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Splicing factor, proline- and glutamine-rich (100 kDa DNA-pairing protein) (hPOMp100) (DNA-binding p52/p100 complex, 100 kDa subunit) (Polypyrimidine tract-binding protein-associated-splicing factor) (PSF) (PTB-associated-splicing factor)

 SFPQ_HUMAN              Reviewed;         707 AA.
P23246; P30808; Q5SZ71;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
25-OCT-2017, entry version 200.
RecName: Full=Splicing factor, proline- and glutamine-rich;
AltName: Full=100 kDa DNA-pairing protein;
Short=hPOMp100;
AltName: Full=DNA-binding p52/p100 complex, 100 kDa subunit;
AltName: Full=Polypyrimidine tract-binding protein-associated-splicing factor {ECO:0000303|PubMed:9848648};
Short=PSF {ECO:0000303|PubMed:8449401};
Short=PTB-associated-splicing factor;
Name=SFPQ; Synonyms=PSF;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, ALTERNATIVE
SPLICING, AND FUNCTION.
TISSUE=Fetal brain;
PubMed=8449401; DOI=10.1101/gad.7.3.393;
Patton J.G., Porro E.B., Galceran J., Tempst P., Nadal-Ginard B.;
"Cloning and characterization of PSF, a novel pre-mRNA splicing
factor.";
Genes Dev. 7:393-406(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
PROTEIN SEQUENCE OF 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, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[5]
PROTEIN SEQUENCE OF 48-68 AND 213-246, BLOCKAGE OF N-TERMINUS,
DNA-BINDING, AND SUBUNIT.
PubMed=8439294; DOI=10.1042/bj2900267;
Zhang W.-W., Zhang L.-X., Busch R.K., Farres J., Busch H.;
"Purification and characterization of a DNA-binding heterodimer of 52
and 100 kDa from HeLa cells.";
Biochem. J. 290:267-272(1993).
[6]
PROTEIN SEQUENCE OF 292-311; 415-421 AND 503-510, AND IDENTIFICATION
IN U5/4/6 SNRNP COMPLEXES.
PubMed=9409622;
Teigelkamp S., Mundt C., Achsel T., Will C.L., Luehrmann R.;
"The human U5 snRNP-specific 100-kD protein is an RS domain-
containing, putative RNA helicase with significant homology to the
yeast splicing factor Prp28p.";
RNA 3:1313-1326(1997).
[7]
PROTEIN SEQUENCE OF 299-314 AND 480-493, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 312-707.
TISSUE=Fetal skeletal muscle;
PubMed=2480877;
Gower H.J., Moore S.E., Dickson G., Elsom V.L., Nayak R., Walsh F.S.;
"Cloning and characterization of a myoblast cell surface antigen
defined by 24.1D5 monoclonal antibody.";
Development 105:723-731(1989).
[9]
PROTEIN SEQUENCE OF 414-421 AND 427-448, SUBCELLULAR LOCATION,
INTERACTION WITH SNRPA, AND IDENTIFICATION IN A SNRNP-FREE COMPLEX
WITH SNRPA.
PubMed=9848648; DOI=10.1017/S1355838298981183;
Lutz C.S., Cooke C., O'Connor J.P., Kobayashi R., Alwine J.C.;
"The snRNP-free U1A (SF-A) complex(es): identification of the largest
subunit as PSF, the polypyrimidine-tract binding protein-associated
splicing factor.";
RNA 4:1493-1499(1998).
[10]
PROTEIN SEQUENCE OF 600-606 AND 667-677, INTERACTION WITH PTBP1, AND
SUBCELLULAR LOCATION.
PubMed=10653975;
DOI=10.1002/(SICI)1097-4644(20000315)76:4<559::AID-JCB4>3.0.CO;2-U;
Meissner M., Dechat T., Gerner C., Grimm R., Foisner R., Sauermann G.;
"Differential nuclear localization and nuclear matrix association of
the splicing factors PSF and PTB.";
J. Cell. Biochem. 76:559-566(2000).
[11]
FUNCTION, INTERACTION WITH PRE-MRNA, AND IDENTIFICATION IN SPLICEOSOME
COMPLEX.
