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Related Concept Videos

Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
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...

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Updated: Jun 21, 2026

Phosphopeptide Enrichment Coupled with Label-free Quantitative Mass Spectrometry to Investigate the Phosphoproteome in Prostate Cancer
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Phosphopeptide Enrichment Coupled with Label-free Quantitative Mass Spectrometry to Investigate the Phosphoproteome in Prostate Cancer

Published on: August 2, 2018

The phosphoproteomics data explosion.

Simone Lemeer1, Albert J R Heck

  • 1Biomolecular Mass Spectrometry and Proteomics Group, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padualaan 8, Utrecht, The Netherlands.

Current Opinion in Chemical Biology
|July 22, 2009
PubMed
Summary
This summary is machine-generated.

Global phosphoproteomics is rapidly expanding, with over 25,000 human phosphorylation sites cataloged. Technological advancements in phosphopeptide enrichment and mass spectrometry are driving this exponential growth in data.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Proteomics

Background:

  • The human proteome contains over 500,000 potential phosphorylation sites, crucial for cellular signaling.
  • Protein phosphorylation is a dynamic process regulated by kinases and phosphatases.
  • Large-scale analysis of phosphorylation events has advanced significantly.

Purpose of the Study:

  • To summarize the current state of large-scale phosphoproteomics.
  • To highlight the rapid growth of phosphoproteomics data.
  • To identify key technological drivers in the field.

Main Methods:

  • Leveraging public data repositories containing phosphoproteomics information.
  • Analyzing trends in data generation rates.
  • Identifying contributions of technological advancements, including phosphopeptide enrichment and mass spectrometry.

Main Results:

  • Public databases currently list approximately 25,000 phosphorylation sites on 7,000 human proteins.
  • The volume of phosphoproteomics data is increasing exponentially, with studies reporting around 10,000 new sites.
  • Advances in selective phosphopeptide enrichment and sensitive mass spectrometry are primary contributors to this growth.

Conclusions:

  • Global phosphoproteomics is a rapidly expanding field.
  • Technological innovations are key to the accelerating discovery of phosphorylation sites.
  • The growing dataset will enhance understanding of cellular signaling pathways.