Q8NEZ5: F-box only protein 22 (FBXO22)

F-box only protein 22 (FBXO22) is a 403-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8NEZ5.

Gene
FBXO22
Organism
Homo sapiens
Length
403 residues
Mean pLDDT
86.3
Model
AF-Q8NEZ5-F1 v6
Model created
1 Aug 2025
PDB structures
7

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Model confidence (pLDDT)

The mean pLDDT of this model is 86.3 (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 accurate65%
70 to 90Confident: backbone generally right22%
50 to 70Low: treat with caution7%
Below 50Very low: often disordered regions6%

What pLDDT means and how to read it

Function

Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex that is implicated in the control of various cellular processes such as cell cycle control, transcriptional regulation, DNA damage repair, and apoptosis. Promotes the proteasome-dependent degradation of key sarcomeric proteins, such as alpha-actinin (ACTN2) and filamin-C (FLNC), essential for maintenance of normal contractile function. Acts as a key regulator of histone methylation marks namely H3K9 and H3K36 methylation through the regulation of histone demethylase KDM4A protein levels (PubMed:21768309). In complex with KDM4A, also regulates the abundance of TP53 by targeting methylated…

Subunit structure

Directly interacts with SKP1 and CUL1 (PubMed:21768309, PubMed:22972877). Interacts (via C-terminal) with KDM4A (PubMed:21768309). Interacts with TP53 (PubMed:26868148). Interacts with MTOR; this interaction promotes 'lys-27'-linked ubiquitination of MTOR (PubMed:37979583)

Subcellular location

Cytoplasm, Nucleus, Cytoplasm, myofibril, sarcomere, Z line

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8S7DEM3.2 ÅD=12-403
8S7EEM3.4 ÅB=12-403
8UA3EM3.8 ÅC=1-403
8UA6EM3.9 ÅC=1-403
29HGEM4.0 ÅA=1-403
29HHEM4.2 ÅA=1-403
29HIEM5.9 ÅA=1-403

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