ID A0A0U2QTG8_HPV16 Unreviewed; 158 AA. AC A0A0U2QTG8; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 20-JUN-2018, entry version 13. DE RecName: Full=Protein E6 {ECO:0000256|HAMAP-Rule:MF_04006, ECO:0000256|RuleBase:RU363123, ECO:0000256|SAAS:SAAS01013181}; 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 Firstpapillomavirinae; 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:SAAS01013177}. 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:SAAS01013174}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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 {ECO:0000256|HAMAP-Rule:MF_04006, KW ECO:0000256|RuleBase:RU363123, ECO:0000256|SAAS:SAAS01013178}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_04006, KW ECO:0000256|RuleBase:RU363123, ECO:0000256|SAAS:SAAS01013184}; 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:SAAS01013183}; KW Host nucleus {ECO:0000256|HAMAP-Rule:MF_04006, KW ECO:0000256|RuleBase:RU363123, ECO:0000256|SAAS:SAAS01013175}; KW Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04006, KW ECO:0000256|SAAS:SAAS01013182}; KW Inhibition of host innate immune response by virus {ECO:0000256|HAMAP- KW Rule:MF_04006, ECO:0000256|SAAS:SAAS01013176}; 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:SAAS01013173}; KW Modulation of host cell apoptosis by virus {ECO:0000256|HAMAP- KW Rule:MF_04006, ECO:0000256|SAAS:SAAS01013180}; KW Transcription {ECO:0000256|HAMAP-Rule:MF_04006, KW ECO:0000256|RuleBase:RU363123, ECO:0000256|SAAS:SAAS01013169}; KW Transcription regulation {ECO:0000256|HAMAP-Rule:MF_04006, KW ECO:0000256|RuleBase:RU363123, ECO:0000256|SAAS:SAAS01013179}; 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:SAAS01013172}; KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_04006, KW ECO:0000256|RuleBase:RU363123, ECO:0000256|SAAS:SAAS01013170}. 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 //