SFPQ_HUMAN
ID SFPQ_HUMAN Reviewed; 707 AA.
AC P23246; P30808; Q5SZ71;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 235.
DE RecName: Full=Splicing factor, proline- and glutamine-rich;
DE AltName: Full=100 kDa DNA-pairing protein;
DE Short=hPOMp100;
DE AltName: Full=DNA-binding p52/p100 complex, 100 kDa subunit;
DE AltName: Full=Polypyrimidine tract-binding protein-associated-splicing factor {ECO:0000303|PubMed:9848648};
DE Short=PSF {ECO:0000303|PubMed:8449401};
DE Short=PTB-associated-splicing factor;
GN Name=SFPQ; Synonyms=PSF;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, ALTERNATIVE SPLICING,
RP AND FUNCTION.
RC TISSUE=Fetal brain;
RX PubMed=8449401; DOI=10.1101/gad.7.3.393;
RA Patton J.G., Porro E.B., Galceran J., Tempst P., Nadal-Ginard B.;
RT "Cloning and characterization of PSF, a novel pre-mRNA splicing factor.";
RL Genes Dev. 7:393-406(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 33-44; 218-236; 246-267; 272-286; 299-315; 320-330;
RP 350-358; 364-407; 414-425; 431-462; 480-493; 517-536; 549-559; 567-572;
RP 575-581; 600-606; 612-630 AND 667-695, METHYLATION AT LYS-314; ARG-571;
RP ARG-681 AND ARG-693, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [5]
RP PROTEIN SEQUENCE OF 48-68 AND 213-246, BLOCKAGE OF N-TERMINUS, DNA-BINDING,
RP AND SUBUNIT.
RX PubMed=8439294; DOI=10.1042/bj2900267;
RA Zhang W.-W., Zhang L.-X., Busch R.K., Farres J., Busch H.;
RT "Purification and characterization of a DNA-binding heterodimer of 52 and
RT 100 kDa from HeLa cells.";
RL Biochem. J. 290:267-272(1993).
RN [6]
RP PROTEIN SEQUENCE OF 292-311; 415-421 AND 503-510, AND IDENTIFICATION IN
RP U5/4/6 SNRNP COMPLEXES.
RX PubMed=9409622;
RA Teigelkamp S., Mundt C., Achsel T., Will C.L., Luehrmann R.;
RT "The human U5 snRNP-specific 100-kD protein is an RS domain-containing,
RT putative RNA helicase with significant homology to the yeast splicing
RT factor Prp28p.";
RL RNA 3:1313-1326(1997).
RN [7]
RP PROTEIN SEQUENCE OF 299-314 AND 480-493, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 312-707.
RC TISSUE=Fetal skeletal muscle;
RX PubMed=2480877; DOI=10.1242/dev.105.4.723;
RA Gower H.J., Moore S.E., Dickson G., Elsom V.L., Nayak R., Walsh F.S.;
RT "Cloning and characterization of a myoblast cell surface antigen defined by
RT 24.1D5 monoclonal antibody.";
RL Development 105:723-731(1989).
RN [9]
RP PROTEIN SEQUENCE OF 414-421 AND 427-448, SUBCELLULAR LOCATION, INTERACTION
RP WITH SNRPA, AND IDENTIFICATION IN A SNRNP-FREE COMPLEX WITH SNRPA.
RX PubMed=9848648; DOI=10.1017/s1355838298981183;
RA Lutz C.S., Cooke C., O'Connor J.P., Kobayashi R., Alwine J.C.;
RT "The snRNP-free U1A (SF-A) complex(es): identification of the largest
RT subunit as PSF, the polypyrimidine-tract binding protein-associated
RT splicing factor.";
RL RNA 4:1493-1499(1998).
RN [10]
RP PROTEIN SEQUENCE OF 600-606 AND 667-677, INTERACTION WITH PTBP1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=10653975;
RX DOI=10.1002/(sici)1097-4644(20000315)76:4<559::aid-jcb4>3.0.co;2-u;
RA Meissner M., Dechat T., Gerner C., Grimm R., Foisner R., Sauermann G.;
RT "Differential nuclear localization and nuclear matrix association of the
RT splicing factors PSF and PTB.";
RL J. Cell. Biochem. 76:559-566(2000).
RN [11]
RP FUNCTION, INTERACTION WITH PRE-MRNA, AND IDENTIFICATION IN SPLICEOSOME
RP COMPLEX.
RX PubMed=8045264; DOI=10.1002/j.1460-2075.1994.tb06638.x;
RA Gozani O., Patton J.G., Reed R.;
RT "A novel set of spliceosome-associated proteins and the essential splicing
RT factor PSF bind stably to pre-mRNA prior to catalytic step II of the
RT splicing reaction.";
RL EMBO J. 13:3356-3367(1994).
RN [12]
RP CHROMOSOMAL TRANSLOCATION WITH TFE3.
RX PubMed=9393982; DOI=10.1038/sj.onc.1201394;
RA Clark J., Lu Y.-J., Sidhar S.K., Parker C., Gill S., Smedley D.,
RA Hamoudi R., Linehan W.M., Shipley J., Cooper C.S.;
RT "Fusion of splicing factor genes PSF and NonO (p54nrb) to the TFE3 gene in
RT papillary renal cell carcinoma.";
RL Oncogene 15:2233-2239(1997).
