VIE2_HCMVM
ID VIE2_HCMVM Reviewed; 580 AA.
AC Q6SW29; D2K3S1;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 23-FEB-2022, entry version 65.
DE RecName: Full=Viral transcription factor IE2;
DE Short=IE2;
DE AltName: Full=Protein UL122;
GN Name=UL122;
OS Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=295027;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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).
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 (By similarity). {ECO:0000250}.
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host nucleus. Note=Colocalizes with host PML-
CC associated nuclear bodies. {ECO:0000250}.
CC -!- DOMAIN: The SUMO-interacting motif (SIM) is required for efficient
CC transactivation function. {ECO:0000250}.
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; AY446894; AAR31665.1; -; Genomic_DNA.
DR RefSeq; YP_081561.1; NC_006273.2.
DR SMR; Q6SW29; -.
DR BioGRID; 1678116; 10.
DR IntAct; Q6SW29; 8.
DR PRIDE; Q6SW29; -.
DR GeneID; 3077563; -.
DR KEGG; vg:3077563; -.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR Proteomes; UP000000938; 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; ISS: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 3: Inferred from homology;
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; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..580
FT /note="Viral transcription factor IE2"
FT /id="PRO_0000417856"
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..336
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..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..321
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 580 AA; 63097 MW; 215BAFA207681B77 CRC64;
MESSAKRKMD PDNPDEGPSS KVPRPETPVT KATTFLQTML RKEVNSQLSL GDPLFPELAE
ESLKTFEQVT EDCNENPEKD VLTELGDILA QAVNHAGIDS SSTGPTLTTH SCSVSSAPLN
KPTPTSVAVT NTPLPGASAT PELSPRKKPR KTTRPFKVII KPPVPPAPIM LPLIKQEDIK
PEPDFTIQYR NKIIDTAGCI VISDSEEEQG EEVETRGATA SSPSTGSGTP RVTSPTHPLS
QMNHPPLPDP LGRPDEDSSS SSSSSCSSAS DSESESEEMK CSSGGGASVT SSHHGRGGFG
GAASSSLLSC GHQSSGGAST GPRKKKSKRI SELDNEKVRN IMKDKNTPFC TPNVQTRRGR
VKIDEVSRMF RHTNRSLEYK NLPFMIPSMH QVLEEAIKVC KTMQVNNKGI QIIYTRNHEV
KNEVDQVRCR LGSMCNLALS TPFLMEHTMP VTHPPDVAQR TADACNDGVK AVWNLKELHT
HQLCPRSSDY RNMIIHAATP VDLLGALNLC LPLMQKFPKQ VMVRIFSTNQ GGFMLPIYET
AAKAYAVGQF EKPTETPPED LDTLSLAIEA AIQDLRNKSQ
