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Updated: Jan 23, 2026

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
Published on: May 3, 2018
Computational identification of microbial phosphorylation sites by the enhanced characteristics of sequence
Md Mehedi Hasan1, Md Mamunur Rashid1, Mst Shamima Khatun1
1Department of Bioscience and Bioinformatics, Kyushu Institute of Technology, 680-4 Kawazu, Iizuka, Fukuoka, 820-8502, Japan.
Abstract:
Protein phosphorylation on serine (S) and threonine (T) has emerged as a key device in the control of many biological processes. Recently phosphorylation in microbial organisms has attracted much attention for its critical roles in various cellular processes such as cell growth and cell division. Here a novel machine learning predictor, MPSite (Microbial Phosphorylation Site predictor), was developed to identify microbial phosphorylation sites using the enhanced characteristics of sequence features. The final feature vectors optimized via a Wilcoxon rank sum test. A random forest classifier was then trained using the optimum features to build the predictor. Benchmarking investigation using the 5-fold cross-validation and independent datasets test showed that the MPSite is able to achieve robust performance on the S- and T-phosphorylation site prediction. It also outperformed other existing methods on the comprehensive independent datasets. We anticipate that the MPSite is a powerful tool for proteome-wide prediction of microbial phosphorylation sites and facilitates hypothesis-driven functional interrogation of phosphorylation proteins. A web application with the curated datasets is freely available at http://kurata14.bio.kyutech.ac.jp/MPSite/ .
Insights
A new machine learning tool, MPSite, accurately predicts microbial phosphorylation sites on serine and threonine. This tool aids in understanding microbial cell growth and division processes.
Area of Science:
- Biochemistry
- Computational Biology
- Microbiology
Background:
- Protein phosphorylation on serine (S) and threonine (T) regulates critical biological processes.
- Microbial phosphorylation is increasingly recognized for its roles in cell growth and division.
Purpose of the Study:
- To develop a novel machine learning predictor, MPSite, for identifying microbial phosphorylation sites.
- To enhance the accuracy of phosphorylation site prediction using advanced sequence features.
Main Methods:
- Developed MPSite using enhanced sequence features and a random forest classifier.
- Optimized feature vectors using a Wilcoxon rank sum test.
- Validated performance using 5-fold cross-validation and independent datasets.
Main Results:
- MPSite demonstrated robust performance in predicting S- and T-phosphorylation sites.
- The predictor outperformed existing methods on comprehensive independent datasets.
- Achieved high accuracy in identifying microbial phosphorylation sites.
Conclusions:
- MPSite is a powerful tool for proteome-wide prediction of microbial phosphorylation sites.
- Facilitates hypothesis-driven functional studies of phosphorylation in microbial proteins.
- A web application is available for public use.
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