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Regulatory protein E2

 VE2_HPV16               Reviewed;         365 AA.
P03120; Q71BI4;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
23-MAY-2018, entry version 147.
RecName: Full=Regulatory protein E2 {ECO:0000255|HAMAP-Rule:MF_04001};
Name=E2 {ECO:0000255|HAMAP-Rule:MF_04001};
Human papillomavirus type 16.
Viruses; dsDNA viruses, no RNA stage; Papillomaviridae;
Alphapapillomavirus.
NCBI_TaxID=333760;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2990099; DOI=10.1016/0042-6822(85)90214-4;
Seedorf K., Krammer G., Durst M., Suhai S., Rowekamp W.G.;
"Human papillomavirus type 16 DNA sequence.";
Virology 145:181-185(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Isolate European German 131;
Terai M., Fu L., Ma Z., Burk R.D.;
"Cloning and sequencing of non-European human papillomavirus (HPV)
variant complete genomes from cervicovaginal cells by an overlapping
PCR method.";
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION.
PubMed=3033289;
Phelps W.C., Howley P.M.;
"Transcriptional trans-activation by the human papillomavirus type 16
E2 gene product.";
J. Virol. 61:1630-1638(1987).
[4]
FUNCTION.
PubMed=1326651;
Del Vecchio A.M., Romanczuk H., Howley P.M., Baker C.C.;
"Transient replication of human papillomavirus DNAs.";
J. Virol. 66:5949-5958(1992).
[5]
PHOSPHORYLATION, SUBCELLULAR LOCATION, AND DIMERIZATION.
PubMed=7645246; DOI=10.1006/viro.1995.1424;
Sanders C.M., Stern P.L., Maitland N.J.;
"Characterization of human papillomavirus type 16 E2 protein and
subdomains expressed in insect cells.";
Virology 211:418-433(1995).
[6]
FUNCTION, AND INTERACTION WITH L2.
PubMed=15681049; DOI=10.1016/j.virusres.2004.07.004;
Okoye A., Cordano P., Taylor E.R., Morgan I.M., Everett R.,
Campo M.S.;
"Human papillomavirus 16 L2 inhibits the transcriptional activation
function, but not the DNA replication function, of HPV-16 E2.";
Virus Res. 108:1-14(2005).
[7]
INTERACTION WITH E7.
PubMed=16439535; DOI=10.1128/JVI.80.4.1787-1797.2006;
Gammoh N., Grm H.S., Massimi P., Banks L.;
"Regulation of human papillomavirus type 16 E7 activity through direct
protein interaction with the E2 transcriptional activator.";
J. Virol. 80:1787-1797(2006).
[8]
FUNCTION, AND INTERACTION WITH HOST BRD4.
PubMed=16611886; DOI=10.1128/JVI.80.9.4276-4285.2006;
Schweiger M.R., You J., Howley P.M.;
"Bromodomain protein 4 mediates the papillomavirus E2 transcriptional
activation function.";
J. Virol. 80:4276-4285(2006).
[9]
INTERACTION WITH HOST TAF1.
PubMed=18580066; DOI=10.1159/000141706;
Centeno F., Ramirez-Salazar E., Garcia-Villa E., Gariglio P.,
Garrido E.;
"TAF1 interacts with and modulates human papillomavirus 16 E2-
dependent transcriptional regulation.";
Intervirology 51:137-143(2008).
[10]
SUMOYLATION, MUTAGENESIS OF LYS-292, AND SUBCELLULAR LOCATION.
PubMed=18619639; DOI=10.1016/j.virol.2008.06.008;
Wu Y.C., Roark A.A., Bian X.L., Wilson V.G.;
"Modification of papillomavirus E2 proteins by the small ubiquitin-
like modifier family members (SUMOs).";
Virology 378:329-338(2008).
[11]
PHOSPHORYLATION.