RN [13]
RP INTERACTION WITH TOP1, AND IDENTIFICATION IN A COMPLEX WITH NONO AND TOP1.
RX PubMed=9756848; DOI=10.1074/jbc.273.41.26261;
RA Straub T., Grue P., Uhse A., Lisby M., Knudsen B.R., Tange T.O.,
RA Westergaard O., Boege F.;
RT "The RNA-splicing factor PSF/p54 controls DNA-topoisomerase I activity by a
RT direct interaction.";
RL J. Biol. Chem. 273:26261-26264(1998).
RN [14]
RP FUNCTION IN DNA UNWINDING.
RX PubMed=10858305; DOI=10.1021/bi992898e;
RA Straub T., Knudsen B.R., Boege F.;
RT "PSF/p54(nrb) stimulates 'jumping' of DNA topoisomerase I between separate
RT DNA helices.";
RL Biochemistry 39:7552-7558(2000).
RN [15]
RP FUNCTION IN TRANSCRIPTION REGULATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=10847580; DOI=10.1210/mend.14.6.0485;
RA Urban R.J., Bodenburg Y., Kurosky A., Wood T.G., Gasic S.;
RT "Polypyrimidine tract-binding protein-associated splicing factor is a
RT negative regulator of transcriptional activity of the porcine p450scc
RT insulin-like growth factor response element.";
RL Mol. Endocrinol. 14:774-782(2000).
RN [16]
RP FUNCTION IN HOMOLOGOUS DNA PAIRING, AND PHOSPHORYLATION.
RX PubMed=10931916; DOI=10.1093/nar/28.16.3022;
RA Akhmedov A.T., Lopez B.S.;
RT "Human 100-kDa homologous DNA-pairing protein is the splicing factor PSF
RT and promotes DNA strand invasion.";
RL Nucleic Acids Res. 28:3022-3030(2000).
RN [17]
RP FUNCTION IN NUCLEAR RETENTION OF A-TO-I EDITED RNAS, AND IDENTIFICATION IN
RP A COMPLEX WITH NONO AND MATR3.
RX PubMed=11525732; DOI=10.1016/s0092-8674(01)00466-4;
RA Zhang Z., Carmichael G.G.;
RT "The fate of dsRNA in the nucleus: a p54(nrb)-containing complex mediates
RT the nuclear retention of promiscuously A-to-I edited RNAs.";
RL Cell 106:465-475(2001).
RN [18]
RP INTERACTION WITH SNRNP70, AND PHOSPHORYLATION.
RX PubMed=11514619; DOI=10.1091/mbc.12.8.2328;
RA Shav-Tal Y., Cohen M., Lapter S., Dye B., Patton J.G., Vandekerckhove J.,
RA Zipori D.;
RT "Nuclear relocalization of the pre-mRNA splicing factor PSF during
RT apoptosis involves hyperphosphorylation, masking of antigenic epitopes, and
RT changes in protein interactions.";
RL Mol. Biol. Cell 12:2328-2340(2001).
RN [19]
RP FUNCTION IN TRANSCRIPTION REGULATION, AND INTERACTION WITH RXRA; THRA AND
RP SIN3A.
RX PubMed=11259580; DOI=10.1128/mcb.21.7.2298-2311.2001;
RA Mathur M., Tucker P.W., Samuels H.H.;
RT "PSF is a novel corepressor that mediates its effect through Sin3A and the
RT DNA binding domain of nuclear hormone receptors.";
RL Mol. Cell. Biol. 21:2298-2311(2001).
RN [20]
RP FUNCTION IN TRANSCRIPTION REGULATION, INTERACTION WITH NR5A1 AND SIN3A, AND
RP IDENTIFICATION IN A COMPLEX WITH NONO AND NR5A1.
RX PubMed=11897684; DOI=10.1210/endo.143.4.8748;
RA Sewer M.B., Nguyen V.Q., Huang C.J., Tucker P.W., Kagawa N., Waterman M.R.;
RT "Transcriptional activation of human CYP17 in H295R adrenocortical cells
RT depends on complex formation among p54(nrb)/NonO, protein-associated
RT splicing factor, and SF-1, a complex that also participates in repression
RT of transcription.";
RL Endocrinology 143:1280-1290(2002).
RN [21]
RP INTERACTION WITH NONO AND U5 SNRNA, AND IDENTIFICATION IN U5/4/6 SNRNP AND
RP SPLICEOSOME COMPLEXES.
RX PubMed=12403470; DOI=10.1017/s1355838202022070;
RA Peng R., Dye B.T., Perez I., Barnard D.C., Thompson A.B., Patton J.G.;
RT "PSF and p54nrb bind a conserved stem in U5 snRNA.";
RL RNA 8:1334-1347(2002).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [23]
RP FUNCTION IN DNA REPAIR, IDENTIFICATION BY MASS SPECTROMETRY, DNA-BINDING,
RP AND SUBUNIT.
RX PubMed=15590677; DOI=10.1074/jbc.m412758200;
RA Bladen C.L., Udayakumar D., Takeda Y., Dynan W.S.;
RT "Identification of the polypyrimidine tract binding protein-associated
RT splicing factor.p54(nrb) complex as a candidate DNA double-strand break
RT rejoining factor.";
RL J. Biol. Chem. 280:5205-5210(2005).
