EBNA2_EBVA8
ID EBNA2_EBVA8 Reviewed; 454 AA.
AC Q69022;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 02-JUN-2021, entry version 79.
DE RecName: Full=Epstein-Barr nuclear antigen 2;
DE Short=EBNA-2;
DE Short=EBV nuclear antigen 2;
GN Name=EBNA2; ORFNames=BYRF1;
OS Epstein-Barr virus (strain AG876) (HHV-4) (Human herpesvirus 4).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX NCBI_TaxID=82830;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6209719; DOI=10.1073/pnas.81.23.7632;
RA Dambaugh T., Hennessy K., Chamnankit L., Kieff E.;
RT "U2 region of Epstein-Barr virus DNA may encode Epstein-Barr nuclear
RT antigen 2.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:7632-7636(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16490228; DOI=10.1016/j.virol.2006.01.015;
RA Dolan A., Addison C., Gatherer D., Davison A.J., McGeoch D.J.;
RT "The genome of Epstein-Barr virus type 2 strain AG876.";
RL Virology 350:164-170(2006).
CC -!- FUNCTION: Plays a key role in the activation of the host resting B-cell
CC and stimulation of B-cell proliferation. Acts by up-regulating the
CC expression of viral EBNA1-6, LMP1, LMP2A and LMP2B genes, as well as
CC several host genes including CD21, CD23 and MYC. Activates
CC transcription by acting as an adapter molecule that binds to cellular
CC sequence-specific DNA-binding proteins such as host CBF1, SMARCB1 and
CC SPI1. Once EBNA2 is near promoter sites, its acidic activating domain
CC recruits basal and activation-associated transcription factors TFIIB,
CC TAF40, TFIIH components ERCC2 and ERCC3, and CBP in order to promote
CC transcription. Alternatively, EBNA2 can affect activities of cell cycle
CC regulators and retard cell cycle progression at G2/M phase. It also
CC induces chromosomal instability, by disrupting mitotic checkpoints,
CC multi-nucleation and formation of micronuclei in infected cells (By
CC similarity). {ECO:0000250|UniProtKB:P12978}.
CC -!- SUBUNIT: Interacts with human SMARCB1/INI1, presumably generating an
CC open chromatin conformation at the EBNA2-responsive target genes.
CC Interacts with human WAPL. Interacts with host CBF1; this interaction
CC allows transcriptional activation by EBNA2. Interacts with host general
CC transcription factors GTF2B, ERCC2 and ERCC3. Interacts (via PXLXP
CC motif) with host ZMYND11/BS69 (via MYND-type zinc finger). Interacts
CC with host EBF1 (By similarity). {ECO:0000250|UniProtKB:P12978}.
CC -!- SUBCELLULAR LOCATION: Host nucleus matrix. Note=Associated with the
CC nuclear matrix. {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the herpesviridae EBNA2 family. {ECO:0000305}.
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DR EMBL; K03332; AAA45902.1; -; Genomic_DNA.
DR EMBL; DQ279927; ABB89222.1; -; Genomic_DNA.
DR RefSeq; YP_001129441.1; NC_009334.1.
DR SASBDB; Q69022; -.
DR SMR; Q69022; -.
DR IntAct; Q69022; 8.
DR PRIDE; Q69022; -.
DR GeneID; 5176198; -.
DR KEGG; vg:5176198; -.
DR Proteomes; UP000007639; Genome.
DR GO; GO:0044204; C:host cell nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0060153; P:modulation by virus of host cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0039586; P:modulation by virus of host PP1 activity; IEA:UniProtKB-KW.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW Activator; Host nucleus; Host-virus interaction;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Modulation of host cell cycle by virus;
KW Modulation of host PP1 activity by virus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Viral immunoevasion.
FT CHAIN 1..454
FT /note="Epstein-Barr nuclear antigen 2"
FT /id="PRO_0000375934"
FT REGION 55..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 350..354
FT /note="PXLXP motif, interaction with host ZMYND11"
FT /evidence="ECO:0000250"
FT MOTIF 404..408
FT /note="PXLXP motif, interaction with host ZMYND11"
FT /evidence="ECO:0000250"
FT COMPBIAS 58..79
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..203
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..269
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..298
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..333
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 454 AA; 48971 MW; A6DE3BA0A6F4037D CRC64;
MPTYYLALHG GQSYNLIVDT DMSGNPSLSV IPTNPYQEQL SNNPLIQLQI VVGENTGAPA
PPQPPPPPPP PPPPERRDAW TQEPLPLDMN PLGSDASQGP LASSIRMLCM AQYLLRNARG
QQGLLRPLGP QTRSQVTLER QPVHNPRQEA PIILLQSPAP PRFTPVPMVA LGHTLQPTPP
PRPTLPQPRI PLIIPPRHTN QPATTPPTAP QRLTLGHQLS LPPHPPPHQS TPHCSSDSTG
LPPPPTSYSI PSMTLSPEPL PPPAAPAHPL PGVIYDQQAL PPTPGPPWWP PVRDPTPTTQ
TPPTNTKQGP DQGQGRGRWR GRGRSKGRGR MHKLPEPRRP GPDTSSPSMP QLSPVVSLHQ
GQGPENSPTP GPSTAGPVCR VTPSATPDIS PIHEPESSDS EEPPFLFPSD WYPPTLEPAE
LDESWEGIFE TTESHSSDEE NVGGPSKRPR TSTQ
