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P23246 (SFPQ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 166. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Splicing factor, proline- and glutamine-rich
Alternative name(s):
100 kDa DNA-pairing protein
Short name=hPOMp100
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
Synonyms:PSF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length707 AA.
Sequence statusComplete.
Protein existenceEvidence 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 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. Transcriptional repression is mediated by an interaction of SFPQ with SIN3A and subsequent recruitment of histone deacetylases (HDACs). Involved in the control of the circadian rhythms. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation. 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. Ref.1 Ref.11 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.22 Ref.32

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-687' and inhibits binding of SFPQ to a ESS1 exonic splicing silencer element-containing RNA. The large PER complex involved in the histone deacetylation is composed of at least HDAC1, PER2, SFPQ and SIN3A. Ref.5 Ref.6 Ref.9 Ref.10 Ref.11 Ref.13 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.27 Ref.29 Ref.32

Subcellular location

Nucleus matrix. Cytoplasm. Note: Predominantly in nuclear matrix. Ref.9 Ref.10 Ref.29

Post-translational modification

The N-terminus is blocked.

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. Phosphorylation of C-terminal tyrosines promotes its cytoplasmic localization, impaired its binding to polypyrimidine RNA and led to cell cycle arrest. In resting T-cells is phosphorylated at Thr-687 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-687. Ref.16 Ref.18 Ref.23 Ref.24 Ref.29 Ref.32

Involvement in 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.

Sequence similarities

Contains 2 RRM (RNA recognition motif) domains.

Caution

Was originally (Ref.8) thought to be myoblast cell surface antigen 24.1D5 and a possible membrane-bound protein ectokinase.

Ontologies

Keywords
   Biological processBiological rhythms
DNA damage
DNA recombination
DNA repair
mRNA processing
mRNA splicing
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
   DomainRepeat
   LigandDNA-binding
RNA-binding
   Molecular functionActivator
Repressor
   PTMAcetylation
Methylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA recombination

Inferred from electronic annotation. Source: UniProtKB-KW

DNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

RNA splicing

Traceable author statement Ref.1. Source: ProtInc

alternative mRNA splicing, via spliceosome

Inferred from mutant phenotype PubMed 19874820. Source: BHF-UCL

histone H3 deacetylation

Inferred from sequence or structural similarity. Source: UniProtKB

mRNA processing

Traceable author statement Ref.1. Source: ProtInc

negative regulation of circadian rhythm

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 22783022. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear matrix

Inferred from direct assay PubMed 19874820. Source: BHF-UCL

nucleoplasm

Inferred from direct assay PubMed 19874820. Source: BHF-UCL

nucleus

Inferred from direct assay. Source: HPA

paraspeckles

Inferred from direct assay PubMed 19874820. Source: BHF-UCL

   Molecular_functionnucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.19. Source: IntAct

transcription regulatory region sequence-specific DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform Long (identifier: P23246-1)

Also known as: A;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Short (identifier: P23246-2)

Also known as: F;

The sequence of this isoform differs from the canonical sequence as follows:
     663-707: RTERFGQGGAGPVGGQGPRGMGPGTPAGYGRGREEYEGPNKKPRF → VRMIDVG

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 707707Splicing factor, proline- and glutamine-rich
PRO_0000081909

Regions

Repeat9 – 1131
Repeat19 – 2132
Repeat25 – 2733
Domain297 – 36973RRM 1
Domain371 – 45282RRM 2
Region9 – 27193 X 3 AA repeats of R-G-G
Compositional bias10 – 266257Gln/Glu/Pro-rich
Compositional bias10 – 156Poly-Gly
Compositional bias20 – 278Poly-Gly
Compositional bias56 – 6510Poly-Pro
Compositional bias67 – 715Poly-Gln
Compositional bias95 – 984Poly-Gln
Compositional bias99 – 1035Poly-Pro
Compositional bias184 – 1885Poly-Pro
Compositional bias571 – 5744Poly-Arg
Compositional bias613 – 6164Poly-Gly
Compositional bias635 – 6417Poly-Gly

