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Entry version 221 (16 Oct 2019)
Sequence version 6 (28 Jul 2009)
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Protein

Heterogeneous nuclear ribonucleoprotein U

Gene

HNRNPU

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 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:10490622, PubMed:18082603, PubMed:19029303, PubMed:22325991, PubMed:25986610, PubMed:28622508). 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 (PubMed:1324173, PubMed:8174554, PubMed:28622508). 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 (By similarity). Plays a role as a RNA polymerase II (Pol II) holoenzyme transcription regulator (PubMed:8174554, PubMed:9353307, PubMed:10490622, PubMed:15711563, PubMed:19617346, PubMed:23811339). 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 (PubMed:10490622, PubMed:15711563). 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 (PubMed:10490622). Positively regulates CBX5-induced transcriptional gene silencing and retention of CBX5 in the nucleus (PubMed:19617346). Negatively regulates glucocorticoid-mediated transcriptional activation (PubMed:9353307). Key regulator of transcription initiation and elongation in embryonic stem cells upon leukemia inhibitory factor (LIF) signaling (By similarity). Involved in the long non-coding RNA H19-mediated Pol II transcriptional repression (PubMed:23811339). Participates in the circadian regulation of the core clock component ARNTL/BMAL1 transcription (By similarity). Plays a role in the regulation of telomere length (PubMed:18082603). Plays a role as a global pre-mRNA alternative splicing modulator by regulating U2 small nuclear ribonucleoprotein (snRNP) biogenesis (PubMed:22325991). Plays a role in mRNA stability (PubMed:17174306, PubMed:17289661, PubMed:19029303). Component of the CRD-mediated complex that promotes MYC mRNA stabilization (PubMed:19029303). 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) (PubMed:17174306). Plays a role in mitotic cell cycle regulation (PubMed:21242313, PubMed:25986610). Involved in the formation of stable mitotic spindle microtubules (MTs) attachment to kinetochore, spindle organization and chromosome congression (PubMed:21242313). Phosphorylation at Ser-59 by PLK1 is required for chromosome alignement and segregation and progression through mitosis (PubMed:25986610). Contributes also to the targeting of AURKA to mitotic spindle MTs (PubMed:21242313). Binds to double- and single-stranded DNA and RNA, poly(A), poly(C) and poly(G) oligoribonucleotides (PubMed:1628625, PubMed:8068679, PubMed:8174554, PubMed:9204873, PubMed:9405365). Binds to chromatin-associated RNAs (caRNAs) (PubMed:28622508). Associates with chromatin to scaffold/matrix attachment region (S/MAR) elements in a chromatin-associated RNAs (caRNAs)-dependent manner (PubMed:7509195, PubMed:1324173, PubMed:9204873, PubMed:9405365, PubMed:10671544, PubMed:11003645, PubMed:11909954, PubMed:28622508). Binds to the Xist RNA (PubMed:26244333). Binds the long non-coding H19 RNA (PubMed:23811339). Binds to SMN1/2 pre-mRNAs at G/U-rich regions (PubMed:22325991). Binds to small nuclear RNAs (snRNAs) (PubMed:22325991). Binds to the 3'-UTR of TNFA mRNA (PubMed:17174306). 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) (By similarity). Also negatively regulates embryonic stem cell differentiation upon LIF signaling (By similarity). Required for embryonic development (By similarity). 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 (By similarity).By similarity24 Publications
(Microbial infection) Negatively regulates immunodeficiency virus type 1 (HIV-1) replication by preventing the accumulation of viral mRNA transcripts in the cytoplasm.1 Publication

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 bindingi504 – 511ATPSequence 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-HSA-72163 mRNA Splicing - Major Pathway
R-HSA-72203 Processing of Capped Intron-Containing Pre-mRNA

SIGNOR Signaling Network Open Resource

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SIGNORi
Q00839

<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 U1 Publication
Short name:
hnRNP U1 Publication
Alternative name(s):
GRIP1201 Publication
Nuclear p120 ribonucleoprotein1 Publication
Scaffold-attachment factor A2 Publications
Short name:
SAF-A2 Publications
p1201 Publication
pp1201 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:C1orf199Imported, HNRPUImported, SAFA, U21.1
<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

