothreonineBy similarity1
Modified residuei366PhosphoserineBy similarity1
Modified residuei371PhosphoserineBy similarity1
Modified residuei413N6-acetyllysineBy similarity1
Modified residuei464N6-acetyllysineBy similarity1
Modified residuei488PhosphoserineBy similarity1
Modified residuei563Dimethylated arginineBy similarity1
Modified residuei618PhosphoserineBy similarity1
Modified residuei673Omega-N-methylarginineCombined sources1
Modified residuei679PhosphothreonineCombined sources1
Modified residuei683PhosphotyrosineBy similarity1
Modified residuei685Dimethylated arginine; alternateBy similarity1
Modified residuei685Omega-N-methylarginine; alternateCombined sources1
Modified residuei687Omega-N-methylarginineBy similarity1

Post-translational modificationi

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.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8VIJ6
MaxQBiQ8VIJ6
PaxDbiQ8VIJ6
PeptideAtlasiQ8VIJ6
PRIDEiQ8VIJ6

2D gel databases

REPRODUCTION-2DPAGEiQ8VIJ6

PTM databases

iPTMnetiQ8VIJ6
PhosphoSitePlusiQ8VIJ6
SwissPalmiQ8VIJ6

Expressioni

Gene expression databases

BgeeiENSMUSG00000028820
GenevisibleiQ8VIJ6 MM

Interactioni

Subunit structurei

Heterodimer with NONO. Monomer and component of the SFPQ-NONO complex, which is probably a heterotetramer of two 52 kDa (NONO) and two 100 kDa (SFPQ) subunits. The coiled coil domain mediates interaction with NONO, and can also mediate formation of long, linear homooligomers (in vitro). 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 (PubMed:15140795). Interacts with RNF43 (By similarity). Interacts with PITX3 and NR4A2/NURR1 (PubMed:19144721). Interacts with PTK6. Interacts with THRAP3; the interaction is dependent on SFPQ phosphorylation at 'Thr-687' and inhibits binding of SFPQ to a ESS1 exonic splicing silencer element-containing RNA (By similarity). The large PER complex involved in the histone deacetylation is composed of at least HDAC1, PER2, SFPQ and SIN3A (PubMed:21680841). Interacts with PER1 and PER2 (PubMed:22966205). Part of the HDP-RNP complex composed of at least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1 RNA (By similarity). Interacts with PQBP1 (By similarity).By similarity4 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi214752, 19 interactors
IntActiQ8VIJ6, 6 interactors
MINTiQ8VIJ6
STRINGi10090.ENSMUSP00000030623

Structurei

3D structure databases

ProteinModelPortaliQ8VIJ6
SMRiQ8VIJ6
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati9 – 1113
Repeati19 – 2123
Repeati25 – 2733
Domaini289 – 361RRM 1PROSITE-ProRule annotationAdd BLAST73
Domaini363 – 444RRM 2PROSITE-ProRule annotationAdd BLAST82

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni9 – 273 X 3 AA repeats of R-G-GAdd BLAST19

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili489 – 588Sequence analysisAdd BLAST100

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi10 – 258Gln/Glu/Pro-richAdd BLAST249
Compositional biasi10 – 15Poly-Gly6
Compositional biasi20 – 27Poly-Gly8
Compositional biasi54 – 63Poly-Pro10
Compositional biasi65 – 69Poly-Gln5
Compositional biasi96 – 100Poly-Pro5
Compositional biasi158 – 161Poly-Pro4
Compositional biasi178 – 182Poly-Pro5
Compositional biasi563 – 566Poly-Arg4
Compositional biasi605 – 608Poly-Gly4
Compositional biasi627 – 633Poly-Gly7

Domaini

The coiled coil domain mediates interaction with NONO, and can also mediate formation of long, linear homooligomers (in vitro). The coiled coil domain is required for optimal DNA binding, and optimal transcription activation.By similarity

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG0115 Eukaryota
ENOG410XQA0 LUCA
GeneTreeiENSGT00390000005004
HOGENOMiHOG000231095
HOVERGENiHBG009801
InParanoidiQ8VIJ6
KOiK13219
OMAiAFERCTE
OrthoDBiEOG091G09T7
PhylomeDBiQ8VIJ6
TreeFamiTF315795

