Reviewed, UniProtKB/Swiss-Prot Q8AZK7 (EBNA5_EBVB9)

Names and origin

Protein names

Recommended name:
    Epstein-Barr nuclear antigen leader protein
      Short name=EBV nuclear antigen leader protein
      Short name=EBNA-LP
Alternative name(s):
    Epstein-Barr nuclear antigen 5
      Short name=EBV nuclear antigen 5
      Short name=EBNA-5

Gene names

Name:	EBNA-LP
Synonyms:	EBNA5

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	506 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Plays an important role in the establishment of B cell immortalization by acting as an EBNA2 coactivator. This transcriptional activation preferentially enhances the expression of the major viral protein LMP1. The interaction between EBNA-LP and host SP100 correlates with coactivation of EBNA2 and the relocalization of SP100 from PML nuclear bodies into nucleoplasm.
Subunit structure	Homooligomer. Interacts with host SP100; this interaction is important for EBNA-LP coactivator activity. Interacts with host HAX1, ERR1 and HSPA2. Interacts with host PRKDC and AKAP8L; these interactions modulate the coactivator function of EBNA-LP. Ref.3 Ref.4 Ref.5 Ref.7 Ref.8
Subcellular location	Host nucleus Ref.2.
Post-translational modification	Phosphorylated by the cellular protein kinase cdc2. Ref.6
Sequence similarities	Belongs to the lymphocryptovirus EBNA-LP family.

Ontologies

Keywords
Biological process	Host-virus interaction Transcription Transcription regulation
Cellular component	Host nucleus
Molecular function	Activator
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	disassembly by symbiont of host cell PML body Ref.7 Inferred from direct assay. Source: UniProtKB regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	host cell PML body Ref.7 Inferred from direct assay. Source: UniProtKB
Molecular function	transcription coactivator activity Ref.7 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDKN2A	Q8N726	1	EBI-1185167,EBI-625922	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 506	506	Epstein-Barr nuclear antigen leader protein		PRO_0000376060
Regions
	Compositional bias	29 – 482	454	Arg-rich
	Compositional bias	500 – 505	6	Poly-Glu
Amino acid modifications
	Modified residue	35	1	Phosphoserine; by host
Experimental info
	Mutagenesis	35	1	S → A: 95% loss of phosphorylation. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q8AZK7-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: CD2C6C3B737AC1E9	FASTA	506	54,739
	10 20 30 40 50 60 MGDRSEGPGP TRPGPPGIGP EGPLGQLLRR HRSPSPTRGG QEPRRVRRRV LVQQEEEVVS 70 80 90 100 110 120 GSPSGPRGDR SEGPGPTRPG PPGIGPEGPL GQLLRRHRSP SPTRGGQEPR RVRRRVLVQQ 130 140 150 160 170 180 EEEVVSGSPS GPRGDRSEGP GPTRPGPPGI GPEGPLGQLL RRHRSPSPTR GGQEPRRVRR 190 200 210 220 230 240 RVLVQQEEEV VSGSPSGPRG DRSEGPGPTR PGPPGIGPEG PLGQLLRRHR SPSPTRGGQE 250 260 270 280 290 300 PRRVRRRVLV QQEEEVVSGS PSGPRGDRSE GPGPTRPGPP GIGPEGPLGQ LLRRHRSPSP 310 320 330 340 350 360 TRGGQEPRRV RRRVLVQQEE EVVSGSPSGP RGDRSEGPGP TRPGPPGIGP EGPLGQLLRR 370 380 390 400 410 420 HRSPSPTRGG QEPRRVRRRV LVQQEEEVVS GSPSGPRGDR SEGPGPTRPG PPGIGPEGPL 430 440 450 460 470 480 GQLLRRHRSP SPTRGGQEPR RVRRRVLVQQ EEEVVSGSPS GPLRPRPRPP ARSLREWLLR 490 500 IRDHFEPPTV TTQRQSVYIE EEEDED

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]	"Conserved regions in the Epstein-Barr virus leader protein define distinct domains required for nuclear localization and transcriptional cooperation with EBNA2." Peng R., Tan J., Ling P.D. J. Virol. 74:9953-9963(2000) [PubMed: 11024123] [Abstract] Cited for: SUBCELLULAR LOCATION.
[3]	"Epstein-Barr virus nuclear antigen 5 interacts with HAX-1, a possible component of the B-cell receptor signalling pathway." Dufva M., Olsson M., Rymo L. J. Gen. Virol. 82:1581-1587(2001) [PubMed: 11413368] [Abstract] Cited for: INTERACTION WITH HUMAN HAX1.
[4]	"EBNA-LP associates with cellular proteins including DNA-PK and HA95." Han I., Harada S., Weaver D., Xue Y., Lane W., Orstavik S., Skalhegg B., Kieff E. J. Virol. 75:2475-2481(2001) [PubMed: 11160753] [Abstract] Cited for: INTERACTION WITH HUMAN PRKDC AND AKAP8L.
[5]	"Physical interaction of Epstein-Barr virus (EBV) nuclear antigen leader protein (EBNA-LP) with human oestrogen-related receptor 1 (hERR1): hERR1 interacts with a conserved domain of EBNA-LP that is critical for EBV-induced B-cell immortalization." Igarashi M., Kawaguchi Y., Hirai K., Mizuno F. J. Gen. Virol. 84:319-327(2003) [PubMed: 12560563] [Abstract] Cited for: INTERACTION WITH HUMAN ERR1.
[6]	"Identification of protein kinases responsible for phosphorylation of Epstein-Barr virus nuclear antigen leader protein at serine-35, which regulates its coactivator function." Kato K., Yokoyama A., Tohya Y., Akashi H., Nishiyama Y., Kawaguchi Y. J. Gen. Virol. 84:3381-3392(2003) [PubMed: 14645919] [Abstract] Cited for: PHOSPHORYLATION, MUTAGENESIS OF SER-35.
[7]	"Mediation of Epstein-Barr virus EBNA-LP transcriptional coactivation by Sp100." Ling P.D., Peng R.S., Nakajima A., Yu J.H., Tan J., Moses S.M., Yang W.H., Zhao B., Kieff E., Bloch K.D., Bloch D.B. EMBO J. 24:3565-3575(2005) [PubMed: 16177824] [Abstract] Cited for: INTERACTION WITH HUMAN SP100.
[8]	"Hsp72 up-regulates Epstein-Barr virus EBNALP coactivation with EBNA2." Peng C.W., Zhao B., Chen H.C., Chou M.L., Lai C.Y., Lin S.Z., Hsu H.Y., Kieff E. Blood 109:5447-5454(2007) [PubMed: 17341665] [Abstract] Cited for: INTERACTION WITH HUMAN HSPA2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	V01555 Genomic DNA. No translation available. AJ507799 Genomic DNA. Translation: CAD53387.1.
RefSeq	YP_401636.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8AZK7. 1 interaction.
Genome annotation databases
GeneID	3783746.
Family and domain databases
InterPro	IPR005030. Herpes_LP. [Graphical view]
Pfam	PF03363. Herpes_LP. 6 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

EBNA5_EBVB9

Accession

Primary (citable) accession number: Q8AZK7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 26, 2009
Last sequence update:	March 1, 2003
Last modified:	January 19, 2010
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)