SMURF2 — SMAD specific E3 ubiquitin protein ligase 2
SMURF2 belongs to a gene co-expression module in 4 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.
SMURF2's module in each cell type
| Cell type | Module | Shares the module with | |
|---|---|---|---|
| CD4⁺ T cells | Mixed Metabolic Ambient Technical artifact | DPYD, ENO2, FABP6, FCGRT, GRAP, SPINK2, SYNJ2BP, TNFRSF10B +1 more | View in SCUBA |
| Endothelial | Endothelial Quiescence Endothelial cell development | CCRL2, CDC42EP3, CGAS, CHSY1, CYTH1, HES5, HIPK3, ID1 +7 more | View in SCUBA |
| Gamma-delta T cells | Activation Stress Response Stress | ARHGAP9, ARHGEF12, ATF3, ATP6V0A2, GALNT6, GPR18, HIC1, HMCES +12 more | |
| Pericytes | TGF-beta Negative Feedback Inflammatory | CTNND1, DAZAP2, EMP1, KAT6A, KBTBD2, KLF7, MLKL, RCAN1 +6 more | View in SCUBA |
About the gene
| Chromosome | 17: 64542282-64662307 |
|---|---|
| Predicted location | Intracellular |
| Essential gene | No |
| Protein class | Enzymes, Metabolic proteins, Predicted intracellular proteins |
| Molecular function | Transferase |
| Biological process | Host-virus interaction, Ubl conjugation pathway |
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 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
Human Protein Atlas · Open Targets · UniProt
Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.