Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (SRMS)

Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (SRMS) is a cytoplasmic, non-receptor tyrosine kinase characterized by its absence of two canonical Src family regulatory elements: the C-terminal regulatory tyrosine and N-terminal myristoylation. SRMS phosphorylates substrates such as DOK1, KHDRBS1/SAM68, VIM, and OTUB1, indicating roles in signal transduction, cell growth, cytoskeletal regulation, and potentially in cancer biology. Its activity is regulated by extrinsic signals, such as EGF, and it contributes to positive regulation of the TORC1 signaling pathway. The function and disease roles of SRMS are still being investigated; it is structurally and functionally similar to other Src family kinases, but its unique regulatory features may confer distinct physiological and pathological roles[3][4].

Other names

SRMSSRMS_HUMAN (UniProt designation)Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites

Drugs targeting SRMS or related kinases would generally act as ATP-competitive inhibitors, blocking kinase activity and downstream signal transduction. Inhibition of tyrosine phosphorylation of substrates involved in mTOR (TORC1) signaling and cell survival pathways.