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Epstein-Barr nuclear antigen leader protein (EBNA-LP) (EBV nuclear antigen leader protein) (Epstein-Barr nuclear antigen 5) (EBNA-5) (EBV nuclear antigen 5)

 EBNA5_EBVB9             Reviewed;         506 AA.
Q8AZK7;
26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
23-MAY-2018, entry version 78.
RecName: Full=Epstein-Barr nuclear antigen leader protein;
Short=EBNA-LP;
Short=EBV nuclear antigen leader protein;
AltName: Full=Epstein-Barr nuclear antigen 5;
Short=EBNA-5;
Short=EBV nuclear antigen 5;
Name=EBNA-LP; Synonyms=EBNA5;
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4).
Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae;
Gammaherpesvirinae; Lymphocryptovirus.
NCBI_TaxID=10377;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=6087149; DOI=10.1038/310207a0;
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.;
"DNA sequence and expression of the B95-8 Epstein-Barr virus genome.";
Nature 310:207-211(1984).
[2]
SUBCELLULAR LOCATION.
PubMed=11024123; DOI=10.1128/JVI.74.21.9953-9963.2000;
Peng R., Tan J., Ling P.D.;
"Conserved regions in the Epstein-Barr virus leader protein define
distinct domains required for nuclear localization and transcriptional
cooperation with EBNA2.";
J. Virol. 74:9953-9963(2000).
[3]
INTERACTION WITH HUMAN HAX1.
PubMed=11413368;
Dufva M., Olsson M., Rymo L.;
"Epstein-Barr virus nuclear antigen 5 interacts with HAX-1, a possible
component of the B-cell receptor signalling pathway.";
J. Gen. Virol. 82:1581-1587(2001).
[4]
INTERACTION WITH HUMAN PRKDC AND AKAP8L.
PubMed=11160753; DOI=10.1128/JVI.75.5.2475-2481.2001;
Han I., Harada S., Weaver D., Xue Y., Lane W., Orstavik S.,
Skalhegg B., Kieff E.;
"EBNA-LP associates with cellular proteins including DNA-PK and
HA95.";
J. Virol. 75:2475-2481(2001).
[5]
INTERACTION WITH HUMAN ERR1.
PubMed=12560563; DOI=10.1099/vir.0.18615-0;
Igarashi M., Kawaguchi Y., Hirai K., Mizuno F.;
"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.";
J. Gen. Virol. 84:319-327(2003).
[6]
PHOSPHORYLATION AT SER-35, AND MUTAGENESIS OF SER-35.
PubMed=14645919; DOI=10.1099/vir.0.19454-0;
Kato K., Yokoyama A., Tohya Y., Akashi H., Nishiyama Y., Kawaguchi Y.;
"Identification of protein kinases responsible for phosphorylation of
Epstein-Barr virus nuclear antigen leader protein at serine-35, which
regulates its coactivator function.";
J. Gen. Virol. 84:3381-3392(2003).
[7]
INTERACTION WITH HUMAN SP100.
PubMed=16177824; DOI=10.1038/sj.emboj.7600820;
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.;
"Mediation of Epstein-Barr virus EBNA-LP transcriptional coactivation
by Sp100.";
EMBO J. 24:3565-3575(2005).
[8]
INTERACTION WITH HUMAN HSPA2.
PubMed=17341665; DOI=10.1182/blood-2006-08-040634;
Peng C.W., Zhao B., Chen H.C., Chou M.L., Lai C.Y., Lin S.Z.,
Hsu H.Y., Kieff E.;
"Hsp72 up-regulates Epstein-Barr virus EBNALP coactivation with
EBNA2.";
Blood 109:5447-5454(2007).
-!- 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: 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.
{ECO:0000269|PubMed:11160753, ECO:0000269|PubMed:11413368,
ECO:0000269|PubMed:12560563, ECO:0000269|PubMed:16177824,
ECO:0000269|PubMed:17341665}.
