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Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Histone Modification02:32

Histone Modification

The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...

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Related Experiment Video

Updated: May 16, 2026

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry
12:49

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry

Published on: April 4, 2018

Position-specific analysis and prediction for protein lysine acetylation based on multiple features.

Sheng-Bao Suo1, Jian-Ding Qiu, Shao-Ping Shi

  • 1Department of Chemistry, Nanchang University, Nanchang, China.

Plos One
|November 23, 2012
PubMed
Summary

We developed PSKAcePred, a computational tool to predict lysine acetylation sites. This method enhances understanding of acetylation mechanisms and aids experimental validation in cellular processes.

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Last Updated: May 16, 2026

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry
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Published on: April 4, 2018

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Bioinformatics

Background:

  • Protein lysine acetylation is a crucial reversible post-translational modification.
  • It regulates vital cellular processes including gene transcription, apoptosis, and signaling.
  • Identifying acetylation sites is key to understanding these mechanisms.

Purpose of the Study:

  • To develop a computational method for predicting lysine acetylation sites.
  • To improve the accuracy of identifying acetylation sites in proteins.

Main Methods:

  • Developed PSKAcePred, a position-specific prediction tool using support vector machines.
  • Incorporated features: amino acid composition, evolutionary similarity, and physicochemical properties.
  • Utilized entropy values for residue selection around potential acetylation sites.

Main Results:

  • Achieved 79.84% accuracy and 59.72% Matthews correlation coefficient via 10-fold cross-validation.
  • Feature analysis confirmed the contribution of all incorporated features to prediction.
  • Position-specific analysis highlighted the importance of neighboring residues in site determination.

Conclusions:

  • PSKAcePred effectively predicts lysine acetylation sites.
  • The study deepens the understanding of acetylation mechanisms.
  • Findings provide valuable guidance for experimental validation in acetylation research.