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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

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti302 – 3021D → V in IBMPFD2. 1 Publication
VAR_070591

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi207 – 2071F → S: Does not affect hydrogel-binding. 1 Publication
Mutagenesisi209 – 2091F → S: Does not affect hydrogel-binding. 1 Publication
Mutagenesisi219 – 2191F → S: Does not affect hydrogel-binding. 1 Publication
Mutagenesisi227 – 2271F → S: Does not affect hydrogel-binding. 1 Publication
Mutagenesisi234 – 2341Y → S: Does not affect hydrogel-binding. 1 Publication
Mutagenesisi240 – 2401F → S: Does not affect hydrogel-binding. 1 Publication
Mutagenesisi244 – 2441Y → S: Does not affect hydrogel-binding. 1 Publication
Mutagenesisi247 – 2471Y → S: Slightly affects hydrogel-binding. 1 Publication
Mutagenesisi256 – 2561F → S: Does not affect hydrogel-binding. 1 Publication
Mutagenesisi262 – 2621Y → S: Slightly affects hydrogel-binding. 1 Publication
Mutagenesisi269 – 2691Y → S: Does not affect hydrogel-binding. 1 Publication
Mutagenesisi276 – 2761Y → S: Impairs hydrogel-binding. 1 Publication
Mutagenesisi283 – 2831Y → S: Slightly affects hydrogel-binding. 1 Publication
Mutagenesisi287 – 2871Y → S: Does not affect hydrogel-binding. 1 Publication
Mutagenesisi290 – 2901Y → S: Impairs hydrogel-binding. 1 Publication
Mutagenesisi295 – 2951Y → S: Impairs hydrogel-binding. 1 Publication
Mutagenesisi300 – 3001Y → S: Slightly affects hydrogel-binding. 1 Publication
Mutagenesisi303 – 3031F → S: Impairs hydrogel-binding. 1 Publication
Mutagenesisi306 – 3061Y → S: Slightly affects hydrogel-binding. 1 Publication
Mutagenesisi313 – 3131Y → S: Slightly affects hydrogel-binding. 1 Publication
Mutagenesisi321 – 3211F → S: Impairs hydrogel-binding. 1 Publication
Mutagenesisi331 – 3311Y → S: Impairs hydrogel-binding. 1 Publication
Mutagenesisi336 – 3361Y → S: Slightly affects hydrogel-binding. 1 Publication
Mutagenesisi347 – 3471Y → S: Does not affect hydrogel-binding. 1 Publication
Mutagenesisi353 – 3531Y → S: Does not affect hydrogel-binding. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

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

Chemistry

ChEMBLiCHEMBL3137265.

Polymorphism and mutation databases

BioMutaiHNRNPA2B1.
DMDMi133257.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 353353Heterogeneous nuclear ribonucleoproteins A2/B1PRO_0000081836Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources1 Publication
Modified residuei29 – 291PhosphoserineCombined sources
Modified residuei85 – 851PhosphoserineCombined sources
Modified residuei104 – 1041N6,N6-dimethyllysine1 Publication
Cross-linki120 – 120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei149 – 1491PhosphoserineCombined sources
Modified residuei168 – 1681N6-acetyllysineCombined sources
Modified residuei173 – 1731N6-acetyllysineCombined sources
Cross-linki186 – 186Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei203 – 2031Dimethylated arginine; alternate1 Publication
Modified residuei203 – 2031Omega-N-methylarginine; alternateCombined sources1 Publication
Modified residuei212 – 2121PhosphoserineCombined sources
Modified residuei213 – 2131Dimethylated arginine; alternate1 Publication
Modified residuei213 – 2131Omega-N-methylarginine; alternate1 Publication
Modified residuei225 – 2251PhosphoserineCombined sources
Modified residuei231 – 2311PhosphoserineCombined sources
Modified residuei236 – 2361PhosphoserineCombined sources
Modified residuei259 – 2591PhosphoserineCombined sources
Modified residuei266 – 2661Asymmetric dimethylarginineBy similarity
Modified residuei324 – 3241PhosphoserineCombined sources
Modified residuei331 – 3311PhosphotyrosineCombined sources
Modified residuei341 – 3411PhosphoserineCombined sources
Modified residuei344 – 3441PhosphoserineCombined sources
Modified residuei347 – 3471PhosphotyrosineCombined sources

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.
PRIDEiP22626.
TopDownProteomicsiP22626-1. [P22626-1]
P22626-2. [P22626-2]

2D gel databases

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

PTM databases

iPTMnetiP22626.
PhosphoSiteiP22626.
SwissPalmiP22626.

Miscellaneous databases

PMAP-CutDBP22626.

