Autocatalytic phosphorylation of FGFR3 cysteine mutants Although each of FGFR3 R248C, S249C, G370C, S371C and Y373C have been shown to undergo ligand-independent dimerization and receptor autophosphorylation, there is conflicting evidence about which mutants also show increased phosphorylation upon ligand stimulation. Mutants showed elevated levels of ligand-independent MAPK pathway activation and supported expression of an in vivo reporter gene (d'Avis, 1998; Adar, 2009). Authored: Rothfels, K, 2012-02-09 EC Number: 2.7.10 Edited: Rothfels, K, 2012-05-16 Pubmed12009017 Pubmed9438390 Reactome Database ID Release 432012082 Reactome, http://www.reactome.org ReactomeREACT_120832 Reviewed: Ezzat, S, 2012-05-15 has a Stoichiometric coefficient of 12 FGFR3 cysteine mutant dimers Activated FGFR3 cysteine mutants