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Recent studies have shown that, in addition to its role as an adhesion receptor, platelet endothelial cell adhesion molecule 1/CD31 becomes phosphorylated on tyrosine residues Y⁶⁶³ and Y⁶⁸⁶ and associates with protein tyrosine phosphatases SHP-1 and SHP-2. In this study, we screened for additional proteins which associate with phosphorylated platelet endothelial cell adhesion molecule 1, using surface plasmon resonance. We found that, besides SHP-1 and SHP-2, platelet endothelial cell adhesion molecule 1 binds the cytoplasmic signalling proteins SHIP and PLC-γ1 via their Src homology 2 domains. Using two phosphopeptides, NSDVQpY⁶⁶³TEVQV and DTETVpY⁶⁸⁶SEVRK, we demonstrate differential binding of SHP-1, SHP-2, SHIP and PLC-γ1. All four cytoplasmic signalling proteins directly associate with cellular platelet endothelial cell adhesion molecule 1, immunoprecipitated from pervanadate …