Expressioni

Gene expression databases

BgeeiP22626.
CleanExiHS_HNRNPA2B1.
ExpressionAtlasiP22626. baseline and differential.
GenevisibleiP22626. HS.

Organism-specific databases

HPAiCAB012403.
HPA001666.

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. 183 interactions.
DIPiDIP-32877N.
IntActiP22626. 97 interactions.
MINTiMINT-4998934.
STRINGi9606.ENSP00000346694.

Structurei

Secondary structure

1
353
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 205Combined sources
Beta strandi22 – 265Combined sources
Helixi34 – 418Combined sources
Beta strandi48 – 525Combined sources
Turni56 – 583Combined sources
Beta strandi63 – 686Combined sources
Helixi72 – 798Combined sources
Beta strandi83 – 864Combined sources
Beta strandi89 – 946Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X4BNMR-A1-103[»]
ProteinModelPortaliP22626.
SMRiP22626. Positions 1-193.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22626.

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 analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi202 – 353152Gly-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.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.
OrthoDBiEOG715Q6V.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti205 – 2051G → S in BAF82118 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti302 – 3021D → V in IBMPFD2. 1 Publication
VAR_070591

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei3 – 1412Missing in isoform A2. 1 PublicationVSP_005830Add
BLAST

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]
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]
UniGeneiHs.487774.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X4BNMR-A1-103[»]
ProteinModelPortaliP22626.
SMRiP22626. Positions 1-193.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109422. 183 interactions.
DIPiDIP-32877N.
IntActiP22626. 97 interactions.
MINTiMINT-4998934.
STRINGi9606.ENSP00000346694.

Chemistry

ChEMBLiCHEMBL3137265.

PTM databases

iPTMnetiP22626.
PhosphoSiteiP22626.
SwissPalmiP22626.

Polymorphism and mutation databases

BioMutaiHNRNPA2B1.
DMDMi133257.

2D gel databases

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

Proteomic databases

EPDiP22626.
MaxQBiP22626.
PaxDbiP22626.
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.
GeneCardsiHNRNPA2B1.
HGNCiHGNC:5033. HNRNPA2B1.
HPAiCAB012403.
HPA001666.
MalaCardsiHNRNPA2B1.
MIMi600124. gene.
615422. phenotype.
neXtProtiNX_P22626.
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.
OrthoDBiEOG715Q6V.
PhylomeDBiP22626.
TreeFamiTF351342.