PubMed=8045264;
Gozani O., Patton J.G., Reed R.;
"A novel set of spliceosome-associated proteins and the essential
splicing factor PSF bind stably to pre-mRNA prior to catalytic step II
of the splicing reaction.";
EMBO J. 13:3356-3367(1994).
[12]
CHROMOSOMAL TRANSLOCATION WITH TFE3.
PubMed=9393982; DOI=10.1038/sj.onc.1201394;
Clark J., Lu Y.-J., Sidhar S.K., Parker C., Gill S., Smedley D.,
Hamoudi R., Linehan W.M., Shipley J., Cooper C.S.;
"Fusion of splicing factor genes PSF and NonO (p54nrb) to the TFE3
gene in papillary renal cell carcinoma.";
Oncogene 15:2233-2239(1997).
[13]
INTERACTION WITH TOP1, AND IDENTIFICATION IN A COMPLEX WITH NONO AND
TOP1.
PubMed=9756848; DOI=10.1074/jbc.273.41.26261;
Straub T., Grue P., Uhse A., Lisby M., Knudsen B.R., Tange T.O.,
Westergaard O., Boege F.;
"The RNA-splicing factor PSF/p54 controls DNA-topoisomerase I activity
by a direct interaction.";
J. Biol. Chem. 273:26261-26264(1998).
[14]
FUNCTION IN DNA UNWINDING.
PubMed=10858305; DOI=10.1021/bi992898e;
Straub T., Knudsen B.R., Boege F.;
"PSF/p54(nrb) stimulates 'jumping' of DNA topoisomerase I between
separate DNA helices.";
Biochemistry 39:7552-7558(2000).
[15]
FUNCTION IN TRANSCRIPTION REGULATION, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=10847580; DOI=10.1210/mend.14.6.0485;
Urban R.J., Bodenburg Y., Kurosky A., Wood T.G., Gasic S.;
"Polypyrimidine tract-binding protein-associated splicing factor is a
negative regulator of transcriptional activity of the porcine p450scc
insulin-like growth factor response element.";
Mol. Endocrinol. 14:774-782(2000).
[16]
FUNCTION IN HOMOLOGOUS DNA PAIRING, AND PHOSPHORYLATION.
PubMed=10931916; DOI=10.1093/nar/28.16.3022;
Akhmedov A.T., Lopez B.S.;
"Human 100-kDa homologous DNA-pairing protein is the splicing factor
PSF and promotes DNA strand invasion.";
Nucleic Acids Res. 28:3022-3030(2000).
[17]
FUNCTION IN NUCLEAR RETENTION OF A-TO-I EDITED RNAS, AND
IDENTIFICATION IN A COMPLEX WITH NONO AND MATR3.
PubMed=11525732; DOI=10.1016/S0092-8674(01)00466-4;
Zhang Z., Carmichael G.G.;
"The fate of dsRNA in the nucleus: a p54(nrb)-containing complex
mediates the nuclear retention of promiscuously A-to-I edited RNAs.";
Cell 106:465-475(2001).
[18]
INTERACTION WITH SNRNP70, AND PHOSPHORYLATION.
PubMed=11514619; DOI=10.1091/mbc.12.8.2328;
Shav-Tal Y., Cohen M., Lapter S., Dye B., Patton J.G.,
Vandekerckhove J., Zipori D.;
"Nuclear relocalization of the pre-mRNA splicing factor PSF during
apoptosis involves hyperphosphorylation, masking of antigenic
epitopes, and changes in protein interactions.";
Mol. Biol. Cell 12:2328-2340(2001).
[19]
FUNCTION IN TRANSCRIPTION REGULATION, AND INTERACTION WITH RXRA; THRA
AND SIN3A.
PubMed=11259580; DOI=10.1128/MCB.21.7.2298-2311.2001;
Mathur M., Tucker P.W., Samuels H.H.;
"PSF is a novel corepressor that mediates its effect through Sin3A and
the DNA binding domain of nuclear hormone receptors.";
Mol. Cell. Biol. 21:2298-2311(2001).
[20]
FUNCTION IN TRANSCRIPTION REGULATION, INTERACTION WITH NR5A1 AND
SIN3A, AND IDENTIFICATION IN A COMPLEX WITH NONO AND NR5A1.
