NetworKIN: a resource for exploring cellular phosphorylation networks

被引：261

作者：

Linding, Rune ^{[1
,2
,3
]}

Jensen, Lars Juhl

Pasculescu, Adrian ^{[1
]}

Olhovsky, Marina ^{[1
]}

Colwill, Karen ^{[1
]}

Bork, Peer ^{[4
,5
]}

Yaffe, Michael B. ^{[2
]}

Pawson, Tony ^{[1
]}

机构：

[1] Mt Sinai Hosp, Samuel Lunenfeld Res Inst, Toronto, ON, Canada

[2] MIT, Cambridge, MA 02139 USA

[3] Inst Canc Res, London SW3 6JB, England

[4] European Mol Biol Lab, Heidelberg, Germany

[5] Max Delbruck Ctr Mol Med, Berlin, Germany

来源：

NUCLEIC ACIDS RESEARCH | 2008年 / 36卷

关键词：

D O I：

10.1093/nar/gkm902

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：D695 / D699

页数：5

共 16 条

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