Structure
atLeast majority ProS Experiment
:order disorder conflict PDB cluster ProS Pfam Domain SEG
437
order/disorder by at least rule
disorder by at least rule
order/disorder by majority rule
Seq 410-427 Hetero trimer : IID00017 Complex
Region 1n4m E 410-421 order
Region 1n4m E 422-427 disorder
Region 1n4m D 410-427 order
Seq 410-427 Hetero dimer : IID00017 Complex
Region 1n4m C 410-427 order
Seq ProS possible 410-427
Hetero trimer : IID00017 Complex
Region 1n4m D 410-427 order
Region 1n4m E 410-421 order
Seq ProS possible 410-427
Hetero dimer : IID00017 Complex
Region 1n4m C 410-427 order
Prediction
ProS 12-28,43-48,60-74,82-94,370-400
Disorder 1-127,194-204,306-398,400-400,403-416,418-418,423-423,425-437
Order 128-193,205-305,399-399,401-402,417-417,419-422,424-424
SEG 39-59
,205-217
,309-330
,343-370
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. E2F2 binds specifically to RB1 in a cell-cycle dependent manner.
Biological Process
Diagram with PDB data
E2F2/RB1 Structure of Rb tumor suppressor bound to the transactivation domain of E2F-2
See also
Diagram with PDB data
LT_SV40/RB1 RETINOBLASTOMA POCKET COMPLEXED WITH SV40 LARGE T ANTIGEN
E1A_ADE05/RB1 Structure of the retinoblastoma protein pocket domain in complex with adenovirus E1A CR1 domain
RB1/E2F1/TFDP1 Structure of the Rb C-terminal domain bound to an E2F1-DP1 heterodimer
RB1/PPP1CA Crystal structure of an Rb C-terminal peptide bound to the catalytic subunit of PP1