NetworKIN: a resource for exploring cellular phosphorylation networks

Linding, R.; Jensen, L.J.; Pasculescu, A.; Olhovsky, M.; Colwill, K.; Bork, P.; Yaffe, M.B.; Pawson, T.

NetworKIN: a resource for exploring cellular phosphorylation networks

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Item Type:	Article
Title:	NetworKIN: a resource for exploring cellular phosphorylation networks
Creators Name:	Linding, R., Jensen, L.J., Pasculescu, A., Olhovsky, M., Colwill, K., Bork, P., 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
ISSN:	0305-1048
Publisher:	Oxford University Press
Volume:	36
Number:	Database issue
Page Range:	D695-D699
Date:	January 2008
Official Publication:	https://doi.org/10.1093/nar/gkm902
PubMed:	View item in PubMed

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