VE6_HPV29
ID VE6_HPV29 Reviewed; 148 AA.
AC P50803;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Protein E6 {ECO:0000255|HAMAP-Rule:MF_04006};
GN Name=E6 {ECO:0000255|HAMAP-Rule:MF_04006};
OS Human papillomavirus 29.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Alphapapillomavirus.
OX NCBI_TaxID=37112;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
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. 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}.
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 -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04006}.
CC Host nucleus {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; U31784; AAA79429.1; -; Genomic_DNA.
DR SMR; P50803; -.
DR PRIDE; P50803; -.
DR Proteomes; UP000009115; 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..148
FT /note="Protein E6"
FT /id="PRO_0000133349"
FT ZN_FING 29..65
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04006"
FT ZN_FING 102..138
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04006"
SQ SEQUENCE 148 AA; 17409 MW; C38395A6C39C200B CRC64;
MSRGDGYPKN IFLLCRDSGV PFEDLRLQCV FCTKELTSPE LAAFCIRELN VVWKSGAPYG
ACARCLLFEG IKRRLKYWQY SCFVEGVEAE TNESIYTQLI RCYMCHKPLV REEKDKHRNE
KRRLHKISGY WRGSCLYCWS RCMGQSPR