ID   VE2_HPV37               Reviewed;         454 AA.
AC   Q80903;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Regulatory protein E2 {ECO:0000255|HAMAP-Rule:MF_04001};
GN   Name=E2 {ECO:0000255|HAMAP-Rule:MF_04001};
OS   Human papillomavirus 37.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Betapapillomavirus.
OX   NCBI_TaxID=37958;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Delius H.;
RL   Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a role in the initiation of viral DNA replication. A
CC       dimer of E2 interacts with a dimer of E1 in order to improve
CC       specificity of E1 DNA binding activity. Once the complex recognizes and
CC       binds DNA at specific sites, the E2 dimer is removed from DNA. E2 also
CC       regulates viral transcription through binding to the E2RE response
CC       element (5'-ACCNNNNNNGGT-3') present in multiple copies in the
CC       regulatory regions of the viral genome. Activates or represses
CC       transcription depending on E2RE's position with regards to proximal
CC       promoter elements including the TATA-box. Repression occurs by
CC       sterically hindering the assembly of the transcription initiation
CC       complex. {ECO:0000255|HAMAP-Rule:MF_04001}.
CC   -!- SUBUNIT: Binds DNA as homodimer. Interacts with protein E1; this
CC       interaction greatly increases E1 DNA-binding activity. Interacts with
CC       protein L1; this interaction enhances E2-dependent replication and
CC       transcription activation. Interacts with protein L2; this interaction
CC       inhibits E2 transcriptional activity but not DNA replication function
CC       E2. Interacts with protein E7; this interaction inhibits E7 oncogenic
CC       activity. Interacts with host TAF1; this interaction modulates E2-
CC       dependent transcriptional regulation. Interacts with host BRD4; this
CC       interaction mediates E2 transcriptional activation function.
CC       Additionally, the interaction with host BRD4 on mitotic chromosomes
CC       mediates tethering of the viral genome. Interacts with host TOPBP1;
CC       this interaction is required for optimal viral DNA replication.
CC       {ECO:0000255|HAMAP-Rule:MF_04001}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04001}.
CC   -!- PTM: Phosphorylated. {ECO:0000255|HAMAP-Rule:MF_04001}.
CC   -!- SIMILARITY: Belongs to the papillomaviridae E2 protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04001}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U31786; AAA79446.1; -; Genomic_DNA.
DR   SMR; Q80903; -.
DR   PRIDE; Q80903; -.
DR   Proteomes; UP000009119; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-UniRule.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.287.30; -; 1.
DR   Gene3D; 2.170.200.10; -; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   HAMAP; MF_04001; PPV_E2; 1.
DR   InterPro; IPR035975; E2/EBNA1_C_sf.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR000427; Papillomavirus_E2_C.
DR   InterPro; IPR001866; Papillomavirus_E2_N.
DR   InterPro; IPR033668; Reg_prot_E2.
DR   InterPro; IPR036050; Regulatory_protein_E2_N.
DR   InterPro; IPR042503; Regulatory_protein_E2_N_1.
DR   InterPro; IPR042504; Regulatory_protein_E2_N_2.
DR   Pfam; PF00511; PPV_E2_C; 1.
DR   Pfam; PF00508; PPV_E2_N; 1.
DR   SUPFAM; SSF51332; SSF51332; 1.
DR   SUPFAM; SSF54957; SSF54957; 1.
PE   3: Inferred from homology;
KW   Activator; DNA replication; DNA-binding; Early protein; Host nucleus;
KW   Phosphoprotein; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..454
FT                   /note="Regulatory protein E2"
FT                   /id="PRO_0000133217"
FT   REGION          1..201
FT                   /note="Transactivation domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04001"
FT   REGION          197..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          370..454
FT                   /note="DNA-binding domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04001"
FT   COMPBIAS        221..236
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..259
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..311
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   454 AA;  51285 MW;  ACA45808A7EA17AA CRC64;
     MDTLSDRFNA LQENLMDIYE SGRDDLETQI MHWQLLRQEQ ILFHYARKNG VMRLGYQPVP
     PLATSEAKAK DAIGMVILLE SLQQSAYGKE SWTLTQTSLE TVRSPPANCF KKGPQNIEVM
     FDNDPENLMV YTAWSFIYYQ TVDDTWNKVE GHVDYYGAYY FEGDLKVYYI QFEGDAARFS
     KTGRWEVHVN KDTIFAPVTS SSPAAGEGTD GAASVHTVSG SPLARGFSTT SVSTRKRTPP
     RRYRRKASSP TTTAARQKRQ GEDTATRRSR STSRGKQATS RGGDRRRRRR ERSYSRDTSS
     SPDRGRGGRS RGGPETRSQS RSLSRSRSRS RSRGSSSRGG VAPDAVGKSV RTVGRDHSGR
     LKRLLDEARD PPVIVLRGDA NKLKCYRYRA KKKHGNLVKY YSTTWSWVGG STNDRIGRSR
     MLLAFQSNTE RELFLKTMKL PPGVDWSLGH LDEL