Modern advances in systems biology and proteomics have increased interest in studying the role of post-translational modification (PTM) of proteins in pathology development mechanisms [Sharma]. The role in the implementation of biological activity of the protein has been found to be due to the three-dimensional (3D) structure and folding features [Díaz-Villanueva]. However, the modification of amino acid residues makes a significant contribution to the structural and functional diversity of proteins [Karve]. PTMs produce a significant effect on a variety of cellular processes (including, but not limited to, DNA reparation, signal transduction, energy generation, and consumption, etc.) through regulation of protein activities and determining supramolecular interactions [Vidal]. In this regard, attempts have been made to determine the role of PTM protein in the development of various pathologies [Karve]. Direct regulation of enzymes with diverse mechanisms is typically accomplished through the dynamic utilization of PTMs. Signal transducers responsible for the mobility of PTMs are guided the same way, thus, balancing and driving the comprehensive network of intracellular signal exchange in response to internal and external stimuli [Martín-Bernabé]. Generally, identification of a specific PTM or, more commonly, their profile in a large-scale proteomic study is intended to associate them with pathophysiological mechanisms [Hitosugi].

pssKB is a computational approach in which high-throughput analysis for characterization of supersecondary strucuture with PTM, associated with metabolic reprograming, can be improved to prognostic value of wide range of diseases and bring a new knowledge of pathogenesis.