Epstein-Barr nuclear antigen 1 - Epstein-Barr virus (strain B95-8) (HHV-4)

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P03211 (EBNA1_EBVB9) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 98. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Epstein-Barr nuclear antigen 1
Short name=EBNA-1
Short name=EBV nuclear antigen 1

Gene names

Name:	EBNA1
ORF Names:	BKRF1

Organism

Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)

Taxonomic identifier

10377 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Gammaherpesvirinae › Lymphocryptovirus

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	641 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.8
Subunit structure	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. Ref.4 Ref.5 Ref.6 Ref.8
Subcellular location	Host nucleus Ref.3.
Sequence similarities	Belongs to the herpesviridae EBNA1 family.

Ontologies

Keywords
Biological process	Host-virus interaction Inhibition of host NF-kappa-B by virus Inhibition of host adaptive immune response by virus Inhibition of host proteasome antigen processing by virus Transcription Transcription regulation Viral immunoevasion
Cellular component	Host nucleus
Ligand	DNA-binding
Molecular function	Activator
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA replication Inferred from electronic annotation. Source: InterPro evasion by virus of host immune response Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro regulation of DNA replication Inferred from electronic annotation. Source: InterPro transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	host cell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA replication origin binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
USP7	Q93009	4	EBI-996522,EBI-302474	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 641

641

Epstein-Barr nuclear antigen 1

PRO_0000116175

Regions

Region

436 – 450

Interaction with USP7

Compositional bias

87 – 352

266

Ala/Gly-rich

Experimental info

Mutagenesis

444

E → A: Slight decrease in binding to USP7. Major decrease in binding to USP7; when associated with A-447. Ref.8

Mutagenesis

447

S → A: Loss of binding to USP7. Major decrease in binding to USP7; when associated with A-444. Ref.8

Secondary structure

641

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P03211 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 4D161653E16FC341
Show »

FASTA

641

56,427

        10         20         30         40         50         60 
MSDEGPGTGP GNGLGEKGDT SGPEGSGGSG PQRRGGDNHG RGRGRGRGRG GGRPGAPGGS 

        70         80         90        100        110        120 
GSGPRHRDGV RRPQKRPSCI GCKGTHGGTG AGAGAGGAGA GGAGAGGGAG AGGGAGGAGG 

       130        140        150        160        170        180 
AGGAGAGGGA GAGGGAGGAG GAGAGGGAGA GGGAGGAGAG GGAGGAGGAG AGGGAGAGGG 

       190        200        210        220        230        240 
AGGAGAGGGA GGAGGAGAGG GAGAGGAGGA GGAGAGGAGA GGGAGGAGGA GAGGAGAGGA 

       250        260        270        280        290        300 
GAGGAGAGGA GGAGAGGAGG AGAGGAGGAG AGGGAGGAGA GGGAGGAGAG GAGGAGAGGA 

       310        320        330        340        350        360 
GGAGAGGAGG AGAGGGAGAG GAGAGGGGRG RGGSGGRGRG GSGGRGRGGS GGRRGRGRER 

       370        380        390        400        410        420 
ARGGSRERAR GRGRGRGEKR PRSPSSQSSS SGSPPRRPPP GRRPFFHPVG EADYFEYHQE 

       430        440        450        460        470        480 
GGPDGEPDVP PGAIEQGPAD DPGEGPSTGP RGQGDGGRRK KGGWFGKHRG QGGSNPKFEN 

       490        500        510        520        530        540 
IAEGLRALLA RSHVERTTDE GTWVAGVFVY GGSKTSLYNL RRGTALAIPQ CRLTPLSRLP 

       550        560        570        580        590        600 
FGMAPGPGPQ PGPLRESIVC YFMVFLQTHI FAEVLKDAIK DLVMTKPAPT CNIRVTVCSF 

