Site-specific prediction of O-GlcNAc modification in proteins using evolutionary scale model.
Protein glycosylation, a vital post-translational modification, is pivotal in various biological processes and disease pathogenesis. Computational approaches, including protein language models and machine learning algorithms, have emerged as valuable tools for predicting O-GlcNAc sites, reducing exp...
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| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2024-01-01
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| Series: | PLoS ONE |
| Online Access: | https://doi.org/10.1371/journal.pone.0316215 |
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| author | Ayesha Khalid Afshan Kaleem Wajahat Qazi Roheena Abdullah Mehwish Iqtedar Shagufta Naz |
| author_facet | Ayesha Khalid Afshan Kaleem Wajahat Qazi Roheena Abdullah Mehwish Iqtedar Shagufta Naz |
| author_sort | Ayesha Khalid |
| collection | DOAJ |
| description | Protein glycosylation, a vital post-translational modification, is pivotal in various biological processes and disease pathogenesis. Computational approaches, including protein language models and machine learning algorithms, have emerged as valuable tools for predicting O-GlcNAc sites, reducing experimental costs, and enhancing efficiency. However, the literature has not reported the prediction of O-GlcNAc sites through the evolutionary scale model (ESM). Therefore, this study employed the ESM-2 model for O-GlcNAc site prediction in humans. Approximately 1100 O-linked glycoprotein sequences retrieved from the O-GlcNAc database were utilized for model training. The ESM-2 model exhibited consistent improvement over epochs, achieving an accuracy of 78.30%, recall of 78.30%, precision of 61.31%, and F1-score of 68.74%. However, compared to the traditional models which show an overfitting on the same data up to 99%, ESM-2 model outperforms in terms of optimal training and testing predictions. These findings underscore the effectiveness of the ESM-2 model in accurately predicting O-GlcNAc sites within human proteins. Accurately predicting O-GlcNAc sites within human proteins can significantly advance glycoproteomic research by enhancing our understanding of protein function and disease mechanisms, aiding in developing targeted therapies, and facilitating biomarker discovery for improved diagnosis and treatment. Furthermore, future studies should focus on more diverse data types, longer protein sequence lengths, and higher computational resources to evaluate various parameters. Accurate prediction of O-GlcNAc sites might enhance the investigation of the site-specific functions of proteins in physiology and diseases. |
| format | Article |
| id | doaj-art-df2e1a093630494499898e819afe9fab |
| institution | OA Journals |
| issn | 1932-6203 |
| language | English |
| publishDate | 2024-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj-art-df2e1a093630494499898e819afe9fab2025-08-20T02:35:31ZengPublic Library of Science (PLoS)PLoS ONE1932-62032024-01-011912e031621510.1371/journal.pone.0316215Site-specific prediction of O-GlcNAc modification in proteins using evolutionary scale model.Ayesha KhalidAfshan KaleemWajahat QaziRoheena AbdullahMehwish IqtedarShagufta NazProtein glycosylation, a vital post-translational modification, is pivotal in various biological processes and disease pathogenesis. Computational approaches, including protein language models and machine learning algorithms, have emerged as valuable tools for predicting O-GlcNAc sites, reducing experimental costs, and enhancing efficiency. However, the literature has not reported the prediction of O-GlcNAc sites through the evolutionary scale model (ESM). Therefore, this study employed the ESM-2 model for O-GlcNAc site prediction in humans. Approximately 1100 O-linked glycoprotein sequences retrieved from the O-GlcNAc database were utilized for model training. The ESM-2 model exhibited consistent improvement over epochs, achieving an accuracy of 78.30%, recall of 78.30%, precision of 61.31%, and F1-score of 68.74%. However, compared to the traditional models which show an overfitting on the same data up to 99%, ESM-2 model outperforms in terms of optimal training and testing predictions. These findings underscore the effectiveness of the ESM-2 model in accurately predicting O-GlcNAc sites within human proteins. Accurately predicting O-GlcNAc sites within human proteins can significantly advance glycoproteomic research by enhancing our understanding of protein function and disease mechanisms, aiding in developing targeted therapies, and facilitating biomarker discovery for improved diagnosis and treatment. Furthermore, future studies should focus on more diverse data types, longer protein sequence lengths, and higher computational resources to evaluate various parameters. Accurate prediction of O-GlcNAc sites might enhance the investigation of the site-specific functions of proteins in physiology and diseases.https://doi.org/10.1371/journal.pone.0316215 |
| spellingShingle | Ayesha Khalid Afshan Kaleem Wajahat Qazi Roheena Abdullah Mehwish Iqtedar Shagufta Naz Site-specific prediction of O-GlcNAc modification in proteins using evolutionary scale model. PLoS ONE |
| title | Site-specific prediction of O-GlcNAc modification in proteins using evolutionary scale model. |
| title_full | Site-specific prediction of O-GlcNAc modification in proteins using evolutionary scale model. |
| title_fullStr | Site-specific prediction of O-GlcNAc modification in proteins using evolutionary scale model. |
| title_full_unstemmed | Site-specific prediction of O-GlcNAc modification in proteins using evolutionary scale model. |
| title_short | Site-specific prediction of O-GlcNAc modification in proteins using evolutionary scale model. |
| title_sort | site specific prediction of o glcnac modification in proteins using evolutionary scale model |
| url | https://doi.org/10.1371/journal.pone.0316215 |
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