Q5XUX0: F-box only protein 31 (FBXO31)

F-box only protein 31 (FBXO31) is a 539-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q5XUX0.

Gene
FBXO31
Organism
Homo sapiens
Length
539 residues
Mean pLDDT
83.1
Model
AF-Q5XUX0-F1 v6
Model created
1 Aug 2025
PDB structures
2

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Model confidence (pLDDT)

The mean pLDDT of this model is 83.1 (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 accurate73%
70 to 90Confident: backbone generally right5%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions21%

What pLDDT means and how to read it

Function

Substrate-recognition component of the SCF(FBXO31) protein ligase complex, which specifically mediates the ubiquitination of proteins amidated at their C-terminus in response to oxidative stress, leading to their degradation by the proteasome (PubMed:39880951). FBXO31 specifically recognizes and binds C-terminal peptides bearing an amide: C-terminal amidation in response to oxidative stress takes place following protein fragmentation (PubMed:39880951). The SCF(FBXO31) also plays a role in G1 arrest following DNA damage by mediating ubiquitination of phosphorylated cyclin-D1 (CCND1), promoting its degradation by the proteasome, resulting in G1 arrest (PubMed:19412162, PubMed:29279382). The…

Subunit structure

Part of a SCF (SKP1-cullin-F-box) protein ligase complex SCF(FBXO31) composed of CUL1, SKP1, RBX1 and FBXO31 (PubMed:16357137, PubMed:19412162, PubMed:31413110, PubMed:39880951). Interacts (when phosphorylated at Ser-33) with CDC20, promoting ubiquitination by the APC/C complex (PubMed:29343641)

Subcellular location

Cytoplasm, Cytoplasm, cytoskeleton, microtubule organizing center, centrosome

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5VZTX-ray2.7 ÅB/D=66-539
5VZUX-ray2.7 ÅB/D=66-539

More AlphaFold highlights

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