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UniProtKB/Swiss-Prot entry P23246


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SFPQ_HUMAN
Primary accession number P23246
Secondary accession numbers P30808 Q5SZ71
Integrated into Swiss-Prot on November 1, 1991
Sequence was last modified on October 1, 1996 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 102)
Name and origin of the protein
Protein name Splicing factor, proline- and glutamine-rich
Synonyms Polypyrimidine tract-binding protein-associated-splicing factor
PTB-associated-splicing factor
PSF
DNA-binding p52/p100 complex, 100 kDa subunit
100 kDa DNA-pairing protein
hPOMp100
Gene name
Name: SFPQ
Synonyms: PSF
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, ALTERNATIVE SPLICING, AND FUNCTION.
TISSUE=Fetal brain;
PubMed=8449401 [NCBI, ExPASy, EBI, Israel, Japan]
Patton J.G., Porro E.B., Galceran J., Tempst P., Nadal-Ginard B.;
"Cloning and characterization of PSF, a novel pre-mRNA splicing factor.";
Genes Dev. 7:393-406(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
PROTEIN SEQUENCE OF 48-68 AND 213-246, BLOCKAGE OF N-TERMINUS, DNA-BINDING, AND SUBUNIT.
PubMed=8439294 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang W.-W., Zhang L.-X., Busch R.K., Farres J., Busch H.;
"Purification and characterization of a DNA-binding heterodimer of 52 and 100 kDa from HeLa cells.";
Biochem. J. 290:267-272(1993).
[5]
PROTEIN SEQUENCE OF 292-311; 415-421 AND 503-510, AND IDENTIFICATION IN U5/4/6 SNRNP COMPLEXES.
PubMed=9409622 [NCBI, ExPASy, EBI, Israel, Japan]
Teigelkamp S., Mundt C., Achsel T., Will C.L., Luehrmann R.;
"The human U5 snRNP-specific 100-kD protein is an RS domain-containing, putative RNA helicase with significant homology to the yeast splicing factor Prp28p.";
RNA 3:1313-1326(1997).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 312-707.
TISSUE=Fetal skeletal muscle;
PubMed=2480877 [NCBI, ExPASy, EBI, Israel, Japan]
Gower H.J., Moore S.E., Dickson G., Elsom V.L., Nayak R., Walsh F.S.;
"Cloning and characterization of a myoblast cell surface antigen defined by 24.1D5 monoclonal antibody.";
Development 105:723-731(1989).
[7]
PROTEIN SEQUENCE OF 414-421 AND 427-448, SUBCELLULAR LOCATION, INTERACTION WITH SNRPA, AND IDENTIFICATION IN A SNRNP-FREE COMPLEX WITH SNRPA.
DOI=10.1017/S1355838298981183; PubMed=9848648 [NCBI, ExPASy, EBI, Israel, Japan]
Lutz C.S., Cooke C., O'Connor J.P., Kobayashi R., Alwine J.C.;
"The snRNP-free U1A (SF-A) complex(es): identification of the largest subunit as PSF, the polypyrimidine-tract binding protein-associated splicing factor.";
RNA 4:1493-1499(1998).
[8]
PROTEIN SEQUENCE OF 600-606 AND 667-677, INTERACTION WITH PTBP1, AND SUBCELLULAR LOCATION.
DOI=10.1002/(SICI)1097-4644(20000315)76:4<559::AID-JCB4>3.3.CO;2-L; PubMed=10653975 [NCBI, ExPASy, EBI, Israel, Japan]
Meissner M., Dechat T., Gerner C., Grimm R., Foisner R., Sauermann G.;
"Differential nuclear localization and nuclear matrix association of the splicing factors PSF and PTB.";
J. Cell. Biochem. 76:559-566(2000).
[9]
FUNCTION, INTERACTION WITH PRE-MRNA, AND IDENTIFICATION IN SPLICEOSOME COMPLEX.
PubMed=8045264 [NCBI, ExPASy, EBI, Israel, Japan]
Gozani O., Patton J.G., Reed R.;
"A novel set of spliceosome-associated proteins and the essential splicing factor PSF bind stably to pre-mRNA prior to catalytic step II of the splicing reaction.";
EMBO J. 13:3356-3367(1994).
[10]
CHROMOSOMAL TRANSLOCATION WITH TFE3.
DOI=10.1038/sj.onc.1201394; PubMed=9393982 [NCBI, ExPASy, EBI, Israel, Japan]
Clark J., Lu Y.-J., Sidhar S.K., Parker C., Gill S., Smedley D., Hamoudi R., Linehan W.M., Shipley J., Cooper C.S.;
