IDEAL

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IDEAL

Intrinsically Disordered proteins with Extensive Annotations and Literature

What is IDEAL ?
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.

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. The help page solves questions in browsing IDEAL.


System Requirements
In order to use this website safely and comfortably, we recommend the use of the following browsers and versions:
Windows Internet Explorer 9.0, Firefox 8.0, Safari 5.0, Google Chrome 16.0
Macintosh Safari 5.0, Firefox 8.0
Statistics
19/Dec/2012: 56 anntations uploaded.
Sataistics of the current IDEAL.
Number of Entry261
Number of Entry containing ProS121
Number of Total residues172,517
Number of Disordered residues12,517
Number of Ordered residues50,499
Number of Conflict residues6,793
Number of Unknown residues102,708
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


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


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