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IID00174
 UniprotQ15797
ProteinMothers against decapentaplegic homolog 1
GeneSMAD1
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
465
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 201-209 Hetero dimer : IID00304Complex
 Evidence NMR 2lay B Reference
       Region 2lay B 201-209 order
 Evidence NMR 2lax B Reference
       Region 2lax B 201-209 order
Seq 208-217 Hetero dimer : IID00328Complex
 Evidence NMR 2lb0 B Reference
       Region 2lb0 B 208-217 order
 Evidence NMR 2laz B Reference
       Region 2laz B 210-217 order
Seqdisorder 217-267
 Evidence X-RAY Reference
       Region 217-267 disorder
Seq 220-233 Hetero dimer : IID00328Complex
 Evidence NMR 2lb1 B Reference
       Region 2lb1 B 220-220 disorder
       Region 2lb1 B 221-233 order
Seq 222-233 Hetero dimer : IID00304Complex
 Evidence NMR 2law B Reference
       Region 2law B 222-233 order
Seq 248-465 Homo trimer :
 Evidence X-RAY 1khu D Reference
       Region 1khu D 248-269 disorder
       Region 1khu D 270-453 order
       Region 1khu D 454-465 disorder
 Evidence X-RAY 1khu C Reference
       Region 1khu C 248-268 disorder
       Region 1khu C 269-465 order
 Evidence X-RAY 1khu B Reference
       Region 1khu B 248-268 disorder
       Region 1khu B 269-465 order
 Evidence X-RAY 1khu A Reference
       Region 1khu A 248-267 disorder
       Region 1khu A 268-465 order
Seq 456-465 Hetero dimer : Q9WUD1
 Evidence X-RAY 3q4a C Reference
       Region 3q4a C 456-459 disorder
       Region 3q4a C 460-465 order
 Evidence X-RAY 3q47 C Reference
       Region 3q47 C 456-458 disorder
       Region 3q47 C 459-464 order
SeqProS possible 201-209 The S214 only (2lay) orT202 and S206 (2lax) were phosphorylated. This linker region is disordered in the smad3. (PubMed=12154125) Hetero dimer : IID00304Complex
       Region 2lax B 201-209 order
       Region 2lay B 201-209 order
SeqProS possible 208-217 The S214 only (2laz) or S210 and S214 (2lb0) were phosphorylated. This linker region is disordered in the smad3. (PubMed=12154125) Hetero dimer : IID00328Complex
       Region 2lb0 B 208-217 order
       Region 2laz B 210-217 order
SeqProS verified 221-233 Hetero dimer : IID00328Complex
       Region 2lb1 B 221-233 order
       Region 217-267 disorder
SeqProS verified 222-233 Hetero dimer : IID00304Complex
       Region 2law B 222-233 order
       Region 217-267 disorder
SeqProS verified 454-465 While the C-terminal tail is disordered in the unphosphorylated form, but ordered in the phosphorylated form. This tail interactions make the heterotrimer formation. Homo trimer :
       Region 1khu A 268-465 order
       Region 1khu B 269-465 order
       Region 1khu C 269-465 order
       Region 1khu D 454-465 disorder
Seqphosphorylation
    322-322 Phosphothreonine; by MINK1
    463-463 Phosphoserine
    465-465 Phosphoserine
Seqacetylation
    1-1 N-acetylmethionine
 
Prediction
NeProc
Disorder 1-6,134-261,457-465
Order 7-133,262-456
ProS 134-212,224-242,251-261,457-465
AlphaFold
Disorder 1-9,143-165,178-258
Order 10-142,166-177,259-465
Pfam Hmmer
PF03165 27-131 1.6e-65
PF03166 265-443 3.7e-121
SEG 30-55 ,133-141 ,179-210 ,219-233
Function
Function in SwissProt
Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD1 is a receptor-regulated SMAD (R-SMAD). SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1. May act synergistically with SMAD4 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression.
Biological Process
Diagram with PDB data
SMAD1/YAP1Structure of the first WW domain of human YAP in complex with a phosphorylated human Smad1 derived peptide
SMAD1/STUB1Crystal structure of the TPR domain of CHIP complexed with phosphorylated Smad1 peptide