Extended Data Fig. 8: DeKinomics study of TYRO3. | Nature Chemical Biology

Extended Data Fig. 8: DeKinomics study of TYRO3.

From: DeKinomics pulse-chases kinase functions in living cells

Extended Data Fig. 8: DeKinomics study of TYRO3.

a, Sequence alignment for locating conserved catalytic lysine residue in TYRO3. Asterisks indicate the conserved residues. b, Confocal immunofluorescence imaging of exogenous TYRO3-K550ONPK (n = 3). Scale bars: 5 μm. c, Heatmap indicating TYRO3 activation induced TYRO3 autophosphorylation. d, The fuzzy c-means clustering of significantly changed pTyr sites upon TYRO3 activation. e, Venn diagram indicating that TYRO3 candidate substrates were determined with 2 criteria: pTyr sites significantly changed in 0–60 sec (ANOVA) and were in cluster 1 with membership > 0.7 in fuzzy c-means clustering.

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