Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 169 (18 Sep 2019)
Sequence version 1 (01 Mar 2002)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Splicing factor, proline- and glutamine-rich

Gene

Sfpq

Organism
Mus musculus (Mouse)
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. 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 (By similarity). 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 (By similarity). 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 (PubMed:21680841, PubMed:22966205). Required for the assembly of nuclear speckles (By similarity). 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 (By similarity).By similarity2 Publications

<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 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-MMU-8849468 PTK6 Regulates Proteins Involved in RNA Processing

<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):
DNA-binding p52/p100 complex, 100 kDa subunit
Polypyrimidine tract-binding protein-associated-splicing factor
Short name:
PSF
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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 4

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1918764 Sfpq

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<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_00000819101 – 699Splicing factor, proline- and glutamine-richAdd BLAST699

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 residuei7Omega-N-methylated arginineBy similarity1
Modified residuei8Phosphoserine; by MKNK2By similarity1
Modified residuei9Asymmetric dimethylarginine; alternateCombined sources1
Modified residuei9Omega-N-methylarginine; alternateCombined sources1
Modified residuei9Omega-N-methylated arginine; alternateBy similarity1
Modified residuei19Omega-N-methylated arginineBy similarity1
Modified residuei25Omega-N-methylated arginineBy similarity1
Modified residuei33PhosphoserineBy similarity1
Modified residuei200N6-acetyllysineCombined sources1
Modified residuei228Omega-N-methylarginineCombined sources1
Modified residuei234Omega-N-methylarginineCombined sources1
Modified residuei237Omega-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-linki263Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei265PhosphoserineBy similarity1
Cross-linki271Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei275Phosphoserine; by MKNK2By similarity1
Modified residuei285Phosphotyrosine; by ALKBy similarity1
Modified residuei306N6,N6-dimethyllysineBy similarity1
Modified residuei311N6-acetyllysineBy similarity1
Modified residuei330N6-acetyllysine; alternateBy similarity1
Cross-linki330Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei360PhosphothreonineBy similarity1
Modified residuei366PhosphoserineBy similarity1
Modified residuei371PhosphoserineBy similarity1
Modified residuei413N6-acetyllysineBy similarity1
Modified residuei464N6-acetyllysineBy similarity1
Modified residuei488PhosphoserineBy similarity1
Modified residuei563Dimethylated arginineBy similarity1
Modified residuei618PhosphoserineBy similarity1
Modified residuei673Omega-N-methylarginineCombined sources1
Modified residuei679PhosphothreonineCombined sources1
Modified residuei683PhosphotyrosineBy similarity1
Modified residuei685Dimethylated arginine; alternateBy similarity1
Modified residuei685Omega-N-methylarginine; alternateCombined sources1
Modified residuei687Omega-N-methylarginineBy similarity1

<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

Phosphorylated on multiple serine and threonine residues during apoptosis (By similarity). Phosphorylation of C-terminal tyrosines promotes its cytoplasmic localization, impaired its binding to polypyrimidine RNA and led to cell cycle arrest (By similarity). In resting T-cells is phosphorylated at Thr-679 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-679.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q8VIJ6

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q8VIJ6

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q8VIJ6

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

More...
PaxDbi
Q8VIJ6

PeptideAtlas

More...
PeptideAtlasi
Q8VIJ6

PRoteomics IDEntifications database

More...
PRIDEi
Q8VIJ6

2D gel databases

REPRODUCTION-2DPAGE

More...
REPRODUCTION-2DPAGEi
Q8VIJ6

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q8VIJ6

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

More...
PhosphoSitePlusi
Q8VIJ6

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q8VIJ6

<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
ENSMUSG00000028820 Expressed in 299 organ(s), highest expression level in heart

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q8VIJ6 MM

<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. Monomer and component of the SFPQ-NONO complex, which is probably a heterotetramer of two 52 kDa (NONO) and two 100 kDa (SFPQ) subunits. The coiled coil domain mediates interaction with NONO, and can also mediate formation of long, linear homooligomers (in vitro). 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 (PubMed:15140795).

Interacts with RNF43 (By similarity).

Interacts with PITX3 and NR4A2/NURR1 (PubMed:19144721).

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 (By similarity). The large PER complex involved in the histone deacetylation is composed of at least HDAC1, PER2, SFPQ and SIN3A (PubMed:21680841).

Interacts with PER1 and PER2 (PubMed:22966205). 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 (By similarity).

Interacts with PQBP1.

Component of a multiprotein complex with NONO and WASL (By similarity).

By similarity4 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
214752, 22 interactors

Protein interaction database and analysis system

More...
IntActi
Q8VIJ6, 8 interactors

Molecular INTeraction database

More...
MINTi
Q8VIJ6

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000030623

<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

3D structure databases

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

More...
SMRi
Q8VIJ6

Database of comparative protein structure models

More...
ModBasei
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>Domaini289 – 361RRM 1PROSITE-ProRule annotationAdd BLAST73
Domaini363 – 444RRM 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 coili489 – 588Sequence analysisAdd 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 – 258Gln/Glu/Pro-richAdd BLAST249
Compositional biasi10 – 15Poly-Gly6
Compositional biasi20 – 27Poly-Gly8
Compositional biasi54 – 63Poly-Pro10
Compositional biasi65 – 69Poly-Gln5
Compositional biasi96 – 100Poly-Pro5
Compositional biasi158 – 161Poly-Pro4
Compositional biasi178 – 182Poly-Pro5
Compositional biasi563 – 566Poly-Arg4
Compositional biasi605 – 608Poly-Gly4
Compositional biasi627 – 633Poly-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.By similarity

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

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q8VIJ6

KEGG Orthology (KO)

More...
KOi
K13219

Identification of Orthologs from Complete Genome Data

More...
OMAi
REENYRM

Database of Orthologous Groups

More...
OrthoDBi
1274880at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q8VIJ6

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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<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.

