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Related Concept Videos

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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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...
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Phosphorylation01:02

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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.
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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.
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Protein Networks02:26

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An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
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Genome comparison is one of the excellent ways to interpret the evolutionary relationships between organisms. The basic principle of genome comparison is that if two species share a common feature, it is likely encoded by the DNA sequence conserved between both species. The advent of genome sequencing technologies in the late 20th century enabled scientists to understand the concept of conservation of domains between species and helped them to deduce evolutionary relationships across diverse...
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Related Experiment Video

Updated: Feb 26, 2026

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
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Databases and Computational Tools for Evolutionary Analysis of Protein Phosphorylation.

Chris Soon Heng Tan1,2

  • 1Institute of Molecular and Cell Biology (IMCB), A*STAR (Agency for Science, Technology and Research), Singapore, 138673, Singapore. cshtan@imcb.a-star.edu.sg.

Methods in Molecular Biology (Clifton, N.J.)
|July 22, 2017
PubMed
Summary

Mass spectrometry-based proteomics has identified many uncharacterized protein phosphorylation sites. Analyzing sequence conservation across species helps prioritize these sites for functional study.

Keywords:
BioinformaticsMass spectrometryPhospho-proteomicsPhosphorylation siteProtein evolutionProtein phosphorylation

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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
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Area of Science:

  • Biochemistry and Molecular Biology
  • Proteomics
  • Bioinformatics

Background:

  • Mass spectrometry (MS)-based techniques have identified hundreds of thousands of protein phosphorylation sites.
  • A significant majority of these identified sites remain functionally uncharacterized.
  • Prioritizing uncharacterized sites is crucial for efficient functional annotation and understanding cellular signaling.

Purpose of the Study:

  • To present a systematic workflow for prioritizing novel phosphorylation sites for functional annotation.
  • To highlight the utility of cross-species sequence conservation analysis for identifying functionally important phosphorylation events.
  • To provide an overview of accessible computational resources for conducting conservation analyses.

Main Methods:

  • Utilizing advancements in MS-based phospho-proteomics data.
  • Implementing comparative sequence analysis across diverse species.
  • Leveraging publicly available bioinformatics tools and databases.

Main Results:

  • A subset of uncharacterized phosphorylation sites can be identified through conservation analysis.
  • Conservation patterns can serve as a proxy for functional importance.
  • The outlined workflow facilitates the systematic prioritization of novel phosphorylation sites.

Conclusions:

  • Cross-species sequence conservation analysis is an effective strategy for prioritizing uncharacterized phosphorylation sites.
  • This approach aids in focusing experimental efforts on potentially critical phosphorylation events.
  • Publicly available computational resources can be effectively integrated into this prioritization workflow.