E1A_ADE05
ID E1A_ADE05 Reviewed; 289 AA.
AC P03255; P06438; Q64825; Q64826;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 159.
DE RecName: Full=Early E1A protein;
DE AltName: Full=Early E1A 32 kDa protein;
OS Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus.
OX NCBI_TaxID=28285;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS EARLY E1A 32 KDA PROTEIN; EARLY
RP E1A 26 KDA PROTEIN AND EARLY E1A 6 KDA PROTEIN).
RX PubMed=6260576; DOI=10.1016/0378-1119(80)90070-0;
RA van Ormondt H., Maat J., van Beveren C.P.;
RT "The nucleotide sequence of the transforming early region E1 of adenovirus
RT type 5 DNA.";
RL Gene 11:299-309(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1727603; DOI=10.1016/0042-6822(92)90082-z;
RA Chroboczek J., Bieber F., Jacrot B.;
RT "The sequence of the genome of adenovirus type 5 and its comparison with
RT the genome of adenovirus type 2.";
RL Virology 186:280-285(1992).
RN [3]
RP PHOSPHORYLATION AT SER-89; SER-219 AND SER-231.
RX PubMed=2966155; DOI=10.1016/s0021-9258(18)68796-4;
RA Tremblay M.L., McGlade C.J., Gerber G.E., Branton P.E.;
RT "Identification of the phosphorylation sites in early region 1A proteins of
RT adenovirus type 5 by amino acid sequencing of peptide fragments.";
RL J. Biol. Chem. 263:6375-6383(1988).
RN [4]
RP ZINC-FINGER, AND MUTAGENESIS OF CYS-154; CYS-157; CYS-171 AND CYS-174.
RX PubMed=1835093; DOI=10.1073/pnas.88.22.9989;
RA Webster L.C., Zhang K., Chance B., Ayene I., Culp J.S., Huang W.-J.,
RA Wu F.Y.-H., Ricciardi R.P.;
RT "Conversion of the E1A Cys4 zinc finger to a nonfunctional His2,Cys2 zinc
RT finger by a single point mutation.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:9989-9993(1991).
RN [5]
RP ZINC-FINGER, AND INTERACTION WITH HUMAN TBP PROTEIN.
RX PubMed=8146144; DOI=10.1073/pnas.91.7.2488;
RA Geisberg J.V., Lee W.S., Berk A.J., Ricciardi R.P.;
RT "The zinc finger region of the adenovirus E1A transactivating domain
RT complexes with the TATA box binding protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:2488-2492(1994).
RN [6]
RP INTERACTION WITH HUMAN CTBP1.
RX PubMed=7479821; DOI=10.1073/pnas.92.23.10467;
RA Schaeper U., Boyd J.M., Verma S., Uhlmann E., Subramanian T.,
RA Chinnadurai G.;
RT "Molecular cloning and characterization of a cellular phosphoprotein that
RT interacts with a conserved C-terminal domain of adenovirus E1A involved in
RT negative modulation of oncogenic transformation.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:10467-10471(1995).
RN [7]
RP INTERACTION WITH HUMAN UBE2I, AND MUTAGENESIS OF LEU-122.
RX PubMed=8824223; DOI=10.1074/jbc.271.42.25906;
RA Hateboer G., Hijmans E.M., Nooij J.B.D., Schlenker S., Jentsch S.,
RA Bernards R.;
RT "mUBC9, a novel adenovirus E1A-interacting protein that complements a yeast
RT cell cycle defect.";
RL J. Biol. Chem. 271:25906-25911(1996).
RN [8]
RP FUNCTION OF ISOFORM EARLY E1A 26 KDA PROTEIN.
RX PubMed=9685342; DOI=10.1074/jbc.273.32.20036;
RA Nakajima T., Morita K., Tsunoda H., Imajoh-Ohmi S., Tanaka H., Yasuda H.,
RA Oda K.;
RT "Stabilization of p53 by adenovirus E1A occurs through its amino-terminal
RT region by modification of the ubiquitin-proteasome pathway.";
RL J. Biol. Chem. 273:20036-20045(1998).
RN [9]
RP INTERACTION WITH HUMAN EP300.
RX PubMed=11433299; DOI=10.1038/35083062;
RA Chan H.M., Krstic-Demonacos M., Smith L., Demonacos C., La Thangue N.B.;
RT "Acetylation control of the retinoblastoma tumour-suppressor protein.";
RL Nat. Cell Biol. 3:667-674(2001).
