IDEAL: Intrinsically Disordered proteins with Extensive Annotations and Literature

Abstract

IDEAL, Intrinsically Disordered proteins with Extensive Annotations and Literature (http://www.ideal.force.cs.is.nagoya-u.ac.jp/IDEAL/), is a collection of knowledge on experimentally verified intrinsically disordered proteins. IDEAL contains manual annotations by curators on intrinsically disordered regions, interaction regions to other molecules, post-translational modification sites, references and structural domain assignments. In particular, IDEAL explicitly describes protean segments that can be transformed from a disordered state to an ordered state. Since in most cases they can act as molecular recognition elements upon binding of partner proteins, IDEAL provides a data resource for functional regions of intrinsically disordered proteins. The information in IDEAL is provided on a user-friendly graphical view and in a computer-friendly XML format.

Figure 1.

IDEAL annotation for catenin β-1. The identifier, IID, protein name, source organism and the link to UniProt are shown below the blue bar which contains the search tool ([1]). Bars [2] and [3] show a summary of the annotated regions using the ‘at least rule’ and ‘majority rule’ criteria. Ordered, disordered and conflict regions are colored in blue, red and orange, respectively. The inner boxes (A) and (B) show a detailed breakdown of the regions in [2] and [3], respectively. These diagrams appear by clicking on the bars. The inner box (B) provides the link to the experimental evidence and the technique supporting the order/disorder regions. ProSs are represented in section [4] as the green bars, which can be expanded by clicking to reveal the inner box (C). Interaction sites and post-translational modification sites are shown in section [5]. These bars expand to show the detailed information in the inner box (D). The bars in section [6] show the domain assignments.