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Systematic Characterization of Lysine Post-translational Modification Sites Using MUscADEL

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Specialty Molecular Biology
Date 2022 Jun 13
PMID 35696083
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Abstract

Among various types of protein post-translational modifications (PTMs), lysine PTMs play an important role in regulating a wide range of functions and biological processes. Due to the generation and accumulation of enormous amount of protein sequence data by ongoing whole-genome sequencing projects, systematic identification of different types of lysine PTM substrates and their specific PTM sites in the entire proteome is increasingly important and has therefore received much attention. Accordingly, a variety of computational methods for lysine PTM identification have been developed based on the combination of various handcrafted sequence features and machine-learning techniques. In this chapter, we first briefly review existing computational methods for lysine PTM identification and then introduce a recently developed deep learning-based method, termed MUscADEL (Multiple Scalable Accurate Deep Learner for lysine PTMs). Specifically, MUscADEL employs bidirectional long short-term memory (BiLSTM) recurrent neural networks and is capable of predicting eight major types of lysine PTMs in both the human and mouse proteomes. The web server of MUscADEL is publicly available at http://muscadel.erc.monash.edu/ for the research community to use.

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References
1.
Hornbeck P, Zhang B, Murray B, Kornhauser J, Latham V, Skrzypek E . PhosphoSitePlus, 2014: mutations, PTMs and recalibrations. Nucleic Acids Res. 2014; 43(Database issue):D512-20. PMC: 4383998. DOI: 10.1093/nar/gku1267. View

2.
Xu H, Zhou J, Lin S, Deng W, Zhang Y, Xue Y . PLMD: An updated data resource of protein lysine modifications. J Genet Genomics. 2017; 44(5):243-250. DOI: 10.1016/j.jgg.2017.03.007. View

3.
Das C, Kundu T . Transcriptional regulation by the acetylation of nonhistone proteins in humans -- a new target for therapeutics. IUBMB Life. 2005; 57(3):137-49. DOI: 10.1080/15216540500090629. View

4.
Glozak M, Sengupta N, Zhang X, Seto E . Acetylation and deacetylation of non-histone proteins. Gene. 2005; 363:15-23. DOI: 10.1016/j.gene.2005.09.010. View

5.
Kim S, Sprung R, Chen Y, Xu Y, Ball H, Pei J . Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell. 2006; 23(4):607-18. DOI: 10.1016/j.molcel.2006.06.026. View