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

Serine/threonine-protein kinase BGLF4

Gene

BGLF4

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 many key roles by phosphorylating several proteins including the viral DNA processivity factor BMRF1, EBNA1 or EBNA2. Modifies the host nuclear envelope structure and induces the redistribution of nuclear envelope-associated proteins by phosphorylating host nucleoporins. Subsequently, promotes the nuclear transport of EBV lytic proteins. Required for efficient lytic DNA replication and release of nucleocapsids from the nucleus. Contributes to the compaction of host cell chromatin in cells undergoing lytic replication, presumably by phosphorylating the host condensin complex and host TOP2A. Induces disassembly of the nuclear lamina by phosphorylating with host LMNA. Phosphorylates substrates involved in capsid assembly and DNA packaging. Facilitates the switch from latent to lytic DNA replication by down-regulating EBNA1 replication function. Phosphorylates the viral immediate-early protein BZLF1 and inhibits its sumoylation by interacting with host SUMO1 and SUMO2.8 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei128 – 1281ATPPROSITE-ProRule annotation
Active sitei195 – 1951Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi110 – 1189ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host IRF3 by virus, Inhibition of host RLR pathway by virus, Modulation of host chromatin by virus, Viral immunoevasion

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase BGLF4 (EC:2.7.11.1)
Gene namesi
ORF Names:BGLF4
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

GO - Cellular componenti

  • host cell nuclear envelope Source: CACAO
  • host cell nucleus Source: CACAO
  • viral tegument Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Host nucleus, Virion, Virion tegument

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 429429Serine/threonine-protein kinase BGLF4PRO_0000086184Add
BLAST

PTM databases

iPTMnetiP13288.

Expressioni

Keywords - Developmental stagei

Early protein

Interactioni

Subunit structurei

Interacts with host NUP62 and NUP153; this interaction plays a role in nuclear targeting of BGLF4. Interacts with host SUMO1 and SUMO2.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
XPCQ018319EBI-1630636,EBI-372610From a different organism.

Protein-protein interaction databases

BioGridi971746. 3 interactions.
IntActiP13288. 3 interactions.
MINTiMINT-6768205.

Structurei

3D structure databases

ProteinModelPortaliP13288.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 409409Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni36 – 405SUMO interaction motif1 Publication
Regioni344 – 3507SUMO interaction motif1 Publication

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

KOiK19455.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008266. Tyr_kinase_AS.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P13288-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDVNMAAELS PTNSSSSGEL SVSPEPPRET QAFLGKVTVI DYFTFQHKHL
60 70 80 90 100
KVTNIDDMTE TLYVKLPENM TRCDHLPITC EYLLGRGSYG AVYAHADNAT
110 120 130 140 150
VKLYDSVTEL YHELMVCDMI QIGKATAEDG QDKALVDYLS ACTSCHALFM
160 170 180 190 200
PQFRCSLQDY GHWHDGSIEP LVRGFQGLKD AVYFLNRHCG LFHSDISPSN
210 220 230 240 250
ILVDFTDTMW GMGRLVLTDY GTASLHDRNK MLDVRLKSSK GRQLYRLYCQ
260 270 280 290 300
REPFSIAKDT YKPLCLLSKC YILRGAGHIP DPSACGPVGA QTALRLDLQS
310 320 330 340 350
LGYSLLYGIM HLADSTHKIP YPNPDMGFDR SDPLYFLQFA APKVVLLEVL
360 370 380 390 400
SQMWNLNLDM GLTSCGESPC VDVTAEHMSQ FLQWCRSLKK RFKESYFFNC
410 420
RPRFEHPHLP GLVAELLADD FFGPDGRRG
Length:429
Mass (Da):48,351
Last modified:May 26, 2009 - v2
Checksum:i241ECF46F613A68B
GO

Sequence cautioni

The sequence CAA24828.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01555 Genomic DNA. Translation: CAA24828.1. Different initiation.
AJ507799 Genomic DNA. Translation: CAD53438.2.
PIRiS33033.
RefSeqiYP_401688.1. NC_007605.1.

Genome annotation databases

GeneIDi3783704.
KEGGivg:3783704.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01555 Genomic DNA. Translation: CAA24828.1. Different initiation.
AJ507799 Genomic DNA. Translation: CAD53438.2.
PIRiS33033.
RefSeqiYP_401688.1. NC_007605.1.

3D structure databases

ProteinModelPortaliP13288.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi971746. 3 interactions.
IntActiP13288. 3 interactions.
MINTiMINT-6768205.

PTM databases

iPTMnetiP13288.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3783704.
KEGGivg:3783704.

Phylogenomic databases

KOiK19455.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008266. Tyr_kinase_AS.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "Identification of new protein kinase-related genes in three herpesviruses, herpes simplex virus, varicella-zoster virus, and Epstein-Barr virus."
    Smith R.F., Smith T.F.
    J. Virol. 63:450-455(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  3. Cited for: SUBCELLULAR LOCATION.
  4. "Detection of Epstein-Barr virus BGLF4 protein kinase in virus replication compartments and virus particles."
    Wang J.T., Yang P.W., Lee C.P., Han C.H., Tsai C.H., Chen M.R.
    J. Gen. Virol. 86:3215-3225(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  5. "Epstein-Barr virus protein kinase BGLF4 is a virion tegument protein that dissociates from virions in a phosphorylation-dependent process and phosphorylates the viral immediate-early protein BZLF1."
    Asai R., Kato A., Kato K., Kanamori-Koyama M., Sugimoto K., Sairenji T., Nishiyama Y., Kawaguchi Y.
    J. Virol. 80:5125-5134(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Epstein-Barr virus BGLF4 kinase induces premature chromosome condensation through activation of condensin and topoisomerase II."
    Lee C.P., Chen J.Y., Wang J.T., Kimura K., Takemoto A., Lu C.C., Chen M.R.
    J. Virol. 81:5166-5180(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Epstein-Barr virus-encoded protein kinase (BGLF4) is involved in production of infectious virus."
    Gershburg E., Raffa S., Torrisi M.R., Pagano J.S.
    J. Virol. 81:5407-5412(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Epstein-Barr virus BGLF4 kinase induces disassembly of the nuclear lamina to facilitate virion production."
    Lee C.P., Huang Y.H., Lin S.F., Chang Y., Chang Y.H., Takada K., Chen M.R.
    J. Virol. 82:11913-11926(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Epstein-Barr virus protein kinase BGLF4 targets the nucleus through interaction with nucleoporins."
    Chang C.W., Lee C.P., Huang Y.H., Yang P.W., Wang J.T., Chen M.R.
    J. Virol. 86:8072-8085(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HOST NUP62 AND NUP153.
  11. "SUMO binding by the Epstein-Barr virus protein kinase BGLF4 is crucial for BGLF4 function."
    Li R., Wang L., Liao G., Guzzo C.M., Matunis M.J., Zhu H., Hayward S.D.
    J. Virol. 86:5412-5421(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HOST SUMO1 AND SUMO2, REGION, SUBCELLULAR LOCATION.
  12. "BGLF4 kinase modulates the structure and transport preference of the nuclear pore complex to facilitate nuclear import of Epstein-Barr virus lytic proteins."
    Chang C.W., Lee C.P., Su M.T., Tsai C.H., Chen M.R.
    J. Virol. 89:1703-1718(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiKR2_EBVB9
AccessioniPrimary (citable) accession number: P13288
Secondary accession number(s): Q777D1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: May 26, 2009
Last modified: May 11, 2016
This is version 96 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

Complete proteome, Reference proteome

Documents

  1. 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.