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IID00135
UniprotO15105
ProteinMothers against decapentaplegic homolog 7
GeneSMAD7
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
426
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 203-217 Hetero dimer : IID00223Complex
 Evidence NMR 2djy B Reference
       Region 2djy B 203-217 order
       Region 2djy B 203-203 high_rmsd
 Evidence NMR 2ltz B Reference
       Region 2ltz B 203-217 order
Seq 203-217 Hetero dimer : IID00223Complex
 Evidence NMR 2kxq B Reference
       Region 2kxq B 203-217 order
       Region 2kxq B 203-203 high_rmsd
Seq 203-217 Hetero dimer : IID00328Complex
 Evidence NMR 2ltx B Reference
       Region 2ltx B 203-217 order
Seq 203-217 Hetero dimer : IID00114Complex
 Evidence NMR 2lty B Reference
       Region 2lty B 203-217 order
Seq 205-217 Hetero dimer : IID00304Complex
 Evidence NMR 2ltw B Reference
       Region 2ltw B 205-217 order
Seq 206-217 Hetero dimer : IID00304Complex
 Evidence NMR 2ltv B Reference
       Region 2ltv B 206-217 order
       Region 2ltv B 217-217 high_rmsd
Seqphosphorylation
    249-249 Phosphoserine
Seqacetylation
    64-64 N6-acetyllysine; alternate
    70-70 N6-acetyllysine; alternate
 
Prediction
NeProc
Disorder 1-87,143-148,216-307
Order 88-142,154-215,308-426
ProS 1-27,33-39,79-87,216-306
AlphaFold
Disorder 1-2,20-87,132-152,205-258,350-355,379-390,425-426
Order 3-19,88-131,153-204,259-349,356-378,391-424
Pfam Hmmer
PF03165 89-202 5.8e-46
PF03166 255-426 1.5e-99
SEG 20-41 ,49-63 ,68-88 ,100-113 ,136-159
Function
Function in SwissProt
Antagonist of signaling by TGF-beta (transforming growth factor) type 1 receptor superfamily members; has been shown to inhibit TGF-beta (Transforming growth factor) and activin signaling by associating with their receptors thus preventing SMAD2 access. Functions as an adapter to recruit SMURF2 to the TGF-beta receptor complex. Also acts by recruiting the PPP1R15A-PP1 complex to TGFBR1, which promotes its dephosphorylation. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator.
Biological Process
Diagram with PDB data
SMAD7/SMURF2Solution structure of Smurf2 WW3 domain-Smad7 PY peptide complex