Systematic Characterization of Lysine Post-translational Modification Sites Using MUscADEL.

Methods Mol Biol

Biomedicine Discovery Institute, Department of Biochemistry and Molecular Biology, Monash University, Melbourne, VIC, Australia.

Published: June 2022

AI Article Synopsis

  • Lysine post-translational modifications (PTMs) are crucial for regulating various biological processes and functions, making their systematic identification essential due to the increasing amount of protein sequence data from genome projects.
  • With advancements in computational methods, researchers have developed techniques that combine handcrafted sequence features and machine learning for identifying lysine PTM substrates and sites.
  • A new deep learning-based method called MUscADEL uses bidirectional long short-term memory networks to predict eight major types of lysine PTMs in human and mouse proteomes, and it is available for public use on its web server.

Article 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.

Download full-text PDF

Source
http://dx.doi.org/10.1007/978-1-0716-2317-6_11DOI Listing

Publication Analysis

Top Keywords

lysine ptms
12
lysine ptm
12
types lysine
8
computational methods
8
methods lysine
8
ptm identification
8
lysine
7
systematic characterization
4
characterization lysine
4
lysine post-translational
4

Similar Publications

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!