Unit
UNIT 24.8 Global Proteomics Analysis of Protein Lysine Methylation
Published Online: 1 NOV 2016
DOI: 10.1002/cpps.16
Copyright © 2013 John Wiley & Sons, Inc. All rights reserved.
Lab Protocol Title

Current Protocols in Protein Science
Additional Information
How to Cite
and 2016. Global proteomics analysis of protein lysine methylation. Curr. Protoc. Protein Sci. 86:24.8.1-24.8.19. doi: 10.1002/cpps.16
Publication History
- Published Online: 1 NOV 2016
- Abstract
- Article
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- Tables
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Abstract
Lysine methylation is a common protein post-translational modification dynamically mediated by protein lysine methyltransferases (PKMTs) and protein lysine demethylases (PKDMs). Beyond histone proteins, lysine methylation on non-histone proteins plays a substantial role in a variety of functions in cells and is closely associated with diseases such as cancer. A large body of evidence indicates that the dysregulation of some PKMTs leads to tumorigenesis via their non-histone substrates. However, most studies on other PKMTs have made slow progress owing to the lack of approaches for extensive screening of lysine methylation sites. However, recently, there has been a series of publications to perform large-scale analysis of protein lysine methylation. In this unit, we introduce a protocol for the global analysis of protein lysine methylation in cells by means of immunoaffinity enrichment and mass spectrometry. © 2016 by John Wiley & Sons, Inc.
Keywords:
- immunoaffinity enrichment;
- methylation;
- mass spectrometry;
- non-histone;
- post-translational modification;
- proteomics
