VE2_HPV6A
ID VE2_HPV6A Reviewed; 368 AA.
AC Q84294;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 02-JUN-2021, entry version 118.
DE RecName: Full=Regulatory protein E2 {ECO:0000255|HAMAP-Rule:MF_04001};
GN Name=E2 {ECO:0000255|HAMAP-Rule:MF_04001};
OS Human papillomavirus type 6a.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Alphapapillomavirus.
OX NCBI_TaxID=37122;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7778283; DOI=10.1006/viro.1995.1283;
RA Hofmann K.J., Cook J.C., Joyce J.G., Brown D.R., Schultz L.D., George H.A.,
RA Rosolowsky M., Fife K.H., Jansen K.U.;
RT "Sequence determination of human papillomavirus type 6a and assembly of
RT virus-like particles in Saccharomyces cerevisiae.";
RL Virology 209:506-518(1995).
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; L41216; AAA74214.1; -; Genomic_DNA.
DR PDB; 1R8H; X-ray; 1.90 A; A/B/C/D/E/F=282-368.
DR PDB; 2AYB; X-ray; 3.20 A; A/B=282-368.
DR PDB; 2AYE; X-ray; 2.30 A; A/B/C/D/E/F=282-368.
DR PDB; 2AYG; X-ray; 3.10 A; A/B=282-368.
DR PDBsum; 1R8H; -.
DR PDBsum; 2AYB; -.
DR PDBsum; 2AYE; -.
DR PDBsum; 2AYG; -.
DR SMR; Q84294; -.
DR EvolutionaryTrace; Q84294; -.
DR Proteomes; UP000007675; 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 1: Evidence at protein level;
KW 3D-structure; Activator; DNA replication; DNA-binding; Early protein;
KW Host nucleus; Phosphoprotein; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..368
FT /note="Regulatory protein E2"
FT /id="PRO_0000133184"
FT REGION 1..200
FT /note="Transactivation domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04001"
FT REGION 205..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..368
FT /note="DNA-binding domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04001"
FT COMPBIAS 205..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 284..292
FT /evidence="ECO:0007829|PDB:1R8H"
FT HELIX 294..307
FT /evidence="ECO:0007829|PDB:1R8H"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:1R8H"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:2AYE"
FT STRAND 331..336
FT /evidence="ECO:0007829|PDB:1R8H"
FT HELIX 340..349
FT /evidence="ECO:0007829|PDB:1R8H"
FT STRAND 357..364
FT /evidence="ECO:0007829|PDB:1R8H"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:1R8H"
SQ SEQUENCE 368 AA; 42124 MW; 857628CED4B8BD1A CRC64;
MEAIAKRLDA CQEQLLELYE ENSTDLNKHV LHWKCMRHES VLLYKAKQMG LSHIGMQVVP
PLKVSEAKGH NAIEMQMHLE SLLKTEYSME PWTLQETSYE MWQTPPKRCF KKRGKTVEVK
FDGCANNTMD YVVWTDVYVQ DTDSWVKVHS MVDAKGIYYT CGQFKTYYVN FVKEAEKYGS
TKQWEVCYGS TVICSPASVS STTQEVSIPE STTYTPAQTS TPVSSSTQED AVQTPPRKRA
RGVQQSPCNA LCVAHIGPVD SGNHNLITNN HDQHQRRNNS NSSATPIVQF QGESNCLKCF
RYRLNDKHRH LFDLISSTWH WASPKAPHKH AIVTVTYHSE EQRQQFLNVV KIPPTIRHKL
GFMSLHLL
