Src kinase-associated phosphoprotein 2 (SKAP2)

SKAP2 (Src kinase-associated phosphoprotein 2) is an adaptor protein predominantly expressed in hematopoietic cells, including neutrophils, macrophages, and B cells. It contains three functional domains: a dimerization domain (DM) promoting self-association, a pleckstrin homology (PH) domain for lipid/membrane interactions, and an SH3 domain for binding Src family kinases and other interactors. SKAP2 regulates integrin-mediated actin cytoskeleton rearrangement and cluster formation, controlling adhesive and effector functions such as phagocytosis, reactive oxygen species (ROS) generation, and antibody-dependent cellular cytotoxicity (ADCC) in immune cells. Loss or deficiency of SKAP2 impairs these effector responses. SKAP2 is also implicated in inhibition of tumor invasiveness and modulation of signal transduction pathways relevant to cancer and inflammatory disease. While SKAP2 has no known direct drug, its role in immune signaling makes it a candidate for further therapeutic exploration.

Other names

Src kinase-associated phosphoprotein 2SKAP2PRAPRA70SAPSSCAP2SKAP-55HOMSKAP55RSKAP-HOMSKAP55 homologPyk2/RAFTK-associated proteinRetinoic acid-induced protein 70Src family-associated phosphoprotein 2Src kinase-associated phosphoprotein of 55-related proteinSrc-associated adapter protein with PH and SH3 domainsFyn-associated phosphoprotein SKAP55 homologue

None assigned directly; as there are no approved drugs specifically targeting SKAP2, assigned mechanisms are theoretical and would relate to interruption/modulation of adaptor-mediated immune signaling.