PubMed=11897684; DOI=10.1210/endo.143.4.8748;
Sewer M.B., Nguyen V.Q., Huang C.J., Tucker P.W., Kagawa N.,
Waterman M.R.;
"Transcriptional activation of human CYP17 in H295R adrenocortical
cells depends on complex formation among p54(nrb)/NonO, protein-
associated splicing factor, and SF-1, a complex that also participates
in repression of transcription.";
Endocrinology 143:1280-1290(2002).
[21]
INTERACTION WITH NONO AND U5 SNRNA, AND IDENTIFICATION IN U5/4/6 SNRNP
AND SPLICEOSOME COMPLEXES.
PubMed=12403470; DOI=10.1017/S1355838202022070;
Peng R., Dye B.T., Perez I., Barnard D.C., Thompson A.B., Patton J.G.;
"PSF and p54nrb bind a conserved stem in U5 snRNA.";
RNA 8:1334-1347(2002).
[22]
FUNCTION IN DNA REPAIR, IDENTIFICATION BY MASS SPECTROMETRY,
DNA-BINDING, AND SUBUNIT.
PubMed=15590677; DOI=10.1074/jbc.M412758200;
Bladen C.L., Udayakumar D., Takeda Y., Dynan W.S.;
"Identification of the polypyrimidine tract binding protein-associated
splicing factor.p54(nrb) complex as a candidate DNA double-strand
break rejoining factor.";
J. Biol. Chem. 280:5205-5210(2005).
[23]
PHOSPHORYLATION AT TYR-293.
PubMed=17537995; DOI=10.1182/blood-2006-01-028647;
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.;
"NPM/ALK binds and phosphorylates the RNA/DNA-binding protein PSF in
anaplastic large-cell lymphoma.";
Blood 110:2600-2609(2007).
[24]
PHOSPHORYLATION AT SER-8 AND SER-283 BY MKNK2.
PubMed=17965020; DOI=10.1074/jbc.M705286200;
Buxade M., Morrice N., Krebs D.L., Proud C.G.;
"The PSF.p54nrb complex is a novel Mnk substrate that binds the mRNA
for tumor necrosis factor alpha.";
J. Biol. Chem. 283:57-65(2008).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-687, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273 AND THR-687, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[27]
INTERACTION WITH RNF43.
PubMed=18655028; DOI=10.1002/pmic.200800083;
Miyamoto K., Sakurai H., Sugiura T.;
"Proteomic identification of a PSF/p54nrb heterodimer as RNF43
oncoprotein-interacting proteins.";
Proteomics 8:2907-2910(2008).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[29]
PHOSPHORYLATION, INTERACTION WITH PTK6, AND SUBCELLULAR LOCATION.
PubMed=19439179; DOI=10.1016/j.cellsig.2009.04.008;
Lukong K.E., Huot M.E., Richard S.;
"BRK phosphorylates PSF promoting its cytoplasmic localization and
cell cycle arrest.";
Cell. Signal. 21:1415-1422(2009).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[31]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-319; LYS-338; LYS-421 AND
LYS-472, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[32]
FUNCTION, PHOSPHORYLATION AT THR-687, INTERACTION WITH THRAP3, AND
MUTAGENESIS OF THR-687.
PubMed=20932480; DOI=10.1016/j.molcel.2010.09.013;
Heyd F., Lynch K.W.;
"Phosphorylation-dependent regulation of PSF by GSK3 controls CD45
alternative splicing.";
Mol. Cell 40:126-137(2010).
[33]
INTERACTION WITH M.TUBERCULOSIS RV3654C (MICROBIAL INFECTION).
PubMed=20454556; DOI=10.1371/journal.pone.0010474;
Danelishvili L., Yamazaki Y., Selker J., Bermudez L.E.;
"Secreted Mycobacterium tuberculosis Rv3654c and Rv3655c proteins
participate in the suppression of macrophage apoptosis.";
PLoS ONE 5:E10474-E10474(2010).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND SER-626, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[35]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[36]
INTERACTION WITH PQBP1.
