NetworKIN: a resource for exploring cellular phosphorylation networks

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

NetworKIN : a resource for exploring cellular phosphorylation networks. / Linding, Rune; Jensen, Lars Juhl; Pasculescu, Adrian; Olhovsky, Marina; Colwill, Karen; Bork, Peer; Yaffe, Michael B; Pawson, Tony.

In: Nucleic Acids Research, Vol. 36, No. Database issue, 2008, p. D695-9.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Linding, R, Jensen, LJ, Pasculescu, A, Olhovsky, M, Colwill, K, Bork, P, Yaffe, MB & Pawson, T 2008, 'NetworKIN: a resource for exploring cellular phosphorylation networks', Nucleic Acids Research, vol. 36, no. Database issue, pp. D695-9. https://doi.org/10.1093/nar/gkm902

APA

Linding, R., Jensen, L. J., Pasculescu, A., Olhovsky, M., Colwill, K., Bork, P., Yaffe, M. B., & Pawson, T. (2008). NetworKIN: a resource for exploring cellular phosphorylation networks. Nucleic Acids Research, 36(Database issue), D695-9. https://doi.org/10.1093/nar/gkm902

Vancouver

Linding R, Jensen LJ, Pasculescu A, Olhovsky M, Colwill K, Bork P et al. NetworKIN: a resource for exploring cellular phosphorylation networks. Nucleic Acids Research. 2008;36(Database issue):D695-9. https://doi.org/10.1093/nar/gkm902

Author

Linding, Rune ; Jensen, Lars Juhl ; Pasculescu, Adrian ; Olhovsky, Marina ; Colwill, Karen ; Bork, Peer ; Yaffe, Michael B ; Pawson, Tony. / NetworKIN : a resource for exploring cellular phosphorylation networks. In: Nucleic Acids Research. 2008 ; Vol. 36, No. Database issue. pp. D695-9.

Bibtex

@article{64e6b1da9de34537a8679a850bab10c5,
title = "NetworKIN: a resource for exploring cellular phosphorylation networks",
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.",
author = "Rune Linding and Jensen, {Lars Juhl} and Adrian Pasculescu and Marina Olhovsky and Karen Colwill and Peer Bork and Yaffe, {Michael B} and Tony Pawson",
year = "2008",
doi = "10.1093/nar/gkm902",
language = "English",
volume = "36",
pages = "D695--9",
journal = "Nucleic Acids Research",
issn = "0305-1048",
publisher = "Oxford University Press",
number = "Database issue",

}

RIS

TY - JOUR

T1 - NetworKIN

T2 - a resource for exploring cellular phosphorylation networks

AU - Linding, Rune

AU - Jensen, Lars Juhl

AU - Pasculescu, Adrian

AU - Olhovsky, Marina

AU - Colwill, Karen

AU - Bork, Peer

AU - Yaffe, Michael B

AU - Pawson, Tony

PY - 2008

Y1 - 2008

N2 - 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.

AB - 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.

U2 - 10.1093/nar/gkm902

DO - 10.1093/nar/gkm902

M3 - Journal article

C2 - 17981841

VL - 36

SP - D695-9

JO - Nucleic Acids Research

JF - Nucleic Acids Research

SN - 0305-1048

IS - Database issue

ER -

ID: 40740202