Epstein-Barr nuclear antigen 2 - Epstein-Barr virus (strain B95-8) (HHV-4)

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P12978 (EBNA2_EBVB9) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 78. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Epstein-Barr nuclear antigen 2
Short name=EBNA-2
Short name=EBV nuclear antigen 2

Gene names

Name:	EBNA2
ORF Names:	BYRF1

Organism

Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)

Taxonomic identifier

10377 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Gammaherpesvirinae › Lymphocryptovirus

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	487 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a key role in the activation of the host resting B-cell and stimulation of B-cell proliferation. Acts by upregulating 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. Ref.11
Subunit structure	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). Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10
Subcellular location	Host nucleus matrix. Note: Associated with the nuclear matrix. Ref.3
Post-translational modification	Phosphorylated. Ref.3
Sequence similarities	Belongs to the herpesviridae EBNA2 family.
Sequence caution	The sequence CAA24877.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Host-virus interaction Inhibition of host innate immune response by virus Inhibition of host interferon signaling pathway by virus Modulation of host PP1 activity by virus Modulation of host cell cycle by virus Transcription Transcription regulation Viral immunoevasion
Cellular component	Host nucleus
Domain	Repeat
Molecular function	Activator
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	evasion by virus of host immune response Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of transcription, DNA-dependent Inferred from direct assay. Source: BHF-UCL transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	host cell nuclear matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 487

487

Epstein-Barr nuclear antigen 2

PRO_0000116176

Regions

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Region

210

SMARCB1/INI1 binding

Region

345 – 358

6.5 X 2 AA tandem repeats of R-G

Motif

383 – 387

PXLXP motif, interaction with host ZMYND11

Motif

437 – 441

PXLXP motif, interaction with host ZMYND11

Compositional bias

59 – 100

Poly-Pro

Experimental info

Mutagenesis

385

L → A: Complete loss of interaction with host ZMYND11. Ref.9

Mutagenesis

439

L → A: Complete loss of interaction with host ZMYND11. Ref.9

Sequence conflict

P → PPPP in AAA45903. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P12978 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: DEF40D7F8ED61D1A
Show »

FASTA

487

52,545

        10         20         30         40         50         60 
MPTFYLALHG GQTYHLIVDT DSLGNPSLSV IPSNPYQEQL SDTPLIPLTI FVGENTGVPP 

        70         80         90        100        110        120 
PLPPPPPPPP PPPPPPPPPP PPPPPPPPSP PPPPPPPPPP QRRDAWTQEP SPLDRDPLGY 

       130        140        150        160        170        180 
DVGHGPLASA MRMLWMANYI VRQSRGDRGL ILPQGPQTAP QARLVQPHVP PLRPTAPTIL 

       190        200        210        220        230        240 
SPLSQPRLTP PQPLMMPPRP TPPTPLPPAT LTVPPRPTRP TTLPPTPLLT VLQRPTELQP 

       250        260        270        280        290        300 
TPSPPRMHLP VLHVPDQSMH PLTHQSTPND PDSPEPRSPT VFYNIPPMPL PPSQLPPPAA 

       310        320        330        340        350        360 
PAQPPPGVIN DQQLHHLPSG PPWWPPICDP PQPSKTQGQS RGQSRGRGRG RGRGRGKGKS 

       370        380        390        400        410        420 
RDKQRKPGGP WRPEPNTSSP SMPELSPVLG LHQGQGAGDS PTPGPSNAAP VCRNSHTATP 

       430        440        450        460        470        480 
NVSPIHEPES HNSPEAPILF PDDWYPPSID PADLDESWDY IFETTESPSS DEDYVEGPSK 


RPRPSIQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 6209719] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"DNA sequence and expression of the B95-8 Epstein-Barr virus genome." Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J., Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C., Tuffnell P.S., Barrell B.G. Nature 310:207-211(1984) [PubMed: 6087149] [Abstract] 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: 2161150] [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: 1850028] [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: 8016657] [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: 7724549] [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: 7983760] [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: 8709224] [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: 11733528] [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: 15383329] [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: 19126642] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	K03333 Genomic DNA. Translation: AAA45903.1. V01555 Genomic DNA. Translation: CAA24877.1. Different initiation. AJ507799 Genomic DNA. Translation: CAD53395.1.
PIR	S42442.
RefSeq	YP_401644.1. NC_007605.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-2576568.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3783761.
Phylogenomic databases
ProtClustDB	CLSP2512498.
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

EBNA2_EBVB9

Accession

Primary (citable) accession number: P12978
Secondary accession number(s): Q69023, Q777H1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	September 21, 2011
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents