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Entry version 214 (18 Sep 2019)
Sequence version 2 (01 Nov 1991)
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Protein

Heterogeneous nuclear ribonucleoproteins A2/B1

Gene

HNRNPA2B1

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

Heterogeneous nuclear ribonucleoprotein (hnRNP) that associates with nascent pre-mRNAs, packaging them into hnRNP particles. The hnRNP particle arrangement on nascent hnRNA is non-random and sequence-dependent and serves to condense and stabilize the transcripts and minimize tangling and knotting. Packaging plays a role in various processes such as transcription, pre-mRNA processing, RNA nuclear export, subcellular location, mRNA translation and stability of mature mRNAs (PubMed:19099192). Forms hnRNP particles with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus. Involved in transport of specific mRNAs to the cytoplasm in oligodendrocytes and neurons: acts by specifically recognizing and binding the A2RE (21 nucleotide hnRNP A2 response element) or the A2RE11 (derivative 11 nucleotide oligonucleotide) sequence motifs present on some mRNAs, and promotes their transport to the cytoplasm (PubMed:10567417). Specifically binds single-stranded telomeric DNA sequences, protecting telomeric DNA repeat against endonuclease digestion (By similarity). Also binds other RNA molecules, such as primary miRNA (pri-miRNAs): acts as a nuclear 'reader' of the N6-methyladenosine (m6A) mark by specifically recognizing and binding a subset of nuclear m6A-containing pri-miRNAs. Binding to m6A-containing pri-miRNAs promotes pri-miRNA processing by enhancing binding of DGCR8 to pri-miRNA transcripts (PubMed:26321680). Involved in miRNA sorting into exosomes following sumoylation, possibly by binding (m6A)-containing pre-miRNAs (PubMed:24356509). Acts as a regulator of efficiency of mRNA splicing, possibly by binding to m6A-containing pre-mRNAs (PubMed:26321680).1 PublicationBy similarity3 Publications
(Microbial infection) Involved in the transport of HIV-1 genomic RNA out of the nucleus, to the microtubule organizing center (MTOC), and then from the MTOC to the cytoplasm: acts by specifically recognizing and binding the A2RE (21 nucleotide hnRNP A2 response element) sequence motifs present on HIV-1 genomic RNA, and promotes its transport.2 Publications

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

GO - Biological processi

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

Molecular functionRibonucleoprotein, RNA-binding
Biological processmRNA processing, mRNA splicing, mRNA transport, Transport

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
R-HSA-8950505 Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P22626

<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 ribonucleoproteins A2/B1
Short name:
hnRNP A2/B1
<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:HNRNPA2B1
Synonyms:HNRPA2B1
<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 7

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:5033 HNRNPA2B1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
600124 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P22626

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

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

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted, 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

Inclusion body myopathy with early-onset Paget disease with or without frontotemporal dementia 2 (IBMPFD2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disease characterized by disabling muscle weakness clinically resembling to limb girdle muscular dystrophy, osteolytic bone lesions consistent with Paget disease, and premature frontotemporal dementia. Clinical features show incomplete penetrance.
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_070591302D → V in IBMPFD2. 1 PublicationCorresponds to variant dbSNP:rs397515326EnsemblClinVar.1

