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Q13151

- ROA0_HUMAN

UniProt

Q13151 - ROA0_HUMAN

Protein

Heterogeneous nuclear ribonucleoprotein A0

Gene

HNRNPA0

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    mRNA-binding component of ribonucleosomes. Specifically binds AU-rich element (ARE)-containing mRNAs. Involved in post-transcriptional regulation of cytokines mRNAs.1 Publication

    GO - Molecular functioni

    1. AU-rich element binding Source: UniProtKB
    2. nucleotide binding Source: InterPro
    3. poly(A) RNA binding Source: UniProtKB
    4. protein kinase binding Source: UniProtKB
    5. RNA binding Source: ProtInc

    GO - Biological processi

    1. 3'-UTR-mediated mRNA stabilization Source: UniProtKB
    2. gene expression Source: Reactome
    3. inflammatory response Source: UniProtKB
    4. mRNA processing Source: ProtInc
    5. mRNA splicing, via spliceosome Source: Reactome
    6. response to lipopolysaccharide Source: UniProtKB
    7. RNA splicing Source: Reactome

    Keywords - Molecular functioni

    Ribonucleoprotein

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_125. Processing of Capped Intron-Containing Pre-mRNA.
    REACT_467. mRNA Splicing - Major Pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heterogeneous nuclear ribonucleoprotein A0
    Short name:
    hnRNP A0
    Gene namesi
    Name:HNRNPA0
    Synonyms:HNRPA0
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:5030. HNRNPA0.

    Subcellular locationi

    Nucleus By similarity
    Note: Component of ribonucleosomes.By similarity

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome
    2. nucleus Source: ProtInc
    3. ribonucleoprotein complex Source: UniProtKB-KW

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162391106.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 305305Heterogeneous nuclear ribonucleoprotein A0PRO_0000081826Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei84 – 841Phosphoserine; by MAPKAPK21 Publication
    Modified residuei133 – 1331N6-acetyllysineBy similarity
    Modified residuei188 – 1881Phosphoserine1 Publication
    Modified residuei291 – 2911Dimethylated arginine1 Publication

    Post-translational modificationi

    Phosphorylated at Ser-84 by MAPKAPK2 in response to LPS treatment, promoting stabilization of GADD45A mRNA.2 Publications
    Arg-291 is dimethylated, probably to asymmetric dimethylarginine.

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ13151.
    PaxDbiQ13151.
    PeptideAtlasiQ13151.
    PRIDEiQ13151.

    2D gel databases

    REPRODUCTION-2DPAGEQ13151.
    SWISS-2DPAGEQ13151.

    PTM databases

    PhosphoSiteiQ13151.

    Expressioni

    Gene expression databases

    BgeeiQ13151.
    CleanExiHS_HNRNPA0.
    GenevestigatoriQ13151.

    Organism-specific databases

    HPAiHPA036569.

    Interactioni

    Protein-protein interaction databases

    BioGridi116149. 87 interactions.
    IntActiQ13151. 27 interactions.
    MINTiMINT-5001237.
    STRINGi9606.ENSP00000316042.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13151.
    SMRiQ13151. Positions 2-193.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini7 – 8680RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini98 – 17578RRM 2PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi191 – 305115Gly-richAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0724.
    HOGENOMiHOG000234442.
    HOVERGENiHBG002295.
    InParanoidiQ13151.
    KOiK12894.
    OMAiPKEDIHA.
    OrthoDBiEOG715Q6V.
    PhylomeDBiQ13151.
    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. 1 hit.
    [Graphical view]
    SMARTiSM00360. RRM. 2 hits.
    [Graphical view]
    PROSITEiPS50102. RRM. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q13151-1 [UniParc]FASTAAdd to Basket

    « Hide

    MENSQLCKLF IGGLNVQTSE SGLRGHFEAF GTLTDCVVVV NPQTKRSRCF    50
    GFVTYSNVEE ADAAMAASPH AVDGNTVELK RAVSREDSAR PGAHAKVKKL 100
    FVGGLKGDVA EGDLIEHFSQ FGTVEKAEII ADKQSGKKRG FGFVYFQNHD 150
    AADKAAVVKF HPIQGHRVEV KKAVPKEDIY SGGGGGGSRS SRGGRGGRGR 200
    GGGRDQNGLS KGGGGGYNSY GGYGGGGGGG YNAYGGGGGG SSYGGSDYGN 250
    GFGGFGSYSQ HQSSYGPMKS GGGGGGGGSS WGGRSNSGPY RGGYGGGGGY 300
    GGSSF 305
    Length:305
    Mass (Da):30,841
    Last modified:November 1, 1996 - v1
    Checksum:i9A976A39345AA149
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS4193.1.
    RefSeqiNP_006796.1. NM_006805.3.
    UniGeneiHs.645902.
    Hs.96996.

    Genome annotation databases

    EnsembliENST00000314940; ENSP00000316042; ENSG00000177733.
    GeneIDi10949.
    KEGGihsa:10949.
    UCSCiuc003lbt.3. human.

    Polymorphism databases

    DMDMi8134660.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS4193.1.
    RefSeqi NP_006796.1. NM_006805.3.
    UniGenei Hs.645902.
    Hs.96996.

    3D structure databases

    ProteinModelPortali Q13151.
    SMRi Q13151. Positions 2-193.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116149. 87 interactions.
    IntActi Q13151. 27 interactions.
    MINTi MINT-5001237.
    STRINGi 9606.ENSP00000316042.

    PTM databases

    PhosphoSitei Q13151.

    Polymorphism databases

    DMDMi 8134660.

    2D gel databases

    REPRODUCTION-2DPAGE Q13151.
    SWISS-2DPAGE Q13151.

    Proteomic databases

    MaxQBi Q13151.
    PaxDbi Q13151.
    PeptideAtlasi Q13151.
    PRIDEi Q13151.

    Protocols and materials databases

    DNASUi 10949.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000314940 ; ENSP00000316042 ; ENSG00000177733 .
    GeneIDi 10949.
    KEGGi hsa:10949.
    UCSCi uc003lbt.3. human.

    Organism-specific databases

    CTDi 10949.
    GeneCardsi GC05M137114.
    HGNCi HGNC:5030. HNRNPA0.
    HPAi HPA036569.
    MIMi 609409. gene.
    neXtProti NX_Q13151.
    PharmGKBi PA162391106.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0724.
    HOGENOMi HOG000234442.
    HOVERGENi HBG002295.
    InParanoidi Q13151.
    KOi K12894.
    OMAi PKEDIHA.
    OrthoDBi EOG715Q6V.
    PhylomeDBi Q13151.
    TreeFami TF351342.

    Enzyme and pathway databases

    Reactomei REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
    REACT_467. mRNA Splicing - Major Pathway.

    Miscellaneous databases

    GeneWikii HNRNPA0.
    GenomeRNAii 10949.
    NextBioi 41601.
    PROi Q13151.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q13151.
    CleanExi HS_HNRNPA0.
    Genevestigatori Q13151.

    Family and domain databases

    Gene3Di 3.30.70.330. 2 hits.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF00076. RRM_1. 1 hit.
    [Graphical view ]
    SMARTi SM00360. RRM. 2 hits.
    [Graphical view ]
    PROSITEi PS50102. RRM. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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. 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].

    Entry informationi

    Entry nameiROA0_HUMAN
    AccessioniPrimary (citable) accession number: Q13151
    Secondary accession number(s): Q6IB18
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 145 of the entry and version 1 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3