Human Gene Nomenclature Database

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HGNCi
HGNC:5048 HNRNPU

Online Mendelian Inheritance in Man (OMIM)

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MIMi
602869 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q00839

<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 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

Epileptic encephalopathy, early infantile, 54 (EIEE54)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of epileptic encephalopathy, a heterogeneous group of severe childhood onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078622171 – 825Missing in EIEE54. 1 PublicationAdd BLAST655
Natural variantiVAR_078623805 – 825Missing in EIEE54; unknown pathological significance. 1 PublicationAdd BLAST21

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>Mutagenesisi59S → A: No change in interaction with AURKA, PLK1 and TPX2. Increases mitotic chromosome misalignment and chromosome segregation defects and time required to progress through mitosis. 1 Publication1
Mutagenesisi59S → E: Increases mitotic chromosome misalignment and chromosome segregation defects and decreases time required to progress through mitosis. 1 Publication1
Mutagenesisi100D → A: No cleavage by caspases during apoptosis. Inhibits CASP3-induced cleavage in vitro. 1 Publication1
Mutagenesisi616 – 620RTQKK → ATQAA: Loss of actin-binding. 1 Publication5

Keywords - Diseasei

Disease mutation, Epilepsy

Organism-specific databases

DisGeNET

More...
DisGeNETi
3192

MalaCards human disease database

More...
MalaCardsi
HNRNPU
MIMi617391 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000153187

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

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Orphaneti
238769 1q44 microdeletion syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA162391486

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
Q00839

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
HNRNPU

Domain mapping of disease mutations (DMDM)

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DMDMi
254763463

<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 methionineiRemovedCombined sources3 Publications
<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_00000818722 – 825Heterogeneous nuclear ribonucleoprotein UAdd BLAST824

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-acetylserine; partialCombined sources2 Publications1
Modified residuei4PhosphoserineCombined sources1
Modified residuei17N6-acetyllysineBy similarity1
Modified residuei21N6-acetyllysineBy similarity1
Modified residuei59Phosphoserine; by PLK1Combined sources1 Publication1
Modified residuei66PhosphoserineCombined sources1
Modified residuei186N6-acetyllysineBy similarity1
Modified residuei187ADP-ribosylserine1 Publication1
Modified residuei255CitrullineBy similarity1
Modified residuei265N6-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-linki265Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki265Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei266PhosphotyrosineBy similarity1
Modified residuei267PhosphoserineCombined sources1
Modified residuei271PhosphoserineCombined sources1
Modified residuei286PhosphothreonineCombined sources1
Modified residuei352N6-acetyllysineCombined sources1
Cross-linki495Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei516N6-acetyllysine; alternateCombined sources1
Cross-linki516Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei524N6-acetyllysine; alternateCombined sources1
Cross-linki524Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei532PhosphothreonineCombined sources1
Cross-linki536Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei551N6-acetyllysineCombined sources1
Modified residuei565N6-acetyllysine; alternateCombined sources1
Cross-linki565Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki574Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei582PhosphothreonineCombined sources1
Cross-linki609Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki626Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei635N6-acetyllysine; alternateCombined sources1
Cross-linki635Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki664Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki670Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei702Omega-N-methylarginineCombined sources1
Modified residuei715Asymmetric dimethylarginineBy similarity1
Modified residuei720Asymmetric dimethylarginineBy similarity1
Modified residuei727Asymmetric dimethylarginineBy similarity1
Modified residuei733Asymmetric dimethylarginine; alternateCombined sources1
Modified residuei733Omega-N-methylarginine; alternateBy similarity1
Modified residuei739Asymmetric dimethylarginine; alternateCombined sources1
Modified residuei739Dimethylated arginine; in A2780 ovarian carcinoma cell line1 Publication1
Modified residuei739Omega-N-methylarginine; alternateCombined sources1
Modified residuei755Asymmetric dimethylarginineCombined sources1
Modified residuei762Asymmetric dimethylarginineCombined sources1
Modified residuei814N6-acetyllysine; alternateCombined sources1
Cross-linki814Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Isoform 2 (identifier: Q00839-2)
Modified residuei215N6-acetyllysineCombined 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

