Kirill E Medvedev1, Jimin Pei2, Nick V Grishin1,3,4. 1. Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX, 75390, USA. 2. McDermott Center for Human Growth and Development, University of Texas Southwestern Medical Center, Dallas, TX, 75390, USA. 3. Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX, 75390, USA. 4. Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, TX, 75390, USA.
Abstract
MOTIVATION: Intrinsically disordered proteins (IDPs) are involved in numerous processes crucial for living organisms. Bias in amino acid composition of these proteins determines their unique biophysical and functional features. Distinct intrinsically disordered regions (IDRs) with compositional bias play different important roles in various biological processes. IDRs enriched in particular amino acids in human proteome have not been described consistently. RESULTS: We developed DisEnrich-the database of human proteome IDRs that are significantly enriched in particular amino acids. Each human protein is described using gene ontology (GO) function terms, disorder prediction for the full-length sequence using three methods, enriched IDR composition and ranks of human proteins with similar enriched IDRs. Distribution analysis of enriched IDRs among broad functional categories revealed significant overrepresentation of R- and Y-enriched IDRs in metabolic and enzymatic activities and F-enriched IDRs in transport. 75% of functional categories contain IDPs with IDRs significantly enriched in hydrophobic residues that are important for protein-protein interactions. AVAILABILITY: The database is available at http://prodata.swmed.edu/DisEnrichDB/. SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online.
MOTIVATION: Intrinsically disordered proteins (IDPs) are involved in numerous processes crucial for living organisms. Bias in amino acid composition of these proteins determines their unique biophysical and functional features. Distinct intrinsically disordered regions (IDRs) with compositional bias play different important roles in various biological processes. IDRs enriched in particular amino acids in human proteome have not been described consistently. RESULTS: We developed DisEnrich-the database of human proteome IDRs that are significantly enriched in particular amino acids. Each human protein is described using gene ontology (GO) function terms, disorder prediction for the full-length sequence using three methods, enriched IDR composition and ranks of human proteins with similar enriched IDRs. Distribution analysis of enriched IDRs among broad functional categories revealed significant overrepresentation of R- and Y-enriched IDRs in metabolic and enzymatic activities and F-enriched IDRs in transport. 75% of functional categories contain IDPs with IDRs significantly enriched in hydrophobic residues that are important for protein-protein interactions. AVAILABILITY: The database is available at http://prodata.swmed.edu/DisEnrichDB/. SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online.
Authors: Zhenling Peng; Jing Yan; Xiao Fan; Marcin J Mizianty; Bin Xue; Kui Wang; Gang Hu; Vladimir N Uversky; Lukasz Kurgan Journal: Cell Mol Life Sci Date: 2014-06-18 Impact factor: 9.261
Authors: Scott L Crick; Murali Jayaraman; Carl Frieden; Ronald Wetzel; Rohit V Pappu Journal: Proc Natl Acad Sci U S A Date: 2006-10-30 Impact factor: 11.205