SMUF2 rabbit pAb

domain:The C2 domain is involved in autoinhibition of the catalytic activity by interacting with the HECT domain.,domain:The second and third WW domains are responsible for interaction with the PY-motif of R-SMAD (SMAD1, SMAD2 and SMAD3).,function: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 SMAD1 and SMAD7 in order to trigger their ubiquitination and proteasome-dependent degradation. In addition, interaction with SMAD7 activates autocatalytic degradation, which is prevented by interaction with SCYE1. Forms a stable complex with the TGF-beta receptor-mediated phosphorylated SMAD2 and SMAD3. In this way, SMAD2 may recruit substrates, such as SNON, for ubiquitin-mediated degradation. Enhances the inhibitory activity of SMAD7 and reduces the transcriptional activity of SMAD2. Coexpression of SMURF2 with SMAD1 results in considerable decrease in steady-state level of SMAD1 protein and a smaller decrease of SMAD2 level.,pathway:Protein modification; protein ubiquitination.,similarity:Contains 1 C2 domain.,similarity:Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain.,similarity:Contains 3 WW domains.,subcellular location:Cytoplasmic in the presence of SMAD7. Co-localizes with CAV1, SMAD7 and TGF-beta receptor in membrane rafts.,subunit:Interacts (via WW domains) with SMAD1. Interacts (via WW domains) with SMAD2 (via PY-motif). Interacts (via WW domains) with SMAD3 (via PY-motif). Interacts with SMAD6. Interacts with SMAD7 (via PY-motif). Does not interact with SMAD4; SMAD4 lacks a PY-motif. Interacts with SCYE1.,tissue specificity:Widely expressed.,