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IID90014
UniprotP26554
ProteinProtein E6
GeneE6
OrganismHuman papillomavirus type 51
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
151
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 80-151 Monomer :
 Evidence NMR 2m3l A Reference
       Region 2m3l A 80-151 order
       Region 2m3l A 145-151 high_rmsd
Seqdisorder 141-151
 Evidence NMR Reference
       Region 141-151 disorder
Seq 142-151 Hetero dimer : IID00513Complex
 Evidence NMR 2m3m B Reference
       Region 2m3m B 142-151 order
SeqProS verified 141-151 Hetero dimer : IID00513Complex
       Region 2m3m B 142-151 order
       Region 141-151 disorder
 
Prediction
NeProc
Disorder 1-5,147-151
Order 6-146
ProS 147-151
AlphaFold
Disorder 142-151
Order 1-141
Pfam Hmmer
PF00518 30-139 1.3e-64
Function
Function in SwissProt
Plays a major role in the induction and maintenance of cellular transformation. Acts mainly as an oncoprotein by stimulating the destruction of many host cell key regulatory proteins. E6 associates with host UBE3A/E6-AP ubiquitin-protein ligase, and inactivates tumor suppressors TP53 and TP73 by targeting them to the 26S proteasome for degradation. In turn, DNA damage and chromosomal instabilities increase and lead to cell proliferation and cancer development. The complex E6/E6AP targets several other substrates to degradation via the proteasome including host DLG1 or NFX1, a repressor of human telomerase reverse transcriptase (hTERT). The resulting increased expression of hTERT prevents the shortening of telomere length leading to cell immortalization. Other cellular targets including BAK1, Fas-associated death domain-containing protein (FADD) and procaspase 8, are degraded by E6/E6AP causing inhibition of apoptosis. E6 also inhibits immune response by interacting with host IRF3 and TYK2. These interactions prevent IRF3 transcriptional activities and inhibit TYK2-mediated JAK-STAT activation by interferon alpha resulting in inhibition of the interferon signaling pathway.