VE6_HPV20
ID VE6_HPV20 Reviewed; 165 AA.
AC P28831;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 23-FEB-2022, entry version 79.
DE RecName: Full=Protein E6 {ECO:0000255|HAMAP-Rule:MF_04006};
GN Name=E6 {ECO:0000255|HAMAP-Rule:MF_04006};
OS Human papillomavirus 20.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Betapapillomavirus.
OX NCBI_TaxID=31547;
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; D90261; BAA14308.1; -; Genomic_DNA.
DR EMBL; U31778; AAA79387.1; -; Genomic_DNA.
DR SMR; P28831; -.
DR Proteomes; UP000008230; 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..165
FT /note="Protein E6"
FT /id="PRO_0000133340"
FT ZN_FING 52..88
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04006"
FT ZN_FING 125..161
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04006"
FT CONFLICT 23
FT /note="F -> P (in Ref. 2; AAA79387)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="H -> D (in Ref. 2; AAA79387)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 165 AA; 18670 MW; 79E37EED96883DE3 CRC64;
MATPPSSEDS ADEGPSNIGE AKFPILEPPL PATICGLAKL LEIPLDDCLI PCNFCGNFLT
HLEVCEFDEK KLTLIWKDHL VFACCRVCCS ATATYEFNQF YESTVLGRDI EQVTGKSVFD
IHVRCYTCMK FLDSIEKLDI CGRKRPFYLV RGSWKGICRL CKHFQ
