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This article is part of the supplement: SNP-SIG 2011: Identification and annotation of SNPs in the context of structure, function and disease

Open Access Proceedings

Disease-related mutations predicted to impact protein function

Christian Schaefer12*, Yana Bromberg5, Dominik Achten1 and Burkhard Rost1234

Author Affiliations

1 TUM, Bioinformatics - i12, Informatics, Boltzmannstrasse 3, 85748 Garching/Munich, Germany

2 TUM Graduate School of Information Science in Health (GSISH), Boltzmannstr. 11, 85748 Garching/Munich, Germany

3 Institute of Advanced Study (TUM-IAS), Lichtenbergstr. 2a, 85748 Garching/Munich, Germany

4 Columbia University, Department of Biochemistry and Molecular Biophysics & New York Consortium on Membrane Protein Structure (NYCOMPS), 701 West, 168th Street, New York, NY 10032, USA

5 Department of Biochemistry and Microbiology, School of Environmental and Biological Sciences, Rutgers University, New Brunswick, NJ 08901, USA

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BMC Genomics 2012, 13(Suppl 4):S11  doi:10.1186/1471-2164-13-S4-S11

Published: 18 June 2012

Additional files

Additional file 1:

SIFT predictions. Non-neutral mutations are enriched in a set of disease-causing variants, whereas they are depleted in variants with no known linkage to disease.

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Open Data

Additional file 2:

Mutation and sequence data. Archive of the five different mutant sets used in this study separated by SNAP/SIFT and PhD-SNP predictions including the protein wild type sequences.

Format: ZIP Size: 17.9MB Download file

Open Data