PubMed=19781729; DOI=10.1016/j.virol.2009.08.046;
Johansson C., Graham S.V., Dornan E.S., Morgan I.M.;
"The human papillomavirus 16 E2 protein is stabilised in S phase.";
Virology 394:194-199(2009).
[12]
INTERACTION WITH HOST TOPBP1.
PubMed=22973044; DOI=10.1128/JVI.01002-12;
Donaldson M.M., Mackintosh L.J., Bodily J.M., Dornan E.S.,
Laimins L.A., Morgan I.M.;
"An interaction between human papillomavirus 16 E2 and TopBP1 is
required for optimum viral DNA replication and episomal genome
establishment.";
J. Virol. 86:12806-12815(2012).
[13]
PHOSPHORYLATION AT SER-243, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=25340539; DOI=10.1371/journal.pone.0110882;
Chang S.W., Liu W.C., Liao K.Y., Tsao Y.P., Hsu P.H., Chen S.L.;
"Phosphorylation of HPV-16 E2 at serine 243 enables binding to Brd4
and mitotic chromosomes.";
PLoS ONE 9:E110882-E110882(2014).
[14]
INTERACTION WITH PROTEIN L1, AND SUBCELLULAR LOCATION.
PubMed=25911730; DOI=10.1099/vir.0.000162;
Siddiqa A., Leon K.C., James C.D., Bhatti M.F., Roberts S.,
Parish J.L.;
"The human papillomavirus type 16 L1 protein directly interacts with
E2 and enhances E2-dependent replication and transcription
activation.";
J. Gen. Virol. 96:2274-2285(2015).
[15]
FUNCTION.
PubMed=26365679; DOI=10.1016/j.virusres.2015.09.008;
Gauson E.J., Wang X., Dornan E.S., Herzyk P., Bristol M., Morgan I.M.;
"Failure to interact with Brd4 alters the ability of HPV16 E2 to
regulate host genome expression and cellular movement.";
Virus Res. 211:1-8(2015).
[16]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-201, AND TRANSACTIVATION
DOMAIN.
PubMed=10089541; DOI=10.1107/S0907444998010889;
Burns J.E., Moroz O.V., Antson A.A., Sanders C.M., Wilson K.S.,
Maitland N.J.;
"Expression, crystallization and preliminary X-ray analysis of the E2
transactivation domain from papillomavirus type 16.";
Acta Crystallogr. D 54:1471-1474(1998).
[17]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 285-365, DIMERIZATION, AND
DNA-BINDING DOMAIN.
PubMed=9878365; DOI=10.1006/jmbi.1998.2260;
Hegde R.S., Androphy E.J.;
"Crystal structure of the E2 DNA-binding domain from human
papillomavirus type 16: implications for its DNA binding-site
selection mechanism.";
J. Mol. Biol. 284:1479-1489(1998).
[18]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-201.
PubMed=10693813; DOI=10.1038/35001638;
Antson A.A., Burns J.E., Moroz O.V., Scott D.J., Sanders C.M.,
Bronstein I.B., Dodson G.G., Wilson K.S., Maitland N.J.;
"Structure of the intact transactivation domain of the human
papillomavirus E2 protein.";
Nature 403:805-809(2000).
[19]
STRUCTURE BY NMR OF 286-365.
PubMed=15702528; DOI=10.1023/B:JNMR.0000048942.96866.76;
Nadra A.D., Eliseo T., Mok Y.K., Almeida C.L., Bycroft M., Paci M.,
de Prat-Gay G., Cicero D.O.;
"Solution structure of the HPV-16 E2 DNA binding domain, a
transcriptional regulator with a dimeric beta-barrel fold.";
J. Biomol. NMR 30:211-214(2004).
[20]
X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 1-201, AND INTERACTION WITH
HOST BRD4.
PubMed=17189190; DOI=10.1016/j.molcel.2006.11.002;
Abbate E.A., Voitenleitner C., Botchan M.R.;
"Structure of the papillomavirus DNA-tethering complex E2:Brd4 and a
peptide that ablates HPV chromosomal association.";
Mol. Cell 24:877-889(2006).
