P54252: Ataxin-3 (ATXN3)

Ataxin-3 (ATXN3) is a 361-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P54252.

Gene
ATXN3
Organism
Homo sapiens
Length
361 residues
Mean pLDDT
75.9
Model
AF-P54252-F1 v6
Model created
1 Aug 2025
PDB structures
7

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Model confidence (pLDDT)

The mean pLDDT of this model is 75.9 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate31%
70 to 90Confident: backbone generally right39%
50 to 70Low: treat with caution15%
Below 50Very low: often disordered regions15%

What pLDDT means and how to read it

Function

Deubiquitinating enzyme involved in protein homeostasis maintenance, transcription, cytoskeleton regulation, myogenesis and degradation of misfolded chaperone substrates (PubMed:12297501, PubMed:16118278, PubMed:17696782, PubMed:23625928, PubMed:28445460, PubMed:33157014). Binds long polyubiquitin chains and trims them, while it has weak or no activity against chains of 4 or less ubiquitins (PubMed:17696782). Involved in degradation of misfolded chaperone substrates via its interaction with STUB1/CHIP: recruited to monoubiquitinated STUB1/CHIP, and restricts the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension (By similarity). Interacts…

Subunit structure

Interacts with STUB1/CHIP (when monoubiquitinated) (By similarity). Interacts with DNA repair proteins RAD23A and RAD23B (PubMed:16020535, PubMed:30455355). Interacts with BECN1 (via its poly-Gln domain) (PubMed:28445460). Interacts with PRKN, UBR2, VCP and tubulin. Short isoform 1 interacts with CASP7 (PubMed:30455355)

Subcellular location

Nucleus matrix, Nucleus, Lysosome membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4YS9X-ray2.0 ÅB=278-329
4WTHX-ray2.25 ÅA/B=278-329
1YZBNMRA=1-182
2AGANMRA=1-185
2DOSNMRA=1-171
2JRINMRA=1-182
2KLZNMRA=222-263

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