ID C9WBC2_9PAPI Unreviewed; 158 AA.
AC C9WBC2;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Protein E6 {ECO:0000256|HAMAP-Rule:MF_04006, ECO:0000256|RuleBase:RU363123};
GN Name=E6 {ECO:0000256|HAMAP-Rule:MF_04006,
GN ECO:0000313|EMBL:ACQ90217.1};
OS Human papillomavirus.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae.
OX NCBI_TaxID=10566 {ECO:0000313|EMBL:ACQ90217.1};
RN [1] {ECO:0000313|EMBL:ACQ90217.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B00484 {ECO:0000313|EMBL:ACQ90217.1};
RA Yu N., Gu W.-W., Liu H.-E., Sun H.-Q., Chen X.-J.;
RT "Variance of E6/E7 Coding Sequence Derived from Human Papillomavirus Type
RT 16.";
RL Submitted (SEP-2008) 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:0000256|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:0000256|HAMAP-Rule:MF_04006}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04006,
CC ECO:0000256|RuleBase:RU363123}. Host nucleus {ECO:0000256|HAMAP-
CC Rule:MF_04006, ECO:0000256|RuleBase:RU363123}.
CC -!- SIMILARITY: Belongs to the papillomaviridae E6 protein family.
CC {ECO:0000256|ARBA:ARBA00006346, ECO:0000256|HAMAP-Rule:MF_04006,
CC ECO:0000256|RuleBase:RU363123}.
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DR EMBL; FJ237042; ACQ90217.1; -; Genomic_DNA.
DR SMR; C9WBC2; -.
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:0006351; P:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR GO; GO:0039648; P:modulation by symbiont of host protein ubiquitination; IEA:UniProtKB-UniRule.
DR GO; GO:0039526; P:perturbation by virus of host apoptosis; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProtKB-UniRule.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.240.40; E6 early regulatory protein; 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; E6 C-terminal domain-like; 2.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159, ECO:0000256|HAMAP-Rule:MF_04006};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_04006};
KW Early protein {ECO:0000256|ARBA:ARBA00022518, ECO:0000256|HAMAP-
KW Rule:MF_04006};
KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200, ECO:0000256|HAMAP-
KW Rule:MF_04006};
KW Host nucleus {ECO:0000256|HAMAP-Rule:MF_04006,
KW ECO:0000256|RuleBase:RU363123};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581, ECO:0000256|HAMAP-
KW Rule:MF_04006};
KW Inhibition of host innate immune response by virus
KW {ECO:0000256|ARBA:ARBA00022632, ECO:0000256|HAMAP-Rule:MF_04006};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_04006};
KW Modulation of host cell apoptosis by virus {ECO:0000256|ARBA:ARBA00023323,
KW ECO:0000256|HAMAP-Rule:MF_04006};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_04006};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW Rule:MF_04006};
KW Viral immunoevasion {ECO:0000256|ARBA:ARBA00023280, ECO:0000256|HAMAP-
KW Rule:MF_04006};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_04006};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|HAMAP-
KW Rule:MF_04006}.
FT ZN_FING 37..73
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04006"
FT ZN_FING 110..146
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04006"
FT MOTIF 156..158
FT /note="PDZ-binding domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04006"
SQ SEQUENCE 158 AA; 19201 MW; 004EF5ADCE6B375B CRC64;
MHQKRTAMFQ DPQERPRKLP QLCTELQTTI HEIILECVYC KQQLLRREVY DFAFRDLCIV
YRDGNPYAVC DKCLKFYSKI SEYRHYCYSL YGTTLEQQYN KPLCDLLIRC INCQKPLCPE
EKQRHLDKKQ RFHNIRGRWT GRCMSCCRSS RTRRETQL
//
