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UniProtKB - P23246 (SFPQ_HUMAN)

Protein

Splicing factor, proline- and glutamine-rich

Gene

SFPQ

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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 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).By similarity12 Publications

Caution

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

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionActivator, DNA-binding, Repressor, RNA-binding
Biological processBiological rhythms, DNA damage, DNA recombination, DNA repair, Immunity, Innate immunity, mRNA processing, mRNA splicing, Transcription, Transcription regulation

Enzyme and pathway databases

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 factor1 Publication
Short name:
PSF1 Publication
Short name:
PTB-associated-splicing factor
Gene namesi
Name:SFPQ
Synonyms:PSF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000116560.10
HGNCiHGNC:10774 SFPQ
MIMi605199 gene
neXtProtiNX_P23246

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
Mutagenesisi535L → A: Impairs DNA binding and ability to mediate transcriptional activation; when associated with A-539; A-546 and A-549. 1 Publication1
Mutagenesisi539L → A: Impairs DNA binding and ability to mediate transcriptional activation; when associated with A-535; A-546 and A-549. 1 Publication1
Mutagenesisi546L → A: Impairs DNA binding and ability to mediate transcriptional activation; when associated with A-535; A-539 and A-549. 1 Publication1
Mutagenesisi549M → A: Impairs DNA binding and ability to mediate transcriptional activation; when associated with A-535; A-539 and A-546. 1 Publication1
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
Cross-linki271Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei273PhosphoserineCombined sources1
Cross-linki279Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
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
ProteomicsDBi54073
54074 [P23246-2]

2D gel databases

SWISS-2DPAGEiP23246

PTM databases

iPTMnetiP23246
PhosphoSitePlusiP23246
SwissPalmiP23246

Expressioni

Gene expression databases

BgeeiENSG00000116560 Expressed in 233 organ(s), highest expression level in oviduct epithelium
CleanExiHS_SFPQ
ExpressionAtlasiP23246 baseline and differential
GenevisibleiP23246 HS

Organism-specific databases

HPAiCAB009886
HPA047513
HPA054689

Interactioni

Subunit structurei

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). Component of a multiprotein complex with NONO and WASL (PubMed:16767080).By similarity18 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. 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.2 Publications

Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi112319, 276 interactors
CORUMiP23246
DIPiDIP-31272N
IntActiP23246, 69 interactors
MINTiP23246
STRINGi9606.ENSP00000349748

Structurei

Secondary structure

1707
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili497 – 596Sequence analysis1 PublicationAdd BLAST100

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

Domaini

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.1 Publication

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

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

Family and domain databases

CDDicd12948 NOPS_PSF, 1 hit
cd12587 RRM1_PSF, 1 hit
Gene3Di3.30.70.330, 2 hits
InterProiView protein in InterPro
IPR012975 NOPS
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR034526 PSF_NOPS
IPR034525 PSF_RRM1
IPR035979 RBD_domain_sf
IPR000504 RRM_dom
PfamiView protein in Pfam
PF08075 NOPS, 1 hit
PF00076 RRM_1, 2 hits
SMARTiView protein in SMART
SM00360 RRM, 2 hits
SUPFAMiSSF54928 SSF54928, 1 hit
PROSITEiView protein in PROSITE
PS50102 RRM, 2 hits

Sequences (2+)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket
Note: Additional isoforms seem to exist.

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H0Y9K7H0Y9K7_HUMAN
Splicing factor, proline- and gluta...
SFPQ
223Annotation score:
H0Y9U2H0Y9U2_HUMAN
Splicing factor, proline- and gluta...
SFPQ
88Annotation score:

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 No translation available.
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

Similar proteinsi

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 No translation available.
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[»]
5WPAX-ray2.29A276-535[»]
ProteinModelPortaliP23246
SMRiP23246
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112319, 276 interactors
CORUMiP23246
DIPiDIP-31272N
IntActiP23246, 69 interactors
MINTiP23246
STRINGi9606.ENSP00000349748

PTM databases

iPTMnetiP23246
PhosphoSitePlusiP23246
SwissPalmiP23246

Polymorphism and mutation databases

BioMutaiSFPQ
DMDMi1709851

2D gel databases

SWISS-2DPAGEiP23246

Proteomic databases

EPDiP23246
MaxQBiP23246
PaxDbiP23246
PeptideAtlasiP23246
PRIDEiP23246
ProteomicsDBi54073
54074 [P23246-2]

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
EuPathDBiHostDB:ENSG00000116560.10
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
OMAiAFERCTE
OrthoDBiEOG091G09T7
PhylomeDBiP23246
TreeFamiTF315795

Enzyme and pathway databases

ReactomeiR-HSA-8849468 PTK6 Regulates Proteins Involved in RNA Processing
SIGNORiP23246

Miscellaneous databases

ChiTaRSiSFPQ human
GeneWikiiSFPQ
GenomeRNAii6421
PROiPR:P23246
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000116560 Expressed in 233 organ(s), highest expression level in oviduct epithelium
CleanExiHS_SFPQ
ExpressionAtlasiP23246 baseline and differential
GenevisibleiP23246 HS

Family and domain databases

CDDicd12948 NOPS_PSF, 1 hit
cd12587 RRM1_PSF, 1 hit
Gene3Di3.30.70.330, 2 hits
InterProiView protein in InterPro
IPR012975 NOPS
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR034526 PSF_NOPS
IPR034525 PSF_RRM1
IPR035979 RBD_domain_sf
IPR000504 RRM_dom
PfamiView protein in Pfam
PF08075 NOPS, 1 hit
PF00076 RRM_1, 2 hits
SMARTiView protein in SMART
SM00360 RRM, 2 hits
SUPFAMiSSF54928 SSF54928, 1 hit
PROSITEiView protein in PROSITE
PS50102 RRM, 2 hits
ProtoNetiSearch...

Entry informationi

Entry nameiSFPQ_HUMAN
AccessioniPrimary (citable) accession number: P23246
Secondary accession number(s): P30808, Q5SZ71
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: October 1, 1996
Last modified: October 10, 2018
This is version 210 of the entry and version 2 of the sequence. See 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

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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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