EBNA6_EBVG
ID EBNA6_EBVG Reviewed; 1009 AA.
AC Q3KST0;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 48.
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 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 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; AY961628; AAY41120.1; -; Genomic_DNA.
DR SMR; Q3KST0; -.
DR IntAct; Q3KST0; 1.
DR PRIDE; Q3KST0; -.
DR Proteomes; UP000007641; 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 Transcription; Transcription regulation; Viral latency;
KW Viral latency initiation and maintenance.
FT CHAIN 1..1009
FT /note="Epstein-Barr nuclear antigen 6"
FT /id="PRO_0000375939"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..495
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..579
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..918
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1009 AA; 112164 MW; BCF79D55DEECD43B CRC64;
MESFEGQGDS RQSPDNERGD NVQTTGEHDQ DPGPGPPSSG ASERLVPEES YSRDQQPWGQ
SRGDENRGWM QRIRRRRRRR AALSGHLLDT EDNVPPWLPP HDIAPYVARN IRDAACRAVK
QSHLQALSNL ILDSGLDTQH ILCFVMAARQ RLQDIRRGPL VVEGGVGWRH WLLTSPSQSW
PMGYRTATLR TLTPVPNRVG ADSIMLTATF GCQNAARTLN TFSATVWTPP HAGPREQERY
AREAEVRFLR GKWQRRYRRI YDLIELCGSL HHIWQNLLQT EENLLDFVRF MGVMSSCNNP
AVNYWFHKTI GNFKPYYPWN APPNENPYHA RRGIKEHVIQ NAFRKAQIQG LSMLATVGEP
RGDATSETSS DEDTGRQGSD VELESSDDEL PYIDPNMEPV QQRPVMFVSR VPAKKPRKLP
WPTPKTHPVK RTNVKTSDRS DKAEAQSTPE RPGPSEQSSV TVEPAHPTPV EMPMVILHQP
PPVPKPVPVK PTPPPSRRRR GACVVYDDDV IEVIDVETTE DSSSVSQPNK PHRKHQDGFQ
RSGRRQKRAA PPTVSPSDTG PPAAGPPAAG PPAAGPHILT PPSARPRIMA PPVVRMFMRE
RQLPQSTGRK PQCFWEMRAS REITQMQQEP SSHLQSATQP TMPRPSWVPS VCALSVMDAG
KAQPIQSSHL SSMSPTQPIS HEEQPRYEDP DAPLDLSLHP DVAAPPAPRA PYQGYQEQPA
PQAPYQGYQE QPAPQAPYQG YQEQPAPQAP YQGYQEQPAP QAPYQGYQEQ PPPQAPYQGY
QEQPAPQAPY QGYQEPPAHG LQSSSYPGYA GPWTPRSQHP CYRHPWAPWS QDPVHGHTQG
PWDPRAPHLP PQWDGSAGHG QDQVSQFPHL QSETGPPRLQ LSSVPLVSSS APSWSSPQPR
APIRPIPTRF PPPPMPLQDS MAVGCDSSGT ACPSMPFASD YSQGAFTPLD INATTPKRPR
VEESSHGPAR CSQATAEAQE ILSDNSEISV FPKDAKQTDY DASTESELD
