Skip to main content

Thank you for visiting You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.


Identifying phosphorylation-site-specific kinases

Watson, N. A. et al. Nat. Commun. 11, 1684 (2020).

Kinase phosphorylation site dependencies have been studied to identify targets for a kinase of interest; however, identification of kinases that phosphorylate a particular site is not routine. To address this problem, Watson et al. have developed KiPIK (kinase inhibitor profiling to identify kinases). The researchers collected data for a large number of kinase inhibitors on in vitro inhibitory activity against a panel of about 500 recombinant human kinases. This information can be interpreted as inhibition fingerprint for kinases. Next, the researchers obtained cell extracts exhibiting phosphorylation activity of interest and screened against the inhibitors in the panel. Quantification of substrate phosphorylation in the presence of each inhibitor provides the inhibition fingerprint, which can then be matched with the previously determined fingerprints for recombinant kinases. The authors have validated this method on many known phosphorylation sites, as well as made predictions for unknown kinases.

Author information



Corresponding author

Correspondence to Arunima Singh.

Rights and permissions

Reprints and Permissions

About this article

Verify currency and authenticity via CrossMark

Cite this article

Singh, A. Identifying phosphorylation-site-specific kinases. Nat Methods 17, 563 (2020).

Download citation


Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing