Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Epstein-Barr nuclear antigen 1

Gene

EBNA1

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

Functioni

Plays an essential role in replication and partitioning of viral genomic DNA during latent viral infection. During this phase, the circular double-stranded viral DNA undergoes replication once per cell cycle and is efficiently partitioned to the daughter cells. EBNA1 activates the initiation of viral DNA replication through binding to specific sites in the viral latent origin of replication, oriP. Additionally, it governs the segregation of viral episomes by mediating their attachment to host cell metaphase chromosomes. Also activates the transcription of several viral latency genes. Finally, it can counteract the stabilization of host p53/TP53 by host USP7, thereby decreasing apoptosis and increasing host cell survival.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Host-virus interaction, Inhibition of host adaptive immune response by virus, Inhibition of host NF-kappa-B by virus, Inhibition of host proteasome antigen processing by virus, Transcription, Transcription regulation, Viral immunoevasion

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Epstein-Barr nuclear antigen 1
Short name:
EBNA-1
Short name:
EBV nuclear antigen 1
Gene namesi
Name:EBNA1
ORF Names:BKRF1
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 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi444 – 4441E → A: Slight decrease in binding to USP7. Major decrease in binding to USP7; when associated with A-447. 1 Publication
Mutagenesisi447 – 4471S → A: Loss of binding to USP7. Major decrease in binding to USP7; when associated with A-444. 1 Publication

Chemistry

ChEMBLiCHEMBL1293281.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 641641Epstein-Barr nuclear antigen 1PRO_0000116175Add
BLAST

Interactioni

Subunit structurei

Interacts with human USP7. Interacts with human EBP2; this interaction is important for the stable segregation of EBV episomes during cell division but not for the replication of the episomes. Interacts with BGLF4; this interaction facilitates the switch from latent to lytic DNA replication by down-regulating EBNA1 replication function.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ORC1Q134152EBI-996522,EBI-374847From a different organism.
ORC2Q134166EBI-996522,EBI-374957From a different organism.
TERF2Q155543EBI-996522,EBI-706637From a different organism.
USP7Q930095EBI-996522,EBI-302474From a different organism.

Protein-protein interaction databases

BioGridi971751. 12 interactions.
DIPiDIP-29054N.
IntActiP03211. 44 interactions.
MINTiMINT-86901.

Chemistry

BindingDBiP03211.

Structurei

Secondary structure

1
641
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi411 – 4133Combined sources
Helixi476 – 48914Combined sources
Beta strandi503 – 51210Combined sources
Helixi514 – 52714Combined sources
Beta strandi537 – 5404Combined sources
Beta strandi545 – 5484Combined sources
Helixi552 – 5543Combined sources
Beta strandi556 – 56712Combined sources
Helixi569 – 58416Combined sources
Helixi590 – 5923Combined sources
Beta strandi593 – 60412Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B3TX-ray2.20A/B461-607[»]
1VHIX-ray2.50A/B466-607[»]
1YY6X-ray1.70B441-450[»]
2FYYX-ray1.50C407-417[»]
2FZ3X-ray1.90C407-417[»]
3MV7X-ray2.00C407-417[»]
3MV8X-ray2.10C407-417[»]
3MV9X-ray2.70C407-417[»]
4PRAX-ray1.85C407-417[»]
4PREX-ray1.65C407-417[»]
4PRIX-ray2.40C407-417[»]
4PRPX-ray2.50C407-417[»]
ProteinModelPortaliP03211.
SMRiP03211. Positions 461-607.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03211.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni436 – 45015Interaction with USP7Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi87 – 352266Ala/Gly-richAdd
BLAST

Sequence similaritiesi

Belongs to the herpesviridae EBNA1 family.Curated

Phylogenomic databases

KOiK19461.

Family and domain databases

Gene3Di3.30.70.390. 1 hit.
InterProiIPR004186. EBNA1_DNA-bd.
IPR000427. Papillomavirus_E2_C.
[Graphical view]
PfamiPF02905. EBV-NA1. 1 hit.
[Graphical view]
ProDomiPD037044. EBNA1_DNA_bd. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF54957. SSF54957. 1 hit.

Sequencei

Sequence statusi: Complete.

