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Russell's viper (Daboia russelii) is an important member of the Viperidae family which is widely distributed across Southern Asia including India. Russell's viper venom (RVV) is indisputably a potent mixture of various toxic and nontoxic components that have evolved to interfere with vital physiological processes like coagulation and fibrinolysis. Many of these components are metallo-or serine proteinases. Venoms from the snakes of Viperidae family are reported to be rich in proteinases which contributes to hemostatic alterations in the victims and is also responsible for tissue-specific hemorrhagic effects. However, till date, not many proteinases have been reported from RVV. In this brief review, the currently available data on the structural and functional attributes of RVV proteinases have been focused and summarized. The pathophysiological significance and the therapeutic/ diagnostic application(s) of the identified RVV proteinases have also been discussed. It is relevant to note that a more detailed analysis of the entire complexity of RVV proteinases will contribute to the better understanding of their role in Russell's viper envenomation and subsequent antivenom therapy. Most importantly, novel RVV proteinases can also be explored for their usefulness in the development of diagnostic/therapeutic agents to deal with life-threatening diseases.