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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...
Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
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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Updated: May 11, 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

Elucidating human phosphatase-substrate networks.

Xun Li1, Matthias Wilmanns, Janet Thornton

  • 1Genome Biology Unit, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany.

Science Signaling
|May 16, 2013
PubMed
Summary
This summary is machine-generated.

This study introduces a new classification for human phosphatases, revealing hidden connections and substrate recognition patterns. The findings aid in understanding phosphatase function and generating new research hypotheses.

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Identification of Kinase-substrate Pairs Using High Throughput Screening
11:13

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

Related Experiment Videos

Last Updated: May 11, 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 Kinase-substrate Pairs Using High Throughput Screening
11:13

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Bioinformatics

Background:

  • Phosphatases are essential enzymes regulating cellular functions through dephosphorylation.
  • Understanding human phosphatase activity and substrate interactions is critical for cell biology.

Purpose of the Study:

  • To develop a structure-based classification of human phosphatases.
  • To elucidate previously unrecognized relationships between phosphatases and their substrates.
  • To create a comprehensive human phosphatase-substrate network and database.

Main Methods:

  • Collating protein and nonprotein substrates.
  • Integrating colocalization and coexpression data.
  • Structure-based classification and sequence analysis of human phosphatases.
  • Developing the DEPOD database.

Main Results:

  • A novel structure-based classification scheme for active human phosphatases was established.
  • A human phosphatase-substrate network was generated, highlighting common recognition mechanisms with kinases.
  • Analysis revealed preferred substrate domains and identified phosphatases with varying substrate specificities.
  • The DEPOD database (http://www.DEPOD.org) was launched as a resource for human phosphatase information.

Conclusions:

  • The classification and network analysis provide new insights into phosphatase-substrate interactions and biological roles.
  • This work facilitates hypothesis generation for phosphatase function and drug discovery.
  • DEPOD serves as a valuable online resource for researchers in the field.