Ubiquitin carboxyl-terminal hydrolase 14 (USP14) is a 494-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P54578.
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The mean pLDDT of this model is 81.9 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 42% |
| 70 to 90 | Confident: backbone generally right | 41% |
| 50 to 70 | Low: treat with caution | 10% |
| Below 50 | Very low: often disordered regions | 8% |
What pLDDT means and how to read it
Proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins (PubMed:35145029). Ensures the regeneration of ubiquitin at the proteasome (PubMed:18162577, PubMed:28396413). Is a reversibly associated subunit of the proteasome and a large fraction of proteasome-free protein exists within the cell (PubMed:18162577). Required for the degradation of the chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis (PubMed:19106094). Also serves as a physiological inhibitor of endoplasmic reticulum-associated degradation (ERAD) under the non-stressed condition by inhibiting the degradation of unfolded endoplasmic reticulum…
Homodimer (Potential). Associates with the 26S proteasome. Interacts with FANCC, CXCR4 and ERN1. Interacts with TRIM14; this interaction recruits USP14 to cleave ubiquitin chains of CGAS and KDM4D (PubMed:27666593, PubMed:35145029)
Cytoplasm, Cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9F6G | X-ray | 1.5 Å | A=248-272, A=295-321 |
| 6IIK | X-ray | 1.97 Å | A/B=96-494 |
| 6IIL | X-ray | 2.2 Å | A/B=96-494 |
| 6IIM | X-ray | 2.21 Å | A/B=96-494 |
| 6IIN | X-ray | 2.53 Å | A/B=101-485 |
| 6LVS | X-ray | 2.73 Å | A/B/C/D/E/F=92-494 |
| 9F19 | X-ray | 2.75 Å | A/B=248-272, A/B=295-321 |
| 7W37 | EM | 3.0 Å | x=1-494 |
| 7W38 | EM | 3.1 Å | x=1-494 |
| 2AYN | X-ray | 3.2 Å | A/B/C=91-494 |
| 7W39 | EM | 3.2 Å | x=1-494 |
| 7W3G | EM | 3.2 Å | x=1-494 |
| 7W3H | EM | 3.2 Å | x=1-494 |
| 7W3F | EM | 3.3 Å | x=1-494 |
| 7W3C | EM | 3.4 Å | x=1-494 |
| 2AYO | X-ray | 3.5 Å | A=91-494 |
| 7W3A | EM | 3.5 Å | x=1-494 |
| 7W3I | EM | 3.5 Å | x=1-494 |
| 7W3J | EM | 3.5 Å | x=1-494 |
| 7W3M | EM | 3.5 Å | x=1-494 |
Showing 20 of 23 experimental structures (best resolution first).
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