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Related Concept Videos

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.
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...
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 Modifications in the RER01:26

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.

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Related Experiment Video

Updated: Jun 6, 2026

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes
09:10

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes

Published on: May 22, 2018

PHOSIDA 2011: the posttranslational modification database.

Florian Gnad1, Jeremy Gunawardena, Matthias Mann

  • 1Department of Proteomics and Signal Transduction, Max-Planck-Institute for Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany.

Nucleic Acids Research
|November 18, 2010
PubMed
Summary
This summary is machine-generated.

PHOSIDA manages over 80,000 post-translational modification sites, including phosphorylation, N-glycosylation, and acetylation, across nine species. This resource offers analysis tools for in silico prediction and motif discovery in proteomic data.

Related Experiment Videos

Last Updated: Jun 6, 2026

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes
09:10

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes

Published on: May 22, 2018

Area of Science:

  • Proteomics
  • Bioinformatics
  • Molecular Biology

Background:

  • Post-translational modifications (PTMs) are crucial for protein function.
  • Accurate identification and management of PTM sites are essential for biological research.

Purpose of the Study:

  • To present the expanded PHOSIDA database, a comprehensive resource for managing and analyzing PTM sites.
  • To highlight the integrated analysis tools available within PHOSIDA.

Main Methods:

  • Curated collection of over 80,000 PTM sites (phosphorylated, N-glycosylated, acetylated) from nine species.
  • Data acquired using high-resolution mass spectrometry with stringent quality control.
  • Development of species-specific prediction tools for phosphorylation and acetylation sites.

Main Results:

  • PHOSIDA now includes >80,000 PTM sites, significantly expanding its scope since the last report.
  • The database integrates high-resolution proteomic data with multiple annotations.
  • Prediction platform enables in silico determination of modified sites based on primary sequence.

Conclusions:

  • PHOSIDA serves as a valuable, continuously growing resource for PTM research.
  • The integrated database, prediction, and toolkit components facilitate advanced proteomic data analysis.
  • PHOSIDA supports in silico analysis and motif discovery for post-translational modifications.