HAMAP rule MF_04004
General rule information
[?]
Accession | MF_04004 |
Dates | 18-DEC-2015 (Created)
28-JUL-2023 (Last updated, Version 11) |
Name | PPV_E7 |
Scope(s) |
Viruses Papillomaviridae |
Template(s) | P03129 (VE7_HPV16); [ Recover all ] |
Triggered by |
HAMAP; MF_04004 (Get profile general information and statistics) |
Propagated annotation
[?]
Identifier, protein and gene names
[?]
Identifier | VE7 |
Protein name | RecName: Full=Protein E7; |
Gene name | Name=E7; |
Comments
[?]
FUNCTION | Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E7 protein has both transforming and trans-activating activities. Induces the disassembly of the E2F1 transcription factor from RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes. Interferes with host histone deacetylation mediated by HDAC1 and HDAC2, leading to transcription activation. Plays also a role in the inhibition of both antiviral and antiproliferative functions of host interferon alpha. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta). |
SUBUNIT | Homodimer. Homooligomer. Interacts with host RB1; this interaction induces dissociation of RB1-E2F1 complex thereby disrupting RB1 activity. Interacts with host EP300; this interaction represses EP300 transcriptional activity. Interacts with protein E2; this interaction inhibits E7 oncogenic activity. Interacts with host TMEM173/STING; this interaction impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta). |
SUBCELLULAR LOCATION | Host cytoplasm. Host nucleus. Note=Predominantly found in the host nucleus. |
DOMAIN | The E7 terminal domain is an intrinsically disordered domain, whose flexibility and conformational transitions confer target adaptability to the oncoprotein. It allows adaptation to a variety of protein targets and exposes the PEST degradation sequence that regulates its turnover in the cell. |
PTM | Highly phosphorylated. |
SIMILARITY | Belongs to the papillomaviridae E7 protein family. |
Keywords
[?]
Gene Ontology
[?]
GO:0003677; Molecular function:DNA binding |
GO:0046872; Molecular function:metal ion binding |
GO:0019904; Molecular function:protein domain specific binding |
GO:0003700; Molecular function:DNA-binding transcription factor activity |
GO:0039645; Biological process:perturbation by virus of host G1/S transition checkpoint |
GO:0039502; Biological process:suppression by virus of host type I interferon-mediated signaling pathway |
GO:0006351; Biological process:DNA-templated transcription |
Cross-references
[?]
Pfam | PF00527; E7; 1; |
PIRSF | PIRSF003407; Papvi_E7; 1; |
Features
[?]
From: VE7_HPV16 (P03129) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
ZN_FING | 58 | 94 | ||||||||||
REGION | Nter | 40 | /note="E7 terminal domain" | C-x*-C-x-x-C | ||||||||
MOTIF | 22 | 26 | /note="LXCXE motif; interaction with host RB1 and TMEM173/STING" | L-x-C-x-E | ||||||||
MOTIF | 76 | 84 | /note="Nuclear export signal" |
Additional information
[?]
Size range | 86-127 amino acids |
Related rules |
None |
Fusion | Nter: None Cter: None |