Post-translational modifications (PTMs) are an important source of protein regulation; they fine-tune the function, localization, and interaction with other molecules of the majority of proteins and are partially responsible for their multifunctionality. PTMs increase the functional diversity of the proteome by the covalent addition of functional groups or proteins, proteolytic cleavage of regulatory subunits, or degradation of entire proteins. These modifications include phosphorylation, glycosylation, ubiquitination, methylation, acetylation, palmitoylation, sumoylation, and succinylation and influence almost all aspects of normal cell biology and pathogenesis. Usually, proteins have several potential modification sites, and their patterns of occupancy are associated with certain functional states. These patterns imply cross talk among PTMs within and between proteins, the majority of which are still to be discovered. Therefore, a lots of works have been done by bio-scientist in the form of wit lab research as well as computational work, numbers of well-known databases have been published such as, Phospho.ELM, http://phospho.elm.eu.org/about.html. PTMD http://ptmd.biocuckoo.org/, etc. To know more about, we have provided 53 PTMs databases of eight categories on a simple and fast way to find, user can search by clicking on the name or picture of the categories or search the name in the above search query.