EBNA2_EBVG
ID EBNA2_EBVG Reviewed; 451 AA.
AC Q3KSV2;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 02-JUN-2021, entry version 54.
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 GD1) (HHV-4) (Human herpesvirus 4).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX NCBI_TaxID=10376;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16306603; DOI=10.1128/jvi.79.24.15323-15330.2005;
RA Zeng M.-S., Li D.-J., Liu Q.-L., Song L.-B., Li M.-Z., Zhang R.-H.,
RA Yu X.-J., Wang H.-M., Ernberg I., Zeng Y.-X.;
RT "Genomic sequence analysis of Epstein-Barr virus strain GD1 from a
RT nasopharyngeal carcinoma patient.";
RL J. Virol. 79:15323-15330(2005).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY961628; AAY41099.1; -; Genomic_DNA.
DR BMRB; Q3KSV2; -.
DR SMR; Q3KSV2; -.
DR IntAct; Q3KSV2; 13.
DR Proteomes; UP000007641; 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; Repeat;
KW Transcription; Transcription regulation; Viral immunoevasion.
FT CHAIN 1..451
FT /note="Epstein-Barr nuclear antigen 2"
FT /id="PRO_0000226600"
FT REPEAT 311..312
FT /note="1"
FT REPEAT 313..314
FT /note="2"
FT REPEAT 315..316
FT /note="3"
FT REPEAT 317..318
FT /note="4"
FT REPEAT 319..320
FT /note="5"
FT REPEAT 321..322
FT /note="6"
FT REPEAT 323..324
FT /note="6"
FT REGION 1..176
FT /note="SMARCB1/INI1 binding"
FT /evidence="ECO:0000250"
FT REGION 52..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..324
FT /note="6.5 X 2 AA tandem repeats of R-G"
FT MOTIF 347..351
FT /note="PXLXP motif, interaction with host ZMYND11"
FT /evidence="ECO:0000250"
FT MOTIF 401..405
FT /note="PXLXP motif, interaction with host ZMYND11"
FT /evidence="ECO:0000250"
FT COMPBIAS 56..71
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..190
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..271
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..326
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 451 AA; 49042 MW; FF12A76055A91C9D CRC64;
MPTFYLALHG GQTYHLIVDT DSVGNPSLSV IPSNPYQEQL SDTPLIPLTI FVGENTGVPP
PPPPPPQRRD AWTQEPSPLD WDPLGYDVGH GPLASAMRML WMANYIVRQS RGDRGLILPQ
GPQTAPQAML VQPHVPPLRP TAPTILSPLS QPRLTPPQPL MMPPRPTPPT PLPPATLTVP
PRPTRPTTLP PTPLLTVLQR PTELQPTPSP PRMHLPVLHV PDQSMHPLTH QSTPNDPDSP
EPRSPTVFYN IPPMPLPPSQ LPPPAAPAQP PPGVINDQQL HHLPSGPPWW PPICDPPQPS
KTQGQSRGQS RGRGRGRGRG RGKSRDKQRK PGGPWRPEPN TSSPSMPELS PVLGLHQGQG
AGDSPTPGPS NAAPVCRNSH TATPNVSPIH EPESHNSPEA PILFPDDWYP PSIDPADLDE
SWDYIFETTE SPSSDEDYVE GPSKRPRPSI Q
