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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...
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.
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...

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Phosphoproteomic Strategy for Profiling Osmotic Stress Signaling in Arabidopsis
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P(3)DB: An Integrated Database for Plant Protein Phosphorylation.

Qiuming Yao1, Curtis Bollinger, Jianjiong Gao

  • 1Department of Computer Science, University of Missouri Columbia, MO, USA.

Frontiers in Plant Science
|September 14, 2012
PubMed
Summary

Researchers created P(3)DB, a plant protein phosphorylation database, to archive and analyze thousands of experimentally determined phosphorylation sites. This resource aids in identifying conserved signaling pathways across multiple plant species.

Keywords:
P3DBdata repositorymass spectrometryphosphoproteomicsplantsprotein phosphorylation

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Published on: May 3, 2018

Area of Science:

  • Molecular Biology
  • Plant Science
  • Biochemistry

Background:

  • Protein phosphorylation is a crucial post-translational modification in eukaryotes.
  • Plants exhibit a high frequency of protein kinases, indicating the importance of phosphorylation in plant signaling.
  • Phosphorylation site mapping has advanced significantly with high-resolution mass spectrometry.

Purpose of the Study:

  • To develop a centralized, user-friendly database for plant protein phosphorylation site data.
  • To facilitate the archiving and querying of thousands of experimentally determined phosphorylation sites in plants.
  • To enable the identification of functionally conserved phosphorylation sites across different plant species.

Main Methods:

  • Development of the Plant Protein Phosphorylation Database (P(3)DB) at p3db.org.
  • Collation of 32,963 non-redundant phosphorylation sites from 23 experimental studies across six plant species.
  • Integration of a BLAST module for querying protein sequences and identifying similar sites.

Main Results:

  • P(3)DB provides a comprehensive repository of plant protein phosphorylation data.
  • The database hosts over 32,000 non-redundant phosphorylation sites.
  • The integrated BLAST tool allows for comparative analysis of phosphorylation sites across species.

Conclusions:

  • P(3)DB serves as a valuable resource for plant biologists studying phosphorylation.
  • The database facilitates research into conserved phosphorylation events and signaling pathways in plants.
  • This resource supports a multi-system approach to understanding plant phosphorylation.