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IID00223
 UniprotQ9HAU4
ProteinE3 ubiquitin-protein ligase SMURF2
GeneSMURF2
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
748
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 10-140 Monomer :
 Evidence NMR 2jqz A Reference
       Region 2jqz A 10-140 order
Seq 250-333 Hetero dimer : IID00135Complex
 Evidence NMR 2kxq A Reference
       Region 2kxq A 250-333 order
Seq 297-333 Hetero dimer : IID00135Complex
 Evidence NMR 2djy A Reference
       Region 2djy A 297-333 order
       Region 2djy A 332-333 high_rmsd
 Evidence NMR 2ltz A Reference
       Region 2ltz A 297-333 order
Seq 369-748 Monomer :
 Evidence X-RAY 1zvd A Reference
       Region 1zvd A 369-741 order
       Region 1zvd A 742-748 disorder
 
Prediction
NeProc
Disorder 1-10,110-275,286-295,338-364
Order 11-109,276-285,296-336,365-748
ProS 110-119,128-141,167-182,202-208,254-275,354-358
AlphaFold
Disorder 1-10,29-30,139-158,167-173,195-252,285-295,331-370,431-431,461-465,524-524,742-748
Order 11-28,31-138,159-166,174-194,253-284,296-330,371-430,432-460,466-523,525-741
Pfam Hmmer
PF00168 14-98 2.6e-21
PF00397 159-188 7.8e-13
PF00397 253-282 5.6e-10
PF00397 299-328 4.2e-13
PF00632 443-748 1.7e-176
SEG 341-351
Function
Function in SwissProt
E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (PubMed:11016919). Interacts with SMAD7 to trigger SMAD7-mediated transforming growth factor beta/TGF-beta receptor ubiquitin-dependent degradation, thereby downregulating TGF-beta signaling (PubMed:11163210, PubMed:12717440). In addition, interaction with SMAD7 activates autocatalytic degradation, which is prevented by interaction with AIMP1 (PubMed:18448069). Also forms a stable complex with TGF-beta receptor-mediated phosphorylated SMAD1, SMAD2 and SMAD3, and targets SMAD1 and SMAD2 for ubiquitination and proteasome-mediated degradation (PubMed:11016919, PubMed:11158580, PubMed:11389444). SMAD2 may recruit substrates, such as SNON, for ubiquitin-dependent degradation (PubMed:11389444). Negatively regulates TGFB1-induced epithelial-mesenchymal transition and myofibroblast differentiation (PubMed:30696809).
(Microbial infection) In case of filoviruses Ebola/EBOV and Marburg/MARV infection, the complex formed by viral matrix protein VP40 and SMURF2 facilitates virus budding.
Biological Process
See also
Diagram with PDB data
SMAD7/SMURF2Solution structure of Smurf2 WW3 domain-Smad7 PY peptide complex