RN [24]
RP IDENTIFICATION IN A COMPLEX WITH NONO AND WASL.
RX PubMed=16767080; DOI=10.1038/ncb1433;
RA Wu X., Yoo Y., Okuhama N.N., Tucker P.W., Liu G., Guan J.L.;
RT "Regulation of RNA-polymerase-II-dependent transcription by N-WASP and its
RT nuclear-binding partners.";
RL Nat. Cell Biol. 8:756-763(2006).
RN [25]
RP PHOSPHORYLATION AT TYR-293.
RX PubMed=17537995; DOI=10.1182/blood-2006-01-028647;
RA Galietta A., Gunby R.H., Redaelli S., Stano P., Carniti C., Bachi A.,
RA Tucker P.W., Tartari C.J., Huang C.J., Colombo E., Pulford K., Puttini M.,
RA Piazza R.G., Ruchatz H., Villa A., Donella-Deana A., Marin O., Perrotti D.,
RA Gambacorti-Passerini C.;
RT "NPM/ALK binds and phosphorylates the RNA/DNA-binding protein PSF in
RT anaplastic large-cell lymphoma.";
RL Blood 110:2600-2609(2007).
RN [26]
RP PHOSPHORYLATION AT SER-8 AND SER-283 BY MKNK2.
RX PubMed=17965020; DOI=10.1074/jbc.m705286200;
RA Buxade M., Morrice N., Krebs D.L., Proud C.G.;
RT "The PSF.p54nrb complex is a novel Mnk substrate that binds the mRNA for
RT tumor necrosis factor alpha.";
RL J. Biol. Chem. 283:57-65(2008).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-687, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273 AND THR-687, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [29]
RP INTERACTION WITH RNF43.
RX PubMed=18655028; DOI=10.1002/pmic.200800083;
RA Miyamoto K., Sakurai H., Sugiura T.;
RT "Proteomic identification of a PSF/p54nrb heterodimer as RNF43 oncoprotein-
RT interacting proteins.";
RL Proteomics 8:2907-2910(2008).
RN [30]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [31]
RP PHOSPHORYLATION, INTERACTION WITH PTK6, AND SUBCELLULAR LOCATION.
RX PubMed=19439179; DOI=10.1016/j.cellsig.2009.04.008;
RA Lukong K.E., Huot M.E., Richard S.;
RT "BRK phosphorylates PSF promoting its cytoplasmic localization and cell
RT cycle arrest.";
RL Cell. Signal. 21:1415-1422(2009).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [33]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-319; LYS-338; LYS-421 AND
RP LYS-472, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [34]
RP FUNCTION, PHOSPHORYLATION AT THR-687, INTERACTION WITH THRAP3, AND
RP MUTAGENESIS OF THR-687.
RX PubMed=20932480; DOI=10.1016/j.molcel.2010.09.013;
RA Heyd F., Lynch K.W.;
RT "Phosphorylation-dependent regulation of PSF by GSK3 controls CD45
RT alternative splicing.";
RL Mol. Cell 40:126-137(2010).
RN [35]
RP INTERACTION WITH M.TUBERCULOSIS RV3654C (MICROBIAL INFECTION).
RX PubMed=20454556; DOI=10.1371/journal.pone.0010474;
RA Danelishvili L., Yamazaki Y., Selker J., Bermudez L.E.;
RT "Secreted Mycobacterium tuberculosis Rv3654c and Rv3655c proteins
RT participate in the suppression of macrophage apoptosis.";
RL PLoS ONE 5:E10474-E10474(2010).
RN [36]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND SER-626, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [37]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [38]
RP INTERACTION WITH PQBP1.
RX PubMed=21933836; DOI=10.1093/hmg/ddr430;
RA Kunde S.A., Musante L., Grimme A., Fischer U., Mueller E., Wanker E.E.,
RA Kalscheuer V.M.;
RT "The X-chromosome-linked intellectual disability protein PQBP1 is a
RT component of neuronal RNA granules and regulates the appearance of stress
RT granules.";
RL Hum. Mol. Genet. 20:4916-4931(2011).
RN [39]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33; SER-273 AND SER-283, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [40]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33; SER-273; SER-283;
RP THR-368; SER-374; SER-496; SER-626; THR-687 AND TYR-691, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [41]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [42]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-236; ARG-242; ARG-245; ARG-681;
RP ARG-693 AND ARG-695, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [43]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-338, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [44]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-338, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [45]
RP INTERACTION WITH ERCC6.
RX PubMed=26030138; DOI=10.1371/journal.pone.0128558;
RA Nicolai S., Filippi S., Caputo M., Cipak L., Gregan J., Ammerer G.,
RA Frontini M., Willems D., Prantera G., Balajee A.S., Proietti-De-Santis L.;
RT "Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group
RT B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin
RT Dynamics.";
RL PLoS ONE 10:E0128558-E0128558(2015).
RN [46]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [47]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PRKDC; XRCC5; XRCC6;
RP HEXIM1; NONO; PSPC1; RBM14 AND MATR3.
