iAcety–SmRF: Identification of Acetylation Protein by Using Statistical Moments and Random Forest

Abstract

Acetylation is the most important post-translation modification (PTM) in eukaryotes; it has manifold effects on the level of protein that transform an acetyl group from an acetyl coenzyme to a specific site on a polypeptide chain. Acetylation sites play many important roles, including regulating membrane protein functions and strongly affecting the membrane interaction of proteins and membrane remodeling. Because of these properties, its correct identification is essential to understand its mechanism in biological systems. As such, some traditional methods, such as mass spectrometry and site-directed mutagenesis, are used, but they are tedious and time-consuming. To overcome such limitations, many computer models are being developed to correctly identify their sequences from non-acetyl sequences, but they have poor efficiency in terms of accuracy, sensitivity, and specificity. This work proposes an efficient and accurate computational model for predicting Acetylation using machine learning approaches. The proposed model achieved an accuracy of 100 percent with the 10-fold cross-validation test based on the Random Forest classifier, along with a feature extraction approach using statistical moments. The model is also validated by the jackknife, self-consistency, and independent test, which achieved an accuracy of 100, 100, and 97, respectively, results far better as compared to the already existing models available in the literature.