PupStruct: Prediction of Pupylated Lysine Residues Using Structural Properties of Amino Acids.

Journal: Genes
Published Date:

Abstract

Post-translational modification (PTM) is a critical biological reaction which adds to the diversification of the proteome. With numerous known modifications being studied, pupylation has gained focus in the scientific community due to its significant role in regulating biological processes. The traditional experimental practice to detect pupylation sites proved to be expensive and requires a lot of time and resources. Thus, there have been many computational predictors developed to challenge this issue. However, performance is still limited. In this study, we propose another computational method, named PupStruct, which uses the structural information of amino acids with a radial basis kernel function Support Vector Machine (SVM) to predict pupylated lysine residues. We compared PupStruct with three state-of-the-art predictors from the literature where PupStruct has validated a significant improvement in performance over them with statistical metrics such as sensitivity (0.9234), specificity (0.9359), accuracy (0.9296), precision (0.9349), and Mathew's correlation coefficient (0.8616) on a benchmark dataset.

Authors

  • Vineet Singh
    Faculty of Science Technology and Environment, University of the South Pacific, Suva, Fiji.
  • Alok Sharma
    Center for Integrative Medical Sciences, RIKEN Yokohama, Yokohama, 230-0045, Japan.
  • Abdollah Dehzangi
    1] Signal Processing Laboratory, School of Engineering, Griffith University, Brisbane, Australia [2] Institute for Integrated and Intelligent Systems, Griffith University, Brisbane, Australia.
  • Tatushiko Tsunoda
    Laboratory for Medical Science Mathematics, RIKEN Center for Integrative Medical Sciences, Yokohama 230-0045, Japan.