SMURF2 Antibody – Rabbit Polyclonal

SMURF2: 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.

Protein type: EC 6.3.2.-; Ligase; Ubiquitin conjugating system; Ubiquitin ligase; EC 6.3.2.19

Chromosomal Location of Human Ortholog: 17q22-q23

Cellular Component: cytosol; lipid raft; nucleoplasm; nucleus; plasma membrane; ubiquitin ligase complex

Molecular Function: identical protein binding; ligase activity; protein binding; SMAD binding; transforming growth factor beta receptor binding; ubiquitin-protein ligase activity

Biological Process: BMP signaling pathway; gene expression; negative regulation of transcription from RNA polymerase II promoter; negative regulation of transcription, DNA-dependent; negative regulation of transforming growth factor beta receptor signaling pathway; protein ubiquitination during ubiquitin-dependent protein catabolic process; regulation of transforming growth factor beta receptor signaling pathway; transcription initiation from RNA polymerase II promoter; transcription, DNA-dependent; transforming growth factor beta receptor signaling pathway; ubiquitin-dependent protein catabolic process; ubiquitin-dependent SMAD protein catabolic process