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Entry version 151 (05 Jun 2019)
Sequence version 1 (01 Mar 2002)
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Protein

Heterogeneous nuclear ribonucleoprotein U

Gene

Hnrnpu

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 cellular processes such as nuclear chromatin organization, telomere-length regulation, transcription, mRNA alternative splicing and stability, Xist-mediated transcriptional silencing and mitotic cell progression (PubMed:20833368, PubMed:21235343, PubMed:22162999, PubMed:26244333). Plays a role in the regulation of interphase large-scale gene-rich chromatin organization through chromatin-associated RNAs (caRNAs) in a transcription-dependent manner, and thereby maintains genomic stability (By similarity). Required for the localization of the long non-coding Xist RNA on the inactive chromosome X (Xi) and the subsequent initiation and maintenance of X-linked transcriptional gene silencing during X-inactivation (PubMed:20833368, PubMed:26244333). Plays a role as a RNA polymerase II (Pol II) holoenzyme transcription regulator (PubMed:21235343, PubMed:22162999). Promotes transcription initiation by direct association with the core-TFIIH basal transcription factor complex for the assembly of a functional pre-initiation complex with Pol II in a actin-dependent manner. Blocks Pol II transcription elongation activity by inhibiting the C-terminal domain (CTD) phosphorylation of Pol II and dissociates from Pol II pre-initiation complex prior to productive transcription elongation. Positively regulates CBX5-induced transcriptional gene silencing and retention of CBX5 in the nucleus. Negatively regulates glucocorticoid-mediated transcriptional activation (By similarity). Key regulator of transcription initiation and elongation in embryonic stem cells upon leukemia inhibitory factor (LIF) signaling (PubMed:21235343). Involved in the long non-coding RNA H19-mediated Pol II transcriptional repression (By similarity). Participates in the circadian regulation of the core clock component ARNTL/BMAL1 transcription (PubMed:18332112). Plays a role in the regulation of telomere length. Plays a role as a global pre-mRNA alternative splicing modulator by regulating U2 small nuclear ribonucleoprotein (snRNP) biogenesis. Plays a role in mRNA stability. Component of the CRD-mediated complex that promotes MYC mRNA stabilization. Enhances the expression of specific genes, such as tumor necrosis factor TNFA, by regulating mRNA stability, possibly through binding to the 3'-untranslated region (UTR). Plays a role in mitotic cell cycle regulation. Involved in the formation of stable mitotic spindle microtubules (MTs) attachment to kinetochore, spindle organization and chromosome congression. Phosphorylation at Ser-58 by PLK1 is required for chromosome alignement and segregation and progression through mitosis. Contributes also to the targeting of AURKA to mitotic spindle MTs. Binds to double- and single-stranded DNA and RNA, poly(A), poly(C) and poly(G) oligoribonucleotides. Binds to chromatin-associated RNAs (caRNAs). Associates with chromatin to scaffold/matrix attachment region (S/MAR) elements in a chromatin-associated RNAs (caRNAs)-dependent manner (By similarity). Binds (via RNA-binding RGG-box region) to the long non-coding Xist RNA; this binding is direct and bridges the Xist RNA and the inactive chromosome X (Xi) (PubMed:20833368, PubMed:26244333). Binds the long non-coding H19 RNA. Binds to SMN1/2 pre-mRNAs at G/U-rich regions. Binds to small nuclear RNAs (snRNAs). Binds to the 3'-UTR of TNFA mRNA (By similarity). Also negatively regulates embryonic stem cell differentiation upon LIF signaling (PubMed:21235343). Required for embryonic development (PubMed:16022389). Binds to brown fat long non-coding RNA 1 (Blnc1); facilitates the recruitment of Blnc1 by ZBTB7B required to drive brown and beige fat development and thermogenesis (PubMed:28784777).By similarity7 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi480 – 487ATPSequence analysis8

<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, Chromatin regulator, Developmental protein, DNA-binding, Repressor, Ribonucleoprotein, RNA-binding
Biological processBiological rhythms, Cell cycle, Cell division, Differentiation, Mitosis, mRNA processing, mRNA splicing, Transcription, Transcription regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-72163 mRNA Splicing - Major Pathway
R-MMU-72203 Processing of Capped Intron-Containing Pre-mRNA

<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:
Heterogeneous nuclear ribonucleoprotein UImported
Short name:
hnRNP U1 Publication
Alternative name(s):
Scaffold-attachment factor A1 Publication
Short name:
SAF-A1 Publication
<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:HnrnpuImported
Synonyms:HnrpuImported
<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 1

