O60828: Polyglutamine-binding protein 1 (PQBP1)

Polyglutamine-binding protein 1 (PQBP1) is a 265-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O60828.

Gene
PQBP1
Organism
Homo sapiens
Length
265 residues
Mean pLDDT
70.6
Model
AF-O60828-F1 v6
Model created
1 Aug 2025
PDB structures
3

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Model confidence (pLDDT)

The mean pLDDT of this model is 70.6 (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 accurate8%
70 to 90Confident: backbone generally right44%
50 to 70Low: treat with caution38%
Below 50Very low: often disordered regions11%

What pLDDT means and how to read it

Function

Intrinsically disordered protein that acts as a scaffold, and which is involved in different processes, such as pre-mRNA splicing, transcription regulation, innate immunity and neuron development (PubMed:10198427, PubMed:10332029, PubMed:12062018, PubMed:20410308, PubMed:23512658). Interacts with splicing-related factors via the intrinsically disordered region and regulates alternative splicing of target pre-mRNA species (PubMed:10332029, PubMed:12062018, PubMed:20410308, PubMed:23512658). May suppress the ability of POU3F2 to transactivate the DRD1 gene in a POU3F2 dependent manner. Can activate transcription directly or via association with the transcription machinery (PubMed:10198427).…

Subunit structure

Interacts with POU3F2/Brn-2, ATXN1, TXNL4A, HTT and AR (PubMed:10332029, PubMed:10873650, PubMed:19303059, PubMed:24781215). Interaction with ATXN1 correlates positively with the length of the polyglutamine tract (PubMed:12062018). Interacts with RNA polymerase II large subunit in a phosphorylation-dependent manner (PubMed:12062018). Forms a ternary complex with ATXN1 mutant and phosphorylated…

Subcellular location

Nucleus, Nucleus speckle, Cytoplasmic granule

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4BWQX-ray2.1 ÅB/D/F/H=223-265
4BWSX-ray2.5 ÅB/E=229-265
4CDOX-ray2.5 ÅA/C=224-265

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