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Q13151 (ROA0_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heterogeneous nuclear ribonucleoprotein A0

Short name=hnRNP A0
Gene names
Name:HNRNPA0
Synonyms:HNRPA0
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length305 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

mRNA-binding component of ribonucleosomes. Specifically binds AU-rich element (ARE)-containing mRNAs. Involved in post-transcriptional regulation of cytokines mRNAs. Ref.6

Subcellular location

Nucleus By similarity. Note: Component of ribonucleosomes By similarity.

Post-translational modification

Phosphorylated at Ser-84 by MAPKAPK2 in response to LPS treatment, promoting stabilization of GADD45A mRNA. Ref.8

Arg-291 is dimethylated, probably to asymmetric dimethylarginine. Ref.5

Sequence similarities

Contains 2 RRM (RNA recognition motif) domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 305305Heterogeneous nuclear ribonucleoprotein A0
PRO_0000081826

Regions

Domain7 – 8680RRM 1
Domain98 – 17578RRM 2
Compositional bias191 – 305115Gly-rich

Amino acid modifications

Modified residue11N-acetylmethionine Ref.7 Ref.11
Modified residue841Phosphoserine; by MAPKAPK2 Ref.8
Modified residue1331N6-acetyllysine By similarity
Modified residue1881Phosphoserine Ref.10
Modified residue2911Dimethylated arginine Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q13151 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 9A976A39345AA149

FASTA30530,841
        10         20         30         40         50         60 
MENSQLCKLF IGGLNVQTSE SGLRGHFEAF GTLTDCVVVV NPQTKRSRCF GFVTYSNVEE 

        70         80         90        100        110        120 
ADAAMAASPH AVDGNTVELK RAVSREDSAR PGAHAKVKKL FVGGLKGDVA EGDLIEHFSQ 

       130        140        150        160        170        180 
FGTVEKAEII ADKQSGKKRG FGFVYFQNHD AADKAAVVKF HPIQGHRVEV KKAVPKEDIY 

       190        200        210        220        230        240 
SGGGGGGSRS SRGGRGGRGR GGGRDQNGLS KGGGGGYNSY GGYGGGGGGG YNAYGGGGGG 

       250        260        270        280        290        300 
SSYGGSDYGN GFGGFGSYSQ HQSSYGPMKS GGGGGGGGSS WGGRSNSGPY RGGYGGGGGY 


GGSSF 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of a novel, low abundance hnRNP protein: A0."
Myer V.E., Steitz J.A.
RNA 1:171-182(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 143-154 AND 287-305.
Tissue: Placenta.
[2]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain, Eye, Lung, Muscle, Placenta and Skin.
[5]Bienvenut W.V., Zebisch A., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 9-24; 99-126; 140-154; 173-189 AND 285-305, METHYLATION AT ARG-291, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Colon carcinoma and Ovarian carcinoma.
[6]"Inhibition of SAPK2a/p38 prevents hnRNP A0 phosphorylation by MAPKAP-K2 and its interaction with cytokine mRNAs."
Rousseau S., Morrice N., Peggie M., Campbell D.G., Gaestel M., Cohen P.
EMBO J. 21:6505-6514(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, RNA-BINDING.
[7]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"DNA damage activates a spatially distinct late cytoplasmic cell-cycle checkpoint network controlled by MK2-mediated RNA stabilization."
Reinhardt H.C., Hasskamp P., Schmedding I., Morandell S., van Vugt M.A., Wang X., Linding R., Ong S.E., Weaver D., Carr S.A., Yaffe M.B.
Mol. Cell 40:34-49(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA-BINDING, PHOSPHORYLATION AT SER-84 BY MAPKAPK2.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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-188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U23803 mRNA. Translation: AAA65094.1.
CR456986 mRNA. Translation: CAG33267.1.
CH471062 Genomic DNA. Translation: EAW62182.1.
BC001008 mRNA. Translation: AAH01008.1.
BC007271 mRNA. Translation: AAH07271.1.
BC009284 mRNA. Translation: AAH09284.1.
BC011972 mRNA. Translation: AAH11972.1.
BC012980 mRNA. Translation: AAH12980.1.
BC018949 mRNA. Translation: AAH18949.1.
BC019271 mRNA. Translation: AAH19271.1.
BC028976 mRNA. Translation: AAH28976.1.
BC030249 mRNA. Translation: AAH30249.1.
RefSeqNP_006796.1. NM_006805.3.
UniGeneHs.645902.
Hs.96996.

3D structure databases

ProteinModelPortalQ13151.
SMRQ13151. Positions 2-181.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116149. 84 interactions.
IntActQ13151. 27 interactions.
MINTMINT-5001237.
STRING9606.ENSP00000316042.

PTM databases

PhosphoSiteQ13151.

Polymorphism databases

DMDM8134660.

2D gel databases

REPRODUCTION-2DPAGEQ13151.
SWISS-2DPAGEQ13151.

Proteomic databases

PaxDbQ13151.
PeptideAtlasQ13151.
PRIDEQ13151.

Protocols and materials databases

DNASU10949.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000314940; ENSP00000316042; ENSG00000177733.
GeneID10949.
KEGGhsa:10949.
UCSCuc003lbt.3. human.

Organism-specific databases

CTD10949.
GeneCardsGC05M137114.
HGNCHGNC:5030. HNRNPA0.
HPAHPA036569.
MIM609409. gene.
neXtProtNX_Q13151.
PharmGKBPA162391106.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0724.
HOGENOMHOG000234442.
HOVERGENHBG002295.
InParanoidQ13151.
KOK12894.
OMAGPMKQNL.
OrthoDBEOG715Q6V.
PhylomeDBQ13151.
TreeFamTF351342.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

BgeeQ13151.
CleanExHS_HNRNPA0.
GenevestigatorQ13151.

Family and domain databases

Gene3D3.30.70.330. 2 hits.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 2 hits.
[Graphical view]
PROSITEPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiHNRNPA0.
GenomeRNAi10949.
NextBio41601.
PROQ13151.
SOURCESearch...

Entry information

Entry nameROA0_HUMAN
AccessionPrimary (citable) accession number: Q13151
Secondary accession number(s): Q6IB18
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM