Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2007 Jan;35(Database issue):D786-93.
doi: 10.1093/nar/gkl893. Epub 2006 Dec 1.

DisProt: the Database of Disordered Proteins

Megan Sickmeier  1 , Justin A Hamilton, Tanguy LeGall, Vladimir Vacic, Marc S Cortese, Agnes Tantos, Beata Szabo, Peter Tompa, Jake Chen, Vladimir N Uversky, Zoran Obradovic, A Keith Dunker
Affiliations

DisProt: the Database of Disordered Proteins

Megan Sickmeier et al. Nucleic Acids Res. 2007 Jan.

Abstract

The Database of Protein Disorder (DisProt) links structure and function information for intrinsically disordered proteins (IDPs). Intrinsically disordered proteins do not form a fixed three-dimensional structure under physiological conditions, either in their entireties or in segments or regions. We define IDP as a protein that contains at least one experimentally determined disordered region. Although lacking fixed structure, IDPs and regions carry out important biological functions, being typically involved in regulation, signaling and control. Such functions can involve high-specificity low-affinity interactions, the multiple binding of one protein to many partners and the multiple binding of many proteins to one partner. These three features are all enabled and enhanced by protein intrinsic disorder. One of the major hindrances in the study of IDPs has been the lack of organized information. DisProt was developed to enable IDP research by collecting and organizing knowledge regarding the experimental characterization and the functional associations of IDPs. In addition to being a unique source of biological information, DisProt opens doors for a plethora of bioinformatics studies. DisProt is openly available at http://www.disprot.org.

PubMed Disclaimer

Figures

Figure 1
Figure 1
DisProt screen captures. (A) protein display for DP000039, Non-histone chromosomal protein HMG-17, and (B) bibliography query page.
Figure 2
Figure 2
The number of papers tallied by year referencing protein disorder that are included in the searchable bibliography of DisProt.
Figure 3
Figure 3
Simplified IDEF1X representation of the DisProt database structure. Boxes with round edges represent tables with at least one foreign key. Dashed lines with an oval at one end and a cross at the other represent mandatory relationships (not null foreign keys), plane lines with an oval at one end and a cross at the other represent identifying relationship (foreign keys, possibly null, for which the field names in the tables are identical), dashed lines with an oval at both ends represent non-identifying optional relationships (foreign keys, possibly null, for which the field names are not identical).
See this image and copyright information in PMC

References

    1. Fischer E. Einfluss der configuration auf die wirkung derenzyme. Ber. Dt. Chem. Ges. 1894;27:2985–2993.
    1. Koshland D.E., Jr, Ray W.J., Jr, Erwin M.J. Protein structure and enzyme action. Fed. Proc. 1958;17:1145–1150. - PubMed
    1. Xie L., Bourne P.E. Functional coverage of the human genome by existing structures, structural genomics targets, and homology models. PLoS. Comput. Biol. 2005;1:e31. - PMC - PubMed
    1. Landsteiner D.P. The Specificity of Serological Reactions. New York: Dover; 1936.
    1. Pauling L. A theory of the structure and process of formation of antibodies. J. Am. Chem. Soc. 1940;62:2643–2657.

Publication types