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Related Concept Videos

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...

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Related Experiment Video

Updated: May 29, 2026

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

A novel sequence-based method for phosphorylation site prediction with feature selection and analysis.

Zhi-Song He1, Xiao-He Shi, Xiang-Ying Kong

  • 1CAS-MPG Partner Institute for Computational Biology, Shanghai Institutes for Biological Sciences (SIBS), Chinese Academy of Sciences (CAS), Shanghai, China. jfsamery@gmail.com

Protein and Peptide Letters
|September 17, 2011
PubMed
Summary
This summary is machine-generated.

This study introduces a novel computational method for predicting protein phosphorylation sites. The sequence-based approach accurately identifies serine, threonine, and tyrosine phosphorylation sites, aiding disease diagnosis.

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A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes
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A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes

Published on: May 22, 2018

Related Experiment Videos

Last Updated: May 29, 2026

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes
09:10

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes

Published on: May 22, 2018

Area of Science:

  • Biochemistry
  • Bioinformatics
  • Computational Biology

Background:

  • Phosphorylation is a critical post-translational modification.
  • Identifying phosphorylation sites is vital for disease diagnosis.
  • Experimental methods for detection are time-consuming.

Purpose of the Study:

  • To develop a novel computational method for predicting protein phosphorylation sites.
  • To provide an efficient alternative to experimental detection methods.
  • To identify serine, threonine, and tyrosine phosphorylation sites.

Main Methods:

  • A sequence-based prediction method using the Nearest Neighbor algorithm.
  • Peptide extraction around phosphorylation sites using a sliding window.
  • Feature extraction from the Amino Acid Index (AAIndex) database.
  • Feature selection using Incremental Feature Selection (mRMR).

Main Results:

  • Three distinct predictors were developed for serine, threonine, and tyrosine phosphorylation sites.
  • Accuracies achieved were 66.64% (serine), 66.11% (threonine), and 66.69% (tyrosine).
  • Results were validated through rigorous jackknife cross-validation tests.

Conclusions:

  • The developed computational method offers a valuable tool for predicting phosphorylation sites.
  • This approach can supplement experimental methods in research and diagnostics.
  • The method demonstrates potential for improving the efficiency of phosphorylation site identification.