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Updated: Jan 2, 2026

Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays
Published on: November 29, 2014
Formator: Predicting Lysine Formylation Sites Based on the Most Distant Undersampling and Safe-Level Synthetic
Abstract:
Lysine formylation is a reversible type of protein post-translational modification and has been found to be involved in a myriad of biological processes, including modulation of chromatin conformation and gene expression in histones and other nuclear proteins. Accurate identification of lysine formylation sites is essential for elucidating the underlying molecular mechanisms of formylation. Traditional experimental methods are time-consuming and expensive. As such, it is desirable and necessary to develop computational methods for accurate prediction of formylation sites. In this study, we propose a novel predictor, termed Formator, for identifying lysine formylation sites from sequences information. Formator is developed using the ensemble learning (EL) strategy based on four individual support vector machine classifiers via a voting system. Moreover, the most distant undersampling and Safe-Level-SMOTE oversampling techniques were integrated to deal with the data imbalance problem of the training dataset. Four effective feature extraction methods, namely bi-profile Bayes (BPB), k-nearest neighbor (KNN), amino acid physicochemical properties (AAindex), and composition and transition (CTD) were employed to encode the surrounding sequence features of potential formylation sites. Extensive empirical studies show that Formator achieved the accuracy of 87.24 and 74.96 percent on jackknife test and the independent test, respectively. Performance comparison results on the independent test indicate that Formator outperforms current existing prediction tool, LFPred, suggesting that it has a great potential to serve as a useful tool in identifying novel lysine formylation sites and facilitating hypothesis-driven experimental efforts.
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