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Proteins are part of the basic building blocks of living organisms. In eukaryotes, they perform a broad range of regulatory functions as part of intracellular signaling pathways and also constitute the extracellular structures (ECM) that are incorporated into the cell nucleus. Given the complexity of the phosphorylation system in cells and the high degree of protein phosphorylation in mammalian cells, it is highly likely that protein phosphorylation plays a major role in intracellular signaling processes. At least several hundred protein kinases are known to exist in mammals. On the other hand, only a few hundred phosphatases are known to exist in this same species. This imbalance between kinases and phosphatases results in the prevalent role of the kinases in phosphorylating the majority of cellular proteins. However, despite the fact that protein phosphorylation is, by far, the most common modification of proteins in mammalian cells, the mechanisms involved in the regulatory phosphorylation of proteins are still poorly understood. Here, we describe the current knowledge about the PA-proteome, which is the phosphatase complement in the cell, including
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