iPhosT-PseAAC: Identify phosphothreonine sites by incorporating sequence statistical moments into PseAAC

Anal Biochem. 2018 Jun 1:550:109-116. doi: 10.1016/j.ab.2018.04.021. Epub 2018 Apr 25.

Abstract

Among all the post-translational modifications (PTMs) of proteins, Phosphorylation is known to be the most important and highly occurring PTM in eukaryotes and prokaryotes. It has an important regulatory mechanism which is required in most of the pathological and physiological processes including neural activity and cell signalling transduction. The process of threonine phosphorylation modifies the threonine by the addition of a phosphoryl group to the polar side chain, and generates phosphothreonine sites. The investigation and prediction of phosphorylation sites is important and various methods have been developed based on high throughput mass-spectrometry but such experimentations are time consuming and laborious therefore, an efficient and accurate novel method is proposed in this study for the prediction of phosphothreonine sites. The proposed method uses context-based data to calculate statistical moments. Position relative statistical moments are combined together to train neural networks. Using 10-fold cross validation, 94.97% accurate result has been obtained whereas for Jackknife testing, 96% accurate results have been obtained. The overall accuracy of the system is 94.4% to sensitivity value 94% and specificity 94.6%. These results suggest that the proposed method may play an essential role to the other existing methods for phosphothreonine sites prediction.

Keywords: ANN; Cross-validation; Hahn polynomials; Phosphothreonine; Statistical moments.

MeSH terms

  • Phosphoproteins* / chemistry
  • Phosphoproteins* / genetics
  • Phosphorylation
  • Phosphothreonine / chemistry*
  • Sequence Analysis, Protein / methods*
  • Software*

Substances

  • Phosphoproteins
  • Phosphothreonine