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IID00132
UniprotQ13485
ProteinMothers against decapentaplegic homolog 4
GeneSMAD4
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
552
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 10-140 Homo dimer :
 Evidence X-RAY 5mf0 B Reference
       Region 5mf0 B 10-13 disorder
       Region 5mf0 B 14-138 order
       Region 5mf0 B 139-140 disorder
 Evidence X-RAY 5mf0 A Reference
       Region 5mf0 A 10-15 disorder
       Region 5mf0 A 16-138 order
       Region 5mf0 A 139-140 disorder
 Evidence X-RAY 5mez B Reference
       Region 5mez B 10-14 disorder
       Region 5mez B 15-136 order
       Region 5mez B 137-140 disorder
 Evidence X-RAY 5mez A Reference
       Region 5mez A 10-14 disorder
       Region 5mez A 15-139 order
       Region 5mez A 140-140 disorder
Seq 10-140 Monomer :
 Evidence X-RAY 5mey A Reference
       Region 5mey A 10-14 disorder
       Region 5mey A 15-138 order
       Region 5mey A 139-140 disorder
Seq 133-149 Hetero tetramer : IID50169Complex
 Evidence X-RAY 5uwu D Reference
       Region 5uwu D 133-140 disorder
       Region 5uwu D 141-149 order
Seq 285-552 Homo trimer :
 Evidence X-RAY 1ygs A Reference
       Region 1ygs A 319-456 order
       Region 1ygs A 457-491 disorder
       Region 1ygs A 492-543 order
       Region 1ygs A 544-552 disorder
 Evidence X-RAY 1g88 C Reference
       Region 1g88 C 285-294 order
       Region 1g88 C 295-311 disorder
       Region 1g88 C 312-465 order
       Region 1g88 C 466-478 disorder
       Region 1g88 C 479-550 order
       Region 1g88 C 551-552 disorder
 Evidence X-RAY 1g88 B Reference
       Region 1g88 B 285-296 order
       Region 1g88 B 297-308 disorder
       Region 1g88 B 309-466 order
       Region 1g88 B 467-478 disorder
       Region 1g88 B 479-550 order
       Region 1g88 B 551-552 disorder
 Evidence X-RAY 1g88 A Reference
       Region 1g88 A 285-296 order
       Region 1g88 A 297-310 disorder
       Region 1g88 A 311-460 order
       Region 1g88 A 461-486 disorder
       Region 1g88 A 487-545 order
       Region 1g88 A 546-552 disorder
 Evidence X-RAY 1dd1 C Reference
       Region 1dd1 C 285-294 order
       Region 1dd1 C 295-311 disorder
       Region 1dd1 C 312-468 order
       Region 1dd1 C 469-478 disorder
       Region 1dd1 C 479-552 order
 Evidence X-RAY 1dd1 B Reference
       Region 1dd1 B 285-296 order
       Region 1dd1 B 297-306 disorder
       Region 1dd1 B 307-469 order
       Region 1dd1 B 470-478 disorder
       Region 1dd1 B 479-552 order
 Evidence X-RAY 1dd1 A Reference
       Region 1dd1 A 285-296 order
       Region 1dd1 A 297-310 disorder
       Region 1dd1 A 311-460 order
       Region 1dd1 A 461-486 disorder
       Region 1dd1 A 487-545 order
       Region 1dd1 A 546-552 disorder
Seq 314-549 Hetero trimer : IID00127Complex
 Evidence X-RAY 1u7v B Reference
       Region 1u7v B 314-461 order
       Region 1u7v B 462-489 disorder
       Region 1u7v B 490-549 order
Seq 314-549 Hetero dimer : P12757
 Evidence X-RAY 5c4v E Reference
       Region 5c4v E 314-318 disorder
       Region 5c4v E 319-463 order
       Region 5c4v E 464-491 disorder
       Region 5c4v E 492-542 order
       Region 5c4v E 543-549 disorder
 Evidence X-RAY 5c4v C Reference
       Region 5c4v C 314-318 disorder
       Region 5c4v C 319-455 order
       Region 5c4v C 456-491 disorder
       Region 5c4v C 492-542 order
       Region 5c4v C 543-549 disorder
 Evidence X-RAY 5c4v A Reference
       Region 5c4v A 314-318 disorder
       Region 5c4v A 319-459 order
       Region 5c4v A 460-490 disorder
       Region 5c4v A 491-541 order
       Region 5c4v A 542-549 disorder
Seq 314-552 Hetero trimer : IID00113Complex
 Evidence X-RAY 1u7f B Reference
       Region 1u7f B 314-417 order
       Region 1u7f B 418-423 disorder
       Region 1u7f B 424-455 order
       Region 1u7f B 456-489 disorder
       Region 1u7f B 490-546 order
       Region 1u7f B 547-552 disorder
Seq 319-552 Hetero dimer : IID00131Complex
 Evidence X-RAY 1mr1 B Reference
       Region 1mr1 B 319-452 order
       Region 1mr1 B 453-491 disorder
       Region 1mr1 B 492-550 order
       Region 1mr1 B 551-552 disorder
 Evidence X-RAY 1mr1 A Reference
       Region 1mr1 A 319-461 order
       Region 1mr1 A 462-491 disorder
       Region 1mr1 A 492-543 order
       Region 1mr1 A 544-552 disorder
Seqacetylation
    37-37 N6-acetyllysine
    428-428 N6-acetyllysine
    507-507 N6-acetyllysine
 
Prediction
NeProc
Disorder 1-19,148-310,470-479,546-552
Order 20-147,311-469,485-545
ProS 15-19,148-151,157-196,206-310,470-475,546-552
AlphaFold
Disorder 1-8,138-286,297-310,466-490,544-552
Order 9-137,287-296,311-465,491-543
Pfam Hmmer
PF03165 33-137 6.1e-64
PF03166 317-532 3.2e-145
SEG 45-55 ,287-300 ,446-466
Function
Function in SwissProt
In muscle physiology, plays a central role in the balance between atrophy and hypertrophy. When recruited by MSTN, promotes atrophy response via phosphorylated SMAD2/4. MSTN decrease causes SMAD4 release and subsequent recruitment by the BMP pathway to promote hypertrophy via phosphorylated SMAD1/5/8. Acts synergistically with SMAD1 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression. Binds to SMAD binding elements (SBEs) (5'-GTCT/AGAC-3') within BMP response element (BMPRE) of cardiac activating regions (By similarity). Common SMAD (co-SMAD) is the coactivator and mediator of signal transduction by TGF-beta (transforming growth factor). Component of the heterotrimeric SMAD2/SMAD3-SMAD4 complex that forms in the nucleus and is required for the TGF-mediated signaling (PubMed:25514493). Promotes binding of the SMAD2/SMAD4/FAST-1 complex to DNA and provides an activation function required for SMAD1 or SMAD2 to stimulate transcription. Component of the multimeric SMAD3/SMAD4/JUN/FOS complex which forms at the AP1 promoter site; required for synergistic transcriptional activity in response to TGF-beta. May act as a tumor suppressor. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator.
Biological Process
See also
Diagram with PDB data
SMAD3/SMAD3/SMAD4Crystal Structure of the phosphorylated Smad3/Smad4 heterotrimeric complex
SMAD2/SMAD2/SMAD4Crystal Structure of the phosphorylated Smad2/Smad4 heterotrimeric complex