Research Article
Modularity of intrinsic disorder in the human proteome†
Melissa M. Pentony,
David T. Jones,
Melissa M. Pentony
Department of Biology, Centre for Genomics and Systems Biology, New York University, New York
Search for more papers by this authorCorresponding Author
David T. Jones
Bioinformatics Group, Department of Computer Science, University College London, London, United Kingdom
Bioinformatics Group, Department of Computer science, University College London, London, United Kingdom===Search for more papers by this authorMelissa M. Pentony,
David T. Jones,
Melissa M. Pentony
Department of Biology, Centre for Genomics and Systems Biology, New York University, New York
Search for more papers by this authorCorresponding Author
David T. Jones
Bioinformatics Group, Department of Computer Science, University College London, London, United Kingdom
Bioinformatics Group, Department of Computer science, University College London, London, United Kingdom===Search for more papers by this author†
The authors state no conflict of interest.
Abstract
Predicting regions of disorder has become of increasing interest when determining protein structure and function. With ∼33% of eukaryotic proteins having significant disordered regions, and an increasing occurrence of disorder in higher organisms, an analysis of the importance of disorder from an evolutionary perspective was clearly warranted. Focusing on the human proteome, we have studied how abundant disorder is and its relevance to protein function and structure. We have shown that disordered regions frequently appear to be independent functional units, and judged by complete association to certain protein domains, may be evolutionarily conserved. Our work also supports previous analyses on association between disorder and alternate splicing and provides support for the modularity of disorder by showing that with respect to splicing events, disordered regions frequently appear to be spliced as whole units. Proteins 2010. © 2009 Wiley-Liss, Inc.
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