Ubiquitination of proteins is required for their proteasomal degradation and plays an important role in the progression of cancer.[23] Immunoprecipitation of EZH2 followed by antiubiquitin immunoblotting demonstrated that ubiquitinated EZH2 was markedly increased in SS‐DUXAP9‐transfected cells, whereas EZH2 ubiquitination was significantly decreased in DUXAP9‐overexpressing cells (Figure 7G–I). This evidence concerns the gene DUXAP9 and cancer.