Compendium of protein lysine acetylation

Compendium of Protein Lysine Acetylation is a comprehensive database that catalogs information on lysine acetylation, a critical post-translational modification (PTM) in proteins. Lysine acetylation involves the addition of an acetyl group to the ε-amino group of a lysine residue, which can significantly alter the function, localization, and interaction of proteins within the cell. This modification plays a pivotal role in various cellular processes, including gene expression, DNA repair, cell cycle regulation, and metabolism.

Overview

The Compendium of Protein Lysine Acetylation aims to provide a detailed and accessible repository of information on lysine acetylated proteins and their functional implications in different biological contexts. It encompasses data from multiple species, ranging from bacteria to humans, and integrates information from various experimental techniques, including mass spectrometry-based proteomics, biochemical assays, and computational predictions.

Content and Features

The database includes several key features:

• Comprehensive Data: It contains detailed entries on lysine-acetylated proteins, including the specific lysine residues that are acetylated, the enzymes (e.g., acetyltransferases and deacetylases) responsible for these modifications, and the functional consequences of acetylation.
• Search Functionality: Users can search the database by protein name, lysine residue, modification effect, and other relevant criteria, making it easier to find specific information.
• Cross-Species Information: By including data from various species, the compendium allows for comparative analyses of lysine acetylation patterns and their evolutionary conservation.
• Experimental Data: Entries are supported by experimental evidence, providing a reliable resource for researchers interested in the functional study of protein lysine acetylation.

Importance of Lysine Acetylation

Lysine acetylation is a reversible modification that plays a significant role in regulating protein function. It can influence protein activity, protein-protein interactions, and protein stability. In the context of gene expression, acetylation of histone proteins leads to chromatin remodeling, which can activate or repress transcription. Beyond histones, acetylation of non-histone proteins is involved in regulating various cellular pathways and processes, highlighting the broad impact of this modification on cell biology.

Applications

The Compendium of Protein Lysine Acetylation serves as a valuable resource for researchers in the fields of biochemistry, molecular biology, and cell biology. It supports the discovery of novel acetylated proteins and the exploration of their functional roles, contributing to our understanding of cellular regulation and the development of therapeutic strategies targeting acetylation-related pathways.

Challenges and Future Directions

Despite its comprehensive nature, the compendium faces challenges, including the need for continuous updates to incorporate new findings and the improvement of computational methods to predict lysine acetylation sites accurately. Future developments may focus on enhancing the database's interactivity, integrating more diverse types of data, and expanding its scope to include emerging areas of research in protein acetylation.