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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-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 (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

GO - Molecular functioni

  • miRNA binding Source: UniProtKB
  • mRNA 3'-UTR binding Source: UniProtKB
  • N6-methyladenosine-containing RNA binding Source: UniProtKB
  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB
  • pre-mRNA intronic binding Source: Ensembl
  • RNA binding Source: HGNC
  • single-stranded telomeric DNA binding Source: HGNC

GO - Biological processi

  • gene expression Source: Reactome
  • miRNA transport Source: UniProtKB
  • mRNA export from nucleus Source: UniProtKB
  • mRNA processing Source: HGNC
  • mRNA splicing, via spliceosome Source: UniProtKB
  • negative regulation of mRNA splicing, via spliceosome Source: Ensembl
  • negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  • primary miRNA processing Source: UniProtKB
  • RNA transport Source: HGNC
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

BioCyciZFISH:ENSG00000122566-MONOMER.
ReactomeiR-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72203. Processing of Capped Intron-Containing Pre-mRNA.
SIGNORiP22626.

Names & Taxonomyi

Protein namesi
Recommended name:
Heterogeneous nuclear ribonucleoproteins A2/B1
Short name:
hnRNP A2/B1
Gene namesi
Name:HNRNPA2B1
Synonyms:HNRPA2B1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:5033. HNRNPA2B1.

Subcellular locationi

Isoform A2 :

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • intracellular ribonucleoprotein complex Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • spliceosomal complex Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted, Spliceosome

Pathology & Biotechi

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.
See also OMIM:615422
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_070591302D → V in IBMPFD2. 1 PublicationCorresponds to variant rs397515326dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

DisGeNETi3181.
MalaCardsiHNRNPA2B1.
MIMi615422. phenotype.
OpenTargetsiENSG00000122566.
Orphaneti52430. Inclusion body myopathy with Paget disease of bone and frontotemporal dementia.
PharmGKBiPA162391140.

Polymorphism and mutation databases

BioMutaiHNRNPA2B1.
DMDMi133257.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000818361 – 353Heterogeneous nuclear ribonucleoproteins A2/B1Add BLAST353

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1 Publication1
Modified residuei4PhosphothreonineCombined sources1
Modified residuei29PhosphoserineCombined sources1
Modified residuei38Omega-N-methylarginineBy similarity1
Modified residuei85PhosphoserineCombined sources1
Modified residuei104N6,N6-dimethyllysine1 Publication1
Cross-linki120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei140PhosphothreonineCombined sources1
Modified residuei149PhosphoserineCombined sources1
Modified residuei159PhosphothreonineCombined sources1
Modified residuei168N6-acetyllysineCombined sources1
Modified residuei173N6-acetyllysineCombined sources1
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

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, methlytion 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

EPDiP22626.
MaxQBiP22626.
PaxDbiP22626.
PeptideAtlasiP22626.
PRIDEiP22626.
TopDownProteomicsiP22626-1. [P22626-1]
P22626-2. [P22626-2]

2D gel databases

REPRODUCTION-2DPAGEIPI00396378.
IPI00414696.
P22626.
SWISS-2DPAGEP22626.
UCD-2DPAGEP22626.

PTM databases

iPTMnetiP22626.
PhosphoSitePlusiP22626.
SwissPalmiP22626.

Miscellaneous databases

PMAP-CutDBP22626.

Expressioni

Gene expression databases

BgeeiENSG00000122566.
CleanExiHS_HNRNPA2B1.
ExpressionAtlasiP22626. baseline and differential.
GenevisibleiP22626. HS.

Organism-specific databases

HPAiCAB012403.
HPA001666.
HPA005812.
HPA065537.

Interactioni

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

Binary interactionsi

WithEntry#Exp.IntActNotes
ZMAT3Q9HA383EBI-299649,EBI-2548480

Protein-protein interaction databases

BioGridi109422. 191 interactors.
DIPiDIP-32877N.
IntActiP22626. 100 interactors.
MINTiMINT-4998934.
STRINGi9606.ENSP00000346694.

