VE2_HPV08
ID VE2_HPV08 Reviewed; 498 AA.
AC P06422;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 121.
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 8.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Betapapillomavirus.
OX NCBI_TaxID=10579;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3009874; DOI=10.1128/jvi.58.2.626-634.1986;
RA Fuchs P.G., Iftner T., Weninger J., Pfister H.;
RT "Epidermodysplasia verruciformis-associated human papillomavirus 8: genomic
RT sequence and comparative analysis.";
RL J. Virol. 58:626-634(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 P06422; P49715: CEBPA; Xeno; NbExp=4; IntAct=EBI-7136851, EBI-1172054;
CC P06422; P17676: CEBPB; Xeno; NbExp=4; IntAct=EBI-7136851, EBI-969696;
CC P06422; Q09472: EP300; Xeno; NbExp=7; IntAct=EBI-7136851, EBI-447295;
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; M12737; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A03666; W2WL8.
DR SMR; P06422; -.
DR IntAct; P06422; 78.
DR MINT; P06422; -.
DR PRIDE; P06422; -.
DR Proteomes; UP000009103; 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 Activator; DNA replication; DNA-binding; Early protein; Host nucleus;
KW Phosphoprotein; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..498
FT /note="Regulatory protein E2"
FT /id="PRO_0000133187"
FT REGION 1..201
FT /note="Transactivation domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04001"
FT REGION 196..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..498
FT /note="DNA-binding domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04001"
FT COMPBIAS 196..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..277
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..330
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 498 AA; 56329 MW; CC8003CE4DA69C48 CRC64;
MENLSERFNV LQDQLMNIYE AAEQTLEAQI AHWLLLRKEA VLLYFARQKG ITRIGYQPVP
PLAVSEAKAK QAIGIMLQLQ SLQKSEFADE PWTLVDTSIE TYKNAPENHF KKGATPVEVI
YDKQPDNANV YTMWKHIYYT DADDKWHKTT SGVNQTGIYY MQGSFRHYYV VFADDARRYS
ATGEWEVKIN KDTVFAPVTS STPPGSPPGQ ADTDTAAKTP TTSADSTSRQ QRSPAKQPQQ
TETKGRRYGR RPSSRTRPQK EQRRSRSRHR TRSRSRSLSR VRAVGSTTVS RSRSSSLTKA
VRPRSRSRSR GRATATSRRR AGRGSPRRRR STSRSPSTNT FKRSQRGGGR RGRGRGSRGR
RERSSSTSPT PTKRSRGESS RLRGVSPSEV GRSVQSVSAK HTGRLGRLLD EAIDPPVILV
RGEANTLKCF RNRARVRYRG LFKYFSTTWS WVAGDSTERL GRSRMLILFT SAGQRKDFDE
TVKYPKGVDT SYGNLDSL
