Dataset Information

Identification of S-nitrosylation sites based on multiple features combination.

ABSTRACT: Protein S-nitrosylation (SNO) is a typical reversible, redox-dependent and post-translational modification that involves covalent modification of cysteine residues with nitric oxide (NO) for the thiol group. Numerous experiments have shown that SNO plays a major role in cell function and pathophysiology. In order to rapidly analysis the big sets of data, the computing methods for identifying the SNO sites are being considered as necessary auxiliary tools. In this study, multiple features including Parallel correlation pseudo amino acid composition (PC-PseAAC), Basic kmer1 (kmer1), Basic kmer2 (kmer2), General parallel correlation pseudo amino acid composition (PC-PseAAC_G), Adapted Normal distribution Bi-Profile Bayes (ANBPB), Double Bi-Profile Bayes (DBPB), Bi-Profile Bayes (BPB), Incorporating Amino Acid Pairwise (IAAPair) and Position-specific Tri-Amino Acid Propensity(PSTAAP) were employed to extract the sequence information. To remove information redundancy, information gain (IG) was applied to evaluate the importance of amino acids, which is the information entropy of class after subtracting the conditional entropy for the given amino acid. The prediction performance of the SNO sites was found to be best by using the cross-validation and independent tests. In addition, we also calculated four commonly used performance measurements, i.e. Sensitivity (Sn), Specificity (Sp), Accuracy (Acc), and the Matthew's Correlation Coefficient (MCC). For the training dataset, the overall Acc was 83.11%, the MCC was 0.6617. For an independent test dataset, Acc was 73.17%, and MCC was 0.3788. The results indicate that our method is likely to complement the existing prediction methods and is a useful tool for effective identification of the SNO sites.

SUBMITTER: Li T

PROVIDER: S-EPMC6395632 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature

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Identification of S-nitrosylation sites based on multiple features combination.

Li Taoying T Song Runyu R Yin Qian Q Gao Mingyue M Chen Yan Y

Scientific reports 20190228 1

Protein S-nitrosylation (SNO) is a typical reversible, redox-dependent and post-translational modification that involves covalent modification of cysteine residues with nitric oxide (NO) for the thiol group. Numerous experiments have shown that SNO plays a major role in cell function and pathophysiology. In order to rapidly analysis the big sets of data, the computing methods for identifying the SNO sites are being considered as necessary auxiliary tools. In this study, multiple features includi ...[more]

PMID: 30816267

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Project description:BackgroundProtein phosphoglycerylation, the addition of a 1,3-bisphosphoglyceric acid (1,3-BPG) to a lysine residue of a protein and thus to form a 3-phosphoglyceryl-lysine, is a reversible and non-enzymatic post-translational modification (PTM) and plays a regulatory role in glucose metabolism and glycolytic process. As the number of experimentally verified phosphoglycerylated sites has increased significantly, statistical or machine learning methods are imperative for investigating the characteristics of phosphoglycerylation sites. Currently, research into phosphoglycerylation is very limited, and only a few resources are available for the computational identification of phosphoglycerylation sites.ResultWe present a bioinformatics investigation of phosphoglycerylation sites based on sequence-based features. The TwoSampleLogo analysis reveals that the regions surrounding the phosphoglycerylation sites contain a high relatively of positively charged amino acids, especially in the upstream flanking region. Additionally, the non-polar and aliphatic amino acids are more abundant surrounding phosphoglycerylated lysine following the results of PTM-Logo, which may play a functional role in discriminating between phosphoglycerylation and non-phosphoglycerylation sites. Many types of features were adopted to build the prediction model on the training dataset, including amino acid composition, amino acid pair composition, positional weighted matrix and position-specific scoring matrix. Further, to improve the predictive power, numerous top features ranked by F-score were considered as the final combination for classification, and thus the predictive models were trained using DT, RF and SVM classifiers. Evaluation by five-fold cross-validation showed that the selected features was most effective in discriminating between phosphoglycerylated and non-phosphoglycerylated sites.ConclusionThe SVM model trained with the selected sequence-based features performed well, with a sensitivity of 77.5%, a specificity of 73.6%, an accuracy of 74.9%, and a Matthews Correlation Coefficient value of 0.49. Furthermore, the model also consistently provides the effective performance in independent testing set, yielding sensitivity of 75.7% and specificity of 64.9%. Finally, the model has been implemented as a web-based system, namely iDPGK, which is now freely available at http://mer.hc.mmh.org.tw/iDPGK/ .

Dataset Information

Identification of S-nitrosylation sites based on multiple features combination.

Publications

Identification of S-nitrosylation sites based on multiple features combination.

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