Cleaved at Asp-100 by CASP3 during T-cell apoptosis, resulting in a loss of DNA- and chromatin-binding activities (PubMed:9405365, PubMed:10671544).2 Publications
Extensively phosphorylated (PubMed:7993898). Phosphorylated on Ser-59 by PLK1 and dephosphorylated by protein phosphatase 2A (PP2A) in mitosis (PubMed:25986610).2 Publications
Arg-739 is dimethylated, probably to asymmetric dimethylarginine (Ref. 8). Arg-733 is dimethylated, probably to asymmetric dimethylarginine (By similarity).By similarity1 Publication
Citrullinated by PADI4.By similarity

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>Sitei100 – 101Cleavage; by CASP32 Publications2

Keywords - PTMi

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

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q00839

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q00839

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q00839

MaxQB - The MaxQuant DataBase

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MaxQBi
Q00839

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

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PaxDbi
Q00839

PeptideAtlas

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PeptideAtlasi
Q00839

PRoteomics IDEntifications database

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PRIDEi
Q00839

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
57874 [Q00839-1]
57875 [Q00839-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q00839

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

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PhosphoSitePlusi
Q00839

SwissPalm database of S-palmitoylation events

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SwissPalmi
Q00839

<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

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000153187 Expressed in 240 organ(s), highest expression level in female gonad

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q00839 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q00839 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB011532
HPA041057
HPA058707

<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 (PubMed:28622508). ATP hydrolysis is required to cycle from an oligomeric to monomeric state to compact chromatin (PubMed:28622508).

Component of the coding region determinant (CRD)-mediated complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1 (PubMed:19029303). Identified in the spliceosome C complex (PubMed:11991638).

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (PubMed:17289661, PubMed:19029303). Associates with heterogeneous nuclear ribonucleoprotein (hnRNP) particles (PubMed:8174554, PubMed:9204873, PubMed:9405365, PubMed:11909954). 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:10490622). 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 (PubMed:10490622). Associates with the telomerase holoenzyme complex (PubMed:18082603). Associates with spindle microtubules (MTs) in a TPX2-dependent manner (PubMed:21242313).

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 (PubMed:15711563, PubMed:23811339).

Interacts with AURKA (PubMed:21242313, PubMed:25986610).

Interacts (via C-terminus) with CBX5; this interaction is, at least in part, RNA-dependent (PubMed:19617346).

Interacts with CR2 (PubMed:7753047).

Interacts with CRY1 (By similarity).

Interacts (via C-terminus) with EP300; this interaction enhances DNA-binding to nuclear scaffold/matrix attachment region (S/MAR) elements (PubMed:11909954).

Interacts with ERBB4 (PubMed:20858735).

Interacts with GEMIN5 (PubMed:25911097).

Interacts with IGF2BP1 (PubMed:17289661, PubMed:23640942).

Interacts with IGF2BP2 and IGF2BP3 (PubMed:23640942).

Interacts with NCL; this interaction occurs during mitosis (PubMed:21242313).

Interacts (via C-terminus) with NR3C1 (via C-terminus) (PubMed:9353307).

Interacts with PLK1; this interaction induces phosphorylation of HNRNPU at Ser-59 in mitosis (PubMed:25986610).

Interacts with POU3F4 (PubMed:9105675).

Interacts with SMARCA4; this interaction occurs in embryonic stem cells and stimulates global Pol II-mediated transcription.

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 (By similarity).

Interacts with TPX2; this interaction recruits HNRNPU to spindle microtubules (MTs) (PubMed:21242313, PubMed:25986610).

Interacts with UBQLN2 (PubMed:25616961).

Interacts (via RNA-binding RGG-box region) with ZBTB7B; the interaction facilitates the recruitment of long non-coding RNA Blnc1 by ZBTB7B (By similarity).

Interacts with ERCC6 (PubMed:26030138).

By similarity23 Publications

(Microbial infection) Interacts with HIV-1 protein Rev.

