PDGF receptor Phosphorylation sites

The c-terminal sequence of c-fms, downstream of the kinase domain, has little homology to the PDGF receptor (13%). There are two tyrosine residues in this region at positions 924 and 970, the former being preceded by an aspartic acid residue. Feline c-fms is probably phosphorylated at four sites on tyrosine [28] but the mapping of their positions in the primary structure has not yet been published. 

Fig. 2. Presentation of the intracellular domain of the PDGF (platelet-derived growth factor) receptor. The two catalytically active kinase domains are highlighted. Docking sites for SH2 domains are symbolized with a pTyr sidechain. SH2 domains identified to bind to the corresponding phosphorylated tyrosines (numbered on the left) are schematically depicted and labeled on the right...

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