Motivation: Modern techniques have produced many sequence annotation databases and protein structure portals, but these web resources are rarely integrated in ways that permit straightforward exploration of protein functional residues and their co-localization. Results: We have created the AMASS Database, which maps 1D sequence annotation databases to 3D protein structures with an intuitive visualization interface. Our platform also provides an analysis service that screens mass spectrometry sequence data for posttranslational modifications that reside in functionally-relevant locations within protein structures. The system is built upon the premise that functional residues such as active sites, cancer mutations, and post-translational modifications within proteins may co-localize and share common functions.
['Clinton J. Mielke', 'Lawrence J. Mandarino', 'Valentin Dinu']
AMASS: A Database for Investigating Protein Structures