RN [10]
RP INTERACTION WITH HUMAN ZMYND11/BS69, AND MUTAGENESIS OF LEU-115.
RX PubMed=11733528; DOI=10.1074/jbc.m110078200;
RA Ansieau S., Leutz A.;
RT "The conserved Mynd domain of BS69 binds cellular and oncoviral proteins
RT through a common PXLXP motif.";
RL J. Biol. Chem. 277:4906-4910(2002).
RN [11]
RP REVIEW ON FUNCTION.
RX PubMed=12204530; DOI=10.1016/s1535-6108(02)00102-2;
RA Sherr C.J., McCormick F.;
RT "The RB and p53 pathways in cancer.";
RL Cancer Cell 2:103-112(2002).
RN [12]
RP FUNCTION.
RX PubMed=15806172; DOI=10.1038/sj.onc.1208539;
RA Ledl A., Schmidt D., Muller S.;
RT "Viral oncoproteins E1A and E7 and cellular LxCxE proteins repress SUMO
RT modification of the retinoblastoma tumor suppressor.";
RL Oncogene 24:3810-3818(2005).
RN [13]
RP INTERACTION WITH HUMAN EP400.
RX PubMed=18413597; DOI=10.1073/pnas.0802095105;
RA Tworkowski K.A., Chakraborty A.A., Samuelson A.V., Seger Y.R., Narita M.,
RA Hannon G.J., Lowe S.W., Tansey W.P.;
RT "Adenovirus E1A targets p400 to induce the cellular oncoprotein Myc.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:6103-6108(2008).
RN [14]
RP FUNCTION, INTERACTION WITH HUMAN RBX1, INTERACTION WITH SCF(FBXW7) COMPLEX,
RP AND INTERACTION WITH HUMAN CUL1.
RX PubMed=19679664; DOI=10.1074/jbc.m109.006809;
RA Isobe T., Hattori T., Kitagawa K., Uchida C., Kotake Y., Kosugi I., Oda T.,
RA Kitagawa M.;
RT "Adenovirus E1A inhibits SCF(Fbw7) ubiquitin ligase.";
RL J. Biol. Chem. 284:27766-27779(2009).
RN [15]
RP FUNCTION, AND INTERACTION WITH HOST UBE2I.
RX PubMed=20543865; DOI=10.1038/onc.2010.226;
RA Yousef A.F., Fonseca G.J., Pelka P., Ablack J.N., Walsh C., Dick F.A.,
RA Bazett-Jones D.P., Shaw G.S., Mymryk J.S.;
RT "Identification of a molecular recognition feature in the E1A oncoprotein
RT that binds the SUMO conjugase UBC9 and likely interferes with
RT polySUMOylation.";
RL Oncogene 29:4693-4704(2010).
RN [16]
RP INTERACTION WITH HUMAN CTBP1, INTERACTION WITH HUMAN CTBP2, AND MUTAGENESIS
RP OF 281-ASP-LEU-282.
RX PubMed=23747199; DOI=10.1016/j.virol.2013.05.018;
RA Subramanian T., Zhao L.J., Chinnadurai G.;
RT "Interaction of CtBP with adenovirus E1A suppresses immortalization of
RT primary epithelial cells and enhances virus replication during productive
RT infection.";
RL Virology 443:313-320(2013).
RN [17]
RP INTERACTION WITH HUMAN DCAF7, INTERACTION WITH HUMAN DYRK1A, AND
RP INTERACTION WITH HUMAN KPNA4.
RX PubMed=23864635; DOI=10.1128/jvi.00786-13;
RA Cohen M.J., Yousef A.F., Massimi P., Fonseca G.J., Todorovic B., Pelka P.,
RA Turnell A.S., Banks L., Mymryk J.S.;
RT "Dissection of the C-terminal region of E1A redefines the roles of CtBP and
RT other cellular targets in oncogenic transformation.";
RL J. Virol. 87:10348-10355(2013).
RN [18]
RP FUNCTION, INTERACTION WITH HUMAN ZBED1, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF THR-123; LYS-253; 262-ARG-ARG-263; GLU-267 AND
RP 272-LYS-LYS-273.
RX PubMed=25210186; DOI=10.1128/jvi.02538-14;
RA Radko S., Koleva M., James K.M., Jung R., Mymryk J.S., Pelka P.;
RT "Adenovirus E1A targets the DREF nuclear factor to regulate virus gene
RT expression, DNA replication, and growth.";
RL J. Virol. 88:13469-13481(2014).