Family and domain databases

CDDicd12948 NOPS_PSF, 1 hit
cd12587 RRM1_PSF, 1 hit
Gene3Di3.30.70.330, 2 hits
InterProiView protein in InterPro
IPR012975 NOPS
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR034526 PSF_NOPS
IPR034525 PSF_RRM1
IPR035979 RBD_domain_sf
IPR000504 RRM_dom
PfamiView protein in Pfam
PF08075 NOPS, 1 hit
PF00076 RRM_1, 2 hits
SMARTiView protein in SMART
SM00360 RRM, 2 hits
SUPFAMiSSF54928 SSF54928, 1 hit
PROSITEiView protein in PROSITE
PS50102 RRM, 2 hits

Sequencei

Sequence statusi: Complete.

Q8VIJ6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRDRFRSRG GGGGGFHRRG GGGGRGGLHD FRSPPPGMGL NQNRGPMGPG 
        60         70         80         90        100
PGGPKPPLPP PPPHQQQQQP PPQQPPPQQP PPHQQPPPHQ PPHQQPPPPP 
       110        120        130        140        150
QESKPVVPQG PGSAPGVSSA PPPAVSAPPA NPPTTGAPPG PGPTPTPPPA 
       160        170        180        190        200
VPSTAPGPPP PSTPSSGVST TPPQTGGPPP PPAGGAGPGP KPGPGPGGPK 
       210        220        230        240        250
GGKMPGGPKP GGGPGMGAPG GHPKPPHRGG GEPRGGRQHH APYHQQHHQG 
       260        270        280        290        300
PPPGGPGPRT EEKISDSEGF KANLSLLRRP GEKTYTQRCR LFVGNLPADI 
       310        320        330        340        350
TEDEFKRLFA KYGEPGEVFI NKGKGFGFIK LESRALAEIA KAELDDTPMR 
       360        370        380        390        400
GRQLRVRFAT HAAALSVRNL SPYVSNELLE EAFSQFGPIE RAVVIVDDRG 
       410        420        430        440        450
RSTGKGIVEF ASKPAARKAF ERCSEGVFLL TTTPRPVIVE PLEQLDDEDG 
       460        470        480        490        500
LPEKLAQKNP MYQKERETPP RFAQHGTFEY EYSQRWKSLD EMEKQQREQV 
       510        520        530        540        550
EKNMKDAKDK LESEMEDAYH EHQANLLRQD LMRRQEELRR MEELHSQEMQ 
       560        570        580        590        600
KRKEMQLRQE EERRRREEEM MIRQREMEEQ MRRQREESYS RMGYMDPRER 
       610        620        630        640        650
DMRMGGGGTM NMGDPYGSGG QKFPPLGGGG GIGYEANPGV PPATMSGSMM 
       660        670        680        690 
GSDMRTERFG QGGAGPVGGQ GPRGMGPGTP AGYGRGREEY EGPNKKPRF
Length:699
Mass (Da):75,442
Last modified:March 1, 2002 - v1
Checksum:i714F786264C63AA0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti47M → Q AA sequence (PubMed:11008015).Curated1
Sequence conflicti546S → N in AAG17365 (PubMed:11008015).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY034062 mRNA Translation: AAK60397.1
AL606985 Genomic DNA No translation available.
BC089305 mRNA Translation: AAH89305.1
AF272847 mRNA Translation: AAG17365.1
CCDSiCCDS18662.1
RefSeqiNP_076092.1, NM_023603.3
UniGeneiMm.257276
Mm.482296

Genome annotation databases

EnsembliENSMUST00000030623; ENSMUSP00000030623; ENSMUSG00000028820
GeneIDi71514
KEGGimmu:71514
UCSCiuc008utz.2 mouse

Similar proteinsi

Entry informationi

Entry nameiSFPQ_MOUSE
AccessioniPrimary (citable) accession number: Q8VIJ6
Secondary accession number(s): A2A7U6, Q9ERW2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: March 1, 2002
Last modified: July 18, 2018
This is version 161 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

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