HuPho: the human phosphatase portal

FEBS J. 2013 Jan;280(2):379-87. doi: 10.1111/j.1742-4658.2012.08712.x. Epub 2012 Aug 24.

Abstract

Phosphatases and kinases contribute to the regulation of protein phosphorylation homeostasis in the cell. Phosphorylation is a key post-translational modification underlying the regulation of many cellular processes. Thus, a comprehensive picture of phosphatase function and the identification of their target substrates would aid a systematic approach to a mechanistic description of cell signalling. Here we present a website designed to facilitate the retrieval of information about human protein phosphatases. To this end we developed a search engine to recover and integrate information annotated in several publicly available web resources. In addition we present a text-mining-assisted annotation effort aimed at extracting phosphatase related data reported in the scientific literature. The HuPho (human phosphatases) website can be accessed at http://hupho.uniroma2.it.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Computational Biology / methods*
  • Databases, Protein
  • Humans
  • Information Storage and Retrieval / methods
  • Internet*
  • Phosphoric Monoester Hydrolases / chemistry
  • Phosphoric Monoester Hydrolases / classification
  • Phosphoric Monoester Hydrolases / metabolism*
  • Phosphorylation
  • Protein Binding
  • Proteomics
  • Substrate Specificity

Substances

  • Phosphoric Monoester Hydrolases