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. Author manuscript; available in PMC: 2021 Oct 1.
Published in final edited form as: Biochim Biophys Acta Mol Cell Res. 2020 Jun 26;1867(10):118786. doi: 10.1016/j.bbamcr.2020.118786

Figure 5. MALDI TOF-MS/MS validation of JAK2 phosphorylation of Y158 on FGF14.

Figure 5.

(A) Homology model of an FGF14 monomer showing potential phosphorylation sites and their corresponding motif in the FGF14–1b sequence (accession number NP_787125). Y158, red, while Y162 is shown as purple. Also showing other predicted phosphorylation sites that are not at the protein:protein interaction interface, including T145, T195, and Y211. (B) MALDI TOF-MS/MS fragmentation spectrum of the phosphopeptide KFKESVFENyYVIYSSMLYR (y = phosphotyrosine), encompassing residues 149–168 of FGF14–1b. The presence of y10 (theoretical m/z of 1293.66, observed m/z of 1293.56) and y11 (theoretical m/z of 1536.69, observed m/z of 1536.63) ions confirms Y158 as the site of phosphorylation (1536.63–1293.56 = 243.07, corresponding to the MW of Y(PO3).