JPOST Repositoryapplication/xmlhttps://storage.jpostdb.org/JPST002915/files/mai100527_012DYRK2.maxq.txthttps://storage.jpostdb.org/JPST002915/files/mai100527_012DYRK2.txthttps://storage.jpostdb.org/JPST002915/files/rawfiles.txtprimaryOK200ProteomicsYasushi IshihamaHomo Sapiens (human)https://repository.jpostdb.org/entry/JPST002915jPOSTjPOSTbig, DYRK2, scale tissue, human being, gyltl1b-b, D16Ertd493e., dDYRK2, Dyrk, Gm10783, peltate hair, Modern, Mbp1, CG4551, froggy, Gyltl1a, Human, D16Ertd272e, DmelCG4551, large, PSK47, Mp86, Dm2, Homo sapiens, MDDGA6, mKIAA0609, DYRK, Dyrk2, scales, 1810038L18Rik, myd, KIAA0609, Man, fg, mmb, gyltl1b, Man (Taxonomy), 2310043O08Rik, scale, MDDGB6, plant peltate hair, mdc1d, expanded, Mbp-1, LARGE, human, BG:DS01523.3, BPFD#36, MDC1D, Mnbh, enr, enlarged, great, Modern Man, ENSMUSG00000074897, humansSignal Transduction Systems, Signal Transductions, para Tyrosine, human being, Peptidomics, Receptor-Mediated, number, Signal Transduction System, L-Threonine, presence, Migrant Workers, Human, 2-Amino-3-hydroxypropionic acid, Receptor Mediated Signal Transduction, Signal Transduction, Homo sapiens, Kinase, Cell Signaling, Man, Phosphotransferase, Threonin, signal transduction by protein phosphorylation, Man (Taxonomy), Migrant Worker, Transients, 2-amino-3-(4-hydroxyphenyl)propanoic acid, 3-(p-Hydroxyphenyl)alanine, Nonmigrant, Signal, Pathways, Nonmigrants, Signal Pathways, L Threonine, Transphosphorylase, Worker, Y, Signal Transduction Pathway, Transient, project description., Squatter, set, signalling pathway, 2-amino-3-hydroxypropanoic acid, L Tyrosine, grupos, Tyr, Squatters, signal transduction by cis-phosphorylation, Signal Transduction Pathways, Transductions, Tyrosin, ATP Phosphotransferases, Signal Pathway, ATP, single organism signaling, Pathway, grupo, Modern, 2-Amino-3-(p-hydroxyphenyl)propionic acid, signal transduction by conformational transition, Receptor-Mediated Signal Transductions, total expressed protein, para-Tyrosine, Phosphotransferases, signal transduction by trans-phosphorylation, group, Tyrosine, signaling cascade, count in organism, Serin, 3-Hydroxyalanine, tirosina, Receptor-Mediated Signal Transduction, Migrant, Systems, Nomad, Workers, signalling cascade, Transduction, Migrants and Transients, Transphosphorylases, ensemble, Kinases, System, L-isomer, Rest, human, L isomer, signaling pathway, signalling process, Modern Man, Nomads, Migrants, L Serine, L-Tyrosine, L-Serine, Proteomes, groupe, humans, GruppefalseLarge-scale Discovery of Substrates of the Human Kinome (DYRK2) [Reanalysis: JPST000508]Kinase -networks are important for cellular signal transduction. Despite tremendous efforts to uncover these signaling pathways, huge numbers of uncharacterized phosphosites still remain in the human proteome. Because of the transient nature of kinase-substrate interactions in vivo, it is almost impossible to identify direct substrates. Here, we present a novel strategy for the rapid and high-throughput discovery for of kinase substrates of kinase using quantitative proteomics. Using 385 purified kinases, we identified a total of 175,574 potential direct kinase substrates of kinases. In addition, we identified novel kinase groups, such as one group containing 30 threonine-directed kinases and another containing 15 serine/threonine/tyrosine kinase sgroup. Surprisingly, we observed that the diversity of substrates for tyrosine kinases was much higher than that for serine-threonine kinases. [Original project description]Wed Feb 21 00:00:00 GMT 2024RPXD0499359606