Helmholtz Gemeinschaft


NetworKIN: a resource for exploring cellular phosphorylation networks

[img] PDF - Requires a PDF viewer such as GSview, Xpdf or Adobe Acrobat Reader

Item Type:Article
Title:NetworKIN: a resource for exploring cellular phosphorylation networks
Creators Name:Linding, R. and Jensen, L.J. and Pasculescu, A. and Olhovsky, M. and Colwill, K. and Bork, P. and Yaffe, M.B. and Pawson, T.
Abstract:Protein kinases control cellular responses by phosphorylating specific substrates. Recent proteome-wide mapping of protein phosphorylation sites by mass spectrometry has discovered thousands of in vivo sites. Systematically assigning all 518 human kinases to all these sites is a challenging problem. The NetworKIN database (http://networkin.info) integrates consensus substrate motifs with context modelling for improved prediction of cellular kinase-substrate relations. Based on the latest human phosphoproteome from the Phospho.ELM and PhosphoSite databases, the resource offers insight into phosphorylation-modulated interaction networks. Here, we describe how NetworKIN can be used for both global and targeted molecular studies. Via the web interface users can query the database of precomputed kinase-substrate relations or obtain predictions on novel phosphoproteins. The database currently contains a predicted phosphorylation network with 20 224 site-specific interactions involving 3978 phosphoproteins and 73 human kinases from 20 families.
Keywords:Amino Acid Sequence, Consensus Sequence, Internet, Phosphoproteins, Phosphorylation, Protein Databases, Protein Kinases, Proteomics, User-Computer Interface
Source:Nucleic Acids Research
Publisher:Oxford University Press (U.K.)
Number:Database issue
Page Range:D695-D699
Date:January 2008
Official Publication:https://doi.org/10.1093/nar/gkm902
PubMed:View item in PubMed

Repository Staff Only: item control page


Downloads per month over past year

Open Access
MDC Library