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Protein

Heterogeneous nuclear ribonucleoproteins A2/B1

Gene

Hnrnpa2b1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. Forms hnRNP particles with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus (PubMed:19099192). 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:9578590, PubMed:10567417). Specifically binds single-stranded telomeric DNA sequences, protecting telomeric DNA repeat against endonuclease digestion (PubMed:15659580). 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. Involved in miRNA sorting into exosomes following sumoylation, possibly by binding (m6A)-containing pre-miRNAs. Acts as a regulator of efficiency of mRNA splicing, possibly by binding to m6A-containing pre-mRNAs (By similarity).1 PublicationBy similarity3 Publications

GO - Molecular functioni

  • miRNA binding Source: UniProtKB
  • mRNA 3'-UTR binding Source: UniProtKB
  • mRNA CDS binding Source: RGD
  • N6-methyladenosine-containing RNA binding Source: UniProtKB
  • nucleotide binding Source: InterPro
  • regulatory region RNA binding Source: RGD
  • RNA binding Source: RGD
  • single-stranded telomeric DNA binding Source: UniProtKB

GO - Biological processi

  • lung development Source: RGD
  • male gonad development Source: RGD
  • miRNA transport Source: UniProtKB
  • mRNA export from nucleus Source: UniProtKB
  • mRNA splicing, via spliceosome Source: UniProtKB
  • oligodendrocyte differentiation Source: RGD
  • primary miRNA processing Source: UniProtKB
  • response to mineralocorticoid Source: RGD
  • RNA transport Source: RGD
  • telomere capping Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing, mRNA transport, Transport

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Heterogeneous nuclear ribonucleoproteins A2/B1Imported
Short name:
hnRNP A2/B1
Gene namesi
Name:Hnrnpa2b1By similarity
Synonyms:HnrnpImported, Hnrpa2b1By similarity
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1310403. Hnrnpa2b1.

Subcellular locationi

Isoform B1 :
Isoform A2 :
Isoform A2b :
Isoform B1b :

GO - Cellular componenti

  • chromatin Source: RGD
  • cytoplasm Source: RGD
  • extracellular exosome Source: UniProtKB
  • intracellular ribonucleoprotein complex Source: UniProtKB
  • neuronal cell body Source: RGD
  • neuronal ribonucleoprotein granule Source: RGD
  • neuron projection Source: RGD
  • nucleoplasm Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB
  • perikaryon Source: RGD
  • spliceosomal complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi266 – 2661R → A: Decreased methylation. Does not affect subcellular location. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 353353Heterogeneous nuclear ribonucleoproteins A2/B1PRO_0000365101Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei29 – 291PhosphoserineBy similarity
Modified residuei85 – 851PhosphoserineBy similarity
Modified residuei104 – 1041N6,N6-dimethyllysineBy similarity
Cross-linki120 – 120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei149 – 1491PhosphoserineBy similarity
Modified residuei168 – 1681N6-acetyllysineBy similarity
Modified residuei173 – 1731N6-acetyllysineBy similarity
Cross-linki186 – 186Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei203 – 2031Dimethylated arginine; alternateBy similarity
Modified residuei203 – 2031Omega-N-methylarginine; alternateBy similarity
Modified residuei212 – 2121PhosphoserineCombined sources
Modified residuei213 – 2131Dimethylated arginine; alternateBy similarity
Modified residuei213 – 2131Omega-N-methylarginine; alternateBy similarity
Modified residuei225 – 2251PhosphoserineBy similarity
Modified residuei231 – 2311PhosphoserineBy similarity
Modified residuei236 – 2361PhosphoserineBy similarity
Modified residuei259 – 2591PhosphoserineCombined sources
Modified residuei266 – 2661Asymmetric dimethylarginine1 Publication
Modified residuei324 – 3241PhosphoserineBy similarity
Modified residuei331 – 3311PhosphotyrosineBy similarity
Modified residuei341 – 3411PhosphoserineBy similarity
Modified residuei344 – 3441PhosphoserineCombined sources
Modified residuei347 – 3471PhosphotyrosineBy similarity

Post-translational modificationi

Asymmetric dimethylation at Arg-266 constitutes the major methylation site (PubMed:24098712). According to a report, methlytion affects subcellular location and promotes nuclear localization (PubMed:10772824). According to another report, methylation at Arg-266 does not influence nucleocytoplasmic shuttling (PubMed:24098712).2 Publications
Sumoylated in exosomes, promoting miRNAs-binding.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiA7VJC2.
PRIDEiA7VJC2.

