These data therefore confirm the bioinformatics predictions that Runx1 could be cleaved by caspase-2 at DVPD99↓G. However, the inefficiency of this cleavage and the sensitivity of Runx1 to processing by other caspases argue against the notion that Runx1 is a caspase-2-specific substrate, which could account for the tumour-suppressor activity of this protease. This evidence concerns the gene RUNX1 and neoplasm.