"Fusion of splicing factor genes PSF and NonO (p54nrb) to the TFE3 gene in papillary renal cell carcinoma.";
Oncogene 15:2233-2239(1997).
[11]
INTERACTION WITH TOP1, AND IDENTIFICATION IN A COMPLEX WITH NONO AND TOP1.
DOI=10.1074/jbc.273.41.26261; PubMed=9756848 [NCBI, ExPASy, EBI, Israel, Japan]
Straub T., Grue P., Uhse A., Lisby M., Knudsen B.R., Tange T.O., Westergaard O., Boege F.;
"The RNA-splicing factor PSF/p54 controls DNA-topoisomerase I activity by a direct interaction.";
J. Biol. Chem. 273:26261-26264(1998).
[12]
FUNCTION IN DNA UNWINDING.
DOI=10.1021/bi992898e; PubMed=10858305 [NCBI, ExPASy, EBI, Israel, Japan]
Straub T., Knudsen B.R., Boege F.;
"PSF/p54(nrb) stimulates 'jumping' of DNA topoisomerase I between separate DNA helices.";
Biochemistry 39:7552-7558(2000).
[13]
FUNCTION IN TRANSCRIPTION REGULATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
DOI=10.1210/me.14.6.774; PubMed=10847580 [NCBI, ExPASy, EBI, Israel, Japan]
Urban R.J., Bodenburg Y., Kurosky A., Wood T.G., Gasic S.;
"Polypyrimidine tract-binding protein-associated splicing factor is a negative regulator of transcriptional activity of the porcine p450scc insulin-like growth factor response element.";
Mol. Endocrinol. 14:774-782(2000).
[14]
FUNCTION IN HOMOLOGOUS DNA PAIRING, AND PHOSPHORYLATION.
DOI=10.1093/nar/28.16.3022; PubMed=10931916 [NCBI, ExPASy, EBI, Israel, Japan]
Akhmedov A.T., Lopez B.S.;
"Human 100-kDa homologous DNA-pairing protein is the splicing factor PSF and promotes DNA strand invasion.";
Nucleic Acids Res. 28:3022-3030(2000).
[15]
FUNCTION IN NUCLEAR RETENTION OF A-TO-I EDITED RNAS, AND IDENTIFICATION IN A COMPLEX WITH NONO AND MATR3.
DOI=10.1016/S0092-8674(01)00466-4; PubMed=11525732 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Z., Carmichael G.G.;
"The fate of dsRNA in the nucleus: a p54(nrb)-containing complex mediates the nuclear retention of promiscuously A-to-I edited RNAs.";
Cell 106:465-475(2001).
[16]
INTERACTION WITH SNRP70, AND PHOSPHORYLATION.
PubMed=11514619 [NCBI, ExPASy, EBI, Israel, Japan]
Shav-Tal Y., Cohen M., Lapter S., Dye B., Patton J.G., Vandekerckhove J., Zipori D.;
"Nuclear relocalization of the pre-mRNA splicing factor PSF during apoptosis involves hyperphosphorylation, masking of antigenic epitopes, and changes in protein interactions.";
Mol. Biol. Cell 12:2328-2340(2001).
[17]
FUNCTION IN TRANSCRIPTION REGULATION, AND INTERACTION WITH RXRA; THRA AND SIN3A.
DOI=10.1128/MCB.21.7.2298-2311.2001; PubMed=11259580 [NCBI, ExPASy, EBI, Israel, Japan]
Mathur M., Tucker P.W., Samuels H.H.;
"PSF is a novel corepressor that mediates its effect through Sin3A and the DNA binding domain of nuclear hormone receptors.";
Mol. Cell. Biol. 21:2298-2311(2001).
[18]
FUNCTION IN TRANSCRIPTION REGULATION, INTERACTION WITH NR5A1 AND SIN3A, AND IDENTIFICATION IN A COMPLEX WITH NONO AND NR5A1.
DOI=10.1210/en.143.4.1280; PubMed=11897684 [NCBI, ExPASy, EBI, Israel, Japan]
Sewer M.B., Nguyen V.Q., Huang C.J., Tucker P.W., Kagawa N., Waterman M.R.;
"Transcriptional activation of human CYP17 in H295R adrenocortical cells depends on complex formation among p54(nrb)/NonO, protein-associated splicing factor, and SF-1, a complex that also participates in repression of transcription.";
Endocrinology 143:1280-1290(2002).
[19]
INTERACTION WITH NONO AND U5 SNRNA, AND IDENTIFICATION IN IN U5/4/6 SNRNP SND SPLICEOSOME COMPLEXES.
DOI=10.1017/S1355838202022070; PubMed=12403470 [NCBI, ExPASy, EBI, Israel, Japan]
Peng R., Dye B.T., Perez I., Barnard D.C., Thompson A.B., Patton J.G.;
"PSF and p54nrb bind a conserved stem in U5 snRNA.";
RNA 8:1334-1347(2002).
