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P23246

- SFPQ_HUMAN

UniProt

P23246 - SFPQ_HUMAN

Protein

Splicing factor, proline- and glutamine-rich

Gene

SFPQ

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 168 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    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 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). 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. 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.10 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei662 – 6632Breakpoint for translocation to form SFPQ-TFE3

    GO - Molecular functioni

    1. core promoter binding Source: UniProtKB
    2. nucleotide binding Source: InterPro
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: IntAct
    5. transcription regulatory region sequence-specific DNA binding Source: UniProtKB

    GO - Biological processi

    1. alternative mRNA splicing, via spliceosome Source: BHF-UCL
    2. DNA recombination Source: UniProtKB-KW
    3. DNA repair Source: UniProtKB-KW
    4. histone H3 deacetylation Source: UniProtKB
    5. mRNA processing Source: ProtInc
    6. negative regulation of circadian rhythm Source: UniProtKB
    7. negative regulation of transcription, DNA-templated Source: UniProtKB
    8. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    9. regulation of circadian rhythm Source: UniProtKB
    10. rhythmic process Source: UniProtKB-KW
    11. RNA splicing Source: ProtInc
    12. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Biological rhythms, DNA damage, DNA recombination, DNA repair, mRNA processing, mRNA splicing, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:SFPQ
    Synonyms:PSF
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:10774. SFPQ.

    Subcellular locationi

    Nucleus matrix. Cytoplasm
    Note: Predominantly in nuclear matrix.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nuclear matrix Source: BHF-UCL
    3. nucleoplasm Source: BHF-UCL
    4. nucleus Source: HPA
    5. paraspeckles Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving SFPQ may be a cause of papillary renal cell carcinoma (PRCC). Translocation t(X;1)(p11.2;p34) with TFE3.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi687 – 6871T → A: Abolishes phosphorylation by GSK3B. Impairs interaction with THRAP3. 1 Publication
    Mutagenesisi687 – 6871T → D: No effect on interaction with THRAP3 (phosphomimetic). 1 Publication

    Organism-specific databases

    Orphaneti319308. Translocation renal cell carcinoma.
    PharmGKBiPA35690.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 707707Splicing factor, proline- and glutamine-richPRO_0000081909Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei8 – 81Phosphoserine; by MKNK21 Publication
    Modified residuei33 – 331Phosphoserine2 Publications
    Modified residuei208 – 2081N6-acetyllysineBy similarity
    Modified residuei273 – 2731Phosphoserine2 Publications
    Modified residuei283 – 2831Phosphoserine; by MKNK22 Publications
    Modified residuei293 – 2931Phosphotyrosine; by ALK1 Publication
    Modified residuei314 – 3141N6,N6-dimethyllysine1 Publication
    Modified residuei319 – 3191N6-acetyllysine1 Publication
    Modified residuei338 – 3381N6-acetyllysine1 Publication
    Modified residuei379 – 3791Phosphoserine1 Publication
    Modified residuei421 – 4211N6-acetyllysine1 Publication
    Modified residuei472 – 4721N6-acetyllysine1 Publication
    Modified residuei571 – 5711Dimethylated arginine1 Publication
    Modified residuei626 – 6261Phosphoserine1 Publication
    Modified residuei681 – 6811Omega-N-methylarginine1 Publication
    Modified residuei687 – 6871Phosphothreonine3 Publications
    Modified residuei693 – 6931Dimethylated arginine1 Publication

    Post-translational modificationi

    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-687.11 Publications

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP23246.
    PaxDbiP23246.
    PeptideAtlasiP23246.
    PRIDEiP23246.

    2D gel databases

    SWISS-2DPAGEP23246.

    PTM databases

    PhosphoSiteiP23246.

    Expressioni

    Gene expression databases

    ArrayExpressiP23246.
    BgeeiP23246.
    CleanExiHS_SFPQ.
    GenevestigatoriP23246.

    Organism-specific databases

    HPAiCAB009886.
    HPA047513.

