MassIVEapplication/xmlftp://massive-ftp.ucsd.edu/v02/MSV000084244/primary200OK0000Daniel C Lieblerhttps://massive.ucsd.edu/ProteoSAFe/dataset.jsp?task=c406809dfde243f0bc76706092f6ff3cdaniel.liebler@Vanderbilt.EduMassIVE52UNIMOD:4 - "Iodoacetamide derivative."[C] [339.2065] S-sulphenylcysteine tagged with DYn-2-triazohexanoic acid group (heavy)[C] [333.1689] S-sulphenylcysteine tagged with DYn-2-triazohexanoic acid groupUNIMOD:35 - "Oxidation or Hydroxylation."ProteomicsQ ExactiveHomo Sapiens (ncbitaxon:9606)Vanderbilt UniversityCysteine S-sulphenylation provides redox regulation of protein functions, but the global cellular impact of this transient post-translational modification remains unexplored. We describe a chemoproteomic workflow to map and quantify over 1,000 S-sulphenylation sites on more than 700 proteins in intact cells. Quantitative analysis of human cells stimulated with hydrogen peroxide or epidermal growth factor measured hundreds of site selective redox changes. Different cysteines in the same proteins displayed dramatic differences in susceptibility to S-sulphenylation. Newly discovered S-sulphenylations provided mechanistic support for proposed cysteine redox reactions and suggested novel redox mechanisms, including S-sulphenyl-mediated redox regulation of the transcription factor HIF1A by SIRT6. S-sulphenylation is favored at solvent-exposed protein surfaces and is associated with sequence motifs that are distinct from those for other thiol modifications. S-sulphenylations affect regulators of phosphorylation, acetylation and ubiquitylation, which suggest regulatory crosstalk between redox control and signalling pathways.Site-specific mapping and quantification of protein S-sulphenylation in cells.Yang Jing J, Gupta Vinayak V, Carroll Kate S KS, Liebler Daniel C DCsite, Cell., Vitamin K Dependent, Vitamin K-Dependent Protein S, Cofactor Protein S, Vitamin K Dependent Protein S, Protein S, region, Vitamin K-Dependent, CofactorPost Translational Amino Acid Modification, T-cell leukemia, posttranslational modification, E 920, methionine aminopeptidase activity, determination, H2O2, Compounds, AGL4, Oxydol, TGF-alpha receptor binding, protein, Protein Processing, dihydrogen dioxide, Solvent, phosphorylation, Social Controls, prevention, Thiol, protein polypeptide chains, Human Urinary Gastric Inhibitor, hif-1alpha, RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity, 2, 2-amino-3-mercaptopropanoic acid, Cystein, protein aggregate, Work Flow, prevention and control, Formal Social Controls, peptidase M activity, imprinted and ancient gene protein, adenomas, Post-Translational Protein, C, rabGAPLP, perhydrol, posttranslational amino acid modification, L-methionine aminopeptidase activity, Ubiquitylation, Migrant Worker, Man (Taxonomy), Hydroperoxide, reference sample, Post-Translational, cisteina, Moods, Nonmigrant, F10N7_150, RabGAP-5, proteins, Growth Factor-Urogastrone, Posttranslational Protein Processing, Transient, RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity, Social, preventive measures, transforming growth factor alpha receptor binding, HIF-1alpha, RUSC3, signaling process, HIF1a, Squatters, AGAMOUS-like 4, ARNT-interacting protein, zinc ion regulated proximal promoter sequence-specific DNA binding, sequence-specific transcription regulatory region DNA binding RNA polymerase II transcription factor recruiting transcription factor activity, Half Cystine, TRANSCRIPTION FACTOR, single organism signaling, RNA polymerase II distal enhancer sequence-specific binding, distinct from, RNA polymerase II core promoter proximal region sequence-specific binding, Post-Translational Modification, Thiols, Mercaptans, preventive therapy, Zinc Cysteinate, Modern, Modifications, Mercapto Compounds, acetylation, MYH-associated polyposis, autosomal recessive familial adenomatous polyposis, Maps, metal ion regulated sequence-specific DNA binding RNA polymerase II transcription factor activity, HIF-1A, Cys, Workflows, Post Translational Modifications, Perhydrol, Migrant, beta Urogastrone, Workers, sequence-specific distal enhancer binding RNA polymerase II transcription factor activity, (2R)-2-amino-3-sulfanylpropanoic acid, Urogastrone, Migrants and Transients, region, autosomal recessive, F14P3.4, RUTBC3, Superoxol, Factors, PTM, Hydrogen peroxide (H2O2), Processing, Control, F14P3_4, Epidermal growth factor, L-Cysteine, Controls, exposed, Transcription factor, human, L-Cystein, RABGAP5, Amino Acid Modification, post-translational modification, BHLHE78, multiple colorectal, copper ion regulated