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P12978

- EBNA2_EBVB9

UniProt

P12978 - EBNA2_EBVB9

Protein

Epstein-Barr nuclear antigen 2

Gene

EBNA2

Organism
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (01 Oct 1989)
      Previous versions | rss
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    Functioni

    Plays a key role in the activation of the host resting B-cell and stimulation of B-cell proliferation. Acts by up-regulating the expression of viral EBNA1-6, LMP1, LMP2A and LMP2B genes, as well as several host genes including CD21, CD23 and MYC. Activates transcription by acting as an adapter molecule that binds to cellular sequence-specific DNA-binding proteins such as host CBF1, SMARCB1 and SPI1. Once EBNA2 is near promoter sites, its acidic activating domain recruits basal and activation-associated transcription factors TFIIB, TAF40, TFIIH components ERCC2 and ERCC3, and CBP in order to promote transcription. Alternatively, EBNA2 can affect activities of cell cycle regulators and retard cell cycle progression at G2/M phase. It also induces chromosomal instability, by disrupting mitotic checkpoints, multi-nucleation and formation of micronuclei in infected cells.1 Publication

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. modulation by virus of host cell cycle Source: UniProtKB-KW
    2. modulation by virus of host PP1 activity Source: UniProtKB-KW
    3. positive regulation of transcription, DNA-templated Source: BHF-UCL
    4. suppression by virus of host type I interferon-mediated signaling pathway Source: UniProtKB-KW
    5. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Modulation of host cell cycle by virus, Modulation of host PP1 activity by virus, Transcription, Transcription regulation, Viral immunoevasion

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Epstein-Barr nuclear antigen 2
    Short name:
    EBNA-2
    Short name:
    EBV nuclear antigen 2
    Gene namesi
    Name:EBNA2
    ORF Names:BYRF1
    OrganismiEpstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
    Taxonomic identifieri10377 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeGammaherpesvirinaeLymphocryptovirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000007640: Genome

    Subcellular locationi

    Host nucleus matrix 1 Publication
    Note: Associated with the nuclear matrix.

    GO - Cellular componenti

    1. host cell nuclear matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Host nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi385 – 3851L → A: Complete loss of interaction with host ZMYND11. 1 Publication
    Mutagenesisi439 – 4391L → A: Complete loss of interaction with host ZMYND11. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 487487Epstein-Barr nuclear antigen 2PRO_0000116176Add
    BLAST

    Post-translational modificationi

    Phosphorylated.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Interactioni

    Subunit structurei

    Interacts with human SMARCB1/INI1, presumably generating an open chromatin conformation at the EBNA2-responsive target genes. Interacts with human WAPAL. Interacts with host CBF1; this interaction allows transcriptional activation by EBNA2. Interacts with host general transcription factors GTF2B, ERCC2 and ERCC3. Interacts (via PXLXP motif) with host ZMYND11/BS69 (via MYND-type zinc finger).6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RBPJQ063302EBI-8052923,EBI-632552From a different organism.
    ZMYND11Q153262EBI-8052923,EBI-2623509From a different organism.

    Protein-protein interaction databases

    IntActiP12978. 4 interactions.
    MINTiMINT-2576568.

    Structurei

    Secondary structure

    1
    487
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi455 – 4639

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2MKRNMR-B453-465[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati345 – 34621
    Repeati347 – 34822
    Repeati349 – 35023
    Repeati351 – 35224
    Repeati353 – 35425
    Repeati355 – 35626
    Repeati357 – 35827

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 210210SMARCB1/INI1 bindingAdd
    BLAST
    Regioni345 – 358146.5 X 2 AA tandem repeats of R-GAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi383 – 3875PXLXP motif, interaction with host ZMYND11
    Motifi437 – 4415PXLXP motif, interaction with host ZMYND11

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi59 – 10042Poly-ProAdd
    BLAST

    Sequence similaritiesi

    Belongs to the herpesviridae EBNA2 family.Curated

    Keywords - Domaini

    Repeat

    Sequencei

    Sequence statusi: Complete.

