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VIE1_HCMVM
ID   VIE1_HCMVM              Reviewed;         491 AA.
AC   F5HCM1;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Immediate early protein IE1;
DE            Short=IE1;
DE   AltName: Full=55 kDa immediate-early protein 1;
DE   AltName: Full=IE1p72 {ECO:0000250|UniProtKB:P03169};
DE   AltName: Full=IE72 {ECO:0000250|UniProtKB:P13202};
GN   Name=UL123;
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: Plays an important role in transactivating viral early genes
CC       as well as activating its own promoter, probably by altering the viral
CC       chromatin structure (By similarity). Expression of IE1 and IE2 proteins
CC       is critical for the establishment of lytic infection and reactivation
CC       from viral latency (By similarity). Disrupts PML-associated ND10
CC       nuclear bodies by interfering with host PML and SP100 sumoylation
CC       thereby altering the regulation of type I and type II interferon-
CC       induced gene expression (By similarity). Promotes efficient viral
CC       growth by interacting with and directing host SP100 to degradation,
CC       leading to enhanced acetylation level of histones (By similarity). In
CC       addition, functions in counteracting the host innate antiviral response
CC       (By similarity). Inhibits the type I interferon pathway by directly
CC       interacting with and sequestrating host STAT2 (By similarity). Also
CC       targets type II interferon pathway by repressing IL6- and STAT3 target
CC       genes (By similarity). Repression of STAT3 genes is due to STAT3
CC       nuclear accumulation and disruption of IL6-induced STAT3
CC       phosphorylation by IE1 (By similarity). This repression is followed by
CC       phosphorylation and activation of STAT1 (By similarity). Inhibits host
CC       ISG transcription by sequestering host ISGF3 in a PML- and
CC       STAT2- binding dependent manner (By similarity). Alters host cell cycle
CC       progression, probably through its interaction with host E2F1 or RB1
CC       that overcomes the RB1-mediated repression of E2F-responsive promoters
CC       (By similarity). {ECO:0000250|UniProtKB:P03169,
CC       ECO:0000250|UniProtKB:P13202}.
CC   -!- SUBUNIT: Interacts with human p53/TP53; this interaction inhibits
CC       p53/TP53-dependent transactivation activity. Interacts with host STAT1.
CC       Interacts with host STAT2; this interaction promotes viral growth and
CC       counteracts the antiviral interferon response. May also interact with
CC       the host STAT1-STAT2 heterodimer. Interacts with host STAT3; this
CC       interaction leads to STAT3 nuclear accumulation and disruption of IL6-
CC       induced STAT3 phosphorylation. Interacts with host PML; this
CC       interaction probably inhibits PML regulation of type I and type II
CC       interferon-induced gene expression. Interacts with host DAXX. Interacts
CC       with host SP100. Interacts with host E2F1. Interacts with host RB1.
CC       Interacts with host HDAC1; this interaction inhibits histone
CC       deacetylation and promotes viral transcription. Interacts with host
CC       HDAC2; this interaction inhibits histone deacetylation and promotes
CC       viral transcription. Interacts with host HDAC3; this interaction
CC       inhibits histone deacetylation and promotes viral transcription.
CC       {ECO:0000250|UniProtKB:P03169}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250|UniProtKB:P03169}.
CC       Note=Colocalizes with host PML-associated nuclear bodies very early
CC       post infection. {ECO:0000250|UniProtKB:P03169}.
CC   -!- DOMAIN: The N-terminal region is required for nuclear targeting. The C-
CC       terminal 16-amino acid is termed the chromosome-tethering domain (CTD)
CC       and is required for the association of IE1, host PML and host STAT2
CC       with the mitotic chromosomes. Targets host nucleosomes by directly
CC       binding to the acidic pocket of core histones.
CC       {ECO:0000250|UniProtKB:P03169}.
CC   -!- PTM: Sumoylated by host PML/nuclear domain 10 (By similarity).
CC       Sumoylation abolishes the interaction with host STAT2 and thus the IE1-
CC       mediated repression of interferon-stimulated genes (By similarity).