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>Mutagenesisi207F → S: Does not affect hydrogel-binding. 1 Publication1
Mutagenesisi209F → S: Does not affect hydrogel-binding. 1 Publication1
Mutagenesisi219F → S: Does not affect hydrogel-binding. 1 Publication1
Mutagenesisi227F → S: Does not affect hydrogel-binding. 1 Publication1
Mutagenesisi234Y → S: Does not affect hydrogel-binding. 1 Publication1
Mutagenesisi240F → S: Does not affect hydrogel-binding. 1 Publication1
Mutagenesisi244Y → S: Does not affect hydrogel-binding. 1 Publication1
Mutagenesisi247Y → S: Slightly affects hydrogel-binding. 1 Publication1
Mutagenesisi256F → S: Does not affect hydrogel-binding. 1 Publication1
Mutagenesisi262Y → S: Slightly affects hydrogel-binding. 1 Publication1
Mutagenesisi269Y → S: Does not affect hydrogel-binding. 1 Publication1
Mutagenesisi276Y → S: Impairs hydrogel-binding. 1 Publication1
Mutagenesisi283Y → S: Slightly affects hydrogel-binding. 1 Publication1
Mutagenesisi287Y → S: Does not affect hydrogel-binding. 1 Publication1
Mutagenesisi290Y → S: Impairs hydrogel-binding. 1 Publication1
Mutagenesisi295Y → S: Impairs hydrogel-binding. 1 Publication1
Mutagenesisi300Y → S: Slightly affects hydrogel-binding. 1 Publication1
Mutagenesisi303F → S: Impairs hydrogel-binding. 1 Publication1
Mutagenesisi306Y → S: Slightly affects hydrogel-binding. 1 Publication1
Mutagenesisi313Y → S: Slightly affects hydrogel-binding. 1 Publication1
Mutagenesisi321F → S: Impairs hydrogel-binding. 1 Publication1
Mutagenesisi331Y → S: Impairs hydrogel-binding. 1 Publication1
Mutagenesisi336Y → S: Slightly affects hydrogel-binding. 1 Publication1
Mutagenesisi347Y → S: Does not affect hydrogel-binding. 1 Publication1
Mutagenesisi353Y → S: Does not affect hydrogel-binding. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

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DisGeNETi
3181

MalaCards human disease database

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MalaCardsi
HNRNPA2B1
MIMi615422 phenotype

Open Targets

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OpenTargetsi
ENSG00000122566

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

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Orphaneti
52430 Inclusion body myopathy with Paget disease of bone and frontotemporal dementia

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA162391140

Chemistry databases

Drug and drug target database

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DrugBanki
DB11638 Artenimol
DB09130 Copper

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
HNRNPA2B1

Domain mapping of disease mutations (DMDM)

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DMDMi
133257

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000818361 – 353Heterogeneous nuclear ribonucleoproteins A2/B1Add BLAST353

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 residuei1N-acetylmethionineCombined sources1 Publication1
Modified residuei4PhosphothreonineCombined 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-linki22Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei29PhosphoserineCombined sources1
Modified residuei38Omega-N-methylarginineBy similarity1
Modified residuei85PhosphoserineCombined sources1
Modified residuei104N6,N6-dimethyllysine; alternate1 Publication1
Cross-linki104Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki112Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei140PhosphothreonineCombined sources1
Modified residuei149PhosphoserineCombined sources1
Cross-linki152Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei159PhosphothreonineCombined sources1
Modified residuei168N6-acetyllysine; alternateCombined sources1
Cross-linki168Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei173N6-acetyllysine; alternateCombined sources1
Cross-linki173Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei176PhosphothreonineCombined sources1
Cross-linki186Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei189PhosphoserineCombined sources1
Modified residuei201PhosphoserineCombined sources1
Modified residuei203Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei203Dimethylated arginine; alternate1 Publication1
Modified residuei203Omega-N-methylarginine; alternateCombined sources1 Publication1
Modified residuei212PhosphoserineCombined sources1
Modified residuei213Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei213Dimethylated arginine; alternate1 Publication1
Modified residuei213Omega-N-methylarginine; alternateCombined sources1 Publication1
Modified residuei225PhosphoserineCombined sources1
Modified residuei228Omega-N-methylarginineCombined sources1
Modified residuei231PhosphoserineCombined sources1
Modified residuei236PhosphoserineCombined sources1
Modified residuei238Omega-N-methylarginineCombined sources1
Modified residuei259PhosphoserineCombined sources1
Modified residuei266Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei266Omega-N-methylarginine; alternateCombined sources1
Modified residuei324PhosphoserineCombined sources1
Modified residuei325Omega-N-methylarginineCombined sources1
Modified residuei331PhosphotyrosineCombined sources1
Modified residuei341PhosphoserineCombined sources1
Modified residuei344PhosphoserineCombined sources1
Modified residuei347PhosphotyrosineCombined sources1
Modified residuei350Omega-N-methylarginineCombined sources1
Isoform A2 (identifier: P22626-2)
Cross-linki5Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

<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

Sumoylated in exosomes, promoting miRNAs-binding.1 Publication
Asymmetric dimethylation at Arg-266 constitutes the major methylation site (By similarity). According to a report, methylation affects subcellular location and promotes nuclear localization (PubMed:10772824). According to another report, methylation at Arg-266 does not influence nucleocytoplasmic shuttling (By similarity).By similarity1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P22626