Sites

Site662 – 6632Breakpoint for translocation to form SFPQ-TFE3

Amino acid modifications

Modified residue81Phosphoserine; by MKNK2 Ref.24
Modified residue331Phosphoserine Ref.33 Ref.35
Modified residue2081N6-acetyllysine By similarity
Modified residue2731Phosphoserine Ref.26 Ref.35
Modified residue2831Phosphoserine; by MKNK2 Ref.24 Ref.35
Modified residue2931Phosphotyrosine; by ALK Ref.23
Modified residue3141N6,N6-dimethyllysine Ref.4
Modified residue3191N6-acetyllysine Ref.31
Modified residue3381N6-acetyllysine Ref.31
Modified residue3791Phosphoserine Ref.30
Modified residue4211N6-acetyllysine Ref.31
Modified residue4721N6-acetyllysine Ref.31
Modified residue5711Dimethylated arginine Ref.4
Modified residue6261Phosphoserine Ref.33
Modified residue6811Omega-N-methylarginine Ref.4
Modified residue6871Phosphothreonine Ref.25 Ref.26 Ref.32
Modified residue6931Dimethylated arginine Ref.4

Natural variations

Alternative sequence663 – 70745RTERF…KKPRF → VRMIDVG in isoform Short.
VSP_005855

Experimental info

Mutagenesis6871T → A: Abolishes phosphorylation by GSK3B. Impairs interaction with THRAP3. Ref.32
Mutagenesis6871T → D: No effect on interaction with THRAP3 (phosphomimetic). Ref.32
Sequence conflict2431G → R AA sequence Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform Long (A) [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 6D8D5EA95E235847

FASTA70776,149
        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 

« Hide

Isoform Short (F) [UniParc].

Checksum: 46BAE5D117400578
Show »

