Linear motif atlas for phosphorylation-dependent signaling
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Linear motif atlas for phosphorylation-dependent signaling. / Miller, Martin Lee; Jensen, Lars Juhl; Diella, Francesca; Jørgensen, Claus; Tinti, Michele; Li, Lei; Hsiung, Marilyn; Parker, Sirlester A; Bordeaux, Jennifer; Sicheritz-Ponten, Thomas; Olhovsky, Marina; Pasculescu, Adrian; Alexander, Jes; Knapp, Stefan; Blom, Nikolaj; Bork, Peer; Li, Shawn; Cesareni, Gianni; Pawson, Tony; Turk, Benjamin E; Yaffe, Michael B; Brunak, Søren; Linding, Rune.
In: Science Signaling, Vol. 1, No. 35, 2008, p. ra2.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Linear motif atlas for phosphorylation-dependent signaling
AU - Miller, Martin Lee
AU - Jensen, Lars Juhl
AU - Diella, Francesca
AU - Jørgensen, Claus
AU - Tinti, Michele
AU - Li, Lei
AU - Hsiung, Marilyn
AU - Parker, Sirlester A
AU - Bordeaux, Jennifer
AU - Sicheritz-Ponten, Thomas
AU - Olhovsky, Marina
AU - Pasculescu, Adrian
AU - Alexander, Jes
AU - Knapp, Stefan
AU - Blom, Nikolaj
AU - Bork, Peer
AU - Li, Shawn
AU - Cesareni, Gianni
AU - Pawson, Tony
AU - Turk, Benjamin E
AU - Yaffe, Michael B
AU - Brunak, Søren
AU - Linding, Rune
PY - 2008
Y1 - 2008
N2 - Systematic and quantitative analysis of protein phosphorylation is revealing dynamic regulatory networks underlying cellular responses to environmental cues. However, matching these sites to the kinases that phosphorylate them and the phosphorylation-dependent binding domains that may subsequently bind to them remains a challenge. NetPhorest is an atlas of consensus sequence motifs that covers 179 kinases and 104 phosphorylation-dependent binding domains [Src homology 2 (SH2), phosphotyrosine binding (PTB), BRCA1 C-terminal (BRCT), WW, and 14-3-3]. The atlas reveals new aspects of signaling systems, including the observation that tyrosine kinases mutated in cancer have lower specificity than their non-oncogenic relatives. The resource is maintained by an automated pipeline, which uses phylogenetic trees to structure the currently available in vivo and in vitro data to derive probabilistic sequence models of linear motifs. The atlas is available as a community resource (http://netphorest.info).
AB - Systematic and quantitative analysis of protein phosphorylation is revealing dynamic regulatory networks underlying cellular responses to environmental cues. However, matching these sites to the kinases that phosphorylate them and the phosphorylation-dependent binding domains that may subsequently bind to them remains a challenge. NetPhorest is an atlas of consensus sequence motifs that covers 179 kinases and 104 phosphorylation-dependent binding domains [Src homology 2 (SH2), phosphotyrosine binding (PTB), BRCA1 C-terminal (BRCT), WW, and 14-3-3]. The atlas reveals new aspects of signaling systems, including the observation that tyrosine kinases mutated in cancer have lower specificity than their non-oncogenic relatives. The resource is maintained by an automated pipeline, which uses phylogenetic trees to structure the currently available in vivo and in vitro data to derive probabilistic sequence models of linear motifs. The atlas is available as a community resource (http://netphorest.info).
KW - 14-3-3 Proteins
KW - Amino Acid Motifs
KW - Animals
KW - BRCA1 Protein
KW - Consensus Sequence
KW - Databases, Protein
KW - Humans
KW - Phosphorylation
KW - Phosphotransferases
KW - Phosphotyrosine
KW - Protein Binding
KW - Signal Transduction
KW - src Homology Domains
U2 - 10.1126/scisignal.1159433
DO - 10.1126/scisignal.1159433
M3 - Journal article
C2 - 18765831
VL - 1
SP - ra2
JO - Science Signaling
JF - Science Signaling
SN - 1945-0877
IS - 35
ER -
ID: 40740054