STAM-binding protein (STAMBP) is a 424-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O95630.
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The mean pLDDT of this model is 84.0 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 65% |
| 70 to 90 | Confident: backbone generally right | 18% |
| 50 to 70 | Low: treat with caution | 2% |
| Below 50 | Very low: often disordered regions | 15% |
What pLDDT means and how to read it
Zinc metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains (PubMed:15314065, PubMed:23542699, PubMed:34425109). Does not cleave 'Lys-48'-linked polyubiquitin chains (PubMed:15314065). Plays a role in signal transduction for cell growth and MYC induction mediated by IL-2 and GM-CSF (PubMed:10383417). Potentiates BMP (bone morphogenetic protein) signaling by antagonizing the inhibitory action of SMAD6 and SMAD7 (PubMed:11483516). Has a key role in regulation of cell surface receptor-mediated endocytosis and ubiquitin-dependent sorting of receptors to lysosomes (PubMed:15314065, PubMed:17261583). Endosomal localization of STAMBP is required for efficient EGFR…
Interacts with STAM (PubMed:10383417, PubMed:15314065). Interacts with SMAD6 and SMAD7 (PubMed:11483516). Interacts with CHMP3; the interaction appears to relieve the autoinhibition of CHMP3 (PubMed:17146056, PubMed:17261583). Interacts with SMURF2 and RNF11; this interaction promotes ubiquitination (PubMed:14755250)
Nucleus, Membrane, Cytoplasm, Early endosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3RZV | X-ray | 1.67 Å | A=219-424 |
| 2XZE | X-ray | 1.75 Å | A/B=1-146 |
| 3RZU | X-ray | 2.5 Å | A/B/C/D/E/F/G=243-424 |
| 9LE4 | X-ray | 2.6 Å | A/C/E/G=1-146, B/D/F/H=243-424 |
| 5IXF | NMR | B=228-241 |
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