VE6_HPV11
ID VE6_HPV11 Reviewed; 150 AA.
AC P04019;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-1986, sequence version 1.
DT 07-APR-2021, entry version 101.
DE RecName: Full=Protein E6 {ECO:0000255|HAMAP-Rule:MF_04006};
GN Name=E6 {ECO:0000255|HAMAP-Rule:MF_04006};
OS Human papillomavirus 11.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Alphapapillomavirus.
OX NCBI_TaxID=10580;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3008427; DOI=10.1016/0042-6822(86)90110-8;
RA Dartmann K., Schwarz E., Gissmann L., zur Hausen H.;
RT "The nucleotide sequence and genome organization of human papilloma virus
RT type 11.";
RL Virology 151:124-130(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8956761; DOI=10.1001/archotol.1996.01890240110025;
RA Fife K.H., Fan L., Fritsch M.H., Bryan J., Brown D.R.;
RT "Association of human papillomavirus type 11 DNA with squamous cell
RT carcinoma of the tongue.";
RL Arch. Otolaryngol. Head Neck Surg. 122:1404-1408(1996).
RN [3]
RP FUNCTION, AND INTERACTION WITH HOST EP300 AND TP53.
RX PubMed=15664194; DOI=10.1016/j.molcel.2004.12.016;
RA Thomas M.C., Chiang C.M.;
RT "E6 oncoprotein represses p53-dependent gene activation via inhibition of
RT protein acetylation independently of inducing p53 degradation.";
RL Mol. Cell 17:251-264(2005).
RN [4]
RP INTERACTION WITH HOST UBE3A/E6-AP, AND FUNCTION.
RX PubMed=17023019; DOI=10.1016/j.virol.2006.08.038;
RA Brimer N., Lyons C., Vande Pol S.B.;
RT "Association of E6AP (UBE3A) with human papillomavirus type 11 E6
RT protein.";
RL Virology 358:303-310(2007).
RN [5]
RP FUNCTION.
RX PubMed=26743580; DOI=10.1099/jgv.0.000392;
RA Underbrink M.P., Dupuis C., Wang J., Tyring S.K.;
RT "E6 proteins from low-risk human papillomavirus types 6 and 11 are able to
RT protect keratinocytes from apoptosis via Bak degradation.";
RL J. Gen. Virol. 97:715-724(2016).
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. Sequesters tumor suppressor
CC TP53 in the host cytoplasm and modulates its activity by interacting
CC with host EP300 that results in the reduction of TP53 acetylation and
CC activation. In turn, apoptosis induced by DNA damage is inhibited. E6
CC protects also host keratinocytes from apoptosis by mediating the
CC degradation of host BAK1. May also inhibit host immune response.
CC {ECO:0000255|HAMAP-Rule:MF_04006, ECO:0000269|PubMed:15664194,
CC ECO:0000269|PubMed:17023019, ECO:0000269|PubMed:26743580}.
CC -!- SUBUNIT: Forms homodimers. Interacts with ubiquitin-protein ligase
CC UBE3A/E6-AP; this interaction stimulates UBE3A ubiquitin activity.
CC Interacts with host TP53 and EP300; this interaction inhibits TP53
CC activity. {ECO:0000255|HAMAP-Rule:MF_04006,
CC ECO:0000269|PubMed:15664194, ECO:0000269|PubMed:17023019}.
CC -!- INTERACTION:
CC P04019; Q05086: UBE3A; Xeno; NbExp=5; IntAct=EBI-1177232, EBI-954357;
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250|UniProtKB:P03126,
CC ECO:0000255|HAMAP-Rule:MF_04006}. Host nucleus
CC {ECO:0000250|UniProtKB:P03126, ECO:0000255|HAMAP-Rule:MF_04006}.
CC -!- MISCELLANEOUS: Belongs to the low risk human alphapapillomavirus
CC family. The cancer-causing human papillomavirus E6 protein has a unique
CC carboxy terminal PDZ domain containing substrate but low risk E6s do
CC not possess this domain. {ECO:0000255|HAMAP-Rule:MF_04006}.
CC -!- SIMILARITY: Belongs to the papillomaviridae E6 protein family.
CC {ECO:0000305}.
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DR EMBL; M14119; AAA46927.1; -; Genomic_DNA.
DR EMBL; L36108; AAA21703.1; -; Genomic_DNA.
DR PIR; A03684; W6WL11.
DR SMR; P04019; -.
DR IntAct; P04019; 9.
DR MINT; P04019; -.
DR PRIDE; P04019; -.
DR Proteomes; UP000008222; 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 1: Evidence at protein level;
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..150
FT /note="Protein E6"
FT /id="PRO_0000133331"
FT ZN_FING 31..67
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04006"
FT ZN_FING 104..140
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04006"
SQ SEQUENCE 150 AA; 17406 MW; A685DC7DCA090CCA CRC64;
MESKDASTSA TSIDQLCKTF NLSLHTLQIQ CVFCRNALTT AEIYAYAYKN LKVVWRDNFP
FAACACCLEL QGKINQYRHF NYAAYAPTVE EETNEDILKV LIRCYLCHKP LCEIEKLKHI
LGKARFIKLN NQWKGRCLHC WTTCMEDLLP
