Autocatalytic phosphorylation of FGFR1b Authored: de Bono, B, 2007-01-10 10:27:18 EC Number: 2.7.10 Pubmed1379698 Pubmed16507368 Pubmed1656221 Pubmed8622701 Reactome Database ID Release 43190427 Reactome, http://www.reactome.org ReactomeREACT_9493 Reviewed: Mohammadi, M, 2007-02-06 21:44:35 Studies have mapped 8 tyrosine residues in the cytoplasmic domain of FGFR1 that are important for signaling. Autophosphorylation of residues 653 and 654, located in the activation loop of the kinase, is necessary to maintain the receptor in the active state. Phosphorylation of other tyrosine residues by the intrinsic protein tyrosine kinase activity of the activated receptor creates binding sites on its cytoplasmic tail for membrane bound docking proteins to gather intracellular signaling mediators. has a Stoichiometric coefficient of 14 Activated FGFR1b homodimer FGFR1b homodimer bound to FGF