PTM databases

iPTMnetiA7VJC2.
SwissPalmiA7VJC2.

Expressioni

Tissue specificityi

In the brain, isoform A2 and isoform B1 are abundant in large ganglion-type neurons, such as Purkinje cells, and are less abundant in neighboring glia cells. Isoform A2 is more abundant than isoform B1 in brain. In testis, isoform A2 and isoform B1 are present in spermatogonia and spermatocytes, but not in spermatids or sperm. Isoform A2 is more abundant in the adrenal medulla than in the cortical cells. Isoform B1 is found in both adrenal medulla and cortical cells. Isoform A2 is more abundant than isoform B1 in the adrenal gland. Isoform A2 and isoform B1 are both detected in pancreas and kidney, and at lower levels in heart and lung. Isoform B1 is more abundant than isoform A2 in heart, lung and intestine (at protein level). Isoform A2b and isoform B1b are testis-specific.1 Publication

Interactioni

Subunit structurei

Identified in the spliceosome C complex. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with IGF2BP1. Interacts with C9orf72. Interacts with DGCR8. Interacts with TARDBP. Interacts with CKAP5.By similarity

Protein-protein interaction databases

BioGridi263391. 2 interactions.
STRINGi10116.ENSRNOP00000015152.

Structurei

3D structure databases

ProteinModelPortaliA7VJC2.
SMRiA7VJC2. Positions 1-193.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 10484RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini112 – 19180RRM 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni193 – 353161Low complexity (LC) region1 PublicationAdd
BLAST
Regioni308 – 34740Nuclear targeting sequenceBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi9 – 157Nuclear localization signalSequence analysisBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi202 – 349148Gly-richSequence analysisAdd
BLAST

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 evidences suggest that formation of cross-beta structures by LC regions mediate the formation of RNA granules, liquid-like droplets, and hydrogels.By similarity

Sequence similaritiesi

Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0118. Eukaryota.
COG0724. LUCA.
HOGENOMiHOG000234442.
HOVERGENiHBG108415.
InParanoidiA7VJC2.
KOiK13158.
PhylomeDBiA7VJC2.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 2 hits.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.1 Publication

Isoform B11 Publication (identifier: A7VJC2-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
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 DDHDPVDKIF 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):37,478
Last modified:October 23, 2007 - v1
Checksum:i1C2E7BA8C8E98D6E
GO
Isoform A21 Publication (identifier: A7VJC2-2) [UniParc]FASTAAdd to basket

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

Show »
Length:341
Mass (Da):36,054
Checksum:i69E3B065C874EA70
GO
Isoform A2b (identifier: A7VJC2-3) [UniParc]FASTAAdd to basket

Also known as: B0a1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     3-14: Missing.
     254-293: Missing.

Show »
Length:301
Mass (Da):32,536
Checksum:i19139C701AB31D62
GO
Isoform B1b (identifier: A7VJC2-4) [UniParc]FASTAAdd to basket

Also known as: B0b1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     254-293: Missing.

Show »
Length:313
Mass (Da):33,959
Checksum:i24C88124F1569BCE
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei3 – 1412Missing in isoform A2 and isoform A2b. 1 PublicationVSP_053031Add
BLAST
Alternative sequencei254 – 29340Missing in isoform A2b and isoform B1b. 1 PublicationVSP_053032Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB006815 mRNA. Translation: BAF79675.1.
AB006816 mRNA. Translation: BAF79676.1.
AB006817 mRNA. Translation: BAF79677.1.
AB006818 mRNA. Translation: BAF79678.1.
RefSeqiNP_001098083.1. NM_001104613.1. [A7VJC2-1]
UniGeneiRn.4057.

