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Protein

Splicing factor, proline- and glutamine-rich

Gene

SFPQ

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

DNA- and RNA binding protein, involved in several nuclear processes. Essential pre-mRNA splicing factor required early in spliceosome formation and for splicing catalytic step II, probably as a heteromer with NONO. Binds to pre-mRNA in spliceosome C complex, and specifically binds to intronic polypyrimidine tracts. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45, a phosphorylated form is sequestered by THRAP3 from the pre-mRNA in resting T-cells; T-cell activation and subsequent reduced phosphorylation is proposed to lead to release from THRAP3 allowing binding to pre-mRNA splicing regulatotry elements which represses exon inclusion. Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b. May be involved in a pre-mRNA coupled splicing and polyadenylation process as component of a snRNP-free complex with SNRPA/U1A. The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs. SFPQ may be involved in homologous DNA pairing; in vitro, promotes the invasion of ssDNA between a duplex DNA and produces a D-loop formation. The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1; in vitro, stimulates dissociation of TOP1 from DNA after cleavage and enhances its jumping between separate DNA helices. The SFPQ-NONO heteromer may be involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends; in vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex. SFPQ is involved in transcriptional regulation. Transcriptional repression is mediated by an interaction of SFPQ with SIN3A and subsequent recruitment of histone deacetylases (HDACs). The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional avtivity. SFPQ isoform Long binds to the DNA binding domains (DBD) of nuclear hormone receptors, like RXRA and probably THRA, and acts as transcriptional corepressor in absence of hormone ligands. Binds the DNA sequence 5'-CTGAGTC-3' in the insulin-like growth factor response element (IGFRE) and inhibits IGF-I-stimulated transcriptional activity. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation.10 Publications

GO - Molecular functioni

GO - Biological processi

  • alternative mRNA splicing, via spliceosome Source: BHF-UCL
  • chromosome organization Source: Ensembl
  • double-strand break repair via homologous recombination Source: MGI
  • histone H3 deacetylation Source: UniProtKB
  • mRNA processing Source: ProtInc
  • negative regulation of circadian rhythm Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: ParkinsonsUK-UCL
  • positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
  • positive regulation of sister chromatid cohesion Source: Ensembl
  • regulation of circadian rhythm Source: UniProtKB
  • rhythmic process Source: UniProtKB-KW
  • RNA splicing Source: ProtInc
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

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

Keywords - Ligandi

DNA-binding, RNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000116560-MONOMER.
ReactomeiR-HSA-8849468. PTK6 Regulates Proteins Involved in RNA Processing.
SIGNORiP23246.

Names & Taxonomyi

Protein namesi
Recommended name:
Splicing factor, proline- and glutamine-rich
Alternative name(s):
100 kDa DNA-pairing protein
Short name:
hPOMp100
DNA-binding p52/p100 complex, 100 kDa subunit
Polypyrimidine tract-binding protein-associated-splicing factor
Short name:
PSF
Short name:
PTB-associated-splicing factor
Gene namesi
Name:SFPQ
Synonyms:PSF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:10774. SFPQ.

Subcellular locationi

GO - Cellular componenti

  • chromatin Source: ParkinsonsUK-UCL
  • cytoplasm Source: UniProtKB-SubCell
  • extracellular matrix Source: BHF-UCL
  • nuclear matrix Source: BHF-UCL
  • nucleoplasm Source: BHF-UCL
  • nucleus Source: ParkinsonsUK-UCL
  • paraspeckles Source: BHF-UCL
  • RNA polymerase II transcription factor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi687T → A: Abolishes phosphorylation by GSK3B. Impairs interaction with THRAP3. 1 Publication1
Mutagenesisi687T → D: No effect on interaction with THRAP3 (phosphomimetic). 1 Publication1

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei662 – 663Breakpoint for translocation to form SFPQ-TFE32

Organism-specific databases

DisGeNETi6421.
MalaCardsiSFPQ.
OpenTargetsiENSG00000116560.
Orphaneti319308. Translocation renal cell carcinoma.
PharmGKBiPA35690.

