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SLP76 (SH2 domain containing leukocyte protein of 76 kDa) is a hematopoietic cell-specific adaptor protein that is crucial for T-cell receptor (TCR) signaling, hemostasis and platelet function. TCR ligation and fibrinogen binding to integrin alpha 2 beta 3 stimulates the phosphorylation of the tyrosine residues in the amino terminus, and facilitates SLP76 binding to the SH2 domain of Vav, which can activate JNK. SLP76 also comprises a proline-rich domain region that associates with the SH3 domain of Grb2 linking SLP76 to the Ras to Raf to ERK1 & 2 signaling pathway, LAT, PLC gamma, Fyn-binding protein (SLAP130), the SH2 containing phosphatase 1 and Nck, which mediates the regulation of cytoskeletal actin polymerization. Phosphorylation of tyrosine 145 has been shown to be important for optimal SLP76 function.