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IID00076
 UniprotQ14186
ProteinTranscription factor Dp-1
GeneTFDP1
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
 Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
410
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 199-350 Hetero trimer : IID00017Complex,IID00064Complex
 Evidence X-RAY 2aze A Reference
       Region 2aze A 199-346 order
       Region 2aze A 347-350 disorder
Seq 199-350 Hetero trimer : IID00130Complex,Q15329
 Evidence X-RAY 5tuv D Reference
       Region 5tuv D 199-207 disorder
       Region 5tuv D 208-245 order
       Region 5tuv D 246-249 disorder
       Region 5tuv D 250-306 order
       Region 5tuv D 307-350 disorder
 Evidence X-RAY 5tuv A Reference
       Region 5tuv A 199-247 order
       Region 5tuv A 248-248 disorder
       Region 5tuv A 249-305 order
       Region 5tuv A 306-350 disorder
Seq 199-350 Hetero dimer : Q16254
 Evidence X-RAY 5tuu A Reference
       Region 5tuu A 199-339 order
       Region 5tuu A 340-350 disorder
Seq 392-410 Hetero dimer : IID00549Complex
 Evidence NMR 5gow A Reference
       Region 5gow A 392-410 order
       Region 5gow A 410-410 high_rmsd
SeqProS predicted 392-410 The unbound state of this region is predicted to be disordered by DICHOT and MobiDB. Hetero dimer : IID00549Complex
       Region 5gow A 392-410 order
Seqphosphorylation
    23-23 Phosphoserine
Seqacetylation
    3-3 N6-acetyllysine
 
Prediction
NeProc
Disorder 9-12,24-112,156-158,342-410
Order 1-8,13-23,113-149,159-250,255-341
ProS 9-12,32-36,62-66,82-112,382-394,401-405
AlphaFold
Disorder 1-26,33-112,151-156,196-198,342-410
Order 27-32,113-150,157-195,199-341
Pfam Hmmer
PF02319 111-193 4.9e-43
SEG 103-115 ,181-192 ,216-231 ,395-410
Function
Function in SwissProt
Can stimulate E2F-dependent transcription. Binds DNA cooperatively with E2F family members 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 (PubMed:8405995, PubMed:7739537). The E2F1:DP complex appears to mediate both cell proliferation and apoptosis. Blocks adipocyte differentiation by repressing CEBPA binding to its target gene promoters (PubMed:20176812).
Biological Process
Diagram with PDB data
TFDP1/GTF2H1Solution structure of the complex between DP1 acidic region and TFIIH p62 PH domain
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
RBL1/E2F5/TFDP1Crystal structure of the E2F5-DP1-p107 ternary complex
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
HDAC1/RBL1p107 pocket domain complexed with HDAC1 peptide
E2F2/RB1Structure of Rb tumor suppressor bound to the transactivation domain of E2F-2