ID   A0A0U2QTG8_HPV16        Unreviewed;       158 AA.
AC   A0A0U2QTG8;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   31-JAN-2018, entry version 10.
DE   RecName: Full=Protein E6 {ECO:0000256|HAMAP-Rule:MF_04006, ECO:0000256|RuleBase:RU363123, ECO:0000256|SAAS:SAAS00967225};
GN   Name=E6 {ECO:0000256|HAMAP-Rule:MF_04006,
GN   ECO:0000313|EMBL:ALU65790.1};
OS   Human papillomavirus type 16.
OC   Viruses; dsDNA viruses, no RNA stage; Papillomaviridae;
OC   Alphapapillomavirus.
OX   NCBI_TaxID=333760 {ECO:0000313|EMBL:ALU65790.1};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1] {ECO:0000313|EMBL:ALU65790.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HPV16Hap78 {ECO:0000313|EMBL:ALU65790.1};
RX   PubMed=26694554;
RA   Vidal J.P., Felix S.P., Chaves C.B., Patury P., Franco V.F.,
RA   de Morais E.A., de Carvalho N.A., Carvalho A.C., Neto O.F.,
RA   Vieira L.M., Correa F.M., Martins L.F., Negrao A., de Almeida L.M.,
RA   Moreira M.A.;
RT   "Genetic diversity of HPV16 and HPV18 in Brazilian patients with
RT   invasive cervical cancer.";
RL   J. Med. Virol. 0:0-0(2015).
CC   -!- SUBUNIT: Forms homodimers. Interacts with ubiquitin-protein ligase
CC       UBE3A/E6-AP and thus forms a complex with human TP53. Interacts
CC       with human NFX1 and MAGI3. Interacts with human IRF3; this
CC       interaction inhibits the establishment of antiviral state.
CC       Interacts with human TYK2; this interaction inhibits JAK-STAT
CC       activation by interferon alpha. Interacts with host DLG1; this
CC       interaction leads to the proteasomal degradation of DLG1.
CC       {ECO:0000256|HAMAP-Rule:MF_04006}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm
CC       {ECO:0000256|RuleBase:RU363123}. Host nucleus
CC       {ECO:0000256|RuleBase:RU363123, ECO:0000256|SAAS:SAAS00967219}.
CC   -!- MISCELLANEOUS: Belongs to the high risk human alphapapillomavirus
CC       family. The cancer-causing human papillomavirus E6 protein has a
CC       unique carboxy terminal PDZ domain containing substrate.
CC       {ECO:0000256|HAMAP-Rule:MF_04006}.
CC   -!- SIMILARITY: Belongs to the papillomaviridae E6 protein family.
CC       {ECO:0000256|RuleBase:RU363123, ECO:0000256|SAAS:SAAS00967212}.
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DR   EMBL; KP965095; ALU65790.1; -; Genomic_DNA.
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:0030165; F:PDZ domain 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:0039548; P:suppression by virus of host IRF3 activity; 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   HAMAP; MF_04006; HPV_E6; 1.
DR   InterPro; IPR001334; E6.
DR   Pfam; PF00518; E6; 1.
PE   3: Inferred from homology;
KW   Activator {ECO:0000256|HAMAP-Rule:MF_04006,
KW   ECO:0000256|RuleBase:RU363123, ECO:0000256|SAAS:SAAS00967221};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_04006,
KW   ECO:0000256|RuleBase:RU363123, ECO:0000256|SAAS:SAAS00967216};
KW   Early protein {ECO:0000256|HAMAP-Rule:MF_04006,
KW   ECO:0000256|RuleBase:RU363123};
KW   Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04006,
KW   ECO:0000256|SAAS:SAAS00967220};
KW   Host nucleus {ECO:0000256|HAMAP-Rule:MF_04006,
KW   ECO:0000256|RuleBase:RU363123, ECO:0000256|SAAS:SAAS00967213};
KW   Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04006,
KW   ECO:0000256|SAAS:SAAS00967222};
KW   Inhibition of host innate immune response by virus {ECO:0000256|HAMAP-
KW   Rule:MF_04006, ECO:0000256|SAAS:SAAS00967214};
KW   Inhibition of host IRF3 by virus {ECO:0000256|HAMAP-Rule:MF_04006};
KW   Inhibition of host RLR pathway by virus {ECO:0000256|HAMAP-
KW   Rule:MF_04006};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_04006,
KW   ECO:0000256|RuleBase:RU363123, ECO:0000256|SAAS:SAAS00967227};
KW   Modulation of host cell apoptosis by virus {ECO:0000256|HAMAP-
KW   Rule:MF_04006, ECO:0000256|SAAS:SAAS00967217};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_04006,
KW   ECO:0000256|RuleBase:RU363123, ECO:0000256|SAAS:SAAS00967226};
KW   Transcription regulation {ECO:0000256|HAMAP-Rule:MF_04006,
KW   ECO:0000256|RuleBase:RU363123, ECO:0000256|SAAS:SAAS00967223};
KW   Viral immunoevasion {ECO:0000256|HAMAP-Rule:MF_04006};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_04006, ECO:0000256|RuleBase:RU363123,
KW   ECO:0000256|SAAS:SAAS00967218};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_04006,
KW   ECO:0000256|RuleBase:RU363123, ECO:0000256|SAAS:SAAS00967224}.
FT   ZN_FING      37     73       {ECO:0000256|HAMAP-Rule:MF_04006}.
FT   ZN_FING     110    146       {ECO:0000256|HAMAP-Rule:MF_04006}.
FT   MOTIF       156    158       PDZ-binding domain. {ECO:0000256|HAMAP-
FT                                Rule:MF_04006}.
SQ   SEQUENCE   158 AA;  19130 MW;  9F0CF5ADCD9977FE CRC64;
     MHQKRTAMFQ DPQERPRKLP QLCTELQTTI HDIILECVYC KQQLLRREVY DFAFRDLCIV
     YRDGNPYAVC DKCLKFYSKI SEYRHYCYSV YGTTLEQQYN KPLCDLLIRC INCQKPLCPE
     EKQRHLDKKQ RFHNIRGLWT GRCMSCCRSS RTRRETQL
//