FASTA66972,263

References

« Hide 'large scale' references
[1]"Cloning and characterization of PSF, a novel pre-mRNA splicing factor."
Patton J.G., Porro E.B., Galceran J., Tempst P., Nadal-Ginard B.
Genes Dev. 7:393-406(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, ALTERNATIVE SPLICING, FUNCTION.
Tissue: Fetal brain.
[2]"The DNA sequence and biological annotation of human chromosome 1."
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. expand/collapse author list , 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.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 33-44; 218-236; 246-267; 272-286; 299-315; 320-330; 350-358; 364-407; 414-425; 431-462; 480-493; 517-536; 549-559; 567-572; 575-581; 600-606; 612-630 AND 667-695, METHYLATION AT LYS-314; ARG-571; ARG-681 AND ARG-693, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[5]"Purification and characterization of a DNA-binding heterodimer of 52 and 100 kDa from HeLa cells."
Zhang W.-W., Zhang L.-X., Busch R.K., Farres J., Busch H.
Biochem. J. 290:267-272(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 48-68 AND 213-246, BLOCKAGE OF N-TERMINUS, DNA-BINDING, SUBUNIT.
[6]"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."
Teigelkamp S., Mundt C., Achsel T., Will C.L., Luehrmann R.
RNA 3:1313-1326(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 292-311; 415-421 AND 503-510, IDENTIFICATION IN U5/4/6 SNRNP COMPLEXES.
[7]Lubec G., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 299-314 AND 480-493, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Fetal brain cortex.
[8]"Cloning and characterization of a myoblast cell surface antigen defined by 24.1D5 monoclonal antibody."
Gower H.J., Moore S.E., Dickson G., Elsom V.L., Nayak R., Walsh F.S.
Development 105:723-731(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 312-707.
Tissue: Fetal skeletal muscle.
[9]"The snRNP-free U1A (SF-A) complex(es): identification of the largest subunit as PSF, the polypyrimidine-tract binding protein-associated splicing factor."
Lutz C.S., Cooke C., O'Connor J.P., Kobayashi R., Alwine J.C.
RNA 4:1493-1499(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 414-421 AND 427-448, SUBCELLULAR LOCATION, INTERACTION WITH SNRPA, IDENTIFICATION IN A SNRNP-FREE COMPLEX WITH SNRPA.
[10]"Differential nuclear localization and nuclear matrix association of the splicing factors PSF and PTB."
Meissner M., Dechat T., Gerner C., Grimm R., Foisner R., Sauermann G.
J. Cell. Biochem. 76:559-566(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 600-606 AND 667-677, INTERACTION WITH PTBP1, SUBCELLULAR LOCATION.
[11]"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."
Gozani O., Patton J.G., Reed R.
EMBO J. 13:3356-3367(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PRE-MRNA, IDENTIFICATION IN SPLICEOSOME COMPLEX.
[12]"Fusion of splicing factor genes PSF and NonO (p54nrb) to the TFE3 gene in papillary renal cell carcinoma."
Clark J., Lu Y.-J., Sidhar S.K., Parker C., Gill S., Smedley D., Hamoudi R., Linehan W.M., Shipley J., Cooper C.S.
Oncogene 15:2233-2239(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH TFE3.
[13]"The RNA-splicing factor PSF/p54 controls DNA-topoisomerase I activity by a direct interaction."
Straub T., Grue P., Uhse A., Lisby M., Knudsen B.R., Tange T.O., Westergaard O., Boege F.
J. Biol. Chem. 273:26261-26264(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TOP1, IDENTIFICATION IN A COMPLEX WITH NONO AND TOP1.
[14]"PSF/p54(nrb) stimulates 'jumping' of DNA topoisomerase I between separate DNA helices."
Straub T., Knudsen B.R., Boege F.
Biochemistry 39:7552-7558(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DNA UNWINDING.
[15]"Polypyrimidine tract-binding protein-associated splicing factor is a negative regulator of transcriptional activity of the porcine p450scc insulin-like growth factor response element."
Urban R.J., Bodenburg Y., Kurosky A., Wood T.G., Gasic S.
Mol. Endocrinol. 14:774-782(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TRANSCRIPTION REGULATION, IDENTIFICATION BY MASS SPECTROMETRY.
[16]"Human 100-kDa homologous DNA-pairing protein is the splicing factor PSF and promotes DNA strand invasion."
Akhmedov A.T., Lopez B.S.
Nucleic Acids Res. 28:3022-3030(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN HOMOLOGOUS DNA PAIRING, PHOSPHORYLATION.
[17]"The fate of dsRNA in the nucleus: a p54(nrb)-containing complex mediates the nuclear retention of promiscuously A-to-I edited RNAs."
Zhang Z., Carmichael G.G.
Cell 106:465-475(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NUCLEAR RETENTION OF A-TO-I EDITED RNAS, IDENTIFICATION IN A COMPLEX WITH NONO AND MATR3.
[18]"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: INTERACTION WITH SNRNP70, PHOSPHORYLATION.
[19]"PSF is a novel corepressor that mediates its effect through Sin3A and the DNA binding domain of nuclear hormone receptors."
Mathur M., Tucker P.W., Samuels H.H.
Mol. Cell. Biol. 21:2298-2311(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TRANSCRIPTION REGULATION, INTERACTION WITH RXRA; THRA AND SIN3A.
[20]"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."
Sewer M.B., Nguyen V.Q., Huang C.J., Tucker P.W., Kagawa N., Waterman M.R.
Endocrinology 143:1280-1290(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TRANSCRIPTION REGULATION, INTERACTION WITH NR5A1 AND SIN3A, IDENTIFICATION IN A COMPLEX WITH NONO AND NR5A1.
[21]"PSF and p54nrb bind a conserved stem in U5 snRNA."
Peng R., Dye B.T., Perez I., Barnard D.C., Thompson A.B., Patton J.G.
RNA 8:1334-1347(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NONO AND U5 SNRNA, IDENTIFICATION IN IN U5/4/6 SNRNP SND SPLICEOSOME COMPLEXES.
[22]"Identification of the polypyrimidine tract binding protein-associated splicing factor.p54(nrb) complex as a candidate DNA double-strand break rejoining factor."
Bladen C.L., Udayakumar D., Takeda Y., Dynan W.S.
J. Biol. Chem. 280:5205-5210(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DNA REPAIR, IDENTIFICATION BY MASS SPECTROMETRY, DNA-BINDING, SUBUNIT.
[23]"NPM/ALK binds and phosphorylates the RNA/DNA-binding protein PSF in anaplastic large-cell lymphoma."
Galietta A., Gunby R.H., Redaelli S., Stano P., Carniti C., Bachi A., Tucker P.W., Tartari C.J., Huang C.J., Colombo E., Pulford K., Puttini M., Piazza R.G., Ruchatz H., Villa A., Donella-Deana A., Marin O., Perrotti D., Gambacorti-Passerini C.
Blood 110:2600-2609(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-293.
[24]"The PSF.p54nrb complex is a novel Mnk substrate that binds the mRNA for tumor necrosis factor alpha."
Buxade M., Morrice N., Krebs D.L., Proud C.G.
J. Biol. Chem. 283:57-65(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-8 AND SER-283 BY MKNK2.
[25]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-687, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[26]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273 AND THR-687, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[27]"Proteomic identification of a PSF/p54nrb heterodimer as RNF43 oncoprotein-interacting proteins."
Miyamoto K., Sakurai H., Sugiura T.
Proteomics 8:2907-2910(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNF43.
[28]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"BRK phosphorylates PSF promoting its cytoplasmic localization and cell cycle arrest."
Lukong K.E., Huot M.E., Richard S.
Cell. Signal. 21:1415-1422(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, INTERACTION WITH PTK6, SUBCELLULAR LOCATION.
[30]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[31]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-319; LYS-338; LYS-421 AND LYS-472, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[32]"Phosphorylation-dependent regulation of PSF by GSK3 controls CD45 alternative splicing."
Heyd F., Lynch K.W.
Mol. Cell 40:126-137(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT THR-687, INTERACTION WITH THRAP3, MUTAGENESIS OF THR-687.
[33]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND SER-626, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[34]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[35]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33; SER-273 AND SER-283, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X70944 mRNA. Translation: CAA50283.1.
AL590434 Genomic DNA. Translation: CAI12467.1.
CH471059 Genomic DNA. Translation: EAX07426.1.
X16850 mRNA. Translation: CAA34747.1.
CCDSCCDS388.1. [P23246-1]
PIRA46302.
S29770.
RefSeqNP_005057.1. NM_005066.2. [P23246-1]
XP_005271168.1. XM_005271111.2. [P23246-1]
XP_005271169.1. XM_005271112.2. [P23246-1]
XP_005271170.1. XM_005271113.2. [P23246-1]
XP_005271172.1. XM_005271115.2. [P23246-2]
XP_005271173.1. XM_005271116.2. [P23246-2]
UniGeneHs.355934.
Hs.611911.