Polymorphism and mutation databases

BioMutaiSFPQ.
DMDMi1709851.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000819091 – 707Splicing factor, proline- and glutamine-richAdd BLAST707

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei8Phosphoserine; by MKNK21 Publication1
Modified residuei9Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei9Omega-N-methylarginine; alternateBy similarity1
Modified residuei33PhosphoserineCombined sources1
Modified residuei208N6-acetyllysineBy similarity1
Modified residuei236Omega-N-methylarginineCombined sources1
Modified residuei242Omega-N-methylarginineCombined sources1
Modified residuei245Omega-N-methylarginineCombined sources1
Modified residuei273PhosphoserineCombined sources1
Modified residuei283Phosphoserine; by MKNK2Combined sources1 Publication1
Modified residuei293Phosphotyrosine; by ALK1 Publication1
Modified residuei314N6,N6-dimethyllysine1 Publication1
Modified residuei319N6-acetyllysineCombined sources1
Modified residuei338N6-acetyllysine; alternateCombined sources1
Cross-linki338Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei368PhosphothreonineCombined sources1
Modified residuei374PhosphoserineCombined sources1
Modified residuei379PhosphoserineCombined sources1
Modified residuei421N6-acetyllysineCombined sources1
Modified residuei472N6-acetyllysineCombined sources1
Modified residuei496PhosphoserineCombined sources1
Modified residuei571Dimethylated arginine1 Publication1
Modified residuei626PhosphoserineCombined sources1
Modified residuei681Omega-N-methylarginineCombined sources1 Publication1
Modified residuei687PhosphothreonineCombined sources1 Publication1
Modified residuei691PhosphotyrosineCombined sources1
Modified residuei693Dimethylated arginine; alternate1 Publication1
Modified residuei693Omega-N-methylarginine; alternateCombined sources1
Modified residuei695Omega-N-methylarginineCombined sources1

Post-translational modificationi

The N-terminus is blocked.
Phosphorylated on multiple serine and threonine residues during apoptosis. In vitro phosphorylated by PKC. Phosphorylation stimulates binding to DNA and D-loop formation, but inhibits binding to RNA. Phosphorylation of C-terminal tyrosines promotes its cytoplasmic localization, impaired its binding to polypyrimidine RNA and led to cell cycle arrest. In resting T-cells is phosphorylated at Thr-687 by GSK3B which is proposed to promote association with THRAP and to prevent binding to PTPRC/CD45 pre-mRNA; T-cell activation leads to reduced phosphorylation at Thr-687.6 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP23246.
MaxQBiP23246.
PaxDbiP23246.
PeptideAtlasiP23246.
PRIDEiP23246.

2D gel databases

SWISS-2DPAGEP23246.

PTM databases

iPTMnetiP23246.
PhosphoSitePlusiP23246.
SwissPalmiP23246.

Expressioni

Gene expression databases

BgeeiENSG00000116560.
CleanExiHS_SFPQ.
ExpressionAtlasiP23246. baseline and differential.
GenevisibleiP23246. HS.

Organism-specific databases

HPAiCAB009886.
HPA047513.
HPA054689.

Interactioni

Subunit structurei

Monomer and component of the SFPQ-NONO complex, which is probably a heterotetramer of two 52 kDa (NONO) and two 100 kDa (SFPQ) subunits. SFPQ is a component of spliceosome and U5.4/6 snRNP complexes. Interacts with SNRPA/U1A. Component of a snRNP-free complex with SNRPA/U1A. Part of complex consisting of SFPQ, NONO and MATR3. Interacts with polypyrimidine tract-binding protein 1/PTB. Part of a complex consisting of SFPQ, NONO and NR5A1. Interacts with RXRA, probably THRA, and SIN3A. Interacts with TOP1. Part of a complex consisting of SFPQ, NONO and TOP1. Interacts with SNRNP70 in apoptotic cells. Interacts with PSPC1. Interacts with RNF43. Interacts with PITX3 and NR4A2/NURR1. Interacts with PTK6. Interacts with THRAP3; the interaction is dependent on SFPQ phosphorylation at 'Thr-687' and inhibits binding of SFPQ to a ESS1 exonic splicing silencer element-containing RNA. The large PER complex involved in the histone deacetylation is composed of at least HDAC1, PER2, SFPQ and SIN3A. Interacts with PER1 and PER2.15 Publications
(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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
EBNA-LPQ8AZK72EBI-355453,EBI-1185167From a different organism.
HNF4AP412352EBI-355453,EBI-1049011
PTBP1P265992EBI-355453,EBI-350540
PTK6Q138825EBI-355453,EBI-1383632
RxraP287003EBI-355463,EBI-346715From a different organism.
SIN3AQ96ST32EBI-355453,EBI-347218
SNRPAP090124EBI-355453,EBI-607085
THRAP046252EBI-355463,EBI-286261From a different organism.
THRAP3Q9Y2W16EBI-355453,EBI-352039

GO - Molecular functioni

  • histone deacetylase binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

BioGridi112319. 194 interactors.
DIPiDIP-31272N.
IntActiP23246. 60 interactors.
MINTiMINT-1141893.
STRINGi9606.ENSP00000349748.

