Related Experiment Video
Updated: Jan 1, 2026

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes
Published on: May 22, 2018
The human DEPhOsphorylation Database DEPOD: 2019 update.
1Signalling Research Centres BIOSS and CIBSS, Faculty of Biology, University of Freiburg, Schänzlestrasse 18, 79104 Freiburg, Germany.
The updated human Dephosphorylation Database (DEPOD) now links to 69 databases, offering enhanced tools for exploring phosphatase-kinase networks and dephosphorylation sites. This resource aids research into signaling pathways and disease associations.
Area of Science:
- Biochemistry
- Molecular Biology
- Bioinformatics
Background:
- The human Dephosphorylation Database (DEPOD) is a vital resource for studying human phosphatases, their substrates, and dephosphorylation sites.
- Understanding these interactions is crucial for elucidating cellular signaling pathways.
Purpose of the Study:
- To update and enhance the DEPOD resource with integrated data from external databases.
- To provide improved tools for visualizing and analyzing phosphatase-related biological information.
- To facilitate research on phosphatase-kinase networks and their role in human health.
Main Methods:
- Manual curation of human phosphatases, protein/non-protein substrates, and dephosphorylation sites.
- Integration and linking of annotations from 69 open-access databases (e.g., disease associations, kinases, protein interactions, genome browsers).
- Development of visualization tools for protein interactions, structures, networks, conservation, and motifs.
Main Results:
- The updated DEPOD includes 254 human phosphatases, 336 protein and 83 non-protein substrates, and 1215 curated phosphatase-substrate relationships.
- Enhanced data accessibility with user-friendly download formats.
- Expanded data scope through integration with diverse biological databases.
Conclusions:
- DEPOD serves as a key, continuously updated resource for research on human phosphatase-kinase networks.
- The enhanced database facilitates deeper investigation into dephosphorylation events and associated signaling pathways.
- Improved data accessibility and visualization tools empower researchers in the field.
Related Concept Videos
Phosphorylation
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
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
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein....
Phosphodiester Linkages
Phosphodiester bond forms when a phosphoric acid molecule (H3PO4) links with two hydroxyl groups (–OH) of two other molecules, forming two ester bonds. Two water molecules are released in this process. The phosphodiester bond is commonly found in nucleic acids (DNA and RNA) and plays a critical role in their structure and function.
Phosphodiester Bonds Link Nucleotides Together
DNA and RNA are polynucleotides or long chains of nucleotides that are linked together. A nucleotide is...
Phosphoinositides and PIPs
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...

