UniPTM: Multiple PTM site prediction on full-length protein sequence
Rattachement africain : hk, us, cn. Niveau de preuve : code pays fourni par la source.
Le résumé fourni par la source
Abstract Post-translational modifications (PTMs) enrich the functional diversity of proteins by attaching chemical groups to the side chains of amino acids. In recent years, a myr-iad of AI models have been proposed to predict many specific types of PTMs. However, those models typically adopt the sliding window approach to extract short and equal-length protein fragments from full-length proteins for model training. Unfortunately, such a subtle step results in the loss of long-range information from distal amino acids, which may impact the PTM formation process. In this study, we introduce UniPTM, a window-free model designed to train and test on natural and full-length protein sequences, enabling the prediction of multiple types of PTMs in a holistic manner. Moreover, we established PTMseq, the first comprehensive dataset of full-length pro-tein sequences with annotated PTMs, to train and validate our model. UniPTM has undergone extensive validations and significantly outperforms existing models, eluci-dating the influence of protein sequence completeness on PTM. Consequently, UniPTM offers interpretable and biologically meaningful predictions, enhancing our understand-ing of protein functionally and regulation. The source code and PTMseq dataset for UniPTM are available at https://www.github.com/TransPTM/UniPTM .
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Le contrôle bibliographique ouvert
DOI retrouvé dans Crossref DOI retrouvé ; titre concordant.
- Titre Crossref
- UniPTM: Multiple PTM site prediction on full-length protein sequence
- Date Crossref
- 06/08/2024
- Éditeur
- openRxiv
- Type
- posted-content
Ce recoupement confirme des métadonnées liées au DOI. Il ne confirme ni la méthode ni les conclusions de l’étude, et il ne compte pas comme une seconde source scientifique indépendante.
Les institutions déclarées
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