core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, PASD8, Migrants, Posttranslational Modifications, E430016J11Rik, Regulation, TGFalpha receptor binding, metal ion regulated sequence-specific DNA binding, Posttranslational Modification, Work Flows, humans, metal ion regulated proximal promoter sequence-specific DNA binding, Regulations, HOOH, EGF receptor binding, biological signaling, Cysteine Hydrochloride, human being, Post-Translational Protein Modifications, Sulfhydryl, number, L-Zystein, Gene, SEPALLATA 2, protein-containing complex, Hydrogen Peroxide (H2O2), Ximpact, Transcription Factor, presence, AI043036, Migrant Workers, AA959795, Posttranslational, Human, beta-Urogastrone, zinc ion regulated core promoter proximal region sequence-specific DNA binding, MOP1, polypeptide chain, Homo sapiens, SIR2L6, Gene Products, Post Translational Modification, Mood, Post-Translational Modifications, Growth Factor, Half-Cystine, Man, familial adenomatous polyposis, epidermal growth factor, Post Translational, MAP, Modification, Transcription, transforming growth factor alpha receptor ligand, epidermal growth factor receptor ligand, L Cysteine, HIF1, E-920, familial adenomatous polyposis 2, Transients, EGFR binding, Acetylations, Nonmigrants, Peroxide, Hcys, posttranslational protein modification, Worker, Sir2l6, 2810449N18Rik, Protein Modifications, autosomal recessive multiple colorectal adenomas, Squatter, Post-Translational Amino Acid Modification, Epidermal Growth Factor-Urogastrone, extruding from, CYSTEINE, Posttranslational Amino Acid Modification, RNA polymerase II proximal promoter sequence-specific DNA binding, [OH(OH)], copper ion regulated proximal promoter sequence-specific DNA binding, EGF receptor ligand, Posttranslational Protein, FREE CYSTEINE, site, (2R)-2-amino-3-mercaptopropanoic acid, Controlled, hif1a, signalling., Controlling, MUTYH-Associated Polyposis, pro-epidermal growth factor, Formal Social Control, protein complex, exits through, Affects, Proteins, Phosphorylations, Post-Translational Protein Modification, zinc ion regulated core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, homeobox 1, Factor, hif1alpha, impact-a, Cell, transcription factor activity, count in organism, Mercaptan, transforming growth factor alpha, native protein, natural protein, Social Control, xhif1a, Protein, chemical analysis, Nomad, RNA polymerase II transcription factor activity, sequence, IMPACT, imprinted and ancient gene protein homolog, Protein Modification, metal ion regulated core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, KNOTTED1-like homeobox gene 5, Zystein, susceptibility, Hydrogen, Sulfhydryl Compound, 2-amino-3-sulfanylpropanoic acid, Post Translational Protein Processing, HIF1-ALPHA, prophylaxis, L-2-Amino-3-mercaptopropionic acid, (R)-2-amino-3-mercaptopropanoic acid, MYH-Associated Polyposis, metal ion regulated core promoter proximal region sequence-specific binding, copper ion regulated core promoter proximal region sequence-specific binding, 2-Amino-3-mercaptopropionic acid, F10N7.150, primary structure of sequence macromolecule, post-translational amino acid modification, Protein Gene Products, Gene Proteins, HIF1alpha, Post Translational Protein Modification, EGF, Epidermal, signalling process, Compound, Mercapto, control, Isolation of Nuclei TAgged in specific Cell Types, Nomads, Modern Man, Post-Translational Protein Processing, E920, MAP syndrome, regulation, bHLHe78, assay, RWDD5, FAP2, colorectal adenomatous polyposissite, Cell., Vitamin K Dependent, Vitamin K-Dependent Protein S, Cofactor Protein S, Vitamin K Dependent Protein S, Protein S, region, Vitamin K-Dependent, CofactorPost Translational Amino Acid Modification, T-cell leukemia, posttranslational modification, CG14637, E 920, methionine aminopeptidase activity, determination, CG 1618, H2O2, Compounds, AGL4, dNSF, Oxydol, TGF-alpha receptor binding, protein, Protein Processing, dihydrogen dioxide, Solvent, phosphorylation, Social Controls, prevention, Thiol, protein polypeptide chains, DmNSF, Human Urinary Gastric Inhibitor, hif-1alpha, RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity, dNSF1, dNsf1, 2, 2-amino-3-mercaptopropanoic acid, Cystein, protein aggregate, Work Flow, prevention and control, Formal Social Controls, peptidase M activity, imprinted and ancient gene protein, adenomas, Post-Translational Protein, C, rabGAPLP, perhydrol, posttranslational amino acid modification, L-methionine aminopeptidase activity, Ubiquitylation, Migrant Worker, Man (Taxonomy), Hydroperoxide, reference sample, CG9397, Post-Translational, cisteina, Moods, Nonmigrant, ABS, F10N7_150, RabGAP-5, proteins, Growth