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The intrinsic protein tyrosine kinase activity of the activated FGFR2c receptor leads to multiple phosphorylation events, creating a number of binding sites on its cytoplasmic tail for membrane bound docking proteins to gather intracellular signaling mediators. Two isoforms of FGFR2c generated by alternative splicing and differing only by the presence ("long") or absence ("short") of two amino acid residues at positions 428-429 are equally active in autophosphorylation, but differ in their abilities to interact with downstream targets. Based on sequence alignment, FGFR2 contains all 8 of the cytoplasmic tyrosine residues identified in FGFR1. <br>
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