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P03206 (BZLF1_EBVB9) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Trans-activator protein BZLF1

Short name=EB1
Alternative name(s):
Zebra
Gene names
ORF Names:BZLF1
OrganismEpstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4) [Reference proteome]
Taxonomic identifier10377 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeGammaherpesvirinaeLymphocryptovirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length245 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a key role in the switch from latent infection to lytic cycle producing new virions. Acts as a transcription factor, inducing early lytic cycle genes, and as a origin binding protein for genome replication. BZLF1 activates the promoter of another EBV gene (BSLF2+BMLF1). Ref.4 Ref.5 Ref.6 Ref.9 Ref.11

Subunit structure

Interacts with human UBN1, CRTC2 and GNB2L1/RACK1. Ref.7 Ref.8 Ref.10

Subcellular location

Host nucleus Ref.7.

Sequence similarities

Belongs to the bZIP family.

Contains 1 bZIP (basic-leucine zipper) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 245245Trans-activator protein BZLF1
PRO_0000076541

Regions

Domain170 – 22859bZIP
Region178 – 19518Basic motif By similarity
Region196 – 22833Leucine-zipper By similarity

Secondary structure

....... 245
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P03206 [UniParc].

Last modified July 1, 1989. Version 2.
Checksum: 7F3D55D79F1F0196

FASTA24526,860
        10         20         30         40         50         60 
MMDPNSTSED VKFTPDPYQV PFVQAFDQAT RVYQDLGGPS QAPLPCVLWP VLPEPLPQGQ 

        70         80         90        100        110        120 
LTAYHVSTAP TGSWFSAPQP APENAYQAYA APQLFPVSDI TQNQQTNQAG GEAPQPGDNS 

       130        140        150        160        170        180 
TVQTAAAVVF ACPGANQGQQ LADIGVPQPA PVAAPARRTR KPQQPESLEE CDSELEIKRY 

       190        200        210        220        230        240 
KNRVASRKCR AKFKQLLQHY REVAAAKSSE NDRLRLLLKQ MCPSLDVDSI IPRTPDVLHE 


DLLNF 

« Hide

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Epstein-Barr virus gene expression in P3HR1-superinfected Raji cells."
Biggin M., Bodescot M., Perricaudet M., Farrel P.
J. Virol. 61:3120-3132(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], CHARACTERIZATION.
[3]"Epstein-Barr virus BZLF1 trans-activator specifically binds to a consensus AP-1 site and is related to c-fos."
Farrel P.J., Rowe D.T., Rooney C.M., Kouzarides T.
EMBO J. 8:127-132(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING.
[4]"Structure and function of the Epstein-Barr virus BZLF1 protein."
Packham G., Economou A., Rooney C.M., Rowe D.T., Farrel P.J.
J. Virol. 64:2110-2116(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE, FUNCTION.
[5]"The BZLF1 protein of EBV has a coiled coil dimerisation domain without a heptad leucine repeat but with homology to the C/EBP leucine zipper."
Kouzarides T., Packham G., Cook A., Farrell P.J.
Oncogene 6:195-204(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"A transcription factor with homology to the AP-1 family links RNA transcription and DNA replication in the lytic cycle of Epstein-Barr virus."
Schepers A., Pich D., Hammerschmidt W.
EMBO J. 12:3921-3929(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"The PKC targeting protein RACK1 interacts with the Epstein-Barr virus activator protein BZLF1."
Baumann M., Gires O., Kolch W., Mischak H., Zeidler R., Pich D., Hammerschmidt W.
Eur. J. Biochem. 267:3891-3901(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN GNB2L1, SUBCELLULAR LOCATION.
[8]"Ubinuclein, a novel nuclear protein interacting with cellular and viral transcription factors."
Aho S., Buisson M., Pajunen T., Ryoo Y.W., Giot J.-F., Gruffat H., Sergeant A., Uitto J.
J. Cell Biol. 148:1165-1176(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN UBN1.
[9]"Epstein-Barr virus BZLF1 gene, a switch from latency to lytic infection, is expressed as an immediate-early gene after primary infection of B lymphocytes."
Wen W., Iwakiri D., Yamamoto K., Maruo S., Kanda T., Takada K.
J. Virol. 81:1037-1042(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"TORC2, a coactivator of cAMP-response element-binding protein, promotes Epstein-Barr virus reactivation from latency through interaction with viral BZLF1 protein."
Murata T., Sato Y., Nakayama S., Kudoh A., Iwahori S., Isomura H., Tajima M., Hishiki T., Ohshima T., Hijikata M., Shimotohno K., Tsurumi T.
J. Biol. Chem. 284:8033-8041(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN CRTC2.
[11]"Interaction of Epstein-Barr virus BZLF1 C-terminal tail structure and core zipper is required for DNA replication but not for promoter transactivation."
McDonald C.M., Petosa C., Farrell P.J.
J. Virol. 83:3397-3401(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Structural basis of lytic cycle activation by the Epstein-Barr virus ZEBRA protein."
Petosa C., Morand P., Baudin F., Moulin M., Artero J.B., Muller C.W.
Mol. Cell 21:565-572(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 175-236.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V01555 Genomic DNA. Translation: CAA24861.1.
AJ507799 Genomic DNA. Translation: CAD53423.1.
M17547 mRNA. Translation: AAA66529.1.
RefSeqYP_401673.1. NC_007605.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZSDX-ray1.70C54-64[»]
2AK4X-ray2.50C/H/M/S52-64[»]
2AXFX-ray1.80C77-86[»]
2AXGX-ray2.00C77-86[»]
2C9LX-ray2.25Y/Z175-236[»]
2C9NX-ray3.30Y/Z175-236[»]
3KWWX-ray2.18C52-64[»]
3KXFX-ray3.10Q/R/S/T52-64[»]
3SPVX-ray1.30C190-197[»]
3VFNX-ray1.50C52-64[»]
3VFOX-ray1.70C52-64[»]
3VFPX-ray1.85C52-64[»]
3VFRX-ray1.85C52-64[»]
ProteinModelPortalP03206.
SMRP03206. Positions 178-236.
ModBaseSearch...

Protein-protein interaction databases

IntActP03206. 3 interactions.
MINTMINT-6768270.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3783744.

Phylogenomic databases

ProtClustDBCLSP2512075.

Family and domain databases

InterProIPR004827. bZIP.
IPR017339. Trans-activator_BZLF1_HHV-4.
[Graphical view]
PfamPF00170. bZIP_1. 1 hit.
[Graphical view]
PIRSFPIRSF037966. BZLF1. 1 hit.
SMARTSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEPS50217. BZIP. False negative.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP03206.
ChEMBLCHEMBL1293280.
EvolutionaryTraceP03206.

Entry information

Entry nameBZLF1_EBVB9
AccessionPrimary (citable) accession number: P03206
Secondary accession number(s): Q69127, Q777E5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1989
Last modified: April 3, 2013
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families