    Interactioni

    Subunit structurei

    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. Interacts with PER1 and PER2.15 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EBNA-LPQ8AZK72EBI-355453,EBI-1185167From a different organism.
    PTBP1P265992EBI-355453,EBI-350540
    PTK6Q138825EBI-355453,EBI-1383632
    RxraP287003EBI-355463,EBI-346715From a different organism.
    SIN3AQ96ST32EBI-355453,EBI-347218
    SNRPAP090124EBI-355453,EBI-607085
    THRAP046252EBI-355463,EBI-286261From a different organism.
    THRAP3Q9Y2W16EBI-355453,EBI-352039

    Protein-protein interaction databases

    BioGridi112319. 132 interactions.
    IntActiP23246. 48 interactions.
    MINTiMINT-1141893.
    STRINGi9606.ENSP00000349748.

    Structurei

    3D structure databases

    ProteinModelPortaliP23246.
    SMRiP23246. Positions 287-535.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati9 – 1131
    Repeati19 – 2132
    Repeati25 – 2733
    Domaini297 – 36973RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini371 – 45282RRM 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni9 – 27193 X 3 AA repeats of R-G-GAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi10 – 266257Gln/Glu/Pro-richAdd
    BLAST
    Compositional biasi10 – 156Poly-Gly
    Compositional biasi20 – 278Poly-Gly
    Compositional biasi56 – 6510Poly-Pro
    Compositional biasi67 – 715Poly-Gln
    Compositional biasi95 – 984Poly-Gln
    Compositional biasi99 – 1035Poly-Pro
    Compositional biasi184 – 1885Poly-Pro
    Compositional biasi571 – 5744Poly-Arg
    Compositional biasi613 – 6164Poly-Gly
    Compositional biasi635 – 6417Poly-Gly

    Sequence similaritiesi

    Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG298586.
    HOGENOMiHOG000231095.
    HOVERGENiHBG009801.
    InParanoidiP23246.
    KOiK13219.
    OMAiAPGGHPK.
    OrthoDBiEOG7327P0.
    PhylomeDBiP23246.
    TreeFamiTF315795.

    Family and domain databases

    Gene3Di3.30.70.330. 2 hits.
    InterProiIPR012975. NOPS.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    PfamiPF08075. NOPS. 1 hit.
    PF00076. RRM_1. 2 hits.
    [Graphical view]
    SMARTiSM00360. RRM. 2 hits.
    [Graphical view]
    PROSITEiPS50102. RRM. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform Long (identifier: P23246-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MSRDRFRSRG GGGGGFHRRG GGGGRGGLHD FRSPPPGMGL NQNRGPMGPG    50
    PGQSGPKPPI PPPPPHQQQQ QPPPQQPPPQ QPPPHQPPPH PQPHQQQQPP 100
    PPPQDSSKPV VAQGPGPAPG VGSAPPASSS APPATPPTSG APPGSGPGPT 150
    PTPPPAVTSA PPGAPPPTPP SSGVPTTPPQ AGGPPPPPAA VPGPGPGPKQ 200
    GPGPGGPKGG KMPGGPKPGG GPGLSTPGGH PKPPHRGGGE PRGGRQHHPP 250
    YHQQHHQGPP PGGPGGRSEE KISDSEGFKA NLSLLRRPGE KTYTQRCRLF 300
    VGNLPADITE DEFKRLFAKY GEPGEVFINK GKGFGFIKLE SRALAEIAKA 350
    ELDDTPMRGR QLRVRFATHA AALSVRNLSP YVSNELLEEA FSQFGPIERA 400
    VVIVDDRGRS TGKGIVEFAS KPAARKAFER CSEGVFLLTT TPRPVIVEPL 450
    EQLDDEDGLP EKLAQKNPMY QKERETPPRF AQHGTFEYEY SQRWKSLDEM 500
    EKQQREQVEK NMKDAKDKLE SEMEDAYHEH QANLLRQDLM RRQEELRRME 550
    ELHNQEMQKR KEMQLRQEEE RRRREEEMMI RQREMEEQMR RQREESYSRM 600
    GYMDPRERDM RMGGGGAMNM GDPYGSGGQK FPPLGGGGGI GYEANPGVPP 650
    ATMSGSMMGS DMRTERFGQG GAGPVGGQGP RGMGPGTPAG YGRGREEYEG 700
    PNKKPRF 707
    Length:707
    Mass (Da):76,149
    Last modified:October 1, 1996 - v2
    Checksum:i6D8D5EA95E235847
    GO
    Isoform Short (identifier: P23246-2) [UniParc]FASTAAdd to Basket