RN [19]
RP INTERACTION WITH HUMAN TMEM173, FUNCTION, AND MUTAGENESIS OF
RP 122-LEU--GLU-126.
RX PubMed=26405230; DOI=10.1126/science.aab3291;
RA Lau L., Gray E.E., Brunette R.L., Stetson D.B.;
RT "DNA tumor virus oncogenes antagonize the cGAS-STING DNA-sensing pathway.";
RL Science 350:568-571(2015).
RN [20]
RP SUBCELLULAR LOCATION, AND NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=25194920; DOI=10.1016/j.virol.2014.08.014;
RA Cohen M.J., King C.R., Dikeakos J.D., Mymryk J.S.;
RT "Functional analysis of the C-terminal region of human adenovirus E1A
RT reveals a misidentified nuclear localization signal.";
RL Virology 468:238-243(2014).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 40-49 IN COMPLEX WITH HUMAN RB1.
RX PubMed=17974914; DOI=10.1101/gad.1590607;
RA Liu X., Marmorstein R.;
RT "Structure of the retinoblastoma protein bound to adenovirus E1A reveals
RT the molecular basis for viral oncoprotein inactivation of a tumor
RT suppressor.";
RL Genes Dev. 21:2711-2716(2007).
CC -!- FUNCTION: Plays a role in viral genome replication by driving entry of
CC quiescent cells into the cell cycle. Stimulation of progression from G1
CC to S phase allows the virus to efficiently use the cellular DNA
CC replicating machinery to achieve viral genome replication. E1A protein
CC has both transforming and trans-activating activities. Induces the
CC disassembly of the E2F1 transcription factor from RB1 by direct
CC competition for the same binding site on RB1, with subsequent
CC transcriptional activation of E2F1-regulated S-phase genes and of the
CC E2 region of the adenoviral genome. Release of E2F1 leads to the ARF-
CC mediated inhibition of MDM2 and causes TP53/p53 to accumulate because
CC it is not targeted for degradation by MDM2-mediated ubiquitination
CC anymore. This increase in TP53, in turn, would arrest the cell
CC proliferation and direct its death but this effect is counteracted by
CC the viral protein E1B-55K. Inactivation of the ability of RB1 to arrest
CC the cell cycle is critical for cellular transformation, uncontrolled
CC cellular growth and proliferation induced by viral infection.
CC Interaction with RBX1 and CUL1 inhibits ubiquitination of the proteins
CC targeted by SCF(FBXW7) ubiquitin ligase complex, and may be linked to
CC unregulated host cell proliferation. The tumorigenesis-restraining
CC activity of E1A may be related to the disruption of the host CtBP-CtIP
CC complex through the CtBP binding motif. Interaction with host
CC TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic
CC DNA and promote the production of type I interferon (IFN-alpha and IFN-
CC beta) (PubMed:26405230). Promotes the sumoylation of host ZBED1/hDREF
CC with SUMO1 (PubMed:25210186). {ECO:0000269|PubMed:15806172,
CC ECO:0000269|PubMed:19679664, ECO:0000269|PubMed:20543865,
CC ECO:0000269|PubMed:25210186, ECO:0000269|PubMed:26405230,
CC ECO:0000269|PubMed:9685342, ECO:0000303|PubMed:12204530}.
CC -!- SUBUNIT: Interacts with host UBE2I; this interaction interferes with
CC polySUMOylation (Probable) (PubMed:8824223, PubMed:20543865). Interacts
CC with host RB1; this interaction induces the aberrant dissociation of
CC RB1-E2F1 complex thereby disrupting the activity of RB1 and activating
CC E2F1-regulated genes (PubMed:17974914). Interacts with host ATF7; the
CC interaction enhances ATF7-mediated viral transactivation activity which
CC requires the zinc binding domains of both proteins (By similarity).