Q8VIJ6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSRDRFRSRG GGGGGFHRRG GGGGRGGLHD FRSPPPGMGL NQNRGPMGPG
60 70 80 90 100
PGGPKPPLPP PPPHQQQQQP PPQQPPPQQP PPHQQPPPHQ PPHQQPPPPP
110 120 130 140 150
QESKPVVPQG PGSAPGVSSA PPPAVSAPPA NPPTTGAPPG PGPTPTPPPA
160 170 180 190 200
VPSTAPGPPP PSTPSSGVST TPPQTGGPPP PPAGGAGPGP KPGPGPGGPK
210 220 230 240 250
GGKMPGGPKP GGGPGMGAPG GHPKPPHRGG GEPRGGRQHH APYHQQHHQG
260 270 280 290 300
PPPGGPGPRT EEKISDSEGF KANLSLLRRP GEKTYTQRCR LFVGNLPADI
310 320 330 340 350
TEDEFKRLFA KYGEPGEVFI NKGKGFGFIK LESRALAEIA KAELDDTPMR
360 370 380 390 400
GRQLRVRFAT HAAALSVRNL SPYVSNELLE EAFSQFGPIE RAVVIVDDRG
410 420 430 440 450
RSTGKGIVEF ASKPAARKAF ERCSEGVFLL TTTPRPVIVE PLEQLDDEDG
460 470 480 490 500
LPEKLAQKNP MYQKERETPP RFAQHGTFEY EYSQRWKSLD EMEKQQREQV
510 520 530 540 550
EKNMKDAKDK LESEMEDAYH EHQANLLRQD LMRRQEELRR MEELHSQEMQ
560 570 580 590 600
KRKEMQLRQE EERRRREEEM MIRQREMEEQ MRRQREESYS RMGYMDPRER
610 620 630 640 650
DMRMGGGGTM NMGDPYGSGG QKFPPLGGGG GIGYEANPGV PPATMSGSMM
660 670 680 690
GSDMRTERFG QGGAGPVGGQ GPRGMGPGTP AGYGRGREEY EGPNKKPRF
Length:699
Mass (Da):75,442
Last modified:March 1, 2002 - v1
<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:i714F786264C63AA0
GO

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 conflicti47M → Q AA sequence (PubMed:11008015).Curated1
Sequence conflicti546S → N in AAG17365 (PubMed:11008015).Curated1

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
AY034062 mRNA Translation: AAK60397.1
AL606985 Genomic DNA No translation available.
BC089305 mRNA Translation: AAH89305.1
AF272847 mRNA Translation: AAG17365.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS18662.1

NCBI Reference Sequences

More...
RefSeqi
NP_076092.1, NM_023603.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000030623; ENSMUSP00000030623; ENSMUSG00000028820

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
71514

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:71514

UCSC genome browser

More...
UCSCi
uc008utz.2 mouse

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY034062 mRNA Translation: AAK60397.1
AL606985 Genomic DNA No translation available.
BC089305 mRNA Translation: AAH89305.1
AF272847 mRNA Translation: AAG17365.1
CCDSiCCDS18662.1
RefSeqiNP_076092.1, NM_023603.3

3D structure databases

SMRiQ8VIJ6
ModBaseiSearch...

Protein-protein interaction databases

BioGridi214752, 22 interactors
IntActiQ8VIJ6, 8 interactors
MINTiQ8VIJ6
STRINGi10090.ENSMUSP00000030623

PTM databases

iPTMnetiQ8VIJ6
PhosphoSitePlusiQ8VIJ6
SwissPalmiQ8VIJ6

2D gel databases

REPRODUCTION-2DPAGEiQ8VIJ6

Proteomic databases

EPDiQ8VIJ6
jPOSTiQ8VIJ6
MaxQBiQ8VIJ6
PaxDbiQ8VIJ6
PeptideAtlasiQ8VIJ6
PRIDEiQ8VIJ6

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030623; ENSMUSP00000030623; ENSMUSG00000028820
GeneIDi71514
KEGGimmu:71514
UCSCiuc008utz.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
6421
MGIiMGI:1918764 Sfpq

Phylogenomic databases

eggNOGiKOG0115 Eukaryota
ENOG410XQA0 LUCA
GeneTreeiENSGT00940000156221
HOGENOMiHOG000231095
InParanoidiQ8VIJ6
KOiK13219
OMAiREENYRM
OrthoDBi1274880at2759
PhylomeDBiQ8VIJ6
TreeFamiTF315795

Enzyme and pathway databases

ReactomeiR-MMU-8849468 PTK6 Regulates Proteins Involved in RNA Processing

Miscellaneous databases

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

More...
ChiTaRSi
Sfpq mouse

Protein Ontology

More...
PROi
PR:Q8VIJ6

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000028820 Expressed in 299 organ(s), highest expression level in heart
GenevisibleiQ8VIJ6 MM

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...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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_MOUSE
<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: Q8VIJ6
Secondary accession number(s): A2A7U6, Q9ERW2
<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: July 5, 2005
Last sequence update: March 1, 2002
Last modified: September 18, 2019
This is version 169 of the entry and version 1 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

<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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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