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IDEAL - Intrinsically Disordered proteins with Extensive Annotations and Literature (RRID:SCR_006027)Copy Citation Copied
URL: http://www.ideal.force.cs.is.nagoya-u.ac.jp/IDEAL/
Proper Citation: IDEAL - Intrinsically Disordered proteins with Extensive Annotations and Literature (RRID:SCR_006027)
Description: IDEAL, Intrinsically Disordered proteins with Extensive Annotations and Literature, is a collection of knowledge on experimentally verified intrinsically disordered proteins (IDPs) or intrinsically disordered regions (IDRs). IDEAL contains manually curated annotations on IDPs in locations, structures, and functional sites such as protein binding regions and posttranslational modification sites together with references and structural domain assignments. Protean segment One of the unique phenomena seen in IDPs is so-called the coupled folding and binding, where a short flexible segment can bind to its binding partner with forming a specific structure to act as a molecular recognition element. IDEAL explicitly annotates these regions as protean segment (ProS) when unstructured and structured information are both available in the region. Access to the data All the entries are tabulated in the list and individual entries can be retrieved by using the search tool at the upper-right corner in this page. IDEAL also provides the BLAST search, which can find homologs in IDEAL. All the information in IDEAL can be downloaded in the XML file.
Abbreviations: IDEAL
Synonyms: IDEAL - Intrinsically Disordered proteins with Extensive Annotations Literature, Intrinsically Disordered proteins with Extensive Annotations and Literature
Resource Type: analysis service resource, data analysis service, data or information resource, production service resource, database, service resource
Defining Citation: PMID:22067451
Keywords: intrinsically disordered protein, protein, intrinsically disordered region, region, location, structure, functional site, protein binding region, binding region, posttranslational modification site, reference, structural domain assignment, blast, homolog, simian virus 40, epstein-barr virus, human herpesvirus 1, residue, protean segment, bio.tools
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