STAP1 is a signal-transducing adaptor protein. It is composed of a Pleckstrin Homology (PH) and SH2 domains along with several tyrosine phosphorylation sites. STAP-1 is an orthologue of BRDG1 (also known as BCR downstream signaling 1). STAP1 protein functions as a docking protein acting downstream of Tec tyrosine kinase in B cell antigen receptor signaling. The protein is phosphorylated by Tec and participates in a positive feedback loop, increasing Tec activity []. STAP-1 has been shown to interact with STAT5 []. This entry represents the SH2 domain of STAP1.In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites [, , ].
STAP1 and STAP2 are signal-transducing adaptor proteins. They contain Pleckstrin Homology (PH) and SH2 domains along with several tyrosine phosphorylation sites.STAP1 functions as a docking protein acting downstream of Tec tyrosine kinase in B cell antigen receptor signaling. It is phosphorylated by Tec and participates in a positive feedback loop, increasing Tec activity []. STAP-1 has been shown to interact with STAT5 []. STAP2 is a substrate of breast tumour kinase, an Src-type non-receptor tyrosine kinase that mediates the interactions linking proteins involved in signal transduction pathways [].