Genome annotation databases

GeneIDi362361.
KEGGirno:362361.
UCSCiRGD:1310403. rat. [A7VJC2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB006815 mRNA. Translation: BAF79675.1.
AB006816 mRNA. Translation: BAF79676.1.
AB006817 mRNA. Translation: BAF79677.1.
AB006818 mRNA. Translation: BAF79678.1.
RefSeqiNP_001098083.1. NM_001104613.1. [A7VJC2-1]
UniGeneiRn.4057.

3D structure databases

ProteinModelPortaliA7VJC2.
SMRiA7VJC2. Positions 1-193.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi263391. 2 interactions.
STRINGi10116.ENSRNOP00000015152.

PTM databases

iPTMnetiA7VJC2.
SwissPalmiA7VJC2.

Proteomic databases

PaxDbiA7VJC2.
PRIDEiA7VJC2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi362361.
KEGGirno:362361.
UCSCiRGD:1310403. rat. [A7VJC2-1]

Organism-specific databases

CTDi3181.
RGDi1310403. Hnrnpa2b1.

Phylogenomic databases

eggNOGiKOG0118. Eukaryota.
COG0724. LUCA.
HOGENOMiHOG000234442.
HOVERGENiHBG108415.
InParanoidiA7VJC2.
KOiK13158.
PhylomeDBiA7VJC2.

Miscellaneous databases

PROiA7VJC2.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 2 hits.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of the hnRNP A2/B1 proteins: tissue-specific expression and novel isoforms."
    Kamma H., Horiguchi H., Wan L., Matsui M., Fuiwara M., Fujimoto M., Yazawa T., Dreyfuss G.
    Exp. Cell Res. 246:399-411(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A2; B1; A2B AND B1B), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "hnRNP A2 selectively binds the cytoplasmic transport sequence of myelin basic protein mRNA."
    Hoek K.S., Kidd G.J., Carson J.H., Smith R.
    Biochemistry 37:7021-7029(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 100-113; 116-137 AND 2014-226, FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION.
  3. "Mutational analysis of a heterogeneous nuclear ribonucleoprotein A2 response element for RNA trafficking."
    Munro T.P., Magee R.J., Kidd G.J., Carson J.H., Barbarese E., Smith L.M., Smith R.
    J. Biol. Chem. 274:34389-34395(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING.
  4. Cited for: METHYLATION.
  5. "hnRNP A2, a potential ssDNA/RNA molecular adapter at the telomere."
    Moran-Jones K., Wayman L., Kennedy D.D., Reddel R.R., Sara S., Snee M.J., Smith R.
    Nucleic Acids Res. 33:486-496(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Nuclear functions of heterogeneous nuclear ribonucleoproteins A/B."
    He Y., Smith R.
    Cell. Mol. Life Sci. 66:1239-1256(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  7. "Proteome profile of the mature rat olfactory bulb."
    Maurya D.K., Sundaram C.S., Bhargava P.
    Proteomics 9:2593-2599(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  8. "Differential subcellular distributions and trafficking functions of hnRNP A2/B1 spliceoforms."
    Han S.P., Friend L.R., Carson J.H., Korza G., Barbarese E., Maggipinto M., Hatfield J.T., Rothnagel J.A., Smith R.
    Traffic 11:886-898(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION (ISOFORMS B1; A2; A2B AND B1B).
  9. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212; SER-259 AND SER-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Arginine methylation of hnRNP A2 does not directly govern its subcellular localization."
    Friend L.R., Landsberg M.J., Nouwens A.S., Wei Y., Rothnagel J.A., Smith R.
    PLoS ONE 8:E75669-E75669(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT MET-1, METHYLATION AT ARG-266, SUBCELLULAR LOCATION (ISOFORM A2), MUTAGENESIS OF ARG-266.

Entry informationi

Entry nameiROA2_RAT
AccessioniPrimary (citable) accession number: A7VJC2
Secondary accession number(s): A7VJC1, A7VJC3, A7VJC4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: October 23, 2007
Last modified: June 8, 2016
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.