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Phosphorylation

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 Kinases and Phosphatases

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 Phosphatases

Protein Kinases and Phosphatases

Covalently Linked Protein Regulators

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....

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Related Experiment Video

Updated: Jan 11, 2026

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

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

Published on: May 22, 2018

SIGNOR 4.0: the 2025 update with focus on phosphorylation data.

Prisca Lo Surdo¹, Marta Iannuccelli², Klas Karis³

¹Department of Biology and Biotechnologies "Charles Darwin", Laboratory affiliated to Istituto Pasteur Italia-Fondazione Cenci Bolognetti, La Sapienza University of Rome, Rome 00185, Italy.

Nucleic Acids Research

|November 17, 2025

Summary

This summary is machine-generated.

The SIGNOR 4.0 database now offers enhanced signaling network data, including a new PhosphoSIGNOR interface for detailed phosphorylation analysis. This resource aids in mapping cellular signaling alterations and understanding disease mechanisms.

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Area of Science:

Systems Biology
Molecular Biology
Bioinformatics

Background:

The SIGnaling Network Open Resource (SIGNOR) is a manually curated database of causal biological interactions.
Signaling events are annotated with effects (activation/inactivation) and mechanisms (e.g., phosphorylation).

Purpose of the Study:

To present the latest update (version 4.0) of the SIGNOR database.
To introduce PhosphoSIGNOR, a specialized subdomain for phosphorylation data.
To enhance data curation and expand the scope of signaling network analysis.

Main Methods:

Manual curation of causal interactions between biological entities.
Integration of text-mining tools for assisted curation.
Development of a dedicated user interface (PhosphoSIGNOR) for phosphorylation data.
Expansion of curation efforts, focusing on phosphorylation events.

Main Results:

SIGNOR 4.0 features improved curation tools and increased content, with a focus on phosphorylation.
PhosphoSIGNOR provides targeted access and visualization of phosphorylation-specific information.
The expanded dataset facilitates comprehensive mapping of signaling alterations and their link to cellular processes.

Conclusions:

SIGNOR 4.0 and PhosphoSIGNOR offer a robust resource for exploring signaling networks.
The platform supports hypothesis generation and mechanistic insights, particularly in cancer systems biology.
Enhanced data accessibility and visualization empower researchers in understanding complex cellular signaling.