ID   VE2_HPV42               Reviewed;         398 AA.
AC   P27223;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Regulatory protein E2 {ECO:0000255|HAMAP-Rule:MF_04001};
GN   Name=E2 {ECO:0000255|HAMAP-Rule:MF_04001};
OS   Human papillomavirus 42.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Alphapapillomavirus.
OX   NCBI_TaxID=10590;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1309278; DOI=10.1016/0042-6822(92)90091-3;
RA   Philipp W., Honore N., Sapp M., Cole S.T., Streeck R.E.;
RT   "Human papillomavirus type 42: new sequences, conserved genome
RT   organization.";
RL   Virology 186:331-334(1992).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAA47044.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M73236; AAA47044.1; ALT_INIT; Genomic_DNA.
DR   PIR; B39451; W2WL42.
DR   SMR; P27223; -.
DR   Proteomes; UP000009122; 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..398
FT                   /note="Regulatory protein E2"
FT                   /id="PRO_0000133222"
FT   REGION          1..201
FT                   /note="Transactivation domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04001"
FT   REGION          256..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          311..398
FT                   /note="DNA-binding domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04001"
FT   COMPBIAS        258..280
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   398 AA;  45309 MW;  4D41D7196372808C CRC64;
     MERLAKRLDA CQEQLLELYE ENSRDLQKHI EHWKCLRMEA VVLYKAREMG FANIGHQIVP
     TLETCRAKAH MAIEIHLALE TLLQSSYGKE PWTLQETSNE LWLTNPKKCF KKQGRTVEVI
     FDGKQDNAMH YTAWTYIYIQ TVQGTWCKVQ GHVCHAGLYY IVENMKQFYC NFKEEAKKYG
     VTDQWEVHDG NQVIVSPAPI SSTTSTDAEI PSTGSTKLVQ QVCTTNPLHT TTSIDNHHAD
     CTDGTAYNVP IQTSPPRKRY RQCGQSPSQH LQHSNPSIPS IPSASVDPGL CGVRTNSENC
     NKRRNHCGSQ ATPVIHLQGD PNCLKCLRFR LKRNCSHLFT QVSSTWHLTE NDCTRDTKTG
     IITIHYYDEA QRNLFLNTVK IPSGIKSCIG YMSMLQFI