E3 ubiquitin-protein ligase SMURF1; hSMURF1; SMAD ubiquitination regulatory factor 1; SMAD-specific E3 ubiquitin-protein ligase 1 (SMURF1, KIAA1625)

Function: - E3 ubiquitin-protein ligase - acts as a negative regulator of BMP signaling pathway - acts by mediating ubiquitination & degradation of SMAD1 & SMAD5 (BMP pathway) - promotes ubiquitination & subsequent proteasomal degradation of TRAF family members - protein modification; protein ubiquitination - ubiquitinated by the SCF(FBXL15) complex at Lys-381 & Lys-383, leading to its degradation by the proteasome - Lys-383 is the primary ubiquitination site - interacts with TRAF4 - interacts (via HECT domain) with FBXL15 (via LRR repeats) - interacts with SMAD7 & TGFBR1 - SMAD7 recruits SMURF1 to TGFBR1 & regulates TGF-beta receptor degradation Structure: - contains 1 C2 domain - contains 1 HECT domain (E6AP-type E3 ubiquitin-protein ligase) - contains 2 WW domains Compartment: cytoplasm Alternative splicing: named isoforms=2; long short

Properties

SIZE: entity length = 757 aa MW = 86 kD COMPARTMENT: cytoplasm MOTIF: C2 domain {1-99} MOTIF: binding site FOR-BINDING-OF: phospholipid Ca+2-binding site WW domain (W/rsp5/WWP domain) {234-267} WW domain (W/rsp5/WWP domain) {306-339} HECT domain {420-757} MOTIF: cysteine residue {C725}

References

UniProt :accession Q9HCE7

Databases & Figures

OMIM 605568 UniProt Q9HCE7 PFAM correlations Entrez Gene 57154 Kegg hsa:57154 TGF-beta/BMP signaling