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Updated: May 20, 2026
10:17
A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
Published on: April 29, 2022
HuPho: the human phosphatase portal
Susanna Liberti1, Francesca Sacco, Alberto Calderone
1Department of Biology, University of Rome Tor Vergata, Rome, Italy. susanna.liberti@gmail.com
The FEBS Journal
|July 19, 2012
Summary
This study introduces HuPho, a website for accessing information on human protein phosphatases. It integrates data from public resources and scientific literature to aid cell signaling research.
Area of Science:
- Biochemistry
- Molecular Biology
- Bioinformatics
Background:
- Protein phosphorylation is crucial for cellular processes.
- Phosphatases and kinases maintain phosphorylation balance.
- Understanding phosphatase function is key to cell signaling.
Purpose of the Study:
- To create a centralized resource for human protein phosphatase information.
- To facilitate retrieval and integration of phosphatase-related data.
- To support mechanistic descriptions of cell signaling pathways.
Main Methods:
- Developed a dedicated search engine for human protein phosphatases.
- Integrated data from multiple public web resources.
- Employed text-mining for literature-based data extraction.
Main Results:
- Launched the HuPho website (http://hupho.uniroma2.it).
- Consolidated information on human protein phosphatases.
- Enabled efficient data retrieval from diverse sources.
Conclusions:
- HuPho provides a valuable tool for researchers studying protein phosphorylation.
- The website aids in understanding phosphatase roles in cell signaling.
- Facilitates systematic analysis of phosphatase function and targets.
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