[20]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-7; ARG-9; ARG-19 AND ARG-25, AND MASS SPECTROMETRY.
DOI=10.1038/nmeth715; PubMed=15782174 [NCBI, ExPASy, EBI, Israel, Japan]
Ong S.E., Mittler G., Mann M.;
"Identifying and quantifying in vivo methylation sites by heavy methyl SILAC.";
Nat. Methods 1:119-126(2004).
[21]
FUNCTION IN DNA REPAIR, IDENTIFICATION BY MASS SPECTROMETRY, DNA-BINDING, AND SUBUNIT.
DOI=10.1074/jbc.M412758200; PubMed=15590677 [NCBI, ExPASy, EBI, Israel, Japan]
Bladen C.L., Udayakumar D., Takeda Y., Dynan W.S.;
"Identification of the polypyrimidine tract binding protein-associated splicing factor.p54(nrb) complex as a candidate DNA double-strand break rejoining factor.";
J. Biol. Chem. 280:5205-5210(2005).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-687, AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
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 an heteromer with NONO. Binds to pre-mRNA in spliceosome C complex, and specifically binds to intronic polypyrimidine tracts. 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.
  • SUBUNIT: Interacts with PSPC1 (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/SF-1. Interacts with RXRA, probably THRA, and SIN3A. Interacts with TOP1. Part of a complex consisting of SFPQ, NONO and TOP1. Interacts with SNRP70 in apoptotic cells (By similarity).
  • INTERACTION:
    Q9NQT4:EXOSC5; NbExp=1; IntAct=EBI-355453, EBI-371876;
    Q15233:NONO; NbExp=1; IntAct=EBI-355463, EBI-350527;
    P26599:PTBP1; NbExp=1; IntAct=EBI-355453, EBI-350540;
    P28700:Rxra (xeno); NbExp=3; IntAct=EBI-355463, EBI-346715;
    Q96ST3:SIN3A; NbExp=2; IntAct=EBI-355453, EBI-347218;
    P09012:SNRPA; NbExp=4; IntAct=EBI-355453, EBI-607085;
    P04625:THRA (xeno); NbExp=2; IntAct=EBI-355463, EBI-286261;
  • SUBCELLULAR LOCATION: Nucleus matrix. Note=Predominantly in nuclear matrix.
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing. Additional isoforms seem to exist.
    NameLong
    SynonymsA
    Isoform IDP23246-1
    This is the isoform sequence displayed in this entry.
    NameShort
    SynonymsF
    Isoform IDP23246-2
    Features which should be applied to build the isoform sequence: VSP_005855.
  • 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.
  • PTM: Arg-7, Arg-9, Arg-19 and Arg-25 are dimethylated, probably to asymmetric dimethylarginine.
  • DISEASE: A chromosomal aberration involving SFPQ may be a cause of papillary renal cell carcinoma (PRCC). Translocation t(X;1)(p11.2;p34) with TFE3.
  • SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
  • CAUTION: Was originally (Ref.4) thought to be myoblast cell surface antigen 24.1D5 and a possible membrane-bound protein ectokinase.
  • WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/PSFID167.html";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X70944; CAA50283.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL590434; CAI12467.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471059; EAX07426.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X16850; CAA34747.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A46302; A46302.
S29770; S29770.
RefSeq NP_005057.1; -.
UniGene Hs.355934
3D structure databases
HSSP O08583; 1NO8. [HSSP ENTRY / PDB]
SMR P23246; 290-374.
ModBase P23246.
Protein-protein interaction databases
IntAct P23246; -.
PTM databases
PhosphoSite P23246; -.
2D gel databases
SWISS-2DPAGE P23246; -.
Organism-specific databases
H-InvDB HIX0000409; -.
HGNC HGNC:10774; SFPQ.
GenAtlas SFPQ.
HPA CAB009886; -.
MIM 605199; gene. [NCBI / EBI]
PharmGKB PA35690; -.
GeneCards P23246.
Gene expression databases
ArrayExpress P23246; -.
