ArticleInternational journal of molecular sciences2024
Attenphos: General Phosphorylation Site Prediction Model Based on Attention Mechanism.
Article in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers, 1 of them a synthesis that pooled it.
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Who cites it
5 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Protein Sequence Analysis landscape: A Systematic Review of Task Types, Databases, Datasets, Word Embeddings Methods, and Language Models.Database : the journal of biological databases and curation · 2025Pooled it
- DeepPTMPred: a multi-modal deep learning framework for accurate prediction of protein post-translational modification sites.Briefings in bioinformatics · 2026Article
- ProtPSP: Determination of Protein Phosphorylation Sites with the Protein Large Language Model.ACS omega · 2025Article
- Post-Translational Modifications in Respiratory Virus Infection: Recent Insights into the Development of In Vitro Models.International journal of molecular sciences · 2025Review
- Advances in Prediction of Posttranslational Modification Sites Known to Localize in Protein Supersecondary Structures.Methods in molecular biology (Clifton, N.J.) · 2025Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Phosphorylation site prediction has important application value in the field of bioinformatics. It can act as an important reference and help with protein function research, protein structure research, and drug discovery. So, it is of great significance to propose scientific and effective calculation methods to accurately predict phosphorylation sites. In this study, we propose a new method, Attenphos, based on the self-attention mechanism for predicting general phosphorylation sites in proteins. The method not only captures the long-range dependence information of proteins but also better represents the correlation between amino acids through feature vector encoding transformation. Attenphos takes advantage of the one-dimensional convolutional layer to reduce the number of model parameters, improve model efficiency and prediction accuracy, and enhance model generalization. Comparisons between our method and existing state-of-the-art prediction tools were made using balanced datasets from human proteins and unbalanced datasets from mouse proteins. We performed prediction comparisons using independent test sets. The results showed that Attenphos demonstrated the best overall performance in the prediction of Serine (S), Threonine (T), and Tyrosine (Y) sites on both balanced and unbalanced datasets. Compared to current state-of-the-art methods, Attenphos has significantly higher prediction accuracy. This proves the potential of Attenphos in accelerating the identification and functional analysis of protein phosphorylation sites and provides new tools and ideas for biological research and drug discovery.
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Registered trials
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