Q9HAU4: E3 ubiquitin-protein ligase SMURF2 (SMURF2)

E3 ubiquitin-protein ligase SMURF2 (SMURF2) is a 748-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9HAU4.

Gene
SMURF2
Organism
Homo sapiens
Length
748 residues
Mean pLDDT
76.9
Model
AF-Q9HAU4-F1 v6
Model created
1 Aug 2025
PDB structures
8

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Model confidence (pLDDT)

The mean pLDDT of this model is 76.9 (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 accurate36%
70 to 90Confident: backbone generally right39%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions15%

What pLDDT means and how to read it

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 (PubMed:11016919, PubMed:38016474). Interacts with SMAD7 to trigger SMAD7-mediated transforming growth factor beta/TGF-beta receptor ubiquitin-dependent degradation, thereby down-regulating TGF-beta signaling (PubMed:11163210, PubMed:12717440, PubMed:21791611). In addition, interaction with SMAD7 activates autocatalytic degradation, which is prevented by interaction with AIMP1 (PubMed:18448069). Also forms a stable complex with TGF-beta receptor-mediated phosphorylated SMAD1, SMAD2 and SMAD3, and targets…

Subunit structure

Interacts (via WW domains) with SMAD1 (PubMed:11158580). Interacts (via WW domains) with SMAD2 (via PY-motif) (PubMed:11158580, PubMed:11389444). Interacts (via WW domains) with SMAD3 (via PY-motif) (PubMed:11158580, PubMed:11389444). Interacts with SMAD6 (PubMed:11158580). Interacts with SMAD7 (via PY-motif) and TGFBR1; SMAD7 recruits SMURF2 to the TGF-beta receptor and regulates its…

Subcellular location

Nucleus, Cytoplasm, Cell membrane, Membrane raft

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9FSHX-ray2.08 ÅA=251-748
1ZVDX-ray2.1 ÅA=369-748
6FX4X-ray2.5 ÅA/C=631-745
7M3QX-ray2.5 ÅA=366-748
2DJYNMRA=297-333
2JQZNMRA=10-140
2KXQNMRA=250-333
2LTZNMRA=297-333

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