CleanEx HS_SFPQ; -.
GermOnline ENSG00000116560; Homo sapiens.
Ontologies
GO
GO:0016363; Cellular component: nuclear matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0003677; Molecular function: DNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0000166; Molecular function: nucleotide binding (inferred from electronic annotation from InterPro).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0003723; Molecular function: RNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006310; Biological process: DNA recombination (inferred from electronic annotation from UniProtKB-KW).
GO:0006281; Biological process: DNA repair (inferred from electronic annotation from UniProtKB-KW).
GO:0006397; Biological process: mRNA processing (traceable author statement from ProtInc).
GO:0006355; Biological process: regulation of transcription, DNA-dependent (inferred from electronic annotation from UniProtKB-KW).
GO:0008380; Biological process: RNA splicing (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR012677; a_b_plait_nuc_bd.
IPR012975; NOPS.
IPR000504; RRM_RNP1.
Graphical view of domain structure.
Gene3D G3DSA:3.30.70.330; a_b_plait_nuc_bd; 2.
Pfam PF08075; NOPS; 1.
PF00076; RRM_1; 2.
Pfam graphical view of domain structure.
SMART SM00360; RRM; 2.
SMART graphical view of domain structure.
PROSITE PS50102; RRM; 2.
PROSITE graphical view of domain structure (profiles).
ProtoNet P23246.
Proteomic databases
PeptideAtlas P23246; -.
Genome annotation databases
Ensembl ENSG00000116560; Homo sapiens. [Contig view]
GeneID 6421; -.
KEGG hsa:6421; -.
Phylogenomic databases
HOGENOM P23246; -.
HOVERGEN P23246; -.
Other
LinkHub P23246; -.
NextBio 24935; -.
SOURCE SFPQ; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Activator; Alternative splicing; Chromosomal rearrangement; Direct protein sequencing; DNA damage; DNA recombination; DNA repair; DNA-binding; Methylation; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Repeat; Repressor; RNA-binding; Transcription; Transcription regulation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   707  707     Splicing factor, proline- and glutamine-rich. PRO_0000081909
REPEAT   9    11  3     1. 
REPEAT   19    21  3     2. 
REPEAT   25    27  3     3. 
DOMAIN   297   369  73     RRM 1. 
DOMAIN   371   452  82     RRM 2. 
REGION   9    27  19     3 X 3 AA repeats of R-G-G. 
COMPBIAS   10   266  257     Gln/Glu/Pro-rich. 
COMPBIAS   10    15  6     Poly-Gly. 
COMPBIAS   20    27  8     Poly-Gly. 
COMPBIAS   56    65  10     Poly-Pro. 
COMPBIAS   67    71  5     Poly-Gln. 
COMPBIAS   95    98  4     Poly-Gln. 
COMPBIAS   99   103  5     Poly-Pro. 
COMPBIAS   184   188  5     Poly-Pro. 
COMPBIAS   571   574  4     Poly-Arg. 
COMPBIAS   613   616  4     Poly-Gly. 
COMPBIAS   635   641  7     Poly-Gly. 
SITE   662   663  2     Breakpoint for translocation to form SFPQ-TFE3. 
MOD_RES   7     7        Omega-N-methylated arginine. 
MOD_RES   9     9        Omega-N-methylated arginine. 
MOD_RES   19    19        Omega-N-methylated arginine. 
MOD_RES   25    25        Omega-N-methylated arginine. 
MOD_RES   33    33        Phosphoserine. 
MOD_RES   687   687        Phosphothreonine. 
VAR_SEQ   663   707        RTERFGQGGAGPVGGQGPRGMGPGTPAGYGRGREEYEGPN KKPRF -> VRMIDVG (in isoform Short). VSP_005855
CONFLICT   243   243        G -> R (in Ref. 4; AA sequence). 
Sequence information
Length: 707 AA [This is the length of the unprocessed precursor] Molecular weight: 76149 Da [This is the MW of the unprocessed precursor] CRC64: 6D8D5EA95E235847 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSRDRFRSRG GGGGGFHRRG GGGGRGGLHD FRSPPPGMGL NQNRGPMGPG PGQSGPKPPI 

