DisProt: a database of protein disorder

  • Authors:

  • Slobodan Vucetic;Zoran Obradovic;Vladimir Vacic;Predrag Radivojac;Kang Peng;Lilia M. Iakoucheva;Marc S. Cortese;J. David Lawson;Celeste J. Brown;Jason G. Sikes;Crystal D. Newton;A. Keith Dunker

  • Affiliations:

  • Center for Information Science and Technology, Temple University Philadelphia, PA 19122, USA;Center for Information Science and Technology, Temple University Philadelphia, PA 19122, USA;Center for Information Science and Technology, Temple University Philadelphia, PA 19122, USA;Center for Computational Biology and Bioinformatics, Indiana University School of Medicine Indianapolis, IN 46202, USA;Center for Information Science and Technology, Temple University Philadelphia, PA 19122, USA;Laboratory of Statistical Genetics, The Rockefeller University New York, NY 10021, USA;Center for Computational Biology and Bioinformatics, Indiana University School of Medicine Indianapolis, IN 46202, USA;Concurrent Pharmaceuticals 502 W. Office Center Dr, Fort Washington, PA 19034, USA;Department of Biological Sciences, University of Idaho ID 83844, USA;School of Molecular Biosciences, Washington State University Pullman, WA 99164, USA;School of Molecular Biosciences, Washington State University Pullman, WA 99164, USA;Center for Computational Biology and Bioinformatics, Indiana University School of Medicine Indianapolis, IN 46202, USA

  • Venue:
  • Bioinformatics
  • Year:
  • 2005

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Abstract

Summary: The Database of Protein Disorder (DisProt) is a curated database that provides structure and function information about proteins that lack a fixed three-dimensional (3D) structure under putatively native conditions, either in their entirety or in part. Starting from the central premise that intrinsic disorder is an important structural class of protein and in order to meet the increasing interest thereof, DisProt is aimed at becoming a central repository of disorder-related information. For each disordered protein, the database includes the name of the protein, various aliases, accession codes, amino acid sequence, location of the disordered region(s), and methods used for structural (disorder) characterization. If applicable, most entries also list the biological function(s) of each disordered region, how each region of disorder is used for function, as well as provide links to PubMed abstracts and major protein databases. Availability: www.disprot.org Contact: kedunker@iupui.edu