    Also known as: F

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

    Show »
    Length:669
    Mass (Da):72,263
    Checksum:i46BAE5D117400578
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti243 – 2431G → R AA sequence (PubMed:8439294)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei663 – 70745RTERF…KKPRF → VRMIDVG in isoform Short. CuratedVSP_005855Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X70944 mRNA. Translation: CAA50283.1.
    AL590434 Genomic DNA. Translation: CAI12467.1.
    CH471059 Genomic DNA. Translation: EAX07426.1.
    X16850 mRNA. Translation: CAA34747.1.
    CCDSiCCDS388.1. [P23246-1]
    PIRiA46302.
    S29770.
    RefSeqiNP_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]
    UniGeneiHs.355934.
    Hs.611911.

    Genome annotation databases

    EnsembliENST00000357214; ENSP00000349748; ENSG00000116560. [P23246-1]
    GeneIDi6421.
    KEGGihsa:6421.
    UCSCiuc001bys.3. human. [P23246-1]

    Polymorphism databases

    DMDMi1709851.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X70944 mRNA. Translation: CAA50283.1 .
    AL590434 Genomic DNA. Translation: CAI12467.1 .
    CH471059 Genomic DNA. Translation: EAX07426.1 .
    X16850 mRNA. Translation: CAA34747.1 .
    CCDSi CCDS388.1. [P23246-1 ]
    PIRi A46302.
    S29770.
    RefSeqi NP_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 ]
    UniGenei Hs.355934.
    Hs.611911.

    3D structure databases

    ProteinModelPortali P23246.
    SMRi P23246. Positions 287-535.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112319. 132 interactions.
    IntActi P23246. 48 interactions.
    MINTi MINT-1141893.
    STRINGi 9606.ENSP00000349748.

    PTM databases

    PhosphoSitei P23246.

    Polymorphism databases

    DMDMi 1709851.

    2D gel databases

    SWISS-2DPAGE P23246.

    Proteomic databases

    MaxQBi P23246.
    PaxDbi P23246.
    PeptideAtlasi P23246.
    PRIDEi P23246.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000357214 ; ENSP00000349748 ; ENSG00000116560 . [P23246-1 ]
    GeneIDi 6421.
    KEGGi hsa:6421.
    UCSCi uc001bys.3. human. [P23246-1 ]

    Organism-specific databases

    CTDi 6421.
    GeneCardsi GC01M035641.
    HGNCi HGNC:10774. SFPQ.
    HPAi CAB009886.
    HPA047513.
    MIMi 605199. gene.
    neXtProti NX_P23246.
    Orphaneti 319308. Translocation renal cell carcinoma.
    PharmGKBi PA35690.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG298586.
    HOGENOMi HOG000231095.
    HOVERGENi HBG009801.
    InParanoidi P23246.
    KOi K13219.
    OMAi APGGHPK.
    OrthoDBi EOG7327P0.
    PhylomeDBi P23246.
    TreeFami TF315795.

    Miscellaneous databases

    ChiTaRSi SFPQ. human.
    GeneWikii SFPQ.
    GenomeRNAii 6421.
    NextBioi 24935.
    PROi P23246.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P23246.
    Bgeei P23246.
    CleanExi HS_SFPQ.
    Genevestigatori P23246.

    Family and domain databases

    Gene3Di 3.30.70.330. 2 hits.
    InterProi IPR012975. NOPS.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF08075. NOPS. 1 hit.
    PF00076. RRM_1. 2 hits.
    [Graphical view ]
    SMARTi SM00360. RRM. 2 hits.
    [Graphical view ]
    PROSITEi PS50102. RRM. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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. 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. 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].

    Entry informationi

    Entry nameiSFPQ_HUMAN
    AccessioniPrimary (citable) accession number: P23246
    Secondary accession number(s): P30808, Q5SZ71
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 168 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Caution

    Was originally thought to be myoblast cell surface antigen 24.1D5 and a possible membrane-bound protein ectokinase.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3