HNRNPA2B1
entrez
3181
canonical
uniprot
P22626
canonical
ensembl
ENSG00000122566
resolver
ensp
ENSP00000346694
resolver
ensp
ENSP00000478691
resolver
ensp
ENSP00000503060
resolver
ensp
ENSP00000504049
resolver
ensp
ENSP00000538171
resolver
ensp
ENSP00000538172
resolver
ensp
ENSP00000538173
resolver
ensp
ENSP00000538174
resolver
ensp
ENSP00000538175
resolver
ensp
ENSP00000538177
resolver
ensp
ENSP00000538179
resolver
ensp
ENSP00000538185
resolver
ensp
ENSP00000593841
resolver
ensp
ENSP00000730671
resolver
enst
ENST00000677321
resolver
enst
ENST00000868112
resolver
enst
ENST00000868115
resolver
genesymbol
HNRNPA2B1
resolver
genesymbol_syn
HNRPA2B1
resolver
hgnc
HGNC:5033
resolver
uniprot
A0A024RA27
resolver
uniprot
A0A024RA61
resolver
uniprot
A0A7I2V4N1
resolver
uniprot
A8K064
resolver
uniprot
P22627
resolver
uniprot
Q9UC98
resolver
uniprot
Q9UDJ2
resolver
uniprot_entry
A0A7I2V4N1_HUMAN
resolver
uniprot_entry
ROA2_HUMAN
resolver
uniprot_sec
A0A024RA27
resolver
uniprot_sec
A0A024RA61
resolver
uniprot_sec
A8K064
resolver
uniprot_sec
P22627
resolver
uniprot_sec
Q9UC98
resolver
uniprot_sec
Q9UDJ2
resolver
amino_acid_sequence
MEKTLETVPLERKKREKEQFRKLFIGGLSFETTEESLRNYYEQWGKLTDCVVMRDPASKRSRGFGFVTFSSMAEVDAAMAARPHSIDGRVVEPKRAVAREESGKPGAHVTVKKLFVGGIKEDTEEHHLRDYFEEYGKIDTIEIITDRQSGKKRGFGFVTFDDHDPVDKIVLQKYHTINGHNAEVRKALSRQEMQEVQSSRSGRGGNFGFGDSRGGGGNFGPGPGSNFRGGSDGYGSGRGFGDGYNGYGGGPGGGNFGGSPGYGGGRGGYGGGGPGYGNQGGGYGGGYDNYGGGNYGSGNYNDFGNYNQQPSNYGPMKSGNFGGSRNMGGPYGGGNYGPGGSGGSGGYGGRSRY
uniprot
proteins
disease_involvement
DISEASE: Inclusion body myopathy with early-onset Paget disease with or without frontotemporal dementia 2 (IBMPFD2) [MIM:615422]: An 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. {ECO:0000269|PubMed:23455423}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Oculopharyngeal muscular dystrophy 2 (OPMD2) [MIM:620460]: An autosomal dominant, early-onset myopathy characterized by progressive muscle weakness, ptosis, ophthalmoplegia, dysphagia, and variable degrees of respiratory insufficiency. {ECO:0000269|PubMed:35484142}. Note=The disease is caused by variants affecting the gene represented in this entry. The disease is caused by frameshift variants that cluster in the low complexity disordered region. They abolish the native stop codon, and extend the reading frame resulting in a common C-terminal sequence. All variants escape degradation by the RNA quality control system, and mutant proteins accumulate in the cytoplasm due to impaired nucleocytoplasmic trafficking. {ECO:0000269|PubMed:35484142}.
uniprot
proteins
function
FUNCTION: 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). Plays a role in the splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (PubMed:20010808). Also plays a role in the activation of the innate immune response (PubMed:31320558). Mechanistically, senses the presence of viral DNA in the nucleus, homodimerizes and is demethylated by JMJD6 (PubMed:31320558). In turn, translocates to the cytoplasm where it activates the TBK1-IRF3 pathway, leading to interferon alpha/beta production (PubMed:31320558). {ECO:0000250|UniProtKB:A7VJC2, ECO:0000269|PubMed:10567417, ECO:0000269|PubMed:20010808, ECO:0000269|PubMed:24356509, ECO:0000269|PubMed:26321680, ECO:0000303|PubMed:19099192}.; FUNCTION: (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. {ECO:0000269|PubMed:15294897, ECO:0000269|PubMed:17004321}.
