Q9HCE7: E3 ubiquitin-protein ligase SMURF1 (SMURF1)

E3 ubiquitin-protein ligase SMURF1 (SMURF1) is a 757-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9HCE7.

Gene
SMURF1
Organism
Homo sapiens
Length
757 residues
Mean pLDDT
73.3
Model
AF-Q9HCE7-F1 v6
Model created
1 Aug 2025
PDB structures
7

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Model confidence (pLDDT)

The mean pLDDT of this model is 73.3 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate37%
70 to 90Confident: backbone generally right33%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions22%

What pLDDT means and how to read it

Function

E3 ubiquitin-protein ligase that acts as a negative regulator of BMP signaling pathway. Mediates ubiquitination and degradation of SMAD1 and SMAD5, 2 receptor-regulated SMADs specific for the BMP pathway. Promotes ubiquitination and subsequent proteasomal degradation of TRAF family members and RHOA. Promotes ubiquitination and subsequent proteasomal degradation of MAVS (PubMed:23087404). Acts as a positive regulator of smoothened signaling pathway by mediating ubiquitination of PTCH1, leading to endocytosis and lysosomal degradation of PTCH1 (By similarity). Acts as an antagonist of TGF-beta signaling by ubiquitinating TGFBR1 and targeting it for degradation (PubMed:21791611). Plays a role…

Subunit structure

Interacts with TRAF4. Interacts (via HECT domain) with FBXL15 (via LRR repeats). Interacts with SMAD7 and TGFBR1; SMAD7 recruits SMURF1 to TGFBR1 and regulates TGF-beta receptor degradation. Interacts with MAVS; the interaction is mediated by NDFIP1 (PubMed:23087404)

Subcellular location

Cytoplasm, Cell membrane

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
3PYCX-ray1.96 ÅA=13-140
9FSJX-ray2.05 ÅA=377-751
9FSKX-ray2.75 ÅA/B/C/D=377-751
2LAZNMRA=235-267
2LB0NMRA=235-267
2LB1NMRA=305-340
2LTXNMRA=306-340

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