    P12978-1 [UniParc]FASTAAdd to Basket

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    MPTFYLALHG GQTYHLIVDT DSLGNPSLSV IPSNPYQEQL SDTPLIPLTI    50
    FVGENTGVPP PLPPPPPPPP PPPPPPPPPP PPPPPPPPSP PPPPPPPPPP 100
    QRRDAWTQEP SPLDRDPLGY DVGHGPLASA MRMLWMANYI VRQSRGDRGL 150
    ILPQGPQTAP QARLVQPHVP PLRPTAPTIL SPLSQPRLTP PQPLMMPPRP 200
    TPPTPLPPAT LTVPPRPTRP TTLPPTPLLT VLQRPTELQP TPSPPRMHLP 250
    VLHVPDQSMH PLTHQSTPND PDSPEPRSPT VFYNIPPMPL PPSQLPPPAA 300
    PAQPPPGVIN DQQLHHLPSG PPWWPPICDP PQPSKTQGQS RGQSRGRGRG 350
    RGRGRGKGKS RDKQRKPGGP WRPEPNTSSP SMPELSPVLG LHQGQGAGDS 400
    PTPGPSNAAP VCRNSHTATP NVSPIHEPES HNSPEAPILF PDDWYPPSID 450
    PADLDESWDY IFETTESPSS DEDYVEGPSK RPRPSIQ 487
    Length:487
    Mass (Da):52,545
    Last modified:October 1, 1989 - v1
    Checksum:iDEF40D7F8ED61D1A
    GO

    Sequence cautioni

    The sequence CAA24877.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti88 – 881P → PPPP in AAA45903. (PubMed:6209719)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K03333 Genomic DNA. Translation: AAA45903.1.
    V01555 Genomic DNA. Translation: CAA24877.1. Different initiation.
    AJ507799 Genomic DNA. Translation: CAD53395.1.
    PIRiS42442.
    RefSeqiYP_401644.1. NC_007605.1.

    Genome annotation databases

    GeneIDi3783761.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K03333 Genomic DNA. Translation: AAA45903.1 .
    V01555 Genomic DNA. Translation: CAA24877.1 . Different initiation.
    AJ507799 Genomic DNA. Translation: CAD53395.1 .
    PIRi S42442.
    RefSeqi YP_401644.1. NC_007605.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2MKR NMR - B 453-465 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P12978. 4 interactions.
    MINTi MINT-2576568.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 3783761.

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. "U2 region of Epstein-Barr virus DNA may encode Epstein-Barr nuclear antigen 2."
      Dambaugh T., Hennessy K., Chamnankit L., Kieff E.
      Proc. Natl. Acad. Sci. U.S.A. 81:7632-7636(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Subnuclear localization and phosphorylation of Epstein-Barr virus latent infection nuclear proteins."
      Petti L., Sample C., Kieff E.
      Virology 176:563-574(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.
    4. "Epstein-Barr virus nuclear protein 2 mutations define essential domains for transformation and transactivation."
      Cohen J.I., Wang F., Kieff E.
      J. Virol. 65:2545-2554(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAINS.
    5. "Mediation of Epstein-Barr virus EBNA2 transactivation by recombination signal-binding protein J kappa."
      Henkel T., Ling P.D., Hayward S.D., Peterson M.G.
      Science 265:92-95(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HUMAN CBF1.
    6. "The 62- and 80-kDa subunits of transcription factor IIH mediate the interaction with Epstein-Barr virus nuclear protein 2."
      Tong X., Drapkin R., Reinberg D., Kieff E.
      Proc. Natl. Acad. Sci. U.S.A. 92:3259-3263(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HUMAN ERCC2 AND ERCC3.
    7. "The Epstein-Barr virus nuclear protein 2 acidic domain can interact with TFIIB, TAF40, and RPA70 but not with TATA-binding protein."
      Tong X., Wang F., Thut C.J., Kieff E.
      J. Virol. 69:585-588(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HUMAN GTF2B.
    8. "Epstein-Barr virus nuclear protein 2 (EBNA2) binds to a component of the human SNF-SWI complex, hSNF5/Ini1."
      Wu D.Y., Kalpana G.V., Goff S.P., Schubach W.H.
      J. Virol. 70:6020-6028(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HUMAN SMARCB1/INI1.
    9. "The conserved Mynd domain of BS69 binds cellular and oncoviral proteins through a common PXLXP motif."
      Ansieau S., Leutz A.
      J. Biol. Chem. 277:4906-4910(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HUMAN ZMYND11/BS69, MUTAGENESIS OF LEU-385 AND LEU-439.
    10. "Identification and cloning of a novel chromatin-associated protein partner of Epstein-Barr nuclear protein 2."
      Kwiatkowski B.A., Ragoczy T., Ehly J., Schubach W.H.
      Exp. Cell Res. 300:223-233(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HUMAN WAPAL.
    11. "Epstein-Barr virus nuclear antigen 2 disrupts mitotic checkpoint and causes chromosomal instability."
      Pan S.H., Tai C.C., Lin C.S., Hsu W.B., Chou S.F., Lai C.C., Chen J.Y., Tien H.F., Lee F.Y., Wang W.B.
      Carcinogenesis 30:366-375(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiEBNA2_EBVB9
    AccessioniPrimary (citable) accession number: P12978
    Secondary accession number(s): Q69023, Q777H1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 89 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3