uniprot
proteins
mass_dalton
37430
uniprot
proteins
mutagenesis
MUTAGEN 207; /note="F->S: Does not affect hydrogel-binding."; /evidence="ECO:0000269|PubMed:26544936"; MUTAGEN 209; /note="F->S: Does not affect hydrogel-binding."; /evidence="ECO:0000269|PubMed:26544936"; MUTAGEN 219; /note="F->S: Does not affect hydrogel-binding."; /evidence="ECO:0000269|PubMed:26544936"; MUTAGEN 227; /note="F->S: Does not affect hydrogel-binding."; /evidence="ECO:0000269|PubMed:26544936"; MUTAGEN 228; /note="R->A: About 10-fold increase in interferon beta production."; /evidence="ECO:0000269|PubMed:26544936"; MUTAGEN 234; /note="Y->S: Does not affect hydrogel-binding."; /evidence="ECO:0000269|PubMed:26544936"; MUTAGEN 240; /note="F->S: Does not affect hydrogel-binding."; /evidence="ECO:0000269|PubMed:26544936"; MUTAGEN 244; /note="Y->S: Does not affect hydrogel-binding."; /evidence="ECO:0000269|PubMed:26544936"; MUTAGEN 247; /note="Y->S: Slightly affects hydrogel-binding."; /evidence="ECO:0000269|PubMed:26544936"; MUTAGEN 256; /note="F->S: Does not affect hydrogel-binding."; /evidence="ECO:0000269|PubMed:26544936"; MUTAGEN 262; /note="Y->S: Slightly affects hydrogel-binding."; /evidence="ECO:0000269|PubMed:26544936"; MUTAGEN 269; /note="Y->S: Does not affect hydrogel-binding."; /evidence="ECO:0000269|PubMed:26544936"; MUTAGEN 276; /note="Y->S: Impairs hydrogel-binding."; /evidence="ECO:0000269|PubMed:26544936"; MUTAGEN 283; /note="Y->S: Slightly affects hydrogel-binding."; /evidence="ECO:0000269|PubMed:26544936"; MUTAGEN 287; /note="Y->S: Does not affect hydrogel-binding."; /evidence="ECO:0000269|PubMed:26544936"; MUTAGEN 290; /note="Y->S: Impairs hydrogel-binding."; /evidence="ECO:0000269|PubMed:26544936"; MUTAGEN 295; /note="Y->S: Impairs hydrogel-binding."; /evidence="ECO:0000269|PubMed:26544936"; MUTAGEN 300; /note="Y->S: Slightly affects hydrogel-binding."; /evidence="ECO:0000269|PubMed:26544936"; MUTAGEN 303; /note="F->S: Impairs hydrogel-binding."; /evidence="ECO:0000269|PubMed:26544936"; MUTAGEN 306; /note="Y->S: Slightly affects hydrogel-binding."; /evidence="ECO:0000269|PubMed:26544936"; MUTAGEN 313; /note="Y->S: Slightly affects hydrogel-binding."; /evidence="ECO:0000269|PubMed:26544936"; MUTAGEN 321; /note="F->S: Impairs hydrogel-binding."; /evidence="ECO:0000269|PubMed:26544936"; MUTAGEN 331; /note="Y->S: Impairs hydrogel-binding."; /evidence="ECO:0000269|PubMed:26544936"; MUTAGEN 336; /note="Y->S: Slightly affects hydrogel-binding."; /evidence="ECO:0000269|PubMed:26544936"; MUTAGEN 347; /note="Y->S: Does not affect hydrogel-binding."; /evidence="ECO:0000269|PubMed:26544936"; MUTAGEN 353; /note="Y->S: Does not affect hydrogel-binding."; /evidence="ECO:0000269|PubMed:26544936
uniprot
proteins
post_translational_modification
PTM: Sumoylated in exosomes, promoting miRNAs-binding. {ECO:0000269|PubMed:24356509}.; PTM: 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). {ECO:0000250|UniProtKB:A7VJC2, ECO:0000269|PubMed:10772824}.
uniprot
proteins
pubmed
10567417
uniprot
proteins
pubmed
10772824
uniprot
proteins
pubmed
11991638
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
1522214
uniprot
proteins
pubmed
15294897
uniprot
proteins
pubmed
15703215
uniprot
proteins
pubmed
15782174
uniprot
proteins
pubmed
1699755
uniprot
proteins
pubmed
17004321
uniprot
proteins
pubmed
17289661
uniprot
proteins
pubmed
17924679
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19099192
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19429692
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20010808
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
22905912
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23455423
uniprot
proteins
pubmed
24098712
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24356509
uniprot
proteins
pubmed
24549040
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
2557628
uniprot
proteins
pubmed
25678563
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26321680
uniprot
proteins
pubmed
26544936
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
31320558
uniprot
proteins
pubmed
35484142
uniprot
proteins
pubmed
3733753
uniprot
proteins
pubmed
37643469
uniprot
proteins
pubmed
39349455
uniprot
proteins
pubmed
7789969
uniprot
proteins
pubmed
7980541
uniprot
proteins
pubmed
8029005
uniprot
proteins
sequence_length
353
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31320558, ECO:0000269|PubMed:37643469}. Nucleus, nucleoplasm {ECO:0000269|PubMed:17289661}. Cytoplasm {ECO:0000269|PubMed:31320558, ECO:0000269|PubMed:37643469}. Cytoplasmic granule {ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:24356509}. Secreted, extracellular exosome {ECO:0000269|PubMed:24356509}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs (PubMed:17289661). Component of ribonucleosomes (PubMed:17289661). Not found in the nucleolus (PubMed:17289661). Found in exosomes following sumoylation (PubMed:24356509). {ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:24356509}.; SUBCELLULAR LOCATION: [Isoform A2]: Nucleus {ECO:0000269|PubMed:10772824, ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:24098712}. Cytoplasm {ECO:0000269|PubMed:10772824, ECO:0000269|PubMed:17289661}. Note=Predominantly nucleoplasmic, however is also found in the cytoplasm of cells in some tissues (PubMed:17289661). {ECO:0000269|PubMed:17289661}.
uniprot
proteins