NAR Molecular Biology Database Collection entry number 1788
Guangyou Duan, Xun Li, Maja Köhn
European Molecular Biology Laboratory, Genome Biology Unit, Meyerhofstrasse 1, 69117 Heidelberg, Germany
DEPOD - the human DEPhOsphorylation Database (version 1.1) is a manually curated database collecting human active and inactive phosphatases, their experimentally verified protein and non-protein substrates, and dephosphorylation site information, and pathways in which they are involved. It also provides links to popular kinase databases and protein-protein interaction databases for these phosphatases and substrates. DEPOD aims to be a valuable resource for studying human phosphatases and their substrate specificities and molecular mechanisms; phosphatase-targeted drug discovery and development; connecting phosphatases with kinases through their common substrates; completing the human phosphorylation/dephosphorylation network.
Since the first release, more human phosphatases and substrates, their associated signaling pathways (also from new sources), and interacting proteins for all phosphatases and protein substrates have been added into DEPOD. The user interface has been further optimized; for example, the interactive human phosphatase–substrate network contains now a ‘highlight node’ function for phosphatases, which includes the visualization of neighbors in the network.
The authors would like to thank the users of DEPOD for their support as well as colleagues and users for their feedback to the DEPOD database. X.L. thanks EMBL and Marie Curie Actions for the EMBL Interdisciplinary Postdoc (EIPOD) fellowship. M.K. thanks the German Science Foundation (DFG) for support within the Emmy-Noether program.
Li, X., Wilmanns, M., Thornton, J. and Kohn, M. (2013) Elucidating Human Phosphatase-Substrate Networks. Sci. Signal., 6, rs10.
Category: Protein sequence databases
Subcategory: Databases of individual protein families
Go to the article in the NAR Database issue.
Oxford University Press is not responsible for the content of external internet sites