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Intrinsic disorder is one of the many traits that can affect the functionality of multiple naturally occurring proteins in biological systems. This thesis reports on the latest findings on mechanisms that intrinsically disordered proteins or intrinsically disordered regions utilize in specific recognition at the molecular level. Here, the general characteristics of intrinsically disordered proteins are summarized, along with the extent of their abundance throughout different lifeforms and the variety of their molecular recognition mechanisms depicted on specific examples. Furthermore, this thesis focuses on protein transitions between ordered and disordered states induced by interaction with its' binding partner. In the last two chapters, characteristic features of intrinsically disordered proteins are described, and attention is paid to the way these features influence cellular signaling pathways such as interactional promiscuity, the role of signaling hubs, alternative splicing, and post- translational modification.