P23246 (SFPQ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	SFPQ
Synonyms:	PSF

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	707 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	DNA- and RNA binding protein, involved in several nuclear processes. Essential pre-mRNA splicing factor required early in spliceosome formation and for splicing catalytic step II, probably as a heteromer with NONO. Binds to pre-mRNA in spliceosome C complex, and specifically binds to intronic polypyrimidine tracts. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45, a phosphorylated form is sequestered by THRAP3 from the pre-mRNA in resting T-cells; T-cell activation and subsequent reduced phosphorylation is proposed to lead to release from THRAP3 allowing binding to pre-mRNA splicing regulatotry elements which represses exon inclusion. Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b. May be involved in a pre-mRNA coupled splicing and polyadenylation process as component of a snRNP-free complex with SNRPA/U1A. The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs. SFPQ may be involved in homologous DNA pairing; in vitro, promotes the invasion of ssDNA between a duplex DNA and produces a D-loop formation. The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1; in vitro, stimulates dissociation of TOP1 from DNA after cleavage and enhances its jumping between separate DNA helices. The SFPQ-NONO heteromer may be involved in DNA nonhomologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends; in vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex. SFPQ is involved in transcriptional regulation. Transcriptional repression is probably mediated by an interaction of SFPQ with SIN3A and subsequent recruitment of histone deacetylases (HDACs). The SFPQ-NONO/SF-1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional avtivity. SFPQ isoform Long binds to the DNA binding domains (DBD) of nuclear hormone receptors, like RXRA and probably THRA, and acts as transcriptional corepressor in absence of hormone ligands. Binds the DNA sequence 5'-CTGAGTC-3' in the insulin-like growth factor response element (IGFRE) and inhibits IGF-I-stimulated transcriptional activity. Ref.1 Ref.11 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.22 Ref.31
Subunit structure	Monomer and component of the SFPQ-NONO complex, which is probably a heterotetramer of two 52 kDa (NONO) and two 100 kDa (SFPQ) subunits. SFPQ is a component of spliceosome and U5.4/6 snRNP complexes. Interacts with SNRPA/U1A. Component of a snRNP-free complex with SNRPA/U1A. Part of complex consisting of SFPQ, NONO and MATR3. Interacts with polypyrimidine tract-binding protein 1/PTB. Part of a complex consisting of SFPQ, NONO and NR5A1. Interacts with RXRA, probably THRA, and SIN3A. Interacts with TOP1. Part of a complex consisting of SFPQ, NONO and TOP1. Interacts with SNRNP70 in apoptotic cells. Interacts with PSPC1. Interacts with RNF43. Interacts with PITX3 and NR4A2/NURR1. Interacts with PTK6. Interacts with THRAP3; the interaction is dependent on SFPQ phosphorylation at 'Thr-687' and inhibits binding of SFPQ to a ESS1 exonic splicing silencer element-containing RNA. Ref.5 Ref.6 Ref.9 Ref.10 Ref.11 Ref.13 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.27 Ref.28 Ref.31
Subcellular location	Nucleus matrix. Cytoplasm. Note: Predominantly in nuclear matrix. Ref.9 Ref.10 Ref.28
Post-translational modification	The N-terminus is blocked. Phosphorylated on multiple serine and threonine residues during apoptosis. In vitro phosphorylated by PKC. Phosphorylation stimulates binding to DNA and D-loop formation, but inhibits binding to RNA. Phosphorylation of C-terminal tyrosines promotes its cytoplasmic localization, impaired its binding to polypyrimidine RNA and led to cell cycle arrest. In resting T-cells is phosphorylated at Thr-687 by GSK3B which is proposed to promote association with THRAP and to prevent binding to PTPRC/CD45 pre-mRNA; T-cell activation leads to reduced phosphorylation at Thr-687. Ref.16 Ref.18 Ref.23 Ref.24 Ref.28 Ref.31 Arg-7, Arg-9, Arg-19 and Arg-25 are dimethylated, probably to asymmetric dimethylarginine. Ref.4
Involvement in disease	A chromosomal aberration involving SFPQ may be a cause of papillary renal cell carcinoma (PRCC). Translocation t(X;1)(p11.2;p34) with TFE3.
Sequence similarities	Contains 2 RRM (RNA recognition motif) domains.
Caution	Was originally (Ref.8) thought to be myoblast cell surface antigen 24.1D5 and a possible membrane-bound protein ectokinase.

