Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Epstein-Barr nuclear antigen 2

Gene

EBNA2

Organism
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 - Biological processi

Complete GO annotation...

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]
Proteomesi
  • UP000007640 Componenti: Genome

Subcellular locationi

  • Host nucleus matrix 1 Publication

  • Note: Associated with the nuclear matrix.

GO - Cellular componenti

  • host cell nuclear matrix Source: UniProtKB-SubCell
  • host cell nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Host nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi385L → A: Complete loss of interaction with host ZMYND11. 1 Publication1
Mutagenesisi439L → A: Complete loss of interaction with host ZMYND11. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001161761 – 487Epstein-Barr nuclear antigen 2Add BLAST487

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 WAPL. 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

BioGridi971803. 2 interactors.
DIPiDIP-41174N.
IntActiP12978. 4 interactors.
MINTiMINT-2576568.

Structurei

Secondary structure

1487
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 9Combined sources7
Beta strandi12 – 20Combined sources9
Beta strandi26 – 34Combined sources9
Helixi36 – 39Combined sources4
Beta strandi45 – 52Combined sources8
Helixi455 – 463Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2MKRNMR-B453-465[»]
2N2JNMR-A/B1-58[»]
5HDAX-ray2.39B/D381-389[»]
SMRiP12978.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati345 – 34612
Repeati347 – 34822
Repeati349 – 35032
Repeati351 – 35242
Repeati353 – 35452
Repeati355 – 35662
Repeati357 – 35872

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 210SMARCB1/INI1 bindingAdd BLAST210
Regioni345 – 3586.5 X 2 AA tandem repeats of R-GAdd BLAST14

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi383 – 387PXLXP motif, interaction with host ZMYND115
Motifi437 – 441PXLXP motif, interaction with host ZMYND115

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi59 – 100Poly-ProAdd BLAST42

Sequence similaritiesi

Belongs to the herpesviridae EBNA2 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

KOiK19457.

Sequencei

Sequence statusi: Complete.

P12978-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPTFYLALHG GQTYHLIVDT DSLGNPSLSV IPSNPYQEQL SDTPLIPLTI
60 70 80 90 100
FVGENTGVPP PLPPPPPPPP PPPPPPPPPP PPPPPPPPSP PPPPPPPPPP
110 120 130 140 150
QRRDAWTQEP SPLDRDPLGY DVGHGPLASA MRMLWMANYI VRQSRGDRGL
160 170 180 190 200
ILPQGPQTAP QARLVQPHVP PLRPTAPTIL SPLSQPRLTP PQPLMMPPRP
210 220 230 240 250
TPPTPLPPAT LTVPPRPTRP TTLPPTPLLT VLQRPTELQP TPSPPRMHLP
260 270 280 290 300
VLHVPDQSMH PLTHQSTPND PDSPEPRSPT VFYNIPPMPL PPSQLPPPAA
310 320 330 340 350
PAQPPPGVIN DQQLHHLPSG PPWWPPICDP PQPSKTQGQS RGQSRGRGRG
360 370 380 390 400
RGRGRGKGKS RDKQRKPGGP WRPEPNTSSP SMPELSPVLG LHQGQGAGDS
410 420 430 440 450
PTPGPSNAAP VCRNSHTATP NVSPIHEPES HNSPEAPILF PDDWYPPSID
460 470 480
PADLDESWDY IFETTESPSS DEDYVEGPSK RPRPSIQ
Length:487
Mass (Da):52,545
Last modified:October 1, 1989 - v1
Checksum:iDEF40D7F8ED61D1A
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti88P → PPPP in AAA45903 (PubMed:6209719).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
KEGGivg:3783761.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2MKRNMR-B453-465[»]
2N2JNMR-A/B1-58[»]
5HDAX-ray2.39B/D381-389[»]
SMRiP12978.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi971803. 2 interactors.
DIPiDIP-41174N.
IntActiP12978. 4 interactors.
MINTiMINT-2576568.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3783761.
KEGGivg:3783761.

Phylogenomic databases

KOiK19457.

Family and domain databases

ProtoNetiSearch...

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: November 2, 2016
This is version 102 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

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.