EBNA5_EBVB9
ID EBNA5_EBVB9 Reviewed; 506 AA.
AC Q8AZK7;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 02-JUN-2021, entry version 91.
DE RecName: Full=Epstein-Barr nuclear antigen leader protein;
DE Short=EBNA-LP;
DE Short=EBV nuclear antigen leader protein;
DE AltName: Full=Epstein-Barr nuclear antigen 5;
DE Short=EBNA-5;
DE Short=EBV nuclear antigen 5;
GN Name=EBNA-LP; Synonyms=EBNA5;
OS Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX NCBI_TaxID=10377;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6087149; DOI=10.1038/310207a0;
RA Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J.,
RA Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C.,
RA Tuffnell P.S., Barrell B.G.;
RT "DNA sequence and expression of the B95-8 Epstein-Barr virus genome.";
RL Nature 310:207-211(1984).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=11024123; DOI=10.1128/jvi.74.21.9953-9963.2000;
RA Peng R., Tan J., Ling P.D.;
RT "Conserved regions in the Epstein-Barr virus leader protein define distinct
RT domains required for nuclear localization and transcriptional cooperation
RT with EBNA2.";
RL J. Virol. 74:9953-9963(2000).
RN [3]
RP INTERACTION WITH HUMAN HAX1.
RX PubMed=11413368; DOI=10.1099/0022-1317-82-7-1581;
RA Dufva M., Olsson M., Rymo L.;
RT "Epstein-Barr virus nuclear antigen 5 interacts with HAX-1, a possible
RT component of the B-cell receptor signalling pathway.";
RL J. Gen. Virol. 82:1581-1587(2001).
RN [4]
RP INTERACTION WITH HUMAN PRKDC AND AKAP8L.
RX PubMed=11160753; DOI=10.1128/jvi.75.5.2475-2481.2001;
RA Han I., Harada S., Weaver D., Xue Y., Lane W., Orstavik S., Skalhegg B.,
RA Kieff E.;
RT "EBNA-LP associates with cellular proteins including DNA-PK and HA95.";
RL J. Virol. 75:2475-2481(2001).
RN [5]
RP INTERACTION WITH HUMAN ERR1.
RX PubMed=12560563; DOI=10.1099/vir.0.18615-0;
RA Igarashi M., Kawaguchi Y., Hirai K., Mizuno F.;
RT "Physical interaction of Epstein-Barr virus (EBV) nuclear antigen leader
RT protein (EBNA-LP) with human oestrogen-related receptor 1 (hERR1): hERR1
RT interacts with a conserved domain of EBNA-LP that is critical for EBV-
RT induced B-cell immortalization.";
RL J. Gen. Virol. 84:319-327(2003).
RN [6]
RP PHOSPHORYLATION AT SER-35, AND MUTAGENESIS OF SER-35.
RX PubMed=14645919; DOI=10.1099/vir.0.19454-0;
RA Kato K., Yokoyama A., Tohya Y., Akashi H., Nishiyama Y., Kawaguchi Y.;
RT "Identification of protein kinases responsible for phosphorylation of
RT Epstein-Barr virus nuclear antigen leader protein at serine-35, which
RT regulates its coactivator function.";
RL J. Gen. Virol. 84:3381-3392(2003).
RN [7]
RP INTERACTION WITH HUMAN SP100.
RX PubMed=16177824; DOI=10.1038/sj.emboj.7600820;
RA Ling P.D., Peng R.S., Nakajima A., Yu J.H., Tan J., Moses S.M., Yang W.H.,
RA Zhao B., Kieff E., Bloch K.D., Bloch D.B.;
RT "Mediation of Epstein-Barr virus EBNA-LP transcriptional coactivation by
RT Sp100.";
RL EMBO J. 24:3565-3575(2005).
RN [8]
RP INTERACTION WITH HUMAN HSPA2.
RX PubMed=17341665; DOI=10.1182/blood-2006-08-040634;
RA Peng C.W., Zhao B., Chen H.C., Chou M.L., Lai C.Y., Lin S.Z., Hsu H.Y.,
RA Kieff E.;
RT "Hsp72 up-regulates Epstein-Barr virus EBNALP coactivation with EBNA2.";
RL Blood 109:5447-5454(2007).
CC -!- FUNCTION: Plays an important role in the establishment of B-cell
CC immortalization by acting as an EBNA2 coactivator. This transcriptional
CC activation preferentially enhances the expression of the major viral
CC protein LMP1. The interaction between EBNA-LP and host SP100 correlates
CC with coactivation of EBNA2 and the relocalization of SP100 from PML
CC nuclear bodies into nucleoplasm.
