Ubiquitin carboxyl-terminal hydrolase 35 (USP35) is a 1018-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9P2H5.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 76.1 (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 | 45% |
| 70 to 90 | Confident: backbone generally right | 28% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 23% |
What pLDDT means and how to read it
Deubiquitinase that plays a role in different processes including cell cycle regulation, mitophagy or endoplasmic reticulum stress (PubMed:26348204, PubMed:29449677, PubMed:37004621). Inhibits TNFalpha-induced NF-kappa-B activation through stabilizing TNIP2 protein via deubiquitination (PubMed:26348204). Plays an essential role during mitosis by deubiquitinating and thereby regulating the levels of Aurora B/AURKB protein (PubMed:29449677). In addition, regulates the protein levels of other key component of the chromosomal passenger complex (CPC) such as survivin/BIRC5 or Borealin/CDCA8 by enhancing their stability (PubMed:34438346). Regulates the degradation of mitochondria through the…
Homodimer (via C-terminal region). Interacts with HSP90AA1
Cytoplasm, Mitochondrion
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=834-845 |
| 5TXK | X-ray | 1.84 Å | A=423-944 |
| 7Q44 | X-ray | 2.2 Å | B/D/F=988-1002 |
| 9F19 | X-ray | 2.75 Å | A/B=834-845 |
MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.