1	DisProt	http://disprot.org	http://www.disprot.org/protein.php?id=%protein%	NULL	The Database of Protein Disorder (DisProt) is a curated database that provides information about proteins that lack fixed 3D structure in their putatively native states, either in their entirety or in part. DisProt is a collaborative effort between Center for Computational Biology and Bioinformatics at Indiana University School of Medicine and Center for Information Science and Technology at Temple University.	http://d2p2.pro/img/logos/DisProt_logo.png
2	IDEAL	http://www.ideal.force.cs.is.nagoya-u.ac.jp/IDEAL	http://idp1.force.cs.is.nagoya-u.ac.jp/IDEAL/idealItem.php?id=%protein%	NULL	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. 	http://d2p2.pro/img/logos/IDEAL_logo.png
3	PhosphoSitePlus	http://www.phosphosite.org	http://www.phosphosite.org/proteinSearchSubmitAction.do?accessionIds=%protein%	NULL	PhosphoSitePlus&reg; (PSP) is an online systems biology resource providing comprehensive information and tools for the study of protein post-translational modifications (PTMs). See <a href="http://www.phosphosite.org/staticAboutPhosphosite.do">About PhosphoSite</a> for more information. All PTM data presented on the D<sup>2</sup>P<sup>2</sup> website is taken from this resource, please cite any original sources of the data.\n<br />\nCite the following reference for any research resulting from the use of this data: <a href="http://nar.oxfordjournals.org/content/40/D1/D261.long">Hornbeck PV. et al. (2012) Nucleic Acids Res. 2012 40:D261-70.</a>	http://d2p2.pro/img/logos/PSP_logo.png
4	SUPERFAMILY	http://supfam.org	NULL	NULL	NULL	http://d2p2.pro/img/logos/SUPFAM_logo.png