CC       {ECO:0000250|UniProtKB:P03169, ECO:0000250|UniProtKB:P13202}.
CC   -!- SIMILARITY: Belongs to the HHV-5 IE1 protein family. {ECO:0000305}.
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DR   EMBL; AY446894; AAR31666.1; -; Genomic_DNA.
DR   RefSeq; YP_081562.1; NC_006273.2.
DR   SMR; F5HCM1; -.
DR   BioGRID; 1678066; 14.
DR   PRIDE; F5HCM1; -.
DR   GeneID; 3077513; -.
DR   KEGG; vg:3077513; -.
DR   Reactome; R-HSA-9609690; HCMV Early Events.
DR   Proteomes; UP000000938; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0039695; P:DNA-templated viral transcription; ISS:UniProtKB.
DR   GO; GO:0039645; P:modulation by virus of host G1/S transition checkpoint; IEA:UniProtKB-KW.
DR   GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR010855; Cytomega_IE1/IE2.
DR   Pfam; PF07340; Herpes_IE1; 1.
PE   3: Inferred from homology;
KW   Activator; Early protein;
KW   G1/S host cell cycle checkpoint dysregulation by virus; Host nucleus;
KW   Host-virus interaction; Inhibition of host innate immune response by virus;
KW   Inhibition of host interferon signaling pathway by virus; Isopeptide bond;
KW   Modulation of host cell cycle by virus; Reference proteome;
KW   Ubl conjugation; Viral immunoevasion.
FT   CHAIN           1..491
FT                   /note="Immediate early protein IE1"
FT                   /id="PRO_0000416446"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1..24
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:P03169"
FT   REGION          132..346
FT                   /note="Interaction with host PML, interference with PML
FT                   sumoylation and disruption of PML-associated nuclear
FT                   bodies"
FT                   /evidence="ECO:0000250|UniProtKB:P03169"
FT   REGION          373..445
FT                   /note="Interaction with host STAT2"
FT                   /evidence="ECO:0000250|UniProtKB:P03169"
FT   REGION          410..445
FT                   /note="Interaction with host STAT3"
FT                   /evidence="ECO:0000250|UniProtKB:P03169"
FT   REGION          410..420
FT                   /note="Modulation of STAT3/STAT1 signaling"
FT                   /evidence="ECO:0000250|UniProtKB:P03169"
FT   REGION          421..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          421..472
FT                   /note="Acidic"
FT                   /evidence="ECO:0000250|UniProtKB:P03169"
FT   REGION          449..452
FT                   /note="Interaction with host SUMO1"
FT                   /evidence="ECO:0000250|UniProtKB:P03169"
FT   REGION          475..491
FT                   /note="Chromosome-tethering domain (CTD), binding to
FT                   histones"
FT                   /evidence="ECO:0000250|UniProtKB:P03169"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        425..441
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        450
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   491 AA;  55103 MW;  E5BE99891AC4A4C3 CRC64;
     MESSAKRKMD PDNPDEGPSS KVPRPETPVT KATTFLQTML RKEVNSQLSL GDPLFPELAE
     ESLKTFEQVT EDCNENPEKD VLTELVKQIK VRVDMVRHRI KEHMLKKYTQ TEEKFTGAFN
     MMGGCLQNAL DILDKVHEPF EDMKCIGLTM QSMYENYIVP EDKREMWMAC IKELHDVSKG
     AANKLGGALQ AKARAKKDEL RRKMMYMCYR NIEFFTKNSA FPKTTNGCSQ AMAALQNLPQ
     CSPDEIMSYA QKIFKILDEE RDKVLTHIDH IFMDILTTCV ETMCNEYKVT SDACMMTMYG
     GISLLSEFCR VLCCYVLEET SVMLAKRPLI TKPEVISVMK RRIEEICMKV FAQYILGADP
     LRVCSPSVDD LRAIAEESDE EEAIVAYTLA TAGASSSDSL VSPPESPVPA TIPLSSVIVA
     ENSDQEESEQ SDEEQEEGAQ EEREDTVSVK SEPVSEIEEV ASEEEEDGAE EPTASGGKST
     HPMVTRSKAD Q
 
 
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