Autocatalytic phosphorylation of FGFR2c Authored: de Bono, B, 2007-01-10 10:27:18 EC Number: 2.7.10 Pubmed11294897 Pubmed1379698 Pubmed1656221 Pubmed1697263 Pubmed8622701 Reactome Database ID Release 43190413 Reactome, http://www.reactome.org ReactomeREACT_9432 Reviewed: Mohammadi, M, 2007-02-06 21:44:35 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> has a Stoichiometric coefficient of 16 Activated FGFR2c homodimer bound to FGF FGFR2c homodimer bound to FGF