ID   VE6_HPV5B               Reviewed;         157 AA.
AC   P26556;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   29-SEP-2021, entry version 84.
DE   RecName: Full=Protein E6 {ECO:0000255|HAMAP-Rule:MF_04006};
GN   Name=E6 {ECO:0000255|HAMAP-Rule:MF_04006};
OS   Human papillomavirus type 5b.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Betapapillomavirus.
OX   NCBI_TaxID=10599;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1649510; DOI=10.1016/0042-6822(91)91013-7;
RA   Yabe Y., Sakai A., Hitsumoto T., Kato H., Ogura H.;
RT   "A subtype of human papillomavirus 5 (HPV-5b) and its subgenomic segment
RT   amplified in a carcinoma: nucleotide sequences and genomic organizations.";
RL   Virology 183:793-798(1991).
CC   -!- FUNCTION: Plays a major role in the induction and maintenance of
CC       cellular transformation. E6 associates with host UBE3A/E6-AP ubiquitin-
CC       protein ligase and modulates its activity. Protects host keratinocytes
CC       from apoptosis by mediating the degradation of host BAK1. May also
CC       inhibit host immune response. {ECO:0000255|HAMAP-Rule:MF_04006}.
CC   -!- SUBUNIT: Forms homodimers. Interacts with ubiquitin-protein ligase
CC       UBE3A/E6-AP; this interaction stimulates UBE3A ubiquitin activity.
CC       Interacts with host BAK1. {ECO:0000255|HAMAP-Rule:MF_04006}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04006}.
CC       Host nucleus {ECO:0000255|HAMAP-Rule:MF_04006}.
CC   -!- SIMILARITY: Belongs to the papillomaviridae E6 protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04006, ECO:0000305}.
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DR   EMBL; D90252; BAA14292.1; -; Genomic_DNA.
DR   PIR; E40480; W6WLB5.
DR   SMR; P26556; -.
DR   Proteomes; UP000007669; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0039526; P:modulation by virus of host apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0039649; P:modulation by virus of host ubiquitin-protein ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-UniRule.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.240.40; -; 2.
DR   HAMAP; MF_04006; HPV_E6; 1.
DR   InterPro; IPR001334; E6.
DR   InterPro; IPR038575; E6_sf.
DR   Pfam; PF00518; E6; 1.
DR   SUPFAM; SSF161229; SSF161229; 2.
PE   3: Inferred from homology;
KW   Activator; DNA-binding; Early protein; Host cytoplasm; Host nucleus;
KW   Host-virus interaction; Inhibition of host innate immune response by virus;
KW   Metal-binding; Modulation of host cell apoptosis by virus; Transcription;
KW   Transcription regulation; Viral immunoevasion; Zinc; Zinc-finger.
FT   CHAIN           1..157
FT                   /note="Protein E6"
FT                   /id="PRO_0000133324"
FT   ZN_FING         41..77
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04006"
FT   ZN_FING         114..150
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04006"
SQ   SEQUENCE   157 AA;  18087 MW;  20684B7EF730AA47 CRC64;
     MAEGAEHQQK LTEKDKAELP STIRDLAETL GIPLIDCIIP CNFCGKFLNY LEACEFDYKK
     LSLIWKDYCV FACCRVCCGA TATYEFNQFY EQTVLGRDIE LASGLSIFDI DIRCQTCLAF
     LDIIEKLDCC GRGLPFHKVR NAWKGICRQC KHFYHDW