1 Publication

<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
109433, 577 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1080 CRD-mediated mRNA stability complex

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q00839

Database of interacting proteins

More...
DIPi
DIP-684N

Protein interaction database and analysis system

More...
IntActi
Q00839, 374 interactors

Molecular INTeraction database

More...
MINTi
Q00839

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000283179

<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
Q00839

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q00839

<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 annotation2 PublicationsAdd BLAST35
Domaini267 – 464B30.2/SPRYPROSITE-ProRule annotationAdd BLAST198

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>Regioni488 – 672ATPase domain1 PublicationAdd BLAST185
Regioni611 – 626Actin-binding1 PublicationAdd BLAST16
Regioni714 – 739RNA-binding RGG-box2 PublicationsAdd BLAST26

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 – 160Asp/Glu-rich (acidic)Add BLAST159
Compositional biasi84 – 94Poly-GluAdd BLAST11
Compositional biasi161 – 209Gln-richAdd BLAST49
Compositional biasi703 – 825Gly-richAdd BLAST123
Compositional biasi740 – 750Poly-GlyAdd BLAST11

<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 (PubMed:9405365, PubMed:11003645). The RNA-binding RGG-box region is necessary for its association with inactive X chromosome (Xi) regions and to chromatin-associated RNAs (caRNAs) (PubMed:14608463, PubMed:28622508). Both the DNA-binding domain SAP and the RNA-binding RGG-box region are necessary for the localization of Xist RNA on the Xi (By similarity). The ATPase and RNA-binding RGG-box regions are necessary for oligomerization (PubMed:28622508).By similarity4 Publications

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IR1W Eukaryota
ENOG410Y1WQ LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000156546

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000253920

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q00839

KEGG Orthology (KO)

More...
KOi
K12888

Identification of Orthologs from Complete Genome Data

More...
OMAi
QYQPGYY

Database of Orthologous Groups

More...
OrthoDBi
778148at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q00839

TreeFam database of animal gene trees

More...
TreeFami
TF317301

Family and domain databases

Conserved Domains Database

More...
CDDi
cd12884 SPRY_hnRNP, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.720.30, 1 hit

Integrated resource of protein families, domains and functional sites

More...
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

More...
PANTHERi
PTHR12381:SF11 PTHR12381:SF11, 1 hit

Pfam protein domain database

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

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49899 SSF49899, 1 hit
SSF52540 SSF52540, 1 hit
SSF68906 SSF68906, 1 hit

PROSITE; a protein domain and family database

More...
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 17 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q00839-1) [UniParc]FASTAAdd to basket
Also known as: Long

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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 KAELMERLQA ALDDEEAGGR
60 70 80 90 100
PAMEPGNGSL DLGGDSAGRS GAGLEQEAAA GGDEEEEEEE EEEEGISALD
110 120 130 140 150
GDQMELGEEN GAAGAADSGP MEEEEAASED ENGDDQGFQE GEDELGDEEE
160 170 180 190 200
GAGDENGHGE QQPQPPATQQ QQPQQQRGAA KEAAGKSSGP TSLFAVTVAP
210 220 230 240 250
PGARQGQQQA GGKKKAEGGG GGGRPGAPAA GDGKTEQKGG DKKRGVKRPR
260 270 280 290 300
EDHGRGYFEY IEENKYSRAK SPQPPVEEED EHFDDTVVCL DTYNCDLHFK
310 320 330 340 350
ISRDRLSASS LTMESFAFLW AGGRASYGVS KGKVCFEMKV TEKIPVRHLY
360 370 380 390 400
TKDIDIHEVR IGWSLTTSGM LLGEEEFSYG YSLKGIKTCN CETEDYGEKF
410 420 430 440 450
DENDVITCFA NFESDEVELS YAKNGQDLGV AFKISKEVLA GRPLFPHVLC
460 470 480 490 500
HNCAVEFNFG QKEKPYFPIP EEYTFIQNVP LEDRVRGPKG PEEKKDCEVV
510 520 530 540 550
MMIGLPGAGK TTWVTKHAAE NPGKYNILGT NTIMDKMMVA GFKKQMADTG
560 570 580 590 600
KLNTLLQRAP QCLGKFIEIA ARKKRNFILD QTNVSAAAQR RKMCLFAGFQ
610 620 630 640 650
RKAVVVCPKD EDYKQRTQKK AEVEGKDLPE HAVLKMKGNF TLPEVAECFD
660 670 680 690 700
EITYVELQKE EAQKLLEQYK EESKKALPPE KKQNTGSKKS NKNKSGKNQF
710 720 730 740 750
NRGGGHRGRG GFNMRGGNFR GGAPGNRGGY NRRGNMPQRG GGGGGSGGIG
760 770 780 790 800
YPYPRAPVFP GRGSYSNRGN YNRGGMPNRG NYNQNFRGRG NNRGYKNQSQ
810 820
GYNQWQQGQF WGQKPWSQHY HQGYY
Length:825
Mass (Da):90,584
Last modified:July 28, 2009 - v6
<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:i5D4EC4188436831F
GO
Isoform 2 (identifier: Q00839-2) [UniParc]FASTAAdd to basket
Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     213-231: Missing.

