HuPho: the human phosphatase portal.
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.
Department of Biology, University of Rome Tor Vergata, Rome, Italy. susanna.liberti@gmail.com
Susanna
S
Liberti
Francesca
F
Sacco
Alberto
A
Calderone
Livia
L
Perfetto
Marta
M
Iannuccelli
Simona
S
Panni
Elena
E
Santonico
Anita
A
Palma
Aurelio P
AP
Nardozza
Luisa
L
Castagnoli
Gianni
G
Cesareni
D019295:Computational Biology / Q000379:methods*; D030562:Databases, Protein; D006801:Humans; D016247:Information Storage and Retrieval / Q000379:methods; D020407:Internet; D010744:Phosphoric Monoester Hydrolases / Q000737:chemistry / Q000145:classification / Q000378:metabolism*; D010766:Phosphorylation; D011485:Protein Binding; D040901:Proteomics; D013379:Substrate Specificity
D010744:Phosphoric Monoester Hydrolases