P03211-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDEGPGTGP GNGLGEKGDT SGPEGSGGSG PQRRGGDNHG RGRGRGRGRG
60 70 80 90 100
GGRPGAPGGS GSGPRHRDGV RRPQKRPSCI GCKGTHGGTG AGAGAGGAGA
110 120 130 140 150
GGAGAGGGAG AGGGAGGAGG AGGAGAGGGA GAGGGAGGAG GAGAGGGAGA
160 170 180 190 200
GGGAGGAGAG GGAGGAGGAG AGGGAGAGGG AGGAGAGGGA GGAGGAGAGG
210 220 230 240 250
GAGAGGAGGA GGAGAGGAGA GGGAGGAGGA GAGGAGAGGA GAGGAGAGGA
260 270 280 290 300
GGAGAGGAGG AGAGGAGGAG AGGGAGGAGA GGGAGGAGAG GAGGAGAGGA
310 320 330 340 350
GGAGAGGAGG AGAGGGAGAG GAGAGGGGRG RGGSGGRGRG GSGGRGRGGS
360 370 380 390 400
GGRRGRGRER ARGGSRERAR GRGRGRGEKR PRSPSSQSSS SGSPPRRPPP
410 420 430 440 450
GRRPFFHPVG EADYFEYHQE GGPDGEPDVP PGAIEQGPAD DPGEGPSTGP
460 470 480 490 500
RGQGDGGRRK KGGWFGKHRG QGGSNPKFEN IAEGLRALLA RSHVERTTDE
510 520 530 540 550
GTWVAGVFVY GGSKTSLYNL RRGTALAIPQ CRLTPLSRLP FGMAPGPGPQ
560 570 580 590 600
PGPLRESIVC YFMVFLQTHI FAEVLKDAIK DLVMTKPAPT CNIRVTVCSF
610 620 630 640
DDGVDLPPWF PPMVEGAAAE GDDGDDGDEG GDGDEGEEGQ E
Length:641
Mass (Da):56,427
Last modified:July 21, 1986 - v1
Checksum:i4D161653E16FC341
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01555 Genomic DNA. Translation: CAA24816.1.
M13941 Genomic DNA. Translation: AAA45889.1.
AJ507799 Genomic DNA. Translation: CAD53427.1.
PIRiC43043. QQBE31.
RefSeqiYP_401677.1. NC_007605.1.

Genome annotation databases

GeneIDi3783709.
KEGGivg:3783709.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01555 Genomic DNA. Translation: CAA24816.1.
M13941 Genomic DNA. Translation: AAA45889.1.
AJ507799 Genomic DNA. Translation: CAD53427.1.
PIRiC43043. QQBE31.
RefSeqiYP_401677.1. NC_007605.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B3TX-ray2.20A/B461-607[»]
1VHIX-ray2.50A/B466-607[»]
1YY6X-ray1.70B441-450[»]
2FYYX-ray1.50C407-417[»]
2FZ3X-ray1.90C407-417[»]
3MV7X-ray2.00C407-417[»]
3MV8X-ray2.10C407-417[»]
3MV9X-ray2.70C407-417[»]
4PRAX-ray1.85C407-417[»]
4PREX-ray1.65C407-417[»]
4PRIX-ray2.40C407-417[»]
4PRPX-ray2.50C407-417[»]
ProteinModelPortaliP03211.
SMRiP03211. Positions 461-607.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi971751. 12 interactions.
DIPiDIP-29054N.
IntActiP03211. 44 interactions.
MINTiMINT-86901.

Chemistry

BindingDBiP03211.
ChEMBLiCHEMBL1293281.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3783709.
KEGGivg:3783709.

Phylogenomic databases

KOiK19461.

Miscellaneous databases

EvolutionaryTraceiP03211.
PROiP03211.

Family and domain databases

Gene3Di3.30.70.390. 1 hit.
InterProiIPR004186. EBNA1_DNA-bd.
IPR000427. Papillomavirus_E2_C.
[Graphical view]
PfamiPF02905. EBV-NA1. 1 hit.
[Graphical view]
ProDomiPD037044. EBNA1_DNA_bd. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF54957. SSF54957. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiEBNA1_EBVB9
AccessioniPrimary (citable) accession number: P03211
Secondary accession number(s): Q777E1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: September 7, 2016
This is version 128 of the entry and version 1 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.