Reviewed, UniProtKB/Swiss-Prot P23246 (SFPQ_HUMAN)

Names and origin

Protein names

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

Gene names

Name:	SFPQ
Synonyms:	PSF

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	707 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 an heteromer with NONO. Binds to pre-mRNA in spliceosome C complex, and specifically binds to intronic polypyrimidine tracts. 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.23
Subunit structure	Interacts with PSPC1 By similarity. 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/SF-1. 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 By similarity. Interacts with RNF43.
Subcellular location	Nucleus matrix. Note: Predominantly in nuclear matrix. Ref.9 Ref.10
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. Ref.16 Ref.18 Ref.24 Ref.25 Ref.26 Arg-7, Arg-9, Arg-19 and Arg-25 are dimethylated, probably to asymmetric dimethylarginine. Ref.4 Ref.22
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	Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement
Domain	Repeat
Ligand	DNA-binding RNA-binding
Molecular function	Activator Repressor
PTM	Methylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA recombination Inferred from electronic annotation. Source: UniProtKB-KW DNA repair Inferred from electronic annotation. Source: UniProtKB-KW RNA splicing Ref.1 Traceable author statement. Source: ProtInc mRNA processing Ref.1 Traceable author statement. Source: ProtInc regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nuclear matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
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 protein binding Ref.9 Ref.10 Ref.19 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EXOSC5	Q9NQT4	1	EBI-355453,EBI-371876
NONO	Q15233	1	EBI-355463,EBI-350527
PTBP1	P26599	1	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.

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	7	1	Omega-N-methylated arginine Ref.22
	Modified residue	9	1	Omega-N-methylated arginine Ref.22
	Modified residue	19	1	Omega-N-methylated arginine Ref.22
	Modified residue	25	1	Omega-N-methylated arginine Ref.22
	Modified residue	33	1	Phosphoserine Ref.24 Ref.26
	Modified residue	273	1	Phosphoserine Ref.26
	Modified residue	283	1	Phosphoserine Ref.26
	Modified residue	314	1	N6,N6-dimethyllysine Ref.4
	Modified residue	571	1	Dimethylated arginine Ref.4
	Modified residue	681	1	Omega-N-methylarginine Ref.4
	Modified residue	687	1	Phosphothreonine Ref.25 Ref.26
	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
	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). 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

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of PSF, a novel pre-mRNA splicing factor." Patton J.G., Porro E.B., Galceran J., Tempst P., Nadal-Ginard B. Genes Dev. 7:393-406(1993) [PubMed: 8449401] [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: 16710414] [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: 8439294] [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: 9409622] [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: 2480877] [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: 9848648] [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: 10653975] [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: 8045264] [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: 9393982] [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: 9756848] [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: 10858305] [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: 10847580] [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: 10931916] [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: 11525732] [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: 11514619] [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: 11259580] [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: 11897684] [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: 12403470] [Abstract] Cited for: INTERACTION WITH NONO AND U5 SNRNA, IDENTIFICATION IN IN U5/4/6 SNRNP SND SPLICEOSOME COMPLEXES.
[22]	"Identifying and quantifying in vivo methylation sites by heavy methyl SILAC." Ong S.E., Mittler G., Mann M. Nat. Methods 1:119-126(2004) [PubMed: 15782174] [Abstract] Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-7; ARG-9; ARG-19 AND ARG-25, MASS SPECTROMETRY.
[23]	"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: 15590677] [Abstract] Cited for: FUNCTION IN DNA REPAIR, IDENTIFICATION BY MASS SPECTROMETRY, DNA-BINDING, SUBUNIT.
[24]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, MASS SPECTROMETRY. Tissue: Epithelium.
[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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-687, MASS SPECTROMETRY.
[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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33; SER-273; SER-283 AND THR-687, MASS SPECTROMETRY.
[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: 18655028] [Abstract] Cited for: INTERACTION WITH RNF43.
[28]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
UniGene	Hs.355934
3D structure databases
HSSP	HSSP built from PDB template 1NO8 based on UniProtKB O08583.
SMR	P23246. Positions 290-374.
ModBase	Search...
Protein-protein interaction databases
IntAct	P23246. 23 interactions.
PTM databases
PhosphoSite	P23246.
2-D gel databases
SWISS-2DPAGE	P23246.
Proteomic databases
PeptideAtlas	P23246.
PRIDE	P23246.
Genome annotation databases
Ensembl	ENSG00000116560. Homo sapiens. [Contig view]
GeneID	6421.
KEGG	hsa:6421.
Organism-specific databases
GeneCards	GC01M035470.
H-InvDB	HIX0000409.
HGNC	HGNC:10774. SFPQ.
HPA	CAB009886.
MIM	605199. gene.
PharmGKB	PA35690.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P23246.
HOVERGEN	P23246.
OMA	P23246. KEIQLRQ.
Gene expression databases
ArrayExpress	P23246.
Bgee	P23246.
CleanEx	HS_SFPQ.
GermOnline	ENSG00000116560. Homo sapiens.
Family and domain databases
InterPro	IPR012677. a_b_plait_nuc_bd. IPR012975. NOPS. IPR000504. RRM_RNP1. [Graphical view]
Gene3D	G3DSA:3.30.70.330. a_b_plait_nuc_bd. 2 hits.
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 Resources
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:	June 16, 2009
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)