MassIVEapplication/xmlftp://massive-ftp.ucsd.edu/v03/MSV000087575/primaryOK2000000Kristian Swearingenhttps://massive.ucsd.edu/ProteoSAFe/dataset.jsp?task=eb77659cbd814b67a98c5a7b6fb297f3kristian.swearingen@systemsbiology.orgMassIVE24MOD:00047 - "A protein modification that effectively converts an L-threonine residue to O-phospho-L-threonine."MOD:00046 - "A protein modification that effectively converts an L-serine residue to O-phospho-L-serine."MOD:00048 - "A protein modification that effectively converts an L-tyrosine residue to O4'-phospho-L-tyrosine."MOD:01060 - "A protein modification that effectively converts an L-cysteine residue to S-carboxamidomethyl-L-cysteine."ProteomicsQ Exactive HFPlasmodium Falciparum (ncbitaxon:5833)Institute for Systems Biologyliquid chromatography tandem mass spectroscopy, FUSED, knobbly, Chelating Agent, artificial sequence, MBP-C, R75289, Calcium 40, MBP1, Fused, Gene, protein, protein-containing complex, LC-MS-MS, Buffer, Agent, COLEC1, peptide, Polypeptides, protein polypeptide chains, peptido, polypeptide chain, kinky, 20Ca, Factor IV, LC-MSMS, Gene Products, Kinase, synthetic genetic interaction (sensu inequality), protein aggregate, Phosphotransferase, Chelating Agents, Ca(0), HSMBPC, Eosinophil granule major basic protein, calcio, Calcium-40, LCMSMS, peptides, absent from organism, synthetic genetic interaction defined by inequality, Proteoglycan 2, MBL, proteins, CaCl2, Metal Chelating Agents, Transphosphorylase, Myelin membrane encephalitogenic protein, MBP, calcium chloride anhydrous, Chelators, reaction, MBPD, AI316800, Pregnancy-associated major basic protein, Chelating, peptidos, mKIAA1278, Complexons, Kb, ATP Phosphotransferases, TAG, ATP, Ki, Calcium chloride anhydrous, Blood Coagulation Factor IV, Ca, LC-MS2, Metal Chelating, Coagulation, Metal, protein complex, Proteins, LC-MS/MS, Phosphorylations, artificial gene, synthetic DNA, Kalzium, buffer, Phosphotransferases, BMPG, Peptide, B930045J24, polypeptide, Axin, mld, LC/MS/MS, Phosphopeptide, native protein, natural protein, C76307, Protein, synthetic, Can, Chelator, MBL2D, shi, Hmbpr, Maltose-Binding Protein, covalent modifier, Transphosphorylases, Calcium, absence, Antagonists, Kinases, FU, EMBP, golli-mbp, synthetic constructs, Protein Gene Products, Gene Proteins, Maltose Binding Protein, calcium, SYNTHETIC CONSTRUCT sequences, Coagulation Factor IV, Maltose Binding Proteins, Agents, Metal Antagonists, liquid chromatography-tandem mass spectroscopy, Fu, [CaCl2], artificial, liquid chromatography tandem mass spectrometry, Peptid, Myelin A1 protein, Polypeptide, phosphorylation., fused, 1700112N14Rikliquid chromatography tandem mass spectroscopy, LC-MS2, Transphosphorylases, LCMSMS, artificial sequence, peptides, Kinases, ATCPK1, calcium dependent protein kinase 1, LC-MS/MS, synthetic genetic interaction defined by inequality, artificial gene, Transphosphorylase, synthetic DNA, synthetic constructs, Phosphotransferases, LC-MS-MS, CALCIUM DEPENDENT PROTEIN KINASE, Maltose Binding Protein, Polypeptides, SYNTHETIC CONSTRUCT sequences, LC/MS/MS, Maltose Binding Proteins, peptido, liquid chromatography-tandem mass spectroscopy, LC-MSMS, synthetic, liquid chromatography tandem mass spectrometry, artificial, Peptid, peptidos, Kinase, Polypeptide, Maltose-Binding Protein, synthetic genetic interaction (sensu inequality), ATP Phosphotransferases, Phosphotransferase, Peptide., ATP0PXD026499falseLC-MS/MS-based in vitro kinase assays performed with recombinant maltose-binding protein-tagged P. falciparum calcium dependent protein kinase 4 using synthetic peptides as substratesIn vitro kinase assays were performed with recombinant maltose-binding protein (MBP) tag-fused PfCDPK4 protein using synthetic peptides as substrates. Kinase reaction buffer contained CaCl2 or the calcium chelator EGTA. Triplicate reactions with either the CaCl2 buffer or the EGTA buffer were performed in parallel and the peptides were detected and quantified by LC-MS/MS. The suitability of a peptide as a substrate for PfCDPK4 was quantified as the depletion of the unmodified peptide as it was converted to phosphopeptide. Additionally, autophosphorylation of PfCDPK4 was assessed by performing the reaction in the absence of substrates followed by tryptic digest and LC-MS/MS of the resulting peptides to identify phosphorylation sites.Sat Jun 05 12:23:00 BST 2021MSV000087575