Organism-specific databases

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

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MGIi
MGI:1858195 Hnrnpu

<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

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Nucleus, Spliceosome

<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 describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mice exhibit early embryonic lethality between 9.5 and 11.5 dpc (PubMed:16022389). Mice show retarded development of embryonic ectoderm at 6.5 dpc and growth retardation beginning at 7.5 dpc (PubMed:16022389).1 Publication

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<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_00003879472 – 800Heterogeneous nuclear ribonucleoprotein UAdd BLAST799

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 residuei2N-acetylserineBy similarity1
Modified residuei4PhosphoserineBy similarity1
Modified residuei17N6-acetyllysineCombined sources1
Modified residuei21N6-acetyllysineCombined sources1
Modified residuei58PhosphoserineCombined sources1
Modified residuei181N6-acetyllysineCombined sources1
Modified residuei182ADP-ribosylserineBy similarity1
Modified residuei231Citrulline1 Publication1
Modified residuei241N6-acetyllysine; alternateCombined 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-linki241Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki241Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei242PhosphotyrosineCombined sources1
Modified residuei243PhosphoserineBy similarity1
Modified residuei247PhosphoserineCombined sources1
Modified residuei262PhosphothreonineBy similarity1
Modified residuei328N6-acetyllysineCombined sources1
Cross-linki471Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei492N6-acetyllysine; alternateBy similarity1
Cross-linki492Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei500N6-acetyllysine; alternateBy similarity1
Cross-linki500Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei508PhosphothreonineBy similarity1
Cross-linki512Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei527N6-acetyllysineBy similarity1
Modified residuei541N6-acetyllysine; alternateBy similarity1
Cross-linki541Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki550Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei558PhosphothreonineBy similarity1
Cross-linki585Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki602Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei611N6-acetyllysine; alternateBy similarity1
Cross-linki611Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki640Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki646Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei678Omega-N-methylarginineBy similarity1
Modified residuei691Asymmetric dimethylarginineCombined sources1
Modified residuei696Asymmetric dimethylarginineCombined sources1
Modified residuei703Asymmetric dimethylarginineCombined sources1
Modified residuei709Asymmetric dimethylarginine; alternateCombined sources1
Modified residuei709Omega-N-methylarginine; alternateCombined sources1
Modified residuei709Omega-N-methylated arginine; alternateBy similarity1
Modified residuei715Asymmetric dimethylarginine; alternateCombined sources1
Modified residuei715Dimethylated arginine; alternateBy similarity1
Modified residuei715Omega-N-methylarginine; alternateCombined sources1
Modified residuei715Omega-N-methylated arginine; alternateBy similarity1
Modified residuei730Asymmetric dimethylarginineBy similarity1
Modified residuei737Asymmetric dimethylarginineCombined sources1
Modified residuei789N6-acetyllysine; alternateBy similarity1
Cross-linki789Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity

<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

Cleaved at Asp-94 by CASP3 during T-cell apoptosis, resulting in a loss of DNA- and chromatin-binding activities.By similarity
Extensively phosphorylated. Phosphorylated on Ser-58 by PLK1 and dephosphorylated by protein phosphatase 2A (PP2A) in mitosis.By similarity
Arg-709 and Arg-715 are dimethylated, probably to asymmetric dimethylarginine.
Citrullinated by PADI4.1 Publication

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>Sitei94 – 95Cleavage; by CASP3By similarity2

Keywords - PTMi

Acetylation, ADP-ribosylation, Citrullination, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q8VEK3

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q8VEK3

MaxQB - The MaxQuant DataBase

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MaxQBi
Q8VEK3

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

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PaxDbi
Q8VEK3

PeptideAtlas

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PeptideAtlasi
Q8VEK3

PRoteomics IDEntifications database

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PRIDEi
Q8VEK3

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q8VEK3

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

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PhosphoSitePlusi
Q8VEK3

SwissPalm database of S-palmitoylation events

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SwissPalmi
Q8VEK3

<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
ENSMUSG00000100725 Expressed in 20 organ(s), highest expression level in embryonic stem cell

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q8VEK3 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q8VEK3 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

