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IID00127
 UniprotQ15796
ProteinMothers against decapentaplegic homolog 2
GeneSMAD2
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
 Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
467
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 217-224 Hetero dimer : IID00829Complex
 Evidence NMR 2lb3 B 2lb3: Smad3/Pin1 complex (Structure of the WW domain of PIN1 in complex with a human phosphorylated Smad3 derived peptide); The peptide sequence of Smad3, IPETPPPG (residues 176-183), is identical to the residues 217-224 of Smad2. Reference
       Region 2lb3 B 217-224 order
Seq 241-467 Hetero dimer : IID00131Complex
 Evidence X-RAY 6zvq A Reference
       Region 6zvq A 241-265 disorder
       Region 6zvq A 266-467 order
Seq 241-467 Homo trimer :
 Evidence X-RAY 1khx A Reference
       Region 1khx A 241-264 disorder
       Region 1khx A 265-467 order
Seq 261-456 Hetero dimer : IID00112Complex
 Evidence X-RAY 1dev A Reference
       Region 1dev A 261-262 disorder
       Region 1dev A 263-456 order
 Evidence X-RAY 1dev C Reference
       Region 1dev C 261-423 order
       Region 1dev C 424-427 disorder
       Region 1dev C 428-456 order
Seq 262-458 Hetero hexamer : IID00131Complex
 Evidence X-RAY 5xod A Reference
       Region 5xod A 262-365 order
       Region 5xod A 366-369 disorder
       Region 5xod A 370-456 order
       Region 5xod A 457-458 disorder
Seq 262-458 Hetero pentamer : Q9Y2U8
 Evidence X-RAY 5zoj C Reference
       Region 5zoj C 262-270 disorder
       Region 5zoj C 271-456 order
       Region 5zoj C 457-458 disorder
 Evidence X-RAY 5zoj B Reference
       Region 5zoj B 262-271 disorder
       Region 5zoj B 272-456 order
       Region 5zoj B 457-458 disorder
 Evidence X-RAY 5zoj A Reference
       Region 5zoj A 262-269 disorder
       Region 5zoj A 270-456 order
       Region 5zoj A 457-458 disorder
Seq 262-467 Hetero hexamer : IID00092Complex
 Evidence X-RAY 6m64 E Reference
       Region 6m64 E 262-265 disorder
       Region 6m64 E 266-458 order
       Region 6m64 E 459-464 disorder
 Evidence X-RAY 6m64 C Reference
       Region 6m64 C 262-266 disorder
       Region 6m64 C 267-460 order
       Region 6m64 C 461-464 disorder
 Evidence X-RAY 6m64 A Reference
       Region 6m64 A 262-264 disorder
       Region 6m64 A 265-464 order
 Evidence X-RAY 7co1 E Reference
       Region 7co1 E 262-265 disorder
       Region 7co1 E 266-457 order
       Region 7co1 E 458-467 disorder
 Evidence X-RAY 7co1 C Reference
       Region 7co1 C 262-265 disorder
       Region 7co1 C 266-458 order
       Region 7co1 C 459-467 disorder
 Evidence X-RAY 7co1 A Reference
       Region 7co1 A 262-264 disorder
       Region 7co1 A 265-458 order
       Region 7co1 A 459-467 disorder
Seq 270-467 Hetero trimer : IID00132Complex
 Evidence X-RAY 1u7v C Reference
       Region 1u7v C 270-271 disorder
       Region 1u7v C 272-467 order
 Evidence X-RAY 1u7v A Reference
       Region 1u7v A 270-467 order
Seqdisorder 457-467
 Evidence X-RAY Reference
       Region 457-467 disorder
Seq 459-467 Hetero dimer : IID00301Complex
 Evidence X-RAY 6yia P Reference
       Region 6yia P 459-460 disorder
       Region 6yia P 461-467 order
SeqProS predicted 217-224 This region is predicted to be disordered by AlphaFold (pLDDT <68.5) and NeProc. Hetero dimer : IID00829Complex
       Region 2lb3 B 217-224 order
SeqProS verified 457-467 Homo trimer :
       Region 1khx A 265-467 order
       Region 457-467 disorder
SeqProS verified 457-467 Hetero dimer : IID00131Complex
       Region 6zvq A 266-467 order
       Region 457-467 disorder
SeqProS verified 457-467 Hetero trimer : IID00132Complex
       Region 1u7v A 270-467 order
       Region 1u7v C 272-467 order
       Region 457-467 disorder
Seqphosphorylation
    220-220 Phosphothreonine
    465-465 Phosphoserine; by TGFBR1
    464-464 Phosphoserine
    460-460 Phosphoserine
    458-458 Phosphoserine
    255-255 Phosphoserine
    250-250 Phosphoserine
    245-245 Phosphoserine
    240-240 Phosphoserine; by CAMK2
    467-467 Phosphoserine; by TGFBR1
    8-8 Phosphothreonine; by MAPK3
Seqacetylation
    19-19 N6-acetyllysine
    2-2 N-acetylserine
 
Prediction
NeProc
Disorder 1-35,85-109,178-262,458-467
Order 36-84,115-177,263-457
ProS 1-21,30-35,85-91,102-106,178-221,240-262,458-467
AlphaFold
Disorder 1-6,22-34,80-114,182-261
Order 7-21,35-79,115-181,262-467
Pfam Hmmer
PF03165 38-171 7.4e-66
PF03166 268-445 1.2e-123
SEG 17-40 ,43-54 ,173-181
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 SMAD2/SMAD4 complex, activates transcription. Promotes TGFB1-mediated transcription of odontoblastic differentiation genes in dental papilla cells (By similarity). Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator. May act as a tumor suppressor in colorectal carcinoma (PubMed:8752209).
Biological Process
Diagram with PDB data
SMAD2/SMAD2/SMAD4Crystal Structure of the phosphorylated Smad2/Smad4 heterotrimeric complex
See also
Diagram with PDB data
ZFYVE9/SMAD2CRYSTAL STRUCTURE OF SMAD2 MH2 DOMAIN BOUND TO THE SMAD-BINDING DOMAIN OF SARA