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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...
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...
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.

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Updated: Jun 24, 2026

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

Weak functional constraints on phosphoproteomes.

Christian R Landry1, Emmanuel D Levy, Stephen W Michnick

  • 1Centre Robert-Cedergren, Bio-Informatique et Génomique, Département de Biochimie, C.P. 6128, Succ. Centre-Ville, Montreal, Quebec H3C 3J7, Canada.

Trends in Genetics : TIG
|April 8, 2009
PubMed
Summary
This summary is machine-generated.

Phosphorylation sites (phosphosites) are more conserved than non-phosphorylated residues, especially in disordered protein regions. Functional phosphosites show higher conservation, suggesting many identified phosphosites are non-functional.

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Area of Science:

  • Molecular Biology
  • Evolutionary Biology
  • Biochemistry

Background:

  • Phosphorylation sites (phosphosites) play critical roles in regulating protein function.
  • Previous studies reported conflicting results on the evolutionary conservation of phosphosites.
  • Understanding phosphosite conservation is key to identifying functional regulatory elements.

Purpose of the Study:

  • To resolve conflicting conclusions regarding phosphosite evolutionary conservation.
  • To investigate the influence of disordered regions on phosphosite conservation.
  • To differentiate conservation patterns between functional and non-functional phosphosites.

Main Methods:

  • Comparative analysis of phosphosite conservation across species.
  • Statistical evaluation of conservation levels, accounting for protein disorder.
  • Functional annotation of phosphosites to assess evolutionary patterns.

Main Results:

  • Phosphosites are, on average, more conserved than non-phosphorylated residues when considering disordered regions.
  • Phosphosites with known functions exhibit significantly higher evolutionary conservation.
  • A substantial proportion of identified phosphosites appear to be non-functional, contributing to apparent rapid evolution.

Conclusions:

  • Evolutionary conservation analysis, particularly considering disordered regions, is essential for identifying functional phosphosites.
  • The study resolves discrepancies in previous findings on phosphosite conservation.
  • Findings emphasize the importance of evolutionary information for understanding post-translational modifications in eukaryotes.