PubMed=21933836; DOI=10.1093/hmg/ddr430;
Kunde S.A., Musante L., Grimme A., Fischer U., Mueller E.,
Wanker E.E., Kalscheuer V.M.;
"The X-chromosome-linked intellectual disability protein PQBP1 is a
component of neuronal RNA granules and regulates the appearance of
stress granules.";
Hum. Mol. Genet. 20:4916-4931(2011).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33; SER-273 AND SER-283,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33; SER-273; SER-283;
THR-368; SER-374; SER-496; SER-626; THR-687 AND TYR-691, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[39]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[40]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-236; ARG-242; ARG-245;
ARG-681; ARG-693 AND ARG-695, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[41]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-338, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[42]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-338, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[43]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[44]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PRKDC; XRCC5;
XRCC6; HEXIM1; NONO; PSPC1; RBM14 AND MATR3.
PubMed=28712728; DOI=10.1016/j.molcel.2017.06.020;
Morchikh M., Cribier A., Raffel R., Amraoui S., Cau J., Severac D.,
Dubois E., Schwartz O., Bennasser Y., Benkirane M.;
"HEXIM1 and NEAT1 Long non-coding RNA form a multi-subunit complex
that regulates DNA-mediated innate immune response.";
Mol. Cell 67:387-399(2017).
[45]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-271; LYS-279 AND LYS-338,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[46]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 276-535, COILED COIL,
SUBUNIT, INTERACTION WITH NONO, FUNCTION, DOMAIN, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF LEU-535; LEU-539; LEU-546 AND MET-549.
PubMed=25765647; DOI=10.1093/nar/gkv156;
Lee M., Sadowska A., Bekere I., Ho D., Gully B.S., Lu Y., Iyer K.S.,
Trewhella J., Fox A.H., Bond C.S.;
"The structure of human SFPQ reveals a coiled-coil mediated polymer
essential for functional aggregation in gene regulation.";
Nucleic Acids Res. 43:3826-3840(2015).
-!- 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 binds DNA (PubMed:25765647). The SFPQ-NONO heteromer may
be involved in DNA non-homologous end joining (NHEJ) required for
double-strand break repair and V(D)J recombination and may
stabilize paired DNA ends; in vitro, the complex strongly
stimulates DNA end joining, binds directly to the DNA substrates
and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to
establish a functional preligation complex. SFPQ is involved in
transcriptional regulation. Functions as transcriptional activator
(PubMed:25765647). Transcriptional repression is mediated by an
interaction of SFPQ with SIN3A and subsequent recruitment of
histone deacetylases (HDACs). The SFPQ-NONO-NR5A1 complex binds to
the CYP17 promoter and regulates basal and cAMP-dependent
transcriptional activity. SFPQ isoform Long binds to the DNA
binding domains (DBD) of nuclear hormone receptors, like RXRA and
probably THRA, and acts as transcriptional corepressor in absence
of hormone ligands. Binds the DNA sequence 5'-CTGAGTC-3' in the
insulin-like growth factor response element (IGFRE) and inhibits
IGF-I-stimulated transcriptional activity. 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 (By
similarity). Required for the assembly of nuclear speckles
(PubMed:25765647). Plays a role in the regulation of DNA virus-
mediated innate immune response by assembling into the HDP-RNP
complex, a complex that serves as a platform for IRF3
phosphorylation and subsequent innate immune response activation
through the cGAS-STING pathway (PubMed:28712728).
{ECO:0000250|UniProtKB:Q8VIJ6, ECO:0000269|PubMed:10847580,
ECO:0000269|PubMed:10858305, ECO:0000269|PubMed:10931916,
ECO:0000269|PubMed:11259580, ECO:0000269|PubMed:11525732,
ECO:0000269|PubMed:11897684, ECO:0000269|PubMed:15590677,
ECO:0000269|PubMed:20932480, ECO:0000269|PubMed:25765647,
ECO:0000269|PubMed:28712728, ECO:0000269|PubMed:8045264,
ECO:0000269|PubMed:8449401}.
