Mapping all cholestasis-related single amino acid substitutions in USP53 (Fig. 2a) on a homology model based on our USP54 structure illustrated that several substituted residues are either part of the above-described zinc fingers (explaining the reduced stability and impaired catalytic activity of the H132Y protein) or are located around the active site (Extended Data Fig. 8a–e). This evidence concerns the gene USP53 and cholestasis.