VIE2_HCMVT
ID VIE2_HCMVT Reviewed; 579 AA.
AC Q6SWP7;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 23-FEB-2022, entry version 51.
DE RecName: Full=Viral transcription factor IE2;
DE Short=IE2;
DE AltName: Full=Protein UL122;
GN Name=UL122;
OS Human cytomegalovirus (strain Towne) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=10363;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Towne;
RX PubMed=15105547; DOI=10.1099/vir.0.79888-0;
RA Dolan A., Cunningham C., Hector R.D., Hassan-Walker A.F., Lee L.,
RA Addison C., Dargan D.J., McGeoch D.J., Gatherer D., Emery V.C.,
RA Griffiths P.D., Sinzger C., McSharry B.P., Wilkinson G.W.G., Davison A.J.;
RT "Genetic content of wild-type human cytomegalovirus.";
RL J. Gen. Virol. 85:1301-1312(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Towne;
RX PubMed=19553388; DOI=10.1099/vir.0.013250-0;
RA Bradley A.J., Lurain N.S., Ghazal P., Trivedi U., Cunningham C.,
RA Baluchova K., Gatherer D., Wilkinson G.W., Dargan D.J., Davison A.J.;
RT "High-throughput sequence analysis of variants of human cytomegalovirus
RT strains Towne and AD169.";
RL J. Gen. Virol. 90:2375-2380(2009).
RN [3]
RP INTERACTION WITH HOST TBP AND TF2B.
RX PubMed=8277274; DOI=10.1099/0022-1317-74-12-2691;
RA Caswell R., Hagemeier C., Chiou C.J., Hayward G., Kouzarides T.,
RA Sinclair J.;
RT "The human cytomegalovirus 86K immediate early (IE) 2 protein requires the
RT basic region of the TATA-box binding protein (TBP) for binding, and
RT interacts with TBP and transcription factor TFIIB via regions of IE2
RT required for transcriptional regulation.";
RL J. Gen. Virol. 74:2691-2698(1993).
RN [4]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=9151854; DOI=10.1128/jvi.71.6.4599-4613.1997;
RA Ahn J.H., Hayward G.S.;
RT "The major immediate-early proteins IE1 and IE2 of human cytomegalovirus
RT colocalize with and disrupt PML-associated nuclear bodies at very early
RT times in infected permissive cells.";
RL J. Virol. 71:4599-4613(1997).
RN [5]
RP FUNCTION IN HOST CELL CYCLE MODULATION.
RX PubMed=11867723; DOI=10.1073/pnas.052010099;
RA Song Y.J., Stinski M.F.;
RT "Effect of the human cytomegalovirus IE86 protein on expression of E2F-
RT responsive genes: a DNA microarray analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2836-2841(2002).
RN [6]
RP INTERACTION WITH HOST CHAF1A.
RX PubMed=21445097; DOI=10.1038/cr.2011.53;
RA Lee S.B., Lee C.F., Ou D.S., Dulal K., Chang L.H., Ma C.H., Huang C.F.,
RA Zhu H., Lin Y.S., Juan L.J.;
RT "Host-viral effects of chromatin assembly factor 1 interaction with HCMV
RT IE2.";
RL Cell Res. 21:1230-1247(2011).
CC -!- FUNCTION: Stimulates viral early and late gene expression and thus play
CC a crucial role in the regulation of productive infection. In addition,
CC activates quiescent cells to reenter the cell cycle and up-regulates
CC several E2F-responsive genes, which are responsible for pushing the
CC cell into S phase. In S-phase, inhibits cellular DNA synthesis and
CC blocks further cell cycle progression. {ECO:0000269|PubMed:11867723,
CC ECO:0000269|PubMed:9151854}.
CC -!- SUBUNIT: Interacts with host SUMO-modified form of TATA-binding protein
CC (TBP)-associated factor 12/TAF12 in a SIM-dependent manner; this
CC interaction increases the transactivation activity of IE2. Interacts
CC with host CHAF1A. Interacts with several components of the host
CC transcriptional machinery including TBP, TF2B and CREB1. Interacts with
CC host DNA replication licensing factor MCM3.
CC {ECO:0000269|PubMed:21445097, ECO:0000269|PubMed:8277274}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:9151854}.
CC Note=Colocalizes with host PML-associated nuclear bodies.
CC -!- DOMAIN: The SUMO-interacting motif (SIM) is required for efficient
CC transactivation function.
CC -!- PTM: Sumoylated. The sumoylation is necessary for efficient replication
CC of the virus and thus for the function of this viral transcription
CC factor (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HHV-5 IE2 protein family. {ECO:0000305}.
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DR EMBL; FJ616285; AAR31449.1; -; Genomic_DNA.
DR SMR; Q6SWP7; -.
DR Proteomes; UP000006907; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0039695; P:DNA-templated viral transcription; IDA:UniProtKB.
DR GO; GO:0039646; P:modulation by virus of host G0/G1 transition checkpoint; IEA:UniProtKB-KW.
DR GO; GO:0039645; P:modulation by virus of host G1/S transition checkpoint; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR010855; Cytomega_IE1/IE2.
DR InterPro; IPR005028; Herpes_IE2_3.
DR Pfam; PF07340; Herpes_IE1; 1.
DR Pfam; PF03361; Herpes_IE2_3; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Early protein;
KW G0/G1 host cell cycle checkpoint dysregulation by virus;
KW G1/S host cell cycle checkpoint dysregulation by virus; Host nucleus;
KW Host-virus interaction; Isopeptide bond; Metal-binding;
KW Modulation of host cell cycle by virus; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..579
FT /note="Viral transcription factor IE2"
FT /id="PRO_0000417855"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..208
FT /note="Non-covalent SUMO1 binding region (SIM)"
FT /evidence="ECO:0000250"
FT REGION 206..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 175
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 180
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 579 AA; 62816 MW; 4697632BDA0EFB2C CRC64;
MESSAKRKMD PDNPDEGPSS KVPRPETPVT KATTFLQTML RKEVNSQLSL GDPLFPELAE
ESLKTFERVT EDCNENPEKD VLAELGDILA QAVNHAGIDS SSTGPTLTTH SCSVSSAPLN
KPTPTSVAVT NTPLPGASAT PELSPRKKPR KTTRPFKVII KPPVPPAPIM LPLIKQEDIK
PEPDFTIQYR NKIIDTAGCI VISDSEEEQG EEVETRGATA SSPSTGSGTP RVTSPTHPLS
QMNHPPLPDP LGRPDEDSSS SSSSCSSASD SESESEEMKC SSGGGASVTS SHHGRGGFGG
AASSSLLSCG HQSSGGASTG PRKKKSKRIS ELDNEKVRNI MKDKNTPFCT PNVQTRRGRV
KIDEVSRMFR NTNRSLEYKN LPFTIPSMHQ VLDEAIKACK TMQVNNKGIQ IIYTRNHEVK
SEVDAVRCRL GTMCNLALST PFLMEHTMPV THPPEVAQRT ADACNEGVKA AWSLKELHTH
QLCPRSSDYR NMIIHAATPV DLLGALNLCL PLMQKFPKQV MVRIFSTNQG GFMLPIYETA
AKAYAVGQFE QPTETPPEDL DTLSLAIEAA IQDLRNKSQ
