IDEAL

IDEAL is the abbreviation of “Intrinsically Disordered proteins with Extensive Annotations and Literature”.

Structural annotations: Experimentally observed IDRs and structural regions are shown aligned to a protein sequence. Information on functional regions such as protein binding regions and posttranslational modification (PTM) sites and a 3D view of a protein complex are also provided.

Protean Segment (ProS): One of the unique phenomena seen in IDPs is a so-called “coupled folding and binding” process, where a short flexible segment acts as a molecular recognition element and folds into an ordered structure upon binding to its interaction partner. Provided that experimental evidence of unstructured and structured states is reported, such a region is defined as a protean segment (ProS) in IDEAL.

Liquid-Liquid Phase Separation (LLPS): IDPs are recently shown as one of the major factors to induce Liquid-Liquid Phase Separation (LLPS), in which membraneless organelles are formed in the cells to condensate several specific macromolecules. Proteins involved in LLPS are directly linked to their corresponding datasets in publicly available LLPS databases, if they meet some criteria.

Functional annotations: Many of IDPs are involved in signaling pathways and/or transcriptional regulations. The PPI of these IDPs is frequently modulated by PTMs. “Biological Process” provides a diagrammatic (network, or graph) representation of biological events, initiated by PTMs or other triggers, in sequential order.

Access to the data: All the entries are tabulated in the list. A protein of interest can be retrieved by using the search tool in the menu bar (header). “BLAST search” is to help to find similar proteins in IDEAL entries. The datasets are downloadable in XML and RDF format. Functional diagrams are also described in SBGN. For help, see our user manual.