Abstract
We present here EKPD (http://ekpd.biocuckoo.org), a hierarchical database of eukaryotic protein kinases (PKs) and protein phosphatases (PPs), the key molecules responsible for the reversible phosphorylation of proteins that are involved in almost all aspects of biological processes. As extensive experimental and computational efforts have been carried out to identify PKs and PPs, an integrative resource with detailed classification and annotation information would be of great value for both experimentalists and computational biologists. In this work, we first collected 1855 PKs and 347 PPs from the scientific literature and various public databases. Based on previously established rationales, we classified all of the known PKs and PPs into a hierarchical structure with three levels, i.e. group, family and individual PK/PP. There are 10 groups with 149 families for the PKs and 10 groups with 33 families for the PPs. We constructed 139 and 27 Hidden Markov Model profiles for PK and PP families, respectively. Then we systematically characterized ∼50 000 PKs and >10 000 PPs in eukaryotes. In addition, >500 PKs and >400 PPs were computationally identified by ortholog search. Finally, the online service of the EKPD database was implemented in PHP + MySQL + JavaScript.
Highlights
As one of the most important post-translational modifications of proteins, the reversible phosphorylation is involved in a broad spectrum of biological processes [1,2]
The identification of the eukaryotic protein kinases and PPs is fundamental to a proper understanding of regulatory mechanisms of the reversible phosphorylation and will provide potential drug targets for biomedical design [6,7]
In 1995, Hanks and Hunter carried out a pilot study in which eukaryotic protein kinases (ePKs) were classified into a hierarchical structure with four levels, including group, family, subfamily and individual protein kinases (PKs) based on the conserved sequence and structural profile of the kinase domain [2]
Summary
As one of the most important post-translational modifications of proteins, the reversible phosphorylation is involved in a broad spectrum of biological processes [1,2]. In 1995, Hanks and Hunter carried out a pilot study in which ePKs were classified into a hierarchical structure with four levels, including group, family, subfamily and individual PKs based on the conserved sequence and structural profile of the kinase (catalytic) domain [2].
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