RX PubMed=28712728; DOI=10.1016/j.molcel.2017.06.020;
RA Morchikh M., Cribier A., Raffel R., Amraoui S., Cau J., Severac D.,
RA Dubois E., Schwartz O., Bennasser Y., Benkirane M.;
RT "HEXIM1 and NEAT1 Long non-coding RNA form a multi-subunit complex that
RT regulates DNA-mediated innate immune response.";
RL Mol. Cell 67:387-399(2017).
RN [48]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-271; LYS-279 AND LYS-338, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [49]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 276-535, COILED COIL, SUBUNIT,
RP INTERACTION WITH NONO, FUNCTION, DOMAIN, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF LEU-535; LEU-539; LEU-546 AND MET-549.
RX PubMed=25765647; DOI=10.1093/nar/gkv156;
RA Lee M., Sadowska A., Bekere I., Ho D., Gully B.S., Lu Y., Iyer K.S.,
RA Trewhella J., Fox A.H., Bond C.S.;
RT "The structure of human SFPQ reveals a coiled-coil mediated polymer
RT essential for functional aggregation in gene regulation.";
RL Nucleic Acids Res. 43:3826-3840(2015).
CC -!- FUNCTION: DNA- and RNA binding protein, involved in several nuclear
CC processes. Essential pre-mRNA splicing factor required early in
CC spliceosome formation and for splicing catalytic step II, probably as a
CC heteromer with NONO. Binds to pre-mRNA in spliceosome C complex, and
CC specifically binds to intronic polypyrimidine tracts. Involved in
CC regulation of signal-induced alternative splicing. During splicing of
CC PTPRC/CD45, a phosphorylated form is sequestered by THRAP3 from the
CC pre-mRNA in resting T-cells; T-cell activation and subsequent reduced
CC phosphorylation is proposed to lead to release from THRAP3 allowing
CC binding to pre-mRNA splicing regulatotry elements which represses exon
CC inclusion. Interacts with U5 snRNA, probably by binding to a purine-
CC rich sequence located on the 3' side of U5 snRNA stem 1b. May be
CC involved in a pre-mRNA coupled splicing and polyadenylation process as
CC component of a snRNP-free complex with SNRPA/U1A. The SFPQ-NONO
CC heteromer associated with MATR3 may play a role in nuclear retention of
CC defective RNAs. SFPQ may be involved in homologous DNA pairing; in
CC vitro, promotes the invasion of ssDNA between a duplex DNA and produces
CC a D-loop formation. The SFPQ-NONO heteromer may be involved in DNA
CC unwinding by modulating the function of topoisomerase I/TOP1; in vitro,
CC stimulates dissociation of TOP1 from DNA after cleavage and enhances
CC its jumping between separate DNA helices. The SFPQ-NONO heteromer binds
CC DNA (PubMed:25765647). The SFPQ-NONO heteromer may be involved in DNA
CC non-homologous end joining (NHEJ) required for double-strand break
CC repair and V(D)J recombination and may stabilize paired DNA ends; in
CC vitro, the complex strongly stimulates DNA end joining, binds directly
CC to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5
CC (Ku) dimer to establish a functional preligation complex. SFPQ is
CC involved in transcriptional regulation. Functions as transcriptional
CC activator (PubMed:25765647). Transcriptional repression is mediated by
CC an interaction of SFPQ with SIN3A and subsequent recruitment of histone
CC deacetylases (HDACs). The SFPQ-NONO-NR5A1 complex binds to the CYP17
CC promoter and regulates basal and cAMP-dependent transcriptional
CC activity. SFPQ isoform Long binds to the DNA binding domains (DBD) of
CC nuclear hormone receptors, like RXRA and probably THRA, and acts as
CC transcriptional corepressor in absence of hormone ligands. Binds the
CC DNA sequence 5'-CTGAGTC-3' in the insulin-like growth factor response
CC element (IGFRE) and inhibits IGF-I-stimulated transcriptional activity.
CC Regulates the circadian clock by repressing the transcriptional
CC activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Required for
CC the transcriptional repression of circadian target genes, such as PER1,
CC mediated by the large PER complex through histone deacetylation (By
CC similarity). Required for the assembly of nuclear speckles
CC (PubMed:25765647). Plays a role in the regulation of DNA virus-mediated
CC innate immune response by assembling into the HDP-RNP complex, a
CC complex that serves as a platform for IRF3 phosphorylation and
CC subsequent innate immune response activation through the cGAS-STING
CC pathway (PubMed:28712728). {ECO:0000250|UniProtKB:Q8VIJ6,
CC ECO:0000269|PubMed:10847580, ECO:0000269|PubMed:10858305,
CC ECO:0000269|PubMed:10931916, ECO:0000269|PubMed:11259580,
CC ECO:0000269|PubMed:11525732, ECO:0000269|PubMed:11897684,
CC ECO:0000269|PubMed:15590677, ECO:0000269|PubMed:20932480,
CC ECO:0000269|PubMed:25765647, ECO:0000269|PubMed:28712728,
CC ECO:0000269|PubMed:8045264, ECO:0000269|PubMed:8449401}.
