Journal
FEBS JOURNAL
Volume 287, Issue 13, Pages 2664-2684Publisher
WILEY
DOI: 10.1111/febs.15213
Keywords
Complex Portal; curation; phosphatase complex; protein database; UniProtKB
Categories
Funding
- National Eye Institute (NEI)
- National Human Genome Research Institute (NHGRI)
- National Heart, Lung, and Blood Institute (NHLBI)
- National Institute of Allergy and Infectious Diseases (NIAID)
- National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
- National Institute of General Medical Sciences (NIGMS)
- National Institute of Mental Health (NIMH) of the National Institute of Health [U24HG007822]
- Swiss Federal Government through the State Secretariat for Education, Research and Innovation
- European Molecular Biology Labora-tory core funds
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Phosphatases play an essential role in the regulation of protein phosphorylation. Less abundant than kinases, many phosphatases are components of one or more macromolecular complexes with different substrate specificities and specific functionalities. The expert scientific curation of phosphatase complexes for the UniProt and Complex Portal databases supports the whole scientific community by collating and organising small- and large-scale experimental data from the scientific literature into context-specific central resources, where the data can be freely accessed and used to further academic and translational research. In this review, we discuss how the diverse biological functions of phosphatase complexes are presented in UniProt and the Complex Portal, and how understanding the biological significance of phosphatase complexes in Caenorhabditis elegans offers insight into the mechanisms of substrate diversity in a variety of cellular and molecular processes.
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