LAUSR

Understanding molecular mechanisms involved in calcium-protein interactions and modeling corresponding docking rely on the accurate identification of calcium-binding residues (CaBRs). The defects of experimentally annotating protein functions enhances the development of computational approaches that correctly identify calcium-binding interactions. Studies have reported that current methods severely cross-predict residues that interact with other types of molecules (e.g., nucleic acids, proteins, and small ligands) as CaBRs. In this study, a novel predictor named SCAMPER (Selective CAlciuM-binding PrEdictoR) is proposed for the accurate and specific prediction of CaBRs. SCAMPER is designed using newly compiled dataset with complete UniProt sequences and annotations, which include calcium-binding, nucleic acid-binding, protein-binding, and small ligand-binding residues. We use a novel designed two-layer scheme to perform predictions as well as penalize cross-predictions. Empirical tests on an independent test dataset reveals that the proposed method significantly outperforms state-of-the-art predictors. SCAMPER is proved to be capable of distinguishing CaBRs from different types of metal-ion binding residues. We further perform CaBRs predictions on the whole human proteome, and use the results to hypothesize calcium-binding proteins (CaBPs). The latest experimental verified CaBPs and GO analysis prove the accuracy of our predictions. We implement the proposed method and share the data at http://www.inforstation.com/webservers/SCAMPER/.