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Updated: Jun 21, 2026
11:13
Identification of Kinase-substrate Pairs Using High Throughput Screening
Published on: August 29, 2015
Genomics and evolution of protein phosphatases
Mark J Chen1,2, Jack E Dixon3, Gerard Manning4,2
1Department of Bioinformatics and Computational Biology, Genentech Inc., South San Francisco, CA 94080, USA.
Science Signaling
|April 13, 2017
Summary
This study catalogs the human protein phosphatome, revealing conserved and divergent evolutionary paths for protein phosphatases across eukaryotes. Understanding these enzyme families is crucial for analyzing cellular processes regulated by protein phosphorylation.
Area of Science:
- Biochemistry
- Evolutionary Biology
- Genomics
Background:
- Protein phosphatases counteract protein kinases, regulating cellular phosphorylation.
- Understanding the protein phosphatome is key to deciphering cellular processes.
Purpose of the Study:
- To catalog the human protein phosphatome and analyze its evolutionary history.
- To compare human phosphatases with those from other eukaryotes.
Main Methods:
- Genomic cataloging of human protein phosphatase genes and pseudogenes.
- Comparative phosphatome analysis across nine eukaryotic species.
- Classification of phosphatases into folds, families, and subfamilies.
- Analysis of evolutionary dynamics, including gene losses and expansions.
Main Results:
- Cataloged 189 human protein phosphatase genes and 79 pseudogenes/retrogenes.
- Classified phosphatases into 10 folds, 21 families, and 178 subfamilies across species.
- >80% of human subfamilies are conserved in animals, with significant evolutionary variation.
- Identified 26 predicted catalytically disabled human protein phosphatase domains.
Conclusions:
- The human protein phosphatome exhibits deep evolutionary conservation alongside species-specific adaptations.
- Comparative genomics reveals insights into the evolution of protein phosphorylation regulation.
- This work provides a framework for global analysis of protein phosphorylation in the animal kingdom.
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