Ubiquitin carboxyl-terminal hydrolase 15 (USP15) is a 981-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9Y4E8.
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The mean pLDDT of this model is 75.4 (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 | 43% |
| 70 to 90 | Confident: backbone generally right | 27% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 22% |
What pLDDT means and how to read it
Hydrolase that removes conjugated ubiquitin from target proteins and regulates various pathways such as the TGF-beta receptor signaling, NF-kappa-B and RNF41/NRDP1-PRKN pathways (PubMed:16005295, PubMed:17318178, PubMed:19576224, PubMed:19826004, PubMed:21947082, PubMed:22344298, PubMed:24852371). Acts as a key regulator of TGF-beta receptor signaling pathway, but the precise mechanism is still unclear: according to a report, acts by promoting deubiquitination of monoubiquitinated R-SMADs (SMAD1, SMAD2 and/or SMAD3), thereby alleviating inhibition of R-SMADs and promoting activation of TGF-beta target genes (PubMed:21947082). According to another reports, regulates the TGF-beta receptor…
A homodimer structure has been reported; however it is unclear whether the protein form a homodimer in vivo (PubMed:22001210). Identified in a complex with the COP9 signalosome complex (CSN) (PubMed:16005295). Interacts with SMAD1, SMAD2 and SMAD3; the interaction is direct (PubMed:21947082). Forms a complex with SMURF2 and SMAD7 (PubMed:22344298). Interacts with TGFBR1 (PubMed:22344298).…
Cytoplasm, Nucleus, Mitochondrion
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4A3P | X-ray | 1.4 Å | A=6-223 |
| 3T9L | X-ray | 1.5 Å | A=1-222 |
| 6ML1 | X-ray | 1.9 Å | A/B=275-862, A/B=873-934 |
| 6GHA | X-ray | 1.98 Å | A=284-468, A=786-948 |
| 7R2G | X-ray | 1.98 Å | A/B=284-948 |
| 6CPM | X-ray | 2.01 Å | C/D=275-862, C/D=873-934 |
| 6GH9 | X-ray | 2.09 Å | A/B=284-468, A/B=786-951 |
| 3LMN | X-ray | 2.15 Å | A/B=1-133 |
| 4A3O | X-ray | 2.2 Å | A/B=4-223 |
| 3PPA | X-ray | 2.35 Å | A=6-223 |
| 6CRN | X-ray | 2.5 Å | A/B/C/D=275-934 |
| 3PV1 | X-ray | 2.6 Å | A/B=1-223 |
| 5JJW | X-ray | 3.01 Å | B=1-223 |
| 6DJ9 | X-ray | 3.1 Å | A/B/C/D/E/F=1-134 |
| 1W6V | NMR | A=1-120 |
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