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 [].
STAP2 belongs to the STAP family, whose members are adaptor proteins that play a crucial role in a variety of cellular signal transduction pathways by interacting with signaling or transcriptional molecules. It is composed of a Pleckstrin homology (PH) and a SH2 domain along with several tyrosine phosphorylation sites. It plays an important role in modulating both the innate and adaptive immune systems [, ]. It 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 [].This entry represents the SH2 domain of STAP2.