DeepPhoPred: Accurate Deep Learning Model to Predict Microbial Phosphorylation.

IF 3.2 4区 生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY Proteins-Structure Function and Bioinformatics Pub Date : 2025-02-01 Epub Date: 2024-09-06 DOI:10.1002/prot.26734
Faisal Ahmed, Alok Sharma, Swakkhar Shatabda, Iman Dehzangi
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Abstract

Phosphorylation is a substantial posttranslational modification of proteins that refers to adding a phosphate group to the amino acid side chain after translation process in the ribosome. It is vital to coordinate cellular functions, such as regulating metabolism, proliferation, apoptosis, subcellular trafficking, and other crucial physiological processes. Phosphorylation prediction in a microbial organism can assist in understanding pathogenesis and host-pathogen interaction, drug and antibody design, and antimicrobial agent development. Experimental methods for predicting phosphorylation sites are costly, slow, and tedious. Hence low-cost and high-speed computational approaches are highly desirable. This paper presents a new deep learning tool called DeepPhoPred for predicting microbial phospho-serine (pS), phospho-threonine (pT), and phospho-tyrosine (pY) sites. DeepPhoPred incorporates a two-headed convolutional neural network architecture with the squeeze and excitation blocks followed by fully connected layers that jointly learn significant features from the peptide's structural and evolutionary information to predict phosphorylation sites. Our empirical results demonstrate that DeepPhoPred significantly outperforms the existing microbial phosphorylation site predictors with its highly efficient deep-learning architecture. DeepPhoPred as a standalone predictor, all its source codes, and our employed datasets are publicly available at https://github.com/faisalahm3d/DeepPhoPred.

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DeepPhoPred:预测微生物磷酸化的精确深度学习模型
磷酸化是蛋白质的一种实质性翻译后修饰,是指在核糖体翻译过程后,在氨基酸侧链上添加一个磷酸基团。磷酸化对协调细胞功能至关重要,如调节新陈代谢、增殖、凋亡、亚细胞贩运和其他关键生理过程。预测微生物有机体的磷酸化有助于了解致病机理和宿主与病原体的相互作用、药物和抗体设计以及抗菌剂开发。预测磷酸化位点的实验方法成本高、速度慢且繁琐。因此,低成本、高速度的计算方法非常可取。本文介绍了一种名为 DeepPhoPred 的新型深度学习工具,用于预测微生物磷酸丝氨酸(pS)、磷酸苏氨酸(pT)和磷酸酪氨酸(pY)位点。DeepPhoPred 采用双头卷积神经网络架构,在挤压和激发块之后是全连接层,它们从肽的结构和进化信息中共同学习重要特征,从而预测磷酸化位点。我们的实证结果表明,DeepPhoPred 凭借其高效的深度学习架构,明显优于现有的微生物磷酸化位点预测工具。DeepPhoPred 作为一个独立的预测器,其所有源代码和我们使用的数据集均可在 https://github.com/faisalahm3d/DeepPhoPred 网站上公开获取。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
Proteins-Structure Function and Bioinformatics
Proteins-Structure Function and Bioinformatics 生物-生化与分子生物学
CiteScore
5.90
自引率
3.40%
发文量
172
审稿时长
3 months
期刊介绍: PROTEINS : Structure, Function, and Bioinformatics publishes original reports of significant experimental and analytic research in all areas of protein research: structure, function, computation, genetics, and design. The journal encourages reports that present new experimental or computational approaches for interpreting and understanding data from biophysical chemistry, structural studies of proteins and macromolecular assemblies, alterations of protein structure and function engineered through techniques of molecular biology and genetics, functional analyses under physiologic conditions, as well as the interactions of proteins with receptors, nucleic acids, or other specific ligands or substrates. Research in protein and peptide biochemistry directed toward synthesizing or characterizing molecules that simulate aspects of the activity of proteins, or that act as inhibitors of protein function, is also within the scope of PROTEINS. In addition to full-length reports, short communications (usually not more than 4 printed pages) and prediction reports are welcome. Reviews are typically by invitation; authors are encouraged to submit proposed topics for consideration.
期刊最新文献
A Novel Tetravalent CD95/Fas Fusion Protein With Superior CD95L/FasL Antagonism. Physicochemical Evaluation of Remote Homology in the Twilight Zone. Valacyclovir and Acyclovir Are Substrates of the Guanine Deaminase Cytosolic PSD-95 Interactor (Cypin). Structural Insight Into the Function of DnaB Helicase in Bacterial DNA Replication. DeepPhoPred: Accurate Deep Learning Model to Predict Microbial Phosphorylation.
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