Abstract

Protein post-translational modification (PTM) is an important mechanism that is involved in the regulation of protein function. Considering the high-cost and labor-intensive of experimental identification, many computational prediction methods are currently available for the prediction of PTM sites by using protein local sequence information in the context of conserved motif. Here we proposed a novel computational method by using the combination of multiple kernel support vector machines (SVM) for predicting PTM sites including phosphorylation, O-linked glycosylation, acetylation, sulfation and nitration. To largely make use of local sequence information and site-modification relationships, we developed a local sequence kernel and Gaussian interaction profile kernel, respectively. Multiple kernels were further combined to train SVM for efficiently leveraging kernel information to boost predictive performance. We compared the proposed method with existing PTM prediction methods. The experimental results revealed that the proposed method performed comparable or better performance than the existing prediction methods, suggesting the feasibility of the developed kernels and the usefulness of the proposed method in PTM sites prediction.

Highlights

  • Post-translational modifications (PTMs) refer to the covalent addition and enzymatic modifications of protein during or after protein biosynthesis, which play important roles in modifying protein functions and regulating gene expression (Mann & Jensen, 2003; Minguez et al, 2013; Walsh, 2006)

  • Protein post-translational modifications play an important role in multiple biological processes, and have an intimate relationship with many diseases

  • Identification of potential PTM sites is important to promote our understanding of underlying PTM regulatory mechanisms

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Summary

Introduction

Post-translational modifications (PTMs) refer to the covalent addition and enzymatic modifications of protein during or after protein biosynthesis, which play important roles in modifying protein functions and regulating gene expression (Mann & Jensen, 2003; Minguez et al, 2013; Walsh, 2006). There are extensive studies describing experimental validated modifications on S/T/Y sites, such as acetylation, O-linked glycosylation (O-GalNAc, O-GlcNAc), sulfation and nitration Recent studies have explored that aforementioned types of PTM are involved in the majority of cellular activities and are related to various diseases (Huang et al, 2015; Li et al, 2010). In this respect, identification of potential PTM sites is important to understand the underlying molecular mechanisms for basic research and drug development

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