Oligomer (via ATPase domain and RNA-binding RGG-box region); oligomerization occurs upon ATP-binding in a chromatin-associated RNAs (caRNAs)- and transcription-dependent manner and is required for chromatin decompaction. ATP hydrolysis is required to cycle from an oligomeric to monomeric state to compact chromatin. Component of the coding region determinant (CRD)-mediated complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1. Identified in the spliceosome C complex. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Associates with heterogeneous nuclear ribonucleoprotein (hnRNP) particles (By similarity). Associates (via middle region) with the C-terminal domain (CTD) RNA polymerase II (Pol II) holoenzyme; this association occurs in a RNA-independent manner (PubMed:21235343). Associates (via middle region) with the core-TFIIH basal transcription factor complex; this association inhibits the CTD phosphorylation of RNA polymerase II holoenzyme by downregulating TFIIH kinase activity. Associates with the telomerase holoenzyme complex. Associates with spindle microtubules (MTs) in a TPX2-dependent manner. Interacts (via C-terminus) with actin; this interaction is direct and mediates association with the phosphorylated CTD of RNA polymerase II and is disrupted in presence of the long non-coding H19 RNA. Interacts with AURKA. Interacts (via C-terminus) with CBX5; this interaction is, at least in part, RNA-dependent. Interacts with CR2 (By similarity). Interacts with CRY1 (PubMed:19129230). Interacts (via C-terminus) with EP300; this interaction enhances DNA-binding to nuclear scaffold/matrix attachment region (S/MAR) elements. Interacts with ERBB4. Interacts with GEMIN5. Interacts with IGF2BP1. Interacts with IGF2BP2 and IGF2BP3. Interacts with NCL; this interaction occurs during mitosis. Interacts (via C-terminus) with NR3C1 (via C-terminus). Interacts with PLK1; this interaction induces phosphorylation of HNRNPU at Ser-58 in mitosis. Interacts with POU3F4 (By similarity). Interacts with SMARCA4; this interaction occurs in embryonic stem cells and stimulates global Pol II-mediated transcription (PubMed:22162999). Interacts (via C-terminus) with TOP2A; this interaction protects the topoisomerase TOP2A from degradation and positively regulates the relaxation of supercoiled DNA by TOP2A in a RNA-dependent manner. Interacts with TPX2; this interaction recruits HNRNPU to spindle microtubules (MTs). Interacts with UBQLN2 (By similarity). Interacts (via RNA-binding RGG-box region) with ZBTB7B; the interaction facilitates the recruitment of long non-coding RNA Blnc1 by ZBTB7B (PubMed:28784777).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

WithEntry#Exp.IntActNotes
Smarca4Q3TKT43EBI-529674,EBI-1210244

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
206185, 18 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-1089 CRD-mediated mRNA stability complex

Database of interacting proteins

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DIPi
DIP-34257N

Protein interaction database and analysis system

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IntActi
Q8VEK3, 7 interactors

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000047571

<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

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SMRi
Q8VEK3

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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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 <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>Domaini8 – 42SAPPROSITE-ProRule annotation1 PublicationAdd BLAST35
Domaini244 – 440B30.2/SPRYPROSITE-ProRule annotationAdd BLAST197

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>Regioni464 – 648ATPase domainBy similarityAdd BLAST185
Regioni587 – 602Actin-bindingBy similarityAdd BLAST16
Regioni690 – 715RNA-binding RGG-box2 PublicationsAdd BLAST26

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 coili626 – 653Sequence analysisAdd BLAST28

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 biasi2 – 154Asp/Glu-rich (acidic)Add BLAST153
Compositional biasi679 – 769Gly-richAdd BLAST91

<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 SAP domain is necessary for specific binding to nuclear scaffold/matrix attachment region (S/MAR) elements in DNA. The RNA-binding RGG-box region is necessary for its association with inactive X chromosome (Xi) regions and to chromatin-associated RNAs (caRNAs) (By similarity). Both the DNA-binding domain SAP and the RNA-binding RGG-box region are necessary for the localization of Xist RNA on the Xi (PubMed:20833368). The ATPase and RNA-binding RGG-box regions are necessary for oligomerization (By similarity).By similarity1 Publication

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG2242 Eukaryota
ENOG410Y1WQ LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000156546

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000253920

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q8VEK3

KEGG Orthology (KO)

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KOi
K12888

Identification of Orthologs from Complete Genome Data

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OMAi
AFNQSWQ

Database of Orthologous Groups

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OrthoDBi
778148at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q8VEK3

TreeFam database of animal gene trees

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TreeFami
TF317301

Family and domain databases

Conserved Domains Database

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CDDi
cd12884 SPRY_hnRNP, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.720.30, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR001870 B30.2/SPRY
IPR013320 ConA-like_dom_sf
IPR026745 hnRNP_U
IPR027417 P-loop_NTPase
IPR003034 SAP_dom
IPR036361 SAP_dom_sf
IPR003877 SPRY_dom
IPR035778 SPRY_hnRNP_U