[21]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 285-365.
PubMed=17915949; DOI=10.1021/bi701104q;
Dellarole M., Sanchez I.E., Freire E., de Prat-Gay G.;
"Increased stability and DNA site discrimination of 'single chain'
variants of the dimeric beta-barrel DNA binding domain of the human
papillomavirus E2 transcriptional regulator.";
Biochemistry 46:12441-12450(2007).
[22]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 283-365.
PubMed=21482558; DOI=10.1096/fj.10-176461;
Bose K., Meinke G., Bohm A., Baleja J.D.;
"Design and characterization of an enhanced repressor of human
papillomavirus E2 protein.";
FASEB J. 25:2354-2361(2011).
-!- FUNCTION: Plays a role in the initiation of viral DNA replication.
A dimer of E2 interacts with a dimer of E1 in order to improve
specificity of E1 DNA binding activity. Once the complex
recognizes and binds DNA at specific sites, the E2 dimer is
removed from DNA. E2 also regulates viral transcription through
binding to the E2RE response element (5'-ACCNNNNNNGGT-3') present
in multiple copies in the regulatory regions of the viral genome.
Activates or represses transcription depending on E2RE's position
with regards to proximal promoter elements including the TATA-box.
Repression occurs by sterically hindering the assembly of the
transcription initiation complex. {ECO:0000255|HAMAP-
Rule:MF_04001, ECO:0000269|PubMed:1326651,
ECO:0000269|PubMed:15681049, ECO:0000269|PubMed:16611886,
ECO:0000269|PubMed:25340539, ECO:0000269|PubMed:26365679,
ECO:0000269|PubMed:3033289}.
-!- SUBUNIT: Binds DNA as homodimer. Interacts with protein E1; this
interaction greatly increases E1 DNA-binding activity. Interacts
with protein L1; this interaction enhances E2-dependent
replication and transcription activation. Interacts with protein
L2; this interaction inhibits E2 transcriptional activity but not
DNA replication function E2. Interacts with protein E7; this
interaction inhibits E7 oncogenic activity. Interacts with host
TAF1; this interaction modulates E2-dependent transcriptional
regulation. Interacts with host BRD4; this interaction mediates E2
transcriptional activation function. Additionally, the interaction
with host BRD4 on mitotic chromosomes mediates tethering of the
viral genome. Interacts with host TOPBP1; this interaction is
required for optimal viral DNA replication. {ECO:0000255|HAMAP-
Rule:MF_04001, ECO:0000269|PubMed:15681049,
ECO:0000269|PubMed:16439535, ECO:0000269|PubMed:16611886,
ECO:0000269|PubMed:17189190, ECO:0000269|PubMed:18580066,
ECO:0000269|PubMed:22973044, ECO:0000269|PubMed:25911730,
ECO:0000269|PubMed:7645246, ECO:0000269|PubMed:9878365}.
-!- INTERACTION:
O60885:BRD4 (xeno); NbExp=4; IntAct=EBI-1779322, EBI-723869;
O60885-1:BRD4 (xeno); NbExp=2; IntAct=EBI-1779322, EBI-9345088;
Q9H0C5:BTBD1 (xeno); NbExp=3; IntAct=EBI-1779322, EBI-935503;
P17676:CEBPB (xeno); NbExp=2; IntAct=EBI-1779322, EBI-969696;
P79101:CPSF3 (xeno); NbExp=2; IntAct=EBI-1779322, EBI-7894416;
O19137:CPSF4 (xeno); NbExp=3; IntAct=EBI-1779322, EBI-7894441;
P03114:E1; NbExp=3; IntAct=EBI-1779322, EBI-7387308;
P31274:HOXC9 (xeno); NbExp=3; IntAct=EBI-1779322, EBI-1779423;
P22736:NR4A1 (xeno); NbExp=3; IntAct=EBI-1779322, EBI-721550;
P03132:Rep68 (xeno); NbExp=2; IntAct=EBI-1779322, EBI-7387242;
Q92547:TOPBP1 (xeno); NbExp=2; IntAct=EBI-1779322, EBI-308302;
-!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-
Rule:MF_04001, ECO:0000269|PubMed:18619639,
ECO:0000269|PubMed:25340539, ECO:0000269|PubMed:25911730,
ECO:0000269|PubMed:7645246}.
