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CapsNh-Kcr: Capsule network-based prediction of lysine crotonylation sites in human non-histone proteins

Lysine crotonylation (Kcr) is one of the most important post-translational modifications (PTMs) that is widely detected in both histone and non-histone proteins. In fact, Kcr is reported to be involved in various biological processes, such as metabolism and cell differentiation. However, the availab...

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Autores principales: Khanal, Jhabindra, Kandel, Jeevan, Tayara, Hilal, Chong, Kil To
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Research Network of Computational and Structural Biotechnology 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9735261/
https://www.ncbi.nlm.nih.gov/pubmed/36544479
http://dx.doi.org/10.1016/j.csbj.2022.11.056
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author Khanal, Jhabindra
Kandel, Jeevan
Tayara, Hilal
Chong, Kil To
author_facet Khanal, Jhabindra
Kandel, Jeevan
Tayara, Hilal
Chong, Kil To
author_sort Khanal, Jhabindra
collection PubMed
description Lysine crotonylation (Kcr) is one of the most important post-translational modifications (PTMs) that is widely detected in both histone and non-histone proteins. In fact, Kcr is reported to be involved in various biological processes, such as metabolism and cell differentiation. However, the available experimental methods for Kcr site identification are laborious and costly. To effectively replace existing experimental approaches, some computational methods have been developed in the last few years. The available computational methods still lack some important aspects, as they can only identify Kcr sites on either histone-only or combined histone and nonhistone proteins. Although a tool was developed to identify Kcr sites on non-histone proteins only, its performance is inadequate and the exploration of hidden Kcr patterns (motifs) has been completely ignored, which might be significant for detailed Kcr studies. Therefore, algorithms that can more effectively predict Kcr sites on non-histone proteins with their biological meaning need to be designed. Accordingly, we developed a novel deep learning (capsule network)-based model, named CapsNh-Kcr, for Kcr site prediction, particularly focusing on non-histone proteins. Based on the independent results, the proposed model achieves an AUC of 0.9120, which is approximately 6% higher than that of previous nhKcr model in the prediction of Kcr sites on non-histone proteins. Further, we revealed, for the first time, that the proposed model can represent obvious motif distribution across Kcr sites in non-histone proteins. The source code (in Python) is publicly available at https://github.com/Jhabindra-bioinfo/CapsNh-Kcr.
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spelling pubmed-97352612022-12-20 CapsNh-Kcr: Capsule network-based prediction of lysine crotonylation sites in human non-histone proteins Khanal, Jhabindra Kandel, Jeevan Tayara, Hilal Chong, Kil To Comput Struct Biotechnol J Research Article Lysine crotonylation (Kcr) is one of the most important post-translational modifications (PTMs) that is widely detected in both histone and non-histone proteins. In fact, Kcr is reported to be involved in various biological processes, such as metabolism and cell differentiation. However, the available experimental methods for Kcr site identification are laborious and costly. To effectively replace existing experimental approaches, some computational methods have been developed in the last few years. The available computational methods still lack some important aspects, as they can only identify Kcr sites on either histone-only or combined histone and nonhistone proteins. Although a tool was developed to identify Kcr sites on non-histone proteins only, its performance is inadequate and the exploration of hidden Kcr patterns (motifs) has been completely ignored, which might be significant for detailed Kcr studies. Therefore, algorithms that can more effectively predict Kcr sites on non-histone proteins with their biological meaning need to be designed. Accordingly, we developed a novel deep learning (capsule network)-based model, named CapsNh-Kcr, for Kcr site prediction, particularly focusing on non-histone proteins. Based on the independent results, the proposed model achieves an AUC of 0.9120, which is approximately 6% higher than that of previous nhKcr model in the prediction of Kcr sites on non-histone proteins. Further, we revealed, for the first time, that the proposed model can represent obvious motif distribution across Kcr sites in non-histone proteins. The source code (in Python) is publicly available at https://github.com/Jhabindra-bioinfo/CapsNh-Kcr. Research Network of Computational and Structural Biotechnology 2022-12-01 /pmc/articles/PMC9735261/ /pubmed/36544479 http://dx.doi.org/10.1016/j.csbj.2022.11.056 Text en © 2022 Published by Elsevier B.V. on behalf of Research Network of Computational and Structural Biotechnology. https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Research Article
Khanal, Jhabindra
Kandel, Jeevan
Tayara, Hilal
Chong, Kil To
CapsNh-Kcr: Capsule network-based prediction of lysine crotonylation sites in human non-histone proteins
title CapsNh-Kcr: Capsule network-based prediction of lysine crotonylation sites in human non-histone proteins
title_full CapsNh-Kcr: Capsule network-based prediction of lysine crotonylation sites in human non-histone proteins
title_fullStr CapsNh-Kcr: Capsule network-based prediction of lysine crotonylation sites in human non-histone proteins
title_full_unstemmed CapsNh-Kcr: Capsule network-based prediction of lysine crotonylation sites in human non-histone proteins
title_short CapsNh-Kcr: Capsule network-based prediction of lysine crotonylation sites in human non-histone proteins
title_sort capsnh-kcr: capsule network-based prediction of lysine crotonylation sites in human non-histone proteins
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9735261/
https://www.ncbi.nlm.nih.gov/pubmed/36544479
http://dx.doi.org/10.1016/j.csbj.2022.11.056
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