EBNA6_EBVA8
ID EBNA6_EBVA8 Reviewed; 1069 AA.
AC Q69140;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 23-FEB-2022, entry version 82.
DE RecName: Full=Epstein-Barr nuclear antigen 6;
DE Short=EBNA-6;
DE Short=EBV nuclear antigen 6;
DE AltName: Full=Epstein-Barr nuclear antigen 3C;
DE Short=EBNA-3C;
DE Short=EBV nuclear antigen 3C;
DE AltName: Full=Epstein-Barr nuclear antigen 4B;
DE Short=EBNA-4B;
DE Short=EBV nuclear antigen 4B;
GN Name=EBNA6; ORFNames=BERF3-BERF4;
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=2166806; DOI=10.1128/jvi.64.9.4084-4092.1990;
RA Sample J., Young L., Martin B., Chatman T., Kieff E.D., Rickinson A.;
RT "Epstein-Barr virus types 1 and 2 differ in their EBNA-3A, EBNA-3B, and
RT EBNA-3C genes.";
RL J. Virol. 64:4084-4092(1990).
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 an essential role for the activation and
CC immortalization of human B-cells. Represses transcription of viral
CC promoters TP1 and Cp through interaction with host RBPJ, and inhibits
CC EBNA2-mediated activation of these promoters. Since Cp is the promoter
CC for all EBNA mRNAs, EBNA6 probably contributes to a negative
CC autoregulatory control loop. Alternatively, EBNA6 also regulates the
CC transcription of the EBV oncogene LMP1 in a cell cycle-dependent
CC manner. Modulates the activity of several host proteins involved in
CC cell cycle regulation including host cyclin A, MYC, RB, p21 and p27
CC mainly through binding to the host SCF(SKP2) complex. Inhibits the
CC promoter of host H2AX and targets H2AX to proteasomal degradation in
CC order to promote latency and cell proliferation.
CC {ECO:0000250|UniProtKB:P03204}.
CC -!- SUBUNIT: Interacts with host CTPB1; this interaction seems important
CC for EBNA6-mediated transcriptional repression. Interacts with host MYC;
CC this interaction enhances MYC stability. Interacts (via N-terminus)
CC with host RBPJ. Interacts (via N-terminus) with host histone H2AX; this
CC interaction facilitates H2AX proteasomal degradation. Interacts with
CC host TP73; this interaction inhibits TP73-mediated apoptotic pathway.
CC {ECO:0000250|UniProtKB:P03204}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250|UniProtKB:P03204}. Host
CC nucleus matrix {ECO:0000250|UniProtKB:P03204}. Note=Associated with the
CC nuclear matrix. {ECO:0000250|UniProtKB:P03204}.
CC -!- SIMILARITY: Belongs to the herpesviridae EBNA-6 family. {ECO:0000305}.
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DR EMBL; M34440; AAA45895.1; -; Genomic_DNA.
DR EMBL; DQ279927; ABB89245.1; -; Genomic_DNA.
DR PIR; S27922; S27922.
DR RefSeq; YP_001129465.1; NC_009334.1.
DR MINT; Q69140; -.
DR PRIDE; Q69140; -.
DR GeneID; 5176150; -.
DR KEGG; vg:5176150; -.
DR Proteomes; UP000007639; Genome.
DR GO; GO:0044204; C:host cell nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0039645; P:modulation by virus of host G1/S transition checkpoint; IEA:UniProtKB-KW.
DR GO; GO:0019042; P:viral latency; IEA:UniProtKB-KW.
DR InterPro; IPR007706; EBNA-3/4/6.
DR Pfam; PF05009; EBV-NA3; 1.
PE 3: Inferred from homology;
KW G1/S host cell cycle checkpoint dysregulation by virus; Host nucleus;
KW Host-virus interaction; Modulation of host cell cycle by virus;
KW Reference proteome; Transcription; Transcription regulation; Viral latency;
KW Viral latency initiation and maintenance.
FT CHAIN 1..1069
FT /note="Epstein-Barr nuclear antigen 6"
FT /id="PRO_0000375940"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1008..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..601
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..641
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1052
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1069 AA; 118146 MW; D83B23C41C98709F CRC64;
MESFEGEGDS IQSPDNARGD DVQNTGEHIQ DPGPGPSTGG ASEGLVQNEP DSRDQQSRGQ
RRGDENRGWM QRIRRRRRRR AALSGHLLDM EDNVPPWFPP HDITPYVARN IRDAACQAVK
HSHLQALSNL ILDSGLDTQH LLCFVMAARQ RLQDIRRGPL VVEGGVGWRH WLLTSPSRSW
SMGYRTATLR TLTPVPNRVG ADSIMLTATF GCQNGALAIN TFSATVWIPP PAGPREQERY
AREAEVRFLR GKWQRRFRRI FDLIELCGSL HHVWQNMLQT EENLLDFVRF MGVMSSCNSS
SVNYWFHKTI GNFKPYYPWN APPNENPYHA RRGIKEQVIQ KAFLKAQRQG LSMLATGGGP
RGDATSETSS DEDTGRQGSD VELESSDDEL PYIDPNMEPV QQRPVMFVSR VPVRKPRTLP
WPTPKTHPVK RTIVKTSYRS DEAEEAQSTP ERPGPSKQPS EPVEPAHTTP AGRSTVILHE
PPREPEAVSF KPPPPPSRRR RGACVVYDDD IIEVIDVETT EEETTSMQRQ PPLGQQPPPP
VISTGSAMSS SHTDPSVTQP SKPHRKPQDG FQRSGRRQKR AMPPPVSPSD AGPPSTRPRV
MAPPSTGPRV MATPSTGPRD MAPPSTGPRD MAPPSTGPRD MAPPSTGPRD MAPTVVHMFT
RERLLTQSTG PAPRSFWEMR AGRDAPKIQQ EPSSQQQPAT QSTPPCQSWV PSVYVLPAVD
AGNAQPLQIS HLSSMSPTQP ISHEEQPRYE DPDTPLDLSL HPDTATLPPT QDLYPGREDL
QATQAPYPGY EEPRPPQAPF VGDYGFVQIP SAQWEPHPSQ GTYQGHIDPQ LPAALDLGPE
QPRFPQDPYV YSGGQLSSCP GYAGPWPSRP QHPRYRHTLA LWPREPRHGH SQGPWKPWSA
HLPPQWDGSA GHGQDQVSQF PHLHSETGPP RLQLSSVPQV LYPQPLVSSS APSWSSPQPR
APIRPIPTRF PPPPMPLQDS MAVGCDSSGT ACPSMPFASD YSQGAFTPLD INAPTPKSPR
VEESSHGPAR CSQATSEAQE ILSDNSEISV FPKDAKQTDY DASTESELD
