| IDEAL | | Intrinsically Disordered proteins with Extensive Annotations and Literature | | http://www.ideal.force.cs.is.nagoya-u.ac.jp/IDEAL/ | | June 29th, 2017 | | 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 post-translational modification sites together with references and structural domain assignments. IDEAL also illustrates protein-protein interaction networks. | | http://idp1.force.cs.is.nagoya-u.ac.jp/IDEAL/idealNetwork.php?id=IID00001 | | Primary | | Free to all users | IDEAL: Intrinsically Disordered proteins with Extensive Annotations and Literature.
Fukuchi S, Sakamoto S, Nobe Y, Murakami SD, Amemiya T, Hosoda K, Koike R, Hiroaki H, Ota M.
Nucleic Acids Res. 2012 Jan;40(Database issue):D507-11.
IDEAL in 2014 illustrates interaction networks composed of intrinsically disordered proteins and their binding partners.
Fukuchi S, Amemiya T, Sakamoto S, Nobe Y, Hosoda K, Kado Y, Murakami SD, Koike R, Hiroaki H, Ota M.
Nucleic Acids Res. 2014 Jan;42(Database issue):D320-5.
| | Protein-Protein Interactions | | | Genes / Proteins: | 838 | | Last Content Update: | March 17th, 2017 |
| | Homo sapiens | |  |
|
|
