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. Also plays 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). 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). Predominantly found in the host nucleus. 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. Highly phosphorylated. Belongs to the papillomaviridae E7 protein family.