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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...
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...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...

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Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

CPhos: a program to calculate and visualize evolutionarily conserved functional phosphorylation sites.

Boyang Zhao1, Trairak Pisitkun, Jason D Hoffert

  • 1National Heart, Lung, and Blood Institute, Epithelial Systems Biology Laboratory, National Institutes of Health, Bethesda, MD 20892-1603, USA.

Proteomics
|September 25, 2012
PubMed
Summary
This summary is machine-generated.

CPhos is a new Java program that assesses protein phosphosite conservation across species. This tool helps researchers determine the functional significance of newly discovered phosphosites for experimental validation.

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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 18, 2026

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

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:

  • Proteomics
  • Bioinformatics
  • Evolutionary Biology

Background:

  • High-throughput mass spectrometry (MS) has identified numerous novel protein phosphorylation sites (phosphosites).
  • Determining the functional relevance of these identified phosphosites remains a challenge in phosphoproteomics research.

Purpose of the Study:

  • To develop a computational tool, CPhos, for assessing the evolutionary conservation of phosphosites.
  • To provide a method for prioritizing phosphosites based on their conservation status for further experimental validation.

Main Methods:

  • Developed CPhos, a Java program utilizing an information theory-based approach.
  • Implemented a user-friendly graphical user interface (GUI).
  • Made CPhos available as both a web service and a standalone application.

Main Results:

  • CPhos quantifies phosphosite conservation across different species.
  • The degree of conservation calculated by CPhos correlates with functional significance.
  • Facilitates the analysis and prioritization of phosphosites for researchers.

Conclusions:

  • CPhos offers a valuable computational approach to assess phosphosite conservation.
  • The tool aids in understanding the functional importance of phosphosites discovered through high-throughput MS.
  • CPhos supports phosphoproteomic research by enabling focused experimental validation.