The PANTHER Classification System

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PANTHERi
PTHR12381:SF11 PTHR12381:SF11, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF02037 SAP, 1 hit
PF00622 SPRY, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00513 SAP, 1 hit
SM00449 SPRY, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF49899 SSF49899, 1 hit
SSF52540 SSF52540, 1 hit
SSF68906 SSF68906, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50188 B302_SPRY, 1 hit
PS50800 SAP, 1 hit

<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>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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

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

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

Isoform 1 (identifier: Q8VEK3-1) [UniParc]FASTAAdd to basket

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
MSSSPVNVKK LKVSELKEEL KKRRLSDKGL KADLMDRLQA ALDNEAGGRP
60 70 80 90 100
AMEPGNGSLD LGGDAAGRSG AGLEQEAAAG AEDDEEEEGI AALDGDQMEL
110 120 130 140 150
GEENGAAGAA DAGAMEEEEA ASEDENGDDQ GFQEGEDELG DEEEGAGDEN
160 170 180 190 200
GHGEQQSQPP AAAAQQQPSQ QRGAGKEAAG KSSGPTSLFA VTVAPPGARQ
210 220 230 240 250
GQQQAGGDGK TEQKGGDKKR GVKRPREDHG RGYFEYIEEN KYSRAKSPQP
260 270 280 290 300
PVEEEDEHFD DTVVCLDTYN CDLHFKISRD RLSASSLTME SFAFLWAGGR
310 320 330 340 350
ASYGVSKGKV CFEMKVTEKI PVRHLYTKDI DIHEVRIGWS LTTSGMLLGE
360 370 380 390 400
EEFSYGYSLK GIKTCNCETE DYGEKFDEND VITCFANFET DEVELSYAKN
410 420 430 440 450
GQDLGVAFKI SKEVLADRPL FPHVLCHNCA VEFNFGQKEK PYFPIPEDCT
460 470 480 490 500
FIQNVPLEDR VRGPKGPEEK KDCEVVMMIG LPGAGKTTWV TKHAAENPGK
510 520 530 540 550
YNILGTNTIM DKMMVAGFKK QMADTGKLNT LLQRAPQCLG KFIEIAARKK
560 570 580 590 600
RNFILDQTNV SAAAQRRKMC LFAGFQRKAV VVCPKDEDYK QRTQKKAEVE
610 620 630 640 650
GKDLPEHAVL KMKGNFTLPE VAECFDEITY VELQKEEAQK LLEQYKEESK
660 670 680 690 700
KALPPEKKQN TGSKKSNKNK SGKNQFNRGG GHRGRGGFNM RGGNFRGGAP
710 720 730 740 750
GNRGGYNRRG NMPQRGGGGG SGGIGYPYPR GPVFPGRGGY SNRGNYNRGG
760 770 780 790 800
MPNRGNYNQN FRGRGNNRGY KNQSQGYNQW QQGQFWGQKP WSQHYHQGYY
Length:800
Mass (Da):87,918
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:i2BA7C73043F847B2
GO
Isoform 2 (identifier: Q8VEK3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     784-800: QFWGQKPWSQHYHQGYY → SVHVNVLCEE

Note: Gene prediction based on EST data.
Show »
Length:793
Mass (Da):86,805
Checksum:i78E12271FF261ABA
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
A0A087WPX7A0A087WPX7_MOUSE
Heterogeneous nuclear ribonucleopro...
Hnrnpu Gm28062
105Annotation 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>
A0A087WPF1A0A087WPF1_MOUSE
Heterogeneous nuclear ribonucleopro...
Hnrnpu Gm28062
43Annotation 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>

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.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_059004784 – 800QFWGQ…HQGYY → SVHVNVLCEE in isoform 2. Add BLAST17

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
AK165844 mRNA Translation: BAE38409.1
AC166710 Genomic DNA No translation available.
CH466555 Genomic DNA Translation: EDL13176.1
CH466555 Genomic DNA Translation: EDL13177.1
BC018353 mRNA Translation: AAH18353.1
AF073991 Genomic DNA Translation: AAD29847.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS35804.1 [Q8VEK3-1]

NCBI Reference Sequences

More...
RefSeqi
NP_058085.2, NM_016805.2 [Q8VEK3-1]
XP_017177161.1, XM_017321672.1 [Q8VEK3-1]
XP_017177162.1, XM_017321673.1 [Q8VEK3-2]
XP_017177163.1, XM_017321674.1 [Q8VEK3-2]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000037748; ENSMUSP00000047571; ENSMUSG00000039630 [Q8VEK3-1]
ENSMUST00000161769; ENSMUSP00000124147; ENSMUSG00000039630 [Q8VEK3-2]
ENSMUST00000213673; ENSMUSP00000148926; ENSMUSG00000111145 [Q8VEK3-2]
ENSMUST00000216820; ENSMUSP00000150782; ENSMUSG00000111145 [Q8VEK3-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
51810