-!- SUBUNIT: Heterodimer with NONO (PubMed:25765647). Monomer and
component of the SFPQ-NONO complex, which is probably a
heterotetramer of two 52 kDa (NONO) and two 100 kDa (SFPQ)
subunits (PubMed:8439294, PubMed:25765647). The coiled coil domain
mediates interaction with NONO, and can also mediate formation of
long, linear homooligomers (in vitro) (PubMed:25765647). SFPQ is a
component of spliceosome and U5.4/6 snRNP complexes
(PubMed:9409622, PubMed:8045264, PubMed:12403470). Interacts with
SNRPA/U1A (PubMed:9848648). Component of a snRNP-free complex with
SNRPA/U1A (PubMed:9848648). Part of complex consisting of SFPQ,
NONO and MATR3 (PubMed:11525732). Interacts with polypyrimidine
tract-binding protein 1/PTB (PubMed:10653975). Part of a complex
consisting of SFPQ, NONO and NR5A1 (PubMed:11897684). Interacts
with RXRA, probably THRA, and SIN3A (PubMed:11259580). Interacts
with TOP1 (PubMed:9756848). Part of a complex consisting of SFPQ,
NONO and TOP1 (PubMed:9756848). Interacts with SNRNP70 in
apoptotic cells (PubMed:11514619). Interacts with PSPC1. Interacts
with RNF43 (PubMed:18655028). Interacts with PITX3 and NR4A2/NURR1
(By similarity). Interacts with PTK6 (PubMed:19439179). 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 (PubMed:20932480). The
large PER complex involved in the histone deacetylation is
composed of at least HDAC1, PER2, SFPQ and SIN3A. Interacts with
PER1 and PER2 (By similarity). Interacts with PQBP1
(PubMed:21933836). {ECO:0000250|UniProtKB:Q8VIJ6,
ECO:0000269|PubMed:10653975, ECO:0000269|PubMed:11259580,
ECO:0000269|PubMed:11514619, ECO:0000269|PubMed:11525732,
ECO:0000269|PubMed:11897684, ECO:0000269|PubMed:12403470,
ECO:0000269|PubMed:15590677, ECO:0000269|PubMed:18655028,
ECO:0000269|PubMed:19439179, ECO:0000269|PubMed:20932480,
ECO:0000269|PubMed:21933836, ECO:0000269|PubMed:25765647,
ECO:0000269|PubMed:8045264, ECO:0000269|PubMed:8439294,
ECO:0000269|PubMed:9409622, ECO:0000269|PubMed:9756848,
ECO:0000269|PubMed:9848648}.
-!- SUBUNIT: (Microbial infection) Interacts with M.tuberculosis
protein Rv3654c, which probably leads to the cleavage of PSF,
diminishes the level of caspase-8 in macrophages and suppresses
macrophage apoptosis by blocking the extrinsic pathway. Part of
the HDP-RNP complex composed of at least HEXIM1, PRKDC, XRCC5,
XRCC6, paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3)
and NEAT1 RNA. {ECO:0000269|PubMed:20454556,
ECO:0000269|PubMed:28712728}.
-!- INTERACTION:
Q8AZK7:EBNA-LP (xeno); NbExp=2; IntAct=EBI-355453, EBI-1185167;
P41235:HNF4A; NbExp=2; IntAct=EBI-355453, EBI-1049011;
P26599:PTBP1; NbExp=2; IntAct=EBI-355453, EBI-350540;
Q13882:PTK6; NbExp=5; IntAct=EBI-355453, EBI-1383632;
P28700:Rxra (xeno); NbExp=3; IntAct=EBI-355463, EBI-346715;
Q96ST3:SIN3A; NbExp=2; IntAct=EBI-355453, EBI-347218;
P09012:SNRPA; NbExp=4; IntAct=EBI-355453, EBI-607085;
P04625:THRA (xeno); NbExp=2; IntAct=EBI-355463, EBI-286261;
Q9Y2W1:THRAP3; NbExp=6; IntAct=EBI-355453, EBI-352039;
-!- SUBCELLULAR LOCATION: Nucleus speckle
{ECO:0000269|PubMed:25765647}. Nucleus matrix
{ECO:0000269|PubMed:10653975, ECO:0000269|PubMed:19439179,
ECO:0000269|PubMed:9848648}. Cytoplasm
{ECO:0000269|PubMed:19439179}. Note=Predominantly in nuclear
matrix. {ECO:0000269|PubMed:19439179}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Additional isoforms seem to exist.;
Name=Long; Synonyms=A;
IsoId=P23246-1; Sequence=Displayed;
Name=Short; Synonyms=F;
IsoId=P23246-2; Sequence=VSP_005855;
-!- DOMAIN: The coiled coil domain mediates interaction with NONO, and
can also mediate formation of long, linear homooligomers (in
vitro). The coiled coil domain is required for optimal DNA
binding, and optimal transcription activation.