Ontologies

Keywords
Biological process	DNA damage DNA recombination DNA repair Transcription Transcription regulation mRNA processing mRNA splicing
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement
Domain	Repeat
Ligand	DNA-binding RNA-binding
Molecular function	Activator Repressor
PTM	Acetylation Methylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA recombination Inferred from electronic annotation. Source: UniProtKB-KW DNA repair Inferred from electronic annotation. Source: UniProtKB-KW alternative mRNA splicing, via spliceosome Inferred from mutant phenotype PubMed 19874820. Source: BHF-UCL negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 22783022. Source: BHF-UCL transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear matrix Inferred from direct assay PubMed 19874820. Source: BHF-UCL paraspeckles Inferred from direct assay PubMed 19874820. Source: BHF-UCL
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PTBP1	P26599	2	EBI-355453,EBI-350540
Rxra	P28700	3	EBI-355463,EBI-346715	From a different organism.
SIN3A	Q96ST3	2	EBI-355453,EBI-347218
SNRPA	P09012	4	EBI-355453,EBI-607085
THRA	P04625	2	EBI-355463,EBI-286261	From a different organism.
THRAP3	Q9Y2W1	6	EBI-355453,EBI-352039

Alternative products

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

Note: Additional isoforms seem to exist.

Isoform Long (identifier: P23246-1)

Also known as: A;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Short (identifier: P23246-2)

Also known as: F;