Show »
Length:806
Mass (Da):88,980
Checksum:iBCE1AD365501EDC1
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 17 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A1W2PP22A0A1W2PP22_HUMAN
Heterogeneous nuclear ribonucleopro...
HNRNPU
181Annotation 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>
Q5RI18Q5RI18_HUMAN
Heterogeneous nuclear ribonucleopro...
HNRNPU
602Annotation 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>
A0A1W2PPS1A0A1W2PPS1_HUMAN
Heterogeneous nuclear ribonucleopro...
HNRNPU
804Annotation 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>
A0A1X7SBS1A0A1X7SBS1_HUMAN
Heterogeneous nuclear ribonucleopro...
HNRNPU
744Annotation 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>
A0A1W2PP34A0A1W2PP34_HUMAN
Heterogeneous nuclear ribonucleopro...
HNRNPU
546Annotation 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>
A0A1W2PP35A0A1W2PP35_HUMAN
Heterogeneous nuclear ribonucleopro...
HNRNPU
728Annotation 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>
A0A1W2PPH7A0A1W2PPH7_HUMAN
Heterogeneous nuclear ribonucleopro...
HNRNPU
549Annotation 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>
A0A1W2PPL4A0A1W2PPL4_HUMAN
Heterogeneous nuclear ribonucleopro...
HNRNPU
547Annotation 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>
A0A1W2PQ74A0A1W2PQ74_HUMAN
Heterogeneous nuclear ribonucleopro...
HNRNPU
372Annotation 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>
A0A1W2PQL0A0A1W2PQL0_HUMAN
Heterogeneous nuclear ribonucleopro...
HNRNPU
527Annotation 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>
There are more potential isoformsShow all

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAC19382 differs from that shown. Aberrant splicing.Curated

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 conflicti603A → V in AAH07950 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_078622171 – 825Missing in EIEE54. 1 PublicationAdd BLAST655
Natural variantiVAR_014712712F → L2 PublicationsCorresponds to variant dbSNP:rs1052660Ensembl.1
Natural variantiVAR_078623805 – 825Missing in EIEE54; unknown pathological significance. 1 PublicationAdd BLAST21

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_005846213 – 231Missing in isoform 2. 3 PublicationsAdd BLAST19

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
X65488 mRNA Translation: CAA46472.1
AF068846 mRNA Translation: AAC19382.1 Sequence problems.
BX323046 Genomic DNA No translation available.
BC003367 mRNA Translation: AAH03367.1
BC003621 mRNA Translation: AAH03621.1
BC007950 mRNA Translation: AAH07950.2
BC024767 mRNA Translation: AAH24767.1
BC034925 mRNA Translation: AAH34925.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS31081.1 [Q00839-2]
CCDS41479.1 [Q00839-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
S22765