{ECO:0000269|PubMed:25765647}.
-!- PTM: The N-terminus is blocked.
-!- PTM: Phosphorylated on multiple serine and threonine residues
during apoptosis. In vitro phosphorylated by PKC. Phosphorylation
stimulates binding to DNA and D-loop formation, but inhibits
binding to RNA. 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. {ECO:0000269|PubMed:10931916,
ECO:0000269|PubMed:11514619, ECO:0000269|PubMed:17537995,
ECO:0000269|PubMed:17965020, ECO:0000269|PubMed:19439179,
ECO:0000269|PubMed:20932480}.
-!- DISEASE: Note=A chromosomal aberration involving SFPQ may be a
cause of papillary renal cell carcinoma (PRCC). Translocation
t(X;1)(p11.2;p34) with TFE3.
-!- CAUTION: Was originally thought to be myoblast cell surface
antigen 24.1D5 and a possible membrane-bound protein ectokinase.
{ECO:0000305|PubMed:2480877}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PSFID167.html";
-----------------------------------------------------------------------
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EMBL; X70944; CAA50283.1; -; mRNA.
EMBL; AL590434; CAI12467.1; -; Genomic_DNA.
EMBL; CH471059; EAX07426.1; -; Genomic_DNA.
EMBL; X16850; CAA34747.1; -; mRNA.
CCDS; CCDS388.1; -. [P23246-1]
PIR; A46302; A46302.
PIR; S29770; S29770.
RefSeq; NP_005057.1; NM_005066.2. [P23246-1]
RefSeq; XP_005271169.1; XM_005271112.4. [P23246-1]
RefSeq; XP_005271170.1; XM_005271113.4. [P23246-1]
RefSeq; XP_005271172.1; XM_005271115.4. [P23246-2]
RefSeq; XP_016857542.1; XM_017002053.1. [P23246-1]
RefSeq; XP_016857543.1; XM_017002054.1. [P23246-1]
UniGene; Hs.355934; -.
UniGene; Hs.611911; -.
PDB; 4WII; X-ray; 2.05 A; A/B=276-535.
PDB; 4WIJ; X-ray; 3.49 A; A/B=276-598.
PDB; 4WIK; X-ray; 3.00 A; A/B=369-598.
PDBsum; 4WII; -.
PDBsum; 4WIJ; -.
PDBsum; 4WIK; -.
ProteinModelPortal; P23246; -.
SMR; P23246; -.
BioGrid; 112319; 197.
CORUM; P23246; -.
DIP; DIP-31272N; -.
IntAct; P23246; 62.
MINT; MINT-1141893; -.
STRING; 9606.ENSP00000349748; -.
iPTMnet; P23246; -.
PhosphoSitePlus; P23246; -.
SwissPalm; P23246; -.
BioMuta; SFPQ; -.
DMDM; 1709851; -.
SWISS-2DPAGE; P23246; -.
EPD; P23246; -.
MaxQB; P23246; -.
PaxDb; P23246; -.
PeptideAtlas; P23246; -.
PRIDE; P23246; -.
Ensembl; ENST00000357214; ENSP00000349748; ENSG00000116560. [P23246-1]
GeneID; 6421; -.
KEGG; hsa:6421; -.
UCSC; uc001bys.4; human. [P23246-1]
CTD; 6421; -.
DisGeNET; 6421; -.
EuPathDB; HostDB:ENSG00000116560.10; -.
GeneCards; SFPQ; -.
HGNC; HGNC:10774; SFPQ.
HPA; CAB009886; -.
HPA; HPA047513; -.
HPA; HPA054689; -.
MalaCards; SFPQ; -.
MIM; 605199; gene.
neXtProt; NX_P23246; -.
OpenTargets; ENSG00000116560; -.
Orphanet; 319308; Translocation renal cell carcinoma.
