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IID90003
UniprotP03255
ProteinEarly E1A protein
GeneE1A_ADE05
OrganismHuman adenovirus C serotype 5
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
289
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seqdisorder 1-139
 Evidence NMR Reference
       Region 1-139 disorder
       Region 53-91 disorder
Seq 40-49 Hetero pentamer : IID00017Complex
 Evidence X-RAY 2r7g E Reference
       Region 2r7g E 40-48 order
       Region 2r7g E 49-49 disorder
 Evidence X-RAY 2r7g D Reference
       Region 2r7g D 40-49 order
 Evidence X-RAY 2r7g B Reference
       Region 2r7g B 40-49 order
Seq 53-91 Hetero dimer : IID00092Complex
 Evidence NMR 2kje B Reference
       Region 2kje B 53-80 order
       Region 2kje B 81-91 disorder
       Region 2kje B 85-91 high_rmsd
SeqProS verified 40-49 Hetero pentamer : IID00017Complex
       Region 2r7g B 40-49 order
       Region 2r7g D 40-49 order
       Region 2r7g E 40-48 order
       Region 1-139 disorder
SeqProS verified 53-80 Hetero dimer : IID00092Complex
       Region 2kje B 53-80 order
       Region 53-91 disorder
Seqphosphorylation
    89-89 Phosphoserine; by host
    219-219 Phosphoserine; by host
    231-231 Phosphoserine; by host
 
Prediction
NeProc
Disorder 76-142,165-168,189-245,281-289
Order 1-75,143-164,169-188,246-280
ProS 76-79,103-129,165-168,205-211,222-225,240-245,281-286
AlphaFold
Disorder 1-10,28-38,50-53,55-55,79-118,127-142,181-187,195-195,197-197,199-266,272-289
Order 11-27,39-49,54-54,56-78,119-126,143-180,188-194,196-196,198-198,267-271
Pfam Hmmer
PF02703 1-289 8.4e-202
SEG 133-141 ,189-200 ,255-266
Function
Function in SwissProt
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. E1A protein has both transforming and trans-activating activities. Induces the disassembly of the E2F1 transcription factor from RB1 by direct competition for the same binding site on RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes and of the E2 region of the adenoviral genome. Release of E2F1 leads to the ARF-mediated inhibition of MDM2 and causes TP53/p53 to accumulate because it is not targeted for degradation by MDM2-mediated ubiquitination anymore. This increase in TP53, in turn, would arrest the cell proliferation and direct its death but this effect is counteracted by the viral protein E1B-55K. Inactivation of the ability of RB1 to arrest the cell cycle is critical for cellular transformation, uncontrolled cellular growth and proliferation induced by viral infection. Interaction with RBX1 and CUL1 inhibits ubiquitination of the proteins targeted by SCF(FBXW7) ubiquitin ligase complex, and may be linked to unregulated host cell proliferation. The tumorigenesis-restraining activity of E1A may be related to the disruption of the host CtBP-CtIP complex through the CtBP binding motif. 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) (PubMed:26405230). Promotes the sumoylation of host ZBED1/hDREF with SUMO1 (PubMed:25210186).
Biological Process
Diagram with PDB data
E1A_ADE05/RB1Structure of the retinoblastoma protein pocket domain in complex with adenovirus E1A CR1 domain
E1A_ADE05/CREBBPNMR structure of CBP TAZ2 and adenoviral E1A complex