Drugs that function through allosteric inhibition of kinase signaling represent a promising approach for the targeted discovery of therapeutics. The majority of developed allosteric kinase inhibitors are characterized as type III and IV inhibitors that show good kinome selectivity but generally lack the subtype selectivity of same kinase family. Recently allosteric inhibitors have been developed that bind outside the catalytic kinase domain with high selectivity for specific kinase subtypes. Allosteric inhibitors that bind to the pseudokinase domain of pseudokinase or the extracellular domain of receptor tyrosine kinases are reviewed. We also review recent developments in the field of allosteric kinase inhibitors including examples of proteolysis targeting chimeras, and highlight the unique binding modes for each type of inhibitors and address future opportunities in this area. Allosteric inhibition of kinase signaling is a promising approach for the targeted discovery of therapeutics with exceptional selectivity and the ability of overcoming the acquired resistance of the orthosteric ATP‐binding site inhibitors. The recent developments of allosteric kinase inhibitors that bind outside the catalytic kinase domain further warrant considerable interest and offer unique opportunities in this area.