CC Isoform early E1A 32 kDa protein and isoform early E1A 26 kDa protein
CC interact (via N-terminus) with CUL1 and E3 ubiquitin ligase RBX1; these
CC interactions inhibit RBX1-CUL1-dependent elongation reaction of
CC ubiquitin chains and attenuate ubiquitination of SCF(FBXW7) target
CC proteins (PubMed:19679664). Interacts (via PXLXP motif) with host
CC ZMYND11/BS69 (via MYND-type zinc finger); this interaction inhibits E1A
CC mediated transactivation (PubMed:11733528). Interacts with host EP300;
CC this interaction stimulates the acetylation of RB1 by recruiting EP300
CC and RB1 into a multimeric-protein complex (PubMed:11433299). Interacts
CC with host CTBP1 and CTBP2; this interaction seems to potentiate viral
CC replication (PubMed:23747199, PubMed:7479821). Interacts with host
CC DCAF7 (ref.16). Interacts with host DYRK1A (PubMed:23864635). Interacts
CC with host KPNA4; this interaction allows E1A import into the host
CC nucleus (PubMed:23864635). Interacts with host EP400; this interaction
CC stabilizes MYC (PubMed:18413597). Interacts with host TBP protein; this
CC interaction probably disrupts the TBP-TATA complex (PubMed:8146144).
CC Interacts (via LXCXE motif) with host TMEM173/STING; this interaction
CC impairs the ability of TMEM173/STING to sense cytosolic DNA and promote
CC the production of type I interferon (IFN-alpha and IFN-beta)
CC (PubMed:26405230). Interacts (via C-terminus) with host ZBED1/hDREF
CC (via C-terminus); the interaction is direct (PubMed:25210186).
CC {ECO:0000250|UniProtKB:P03254, ECO:0000269|PubMed:11433299,
CC ECO:0000269|PubMed:11733528, ECO:0000269|PubMed:17974914,
CC ECO:0000269|PubMed:18413597, ECO:0000269|PubMed:19679664,
CC ECO:0000269|PubMed:20543865, ECO:0000269|PubMed:23747199,
CC ECO:0000269|PubMed:23864635, ECO:0000269|PubMed:25210186,
CC ECO:0000269|PubMed:26405230, ECO:0000269|PubMed:7479821,
CC ECO:0000269|PubMed:8146144, ECO:0000269|PubMed:8824223, ECO:0000305}.
CC -!- INTERACTION:
CC P03255; O08769: Cdkn1b; Xeno; NbExp=2; IntAct=EBI-2603114, EBI-7796656;
CC P03255; P45481: Crebbp; Xeno; NbExp=2; IntAct=EBI-2603114, EBI-296306;
CC P03255; Q92793: CREBBP; Xeno; NbExp=3; IntAct=EBI-2603114, EBI-81215;
CC P03255; Q09472: EP300; Xeno; NbExp=3; IntAct=EBI-2603114, EBI-447295;
CC P03255; Q92831: KAT2B; Xeno; NbExp=3; IntAct=EBI-2603114, EBI-477430;
CC P03255; Q9H204: MED28; Xeno; NbExp=2; IntAct=EBI-2603114, EBI-514199;
CC P03255; P10826-2: RARB; Xeno; NbExp=2; IntAct=EBI-2603114, EBI-8583223;
CC P03255; P06400: RB1; Xeno; NbExp=10; IntAct=EBI-2603114, EBI-491274;
CC P03255; P28749: RBL1; Xeno; NbExp=3; IntAct=EBI-2603114, EBI-971402;
CC P03255; Q08999: RBL2; Xeno; NbExp=2; IntAct=EBI-2603114, EBI-971439;
CC P03255; Q86WV6: STING1; Xeno; NbExp=2; IntAct=EBI-2603114, EBI-2800345;
CC P03255; P21675: TAF1; Xeno; NbExp=3; IntAct=EBI-2603114, EBI-491289;
CC P03255; P47825: Taf4; Xeno; NbExp=3; IntAct=EBI-2603114, EBI-277958;
CC P03255; Q15326: ZMYND11; Xeno; NbExp=3; IntAct=EBI-2603114, EBI-2623509;
CC P03255-1; P17980: PSMC3; Xeno; NbExp=2; IntAct=EBI-6692439, EBI-359720;
CC P03255-1; P62195: PSMC5; Xeno; NbExp=2; IntAct=EBI-6692439, EBI-357745;
CC P03255-1; P06400: RB1; Xeno; NbExp=2; IntAct=EBI-6692439, EBI-491274;
CC P03255-1; P42224: STAT1; Xeno; NbExp=2; IntAct=EBI-6692439, EBI-1057697;
CC P03255-2; Q09472: EP300; Xeno; NbExp=3; IntAct=EBI-6859460, EBI-447295;
CC P03255-2; Q92831: KAT2B; Xeno; NbExp=3; IntAct=EBI-6859460, EBI-477430;
CC P03255-2; O15151: MDM4; Xeno; NbExp=3; IntAct=EBI-6859460, EBI-398437;
CC P03255-2; P06400: RB1; Xeno; NbExp=3; IntAct=EBI-6859460, EBI-491274;
CC P03255-2; P42224: STAT1; Xeno; NbExp=2; IntAct=EBI-6859460, EBI-1057697;
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:25194920,
CC ECO:0000269|PubMed:25210186}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Isoforms are derived from the E1 region of the genome.;
CC Name=early E1A 32 kDa protein; Synonyms=289R, L-E1A;
CC IsoId=P03255-1; Sequence=Displayed;
CC Name=early E1A 26 kDa protein; Synonyms=243R, S-E1A;
CC IsoId=P03255-2; Sequence=VSP_000198;
CC Name=early E1A 6 kDa protein;
CC IsoId=P03255-3; Sequence=VSP_028918, VSP_028919;
CC -!- SIMILARITY: Belongs to the adenoviridae E1A protein family.