Enzyme and pathway databases

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

BgeeiP22626.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structures of the heterogeneous nuclear ribonucleoprotein A2, B1, and C2 proteins: a diversity of RNA binding proteins is generated by small peptide inserts."
    Burd C.G., Swanson M.S., Goerlach M., Dreyfuss G.
    Proc. Natl. Acad. Sci. U.S.A. 86:9788-9792(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B1 AND A2).
  2. "Two homologous genes, originated by duplication, encode the human hnRNP proteins A2 and A1."
    Biamonti G., Ruggiu M., Saccone S., Della Valle G., Riva S.
    Nucleic Acids Res. 22:1996-2002(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Liver.
  3. "Structure and expression of the gene (HNRPA2B1) encoding the human hnRNP protein A2/B1."
    Kozu T., Henrich B., Schaefer K.P.
    Genomics 25:365-371(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B1).
    Tissue: Glial tumor.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: PROTEIN SEQUENCE OF 1-12; 22-59; 63-89; 100-147; 153-185; 201-266 AND 326-350, ACETYLATION AT MET-1, METHYLATION AT LYS-104; ARG-203 AND ARG-213, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Ovarian carcinoma.
  7. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 22-38; 154-168; 174-185; 214-228 AND 326-350, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  8. "Purification and partial sequencing of the nuclear autoantigen RA33 shows that it is indistinguishable from the A2 protein of the heterogeneous nuclear ribonucleoprotein complex."
    Steiner G., Hartmuth K., Skriner K., Maurer-Fogy I., Sinski A., Thalmann E., Hassfeld W., Barta A., Smolen J.S.
    J. Clin. Invest. 90:1061-1066(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 39-46; 154-168; 204-228 AND 267-286.
    Tissue: Cervix carcinoma.
  9. "ADP-ribosylation of heterogeneous ribonucleoproteins in HeLa cells."
    Prasad S., Walent J., Dritschilo A.
    Biochem. Biophys. Res. Commun. 204:772-779(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 80-100.
    Tissue: Cervix carcinoma.
  10. "Purification and domain structure of core hnRNP proteins A1 and A2 and their relationship to single-stranded DNA-binding proteins."
    Kumar A., Willams K.R., Szer W.
    J. Biol. Chem. 261:11266-11273(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 100-107; 121-128 AND 174-180.
  11. "Two-dimensional gel electrophoresis, protein electroblotting and microsequencing: a direct link between proteins and genes."
    Bauw G., Rasmussen H.H., van den Bulcke M., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
    Electrophoresis 11:528-536(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 154-160; 204-212 AND 214-228.
  12. "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.
  13. Cited for: SUBCELLULAR LOCATION (ISOFORM A2), METHYLATION.
  14. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
    Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
    RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
  15. "A late role for the association of hnRNP A2 with the HIV-1 hnRNP A2 response elements in genomic RNA, Gag, and Vpr localization."
    Beriault V., Clement J.F., Levesque K., Lebel C., Yong X., Chabot B., Cohen E.A., Cochrane A.W., Rigby W.F., Mouland A.J.
    J. Biol. Chem. 279:44141-44153(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (MICROBIAL INFECTION).
  16. "Identifying and quantifying in vivo methylation sites by heavy methyl SILAC."
    Ong S.E., Mittler G., Mann M.
    Nat. Methods 1:119-126(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "The microtubule-associated protein tumor overexpressed gene binds to the RNA trafficking protein heterogeneous nuclear ribonucleoprotein A2."
    Kosturko L.D., Maggipinto M.J., D'Sa C., Carson J.H., Barbarese E.
    Mol. Biol. Cell 16:1938-1947(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CKAP5.
  18. "Trafficking of HIV-1 RNA is mediated by heterogeneous nuclear ribonucleoprotein A2 expression and impacts on viral assembly."
    Levesque K., Halvorsen M., Abrahamyan L., Chatel-Chaix L., Poupon V., Gordon H., DesGroseillers L., Gatignol A., Mouland A.J.
    Traffic 7:1177-1193(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (MICROBIAL INFECTION).
  19. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259 AND SER-341, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  21. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259 AND SER-341, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259; SER-341 AND SER-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "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.
  26. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "Functional mapping of the interaction between TDP-43 and hnRNP A2 in vivo."
    D'Ambrogio A., Buratti E., Stuani C., Guarnaccia C., Romano M., Ayala Y.M., Baralle F.E.
    Nucleic Acids Res. 37:4116-4126(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TARDBP.
  28. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-212; SER-259 AND SER-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  29. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-168 AND LYS-173, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-149; SER-212; SER-225; SER-231; SER-259; SER-341 AND SER-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  31. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212; SER-225; SER-231; SER-236; SER-259; SER-324; TYR-331 AND SER-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  33. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  34. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  35. Cited for: FUNCTION, SUBCELLULAR LOCATION, SUMOYLATION.
  36. "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: SUBCELLULAR LOCATION (ISOFORM A2).
  37. "C9ORF72, implicated in amytrophic lateral sclerosis and frontotemporal dementia, regulates endosomal trafficking."
    Farg M.A., Sundaramoorthy V., Sultana J.M., Yang S., Atkinson R.A., Levina V., Halloran M.A., Gleeson P.A., Blair I.P., Soo K.Y., King A.E., Atkin J.D.
    Hum. Mol. Genet. 23:3579-3595(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH C9ORF72.
  38. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-85; SER-212; SER-225; SER-231; SER-341; SER-344 AND TYR-347, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  39. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-120 AND LYS-186, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  40. "The LC domain of hnRNPA2 adopts similar conformations in hydrogel polymers, liquid-like droplets, and nuclei."
    Xiang S., Kato M., Wu L.C., Lin Y., Ding M., Zhang Y., Yu Y., McKnight S.L.
    Cell 163:829-839(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN, MUTAGENESIS OF PHE-207; PHE-209; PHE-219; PHE-227; TYR-234; PHE-240; TYR-244; TYR-247; PHE-256; TYR-262; TYR-269; TYR-276; TYR-283; TYR-287; TYR-290; TYR-295; TYR-300; PHE-303; TYR-306; TYR-313; PHE-321; TYR-331; TYR-336; TYR-347 AND TYR-353.
  41. "HNRNPA2B1 is a mediator of m(6)A-dependent nuclear RNA processing events."
    Alarcon C.R., Goodarzi H., Lee H., Liu X., Tavazoie S., Tavazoie S.F.
    Cell 162:1299-1308(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MIRNA-BINDING, INTERACTION WITH DGCR8.
  42. "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability."
    Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C.
    Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-120, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  43. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  44. "Solution structure of RRM domain in heterogeneous nuclear ribonucleoproteins A2/B1."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1-103.
  45. Cited for: VARIANT IBMPFD2 VAL-302.

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: June 8, 2016
This is version 183 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.