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. 2017 Mar 16;7:44637. doi: 10.1038/srep44637

Figure 4. SOS2 phosphorylates EIN3 in vitro.

Figure 4

(a) Putative sites in EIN3 phosphorylated by Ser/Thr kinase, as predicted by NetPhos (http://www.cbs.dtu.dk/ services/NetPhos/). In this prediction, nine amino acids (Ser35, Thr42, Ser83, Thr174, Ser285, Ser325, Ser429, Thr592, Ser606) are potential sites phosphorylated by Ser/Thr protein kinases. (b) Phosphorylation of EIN3 by protein kinase SOS2 in vitro. (c–e) Phosphorylation EIN3 fragments (c), EIN3 fragments with point mutations (d) and full length EIN3 with point mutations (e) by protein kinase SOS2 in vitro. Numbers (1–70, 71–141, 142–220, 221–314, 315–628, 326–538, 430–605, 593–628) indicate GST-EIN3 fragments with corresponding EIN3 sequences. S35A, T42A, S325A and S606A indicate mutation of Ser/Thr to Ala. STA indicates double mutation of Ser35 and Thr42 to Ala. The uncropped images are shown in Supplementary Fig. S4.