In conclusion, together with recently reported studies employing succinate production and computational methods coupled with cellular studies,[16, 19, 20] the lysyl‐hydroxylation based assays and results presented here imply JMJD6 is amenable to inhibition by small‐molecules, in particular 2OG competitors, including some clinically used compounds.[16, 19] Future work can be directed towards optimisation of the 2OG competing inhibitors described here to make potent and selective JMJD6 inhibitors for use in functional assignment and target validation work on JMJD6 for cancer treatment. Here, JMJD6 is linked to cancer.