Proteomics approaches that globally quantify changes in protein abundance and phosphorylation are powerful tools to elucidate mechanisms of viral pathogenesis by providing a snapshot of how cellular pathways and processes are rewired upon infection (Johnson et al., 2020). Importantly, the functional outcomes of many phosphorylation events are well annotated, especially for kinases where phosphorylation directly regulates their activity. State-of-the-art bioinformatics approaches can then be employed to readily identify regulated kinases from phosphorylation profiles, many of which are likely to be established drug targets with therapeutic potential (Ochoa et al., 2016, 2020). Here we present a quantitative survey of the global phosphorylation and protein abundance landscape of SARS-CoV-2 infection, map phosphorylation changes to disrupted kinases and pathways, and use these profiles to rapidly prioritize drugs and compounds with the potential to treat SARS-CoV-2 infection.