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IID00206
UniprotQ01658
ProteinProtein Dr1
GeneDR1
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
176
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-176 Hetero trimer : IID00367Complex,IID00385Complex
 Evidence X-RAY 1jfi B Reference
       Region 1jfi B 1-8 disorder
       Region 1jfi B 9-143 order
       Region 1jfi B 144-176 disorder
SeqProS possible 80-143 The region of helix4 and 5 (80-143) is highly likely a random coil in the absence of TBP and DNA. Hetero trimer : IID00367Complex,IID00385Complex
       Region 1jfi B 9-143 order
Seqphosphorylation
    166-166 Phosphoserine
    167-167 Phosphoserine
    106-106 Phosphoserine
    105-105 Phosphoserine
Seqacetylation
    2-2 N-acetylalanine
 
Prediction
NeProc
Disorder 1-9,57-60,100-114,143-176
Order 10-56,61-99,115-142
ProS 57-60,103-114,143-144,172-176
AlphaFold
Disorder 1-9,161-176
Order 10-160
Pfam Hmmer
PF00808 11-75 8.1e-29
SEG 115-125 ,127-168
Function
Function in SwissProt
The association of the DR1/DRAP1 heterodimer with TBP results in a functional repression of both activated and basal transcription of class II genes. This interaction precludes the formation of a transcription-competent complex by inhibiting the association of TFIIA and/or TFIIB with TBP. Can bind to DNA on its own. Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4.