Q9UHD9: Ubiquilin-2 (UBQLN2)

Ubiquilin-2 (UBQLN2) is a 624-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9UHD9.

Gene
UBQLN2
Organism
Homo sapiens
Length
624 residues
Mean pLDDT
61.0
Model
AF-Q9UHD9-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 61.0 (low 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 accurate3%
70 to 90Confident: backbone generally right27%
50 to 70Low: treat with caution40%
Below 50Very low: often disordered regions30%

What pLDDT means and how to read it

Function

Plays an important role in the regulation of different protein degradation mechanisms and pathways including ubiquitin-proteasome system (UPS), autophagy and the endoplasmic reticulum-associated protein degradation (ERAD) pathway. Mediates the proteasomal targeting of misfolded or accumulated proteins for degradation by binding (via UBA domain) to their polyubiquitin chains and by interacting (via ubiquitin-like domain) with the subunits of the proteasome (PubMed:10983987). Plays a role in the ERAD pathway via its interaction with ER-localized proteins FAF2/UBXD8 and HERPUD1 and may form a link between the polyubiquitinated ERAD substrates and the proteasome (PubMed:18307982,…

Subunit structure

Homodimer. Forms heterodimer with UBQLN1. Binds UBE3A and BTRC. Interacts with the 19S proteasome subunit. Interacts with C9orf72. Interacts with HNRNPA1 and HNRNPU. Found in a complex with UBQLN1 and MAP1LC3A/B/C. Interacts with EPS15, EPN1 and EPN2. Interacts with HERPUD1. Interacts with RAD23A. Interacts with TARDBP. Interacts (via C-terminus) with FAF2 (via N-terminus). Interacts with…

Subcellular location

Cytoplasm, Nucleus, Membrane, Cytoplasmic vesicle, autophagosome

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
1J8CNMRA=1-119
2NBVNMRB=26-103
6MUNNMRB/C=26-103
7F7XNMRB=578-621

More AlphaFold highlights

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