PharmGKB; PA35690; -.
eggNOG; KOG0115; Eukaryota.
eggNOG; ENOG410XQA0; LUCA.
GeneTree; ENSGT00390000005004; -.
HOGENOM; HOG000231095; -.
HOVERGEN; HBG009801; -.
InParanoid; P23246; -.
KO; K13219; -.
OMA; AFERCTE; -.
OrthoDB; EOG091G09T7; -.
PhylomeDB; P23246; -.
TreeFam; TF315795; -.
Reactome; R-HSA-8849468; PTK6 Regulates Proteins Involved in RNA Processing.
SIGNOR; P23246; -.
ChiTaRS; SFPQ; human.
GeneWiki; SFPQ; -.
GenomeRNAi; 6421; -.
PRO; PR:P23246; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000116560; -.
CleanEx; HS_SFPQ; -.
ExpressionAtlas; P23246; baseline and differential.
Genevisible; P23246; HS.
GO; GO:0000785; C:chromatin; IDA:ParkinsonsUK-UCL.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL.
GO; GO:0016363; C:nuclear matrix; IDA:BHF-UCL.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:BHF-UCL.
GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
GO; GO:0042382; C:paraspeckles; IDA:UniProtKB.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; ISS:BHF-UCL.
GO; GO:0003682; F:chromatin binding; ISS:BHF-UCL.
GO; GO:0001047; F:core promoter binding; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; ISS:BHF-UCL.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:ParkinsonsUK-UCL.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0002218; P:activation of innate immune response; IDA:UniProtKB.
GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IMP:BHF-UCL.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:MGI.
GO; GO:0070932; P:histone H3 deacetylation; ISS:UniProtKB.
GO; GO:0006397; P:mRNA processing; TAS:ProtInc.
GO; GO:0042754; P:negative regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:ParkinsonsUK-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:1902177; P:positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
GO; GO:0045876; P:positive regulation of sister chromatid cohesion; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd12948; NOPS_PSF; 1.
CDD; cd12587; RRM1_PSF; 1.
InterPro; IPR012975; NOPS.
InterPro; IPR034526; PSF_NOPS.
InterPro; IPR034525; PSF_RRM1.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
Pfam; PF08075; NOPS; 1.
Pfam; PF00076; RRM_1; 2.
SMART; SM00360; RRM; 2.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50102; RRM; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
Biological rhythms; Chromosomal rearrangement; Coiled coil;
Complete proteome; Cytoplasm; Direct protein sequencing; DNA damage;
DNA recombination; DNA repair; DNA-binding; Immunity; Innate immunity;
Isopeptide bond; Methylation; mRNA processing; mRNA splicing; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Repressor; RNA-binding;
Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 707 Splicing factor, proline- and glutamine-
rich.
/FTId=PRO_0000081909.
REPEAT 9 11 1.
REPEAT 19 21 2.
REPEAT 25 27 3.
DOMAIN 297 369 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 371 452 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
REGION 9 27 3 X 3 AA repeats of R-G-G.
COILED 497 596 {ECO:0000255,
ECO:0000269|PubMed:25765647}.
COMPBIAS 10 266 Gln/Glu/Pro-rich.
COMPBIAS 10 15 Poly-Gly.
COMPBIAS 20 27 Poly-Gly.
COMPBIAS 56 65 Poly-Pro.
COMPBIAS 67 71 Poly-Gln.
COMPBIAS 95 98 Poly-Gln.
COMPBIAS 99 103 Poly-Pro.
COMPBIAS 184 188 Poly-Pro.
COMPBIAS 571 574 Poly-Arg.
COMPBIAS 613 616 Poly-Gly.
COMPBIAS 635 641 Poly-Gly.
SITE 662 663 Breakpoint for translocation to form
SFPQ-TFE3.
MOD_RES 8 8 Phosphoserine; by MKNK2.
{ECO:0000269|PubMed:17965020}.
MOD_RES 9 9 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:Q8VIJ6}.
MOD_RES 9 9 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:Q8VIJ6}.
MOD_RES 33 33 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 208 208 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8VIJ6}.
MOD_RES 236 236 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 242 242 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 245 245 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 273 273 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 283 283 Phosphoserine; by MKNK2.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:17965020}.
