From the research laboratory to the database: the Caenorhabditis elegans kinome in UniProtKB


Zaru R., Magrane M., O'Donovan C., Bateman A., Martin M. J. , Alpi E., ...More

BIOCHEMICAL JOURNAL, vol.474, pp.493-515, 2017 (Journal Indexed in SCI) identifier identifier identifier

  • Publication Type: Article / Review
  • Volume: 474
  • Publication Date: 2017
  • Doi Number: 10.1042/bcj20160991
  • Title of Journal : BIOCHEMICAL JOURNAL
  • Page Numbers: pp.493-515

Abstract

Protein kinases form one of the largest protein families and are found in all species, from viruses to humans. They catalyze the reversible phosphorylation of proteins, often modifying their activity and localization. They are implicated in virtually all cellular processes and are one of the most intensively studied protein families. In recent years, they have become key therapeutic targets in drug development as natural mutations affecting kinase genes are the cause of many diseases. The vast amount of data contained in the primary literature and across a variety of biological data collections highlights the need for a repository where this information is stored in a concise and easily accessible manner. The UniProt Knowledgebase meets this need by providing the scientific community with a comprehensive, high-quality and freely accessible resource of protein sequence and functional information. Here, we describe the expert curation process for kinases, focusing on the Caenorhabditis elegans kinome. The C. elegans kinome is composed of 438 kinases and almost half of them have been functionally characterized, highlighting that C. elegans is a valuable and versatile model organism to understand the role of kinases in biological processes.