Aims to serve as a starting point for functional and structural analysis of interactions between intrinsically Disordered Proteins (IDPs). MFIB is based on the integration of structural and sequence annotation coupled with the results of an extensive manual literature survey. The data contained in MFIB provide a wide coverage of possible IDP-IDP interactions in many ways. Its entries cover the majority of possible oligomeric compositions from dimers to hexamers, including both hetero- and homo-oligomers.
Provides an extensive collection of interactions formed by a disordered protein region and one or more ordered protein partners. DIBS marks proteins as disordered if a closely homologous protein was described to lack intrinsic structure. This application incorporates annotations about functional motifs in disordered partners, further connecting the two complementary models of such interactions. It also serves as the basis for a more complete understanding of Intrinsically Disordered Proteins (IDPs) interactions.