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Related Concept Videos

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.
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...
Protein Families02:47

Protein Families

Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism.   Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members.   If these new proteins contain similar amino acids in key locations, protein...
Cell Specific Gene Expression01:58

Cell Specific Gene Expression

Multicellular organisms contain a variety of structurally and functionally distinct cell types, but the DNA in all the cells originated from the same parent cells. The differences in the cells can be attributed to the differential gene expression. Liver cells, whose functions include detoxification of blood, production of bile to metabolize fats, and synthesis of proteins essential for metabolism, must express a specific set of genes to perform their functions. Gene expression also varies with...

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Related Experiment Video

Updated: Jun 28, 2026

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

P3DB: a plant protein phosphorylation database.

Jianjiong Gao1, Ganesh Kumar Agrawal, Jay J Thelen

  • 1Department of Computer Science, Department of Biochemistry and C.S. Bond Life Sciences Center, University of Missouri, Columbia, MO 65211, USA.

Nucleic Acids Research
|October 22, 2008
PubMed
Summary
This summary is machine-generated.

P(3)DB is a comprehensive plant protein phosphorylation database, offering the largest collection of plant phosphorylation data. This resource aids researchers in exploring protein phosphorylation across various plant species.

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Phosphoproteomic Strategy for Profiling Osmotic Stress Signaling in Arabidopsis

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Identification of Post-translational Modifications of Plant Protein Complexes
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Published on: February 22, 2014

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

  • Biochemistry
  • Molecular Biology
  • Bioinformatics

Background:

  • Protein phosphorylation is a critical post-translational modification regulating numerous cellular processes in plants.
  • Existing resources for plant phosphorylation data are fragmented, hindering comprehensive analysis.
  • A centralized, searchable database is needed to consolidate and facilitate access to this vital information.

Purpose of the Study:

  • To establish P(3)DB, a centralized, web-accessible database for plant protein phosphorylation data.
  • To provide a comprehensive resource for researchers studying protein phosphorylation in plants.
  • To integrate data from multiple plant species and literature sources.

Main Methods:

  • Data compilation from large-scale studies (oilseed rape, Arabidopsis thaliana, soybean) and literature.
  • Development of a web-based interface for browsing, searching, and downloading data.
  • Integration of BLAST and phosphopeptide BLAST browser utilities for sequence similarity searches.

Main Results:

  • P(3)DB currently holds 14,670 nonredundant phosphorylation sites from 6382 substrate proteins in oilseed rape, the largest collection to date.
  • The database is continuously updated with data from Arabidopsis thaliana, soybean, and current literature.
  • User-friendly tools, including BLAST, enable efficient querying and analysis of phosphopeptide data.

Conclusions:

  • P(3)DB serves as a valuable, centralized resource for plant phosphorylation data.
  • The integrated search and analysis tools enhance its utility for plant and non-plant biologists.
  • This database will significantly advance research in plant protein phosphorylation and related fields.