        70         80         90        100        110        120 
PPPPPHQQQQ QPPPQQPPPQ QPPPHQPPPH PQPHQQQQPP PPPQDSSKPV VAQGPGPAPG 

       130        140        150        160        170        180 
VGSAPPASSS APPATPPTSG APPGSGPGPT PTPPPAVTSA PPGAPPPTPP SSGVPTTPPQ 

       190        200        210        220        230        240 
AGGPPPPPAA VPGPGPGPKQ GPGPGGPKGG KMPGGPKPGG GPGLSTPGGH PKPPHRGGGE 

       250        260        270        280        290        300 
PRGGRQHHPP YHQQHHQGPP PGGPGGRSEE KISDSEGFKA NLSLLRRPGE KTYTQRCRLF 

       310        320        330        340        350        360 
VGNLPADITE DEFKRLFAKY GEPGEVFINK GKGFGFIKLE SRALAEIAKA ELDDTPMRGR 

       370        380        390        400        410        420 
QLRVRFATHA AALSVRNLSP YVSNELLEEA FSQFGPIERA VVIVDDRGRS TGKGIVEFAS 

       430        440        450        460        470        480 
KPAARKAFER CSEGVFLLTT TPRPVIVEPL EQLDDEDGLP EKLAQKNPMY QKERETPPRF 

       490        500        510        520        530        540 
AQHGTFEYEY SQRWKSLDEM EKQQREQVEK NMKDAKDKLE SEMEDAYHEH QANLLRQDLM 

       550        560        570        580        590        600 
RRQEELRRME ELHNQEMQKR KEMQLRQEEE RRRREEEMMI RQREMEEQMR RQREESYSRM 

       610        620        630        640        650        660 
GYMDPRERDM RMGGGGAMNM GDPYGSGGQK FPPLGGGGGI GYEANPGVPP ATMSGSMMGS 

       670        680        690        700 
DMRTERFGQG GAGPVGGQGP RGMGPGTPAG YGRGREEYEG PNKKPRF 

P23246 in FASTA format

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View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

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