-!- PTM: Phosphorylated. Phosphorylation at Ser-243 mediates binding
to host Brd4 and is required for host chromosome binding.
{ECO:0000255|HAMAP-Rule:MF_04001, ECO:0000269|PubMed:25340539,
ECO:0000269|PubMed:7645246}.
-!- PTM: Sumoylation plays a regulatory role in E2 transcriptional
activity. {ECO:0000255|HAMAP-Rule:MF_04001,
ECO:0000269|PubMed:18619639}.
-!- MISCELLANEOUS: HPV16, in comparison to HPV types 6 and 11, is more
often associated with malignant genital cancers in humans.
-!- SIMILARITY: Belongs to the papillomaviridae E2 protein family.
{ECO:0000255|HAMAP-Rule:MF_04001}.
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EMBL; K02718; AAA46941.1; -; Genomic_DNA.
EMBL; AF536179; AAQ10715.1; -; Genomic_DNA.
PIR; A03669; W2WLHS.
RefSeq; NP_041328.1; NC_001526.4.
PDB; 1BY9; X-ray; 2.20 A; A=285-365.
PDB; 1DTO; X-ray; 1.90 A; A=1-201.
PDB; 1R8P; NMR; -; A/B=286-365.
PDB; 1ZZF; NMR; -; A/B=286-365.
PDB; 2NNU; X-ray; 1.59 A; A=1-201.
PDB; 2Q79; X-ray; 1.80 A; A=285-365.
PDB; 3MI7; X-ray; 2.20 A; X=283-365.
PDBsum; 1BY9; -.
PDBsum; 1DTO; -.
PDBsum; 1R8P; -.
PDBsum; 1ZZF; -.
PDBsum; 2NNU; -.
PDBsum; 2Q79; -.
PDBsum; 3MI7; -.
ProteinModelPortal; P03120; -.
SMR; P03120; -.
BioGrid; 4263559; 1.
DIP; DIP-44574N; -.
IntAct; P03120; 64.
MINT; P03120; -.
BindingDB; P03120; -.
ChEMBL; CHEMBL4656; -.
iPTMnet; P03120; -.
PRIDE; P03120; -.
GeneID; 1489080; -.
KEGG; vg:1489080; -.
KO; K21811; -.
OrthoDB; VOG0900010D; -.
EvolutionaryTrace; P03120; -.
PRO; PR:P03120; -.
Proteomes; UP000009251; Genome.
Proteomes; UP000106302; Genome.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0044163; C:host cytoskeleton; IDA:CACAO.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003700; F:DNA binding transcription factor activity; IEA:InterPro.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0006275; P:regulation of DNA replication; IEA:InterPro.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0016032; P:viral process; IEA:InterPro.
Gene3D; 3.30.70.330; -; 1.
HAMAP; MF_04001; PPV_E2; 1.
InterPro; IPR035975; E2/EBNA1_C_sf.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR000427; Papillomavirus_E2_C.
InterPro; IPR001866; Papillomavirus_E2_N.
InterPro; IPR033668; Reg_prot_E2.
InterPro; IPR036050; Regulatory_protein_E2_N.
Pfam; PF00511; PPV_E2_C; 1.
Pfam; PF00508; PPV_E2_N; 1.
ProDom; PD000672; E2_early_recog_prot_C; 1.
SUPFAM; SSF51332; SSF51332; 1.
SUPFAM; SSF54957; SSF54957; 1.
1: Evidence at protein level;
3D-structure; Activator; Complete proteome; DNA replication;
DNA-binding; Early protein; Host nucleus; Isopeptide bond;
Phosphoprotein; Reference proteome; Repressor; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 365 Regulatory protein E2.