CC -!- SUBUNIT: Heterodimer with NONO (PubMed:25765647). Monomer and component
CC of the SFPQ-NONO complex, which is probably a heterotetramer of two 52
CC kDa (NONO) and two 100 kDa (SFPQ) subunits (PubMed:8439294,
CC PubMed:25765647). The coiled coil domain mediates interaction with
CC NONO, and can also mediate formation of long, linear homooligomers (in
CC vitro) (PubMed:25765647). SFPQ is a component of spliceosome and U5.4/6
CC snRNP complexes (PubMed:9409622, PubMed:8045264, PubMed:12403470).
CC Interacts with SNRPA/U1A (PubMed:9848648). Component of a snRNP-free
CC complex with SNRPA/U1A (PubMed:9848648). Part of complex consisting of
CC SFPQ, NONO and MATR3 (PubMed:11525732). Interacts with polypyrimidine
CC tract-binding protein 1/PTB (PubMed:10653975). Part of a complex
CC consisting of SFPQ, NONO and NR5A1 (PubMed:11897684). Interacts with
CC RXRA, probably THRA, and SIN3A (PubMed:11259580). Interacts with TOP1
CC (PubMed:9756848). Part of a complex consisting of SFPQ, NONO and TOP1
CC (PubMed:9756848). Interacts with SNRNP70 in apoptotic cells
CC (PubMed:11514619). Interacts with PSPC1. Interacts with RNF43
CC (PubMed:18655028). Interacts with PITX3 and NR4A2/NURR1 (By
CC similarity). Interacts with PTK6 (PubMed:19439179). Interacts with
CC THRAP3; the interaction is dependent on SFPQ phosphorylation at 'Thr-
CC 687' and inhibits binding of SFPQ to a ESS1 exonic splicing silencer
CC element-containing RNA (PubMed:20932480). The large PER complex
CC involved in the histone deacetylation is composed of at least HDAC1,
CC PER2, SFPQ and SIN3A. Interacts with PER1 and PER2 (By similarity).
CC Interacts with PQBP1 (PubMed:21933836). Component of a multiprotein
CC complex with NONO and WASL (PubMed:16767080). Interacts with ERCC6
CC (PubMed:26030138). {ECO:0000250|UniProtKB:Q8VIJ6,
CC ECO:0000269|PubMed:10653975, ECO:0000269|PubMed:11259580,
CC ECO:0000269|PubMed:11514619, ECO:0000269|PubMed:11525732,
CC ECO:0000269|PubMed:11897684, ECO:0000269|PubMed:12403470,
CC ECO:0000269|PubMed:15590677, ECO:0000269|PubMed:16767080,
CC ECO:0000269|PubMed:18655028, ECO:0000269|PubMed:19439179,
CC ECO:0000269|PubMed:20932480, ECO:0000269|PubMed:21933836,
CC ECO:0000269|PubMed:25765647, ECO:0000269|PubMed:26030138,
CC ECO:0000269|PubMed:8045264, ECO:0000269|PubMed:8439294,
CC ECO:0000269|PubMed:9409622, ECO:0000269|PubMed:9756848,
CC ECO:0000269|PubMed:9848648}.
CC -!- SUBUNIT: (Microbial infection) Interacts with M.tuberculosis protein
CC Rv3654c, which probably leads to the cleavage of PSF, diminishes the
CC level of caspase-8 in macrophages and suppresses macrophage apoptosis
CC by blocking the extrinsic pathway. Part of the HDP-RNP complex composed
CC of at least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle proteins (SFPQ,
CC NONO, PSPC1, RBM14, and MATR3) and NEAT1 RNA.
CC {ECO:0000269|PubMed:20454556, ECO:0000269|PubMed:28712728}.
CC -!- INTERACTION:
CC P23246; P41235: HNF4A; NbExp=2; IntAct=EBI-355453, EBI-1049011;
CC P23246; Q15233: NONO; NbExp=5; IntAct=EBI-355453, EBI-350527;
CC P23246; P26599: PTBP1; NbExp=2; IntAct=EBI-355453, EBI-350540;
CC P23246; Q13882: PTK6; NbExp=5; IntAct=EBI-355453, EBI-1383632;
CC P23246; Q96ST3: SIN3A; NbExp=2; IntAct=EBI-355453, EBI-347218;
CC P23246; P09012: SNRPA; NbExp=4; IntAct=EBI-355453, EBI-607085;
CC P23246; Q9Y2W1: THRAP3; NbExp=6; IntAct=EBI-355453, EBI-352039;
CC P23246; Q8AZK7: EBNA-LP; Xeno; NbExp=2; IntAct=EBI-355453, EBI-1185167;
CC P23246-1; P28700: Rxra; Xeno; NbExp=3; IntAct=EBI-355463, EBI-346715;
CC P23246-1; P04625: THRA; Xeno; NbExp=2; IntAct=EBI-355463, EBI-286261;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:25765647}.
CC Nucleus matrix {ECO:0000269|PubMed:10653975,
CC ECO:0000269|PubMed:19439179, ECO:0000269|PubMed:9848648}. Cytoplasm
CC {ECO:0000269|PubMed:19439179}. Note=Predominantly in nuclear matrix.
CC {ECO:0000269|PubMed:19439179}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=Long; Synonyms=A;
CC IsoId=P23246-1; Sequence=Displayed;
CC Name=Short; Synonyms=F;
CC IsoId=P23246-2; Sequence=VSP_005855;
CC -!- DOMAIN: The coiled coil domain mediates interaction with NONO, and can
CC also mediate formation of long, linear homooligomers (in vitro). The
CC coiled coil domain is required for optimal DNA binding, and optimal
CC transcription activation. {ECO:0000269|PubMed:25765647}.