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:51810

UCSC genome browser

More...
UCSCi
uc011wxl.1 mouse [Q8VEK3-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
AK165844 mRNA Translation: BAE38409.1
AC166710 Genomic DNA No translation available.
CH466555 Genomic DNA Translation: EDL13176.1
CH466555 Genomic DNA Translation: EDL13177.1
BC018353 mRNA Translation: AAH18353.1
AF073991 Genomic DNA Translation: AAD29847.1
CCDSiCCDS35804.1 [Q8VEK3-1]
RefSeqiNP_058085.2, NM_016805.2 [Q8VEK3-1]
XP_017177161.1, XM_017321672.1 [Q8VEK3-1]
XP_017177162.1, XM_017321673.1 [Q8VEK3-2]
XP_017177163.1, XM_017321674.1 [Q8VEK3-2]

3D structure databases

SMRiQ8VEK3
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi206185, 18 interactors
ComplexPortaliCPX-1089 CRD-mediated mRNA stability complex
DIPiDIP-34257N
IntActiQ8VEK3, 7 interactors
STRINGi10090.ENSMUSP00000047571

PTM databases

iPTMnetiQ8VEK3
PhosphoSitePlusiQ8VEK3
SwissPalmiQ8VEK3

Proteomic databases

EPDiQ8VEK3
jPOSTiQ8VEK3
MaxQBiQ8VEK3
PaxDbiQ8VEK3
PeptideAtlasiQ8VEK3
PRIDEiQ8VEK3

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000037748; ENSMUSP00000047571; ENSMUSG00000039630 [Q8VEK3-1]
ENSMUST00000161769; ENSMUSP00000124147; ENSMUSG00000039630 [Q8VEK3-2]
ENSMUST00000213673; ENSMUSP00000148926; ENSMUSG00000111145 [Q8VEK3-2]
ENSMUST00000216820; ENSMUSP00000150782; ENSMUSG00000111145 [Q8VEK3-1]
GeneIDi51810
KEGGimmu:51810
UCSCiuc011wxl.1 mouse [Q8VEK3-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3192
MGIiMGI:1858195 Hnrnpu

Phylogenomic databases

eggNOGiKOG2242 Eukaryota
ENOG410Y1WQ LUCA
GeneTreeiENSGT00940000156546
HOGENOMiHOG000253920
InParanoidiQ8VEK3
KOiK12888
OMAiAFNQSWQ
OrthoDBi778148at2759
PhylomeDBiQ8VEK3
TreeFamiTF317301

Enzyme and pathway databases

ReactomeiR-MMU-72163 mRNA Splicing - Major Pathway
R-MMU-72203 Processing of Capped Intron-Containing Pre-mRNA

Miscellaneous databases

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

More...
ChiTaRSi
Hnrnpu mouse

Protein Ontology

More...
PROi
PR:Q8VEK3

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000100725 Expressed in 20 organ(s), highest expression level in embryonic stem cell
ExpressionAtlasiQ8VEK3 baseline and differential
GenevisibleiQ8VEK3 MM

Family and domain databases

CDDicd12884 SPRY_hnRNP, 1 hit
Gene3Di1.10.720.30, 1 hit
InterProiView protein in InterPro
IPR001870 B30.2/SPRY
IPR013320 ConA-like_dom_sf
IPR026745 hnRNP_U
IPR027417 P-loop_NTPase
IPR003034 SAP_dom
IPR036361 SAP_dom_sf
IPR003877 SPRY_dom
IPR035778 SPRY_hnRNP_U
PANTHERiPTHR12381:SF11 PTHR12381:SF11, 1 hit
PfamiView protein in Pfam
PF02037 SAP, 1 hit
PF00622 SPRY, 1 hit
SMARTiView protein in SMART
SM00513 SAP, 1 hit
SM00449 SPRY, 1 hit
SUPFAMiSSF49899 SSF49899, 1 hit
SSF52540 SSF52540, 1 hit
SSF68906 SSF68906, 1 hit
PROSITEiView protein in PROSITE
PS50188 B302_SPRY, 1 hit
PS50800 SAP, 1 hit

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 nameiHNRPU_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: Q8VEK3
Secondary accession number(s): G3XA10, Q9R205
<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 3, 2009
Last sequence update: March 1, 2002
Last modified: June 5, 2019
This is version 151 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, Reference proteome

Documents

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