HNRNPA2B1
Heterogeneous nuclear ribonucleoproteins A2/B1
Also known as: HNRPA2B1, ROA2_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P22626
- Gene
- HNRNPA2B1
- Ensembl
- ENSG00000122566
- Chromosome
- 7
- Canonical length
- 353 aa
- Protein class
- Cancer-related genes, Disease related genes, Human disease related genes, Plasma proteins, Predicted intracellular proteins
- Subcellular location
- Nucleoplasm
- Secretome location
- Intracellular and membrane
- Quaternary structure
- Homodimer
OverviewNCBI Gene
This gene belongs to the A/B subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene has two repeats of quasi-RRM domains that bind to RNAs. This gene has been described to generate two alternatively spliced transcript variants which encode different isoforms. [provided by RefSeq, Jul 2008]
Canonical amino-acid sequenceUniProt
353 residues, UniProt reviewed canonical sequence.
>P22626|HNRNPA2B1
1 MEKTLETVPL ERKKREKEQF RKLFIGGLSF ETTEESLRNY YEQWGKLTDC VVMRDPASKR
61 SRGFGFVTFS SMAEVDAAMA ARPHSIDGRV VEPKRAVARE ESGKPGAHVT VKKLFVGGIK
121 EDTEEHHLRD YFEEYGKIDT IEIITDRQSG KKRGFGFVTF DDHDPVDKIV LQKYHTINGH
181 NAEVRKALSR QEMQEVQSSR SGRGGNFGFG DSRGGGGNFG PGPGSNFRGG SDGYGSGRGF
241 GDGYNGYGGG PGGGNFGGSP GYGGGRGGYG GGGPGYGNQG GGYGGGYDNY GGGNYGSGNY
301 NDFGNYNQQP SNYGPMKSGN FGGSRNMGGP YGGGNYGPGG SGGSGGYGGR SRYLocalizationUniProt · AlphaFold · HPA
Whether an antibody against HNRNPA2B1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Secreted
- Secreted
- Yes
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.5
- Highest tissue expression
- 172 nTPM
Expression across tissuesHPA
Tissue
- lymph node: 172 nTPM
- thymus: 163 nTPM
- tonsil: 162 nTPM
- skeletal muscle: 158 nTPM
- spleen: 149 nTPM
- ovary: 145 nTPM
Single-cell type
- monocyte progenitors: 1,362 nCPM
- syncytiotrophoblasts: 1,256 nCPM
- cytotrophoblasts: 1,148 nCPM
- megakaryocyte progenitors: 1,113 nCPM
- extravillous trophoblasts: 1,107 nCPM
- migrating cytotrophoblasts: 1,092 nCPM
Immune cell
- gdT-cell: 4.8 nTPM
- MAIT T-cell: 4 nTPM
- NK-cell: 3.3 nTPM
- memory CD4 T-cell: 3 nTPM
- memory B-cell: 2.7 nTPM
- naive CD4 T-cell: 2.7 nTPM
Brain region
- white matter: 59 nTPM
- cerebellum: 58 nTPM
- medulla oblongata: 54 nTPM
- pons: 52 nTPM
- choroid plexus: 50 nTPM
- hypothalamus: 49 nTPM
DiseaseUniProt · ClinVar · IEDB · PubMed
Four sources answering four different questions about HNRNPA2B1.
Disease | AllUniProt
Conditions HNRNPA2B1 is implicated in, by any mechanism.
- Inclusion body myopathy with early-onset Paget disease with or without frontotemporal dementia 2 (IBMPFD2) MIM:615422
- Oculopharyngeal muscular dystrophy 2 (OPMD2) MIM:620460
Disease | GeneticClinVar
6 pathogenic / likely-pathogenic of 427 ClinVar records.
Conditions with pathogenic or likely-pathogenic variants.
- Oculopharyngeal muscular dystrophy 2
- Inclusion body myopathy with early-onset Paget disease with or without frontotemporal dementia 2
- Frontotemporal dementia
Disease | ImmuneIEDB
Conditions an epitope on HNRNPA2B1 was assayed in.
- rheumatoid arthritis B and T cell
- osteoarthritis B and T cell
- Behcet's disease B cell
- allergic disease T cell
- systemic lupus erythematosus B cell
- mixed connective tissue disease B cell
- systemic scleroderma B cell
- Sjogren's syndrome B cell
- autoimmune neuropathy B cell
- systemic juvenile rheumatoid arthritis B cell
- reactive arthritis B cell
ReferencesPubMed · IEDB
Publications for HNRNPA2B1 from three distinct lines of evidence, kept separate because they answer different questions: whether antibodies are directed at the protein, whether a B-cell epitope has been mapped on it, and whether a T-cell epitope has. Each is labelled with its source.
Reference: AutoantibodyPubMed
3 publications
- Analysis of Characteristics Similar to Autoimmune Disease in Keloid Patients.
2015 · Aesthetic Plast Surg · RCR 1.5 · 33 citations - Significantly increased antibody response to heterogeneous nuclear ribonucleoproteins in cerebrospinal fluid of multiple sclerosis patients but not in patients with human T-lymphotropic virus type I-associated myelopathy/tropical spastic paraparesis.
2008 · J Neurovirol · RCR 0.6 · 27 citations - Detection and Clinical Associations of Autoantibodies to Heterogeneous Nuclear Ribonucleoprotein (hnRNP) A2/B1 in Patients with Systemic Sclerosis.
2025 · Int J Mol Sci · 1 citations
Reference: B cellIEDB
4 publications
- Cross-reactivity of a human IgG₁ anticitrullinated fibrinogen monoclonal antibody to a citrullinated profilaggrin peptide.
2012 · Protein Sci · RCR 1 · 29 citations - Serum IgA reactivity against GroEL of Streptococcus sanguinis and human heterogeneous nuclear ribonucleoprotein A2/B1 in patients with Behçet disease.
2013 · Br J Dermatol · RCR 0.8 · 19 citations - B cell epitopes of the heterogeneous nuclear ribonucleoprotein A2: identification of a new specific antibody marker for active lupus disease.
2009 · Ann Rheum Dis · RCR 0.5 · 20 citations - Immunodominant T-cell epitopes of hnRNP-A2 associated with disease activity in patients with rheumatoid arthritis.
2010 · Eur J Immunol · RCR 0.4 · 17 citations
Reference: T cellIEDB
3 publications
- Allergen and Epitope Targets of Mouse-Specific T Cell Responses in Allergy and Asthma.
2018 · Front Immunol · RCR 1.1 · 25 citations - Urinary Peptides As a Novel Source of T Cell Allergen Epitopes.
2018 · Front Immunol · RCR 0.5 · 15 citations - Characterization and epitope identification of the T cell response in non-allergic individuals exposed to mouse allergen.
2019 · World Allergy Organ J · RCR 0.4 · 9 citations
Sources: PubMed — antigen-level antibody evidence from a custom retrieval. Records matching a controlled set of autoantibody terms (the MeSH descriptors Autoantibodies and Autoantigens, with title and abstract term variants) were obtained through NCBI E-utilities, and their titles and abstracts parsed for constructions that direct an antibody at a named protein rather than for co-occurrence. Captured names were resolved against UniProt nomenclature and each antigen adjudicated individually against the source text. IEDB — curated epitope assays from the Immune Epitope Database (Vita et al., Nucleic Acids Research 2019). Bibliographic records from PubMed and MeSH, U.S. National Library of Medicine; citation metrics from NIH iCite (Hutchins et al., PLoS Biology 2016). Titles link to PubMed; abstracts are not reproduced here. The NLM does not endorse this analysis.
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 0.22
- gnomAD pLI
- 1
- gnomAD missense Z
- 3
- DepMap mean gene effect
- -0.32
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 6% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- DNA geometric change
- miRNA transport
- mRNA export from nucleus
- mRNA processing
- mRNA splicing, via spliceosome
- mRNA transport
- positive regulation of telomere maintenance via telomere lengthening
- primary miRNA processing
- RNA transport
Molecular functions
- DNA polymerase binding
- G-rich strand telomeric DNA binding
- identical protein binding
- miRNA binding
- molecular condensate scaffold activity
- mRNA 3'-UTR binding
- N6-methyladenosine-containing RNA reader activity
- RNA binding
- single-stranded telomeric DNA binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of HNRNPA2B1 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads HNRNPA2B1 as an antibody target. Whether an autoantibody or antibody against HNRNPA2B1 could matter depends on whether native HNRNPA2B1 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
HNRNPA2B1 is annotated as secreted, so native HNRNPA2B1 circulates and is directly accessible to antibodies. Secreted and cell-surface proteins are the autoantibody targets most likely to act like drugs, blocking or depleting the native protein.
Annotation status
The present source text does not explicitly label HNRNPA2B1 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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