Q9Y4E8: Ubiquitin carboxyl-terminal hydrolase 15 (USP15)

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.

Gene
USP15
Organism
Homo sapiens
Length
981 residues
Mean pLDDT
75.4
Model
AF-Q9Y4E8-F1 v6
Model created
1 Aug 2025
PDB structures
15

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Model confidence (pLDDT)

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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate43%
70 to 90Confident: backbone generally right27%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions22%

What pLDDT means and how to read it

Function

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…

Subunit structure

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).…

Subcellular location

Cytoplasm, Nucleus, Mitochondrion

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4A3PX-ray1.4 ÅA=6-223
3T9LX-ray1.5 ÅA=1-222
6ML1X-ray1.9 ÅA/B=275-862, A/B=873-934
6GHAX-ray1.98 ÅA=284-468, A=786-948
7R2GX-ray1.98 ÅA/B=284-948
6CPMX-ray2.01 ÅC/D=275-862, C/D=873-934
6GH9X-ray2.09 ÅA/B=284-468, A/B=786-951
3LMNX-ray2.15 ÅA/B=1-133
4A3OX-ray2.2 ÅA/B=4-223
3PPAX-ray2.35 ÅA=6-223
6CRNX-ray2.5 ÅA/B/C/D=275-934
3PV1X-ray2.6 ÅA/B=1-223
5JJWX-ray3.01 ÅB=1-223
6DJ9X-ray3.1 ÅA/B/C/D/E/F=1-134
1W6VNMRA=1-120

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