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 . Interacts with SMAD7 to trigger SMAD7-mediated transforming growth factor beta/TGF-beta receptor ubiquitin-dependent degradation, thereby down-regulating TGF-beta signaling ( ). In addition, interaction with SMAD7 activates autocatalytic degradation, which is prevented by interaction with AIMP1 . 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 ( ). SMAD2 may recruit substrates, such as SNON, for ubiquitin-dependent degradation . Negatively regulates TGFB1-induced epithelial-mesenchymal transition and myofibroblast differentiation .
(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.
Subcellular locations: Nucleus, Cytoplasm, Cell membrane, Membrane raft
Cytoplasmic in the presence of SMAD7. Colocalizes with CAV1, SMAD7 and TGF-beta receptor in membrane rafts.
Widely expressed.