3D structure databases

ProteinModelPortalP23246.
SMRP23246. Positions 287-535.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112319. 133 interactions.
IntActP23246. 48 interactions.
MINTMINT-1141893.
STRING9606.ENSP00000349748.

PTM databases

PhosphoSiteP23246.

Polymorphism databases

DMDM1709851.

2D gel databases

SWISS-2DPAGEP23246.

Proteomic databases

MaxQBP23246.
PaxDbP23246.
PeptideAtlasP23246.
PRIDEP23246.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000357214; ENSP00000349748; ENSG00000116560. [P23246-1]
GeneID6421.
KEGGhsa:6421.
UCSCuc001bys.3. human. [P23246-1]

Organism-specific databases

CTD6421.
GeneCardsGC01M035641.
HGNCHGNC:10774. SFPQ.
HPACAB009886.
HPA047513.
MIM605199. gene.
neXtProtNX_P23246.
Orphanet319308. Translocation renal cell carcinoma.
PharmGKBPA35690.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG298586.
HOGENOMHOG000231095.
HOVERGENHBG009801.
InParanoidP23246.
KOK13219.
OMAAPGGHPK.
OrthoDBEOG7327P0.
PhylomeDBP23246.
TreeFamTF315795.

Gene expression databases

ArrayExpressP23246.
BgeeP23246.
CleanExHS_SFPQ.
GenevestigatorP23246.

Family and domain databases

Gene3D3.30.70.330. 2 hits.
InterProIPR012975. NOPS.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF08075. NOPS. 1 hit.
PF00076. RRM_1. 2 hits.
[Graphical view]
SMARTSM00360. RRM. 2 hits.
[Graphical view]
PROSITEPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSFPQ. human.
GeneWikiSFPQ.
GenomeRNAi6421.
NextBio24935.
PROP23246.
SOURCESearch...

Entry information

Entry nameSFPQ_HUMAN
AccessionPrimary (citable) accession number: P23246
Secondary accession number(s): P30808, Q5SZ71
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 166 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM