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Protein

Epstein-Barr nuclear antigen 3

Gene

EBNA3

Organism
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Plays an essential role for activation and immortalization of human B-cells. Represses transcription of viral promoters TP1 and Cp through interaction with host RBPJ, and inhibits EBNA2-mediated activation of these promoters. Since Cp is the promoter for all EBNA mRNAs, EBNA3A probably contributes to a negative autoregulatory control loop.

GO - Biological processi

  • DNA-templated viral transcription Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Epstein-Barr nuclear antigen 3
Short name:
EBNA-3
Short name:
EBV nuclear antigen 3
Alternative name(s):
Epstein-Barr nuclear antigen 3A
Short name:
EBNA-3A
Short name:
EBV nuclear antigen 3A
Gene namesi
Name:EBNA3
ORF Names:BLRF3-BERF1
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

Complete GO annotation...

Keywords - Cellular componenti

Host nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 944944Epstein-Barr nuclear antigen 3PRO_0000116177Add
BLAST

Interactioni

Subunit structurei

Interacts with human UCKL1. Interacts with host CTPB1; this interaction seems important for EBNA3-mediated transcriptional repression. Interacts with host RBPJ.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AHRP358695EBI-993115,EBI-80780From a different organism.
RBPJQ063303EBI-993115,EBI-632552From a different organism.
UCKL1Q9NWZ54EBI-993115,EBI-2466660From a different organism.

Protein-protein interaction databases

IntActiP12977. 4 interactions.
MINTiMINT-1517169.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M05X-ray1.90E/F325-333[»]
1XR8X-ray2.30C406-414[»]
ProteinModelPortaliP12977.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12977.

Family & Domainsi

Sequence similaritiesi

Belongs to the herpesviridae EBNA-3 family.Curated

Family and domain databases

InterProiIPR007706. EBNA-3.
[Graphical view]
PfamiPF05009. EBV-NA3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P12977-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDKDRPGPPA LDDNMEEEVP STSVVQEQVS AGDWENVLIE LSDSSSEKEA
60 70 80 90 100
EDAHLEPAQK GTKRKRVDHD AGGSAPARPM LPPQPDLPGR EAILRRFPLD
110 120 130 140 150
LRTLLQAIGA AATRIDTRAI DQFFGSQISN TEMYIMYAMA IRQAIRDRRR
160 170 180 190 200
NPASRRDQAK WRLQTLAAGW PMGYQAYSSW MYSYTDHQTT PTFVHLQATL
210 220 230 240 250
GCTGGRRCHV TFSAGTFKLP RCTPGDRQWL YVQSSVGNIV QSCNPRYSIF
260 270 280 290 300
FDYMAIHRSL TKIWEEVLTP DQRVSFMEFL GFLQRTDLSY IKSFVSDALG
310 320 330 340 350
TTSIQTPWID DNPSTETAQA WNAGFLRGRA YGIDLLRTEG EHVEGATGET
360 370 380 390 400
REESEDTESD GDDEDLPCIV SRGGPKVKRP PIFIRRLHRL LLMRAGKRTE
410 420 430 440 450
QGKEVLEKAR GSTYGTPRPP VPKPRPEVPQ SDETATSHGS AQVPEPPTIH
460 470 480 490 500
LAAQGMAYPL HEQHGMAPCP VAQAPPTPLP PVSPGDQLPG VFSDGRVACA
510 520 530 540 550
PVPAPAGPIV RPWEPSLTQA AGQAFAPVRP QHMPVEPVPV PTVALERPVY
560 570 580 590 600
PKPVRPAPPK IAMQGPGETS GIRRARERWR PAPWTPNPPR SPSQMSVRDR
610 620 630 640 650
LARLRAEAQV KQASVEVQPP QLTQVSPQQP MEGPLVPEQQ MFPGAPFSQV
660 670 680 690 700
ADVVRAPGVP AMQPQYFDLP LIQPISQGAP VAPLRASMGP VPPVPATQPQ
710 720 730 740 750
YFDIPLTEPI NQGASAAHFL PQQPMEGPLV PEQWMFPGAA LSQSVRPGVA
760 770 780 790 800
QSQYFDLPLT QPINHGAPAA HFLHQPPMEG PWVPEQWMFQ GAPPSQGTDV
810 820 830 840 850
VQHQLDALGY TLHGLNHPGV PVSPAVNQYH LSQAAFGLPI DEDESGEGSD
860 870 880 890 900
TSEPCEALDL SIHGRPCPQA PEWPVQEEGG QDATEVLDLS IHGRPRPRTP
910 920 930 940
EWPVQGEGGQ NVTGPETRRV VVSAVVHMCQ DDEFPDLQDP PDEA
Length:944
Mass (Da):103,494
Last modified:May 26, 2009 - v2
Checksum:i3413D9EA6BA7F06F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01555 Genomic DNA. Translation: CAB56341.1. Sequence problems.
V01555 Genomic DNA. Translation: CAA24856.1. Different termination.
AJ507799 Genomic DNA. Translation: CAD53419.1.
X04060 mRNA. Translation: CAA27693.1. Sequence problems.
PIRiA24938.
C43042. QQBE23.
RefSeqiYP_401669.1. NC_007605.1.

Genome annotation databases

GeneIDi17494212.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01555 Genomic DNA. Translation: CAB56341.1. Sequence problems.
V01555 Genomic DNA. Translation: CAA24856.1. Different termination.
AJ507799 Genomic DNA. Translation: CAD53419.1.
X04060 mRNA. Translation: CAA27693.1. Sequence problems.
PIRiA24938.
C43042. QQBE23.
RefSeqiYP_401669.1. NC_007605.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M05X-ray1.90E/F325-333[»]
1XR8X-ray2.30C406-414[»]
ProteinModelPortaliP12977.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP12977. 4 interactions.
MINTiMINT-1517169.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi17494212.

Miscellaneous databases

EvolutionaryTraceiP12977.

Family and domain databases

InterProiIPR007706. EBNA-3.
[Graphical view]
PfamiPF05009. EBV-NA3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "An Epstein-Barr virus transcription unit is at least 84 kilobases long."
    Bodescot M., Brison O., Perricaudet M.
    Nucleic Acids Res. 14:2611-2620(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Definitive identification of a member of the Epstein-Barr virus nuclear protein 3 family."
    Hennessy K., Wang F., Bushman E.W., Kieff E.
    Proc. Natl. Acad. Sci. U.S.A. 83:5693-5697(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  4. "Subnuclear localization and phosphorylation of Epstein-Barr virus latent infection nuclear proteins."
    Petti L., Sample C., Kieff E.
    Virology 176:563-574(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  5. "The amino-terminal domains of Epstein-Barr virus nuclear proteins 3A, 3B, and 3C interact with RBPJ(kappa)."
    Robertson E.S., Lin J., Kieff E.
    J. Virol. 70:3068-3074(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN RBPJ.
  6. "Epstein-Barr virus encoded nuclear protein EBNA-3 binds a novel human uridine kinase/uracil phosphoribosyltransferase."
    Kashuba E., Kashuba V., Sandalova T., Klein G., Szekely L.
    BMC Cell Biol. 3:23-23(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN UCKL1.
    Tissue: Heart.
  7. "Two nonconsensus sites in the Epstein-Barr virus oncoprotein EBNA3A cooperate to bind the co-repressor carboxyl-terminal-binding protein (CtBP)."
    Hickabottom M., Parker G.A., Freemont P., Crook T., Allday M.J.
    J. Biol. Chem. 277:47197-47204(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN CTBP1.
  8. "The structure of HLA-B8 complexed to an immunodominant viral determinant: peptide-induced conformational changes and a mode of MHC class I dimerization."
    Kjer-Nielsen L., Clements C.S., Brooks A.G., Purcell A.W., Fontes M.R., McCluskey J., Rossjohn J.
    J. Immunol. 169:5153-5160(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 325-333.
  9. "Crystal structures of two peptide-HLA-B*1501 complexes; structural characterization of the HLA-B62 supertype."
    Roder G., Blicher T., Justesen S., Johannesen B., Kristensen O., Kastrup J., Buus S., Gajhede M.
    Acta Crystallogr. D 62:1300-1310(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 406-414.

Entry informationi

Entry nameiEBNA3_EBVB9
AccessioniPrimary (citable) accession number: P12977
Secondary accession number(s): P03202
, Q66540, Q69021, Q8AZJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: May 26, 2009
Last modified: November 11, 2015
This is version 88 of the entry and version 2 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.