ID   VE6_HPV21               Reviewed;         168 AA.
AC   P28832;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   23-FEB-2022, entry version 85.
DE   RecName: Full=Protein E6 {ECO:0000255|HAMAP-Rule:MF_04006};
GN   Name=E6 {ECO:0000255|HAMAP-Rule:MF_04006};
OS   Human papillomavirus 21.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Betapapillomavirus.
OX   NCBI_TaxID=31548;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1310189; DOI=10.1016/0042-6822(92)90029-o;
RA   Kiyono T., Hiraiwa A., Ishibashi M.;
RT   "Differences in transforming activity and coded amino acid sequence among
RT   E6 genes of several papillomaviruses associated with epidermodysplasia
RT   verruciformis.";
RL   Virology 186:628-639(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Delius H.;
RL   Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
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; D90263; BAA14310.1; -; Genomic_DNA.
DR   EMBL; U31779; AAA79394.1; -; Genomic_DNA.
DR   SMR; P28832; -.
DR   Proteomes; UP000009165; 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;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Viral immunoevasion; Zinc; Zinc-finger.
FT   CHAIN           1..168
FT                   /note="Protein E6"
FT                   /id="PRO_0000133341"
FT   ZN_FING         55..91
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04006"
FT   ZN_FING         128..164
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04006"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..25
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        130
FT                   /note="T -> N (in Ref. 2; AAA79394)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        148
FT                   /note="H -> F (in Ref. 2; AAA79394)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        156
FT                   /note="T -> S (in Ref. 2; AAA79394)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   168 AA;  19290 MW;  744E8AF8F0ACE53C CRC64;
     MADSSTDSAD EGPSPKRRHL EEENTSSFLE PPLPATIRDL ANLLEIPLDD CLVPCNFCGN
     FLTHLEVCEF DEKKLSLLWK DHCVFACCRV CCAATATYEY NEFYESTVVG RDIEEITGKS
     IFDIDVRCYT CMKFLDSIEK LDICGRKHFF HKVRGTWKGI CRLCKHFQ