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IID00113
 UniprotP84022
ProteinMothers against decapentaplegic homolog 3
GeneSMAD3
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
425
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-144 Homo dimer :
 Evidence X-RAY 1mhd A Reference
       Region 1mhd A 1-9 disorder
       Region 1mhd A 10-132 order
 Evidence X-RAY 1mhd B Reference
       Region 1mhd B 1-9 disorder
       Region 1mhd B 10-132 order
 Evidence X-RAY 5odg A Reference
       Region 5odg A 11-135 order
 Evidence X-RAY 5odg B Reference
       Region 5odg B 11-134 order
       Region 5odg B 135-135 disorder
 Evidence X-RAY 1ozj A Reference
       Region 1ozj A 1-6 disorder
       Region 1ozj A 7-132 order
       Region 1ozj A 133-144 disorder
 Evidence X-RAY 1ozj B Reference
       Region 1ozj B 1-8 disorder
       Region 1ozj B 9-132 order
       Region 1ozj B 133-144 disorder
Seq 10-136 Homo dimer :
 Evidence X-RAY 6zmn B Reference
       Region 6zmn B 10-22 order
       Region 6zmn B 26-130 order
       Region 6zmn B 131-136 disorder
 Evidence X-RAY 6zmn A Reference
       Region 6zmn A 10-22 order
       Region 6zmn A 26-132 order
       Region 6zmn A 133-136 disorder
 Evidence X-RAY 5od6 B Reference
       Region 5od6 B 11-135 order
 Evidence X-RAY 5od6 A Reference
       Region 5od6 A 11-134 order
       Region 5od6 A 135-135 disorder
Seqdisorder 146-219
 Evidence X-RAY Reference
       Region 146-219 disorder
Seq 176-183
 Evidence NMR 2lb3 B Reference
       Region 2lb3 B 176-183 order
Seq 178-189 Hetero dimer : IID00114Complex
 Evidence NMR 2lb2 B Reference
       Region 2lb2 B 178-189 order
Seq 202-211 Hetero dimer : IID00114Complex
 Evidence NMR 2laj B Reference
       Region 2laj B 202-211 order
Seqdisorder 219-228
 Evidence X-RAY Reference
       Region 219-228 disorder
Seq 220-416 Hetero nonamer : O75593,P0AA25
 Evidence X-RAY 5xoc A Reference
       Region 5xoc A 220-220 disorder
       Region 5xoc A 221-414 order
       Region 5xoc A 415-416 disorder
Seq 220-425 Hetero tetramer : IID00112Complex
 Evidence X-RAY 1mk2 A Reference
       Region 1mk2 A 220-416 order
       Region 1mk2 A 417-425 disorder
Seq 228-425 Hetero trimer : IID00132Complex
 Evidence X-RAY 1u7f C Reference
       Region 1u7f C 228-229 disorder
       Region 1u7f C 230-425 order
 Evidence X-RAY 1u7f A Reference
       Region 1u7f A 228-425 order
Seq 229-425 Monomer :
 Evidence X-RAY 1mjs A Reference
       Region 1mjs A 229-323 order
       Region 1mjs A 324-328 disorder
       Region 1mjs A 329-380 order
       Region 1mjs A 381-387 disorder
       Region 1mjs A 388-418 order
       Region 1mjs A 419-425 disorder
Seq 417-425 Hetero dimer : IID00301Complex
 Evidence X-RAY 6yib P Reference
       Region 6yib P 417-418 disorder
       Region 6yib P 419-425 order
SeqProS verified 178-189 Hetero dimer : IID00114Complex
       Region 2lb2 B 178-189 order
       Region 146-219 disorder
SeqProS verified 202-211 Hetero dimer : IID00114Complex
       Region 2laj B 202-211 order
       Region 146-219 disorder
SeqProS verified 220-228,324-328 Hetero tetramer : IID00112Complex
       Region 1mk2 A 220-416 order
       Region 219-228 disorder
       Region 1mjs A 324-328 disorder
SeqProS verified 324-328,419-424 Hetero trimer : IID00132Complex
       Region 1u7f A 228-425 order
       Region 1u7f C 230-425 order
       Region 1mjs A 324-328 disorder
       Region 1mk2 A 417-425 disorder
Seqphosphorylation
    8-8 Phosphothreonine; by CDK2 and CDK4
    179-179 Phosphothreonine; by CDK2
    204-204 Phosphoserine; by GSK3 and MAPK
    208-208 Phosphoserine; by MAPK
    213-213 Phosphoserine; by CDK2 and CDK4
    416-416 Phosphoserine
    418-418 Phosphoserine; by CK1
    422-422 Phosphoserine; by TGFBR1
    423-423 Phosphoserine; by TGFBR1
    425-425 Phosphoserine; by TGFBR1
Seqacetylation
    2-2 N-acetylserine
    378-378 N6-acetyllysine
 
Prediction
NeProc
Disorder 1-6,136-225,416-425
Order 7-135,226-262,267-415
ProS 136-154,165-212,217-225,416-425
AlphaFold
Disorder 1-6,23-23,143-219,425-425
Order 7-22,24-142,220-424
Pfam Hmmer
PF03165 28-131 2.4e-65
PF03166 226-403 8.4e-124
SEG 33-44 ,133-141
Function
Function in SwissProt
Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD3/SMAD4 complex, activates transcription. Also can form a SMAD3/SMAD4/JUN/FOS complex at the AP-1/SMAD site to regulate TGF-beta-mediated transcription. Has an inhibitory effect on wound healing probably by modulating both growth and migration of primary keratinocytes and by altering the TGF-mediated chemotaxis of monocytes. This effect on wound healing appears to be hormone-sensitive. Regulator of chondrogenesis and osteogenesis and inhibits early healing of bone fractures. 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
SMAD3/SMAD3/SMAD4Crystal Structure of the phosphorylated Smad3/Smad4 heterotrimeric complex
SMAD3/NEDD4LStructure of the second domain of human Nedd4L in complex with a phosphorylated pTPY motif derived from human Smad3
See also
Diagram with PDB data
ZFYVE9/SMAD3SMAD3 SBD complex