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Hudecz"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":["Not available"],"submitter_keywords":["Not available"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PRD000214"],"sample_protocol":["Not available"],"repository":["Pride"],"quantification_method":["Not available"],"modification":["-17.026549","15.994915","57.021464","-18.010565","58.005479","79.966331"],"data_protocol":["Not available"],"omics_type":["Proteomics"],"labhead":["Otto Hudecz"],"instrument_platform":["","Qtrap","FTICR"],"labhead_affiliation":["IMBA - Institute of Molecular Biotechnology"],"submission_type":["PRIDE"],"submitter_mail":["hudecz@imp.univie.ac.at"],"publication":["22067460 Hegemann B, Hutchins JR, Hudecz O, Novatchkova M, Rameseder J, Sykora MM, Liu S, Mazanek M, Lénárt P, Hériché JK, Poser I, Kraut N, Hyman AA, Yaffe MB, Mechtler K, Peters JM; Systematic phosphorylation analysis of human mitotic protein complexes., Sci Signal, 2011 Nov 8, 4, 198, rs12,  10.1126/scisignal.2001993"],"submitter_affiliation":["IMBA - Institute of Molecular Biotechnology"],"submitter_country":["Austria"],"pubmed_abstract":["Progression through mitosis depends on a large number of protein complexes that regulate the major structural and physiological changes necessary for faithful chromosome segregation. Most, if not all, of the mitotic processes are regulated by a set of mitotic protein kinases that control protein activity by phosphorylation. Although many mitotic phosphorylation events have been identified in proteome-scale mass spectrometry studies, information on how these phosphorylation sites are distributed within mitotic protein complexes and which kinases generate these phosphorylation sites is largely lacking. We used systematic protein-affinity purification combined with mass spectrometry to identify 1818 phosphorylation sites in more than 100 mitotic protein complexes. In many complexes, the phosphorylation sites were concentrated on a few subunits, suggesting that these subunits serve as \"switchboards\" to relay the kinase-regulatory signals within the complexes. Consequent bioinformatic analyses identified potential kinase-substrate relationships for most of these sites. In a subsequent in-depth analysis of key mitotic regulatory complexes with the Aurora kinase B (AURKB) inhibitor Hesperadin and a new Polo-like kinase (PLK1) inhibitor, BI 4834, we determined the kinase dependency for 172 phosphorylation sites on 41 proteins. Combination of the results of the cellular studies with Scansite motif prediction enabled us to identify 14 sites on six proteins as direct candidate substrates of AURKB or PLK1."],"pubmed_title":["Systematic phosphorylation analysis of human mitotic protein complexes."],"pubmed_authors":["Hegemann Björn B, Hutchins James R A JR, Hudecz Otto O, Novatchkova Maria M, Rameseder Jonathan J, Sykora Martina M MM, Liu Sihan S, Mazanek Michael M, Lénárt Péter P, Hériché Jean-Karim JK, Poser Ina I, Kraut Norbert N, Hyman Anthony A AA, Yaffe Michael B MB, Mechtler Karl K, Peters Jan-Michael JM"],"sample_synonyms":["Not Available, Unavailable."],"name_synonyms":["Gpi, Org, ORG, human being, Man (Taxonomy), determination, AI461847, Protein., Gpi-1r, Nlk, protein complex, Gpi-1s, Modern, Phi, Proteins, Gpi-1t, Phosphorylations, Gpi1-r, Gene, Gpi1-s, protein, MF, Gpi1-t, protein-containing complex, Amf, phosphorylation, human, Human, Protein Gene Products, Gene Proteins, mOC-X, native protein, Homo sapiens, Modern Man, chemical analysis, Protein, Gene Products, Pgi, NK|GPI, assay, Gpi-1, protein aggregate, Man, Bglap-rs1, NK, Gpi1s, NK/GPI"],"data_synonyms":["Not Available, Unavailable."],"description_synonyms":["hBUBR1, Silencer factor B, Liver-enriched transcriptional activator, TGF-beta5, SCKL4, Preptin, IGF-II., Insulin-like growth factor II, TGFbeta, TCF-5, Glioblastoma-derived T-cell suppressor factor, myopathy with lactic acidosis and sideroblastic anemia, MYH9.11, tgfbeta, CED, CENP-J, Liver activator protein, Transcription factor 5, LAPEP, LAP-3, Shy-dragger syndrome (formerly), MLASA, lap/AP180, MYH9_11, C|EBPbeta, tgfb5, C|EBP-related protein 2, Lapep, LIP1, Pure, EP3060, CALM, CPAP, ced, TGFB, autonomic failure, tgf-beta, BcDNA:GM10787, Nuclear factor NF-IL6, BUB1beta, BSC-1 