title: Modularity of intrinsic disorder in the human proteome.
abstract: Predicting regions of disorder has become of increasing interest when determining protein structure and function. With approximately 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.
authors.affiliation: Department of Biology, Centre for Genomics and Systems Biology, New York University, NY, USA.
authors.forename: Melissa M
authors.initials: MM
authors.lastname: Pentony
authors.forename: David T
authors.initials: DT
authors.lastname: Jones
mesh_terms: D017398:Alternative Splicing; D006801:Humans; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry / Q000235:genetics; D020543:Proteome / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D011506:Proteins; D020543:Proteome