Structurei

Secondary structure

1353
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi16 – 20Combined sources5
Beta strandi22 – 26Combined sources5
Helixi34 – 41Combined sources8
Beta strandi48 – 52Combined sources5
Turni56 – 58Combined sources3
Beta strandi63 – 68Combined sources6
Helixi72 – 79Combined sources8
Beta strandi83 – 86Combined sources4
Beta strandi89 – 94Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X4BNMR-A1-103[»]
ProteinModelPortaliP22626.
SMRiP22626.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22626.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini21 – 104RRM 1PROSITE-ProRule annotationAdd BLAST84
Domaini112 – 191RRM 2PROSITE-ProRule annotationAdd BLAST80

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni193 – 353Low complexity (LC) region1 PublicationAdd BLAST161
Regioni308 – 347Nuclear targeting sequenceBy similarityAdd BLAST40

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi9 – 15Nuclear localization signalSequence analysis7

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi202 – 353Gly-richAdd BLAST152

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.1 Publication

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0118. Eukaryota.
COG0724. LUCA.
GeneTreeiENSGT00760000118873.
HOGENOMiHOG000234442.
HOVERGENiHBG002295.
InParanoidiP22626.
KOiK13158.
OMAiTRQIPNA.
OrthoDBiEOG091G1CPI.
PhylomeDBiP22626.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

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

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 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
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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 rs397515326dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0058303 – 14Missing in isoform A2. 1 PublicationAdd BLAST12

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]
UniGeneiHs.487774.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing

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]
UniGeneiHs.487774.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X4BNMR-A1-103[»]
ProteinModelPortaliP22626.
SMRiP22626.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109422. 191 interactors.
DIPiDIP-32877N.
IntActiP22626. 100 interactors.
MINTiMINT-4998934.
STRINGi9606.ENSP00000346694.

PTM databases

iPTMnetiP22626.
PhosphoSitePlusiP22626.
SwissPalmiP22626.

Polymorphism and mutation databases

BioMutaiHNRNPA2B1.
DMDMi133257.

2D gel databases

REPRODUCTION-2DPAGEIPI00396378.
IPI00414696.
P22626.
SWISS-2DPAGEP22626.
UCD-2DPAGEP22626.

Proteomic databases

EPDiP22626.
MaxQBiP22626.
PaxDbiP22626.
PeptideAtlasiP22626.
PRIDEiP22626.
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]
GeneIDi3181.
KEGGihsa:3181.
UCSCiuc003sxr.5. human. [P22626-1]

Organism-specific databases

CTDi3181.
DisGeNETi3181.
GeneCardsiHNRNPA2B1.
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.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0118. Eukaryota.
COG0724. LUCA.
GeneTreeiENSGT00760000118873.
HOGENOMiHOG000234442.
HOVERGENiHBG002295.
InParanoidiP22626.
KOiK13158.
OMAiTRQIPNA.
OrthoDBiEOG091G1CPI.
PhylomeDBiP22626.
TreeFamiTF351342.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000122566-MONOMER.
ReactomeiR-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72203. Processing of Capped Intron-Containing Pre-mRNA.
SIGNORiP22626.

Miscellaneous databases

ChiTaRSiHNRNPA2B1. human.
EvolutionaryTraceiP22626.
GeneWikiiHNRPA2B1.
GenomeRNAii3181.
PMAP-CutDBP22626.
PROiP22626.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000122566.
CleanExiHS_HNRNPA2B1.
ExpressionAtlasiP22626. baseline and differential.
GenevisibleiP22626. HS.

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...

Entry informationi

Entry nameiROA2_HUMAN
AccessioniPrimary (citable) accession number: P22626
Secondary accession number(s): A0A024RA27
, A0A024RA61, A8K064, P22627, Q9UC98, Q9UDJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: November 1, 1991
Last modified: November 30, 2016
This is version 188 of the entry and version 2 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.