VE2_HPV11
ID VE2_HPV11 Reviewed; 367 AA.
AC P04015;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-1986, sequence version 1.
DT 02-JUN-2021, entry version 138.
DE RecName: Full=Regulatory protein E2 {ECO:0000255|HAMAP-Rule:MF_04001};
GN Name=E2 {ECO:0000255|HAMAP-Rule:MF_04001};
OS Human papillomavirus 11.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Alphapapillomavirus.
OX NCBI_TaxID=10580;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3008427; DOI=10.1016/0042-6822(86)90110-8;
RA Dartmann K., Schwarz E., Gissmann L., zur Hausen H.;
RT "The nucleotide sequence and genome organization of human papilloma virus
RT type 11.";
RL Virology 151:124-130(1986).
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 -!- INTERACTION:
CC P04015; O60885: BRD4; Xeno; NbExp=3; IntAct=EBI-7010556, EBI-723869;
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}.
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DR EMBL; M14119; AAA46930.1; -; Genomic_DNA.
DR PIR; A03668; W2WL11.
DR PDB; 1R6K; X-ray; 2.50 A; A=2-201.
DR PDB; 1R6N; X-ray; 2.40 A; A=2-201.
DR PDBsum; 1R6K; -.
DR PDBsum; 1R6N; -.
DR SMR; P04015; -.
DR IntAct; P04015; 42.
DR MINT; P04015; -.
DR BindingDB; P04015; -.
DR ChEMBL; CHEMBL5830; -.
DR DrugBank; DB04330; Bilh 434.
DR DrugCentral; P04015; -.
DR EvolutionaryTrace; P04015; -.
DR Proteomes; UP000008222; 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; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Activator; DNA replication; DNA-binding; Early protein;
KW Host nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..367
FT /note="Regulatory protein E2"
FT /id="PRO_0000133190"
FT REGION 1..200
FT /note="Transactivation domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04001"
FT REGION 225..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..367
FT /note="DNA-binding domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04001"
FT HELIX 4..21
FT /evidence="ECO:0007829|PDB:1R6N"
FT HELIX 26..48
FT /evidence="ECO:0007829|PDB:1R6N"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:1R6K"
FT HELIX 62..83
FT /evidence="ECO:0007829|PDB:1R6N"
FT TURN 86..89
FT /evidence="ECO:0007829|PDB:1R6N"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:1R6N"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:1R6N"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:1R6N"
FT STRAND 109..121
FT /evidence="ECO:0007829|PDB:1R6N"
FT STRAND 128..141
FT /evidence="ECO:0007829|PDB:1R6N"
FT STRAND 144..152
FT /evidence="ECO:0007829|PDB:1R6N"
FT STRAND 154..161
FT /evidence="ECO:0007829|PDB:1R6N"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:1R6N"
FT HELIX 171..178
FT /evidence="ECO:0007829|PDB:1R6N"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:1R6N"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:1R6N"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:1R6N"
SQ SEQUENCE 367 AA; 41709 MW; F7BAF74D336804F0 CRC64;
MEAIAKRLDA CQDQLLELYE ENSIDIHKHI MHWKCIRLES VLLHKAKQMG LSHIGLQVVP
PLTVSETKGH NAIEMQMHLE SLAKTQYGVE PWTLQDTSYE MWLTPPKRCF KKQGNTVEVK
FDGCEDNVME YVVWTHIYLQ DNDSWVKVTS SVDAKGIYYT CGQFKTYYVN FNKEAQKYGS
TNHWEVCYGS TVICSPASVS STVREVSIAE PTTYTPAQTT APTVSACTTE DGVSAPPRKR
ARGPSTNNTL CVANIRSVDS TINNIVTDNY NKHQRRNNCH SAATPIVQLQ GDSNCLKCFR
YRLNDKYKHL FELASSTWHW ASPEAPHKNA IVTLTYSSEE QRQQFLNSVK IPPTIRHKVG
FMSLHLL
