Comparison of murine and human phosphatome identifies three protein folds in protein phosphatase catalytic domains

초록

Reversible protein phosphorylation and dephosphorylation are two major processes for functional regulation of proteins which are carried out by two different protein superfamilies, namely protein kinases and protein phosphatases. While the importance of protein kinases is well known it is only recently that the importance of protein phosphatases in activation/deactivation of proteins became apparent. Here we report a catalog of mouse and rat protein phosphatases and compared it with human protein phosphatases. We identified 177 and 176 protein phosphatases in mouse and rat respectively and compared these genes with 179 protein phosphatases in human. We found 171 protein phosphatases in mouse and rat are orthologous to Human. Furthermore, we determined the three dimensional structure of protein phosphatase catalytic domains of individual phosphatases and constructed the three dimensional map of protein phosphatases using modeled structures. We found that the protein phosphatase catalytic domains existed in three different structural folds. Thus we could divide these proteins into three different classes on the basis of three-dimensional map of protein phosphatase catalytic domains. We found that the map provides a complete view of the major folds of the protein phosphatase catalytic domains that are highly family specific.