NCBI Reference Sequences

More...
RefSeqi
NP_004492.2, NM_004501.3 [Q00839-2]
NP_114032.2, NM_031844.2 [Q00839-1]
XP_016856604.1, XM_017001115.1
XP_016856605.1, XM_017001116.1
XP_016856606.1, XM_017001117.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000444376; ENSP00000393151; ENSG00000153187 [Q00839-2]
ENST00000640218; ENSP00000491215; ENSG00000153187 [Q00839-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
3192

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:3192

UCSC genome browser

More...
UCSCi
uc001iaz.2 human [Q00839-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<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
X65488 mRNA Translation: CAA46472.1
AF068846 mRNA Translation: AAC19382.1 Sequence problems.
BX323046 Genomic DNA No translation available.
BC003367 mRNA Translation: AAH03367.1
BC003621 mRNA Translation: AAH03621.1
BC007950 mRNA Translation: AAH07950.2
BC024767 mRNA Translation: AAH24767.1
BC034925 mRNA Translation: AAH34925.1
CCDSiCCDS31081.1 [Q00839-2]
CCDS41479.1 [Q00839-1]
PIRiS22765
RefSeqiNP_004492.2, NM_004501.3 [Q00839-2]
NP_114032.2, NM_031844.2 [Q00839-1]
XP_016856604.1, XM_017001115.1
XP_016856605.1, XM_017001116.1
XP_016856606.1, XM_017001117.1

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
1ZRJNMR-A23-42[»]
SMRiQ00839
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi109433, 577 interactors
ComplexPortaliCPX-1080 CRD-mediated mRNA stability complex
CORUMiQ00839
DIPiDIP-684N
IntActiQ00839, 374 interactors
MINTiQ00839
STRINGi9606.ENSP00000283179

PTM databases

iPTMnetiQ00839
PhosphoSitePlusiQ00839
SwissPalmiQ00839

Polymorphism and mutation databases

BioMutaiHNRNPU
DMDMi254763463

Proteomic databases

EPDiQ00839
jPOSTiQ00839
MassIVEiQ00839
MaxQBiQ00839
PaxDbiQ00839
PeptideAtlasiQ00839
PRIDEiQ00839
ProteomicsDBi57874 [Q00839-1]
57875 [Q00839-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
3192

Genome annotation databases

EnsembliENST00000444376; ENSP00000393151; ENSG00000153187 [Q00839-2]
ENST00000640218; ENSP00000491215; ENSG00000153187 [Q00839-1]
GeneIDi3192
KEGGihsa:3192
UCSCiuc001iaz.2 human [Q00839-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3192
DisGeNETi3192

GeneCards: human genes, protein and diseases

More...
GeneCardsi
HNRNPU
HGNCiHGNC:5048 HNRNPU
HPAiCAB011532
HPA041057
HPA058707
MalaCardsiHNRNPU
MIMi602869 gene
617391 phenotype
neXtProtiNX_Q00839
OpenTargetsiENSG00000153187
Orphaneti238769 1q44 microdeletion syndrome
PharmGKBiPA162391486

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IR1W Eukaryota
ENOG410Y1WQ LUCA
GeneTreeiENSGT00940000156546
HOGENOMiHOG000253920
InParanoidiQ00839
KOiK12888
OMAiQYQPGYY
OrthoDBi778148at2759
PhylomeDBiQ00839
TreeFamiTF317301

Enzyme and pathway databases

ReactomeiR-HSA-72163 mRNA Splicing - Major Pathway
R-HSA-72203 Processing of Capped Intron-Containing Pre-mRNA
SIGNORiQ00839

Miscellaneous databases

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

More...
ChiTaRSi
HNRNPU human
EvolutionaryTraceiQ00839

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
HNRPU

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

More...
GenomeRNAii
3192
PharosiQ00839

Protein Ontology

More...
PROi
PR:Q00839

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000153187 Expressed in 240 organ(s), highest expression level in female gonad
ExpressionAtlasiQ00839 baseline and differential
GenevisibleiQ00839 HS

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...

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 nameiHNRPU_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: Q00839
Secondary accession number(s): O75507
, Q8N174, Q96HY9, Q9BQ09
<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: April 1, 1993
Last sequence update: July 28, 2009
Last modified: October 16, 2019
This is version 221 of the entry and version 6 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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