P40818: Ubiquitin carboxyl-terminal hydrolase 8 (USP8)

Ubiquitin carboxyl-terminal hydrolase 8 (USP8) is a 1118-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P40818.

Gene
USP8
Organism
Homo sapiens
Length
1118 residues
Mean pLDDT
71.3
Model
AF-P40818-F1 v6
Model created
1 Aug 2025
PDB structures
9

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Model confidence (pLDDT)

The mean pLDDT of this model is 71.3 (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 accurate36%
70 to 90Confident: backbone generally right28%
50 to 70Low: treat with caution6%
Below 50Very low: often disordered regions30%

What pLDDT means and how to read it

Function

Hydrolase that can remove conjugated ubiquitin from proteins and therefore plays an important regulatory role at the level of protein turnover by preventing degradation. Converts both 'Lys-48' an 'Lys-63'-linked ubiquitin chains. Catalytic activity is enhanced in the M phase. Involved in cell proliferation. Required to enter into S phase in response to serum stimulation. May regulate T-cell anergy mediated by RNF128 via the formation of a complex containing RNF128 and OTUB1. Probably regulates the stability of STAM2 and RASGRF1. Regulates endosomal ubiquitin dynamics, cargo sorting, membrane traffic at early endosomes, and maintenance of ESCRT-0 stability. The level of protein…

Subunit structure

Forms a ternary complex with RNF128 and OTUB1. Interacts (via C-terminal UCH catalytic domain) with OTUB1 isoform 1. Interacts with STAM2 (via SH3 domain). Interacts with DNAJB3, EGFR, EPS15, RASGRF1, RNF41, YWHAE, YWHAG and YWHAZ (By similarity). Interacts with NBR1, RASGRF1, RNF41 and IST1. Associates with the ESCRT-0 complex and with microtubules (By similarity). Interacts with BIRC6/bruce…

Subcellular location

Cytoplasm, Nucleus, Endosome membrane, Cell membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6F09X-ray1.59 ÅA/B/C/D=712-724
8ADMX-ray1.7 ÅP=715-722
2GFOX-ray2.0 ÅA=734-1110
2A9UX-ray2.1 ÅA/B=1-142
8XPNX-ray2.1 ÅA/B/C=734-1110
2GWFX-ray2.3 ÅA/C/E=181-318
3N3KX-ray2.6 ÅA=734-1110
8Y9AX-ray3.1 ÅA=1-142
1WHBNMRA=174-317

More AlphaFold highlights

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