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One extremely harmful lesion is the double\u2010strand break (DSB), which activates a massive signaling network \u2013 the DNA damage response (DDR). The chief activator of the DSB response is the ATM protein kinase, which phosphorylates numerous key players in its various branches. Recent phosphoproteomic screens have extended the scope of damage\u2010induced phosphorylations beyond the direct ATM substrates. We review the evidence for the involvement of numerous other protein kinases in the DDR, obtained from documentation of specific pathways as well as high\u2010throughput screens. The emerging picture of the protein phosphorylation landscape in the DDR broadens the current view on the role of this protein modification in the maintenance of genomic stability. Extensive cross\u2010talk between many of these protein kinases forms an interlaced signaling network that spans numerous cellular processes. 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