CC {ECO:0000305}.
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DR EMBL; M73260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X02996; CAB40663.1; -; Genomic_DNA.
DR EMBL; X02996; CAB40664.1; -; Genomic_DNA.
DR EMBL; X02996; CAB40665.1; -; Genomic_DNA.
DR PIR; A03825; ERAD65.
DR PIR; C03824; Q2AD5.
DR RefSeq; AP_000197.1; AC_000008.1. [P03255-1]
DR PDB; 2KJE; NMR; -; B=53-91.
DR PDB; 2R7G; X-ray; 1.67 A; B/D/E=40-49.
DR PDB; 6H6D; X-ray; 2.40 A; C/F=234-243.
DR PDB; 6H6H; X-ray; 2.40 A; C/F=234-243.
DR PDBsum; 2KJE; -.
DR PDBsum; 2R7G; -.
DR PDBsum; 6H6D; -.
DR PDBsum; 6H6H; -.
DR BMRB; P03255; -.
DR SMR; P03255; -.
DR DIP; DIP-40736N; -.
DR ELM; P03255; -.
DR IntAct; P03255; 38.
DR MINT; P03255; -.
DR iPTMnet; P03255; -.
DR EvolutionaryTrace; P03255; -.
DR Proteomes; UP000004992; Genome.
DR GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:CAFA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0039645; P:modulation by virus of host G1/S transition checkpoint; IEA:UniProtKB-KW.
DR GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-KW.
DR GO; GO:0039649; P:modulation by virus of host ubiquitin-protein ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:BHF-UCL.
DR GO; GO:0033235; P:positive regulation of protein sumoylation; IDA:UniProtKB.
DR GO; GO:0046719; P:regulation by virus of viral protein levels in host cell; IDA:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR GO; GO:0039563; P:suppression by virus of host JAK-STAT cascade via inhibition of STAT1 activity; IEA:UniProtKB-KW.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR DisProt; DP01150; -.
DR IDEAL; IID90003; -.
DR InterPro; IPR014410; Aden_E1A.
DR Pfam; PF02703; Adeno_E1A; 1.
DR PIRSF; PIRSF003669; Aden_E1A; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Early protein;
KW Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host transcription shutoff by virus;
KW G1/S host cell cycle checkpoint dysregulation by virus;
KW Host gene expression shutoff by virus; Host nucleus;
KW Host-virus interaction;
KW Inhibition of eukaryotic host transcription initiation by virus;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Inhibition of host STAT1 by virus; Metal-binding;
KW Modulation of host cell cycle by virus;
KW Modulation of host E3 ubiquitin ligases by virus;
KW Modulation of host ubiquitin pathway by virus; Oncogene; Phosphoprotein;
KW Transcription; Transcription regulation; Viral immunoevasion; Zinc;
KW Zinc-finger.