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: Phosphorylated on multiple serine and threonine residues during
CC apoptosis. In vitro phosphorylated by PKC. Phosphorylation stimulates
CC binding to DNA and D-loop formation, but inhibits binding to RNA.
CC Phosphorylation of C-terminal tyrosines promotes its cytoplasmic
CC localization, impaired its binding to polypyrimidine RNA and led to
CC cell cycle arrest. In resting T-cells is phosphorylated at Thr-687 by
CC GSK3B which is proposed to promote association with THRAP and to
CC prevent binding to PTPRC/CD45 pre-mRNA; T-cell activation leads to
CC reduced phosphorylation at Thr-687. {ECO:0000269|PubMed:10931916,
CC ECO:0000269|PubMed:11514619, ECO:0000269|PubMed:17537995,
CC ECO:0000269|PubMed:17965020, ECO:0000269|PubMed:19439179,
CC ECO:0000269|PubMed:20932480}.
CC -!- DISEASE: Note=A chromosomal aberration involving SFPQ may be a cause of
CC papillary renal cell carcinoma (PRCC). Translocation t(X;1)(p11.2;p34)
CC with TFE3.
CC -!- CAUTION: Was originally thought to be myoblast cell surface antigen
CC 24.1D5 and a possible membrane-bound protein ectokinase.
CC {ECO:0000305|PubMed:2480877}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PSFID167.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X70944; CAA50283.1; -; mRNA.
DR EMBL; AL590434; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07426.1; -; Genomic_DNA.
DR EMBL; X16850; CAA34747.1; -; mRNA.
DR CCDS; CCDS388.1; -. [P23246-1]
DR PIR; A46302; A46302.
DR PIR; S29770; S29770.
DR RefSeq; NP_005057.1; NM_005066.2. [P23246-1]
DR RefSeq; XP_005271169.1; XM_005271112.4. [P23246-1]
DR RefSeq; XP_005271170.1; XM_005271113.4. [P23246-1]
DR RefSeq; XP_005271172.1; XM_005271115.4. [P23246-2]
DR RefSeq; XP_016857542.1; XM_017002053.1. [P23246-1]
DR RefSeq; XP_016857543.1; XM_017002054.1. [P23246-1]
DR PDB; 4WII; X-ray; 2.05 A; A/B=276-535.
DR PDB; 4WIJ; X-ray; 3.49 A; A/B=276-598.
DR PDB; 4WIK; X-ray; 3.00 A; A/B=369-598.
DR PDB; 5WPA; X-ray; 2.29 A; A=276-535.
DR PDB; 6NCQ; X-ray; 1.90 A; A=276-535.
DR PDB; 6OWJ; X-ray; 1.94 A; A/B=276-535.
DR PDB; 6WMZ; X-ray; 2.85 A; A/C=214-598.
DR PDB; 7LRQ; X-ray; 2.30 A; A=276-535.
DR PDB; 7LRU; X-ray; 1.60 A; B=278-456, B=505-535.
DR PDB; 7PU5; X-ray; 3.00 A; B/D/F/H/J/L=277-535.
DR PDBsum; 4WII; -.
DR PDBsum; 4WIJ; -.
DR PDBsum; 4WIK; -.
DR PDBsum; 5WPA; -.
DR PDBsum; 6NCQ; -.
DR PDBsum; 6OWJ; -.
DR PDBsum; 6WMZ; -.
DR PDBsum; 7LRQ; -.
DR PDBsum; 7LRU; -.
DR PDBsum; 7PU5; -.
DR AlphaFoldDB; P23246; -.
DR SASBDB; P23246; -.
DR SMR; P23246; -.
DR BioGRID; 112319; 452.
DR CORUM; P23246; -.
DR DIP; DIP-31272N; -.
DR IntAct; P23246; 128.
DR MINT; P23246; -.
DR STRING; 9606.ENSP00000349748; -.
DR DrugBank; DB11638; Artenimol.
DR DrugBank; DB09130; Copper.
DR GlyGen; P23246; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P23246; -.
DR MetOSite; P23246; -.
DR PhosphoSitePlus; P23246; -.
DR SwissPalm; P23246; -.
DR BioMuta; SFPQ; -.
DR DMDM; 1709851; -.
DR SWISS-2DPAGE; P23246; -.
DR EPD; P23246; -.
DR jPOST; P23246; -.
DR MassIVE; P23246; -.
DR MaxQB; P23246; -.
DR PaxDb; P23246; -.
DR PeptideAtlas; P23246; -.
DR PRIDE; P23246; -.
DR ProteomicsDB; 54073; -. [P23246-1]
DR ProteomicsDB; 54074; -. [P23246-2]
DR Antibodypedia; 4083; 329 antibodies from 35 providers.
DR DNASU; 6421; -.
DR Ensembl; ENST00000357214.6; ENSP00000349748.5; ENSG00000116560.11. [P23246-1]
DR GeneID; 6421; -.
DR KEGG; hsa:6421; -.
DR MANE-Select; ENST00000357214.6; ENSP00000349748.5; NM_005066.3; NP_005057.1.