       610        620        630        640 
DDGVDLPPWF PPMVEGAAAE GDDGDDGDEG GDGDEGEEGQ E

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"DNA sequence and expression of the B95-8 Epstein-Barr virus genome." Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J., Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C., Tuffnell P.S., Barrell B.G. Nature 310:207-211(1984) [PubMed: 6087149] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Nucleotide sequences of mRNAs encoding Epstein-Barr virus nuclear proteins: a probable transcriptional initiation site." Sample J., Hummel M., Braun D., Birkenbach M., Kieff E. Proc. Natl. Acad. Sci. U.S.A. 83:5096-5100(1986) [PubMed: 3460083] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
[3]	"Subnuclear localization and phosphorylation of Epstein-Barr virus latent infection nuclear proteins." Petti L., Sample C., Kieff E. Virology 176:563-574(1990) [PubMed: 2161150] [Abstract] Cited for: SUBCELLULAR LOCATION.
[4]	"EBP2, a human protein that interacts with sequences of the Epstein-Barr virus nuclear antigen 1 important for plasmid maintenance." Shire K., Ceccarelli D.F.J., Avolio-Hunter T.M., Frappier L. J. Virol. 73:2587-2595(1999) [PubMed: 10074103] [Abstract] Cited for: INTERACTION WITH HUMAN EBP2.
[5]	"Protein interaction domains of the ubiquitin-specific protease, USP7/HAUSP." Holowaty M.N., Sheng Y., Nguyen T., Arrowsmith C., Frappier L. J. Biol. Chem. 278:47753-47761(2003) [PubMed: 14506283] [Abstract] Cited for: INTERACTION WITH HUMAN USP7.
[6]	"Protein array identification of substrates of the epstein-barr virus protein kinase BGLF4." Zhu J., Liao G., Shan L., Zhang J., Chen M.R., Hayward G.S., Hayward S.D., Desai P., Zhu H. J. Virol. 83:5219-5231(2009) [PubMed: 19244323] [Abstract] Cited for: INTERACTION WITH BGLF4.
[7]	"Crystal structure of the DNA-binding domain of the Epstein-Barr virus origin-binding protein EBNA 1." Bochkarev A., Barwell J.A., Pfuetzner R.A., Furey W.F. Jr., Edwards A.M., Frappier L. Cell 83:39-46(1995) [PubMed: 7553871] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 469-607.
[8]	"Structure of the p53 binding domain of HAUSP/USP7 bound to Epstein-Barr nuclear antigen 1 implications for EBV-mediated immortalization." Saridakis V., Sheng Y., Sarkari F., Holowaty M.N., Shire K., Nguyen T., Zhang R.G., Liao J., Lee W., Edwards A.M., Arrowsmith C.H., Frappier L. Mol. Cell 18:25-36(2005) [PubMed: 15808506] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 441-450 IN COMPLEX WITH USP7, FUNCTION, INTERACTION WITH HUMAN USP7, MUTAGENESIS OF GLU-444 AND SER-447.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

V01555 Genomic DNA. Translation: CAA24816.1.
M13941 Genomic DNA. Translation: AAA45889.1.
AJ507799 Genomic DNA. Translation: CAD53427.1.

PIR

QQBE31. C43043.

RefSeq

YP_401677.1. NC_007605.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B3T	X-ray	2.20	A/B	461-607	[»]
1VHI	X-ray	2.50	A/B	470-607	[»]
1YY6	X-ray	1.70	B	441-450	[»]
2FYY	X-ray	1.50	C	407-417	[»]
2FZ3	X-ray	1.90	C	407-417	[»]
3MV7	X-ray	2.00	C	407-417	[»]
3MV8	X-ray	2.10	C	407-417	[»]
3MV9	X-ray	2.70	C	407-417	[»]

ProteinModelPortal

P03211.

SMR

P03211. Positions 461-607.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29054N.

IntAct

P03211. 1 interaction.

MINT

MINT-86901.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3783709.

Phylogenomic databases

ProtClustDB

CLSP2512071.

Family and domain databases

InterPro

IPR004186. EBNA1_DNA-bd.
IPR000427. Papillomavirus_E2_C.
[Graphical view]

Gene3D

G3DSA:3.30.70.390. EBNA1_DNA_bd. 1 hit.

Pfam

PF02905. EBV-NA1. 1 hit.
[Graphical view]

ProDom

PD037044. EBNA1_DNA_bd. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF54957. Viral_DNA_bd. 1 hit.

ProtoNet

Search...

Entry information

Entry name

EBNA1_EBVB9

Accession

Primary (citable) accession number: P03211
Secondary accession number(s): Q777E1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	December 14, 2011
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents