Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Splicing factor, proline- and glutamine-rich

Gene

SFPQ

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>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

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-8849468 PTK6 Regulates Proteins Involved in RNA Processing

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P23246

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:SFPQ
Synonyms:PSF
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000116560.10

Human Gene Nomenclature Database

More...
HGNCi
HGNC:10774 SFPQ

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
605199 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P23246

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei662 – 663Breakpoint for translocation to form SFPQ-TFE32

Organism-specific databases

DisGeNET

More...
DisGeNETi
6421

MalaCards human disease database

More...
MalaCardsi
SFPQ

Open Targets

More...
OpenTargetsi
ENSG00000116560

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
319308 MiT family translocation renal cell carcinoma

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA35690

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
SFPQ

Domain mapping of disease mutations (DMDM)

More...
DMDMi
1709851

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000819091 – 707Splicing factor, proline- and glutamine-richAdd BLAST707

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

More...
EPDi
P23246

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P23246

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P23246

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P23246

PeptideAtlas

More...
PeptideAtlasi
P23246

PRoteomics IDEntifications database

More...
PRIDEi
P23246

ProteomicsDB human proteome resource

More...
ProteomicsDBi
54073
54074 [P23246-2]

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
P23246

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P23246

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P23246

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P23246

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000116560 Expressed in 233 organ(s), highest expression level in oviduct epithelium

CleanEx database of gene expression profiles

More...
CleanExi
HS_SFPQ

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P23246 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P23246 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB009886
HPA047513
HPA054689

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
112319, 280 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P23246

Database of interacting proteins

More...
DIPi
DIP-31272N

Protein interaction database and analysis system

More...
IntActi
P23246, 72 interactors

Molecular INTeraction database

More...
MINTi
P23246

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000349748

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P23246

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P23246

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati9 – 1113
Repeati19 – 2123
Repeati25 – 2733
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini297 – 369RRM 1PROSITE-ProRule annotationAdd BLAST73
Domaini371 – 452RRM 2PROSITE-ProRule annotationAdd BLAST82

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni9 – 273 X 3 AA repeats of R-G-GAdd BLAST19

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili497 – 596Sequence analysis1 PublicationAdd BLAST100

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>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

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0115 Eukaryota
ENOG410XQA0 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000156221

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000231095

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG009801

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P23246

KEGG Orthology (KO)

More...
KOi
K13219

Identification of Orthologs from Complete Genome Data

More...
OMAi
NQRPGPQ

Database of Orthologous Groups

More...
OrthoDBi
1274880at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P23246

TreeFam database of animal gene trees

More...
TreeFami
TF315795

Family and domain databases

Conserved Domains Database

More...
CDDi
cd12948 NOPS_PSF, 1 hit
cd12587 RRM1_PSF, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.70.330, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View 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

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF08075 NOPS, 1 hit
PF00076 RRM_1, 2 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00360 RRM, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54928 SSF54928, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50102 RRM, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>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:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0Y9U2H0Y9U2_HUMAN
Splicing factor, proline- and gluta...
SFPQ
88Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti243G → R AA sequence (PubMed:8439294).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_005855663 – 707RTERF…KKPRF → VRMIDVG in isoform Short. CuratedAdd BLAST45

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS388.1 [P23246-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
A46302
S29770

NCBI Reference Sequences

More...
RefSeqi
NP_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]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.355934
Hs.611911

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000357214; ENSP00000349748; ENSG00000116560 [P23246-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
6421

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:6421

UCSC genome browser

More...
UCSCi
uc001bys.4 human [P23246-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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, 280 interactors
CORUMiP23246
DIPiDIP-31272N
IntActiP23246, 72 interactors
MINTiP23246
STRINGi9606.ENSP00000349748

PTM databases

iPTMnetiP23246
PhosphoSitePlusiP23246
SwissPalmiP23246

Polymorphism and mutation databases

BioMutaiSFPQ
DMDMi1709851

2D gel databases

SWISS-2DPAGEiP23246

Proteomic databases

EPDiP23246
jPOSTiP23246
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

Comparative Toxicogenomics Database

More...
CTDi
6421
DisGeNETi6421
EuPathDBiHostDB:ENSG00000116560.10

GeneCards: human genes, protein and diseases

More...
GeneCardsi
SFPQ
HGNCiHGNC:10774 SFPQ
HPAiCAB009886
HPA047513
HPA054689
MalaCardsiSFPQ
MIMi605199 gene
neXtProtiNX_P23246
OpenTargetsiENSG00000116560
Orphaneti319308 MiT family translocation renal cell carcinoma
PharmGKBiPA35690

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0115 Eukaryota
ENOG410XQA0 LUCA
GeneTreeiENSGT00940000156221
HOGENOMiHOG000231095
HOVERGENiHBG009801
InParanoidiP23246
KOiK13219
OMAiNQRPGPQ
OrthoDBi1274880at2759
PhylomeDBiP23246
TreeFamiTF315795

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
SFPQ human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
SFPQ

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
6421

Protein Ontology

More...
PROi
PR:P23246

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSFPQ_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P23246
Secondary accession number(s): P30808, Q5SZ71
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: October 1, 1996
Last modified: January 16, 2019
This is version 213 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

  1. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again