MOD_RES 293 293 Phosphotyrosine; by ALK.
{ECO:0000269|PubMed:17537995}.
MOD_RES 314 314 N6,N6-dimethyllysine.
{ECO:0000269|Ref.4}.
MOD_RES 319 319 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 338 338 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 368 368 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 374 374 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 379 379 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 421 421 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 472 472 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 496 496 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 571 571 Dimethylated arginine.
{ECO:0000269|Ref.4}.
MOD_RES 626 626 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 681 681 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315,
ECO:0000269|Ref.4}.
MOD_RES 687 687 Phosphothreonine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:20932480}.
MOD_RES 691 691 Phosphotyrosine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 693 693 Dimethylated arginine; alternate.
{ECO:0000269|Ref.4}.
MOD_RES 693 693 Omega-N-methylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 695 695 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
CROSSLNK 271 271 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 279 279 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 338 338 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 663 707 RTERFGQGGAGPVGGQGPRGMGPGTPAGYGRGREEYEGPNK
KPRF -> VRMIDVG (in isoform Short).
{ECO:0000305}.
/FTId=VSP_005855.
MUTAGEN 535 535 L->A: Impairs DNA binding and ability to
mediate transcriptional activation; when
associated with A-539; A-546 and A-549.
{ECO:0000269|PubMed:25765647}.
MUTAGEN 539 539 L->A: Impairs DNA binding and ability to
mediate transcriptional activation; when
associated with A-535; A-546 and A-549.
{ECO:0000269|PubMed:25765647}.
MUTAGEN 546 546 L->A: Impairs DNA binding and ability to
mediate transcriptional activation; when
associated with A-535; A-539 and A-549.
{ECO:0000269|PubMed:25765647}.
MUTAGEN 549 549 M->A: Impairs DNA binding and ability to
mediate transcriptional activation; when
associated with A-535; A-539 and A-546.
{ECO:0000269|PubMed:25765647}.
MUTAGEN 687 687 T->A: Abolishes phosphorylation by GSK3B.
Impairs interaction with THRAP3.
{ECO:0000269|PubMed:20932480}.
MUTAGEN 687 687 T->D: No effect on interaction with
THRAP3 (phosphomimetic).
{ECO:0000269|PubMed:20932480}.
CONFLICT 243 243 G -> R (in Ref. 5; AA sequence).
{ECO:0000305}.
HELIX 277 283 {ECO:0000244|PDB:4WII}.
HELIX 295 297 {ECO:0000244|PDB:4WII}.
STRAND 298 303 {ECO:0000244|PDB:4WII}.
HELIX 310 316 {ECO:0000244|PDB:4WII}.
HELIX 317 320 {ECO:0000244|PDB:4WII}.
STRAND 326 329 {ECO:0000244|PDB:4WII}.
TURN 330 333 {ECO:0000244|PDB:4WII}.
STRAND 334 338 {ECO:0000244|PDB:4WII}.
HELIX 342 352 {ECO:0000244|PDB:4WII}.
STRAND 356 361 {ECO:0000244|PDB:4WII}.
STRAND 363 366 {ECO:0000244|PDB:4WII}.
STRAND 370 377 {ECO:0000244|PDB:4WII}.
HELIX 384 391 {ECO:0000244|PDB:4WII}.
HELIX 392 394 {ECO:0000244|PDB:4WII}.
STRAND 397 404 {ECO:0000244|PDB:4WII}.
STRAND 406 408 {ECO:0000244|PDB:4WIJ}.
STRAND 410 420 {ECO:0000244|PDB:4WII}.
HELIX 421 433 {ECO:0000244|PDB:4WII}.
STRAND 439 441 {ECO:0000244|PDB:4WII}.
STRAND 446 449 {ECO:0000244|PDB:4WII}.
STRAND 454 457 {ECO:0000244|PDB:4WII}.
HELIX 461 464 {ECO:0000244|PDB:4WII}.
HELIX 468 473 {ECO:0000244|PDB:4WII}.
STRAND 478 480 {ECO:0000244|PDB:4WII}.
HELIX 486 526 {ECO:0000244|PDB:4WII}.
HELIX 555 588 {ECO:0000244|PDB:4WIJ}.
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


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