TBC1 domain family member 10C (TBC1D10C)

TBC1 domain family member 10C (TBC1D10C), also known as Carabin and EPI64C, is an enzyme belonging to the TBC domain family of GTPase-activating proteins (GAPs)[3][4][1]. It contains an N-terminal GAP domain that inhibits the small GTPases Ras and Rab35, and a C-terminal domain that binds and inhibits calcineurin, a key calcium/calmodulin-regulated phosphatase[1][3][4]. TBC1D10C acts as a negative regulator of Ras and calcineurin signaling pathways and thereby modulates lymphocyte activation, cell spreading, and phagocytosis, particularly in immune cells such as CD8 and CD4 T cells and macrophages[1][2][3]. It serves as a cytoskeletal functional linker and its deficiency has been linked to enhanced CD8 T-cell anti-tumor responses and altered autoimmune risk, suggesting disease relevance in cancer and immunological disorders[2][3]. While essential for negative regulation of immune activation, no drugs have yet been described that directly target TBC1D10C[3].

Other names

CarabinFLJ00332EPI64C

Not applicable (no drugs directly target this protein as of current knowledge); endogenous mechanism is inhibition of Ras and calcineurin signaling, and negative regulation of CD8 T cell activation via NF-κB pathway