The state of a balanced proteome - proteostasis, is crucial for all physiological processes in the organism, the level of individual proteins is determined by the speed of their synthesis, as well as their degradation and availability and transcript levels. One of the important families of phospholipids in cell membranes that interact with proteins is the phosphoinositide family. Each compartment of the membrane contains some of the more characteristic types of phosphoinositides (total of 7 different ones), of which there are 7: phosphatidylinositol-3-monophosphate (PI3P), phosphatidylinositol-4-monophosphate (PI4P), phosphatidylinositol-5-monophosphate (PI5P), phosphatidylinositol-3,4-diphosphate [PI(3, 4)P2], phosphatidylinositol-3,5-diphosphate [PI(3,5)P2], phosphatidylinositol-4,5-diphosphate [PI(4,5)P2] and phosphatidylinositol-3,4,5-triphosphate [PI (3,4,5)P3]. PI3P accounts for approximately 15% of the total phosphoinositides in human cells, accordingly, a detailed analysis of PI3P function as well as the specific FYVE domain that it binds and FYVE domain-containing proteins is provided here. In addition to the FYVE domain, PI3P was found to bind Phox and pleckstrin homologous domains. In this paper, the available transcriptome and proteome data of human and mouse platelets were analyzed for the presence of proteins with the FYVE domain, and a comparison was made between the platelets of these two species. Using the available databases of DepMap and the International Mouse Phenotyping Consortium, the success of creating cell lines with deletions for proteins with the FYVE domain that are highly expressed in the human and mouse proteome was analyzed, as well as the consequences of the lack of selected genes in mice on their lethality and/or hematological phenotype. Furthermore, an overview is given of the mechanism by which PI3P regulates the formation and function of platelets, but also in general how the dysfunction of PI3P formation affects various processes in the cell or in the organism.