IDEAL

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IDEAL provides 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.

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.

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. The help page solves questions in browsing IDEAL.

If you have questions or comments, please send e-mail to .

IDEAL development team
Satoshi Fukuchi, Ph. D. Maebashi Institute of Technology
Motonori Ota, Ph. D. Nagoya University

System Requirements
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References
S. Fukuchi, S. Sakamoto, Y. Nobe, S. D. Murakami, T. Amemiya, K. Hosoda, R. Koike, H. Hiroaki and M. Ota.
"IDEAL: Intrinsically Disordered proteins with Extensive Annotations and Literature".
2012, Nucleic Acids Res., 40, D507-D511.
PMID: 22067451, DOI: 10.1093/nar/gkr884

Funding
IDEAL is supported by Grant-in-Aid for Scientific Research on Innovative Areas of "Target recognition and expression mechanism of intrinsically disordered protein"