KBZIP_HHV8P
ID KBZIP_HHV8P Reviewed; 286 AA.
AC Q2HR82;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 02-JUN-2021, entry version 52.
DE RecName: Full=E3 SUMO-protein ligase K-bZIP;
DE EC=2.3.2.-;
DE AltName: Full=E3 SUMO-protein transferase K-bZIP {ECO:0000305};
GN Name=K8;
OS Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's
OS sarcoma-associated herpesvirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX NCBI_TaxID=868565;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10400794; DOI=10.1128/jvi.73.8.6953-6963.1999;
RA Glenn M., Rainbow L., Aurade F., Davison A., Schulz T.F.;
RT "Identification of a spliced gene from Kaposi's sarcoma-associated
RT herpesvirus encoding a protein with similarities to latent membrane
RT proteins 1 and 2A of Epstein-Barr virus.";
RL J. Virol. 73:6953-6963(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16760382; DOI=10.1099/vir.0.81919-0;
RA Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.;
RT "Kaposi's sarcoma-associated herpesvirus immune modulation: an overview.";
RL J. Gen. Virol. 87:1781-1804(2006).
RN [3]
RP FUNCTION IN CELL CYCLE ARREST.
RX PubMed=12145325; DOI=10.1073/pnas.162352299;
RA Wu F.Y., Tang Q.Q., Chen H., ApRhys C., Farrell C., Chen J., Fujimuro M.,
RA Lane M.D., Hayward G.S.;
RT "Lytic replication-associated protein (RAP) encoded by Kaposi sarcoma-
RT associated herpesvirus causes p21CIP-1-mediated G1 cell cycle arrest
RT through CCAAT/enhancer-binding protein-alpha.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:10683-10688(2002).
RN [4]
RP FUNCTION.
RX PubMed=17652396; DOI=10.1128/jvi.00183-07;
RA Lefort S., Soucy-Faulkner A., Grandvaux N., Flamand L.;
RT "Binding of Kaposi's sarcoma-associated herpesvirus K-bZIP to interferon-
RT responsive factor 3 elements modulates antiviral gene expression.";
RL J. Virol. 81:10950-10960(2007).
RN [5]
RP FUNCTION, AND INTERACTION WITH PROTEIN K8.
RX PubMed=17108053; DOI=10.1128/jvi.01473-06;
RA Izumiya Y., Izumiya C., Van Geelen A., Wang D.H., Lam K.S., Luciw P.A.,
RA Kung H.J.;
RT "Kaposi's sarcoma-associated herpesvirus-encoded protein kinase and its
RT interaction with K-bZIP.";
RL J. Virol. 81:1072-1082(2007).
RN [6]
RP FUNCTION AS SUMO E3 LIGASE.
RX PubMed=20034935; DOI=10.1074/jbc.m109.088088;
RA Chang P.C., Izumiya Y., Wu C.Y., Fitzgerald L.D., Campbell M.,
RA Ellison T.J., Lam K.S., Luciw P.A., Kung H.J.;
RT "Kaposi's sarcoma-associated herpesvirus (KSHV) encodes a SUMO E3 ligase
RT that is SIM-dependent and SUMO-2/3-specific.";
RL J. Biol. Chem. 285:5266-5273(2010).
RN [7]
RP INTERACTION WITH HOST HDAC1 AND HDAC2.
RX PubMed=22416134; DOI=10.1074/jbc.m111.315861;
RA Martinez F.P., Tang Q.;
RT "Leucine zipper domain is required for Kaposi sarcoma-associated
RT herpesvirus (KSHV) K-bZIP protein to interact with histone deacetylase and
RT is important for KSHV replication.";
RL J. Biol. Chem. 287:15622-15634(2012).
RN [8]
RP INTERACTION WITH PROTEIN ORF57.
RX PubMed=23365430; DOI=10.1128/jvi.03459-12;
RA Hunter O.V., Sei E., Richardson R.B., Conrad N.K.;
RT "Chromatin immunoprecipitation and microarray analysis suggest functional
RT cooperation between Kaposi's Sarcoma-associated herpesvirus ORF57 and K-
RT bZIP.";
RL J. Virol. 87:4005-4016(2013).
CC -!- FUNCTION: Plays a role in viral gene regulation and seems to be
CC essential for KSHV reactivation. Disrupts host G1 cell cycle control
CC thus allowing viral transcription and translation to proceed at the
CC early stages of infection. Catalyzes its own SUMO modification as well
CC as that of its interacting partners such as host TP53 AND RB1.
CC {ECO:0000269|PubMed:12145325, ECO:0000269|PubMed:17108053,
CC ECO:0000269|PubMed:17652396, ECO:0000269|PubMed:20034935}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Interacts with host HDAC1 and HDAC2, these interactions
CC suppress HDAC activities. Interacts with protein ORF57. Interacts with
CC protein vPK (PubMed:17108053). {ECO:0000269|PubMed:17108053,
CC ECO:0000269|PubMed:22416134, ECO:0000269|PubMed:23365430}.
CC -!- INTERACTION:
CC Q2HR82; Q2HR75: ORF57; NbExp=5; IntAct=EBI-9006943, EBI-6884751;
CC Q2HR82; Q92769: HDAC2; Xeno; NbExp=7; IntAct=EBI-9006943, EBI-301821;
CC -!- PTM: Sumoylated.
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DR EMBL; AF148805; ABD28901.1; -; Genomic_DNA.
DR RefSeq; YP_001129403.1; NC_009333.1.
DR SMR; Q2HR82; -.
DR BioGRID; 1776965; 21.
DR IntAct; Q2HR82; 6.
DR PRIDE; Q2HR82; -.
DR GeneID; 4961462; -.
DR KEGG; vg:4961462; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000000942; Genome.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IDA:UniProtKB.
DR GO; GO:0039645; P:modulation by virus of host G1/S transition checkpoint; IEA:UniProtKB-KW.
DR GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR010805; KSHV_K8.
DR Pfam; PF07188; KSHV_K8; 1.
PE 1: Evidence at protein level;
KW G1/S host cell cycle checkpoint dysregulation by virus;
KW Host-virus interaction; Modulation of host cell cycle by virus;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..286
FT /note="E3 SUMO-protein ligase K-bZIP"
FT /id="PRO_0000423846"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 286 AA; 31574 MW; 69FE9D78A4BB4FEC CRC64;
MPRMKDIPTK SSPGTDNSEK DEAVIEEDLS LNGQPFFTDN TDGGENEVSW TSSLLSTYVG
CQPPAIPVCE TVIDLTAPSQ SGAPGDEHLP CSLNAETKFH IPDPSWTLSH TPPRGPHISQ
QLPTRRSKRR LHRKFEEERL CTKAKQGAGR PVPASVVKVG NITPHYGEEL TRGDAVPAAP
ITPPYPRVQR PAQPTHVLFS PVFVSLKAEV CDQSHSPTRK QGRYGRVSSK AYTRQLQQAL
EEKDAQLCFL AARLEAHKEQ IIFLRDMLMR MCQQPASPTD APLPPC
