Reviewed, UniProtKB/Swiss-Prot P13288 (KR2_EBVB9)

Names and origin

Protein names

Recommended name:
    Serine/threonine-protein kinase BGLF4
    EC=2.7.11.1

Gene names

ORF Names:

BGLF4

Organism

Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4) [Complete proteome]

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	429 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Plays many key roles by phosphorylating several proteins including the viral DNA processivity factor BMRF1, EBNA1 or EBNA2. 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.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subcellular location	Virion tegument. Host nucleus. Note: the protein is present at discrete sites in nuclei, called replication compartments where viral DNA replication occurs.
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Nucleus Virion Virion tegument
Developmental stage	Early protein
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW protein tyrosine kinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 429	429	Serine/threonine-protein kinase BGLF4		PRO_0000086184
Regions
	Domain	1 – 409	409	Protein kinase
	Nucleotide binding	110 – 118	9	ATP By similarity
Sites
	Active site	221	1	Proton acceptor By similarity
	Binding site	128	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	P13288-1 [UniParc]. Last modified May 26, 2009. Version 2. Checksum: 241ECF46F613A68B	FASTA	429	48,351
	10 20 30 40 50 60 MDVNMAAELS PTNSSSSGEL SVSPEPPRET QAFLGKVTVI DYFTFQHKHL KVTNIDDMTE 70 80 90 100 110 120 TLYVKLPENM TRCDHLPITC EYLLGRGSYG AVYAHADNAT VKLYDSVTEL YHELMVCDMI 130 140 150 160 170 180 QIGKATAEDG QDKALVDYLS ACTSCHALFM PQFRCSLQDY GHWHDGSIEP LVRGFQGLKD 190 200 210 220 230 240 AVYFLNRHCG LFHSDISPSN ILVDFTDTMW GMGRLVLTDY GTASLHDRNK MLDVRLKSSK 250 260 270 280 290 300 GRQLYRLYCQ REPFSIAKDT YKPLCLLSKC YILRGAGHIP DPSACGPVGA QTALRLDLQS 310 320 330 340 350 360 LGYSLLYGIM HLADSTHKIP YPNPDMGFDR SDPLYFLQFA APKVVLLEVL SQMWNLNLDM 370 380 390 400 410 420 GLTSCGESPC VDVTAEHMSQ FLQWCRSLKK RFKESYFFNC RPRFEHPHLP GLVAELLADD FFGPDGRRG

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]	"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: 2535748] [Abstract] Cited for: CHARACTERIZATION.
[3]	"Proteins of purified Epstein-Barr virus." Johannsen E., Luftig M., Chase M.R., Weicksel S., Cahir-McFarland E., Illanes D., Sarracino D., Kieff E. Proc. Natl. Acad. Sci. U.S.A. 101:16286-16291(2004) [PubMed: 15534216] [Abstract] 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: 16298966] [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: 16698993] [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: 17360754] [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: 17360761] [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: 18815303] [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: 19244323] [Abstract] Cited for: FUNCTION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	V01555 Genomic DNA. Translation: CAA24828.1. Different initiation. AJ507799 Genomic DNA. Translation: CAD53438.2.
PIR	S33033.
3D structure databases
ModBase	Search...
Family and domain databases
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00109. PROTEIN_KINASE_TYR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KR2_EBVB9

Accession

Primary (citable) accession number: P13288
Secondary accession number(s): Q777D1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	May 26, 2009
Last modified:	June 16, 2009
This is version 55 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)