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P22626

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
P22626

MaxQB - The MaxQuant DataBase

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MaxQBi
P22626

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

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PaxDbi
P22626

PeptideAtlas

More...
PeptideAtlasi
P22626

PRoteomics IDEntifications database

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PRIDEi
P22626

ProteomicsDB human proteome resource

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ProteomicsDBi
54010 [P22626-1]
54011 [P22626-2]

Consortium for Top Down Proteomics

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TopDownProteomicsi
P22626-1 [P22626-1]
P22626-2 [P22626-2]

2D gel databases

REPRODUCTION-2DPAGE

More...
REPRODUCTION-2DPAGEi
IPI00396378
IPI00414696
P22626

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

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SWISS-2DPAGEi
P22626

University College Dublin 2-DE Proteome Database

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UCD-2DPAGEi
P22626

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P22626

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

More...
PhosphoSitePlusi
P22626

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P22626

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P22626

<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

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Bgeei
ENSG00000122566 Expressed in 241 organ(s), highest expression level in oviduct epithelium

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P22626 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P22626 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB012403
HPA001666
HPA005812
HPA065537

<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

Identified in the spliceosome C complex (PubMed:11991638).

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (PubMed:17289661).

Interacts with IGF2BP1 (PubMed:17289661).

Interacts with C9orf72 (PubMed:24549040).

Interacts with DGCR8 (PubMed:26321680).

Interacts with TARDBP (PubMed:19429692).

Interacts with CKAP5 (PubMed:15703215).

6 Publications

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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
109422, 314 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P22626

Database of interacting proteins

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DIPi
DIP-32877N

Protein interaction database and analysis system

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IntActi
P22626, 151 interactors

Molecular INTeraction database

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MINTi
P22626

STRING: functional protein association networks

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STRINGi
9606.ENSP00000346694

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

Secondary structure

1353
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
P22626

Database of comparative protein structure models

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ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P22626

<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>Domaini21 – 104RRM 1PROSITE-ProRule annotationAdd BLAST84
Domaini112 – 191RRM 2PROSITE-ProRule annotationAdd BLAST80

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>Regioni193 – 353Low complexity (LC) region1 PublicationAdd BLAST161
Regioni308 – 347Nuclear targeting sequenceBy similarityAdd BLAST40

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi9 – 15Nuclear localization signalSequence analysis7

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 biasi202 – 353Gly-richAdd BLAST152

<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 low complexity (LC) region is intrinsically disordered. When incubated at high concentration, it is able to polymerize into labile, amyloid-like fibers and form cross-beta polymerization structures, probably driving the formation of hydrogels. In contrast to irreversible, pathogenic amyloids, the fibers polymerized from LC regions disassemble upon dilution. A number of evidence suggests that formation of cross-beta structures by LC regions mediate the formation of RNA granules, liquid-like droplets, and hydrogels.1 Publication

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0118 Eukaryota
COG0724 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000154431

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000234442

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P22626

KEGG Orthology (KO)

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KOi
K13158

Identification of Orthologs from Complete Genome Data

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OMAi
SRARSYN

Database of Orthologous Groups

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OrthoDBi
1202220at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P22626

TreeFam database of animal gene trees

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TreeFami
TF351342

Family and domain databases

Conserved Domains Database

More...
CDDi
cd12762 RRM1_hnRNPA2B1, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.70.330, 2 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR034489 hnRNP_A2/B1
IPR034486 hnRNPA2B1_RRM1
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR035979 RBD_domain_sf
IPR000504 RRM_dom

The PANTHER Classification System

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PANTHERi
PTHR15241:SF113 PTHR15241:SF113, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00076 RRM_1, 2 hits

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00360 RRM, 2 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF54928 SSF54928, 2 hits

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50102 RRM, 2 hits

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

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

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform B1 (identifier: P22626-1) [UniParc]FASTAAdd to basket
Also known as: hnRNP B1