FT CHAIN 1..289
FT /note="Early E1A protein"
FT /id="PRO_0000221694"
FT ZN_FING 154..174
FT /evidence="ECO:0000269|PubMed:1835093,
FT ECO:0000269|PubMed:8146144"
FT REGION 41..49
FT /note="Interaction with RB1 in competition with E2F1"
FT /evidence="ECO:0000305"
FT REGION 76..140
FT /note="Interaction with UBE2I"
FT REGION 82..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 113..117
FT /note="PXLXP motif, interaction with host ZMYND11"
FT MOTIF 122..126
FT /note="LXCXE motif, interaction with host RB1 and
FT TMEM173/STING"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:26405230"
FT MOTIF 258..289
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:25194920"
FT MOTIF 279..283
FT /note="PXDLS motif, CTBP-binding"
FT /evidence="ECO:0000269|PubMed:7479821"
FT COMPBIAS 220..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 89
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:2966155"
FT MOD_RES 219
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:2966155"
FT MOD_RES 231
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:2966155"
FT VAR_SEQ 29..55
FT /note="ADNLPPPSHFEPPTLHELYDLDVTAPE -> CLNLSLSPSQNRSLQDLPAVL
FT KWRLLS (in isoform early E1A 6 kDa protein)"
FT /evidence="ECO:0000305"
FT /id="VSP_028918"
FT VAR_SEQ 56..289
FT /note="Missing (in isoform early E1A 6 kDa protein)"
FT /evidence="ECO:0000305"
FT /id="VSP_028919"
FT VAR_SEQ 140..185
FT /note="Missing (in isoform early E1A 26 kDa protein)"
FT /evidence="ECO:0000305"
FT /id="VSP_000198"
FT MUTAGEN 115
FT /note="L->A: Complete loss of interaction with host
FT ZMYND11."
FT /evidence="ECO:0000269|PubMed:11733528"
FT MUTAGEN 122..126
FT /note="LTCHE->VTSHD: Abolishes interaction with host
FT TMEM173/STING."
FT /evidence="ECO:0000269|PubMed:26405230"
FT MUTAGEN 122
FT /note="L->I: Abolishes binding to UBE2I."
FT /evidence="ECO:0000269|PubMed:8824223"
FT MUTAGEN 123
FT /note="T->H: Abolishes increased sumoylation of human
FT ZBED1."
FT /evidence="ECO:0000269|PubMed:25210186"
FT MUTAGEN 154
FT /note="C->S: Loss of transactivation."
FT /evidence="ECO:0000269|PubMed:1835093"
FT MUTAGEN 157
FT /note="C->S: Loss of transactivation."
FT /evidence="ECO:0000269|PubMed:1835093"
FT MUTAGEN 171
FT /note="C->S: Loss of transactivation."
FT /evidence="ECO:0000269|PubMed:1835093"
FT MUTAGEN 174
FT /note="C->S: Loss of transactivation."
FT /evidence="ECO:0000269|PubMed:1835093"
FT MUTAGEN 253
FT /note="K->E: Reduces interaction with human ZBED1."
FT /evidence="ECO:0000269|PubMed:25210186"
FT MUTAGEN 262..263
FT /note="RR->EE: Reduces interaction with human ZBED1."
FT /evidence="ECO:0000269|PubMed:25210186"
FT MUTAGEN 267
FT /note="E->K: Reduces interaction with human ZBED1."
FT /evidence="ECO:0000269|PubMed:25210186"
FT MUTAGEN 272..273
FT /note="LL->AA: Abolishes interaction with human ZBED1.
FT Abolishes E1A-mediated increased sumoylation of ZBED1.
FT Abolishes localization of ZBED1 to peripheral areas of PML
FT bodies."
FT /evidence="ECO:0000269|PubMed:25210186"
FT MUTAGEN 281..282
FT /note="DL->AS: 30% decrease in virus replication
FT efficiency. Enhanced immortalization and Ras cooperative
FT transformation."
FT /evidence="ECO:0000269|PubMed:23747199"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:2R7G"
FT HELIX 59..63
FT /evidence="ECO:0007829|PDB:2KJE"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:2KJE"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:2KJE"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:2KJE"
SQ SEQUENCE 289 AA; 31851 MW; 8C5997A3908C40D7 CRC64;
MRHIICHGGV ITEEMAASLL DQLIEEVLAD NLPPPSHFEP PTLHELYDLD VTAPEDPNEE
AVSQIFPDSV MLAVQEGIDL LTFPPAPGSP EPPHLSRQPE QPEQRALGPV SMPNLVPEVI
DLTCHEAGFP PSDDEDEEGE EFVLDYVEHP GHGCRSCHYH RRNTGDPDIM CSLCYMRTCG
MFVYSPVSEP EPEPEPEPEP ARPTRRPKMA PAILRRPTSP VSRECNSSTD SCDSGPSNTP
PEIHPVVPLC PIKPVAVRVG GRRQAVECIE DLLNEPGQPL DLSCKRPRP
