Post-Translational Modification Site Prediction Service

The prediction of protein PTMs is currently an important research topic in the field of protein bioinformatics. PTMs allow proteins to adopt more complex structures, have more sophisticated functions, and perform different tasks more precisely. Different types of PTM can occur at different amino acid residues, and multiple modifications may occur at the same amino acid residue. As the data accumulated, by identifying patterns in the acquired data, researchers tried to infer whether a particular locus has been modified or not. The computational prediction has the advantages of high accuracy, high speed, and low cost, and is a suitable and effective alternative screening method to traditional protein PTM analysis. To date, there are a plethora of computational prediction methods developed for protein PTMs. These methods vary depending on the type of prediction algorithm used, enabling the study of the PTM sites of proteins from their sequences, structures, and evolutionary characteristics. Typically, there are four main steps in the computational approach to predicting a particular type of PTM, including data collection, feature extraction, predictor learning, and performance evaluation.

Fig. 1 A schematic flowchart to show how a predictor works for PTM prediction. (Ramazi, S., & Zahiri, J., 2021)

Computational prediction of PTMs is a promising strategy to perform preliminary analysis and significantly reduce the number of potential targets requiring further in vivo or in vitro confirmation. Based on our experienced experts and multiple machine learning algorithms, we are able to provide not only common PTM site prediction services, such as phosphorylation site, glycosylation site, acetylation site, methylation site, SUMOylation site and ubiquitination site prediction, but also new PTM site prediction services. In addition, we are able to predict whether the PTM site is within the protein-protein interaction region (PPIR). PPIR forms the binding interface between interacting polypeptide chains and is a very important functional domain of proteins. PTMs in PPIR can interfere with or promote protein interactions, and their study can help further elucidate the regulatory mechanisms by which PTMs of targeted proteins regulate their cellular functions.