Structurei

Secondary structure

1707
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi277 – 283Combined sources7
Helixi295 – 297Combined sources3
Beta strandi298 – 303Combined sources6
Helixi310 – 316Combined sources7
Helixi317 – 320Combined sources4
Beta strandi326 – 329Combined sources4
Turni330 – 333Combined sources4
Beta strandi334 – 338Combined sources5
Helixi342 – 352Combined sources11
Beta strandi356 – 361Combined sources6
Beta strandi363 – 366Combined sources4
Beta strandi370 – 377Combined sources8
Helixi384 – 391Combined sources8
Helixi392 – 394Combined sources3
Beta strandi397 – 404Combined sources8
Beta strandi406 – 408Combined sources3
Beta strandi410 – 420Combined sources11
Helixi421 – 433Combined sources13
Beta strandi439 – 441Combined sources3
Beta strandi446 – 449Combined sources4
Beta strandi454 – 457Combined sources4
Helixi461 – 464Combined sources4
Helixi468 – 473Combined sources6
Beta strandi478 – 480Combined sources3
Helixi486 – 526Combined sources41
Helixi555 – 588Combined sources34

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4WIIX-ray2.05A/B276-535[»]
4WIJX-ray3.49A/B276-598[»]
4WIKX-ray3.00A/B369-598[»]
ProteinModelPortaliP23246.
SMRiP23246.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati9 – 1113
Repeati19 – 2123
Repeati25 – 2733
Domaini297 – 369RRM 1PROSITE-ProRule annotationAdd BLAST73
Domaini371 – 452RRM 2PROSITE-ProRule annotationAdd BLAST82

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni9 – 273 X 3 AA repeats of R-G-GAdd BLAST19

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi10 – 266Gln/Glu/Pro-richAdd BLAST257
Compositional biasi10 – 15Poly-Gly6
Compositional biasi20 – 27Poly-Gly8
Compositional biasi56 – 65Poly-Pro10
Compositional biasi67 – 71Poly-Gln5
Compositional biasi95 – 98Poly-Gln4
Compositional biasi99 – 103Poly-Pro5
Compositional biasi184 – 188Poly-Pro5
Compositional biasi571 – 574Poly-Arg4
Compositional biasi613 – 616Poly-Gly4
Compositional biasi635 – 641Poly-Gly7

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0115. Eukaryota.
ENOG410XQA0. LUCA.
GeneTreeiENSGT00390000005004.
HOGENOMiHOG000231095.
HOVERGENiHBG009801.
InParanoidiP23246.
KOiK13219.
OMAiGRQHHAP.
OrthoDBiEOG091G09T7.
PhylomeDBiP23246.
TreeFamiTF315795.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012975. NOPS.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF08075. NOPS. 1 hit.
PF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.
Isoform Long (identifier: P23246-1) [UniParc]FASTAAdd to basket
Also known as: A

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

« Hide

        10         20         30         40         50
MSRDRFRSRG GGGGGFHRRG GGGGRGGLHD FRSPPPGMGL NQNRGPMGPG
60 70 80 90 100
PGQSGPKPPI PPPPPHQQQQ QPPPQQPPPQ QPPPHQPPPH PQPHQQQQPP
110 120 130 140 150
PPPQDSSKPV VAQGPGPAPG VGSAPPASSS APPATPPTSG APPGSGPGPT
160 170 180 190 200
PTPPPAVTSA PPGAPPPTPP SSGVPTTPPQ AGGPPPPPAA VPGPGPGPKQ
210 220 230 240 250
GPGPGGPKGG KMPGGPKPGG GPGLSTPGGH PKPPHRGGGE PRGGRQHHPP
260 270 280 290 300
YHQQHHQGPP PGGPGGRSEE KISDSEGFKA NLSLLRRPGE KTYTQRCRLF
310 320 330 340 350
VGNLPADITE DEFKRLFAKY GEPGEVFINK GKGFGFIKLE SRALAEIAKA
360 370 380 390 400
ELDDTPMRGR QLRVRFATHA AALSVRNLSP YVSNELLEEA FSQFGPIERA
410 420 430 440 450
VVIVDDRGRS TGKGIVEFAS KPAARKAFER CSEGVFLLTT TPRPVIVEPL
460 470 480 490 500
EQLDDEDGLP EKLAQKNPMY QKERETPPRF AQHGTFEYEY SQRWKSLDEM
510 520 530 540 550
EKQQREQVEK NMKDAKDKLE SEMEDAYHEH QANLLRQDLM RRQEELRRME
560 570 580 590 600
ELHNQEMQKR KEMQLRQEEE RRRREEEMMI RQREMEEQMR RQREESYSRM
610 620 630 640 650
GYMDPRERDM RMGGGGAMNM GDPYGSGGQK FPPLGGGGGI GYEANPGVPP
660 670 680 690 700
ATMSGSMMGS DMRTERFGQG GAGPVGGQGP RGMGPGTPAG YGRGREEYEG