DR UCSC; uc001bys.4; human. [P23246-1]
DR CTD; 6421; -.
DR DisGeNET; 6421; -.
DR GeneCards; SFPQ; -.
DR HGNC; HGNC:10774; SFPQ.
DR HPA; ENSG00000116560; Low tissue specificity.
DR MalaCards; SFPQ; -.
DR MIM; 605199; gene.
DR neXtProt; NX_P23246; -.
DR OpenTargets; ENSG00000116560; -.
DR Orphanet; 319308; MiT family translocation renal cell carcinoma.
DR PharmGKB; PA35690; -.
DR VEuPathDB; HostDB:ENSG00000116560; -.
DR eggNOG; KOG0115; Eukaryota.
DR GeneTree; ENSGT00940000156221; -.
DR HOGENOM; CLU_027185_1_0_1; -.
DR InParanoid; P23246; -.
DR OMA; HKGGPGH; -.
DR OrthoDB; 1274880at2759; -.
DR PhylomeDB; P23246; -.
DR TreeFam; TF315795; -.
DR PathwayCommons; P23246; -.
DR Reactome; R-HSA-8849468; PTK6 Regulates Proteins Involved in RNA Processing.
DR Reactome; R-HSA-9635465; Suppression of apoptosis.
DR SignaLink; P23246; -.
DR SIGNOR; P23246; -.
DR BioGRID-ORCS; 6421; 767 hits in 1091 CRISPR screens.
DR ChiTaRS; SFPQ; human.
DR GeneWiki; SFPQ; -.
DR GenomeRNAi; 6421; -.
DR Pharos; P23246; Tbio.
DR PRO; PR:P23246; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P23246; protein.
DR Bgee; ENSG00000116560; Expressed in tendon of biceps brachii and 205 other tissues.
DR ExpressionAtlas; P23246; baseline and differential.
DR Genevisible; P23246; HS.
DR GO; GO:0000785; C:chromatin; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC.
DR GO; GO:0016363; C:nuclear matrix; IDA:BHF-UCL.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
DR GO; GO:0042382; C:paraspeckles; IDA:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISS:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; ISS:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0002218; P:activation of innate immune response; IDA:UniProtKB.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IMP:BHF-UCL.
DR GO; GO:0051276; P:chromosome organization; IEA:Ensembl.
DR GO; GO:0098963; P:dendritic transport of messenger ribonucleoprotein complex; IEA:Ensembl.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:MGI.
DR GO; GO:0070932; P:histone H3 deacetylation; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; TAS:ProtInc.
DR GO; GO:0042754; P:negative regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ParkinsonsUK-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:1902177; P:positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
DR GO; GO:0045876; P:positive regulation of sister chromatid cohesion; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
DR CDD; cd12948; NOPS_PSF; 1.
DR CDD; cd12587; RRM1_PSF; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012975; NOPS.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR034526; PSF_NOPS.
DR InterPro; IPR034525; PSF_RRM1.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF08075; NOPS; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing;
KW Biological rhythms; Chromosomal rearrangement; Coiled coil; Cytoplasm;
KW Direct protein sequencing; DNA damage; DNA recombination; DNA repair;
KW DNA-binding; Immunity; Innate immunity; Isopeptide bond; Methylation;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; RNA-binding; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..707
FT /note="Splicing factor, proline- and glutamine-rich"
FT /id="PRO_0000081909"
FT REPEAT 9..11
FT /note="1"
FT REPEAT 19..21
FT /note="2"
FT REPEAT 25..27
FT /note="3"
FT DOMAIN 297..369
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 371..452
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 9..27
FT /note="3 X 3 AA repeats of R-G-G"
FT REGION 579..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 497..596
FT /evidence="ECO:0000255, ECO:0000269|PubMed:25765647"
FT COMPBIAS 51..108
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..203
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..611
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 662..663
FT /note="Breakpoint for translocation to form SFPQ-TFE3"
FT MOD_RES 8
FT /note="Phosphoserine; by MKNK2"
FT /evidence="ECO:0000269|PubMed:17965020"
FT MOD_RES 9
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8VIJ6"
FT MOD_RES 9
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8VIJ6"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 208
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VIJ6"
FT MOD_RES 236
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 242
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 245
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 283
FT /note="Phosphoserine; by MKNK2"
FT /evidence="ECO:0000269|PubMed:17965020,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 293
FT /note="Phosphotyrosine; by ALK"
FT /evidence="ECO:0000269|PubMed:17537995"
FT MOD_RES 314
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000269|Ref.4"
FT MOD_RES 319
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 338
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 368
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 421
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 472
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 571
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000269|Ref.4"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 681
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:24129315"
FT MOD_RES 687
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:20932480,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 691
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 693
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000269|Ref.4"
FT MOD_RES 693
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 695
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 271
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 279
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 338
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT VAR_SEQ 663..707
FT /note="RTERFGQGGAGPVGGQGPRGMGPGTPAGYGRGREEYEGPNKKPRF -> VRM
FT IDVG (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_005855"
FT MUTAGEN 535
FT /note="L->A: Impairs DNA binding and ability to mediate
FT transcriptional activation; when associated with A-539; A-
FT 546 and A-549."
