School of Computer Science and Engineering, Yulin Normal University, Yulin 537000, China.
School of Computer, Electronics and Information, Guangxi University, Nanning 530004, China.
Int J Mol Sci. 2019 Jan 14;20(2):302. doi: 10.3390/ijms20020302.
Protein phosphorylation is an important chemical modification catalyzed by kinases. It plays important roles in many cellular processes. Predicting kinase⁻substrate interactions is vital to understanding the mechanism of many diseases. Many computational methods have been proposed to identify kinase⁻substrate interactions. However, the prediction accuracy still needs to be improved. Therefore, it is necessary to develop an efficient computational method to predict kinase⁻substrate interactions. In this paper, we propose a novel computational approach, KSIMC, to identify kinase⁻substrate interactions based on matrix completion. Firstly, the kinase similarity and substrate similarity are calculated by aligning sequence of kinase⁻kinase and substrate⁻substrate, respectively. Then, the original association network is adjusted based on the similarities. Finally, the matrix completion is used to predict potential kinase⁻substrate interactions. The experiment results show that our method outperforms other state-of-the-art algorithms in performance. Furthermore, the relevant databases and scientific literature verify the effectiveness of our algorithm for new kinase⁻substrate interaction identification.
蛋白质磷酸化是由激酶催化的一种重要的化学修饰。它在许多细胞过程中起着重要作用。预测激酶-底物相互作用对于理解许多疾病的机制至关重要。已经提出了许多计算方法来识别激酶-底物相互作用。然而,预测准确性仍有待提高。因此,有必要开发一种有效的计算方法来预测激酶-底物相互作用。在本文中,我们提出了一种新的计算方法 KSIMC,基于矩阵补全来识别激酶-底物相互作用。首先,通过对齐激酶-激酶和底物-底物的序列来计算激酶相似性和底物相似性。然后,根据相似性调整原始关联网络。最后,使用矩阵补全来预测潜在的激酶-底物相互作用。实验结果表明,我们的方法在性能上优于其他最先进的算法。此外,相关数据库和科学文献验证了我们的算法在新的激酶-底物相互作用识别方面的有效性。