Heterogeneity was found in annotated variants not only regarding the type and location of amino acid substitutions but also the number and structure of small molecules tested across them, as well as their relative bioactivity compared to WT. These observations reflected the interest in therapeutically targeting disease-relevant variants. In previous sections, it was shown that the majority of proteins have a small amount of variant bioactivity data compared to WT, in particular in proteins with sufficient data for modelling (Figure ). Even in the proteins ). In these cases, the existence of many variants compensated for their data scarcity and still amounted to a relevant variant bioactivity percentage, above 10%. However, for all 13 data-rich proteins, only up to three variantsgenerally the most established clinically relevantcontained more than 500 data points, with some of the remaining variants dropping to as little data as one data point (Supplementary