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IID00064
 UniprotQ01094
ProteinTranscription factor E2F1
GeneE2F1
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
 Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
437
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 87-95 Hetero trimer : IID00032Complex
 Evidence X-RAY 1h24 E Reference
       Region 1h24 E 87-95 order
Seq 104-120 Hetero trimer : Q9BXT4
 Evidence X-RAY 5m9n C Reference
       Region 5m9n C 104-105 disorder
       Region 5m9n C 106-106 order
       Region 5m9n C 107-109 disorder
       Region 5m9n C 110-111 order
       Region 5m9n C 112-120 disorder
Seq 108-116 Hetero dimer : Q7KZF4
 Evidence X-RAY 5m9o B Reference
       Region 5m9o B 108-111 disorder
       Region 5m9o B 112-114 order
       Region 5m9o B 115-116 disorder
Seq 200-301 Hetero trimer : IID00017Complex,IID00076Complex
 Evidence X-RAY 2aze B Reference
       Region 2aze B 200-200 disorder
       Region 2aze B 201-301 order
Seq 409-426 Hetero trimer : IID00017Complex
 Evidence X-RAY 1o9k S Reference
       Region 1o9k S 409-426 order
 Evidence X-RAY 1o9k R Reference
       Region 1o9k R 409-426 order
 Evidence X-RAY 1o9k Q Reference
       Region 1o9k Q 409-426 order
 Evidence X-RAY 1o9k P Reference
       Region 1o9k P 409-426 order
SeqProS possible 87-95 Cyclin binding motif Hetero trimer : IID00032Complex
       Region 1h24 E 87-95 order
SeqProS possible 409-426 This region binds to Rb (IID00017). The binding region in Rb has another binding fragment from E1A (IID90003), which is a verfied ProS. Hetero trimer : IID00017Complex
       Region 1o9k P 409-426 order
       Region 1o9k Q 409-426 order
       Region 1o9k R 409-426 order
       Region 1o9k S 409-426 order
Seqphosphorylation
    364-364 Phosphoserine; by CHEK2
    375-375 Phosphoserine
    403-403 Phosphoserine; by GSK3-beta
    433-433 Phosphothreonine; by GSK3-beta
Seqacetylation
    117-117 N6-acetyllysine
    120-120 N6-acetyllysine
    125-125 N6-acetyllysine
 
Prediction
NeProc
Disorder 1-126,302-395
Order 127-301,396-437
ProS 32-35,61-69,86-96,387-395
AlphaFold
Disorder 1-126,147-147,192-200,301-415,417-417,419-437
Order 127-146,148-191,201-300,416-416,418-418
Pfam Hmmer
PF02319 127-192 2.6e-35
SEG 2-28 ,37-58 ,67-82 ,332-360
Function
Function in SwissProt
Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F1 binds preferentially RB1 in a cell-cycle dependent manner. It can mediate both cell proliferation and TP53/p53-dependent apoptosis. Blocks adipocyte differentiation by binding to specific promoters repressing CEBPA binding to its target gene promoters (PubMed:20176812). Positively regulates transcription of RRP1B (PubMed:20040599).
Biological Process
Diagram with PDB data
E2F1/CCNA2/CDK2CDK2/CyclinA in complex with a 9 residue recruitment peptide from E2F
E2F1/RB1Crystal structure of the retinoblastoma tumour suppressor protein bound to E2F peptide
See also
Diagram with PDB data
LT_SV40/RB1RETINOBLASTOMA POCKET COMPLEXED WITH SV40 LARGE T ANTIGEN
E1A_ADE05/RB1Structure of the retinoblastoma protein pocket domain in complex with adenovirus E1A CR1 domain
RB1/E2F1/TFDP1Structure of the Rb C-terminal domain bound to an E2F1-DP1 heterodimer
RB1/PPP1CACrystal structure of an Rb C-terminal peptide bound to the catalytic subunit of PP1
TFDP1/GTF2H1Solution structure of the complex between DP1 acidic region and TFIIH p62 PH domain