PNKKPRF
Length:707
Mass (Da):76,149
Last modified:October 1, 1996 - v2
Checksum:i6D8D5EA95E235847
GO
Isoform Short (identifier: P23246-2) [UniParc]FASTAAdd to basket
Also known as: F

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

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti243G → R AA sequence (PubMed:8439294).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_005855663 – 707RTERF…KKPRF → VRMIDVG in isoform Short. CuratedAdd BLAST45

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70944 mRNA. Translation: CAA50283.1.
AL590434 Genomic DNA. Translation: CAI12467.1.
CH471059 Genomic DNA. Translation: EAX07426.1.
X16850 mRNA. Translation: CAA34747.1.
CCDSiCCDS388.1. [P23246-1]
PIRiA46302.
S29770.
RefSeqiNP_005057.1. NM_005066.2. [P23246-1]
XP_005271169.1. XM_005271112.4. [P23246-1]
XP_005271170.1. XM_005271113.4. [P23246-1]
XP_005271172.1. XM_005271115.4. [P23246-2]
XP_016857542.1. XM_017002053.1. [P23246-1]
XP_016857543.1. XM_017002054.1. [P23246-1]
UniGeneiHs.355934.
Hs.611911.

Genome annotation databases

EnsembliENST00000357214; ENSP00000349748; ENSG00000116560. [P23246-1]
GeneIDi6421.
KEGGihsa:6421.
UCSCiuc001bys.4. human. [P23246-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70944 mRNA. Translation: CAA50283.1.
AL590434 Genomic DNA. Translation: CAI12467.1.
CH471059 Genomic DNA. Translation: EAX07426.1.
X16850 mRNA. Translation: CAA34747.1.
CCDSiCCDS388.1. [P23246-1]
PIRiA46302.
S29770.
RefSeqiNP_005057.1. NM_005066.2. [P23246-1]
XP_005271169.1. XM_005271112.4. [P23246-1]
XP_005271170.1. XM_005271113.4. [P23246-1]
XP_005271172.1. XM_005271115.4. [P23246-2]
XP_016857542.1. XM_017002053.1. [P23246-1]
XP_016857543.1. XM_017002054.1. [P23246-1]
UniGeneiHs.355934.
Hs.611911.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4WIIX-ray2.05A/B276-535[»]
4WIJX-ray3.49A/B276-598[»]
4WIKX-ray3.00A/B369-598[»]
ProteinModelPortaliP23246.
SMRiP23246.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112319. 194 interactors.
DIPiDIP-31272N.
IntActiP23246. 60 interactors.
MINTiMINT-1141893.
STRINGi9606.ENSP00000349748.

PTM databases

iPTMnetiP23246.
PhosphoSitePlusiP23246.
SwissPalmiP23246.

Polymorphism and mutation databases

BioMutaiSFPQ.
DMDMi1709851.

2D gel databases

SWISS-2DPAGEP23246.

Proteomic databases

EPDiP23246.
MaxQBiP23246.
PaxDbiP23246.
PeptideAtlasiP23246.
PRIDEiP23246.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000357214; ENSP00000349748; ENSG00000116560. [P23246-1]
GeneIDi6421.
KEGGihsa:6421.
UCSCiuc001bys.4. human. [P23246-1]

Organism-specific databases

CTDi6421.
DisGeNETi6421.
GeneCardsiSFPQ.
HGNCiHGNC:10774. SFPQ.
HPAiCAB009886.
HPA047513.
HPA054689.
MalaCardsiSFPQ.
MIMi605199. gene.
neXtProtiNX_P23246.
OpenTargetsiENSG00000116560.
Orphaneti319308. Translocation renal cell carcinoma.
PharmGKBiPA35690.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0115. Eukaryota.
ENOG410XQA0. LUCA.
GeneTreeiENSGT00390000005004.
HOGENOMiHOG000231095.
HOVERGENiHBG009801.
InParanoidiP23246.
KOiK13219.
OMAiGRQHHAP.
OrthoDBiEOG091G09T7.
PhylomeDBiP23246.
TreeFamiTF315795.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000116560-MONOMER.
ReactomeiR-HSA-8849468. PTK6 Regulates Proteins Involved in RNA Processing.
SIGNORiP23246.

Miscellaneous databases

ChiTaRSiSFPQ. human.
GeneWikiiSFPQ.
GenomeRNAii6421.
PROiP23246.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000116560.
CleanExiHS_SFPQ.
ExpressionAtlasiP23246. baseline and differential.
GenevisibleiP23246. HS.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012975. NOPS.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF08075. NOPS. 1 hit.
PF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSFPQ_HUMAN
AccessioniPrimary (citable) accession number: P23246
Secondary accession number(s): P30808, Q5SZ71
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 190 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.