-!- INTERACTION:
O95816:BAG2 (xeno); NbExp=3; IntAct=EBI-1185167, EBI-355275;
Q9JLV1:Bag3 (xeno); NbExp=2; IntAct=EBI-1185167, EBI-309231;
Q8N726:CDKN2A (xeno); NbExp=5; IntAct=EBI-1185167, EBI-625922;
P17844:DDX5 (xeno); NbExp=2; IntAct=EBI-1185167, EBI-351962;
O75953:DNAJB5 (xeno); NbExp=3; IntAct=EBI-1185167, EBI-5655937;
P56524:HDAC4 (xeno); NbExp=5; IntAct=EBI-1185167, EBI-308629;
P61978:HNRNPK (xeno); NbExp=2; IntAct=EBI-1185167, EBI-304185;
P52272:HNRNPM (xeno); NbExp=2; IntAct=EBI-1185167, EBI-486809;
P08107:HSPA1B (xeno); NbExp=3; IntAct=EBI-1185167, EBI-629985;
P11142:HSPA8 (xeno); NbExp=3; IntAct=EBI-1185167, EBI-351896;
P19338:NCL (xeno); NbExp=2; IntAct=EBI-1185167, EBI-346967;
Q15233:NONO (xeno); NbExp=2; IntAct=EBI-1185167, EBI-350527;
Q13200:PSMD2 (xeno); NbExp=2; IntAct=EBI-1185167, EBI-357648;
P23246:SFPQ (xeno); NbExp=2; IntAct=EBI-1185167, EBI-355453;
P68363:TUBA1B (xeno); NbExp=3; IntAct=EBI-1185167, EBI-487083;
P07437:TUBB (xeno); NbExp=3; IntAct=EBI-1185167, EBI-350864;
-!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:11024123}.
-!- PTM: Phosphorylated by the cellular protein kinase cdc2.
{ECO:0000269|PubMed:14645919}.
-!- SIMILARITY: Belongs to the lymphocryptovirus EBNA-LP family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; V01555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AJ507799; CAD53387.1; -; Genomic_DNA.
RefSeq; YP_401636.1; NC_007605.1.
PDB; 5X8N; X-ray; 2.15 A; B=425-446.
PDBsum; 5X8N; -.
SMR; Q8AZK7; -.
BioGrid; 971788; 153.
DIP; DIP-39599N; -.
IntAct; Q8AZK7; 192.
MINT; Q8AZK7; -.
iPTMnet; Q8AZK7; -.
PRIDE; Q8AZK7; -.
GeneID; 3783746; -.
KEGG; vg:3783746; -.
KO; K19456; -.
OrthoDB; VOG0900022K; -.
Proteomes; UP000153037; Genome.
GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
GO; GO:0075341; C:host cell PML body; IDA:BHF-UCL.
GO; GO:0003713; F:transcription coactivator activity; IDA:BHF-UCL.
GO; GO:0075342; P:disruption by symbiont of host cell PML body; IDA:BHF-UCL.
GO; GO:0039695; P:DNA-templated viral transcription; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR005030; Herpes_LP.
Pfam; PF03363; Herpes_LP; 6.
1: Evidence at protein level;
3D-structure; Activator; Complete proteome; Host nucleus;
Host-virus interaction; Phosphoprotein; Reference proteome;
Transcription; Transcription regulation.
CHAIN 1 506 Epstein-Barr nuclear antigen leader
protein.
/FTId=PRO_0000376060.
COMPBIAS 29 482 Arg-rich.
COMPBIAS 500 505 Poly-Glu.
MOD_RES 35 35 Phosphoserine; by host.
{ECO:0000269|PubMed:14645919}.
MUTAGEN 35 35 S->A: 95% loss of phosphorylation.
{ECO:0000269|PubMed:14645919}.
SEQUENCE 506 AA; 54739 MW; CD2C6C3B737AC1E9 CRC64;
MGDRSEGPGP TRPGPPGIGP EGPLGQLLRR HRSPSPTRGG QEPRRVRRRV LVQQEEEVVS
GSPSGPRGDR SEGPGPTRPG PPGIGPEGPL GQLLRRHRSP SPTRGGQEPR RVRRRVLVQQ
EEEVVSGSPS GPRGDRSEGP GPTRPGPPGI GPEGPLGQLL RRHRSPSPTR GGQEPRRVRR
RVLVQQEEEV VSGSPSGPRG DRSEGPGPTR PGPPGIGPEG PLGQLLRRHR SPSPTRGGQE
PRRVRRRVLV QQEEEVVSGS PSGPRGDRSE GPGPTRPGPP GIGPEGPLGQ LLRRHRSPSP
TRGGQEPRRV RRRVLVQQEE EVVSGSPSGP RGDRSEGPGP TRPGPPGIGP EGPLGQLLRR
HRSPSPTRGG QEPRRVRRRV LVQQEEEVVS GSPSGPRGDR SEGPGPTRPG PPGIGPEGPL
GQLLRRHRSP SPTRGGQEPR RVRRRVLVQQ EEEVVSGSPS GPLRPRPRPP ARSLREWLLR
IRDHFEPPTV TTQRQSVYIE EEEDED


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