CC -!- SUBUNIT: Homooligomer. Interacts with host SP100; this interaction is
CC important for EBNA-LP coactivator activity. Interacts with host HAX1,
CC ERR1 and HSPA2. Interacts with host PRKDC and AKAP8L; these
CC interactions modulate the coactivator function of EBNA-LP.
CC {ECO:0000269|PubMed:11160753, ECO:0000269|PubMed:11413368,
CC ECO:0000269|PubMed:12560563, ECO:0000269|PubMed:16177824,
CC ECO:0000269|PubMed:17341665}.
CC -!- INTERACTION:
CC Q8AZK7; O95816: BAG2; Xeno; NbExp=3; IntAct=EBI-1185167, EBI-355275;
CC Q8AZK7; Q9JLV1: Bag3; Xeno; NbExp=2; IntAct=EBI-1185167, EBI-309231;
CC Q8AZK7; Q8N726: CDKN2A; Xeno; NbExp=5; IntAct=EBI-1185167, EBI-625922;
CC Q8AZK7; P17844: DDX5; Xeno; NbExp=2; IntAct=EBI-1185167, EBI-351962;
CC Q8AZK7; O75953: DNAJB5; Xeno; NbExp=3; IntAct=EBI-1185167, EBI-5655937;
CC Q8AZK7; P56524: HDAC4; Xeno; NbExp=5; IntAct=EBI-1185167, EBI-308629;
CC Q8AZK7; P61978: HNRNPK; Xeno; NbExp=2; IntAct=EBI-1185167, EBI-304185;
CC Q8AZK7; P52272: HNRNPM; Xeno; NbExp=2; IntAct=EBI-1185167, EBI-486809;
CC Q8AZK7; P08107: HSPA1B; Xeno; NbExp=3; IntAct=EBI-1185167, EBI-629985;
CC Q8AZK7; P11142: HSPA8; Xeno; NbExp=3; IntAct=EBI-1185167, EBI-351896;
CC Q8AZK7; P19338: NCL; Xeno; NbExp=2; IntAct=EBI-1185167, EBI-346967;
CC Q8AZK7; Q15233: NONO; Xeno; NbExp=2; IntAct=EBI-1185167, EBI-350527;
CC Q8AZK7; Q13200: PSMD2; Xeno; NbExp=2; IntAct=EBI-1185167, EBI-357648;
CC Q8AZK7; P23246: SFPQ; Xeno; NbExp=2; IntAct=EBI-1185167, EBI-355453;
CC Q8AZK7; P68363: TUBA1B; Xeno; NbExp=3; IntAct=EBI-1185167, EBI-487083;
CC Q8AZK7; P07437: TUBB; Xeno; NbExp=3; IntAct=EBI-1185167, EBI-350864;
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:11024123}.
CC -!- PTM: Phosphorylated by the cellular protein kinase cdc2.
CC {ECO:0000269|PubMed:14645919}.
CC -!- SIMILARITY: Belongs to the lymphocryptovirus EBNA-LP family.
CC {ECO:0000305}.
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DR EMBL; V01555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJ507799; CAD53387.1; -; Genomic_DNA.
DR RefSeq; YP_401636.1; NC_007605.1.
DR PDB; 5X8N; X-ray; 2.15 A; B=425-446.
DR PDBsum; 5X8N; -.
DR SMR; Q8AZK7; -.
DR BioGRID; 971788; 154.
DR DIP; DIP-39599N; -.
DR IntAct; Q8AZK7; 192.
DR MINT; Q8AZK7; -.
DR iPTMnet; Q8AZK7; -.
DR PRIDE; Q8AZK7; -.
DR DNASU; 3783746; -.
DR GeneID; 3783746; -.
DR KEGG; vg:3783746; -.
DR Proteomes; UP000153037; Genome.
DR GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
DR GO; GO:0075341; C:host cell PML body; IDA:BHF-UCL.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:BHF-UCL.
DR GO; GO:0075342; P:disruption by symbiont of host cell PML body; IDA:BHF-UCL.
DR GO; GO:0039695; P:DNA-templated viral transcription; IDA:UniProtKB.
DR InterPro; IPR005030; Herpes_LP.
DR Pfam; PF03363; Herpes_LP; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Host nucleus; Host-virus interaction;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..506
FT /note="Epstein-Barr nuclear antigen leader protein"
FT /id="PRO_0000376060"
FT REGION 1..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 35
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:14645919"
FT MUTAGEN 35
FT /note="S->A: 95% loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:14645919"
SQ 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