FT /evidence="ECO:0000269|PubMed:25765647"
FT MUTAGEN 539
FT /note="L->A: Impairs DNA binding and ability to mediate
FT transcriptional activation; when associated with A-535; A-
FT 546 and A-549."
FT /evidence="ECO:0000269|PubMed:25765647"
FT MUTAGEN 546
FT /note="L->A: Impairs DNA binding and ability to mediate
FT transcriptional activation; when associated with A-535; A-
FT 539 and A-549."
FT /evidence="ECO:0000269|PubMed:25765647"
FT MUTAGEN 549
FT /note="M->A: Impairs DNA binding and ability to mediate
FT transcriptional activation; when associated with A-535; A-
FT 539 and A-546."
FT /evidence="ECO:0000269|PubMed:25765647"
FT MUTAGEN 687
FT /note="T->A: Abolishes phosphorylation by GSK3B. Impairs
FT interaction with THRAP3."
FT /evidence="ECO:0000269|PubMed:20932480"
FT MUTAGEN 687
FT /note="T->D: No effect on interaction with THRAP3
FT (phosphomimetic)."
FT /evidence="ECO:0000269|PubMed:20932480"
FT CONFLICT 243
FT /note="G -> R (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:7LRU"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:6OWJ"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:7LRU"
FT STRAND 298..303
FT /evidence="ECO:0007829|PDB:7LRU"
FT HELIX 310..316
FT /evidence="ECO:0007829|PDB:7LRU"
FT HELIX 317..320
FT /evidence="ECO:0007829|PDB:7LRU"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:7LRU"
FT TURN 330..333
FT /evidence="ECO:0007829|PDB:7LRU"
FT STRAND 334..338
FT /evidence="ECO:0007829|PDB:7LRU"
FT HELIX 342..352
FT /evidence="ECO:0007829|PDB:7LRU"
FT STRAND 356..361
FT /evidence="ECO:0007829|PDB:4WII"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:7LRU"
FT STRAND 372..376
FT /evidence="ECO:0007829|PDB:7LRU"
FT HELIX 384..391
FT /evidence="ECO:0007829|PDB:7LRU"
FT TURN 392..394
FT /evidence="ECO:0007829|PDB:7LRU"
FT STRAND 397..404
FT /evidence="ECO:0007829|PDB:7LRU"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:7LRQ"
FT STRAND 410..420
FT /evidence="ECO:0007829|PDB:7LRU"
FT HELIX 421..433
FT /evidence="ECO:0007829|PDB:7LRU"
FT STRAND 437..441
FT /evidence="ECO:0007829|PDB:7LRU"
FT STRAND 446..449
FT /evidence="ECO:0007829|PDB:7LRU"
FT STRAND 455..457
FT /evidence="ECO:0007829|PDB:6NCQ"
FT HELIX 461..464
FT /evidence="ECO:0007829|PDB:6NCQ"
FT STRAND 467..469
FT /evidence="ECO:0007829|PDB:6NCQ"
FT HELIX 470..474
FT /evidence="ECO:0007829|PDB:6NCQ"
FT STRAND 478..480
FT /evidence="ECO:0007829|PDB:6OWJ"
FT HELIX 486..493
FT /evidence="ECO:0007829|PDB:4WIJ"
FT HELIX 505..530
FT /evidence="ECO:0007829|PDB:7LRU"
FT TURN 531..533
FT /evidence="ECO:0007829|PDB:7LRU"
FT HELIX 555..588
FT /evidence="ECO:0007829|PDB:4WIJ"
SQ SEQUENCE 707 AA; 76149 MW; 6D8D5EA95E235847 CRC64;
MSRDRFRSRG GGGGGFHRRG GGGGRGGLHD FRSPPPGMGL NQNRGPMGPG PGQSGPKPPI
PPPPPHQQQQ QPPPQQPPPQ QPPPHQPPPH PQPHQQQQPP PPPQDSSKPV VAQGPGPAPG
VGSAPPASSS APPATPPTSG APPGSGPGPT PTPPPAVTSA PPGAPPPTPP SSGVPTTPPQ
AGGPPPPPAA VPGPGPGPKQ GPGPGGPKGG KMPGGPKPGG GPGLSTPGGH PKPPHRGGGE
PRGGRQHHPP YHQQHHQGPP PGGPGGRSEE KISDSEGFKA NLSLLRRPGE KTYTQRCRLF
VGNLPADITE DEFKRLFAKY GEPGEVFINK GKGFGFIKLE SRALAEIAKA ELDDTPMRGR
QLRVRFATHA AALSVRNLSP YVSNELLEEA FSQFGPIERA VVIVDDRGRS TGKGIVEFAS
KPAARKAFER CSEGVFLLTT TPRPVIVEPL EQLDDEDGLP EKLAQKNPMY QKERETPPRF
AQHGTFEYEY SQRWKSLDEM EKQQREQVEK NMKDAKDKLE SEMEDAYHEH QANLLRQDLM
RRQEELRRME ELHNQEMQKR KEMQLRQEEE RRRREEEMMI RQREMEEQMR RQREESYSRM
GYMDPRERDM RMGGGGAMNM GDPYGSGGQK FPPLGGGGGI GYEANPGVPP ATMSGSMMGS
DMRTERFGQG GAGPVGGQGP RGMGPGTPAG YGRGREEYEG PNKKPRF