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 707	707	Splicing factor, proline- and glutamine-rich		PRO_0000081909
Regions
	Repeat	9 – 11	3	1
	Repeat	19 – 21	3	2
	Repeat	25 – 27	3	3
	Domain	297 – 369	73	RRM 1
	Domain	371 – 452	82	RRM 2
	Region	9 – 27	19	3 X 3 AA repeats of R-G-G
	Compositional bias	10 – 266	257	Gln/Glu/Pro-rich
	Compositional bias	10 – 15	6	Poly-Gly
	Compositional bias	20 – 27	8	Poly-Gly
	Compositional bias	56 – 65	10	Poly-Pro
	Compositional bias	67 – 71	5	Poly-Gln
	Compositional bias	95 – 98	4	Poly-Gln
	Compositional bias	99 – 103	5	Poly-Pro
	Compositional bias	184 – 188	5	Poly-Pro
	Compositional bias	571 – 574	4	Poly-Arg
	Compositional bias	613 – 616	4	Poly-Gly
	Compositional bias	635 – 641	7	Poly-Gly
Sites
	Site	662 – 663	2	Breakpoint for translocation to form SFPQ-TFE3
Amino acid modifications
	Modified residue	8	1	Phosphoserine; by MKNK2 Ref.24
	Modified residue	33	1	Phosphoserine Ref.32 Ref.34
	Modified residue	273	1	Phosphoserine Ref.26 Ref.34
	Modified residue	283	1	Phosphoserine; by MKNK2 Ref.24 Ref.34
	Modified residue	293	1	Phosphotyrosine; by ALK Ref.23
	Modified residue	314	1	N6,N6-dimethyllysine Ref.4
	Modified residue	319	1	N6-acetyllysine Ref.30
	Modified residue	338	1	N6-acetyllysine Ref.30
	Modified residue	379	1	Phosphoserine Ref.29
	Modified residue	421	1	N6-acetyllysine Ref.30
	Modified residue	472	1	N6-acetyllysine Ref.30
	Modified residue	571	1	Dimethylated arginine Ref.4
	Modified residue	626	1	Phosphoserine Ref.32
	Modified residue	681	1	Omega-N-methylarginine Ref.4
	Modified residue	687	1	Phosphothreonine Ref.25 Ref.26 Ref.31
	Modified residue	693	1	Dimethylated arginine Ref.4
Natural variations
	Alternative sequence	663 – 707	45	RTERF…KKPRF → VRMIDVG in isoform Short.		VSP_005855
Experimental info
	Mutagenesis	687	1	T → A: Abolishes phosphorylation by GSK3B. Impairs interaction with THRAP3. Ref.31
	Mutagenesis	687	1	T → D: No effect on interaction with THRAP3 (phosphomimetic). Ref.31
	Sequence conflict	243	1	G → R AA sequence Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long (A) [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 6D8D5EA95E235847	FASTA	707	76,149
	10 20 30 40 50 60 MSRDRFRSRG GGGGGFHRRG GGGGRGGLHD FRSPPPGMGL NQNRGPMGPG PGQSGPKPPI 70 80 90 100 110 120 PPPPPHQQQQ QPPPQQPPPQ QPPPHQPPPH PQPHQQQQPP PPPQDSSKPV VAQGPGPAPG 130 140 150 160 170 180 VGSAPPASSS APPATPPTSG APPGSGPGPT PTPPPAVTSA PPGAPPPTPP SSGVPTTPPQ 190 200 210 220 230 240 AGGPPPPPAA VPGPGPGPKQ GPGPGGPKGG KMPGGPKPGG GPGLSTPGGH PKPPHRGGGE 250 260 270 280 290 300 PRGGRQHHPP YHQQHHQGPP PGGPGGRSEE KISDSEGFKA NLSLLRRPGE KTYTQRCRLF 310 320 330 340 350 360 VGNLPADITE DEFKRLFAKY GEPGEVFINK GKGFGFIKLE SRALAEIAKA ELDDTPMRGR 370 380 390 400 410 420 QLRVRFATHA AALSVRNLSP YVSNELLEEA FSQFGPIERA VVIVDDRGRS TGKGIVEFAS 430 440 450 460 470 480 KPAARKAFER CSEGVFLLTT TPRPVIVEPL EQLDDEDGLP EKLAQKNPMY QKERETPPRF 490 500 510 520 530 540 AQHGTFEYEY SQRWKSLDEM EKQQREQVEK NMKDAKDKLE SEMEDAYHEH QANLLRQDLM 550 560 570 580 590 600 RRQEELRRME ELHNQEMQKR KEMQLRQEEE RRRREEEMMI RQREMEEQMR RQREESYSRM 610 620 630 640 650 660 GYMDPRERDM RMGGGGAMNM GDPYGSGGQK FPPLGGGGGI GYEANPGVPP ATMSGSMMGS 670 680 690 700 DMRTERFGQG GAGPVGGQGP RGMGPGTPAG YGRGREEYEG PNKKPRF
	Isoform Short (F) [UniParc]. Checksum: 46BAE5D117400578	FASTA	669	72,263
	10 20 30 40 50 60 MSRDRFRSRG GGGGGFHRRG GGGGRGGLHD FRSPPPGMGL NQNRGPMGPG PGQSGPKPPI 70 80 90 100 110 120 PPPPPHQQQQ QPPPQQPPPQ QPPPHQPPPH PQPHQQQQPP PPPQDSSKPV VAQGPGPAPG 130 140 150 160 170 180 VGSAPPASSS APPATPPTSG APPGSGPGPT PTPPPAVTSA PPGAPPPTPP SSGVPTTPPQ 190 200 210 220 230 240 AGGPPPPPAA VPGPGPGPKQ GPGPGGPKGG KMPGGPKPGG GPGLSTPGGH PKPPHRGGGE 250 260 270 280 290 300 PRGGRQHHPP YHQQHHQGPP PGGPGGRSEE KISDSEGFKA NLSLLRRPGE KTYTQRCRLF 310 320 330 340 350 360 VGNLPADITE DEFKRLFAKY GEPGEVFINK GKGFGFIKLE SRALAEIAKA ELDDTPMRGR 370 380 390 400 410 420 QLRVRFATHA AALSVRNLSP YVSNELLEEA FSQFGPIERA VVIVDDRGRS TGKGIVEFAS 430 440 450 460 470 480 KPAARKAFER CSEGVFLLTT TPRPVIVEPL EQLDDEDGLP EKLAQKNPMY QKERETPPRF 490 500 510 520 530 540 AQHGTFEYEY SQRWKSLDEM EKQQREQVEK NMKDAKDKLE SEMEDAYHEH QANLLRQDLM 550 560 570 580 590 600 RRQEELRRME ELHNQEMQKR KEMQLRQEEE RRRREEEMMI RQREMEEQMR RQREESYSRM 610 620 630 640 650 660 GYMDPRERDM RMGGGGAMNM GDPYGSGGQK FPPLGGGGGI GYEANPGVPP ATMSGSMMGS DMVRMIDVG

