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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...
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.
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...

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Related Experiment Video

Updated: Jun 17, 2026

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
10:17

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

Published on: April 29, 2022

Understanding protein phosphorylation on a systems level.

Jimmy Lin1, Zhi Xie, Heng Zhu

  • 1Department of Ophthalmology, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.

Briefings in Functional Genomics
|January 9, 2010
PubMed
Summary
This summary is machine-generated.

This study reviews experimental and computational methods for analyzing protein phosphorylation. It highlights how high-throughput techniques and network models advance our understanding of cellular functions regulated by phosphorylation.

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Identification of Post-translational Modifications of Plant Protein Complexes
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Identification of Post-translational Modifications of Plant Protein Complexes

Published on: February 22, 2014

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Last Updated: Jun 17, 2026

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
10:17

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

Published on: April 29, 2022

Identification of Post-translational Modifications of Plant Protein Complexes
10:07

Identification of Post-translational Modifications of Plant Protein Complexes

Published on: February 22, 2014

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Systems Biology

Background:

  • Protein kinase phosphorylation is crucial for regulating protein and cellular functions.
  • High-throughput techniques have significantly advanced the study of protein phosphorylation over the last decade.
  • Computational network models offer insights into cellular processes governed by phosphorylation.

Purpose of the Study:

  • To provide an overview of experimental and computational techniques for systems-level analysis of protein phosphorylation.
  • To highlight advancements in identifying and analyzing phosphoproteins and phosphorylation events.
  • To discuss the integration of technological and computational improvements in phosphorylation research.

Main Methods:

  • Overview of high-throughput experimental approaches for phosphoproteomics.
  • Discussion of computational network modeling techniques for phosphorylation data.
  • Integration of experimental and computational strategies for systems-level analysis.

Main Results:

  • High-throughput methods enable rapid and unbiased surveys of phosphorylation.
  • Network models reveal complex cellular pathways regulated by phosphorylation.
  • Combined approaches offer a comprehensive understanding of phosphorylation networks.

Conclusions:

  • Systems-level analysis of protein phosphorylation is increasingly feasible through integrated techniques.
  • Advancements in experimental and computational methods are revolutionizing the field.
  • Understanding phosphorylation networks is key to deciphering cellular regulation and function.