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Protein

Heterogeneous nuclear ribonucleoproteins A2/B1

Gene

HNRNPA2B1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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. 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 (By similarity). 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. 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).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing, mRNA transport, Transport

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-BTA-72163. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Heterogeneous nuclear ribonucleoproteins A2/B1
Short name:
hnRNP A2/B1
Gene namesi
Name:HNRNPA2B1
Synonyms:HNRPA2B1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 4

Subcellular locationi

  • Nucleusnucleoplasm By similarity
  • Cytoplasmic granule By similarity
  • Secretedexosome By similarity

  • Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Component of ribonucleosomes. Not found in the nucleolus. Found in exosomes follwong sumoylation.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Secreted, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 341341Heterogeneous nuclear ribonucleoproteins A2/B1PRO_0000273979Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171PhosphoserineBy similarity
Modified residuei73 – 731PhosphoserineBy similarity
Modified residuei92 – 921N6,N6-dimethyllysineBy similarity
Cross-linki108 – 108Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei128 – 1281PhosphothreonineBy similarity
Modified residuei137 – 1371PhosphoserineBy similarity
Modified residuei147 – 1471PhosphothreonineBy similarity
Modified residuei156 – 1561N6-acetyllysineBy similarity
Modified residuei161 – 1611N6-acetyllysineBy similarity
Modified residuei164 – 1641PhosphothreonineBy similarity
Cross-linki174 – 174Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei177 – 1771PhosphoserineBy similarity
Modified residuei189 – 1891PhosphoserineBy similarity
Modified residuei191 – 1911Dimethylated arginine; alternateBy similarity
Modified residuei191 – 1911Omega-N-methylarginine; alternateBy similarity
Modified residuei200 – 2001PhosphoserineBy similarity
Modified residuei201 – 2011Dimethylated arginine; alternateBy similarity
Modified residuei201 – 2011Omega-N-methylarginine; alternateBy similarity
Modified residuei213 – 2131PhosphoserineBy similarity
Modified residuei219 – 2191PhosphoserineBy similarity
Modified residuei224 – 2241PhosphoserineBy similarity
Modified residuei247 – 2471PhosphoserineBy similarity
Modified residuei254 – 2541Asymmetric dimethylarginineBy similarity
Modified residuei312 – 3121PhosphoserineBy similarity
Modified residuei319 – 3191PhosphotyrosineBy similarity
Modified residuei329 – 3291PhosphoserineBy similarity
Modified residuei332 – 3321PhosphoserineBy similarity
Modified residuei335 – 3351PhosphotyrosineBy similarity

Post-translational modificationi

Sumoylated in exosomes, promoting miRNAs-binding.By similarity
Asymmetric dimethylation at Arg-254 constitutes the major methylation site (By similarity). According to a report, methlytion affects subcellular location and promotes nuclear localization (By similarity). According to another report, methylation at Arg-254 does not influence nucleocytoplasmic shuttling (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ2HJ60.
PeptideAtlasiQ2HJ60.
PRIDEiQ2HJ60.

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

STRINGi9913.ENSBTAP00000007527.

Structurei

3D structure databases

ProteinModelPortaliQ2HJ60.
SMRiQ2HJ60. Positions 3-181.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 9284RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini100 – 17980RRM 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni181 – 341161Low complexity (LC) regionBy similarityAdd
BLAST
Regioni296 – 33540Nuclear targeting sequenceBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi190 – 341152Gly-richAdd
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.
GeneTreeiENSGT00760000118873.
HOGENOMiHOG000234442.
HOVERGENiHBG002295.
InParanoidiQ2HJ60.
KOiK13158.
OMAiRESDWRE.
OrthoDBiEOG715Q6V.
TreeFamiTF351342.

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]

Sequencei

Sequence statusi: Complete.

Q2HJ60-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEREKEQFRK LFIGGLSFET TEESLRNYYE QWGKLTDCVV MRDPASKRSR
60 70 80 90 100
GFGFVTFSSM AEVDAAMAAR PHSIDGRVVE PKRAVAREES GKPGAHVTVK
110 120 130 140 150
KLFVGGIKED TEEHHLRDYF EEYGKIDTIE IITDRQSGKK RGFGFVTFDD
160 170 180 190 200
HDPVDKIVLQ KYHTINGHNA EVRKALSRQE MQEVQSSRSG RGGNFGFGDS
210 220 230 240 250
RGGGGNFGPG PGSNFRGGSD GYGSGRGFGD GYNGYGGGPG GGNFGGSPGY
260 270 280 290 300
GGGRGGYGGG GPGYGNQGGG YGGGYDNYGG GNYGSGNYND FGNYNQQPSN
310 320 330 340
YGPMKSGNFG GSRNMGGPYG GGNYGPGGSG GSGGYGGRSR Y
Length:341
Mass (Da):36,006
Last modified:March 21, 2006 - v1
Checksum:i39E8AB6ED874FA7C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC113298 mRNA. Translation: AAI13299.1.
RefSeqiNP_001039440.1. NM_001045975.1.
UniGeneiBt.48137.

Genome annotation databases

EnsembliENSBTAT00000007527; ENSBTAP00000007527; ENSBTAG00000005726.
GeneIDi507564.
KEGGibta:507564.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC113298 mRNA. Translation: AAI13299.1.
RefSeqiNP_001039440.1. NM_001045975.1.
UniGeneiBt.48137.

3D structure databases

ProteinModelPortaliQ2HJ60.
SMRiQ2HJ60. Positions 3-181.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000007527.

Proteomic databases

PaxDbiQ2HJ60.
PeptideAtlasiQ2HJ60.
PRIDEiQ2HJ60.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000007527; ENSBTAP00000007527; ENSBTAG00000005726.
GeneIDi507564.
KEGGibta:507564.

Organism-specific databases

CTDi3181.

Phylogenomic databases

eggNOGiKOG0118. Eukaryota.
COG0724. LUCA.
GeneTreeiENSGT00760000118873.
HOGENOMiHOG000234442.
HOVERGENiHBG002295.
InParanoidiQ2HJ60.
KOiK13158.
OMAiRESDWRE.
OrthoDBiEOG715Q6V.
TreeFamiTF351342.

Enzyme and pathway databases

ReactomeiR-BTA-72163. mRNA Splicing - Major Pathway.

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

  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Uterus.

Entry informationi

Entry nameiROA2_BOVIN
AccessioniPrimary (citable) accession number: Q2HJ60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: March 21, 2006
Last modified: July 6, 2016
This is version 87 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, 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.