References

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[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]	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 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, 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, MASS SPECTROMETRY. Tissue: Fetal brain cortex.
[8]	"Cloning and characterization of a myoblast cell surface antigen defined by 24.1D5 monoclonal antibody." Gower H.J., Moore S.E., Dickson G., Elsom V.L., Nayak R., Walsh F.S. Development 105:723-731(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 312-707. Tissue: Fetal skeletal muscle.
[9]	"The snRNP-free U1A (SF-A) complex(es): identification of the largest subunit as PSF, the polypyrimidine-tract binding protein-associated splicing factor." Lutz C.S., Cooke C., O'Connor J.P., Kobayashi R., Alwine J.C. RNA 4:1493-1499(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 414-421 AND 427-448, SUBCELLULAR LOCATION, INTERACTION WITH SNRPA, IDENTIFICATION IN A SNRNP-FREE COMPLEX WITH SNRPA.
[10]	"Differential nuclear localization and nuclear matrix association of the splicing factors PSF and PTB." Meissner M., Dechat T., Gerner C., Grimm R., Foisner R., Sauermann G. J. Cell. Biochem. 76:559-566(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 600-606 AND 667-677, INTERACTION WITH PTBP1, SUBCELLULAR LOCATION.
[11]	"A novel set of spliceosome-associated proteins and the essential splicing factor PSF bind stably to pre-mRNA prior to catalytic step II of the splicing reaction." Gozani O., Patton J.G., Reed R. EMBO J. 13:3356-3367(1994) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PRE-MRNA, IDENTIFICATION IN SPLICEOSOME COMPLEX.
[12]	"Fusion of splicing factor genes PSF and NonO (p54nrb) to the TFE3 gene in papillary renal cell carcinoma." Clark J., Lu Y.-J., Sidhar S.K., Parker C., Gill S., Smedley D., Hamoudi R., Linehan W.M., Shipley J., Cooper C.S. Oncogene 15:2233-2239(1997) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH TFE3.
[13]	"The RNA-splicing factor PSF/p54 controls DNA-topoisomerase I activity by a direct interaction." Straub T., Grue P., Uhse A., Lisby M., Knudsen B.R., Tange T.O., Westergaard O., Boege F. J. Biol. Chem. 273:26261-26264(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TOP1, IDENTIFICATION IN A COMPLEX WITH NONO AND TOP1.
[14]	"PSF/p54(nrb) stimulates 'jumping' of DNA topoisomerase I between separate DNA helices." Straub T., Knudsen B.R., Boege F. Biochemistry 39:7552-7558(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN DNA UNWINDING.
[15]	"Polypyrimidine tract-binding protein-associated splicing factor is a negative regulator of transcriptional activity of the porcine p450scc insulin-like growth factor response element." Urban R.J., Bodenburg Y., Kurosky A., Wood T.G., Gasic S. Mol. Endocrinol. 14:774-782(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN TRANSCRIPTION REGULATION, IDENTIFICATION BY MASS SPECTROMETRY.
[16]	"Human 100-kDa homologous DNA-pairing protein is the splicing factor PSF and promotes DNA strand invasion." Akhmedov A.T., Lopez B.S. Nucleic Acids Res. 28:3022-3030(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN HOMOLOGOUS DNA PAIRING, PHOSPHORYLATION.
[17]	"The fate of dsRNA in the nucleus: a p54(nrb)-containing complex mediates the nuclear retention of promiscuously A-to-I edited RNAs." Zhang Z., Carmichael G.G. Cell 106:465-475(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN NUCLEAR RETENTION OF A-TO-I EDITED RNAS, IDENTIFICATION IN A COMPLEX WITH NONO AND MATR3.
[18]	"Nuclear relocalization of the pre-mRNA splicing factor PSF during apoptosis involves hyperphosphorylation, masking of antigenic epitopes, and changes in protein interactions." Shav-Tal Y., Cohen M., Lapter S., Dye B., Patton J.G., Vandekerckhove J., Zipori D. Mol. Biol. Cell 12:2328-2340(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SNRNP70, PHOSPHORYLATION.
[19]	"PSF is a novel corepressor that mediates its effect through Sin3A and the DNA binding domain of nuclear hormone receptors." Mathur M., Tucker P.W., Samuels H.H. Mol. Cell. Biol. 21:2298-2311(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN TRANSCRIPTION REGULATION, INTERACTION WITH RXRA; THRA AND SIN3A.