/FTId=PRO_0000133195.
REGION 1 200 Transactivation domain.
{ECO:0000255|HAMAP-Rule:MF_04001,
ECO:0000269|PubMed:10089541}.
REGION 285 365 DNA-binding domain. {ECO:0000255|HAMAP-
Rule:MF_04001,
ECO:0000269|PubMed:9878365}.
MOD_RES 243 243 Phosphoserine; by host.
{ECO:0000269|PubMed:25340539}.
CROSSLNK 292 292 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000255|HAMAP-Rule:MF_04001,
ECO:0000269|PubMed:18619639}.
MUTAGEN 292 292 K->R: Complete loss of sumoylation.
{ECO:0000269|PubMed:18619639}.
CONFLICT 77 77 L -> P (in Ref. 2; AAQ10715).
{ECO:0000305}.
CONFLICT 210 210 I -> T (in Ref. 2; AAQ10715).
{ECO:0000305}.
CONFLICT 219 219 P -> S (in Ref. 2; AAQ10715).
{ECO:0000305}.
CONFLICT 310 310 T -> K (in Ref. 2; AAQ10715).
{ECO:0000305}.
HELIX 1 21 {ECO:0000244|PDB:2NNU}.
HELIX 26 48 {ECO:0000244|PDB:2NNU}.
STRAND 52 54 {ECO:0000244|PDB:2NNU}.
HELIX 62 83 {ECO:0000244|PDB:2NNU}.
TURN 86 89 {ECO:0000244|PDB:2NNU}.
TURN 94 97 {ECO:0000244|PDB:2NNU}.
HELIX 99 103 {ECO:0000244|PDB:2NNU}.
STRAND 104 106 {ECO:0000244|PDB:2NNU}.
STRAND 110 121 {ECO:0000244|PDB:2NNU}.
STRAND 127 141 {ECO:0000244|PDB:2NNU}.
STRAND 144 148 {ECO:0000244|PDB:2NNU}.
STRAND 154 161 {ECO:0000244|PDB:2NNU}.
STRAND 164 170 {ECO:0000244|PDB:2NNU}.
HELIX 171 178 {ECO:0000244|PDB:2NNU}.
STRAND 180 182 {ECO:0000244|PDB:2NNU}.
STRAND 184 190 {ECO:0000244|PDB:2NNU}.
STRAND 286 293 {ECO:0000244|PDB:2Q79}.
HELIX 295 305 {ECO:0000244|PDB:2Q79}.
HELIX 306 311 {ECO:0000244|PDB:2Q79}.
STRAND 313 315 {ECO:0000244|PDB:2Q79}.
STRAND 331 336 {ECO:0000244|PDB:2Q79}.
HELIX 340 349 {ECO:0000244|PDB:2Q79}.
STRAND 356 363 {ECO:0000244|PDB:2Q79}.
SEQUENCE 365 AA; 41825 MW; 27581F82B246E112 CRC64;
METLCQRLNV CQDKILTHYE NDSTDLRDHI DYWKHMRLEC AIYYKAREMG FKHINHQVVP
TLAVSKNKAL QAIELQLTLE TIYNSQYSNE KWTLQDVSLE VYLTAPTGCI KKHGYTVEVQ
FDGDICNTMH YTNWTHIYIC EEASVTVVEG QVDYYGLYYV HEGIRTYFVQ FKDDAEKYSK
NKVWEVHAGG QVILCPTSVF SSNEVSSPEI IRQHLANHPA ATHTKAVALG TEETQTTIQR
PRSEPDTGNP CHTTKLLHRD SVDSAPILTA FNSSHKGRIN CNSNTTPIVH LKGDANTLKC
LRYRFKKHCT LYTAVSSTWH WTGHNVKHKS AIVTLTYDSE WQRDQFLSQV KIPKTITVST
GFMSI


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