Q13107: Ubiquitin carboxyl-terminal hydrolase 4 (USP4)

Ubiquitin carboxyl-terminal hydrolase 4 (USP4) is a 963-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13107.

Gene
USP4
Organism
Homo sapiens
Length
963 residues
Mean pLDDT
75.9
Model
AF-Q13107-F1 v6
Model created
1 Aug 2025
PDB structures
2

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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 accurate35%
70 to 90Confident: backbone generally right37%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions19%

What pLDDT means and how to read it

Function

Deubiquitinating enzyme that removes conjugated ubiquitin from target proteins (PubMed:16316627, PubMed:16339847, PubMed:16472766, PubMed:20595234, PubMed:22347420, PubMed:25404403, PubMed:28604766, PubMed:30514904). Deubiquitinates PDPK1 (PubMed:22347420). Deubiquitinates TRIM21 (PubMed:16316627). Deubiquitinates receptor ADORA2A which increases the amount of functional receptor at the cell surface (PubMed:16339847). Deubiquitinates HAS2 (PubMed:28604766). Deubiquitinates MAVs leading to maintain MAVS protein stability, resulting in increased production of type I interferons (IFN-I) and enhanced antiviral innate immune responses against viral infections (PubMed:39589880). Deubiquitinates…

Subunit structure

Interacts with RB1 (both dephosphorylated and hypophosphorylated forms) (PubMed:11571652). Interacts with RBL1 and RBL2 (By similarity). Interacts with ADORA2A (via cytoplasmic C-terminus); the interaction is direct (PubMed:16339847). Interacts with SART3; recruits USP4 to its substrate PRPF3 (PubMed:20595234)

Subcellular location

Cytoplasm, Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2Y6EX-ray2.4 ÅA/B/C/D/E/F=296-490, A/B/C/D/E/F=765-932
5CTRX-ray3.01 ÅC/D=1-230

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