[20]	"Transcriptional activation of human CYP17 in H295R adrenocortical cells depends on complex formation among p54(nrb)/NonO, protein-associated splicing factor, and SF-1, a complex that also participates in repression of transcription." Sewer M.B., Nguyen V.Q., Huang C.J., Tucker P.W., Kagawa N., Waterman M.R. Endocrinology 143:1280-1290(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN TRANSCRIPTION REGULATION, INTERACTION WITH NR5A1 AND SIN3A, IDENTIFICATION IN A COMPLEX WITH NONO AND NR5A1.
[21]	"PSF and p54nrb bind a conserved stem in U5 snRNA." Peng R., Dye B.T., Perez I., Barnard D.C., Thompson A.B., Patton J.G. RNA 8:1334-1347(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NONO AND U5 SNRNA, IDENTIFICATION IN IN U5/4/6 SNRNP SND SPLICEOSOME COMPLEXES.
[22]	"Identification of the polypyrimidine tract binding protein-associated splicing factor.p54(nrb) complex as a candidate DNA double-strand break rejoining factor." Bladen C.L., Udayakumar D., Takeda Y., Dynan W.S. J. Biol. Chem. 280:5205-5210(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN DNA REPAIR, IDENTIFICATION BY MASS SPECTROMETRY, DNA-BINDING, SUBUNIT.
[23]	"NPM/ALK binds and phosphorylates the RNA/DNA-binding protein PSF in anaplastic large-cell lymphoma." Galietta A., Gunby R.H., Redaelli S., Stano P., Carniti C., Bachi A., Tucker P.W., Tartari C.J., Huang C.J., Colombo E., Pulford K., Puttini M., Piazza R.G., Ruchatz H., Villa A., Donella-Deana A., Marin O., Perrotti D., Gambacorti-Passerini C. Blood 110:2600-2609(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-293.
[24]	"The PSF.p54nrb complex is a novel Mnk substrate that binds the mRNA for tumor necrosis factor alpha." Buxade M., Morrice N., Krebs D.L., Proud C.G. J. Biol. Chem. 283:57-65(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-8 AND SER-283 BY MKNK2.
[25]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-687, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[26]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273 AND THR-687, MASS SPECTROMETRY. 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]	"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.
[29]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[30]	"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, MASS SPECTROMETRY.
[31]	"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.
[32]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[33]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[34]	"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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	X70944 mRNA. Translation: CAA50283.1. AL590434 Genomic DNA. Translation: CAI12467.1. CH471059 Genomic DNA. Translation: EAX07426.1. X16850 mRNA. Translation: CAA34747.1.
IPI	IPI00010740. IPI00216613.
PIR	A46302. S29770.
RefSeq	NP_005057.1. NM_005066.2.
UniGene	Hs.355934. Hs.611911.
3D structure databases
ProteinModelPortal	P23246.
ModBase	Search...
Protein-protein interaction databases
IntAct	P23246. 41 interactions.
MINT	MINT-1141893.
STRING	9606.ENSP00000349748.
PTM databases
PhosphoSite	P23246.
Polymorphism databases
DMDM	1709851.
2D gel databases
SWISS-2DPAGE	P23246.
Proteomic databases
PaxDb	P23246.
PeptideAtlas	P23246.
PRIDE	P23246.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000357214; ENSP00000349748; ENSG00000116560.
GeneID	6421.
KEGG	hsa:6421.
UCSC	uc001bys.3. human.
Organism-specific databases
CTD	6421.
GeneCards	GC01M035641.
HGNC	HGNC:10774. SFPQ.
HPA	CAB009886.
MIM	605199. gene.
neXtProt	NX_P23246.
PharmGKB	PA35690.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG298586.
HOGENOM	HOG000231095.
HOVERGEN	HBG009801.
InParanoid	P23246.
KO	K13219.
OMA	APGGHPK.
OrthoDB	EOG4RNB8S.
PhylomeDB	P23246.
Gene expression databases
ArrayExpress	P23246.
Bgee	P23246.
CleanEx	HS_SFPQ.
Genevestigator	P23246.
GermOnline	ENSG00000116560. Homo sapiens.
Family and domain databases
Gene3D	3.30.70.330. 2 hits.
InterPro	IPR012975. NOPS. IPR012677. Nucleotide-bd_a/b_plait. IPR000504. RRM_dom. [Graphical view]
Pfam	PF08075. NOPS. 1 hit. PF00076. RRM_1. 2 hits. [Graphical view]
SMART	SM00360. RRM. 2 hits. [Graphical view]
PROSITE	PS50102. RRM. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SFPQ. human.
GenomeRNAi	6421.
NextBio	24935.
SOURCE	Search...

Entry information

Entry name

SFPQ_HUMAN

Accession

Primary (citable) accession number: P23246
Secondary accession number(s): P30808, Q5SZ71

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 153 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.