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
MEKTLETVPL ERKKREKEQF RKLFIGGLSF ETTEESLRNY YEQWGKLTDC
60 70 80 90 100
VVMRDPASKR SRGFGFVTFS SMAEVDAAMA ARPHSIDGRV VEPKRAVARE
110 120 130 140 150
ESGKPGAHVT VKKLFVGGIK EDTEEHHLRD YFEEYGKIDT IEIITDRQSG
160 170 180 190 200
KKRGFGFVTF DDHDPVDKIV LQKYHTINGH NAEVRKALSR QEMQEVQSSR
210 220 230 240 250
SGRGGNFGFG DSRGGGGNFG PGPGSNFRGG SDGYGSGRGF GDGYNGYGGG
260 270 280 290 300
PGGGNFGGSP GYGGGRGGYG GGGPGYGNQG GGYGGGYDNY GGGNYGSGNY
310 320 330 340 350
NDFGNYNQQP SNYGPMKSGN FGGSRNMGGP YGGGNYGPGG SGGSGGYGGR

SRY
Length:353
Mass (Da):37,430
Last modified:November 1, 1991 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4C2560A3D8E99D62
GO
Isoform A2 (identifier: P22626-2) [UniParc]FASTAAdd to basket
Also known as: hnRNP A2

The sequence of this isoform differs from the canonical sequence as follows:
     3-14: Missing.

Show »
Length:341
Mass (Da):36,006
Checksum:i39E8AB6ED874FA7C
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087WUI2A0A087WUI2_HUMAN
Heterogeneous nuclear ribonucleopro...
HNRNPA2B1
261Annotation score:

Annotation score:1 out of 5

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti205G → S in BAF82118 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_070591302D → V in IBMPFD2. 1 PublicationCorresponds to variant dbSNP:rs397515326EnsemblClinVar.1

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_0058303 – 14Missing in isoform A2. 1 PublicationAdd BLAST12

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
M29064 mRNA Translation: AAA60271.1
M29065 mRNA Translation: AAA36574.1
U09123
, U09120, U09121, U09122 Genomic DNA Translation: AAB60650.1
D28877 Genomic DNA Translation: BAA06031.1
D28877 Genomic DNA Translation: BAA06032.1
AK289429 mRNA Translation: BAF82118.1
CH471073 Genomic DNA Translation: EAW93835.1
CH471073 Genomic DNA Translation: EAW93836.1
CH471073 Genomic DNA Translation: EAW93837.1
CH471073 Genomic DNA Translation: EAW93839.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS43557.1 [P22626-1]
CCDS5397.1 [P22626-2]

Protein sequence database of the Protein Information Resource

More...
PIRi
A56845 B34504

NCBI Reference Sequences

More...
RefSeqi
NP_002128.1, NM_002137.3 [P22626-2]
NP_112533.1, NM_031243.2 [P22626-1]
XP_005249786.1, XM_005249729.1 [P22626-1]
XP_016867598.1, XM_017012109.1 [P22626-2]
XP_016867599.1, XM_017012110.1 [P22626-2]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000354667; ENSP00000346694; ENSG00000122566 [P22626-1]
ENST00000356674; ENSP00000349101; ENSG00000122566 [P22626-2]
ENST00000360787; ENSP00000354021; ENSG00000122566 [P22626-1]
ENST00000608362; ENSP00000497298; ENSG00000122566 [P22626-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
3181

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:3181

UCSC genome browser

More...
UCSCi
uc003sxr.5 human [P22626-1]

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
M29064 mRNA Translation: AAA60271.1
M29065 mRNA Translation: AAA36574.1
U09123
, U09120, U09121, U09122 Genomic DNA Translation: AAB60650.1
D28877 Genomic DNA Translation: BAA06031.1
D28877 Genomic DNA Translation: BAA06032.1
AK289429 mRNA Translation: BAF82118.1
CH471073 Genomic DNA Translation: EAW93835.1
CH471073 Genomic DNA Translation: EAW93836.1
CH471073 Genomic DNA Translation: EAW93837.1
CH471073 Genomic DNA Translation: EAW93839.1
CCDSiCCDS43557.1 [P22626-1]
CCDS5397.1 [P22626-2]
PIRiA56845 B34504
RefSeqiNP_002128.1, NM_002137.3 [P22626-2]
NP_112533.1, NM_031243.2 [P22626-1]
XP_005249786.1, XM_005249729.1 [P22626-1]
XP_016867598.1, XM_017012109.1 [P22626-2]
XP_016867599.1, XM_017012110.1 [P22626-2]

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
1X4BNMR-A1-103[»]
5EN1X-ray2.58A12-195[»]
5HO4X-ray1.85A15-193[»]
5WWEX-ray2.40A12-195[»]
5WWFX-ray2.15A/C12-195[»]
5WWGX-ray2.03A12-195[»]
SMRiP22626
ModBaseiSearch...

Protein-protein interaction databases

BioGridi109422, 314 interactors
CORUMiP22626
DIPiDIP-32877N
IntActiP22626, 151 interactors
MINTiP22626
STRINGi9606.ENSP00000346694

Chemistry databases

DrugBankiDB11638 Artenimol
DB09130 Copper

PTM databases

iPTMnetiP22626
PhosphoSitePlusiP22626
SwissPalmiP22626

Polymorphism and mutation databases

BioMutaiHNRNPA2B1
DMDMi133257

2D gel databases

REPRODUCTION-2DPAGEiIPI00396378
IPI00414696
P22626
SWISS-2DPAGEiP22626
UCD-2DPAGEiP22626

Proteomic databases

EPDiP22626
jPOSTiP22626
MassIVEiP22626
MaxQBiP22626
PaxDbiP22626
PeptideAtlasiP22626
PRIDEiP22626
ProteomicsDBi54010 [P22626-1]
54011 [P22626-2]
TopDownProteomicsiP22626-1 [P22626-1]
P22626-2 [P22626-2]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000354667; ENSP00000346694; ENSG00000122566 [P22626-1]
ENST00000356674; ENSP00000349101; ENSG00000122566 [P22626-2]
ENST00000360787; ENSP00000354021; ENSG00000122566 [P22626-1]
ENST00000608362; ENSP00000497298; ENSG00000122566 [P22626-2]
GeneIDi3181
KEGGihsa:3181
UCSCiuc003sxr.5 human [P22626-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3181
DisGeNETi3181

GeneCards: human genes, protein and diseases

More...
GeneCardsi
HNRNPA2B1
HGNCiHGNC:5033 HNRNPA2B1
HPAiCAB012403
HPA001666
HPA005812
HPA065537
MalaCardsiHNRNPA2B1
MIMi600124 gene
615422 phenotype
neXtProtiNX_P22626
OpenTargetsiENSG00000122566
Orphaneti52430 Inclusion body myopathy with Paget disease of bone and frontotemporal dementia
PharmGKBiPA162391140

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0118 Eukaryota
COG0724 LUCA
GeneTreeiENSGT00940000154431
HOGENOMiHOG000234442
InParanoidiP22626
KOiK13158
OMAiSRARSYN
OrthoDBi1202220at2759
PhylomeDBiP22626
TreeFamiTF351342

Enzyme and pathway databases

ReactomeiR-HSA-72163 mRNA Splicing - Major Pathway
R-HSA-72203 Processing of Capped Intron-Containing Pre-mRNA
R-HSA-8950505 Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation
SIGNORiP22626

Miscellaneous databases

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

More...
ChiTaRSi
HNRNPA2B1 human
EvolutionaryTraceiP22626

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
HNRPA2B1

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

More...
GenomeRNAii
3181

Pharos

More...
Pharosi
P22626
PMAP-CutDBiP22626

Protein Ontology

More...
PROi
PR:P22626

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000122566 Expressed in 241 organ(s), highest expression level in oviduct epithelium
ExpressionAtlasiP22626 baseline and differential
GenevisibleiP22626 HS

Family and domain databases

CDDicd12762 RRM1_hnRNPA2B1, 1 hit
Gene3Di3.30.70.330, 2 hits
InterProiView protein in InterPro
IPR034489 hnRNP_A2/B1
IPR034486 hnRNPA2B1_RRM1
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR035979 RBD_domain_sf
IPR000504 RRM_dom
PANTHERiPTHR15241:SF113 PTHR15241:SF113, 1 hit
PfamiView protein in Pfam
PF00076 RRM_1, 2 hits
SMARTiView protein in SMART
SM00360 RRM, 2 hits
SUPFAMiSSF54928 SSF54928, 2 hits
PROSITEiView protein in PROSITE
PS50102 RRM, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

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

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiROA2_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: P22626
Secondary accession number(s): A0A024RA27
, A0A024RA61, A8K064, P22627, Q9UC98, Q9UDJ2
<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: August 1, 1991
Last sequence update: November 1, 1991
Last modified: September 18, 2019
This is version 214 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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