cell growth inhibitor, myopathy with lactic acidosis and sideroblastic anaemia, sideroblastic anaemia and mitochondrial myopathy, tgfb, Msa, MSA, 3.1.3.2, NF-M, MVA1, Gm81, EP(3)3060, AU045529, Bub1A, BUBR1, TGF-beta-3, SF-B, TGF-beta-1, TGF-beta-2, CG2520, LIP, Pep-7, C/EBPbeta, PP9092, SASS4, 2410015L10Rik, C/EBP-beta, Flt-4, TCF5, LAP, Lap, AGP|EBP, SSK1, CLTH, l(3)neo34, CRP2, Sas-4, Chy, Pep-S, lap, ACP2, PEPS, MARIPOSA, hypotension, Latency-associated peptide, BM032, 5730442G03Rik, HEL-S-106, REGULATORY PARTICLE NON-ATPASE SUBUNIT 5A, lactic acidosis and sideroblastic anemia, MCPH6, Pep7, AI323512, sideroblastic anemia and mitochondrial myopathy, susceptibility to multiple system atrophy 1, VEGFR3, DmelCG2520, Multiplication-stimulating polypeptide, sig, RPN5A, NF-IL6, 4932437H03Rik, DPD1, orthostatic, G-TSF, Nfil6, Interleukin-6-dependent-binding protein, EMBRYO DEFECTIVE 2107, AP180, IL6DBP, dAP-3, Cetermin, C|EBP beta, IL-6DBP, MAD3L, VEGFR-3, dpd1, Polyergin, AA410100, Multiplication-stimulating activity, Liver-enriched inhibitory protein, Peps, Myopathy"],"pubmed_abstract_synonyms":["l(3)01673, IPP2A2, scale tissue, 2.7.11.21, Chromosome Segregations, Activity, determination, Aurora, Mbp1, Phases, Aurora-Related Kinase 2, protein, phosphorylation, prevention, PPP1R48, 5730420M11Rik, Mitotic M, Kinase, Analysis, protein aggregate, myd, prevention and control, AIM-1, Mass Spectrum Analysis, SET, M Phases, AIRK2, reference sample, Analyses, TAF-I, plant peltate hair, Mbp-1, purification, Polo-like kinase, DmelCG4299, preventive measures, isolation and purification, IGAAD, set, PLK1, DmelCG10574, Segregations, Aurora B Kinase, ATP Phosphotransferases, ATP, phapii, preventive therapy, anatomical protrusion, gyltl1b-b, StF-IT-1, Serine-Threonine Protein Kinase 12, aurkb-sv2, aurkb-sv1, Spectrum Analysis, ipl1, results, Spectroscopy, l(3)S025604, Aurora Kinases B, MDDGA6, mKIAA0609, KIAA0609, fg, Transphosphorylases, gyltl1b, HLA-DR-associated protein II, AIRK2-A, Mitoses, DI-2, N-(2, I-2Dm, mdc1d, expanded, Spectrometry, CG4299, anon-WO0172774.3, I-2PP1, MDC1D, ARK-2, TAF-IBETA, enr, l(3)77Aa, enlarged, Chromosome, antagonists and inhibitors, spine, Aurora B Kinases, IPL1, 0256/04, DmelCG12306, Mitotic, TAF-Ibeta, i2pp2a, Protein Kinase, Proteomes, big, Segregation, peltate hair, number, STK12, Gene, Spectrum Analyses, aurkb, XAIRK2-A, protein-containing complex, froggy, PHAPII, Gyltl1a, protrusion, large, ARK2, serine/threonine-protein kinase 13, Ark2, isolation, Gene Products, Mass, ark2, Phosphotransferase, Mass Spectroscopy, Stk1, stk12, Stk5, MDDGB6, STK5, ipp2a2, inhibiteur, 2pp2a, LARGE, Transphosphorylase, STPK13, ATP-protein phosphotransferase, CG10574, AL022959, BPFD#36, aik2, chromosome transmission, 2PP2A, inhibidor, taf-ibeta, Stk12, great, dSET, dSet, Aik2, AIK2, AurB, stk5, Controlled, inhibitors, Controlling, Polo kinase, protein complex, Proteins, igaad, Phosphorylations, total expressed protein, inhibitor, STK-1, l(3)S132408., Phosphotransferases, Aurora B, group, aim1, MS, native protein, I-2PP2A, B Kinase, Aurora Related Kinase 2, mitosis, POLO/PLK1, Protein, Dm I-2, chemical analysis, I2PP2A, AIM1, Mitotic M Phase, Aim1, scales, M Phase, Mass Spectrum Analyses, antagonists, Serine Threonine Protein Kinase 12, Mass Spectrum, Phase, Polo, scale, ensemble, Kinases, prophylaxis, PLK, Plk, 3-dihydro-2-oxo-3-((3Z)-phenyl((4-(1-piperidinylmethyl)phenyl)amino)methylene)-1H-indol-5-yl)-, Protein Gene Products, Gene Proteins, 1324/08, dSET/TAF-Ibeta, Ethanesulfonamide, 2610030F17Rik, POLO, CG12306, control, cardinality, plk, Mitotic M Phases, assay, AA407739, General activity, l(3)S132408"],"pubmed_title_synonyms":["human being, Man (Taxonomy), determination, Protein., protein complex, Modern, Proteins, Phosphorylations, Gene, protein, protein-containing complex, phosphorylation, human, Human, Protein Gene Products, Gene Proteins, native protein, Homo sapiens, Modern Man, chemical analysis, Protein, Gene Products, assay, protein aggregate, Man"],"view_count":["425"],"additional_accession":[]},"is_claimable":false,"name":"MitoCheck (www.mitocheck.org) -  Systematic phosphorylation analysis of human mitotic protein complexes","description":"MitoCheck Mm Bub1b NB LAP CHY 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