Factor-Urogastrone, Posttranslational Protein Processing, Transient, RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity, Social, preventive measures, transforming growth factor alpha receptor binding, HIF-1alpha, RUSC3, signaling process, HIF1a, AGL32, Squatters, AGAMOUS-like 4, ARNT-interacting protein, AA958953, zinc ion regulated proximal promoter sequence-specific DNA binding, MKD15_12, sequence-specific transcription regulatory region DNA binding RNA polymerase II transcription factor recruiting transcription factor activity, Half Cystine, TRANSCRIPTION FACTOR, single organism signaling, RNA polymerase II distal enhancer sequence-specific binding, Data Set., distinct from, RNA polymerase II core promoter proximal region sequence-specific binding, Post-Translational Modification, Thiols, Mercaptans, preventive therapy, MKD15.12, Zinc Cysteinate, Modern, Modifications, Mercapto Compounds, acetylation, MYH-associated polyposis, autosomal recessive familial adenomatous polyposis, Maps, CG9403, metal ion regulated sequence-specific DNA binding RNA polymerase II transcription factor activity, HIF-1A, Cys, l(2)01094, Workflows, Post Translational Modifications, Perhydrol, Migrant, beta Urogastrone, Workers, sequence-specific distal enhancer binding RNA polymerase II transcription factor activity, (2R)-2-amino-3-sulfanylpropanoic acid, Urogastrone, Migrants and Transients, region, autosomal recessive, dnsf1, F14P3.4, RUTBC3, Superoxol, Factors, ARABIDOPSIS BSISTER, PTM, Hydrogen peroxide (H2O2), Processing, Control, F14P3_4, Epidermal growth factor, L-Cysteine, DmelCG9397, Controls, exposed, Transcription factor, human, L-Cystein, RABGAP5, Amino Acid Modification, post-translational modification, BHLHE78, multiple colorectal, copper ion regulated core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, PASD8, Migrants, NSF-1, Posttranslational Modifications, E430016J11Rik, Regulation, TGFalpha receptor binding, metal ion regulated sequence-specific DNA binding, Posttranslational Modification, Work Flows, humans, metal ion regulated proximal promoter sequence-specific DNA binding, Regulations, HOOH, EGF receptor binding, biological signaling, Cysteine Hydrochloride, human being, Post-Translational Protein Modifications, DmRH23, Sulfhydryl, number, TRANSPARENT TESTA16, L-Zystein, Comt, NSF1, DmelCG14637, Gene, SEPALLATA 2, Dmel_CG9403, protein-containing complex, Hydrogen Peroxide (H2O2), Ximpact, Transcription Factor, presence, AI043036, Migrant Workers, AA959795, DOI, NSF, Nsf, Posttranslational, Human, CG1618, beta-Urogastrone, zinc ion regulated core promoter proximal region sequence-specific DNA binding, MOP1, polypeptide chain, Homo sapiens, SIR2L6, Gene Products, Post Translational Modification, Mood, AI324246, Post-Translational Modifications, Growth Factor, 1.28, Half-Cystine, Man, familial adenomatous polyposis, epidermal growth factor, Post Translational, MAP, l(3)00620, doi, Modification, l(2)22F3, Transcription, transforming growth factor alpha receptor ligand, epidermal growth factor receptor ligand, L Cysteine, HIF1, E-920, familial adenomatous polyposis 2, Transients, EGFR binding, Acetylations, Nonmigrants, Peroxide, Hcys, posttranslational protein modification, Worker, Sir2l6, 2810449N18Rik, Protein Modifications, autosomal recessive multiple colorectal adenomas, Squatter, Post-Translational Amino Acid Modification, Epidermal Growth Factor-Urogastrone, extruding from, CYSTEINE, Posttranslational Amino Acid Modification, RNA polymerase II proximal promoter sequence-specific DNA binding, CT9093, [OH(OH)], copper ion regulated proximal promoter sequence-specific DNA binding, EGF receptor ligand, DmelCG1618, Posttranslational Protein, FREE CYSTEINE, site, (2R)-2-amino-3-mercaptopropanoic acid, Jing, l(3)06862, l(3)06863, Controlled, hif1a, com, Controlling, MUTYH-Associated Polyposis, pro-epidermal growth factor, Formal Social Control, protein complex, exits through, Affects, Proteins, Phosphorylations, Post-Translational Protein Modification, zinc ion regulated core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, homeobox 1, Factor, hif1alpha, impact-a, Cell, transcription factor activity, count in organism, Mercaptan, transforming growth factor alpha, native protein, natural protein, Social Control, xhif1a, Protein, chemical analysis, Nomad, RNA polymerase II transcription factor activity, sequence, IMPACT, imprinted and ancient gene protein homolog, dNSF-1, Protein Modification, metal ion regulated core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, l(3)04505, KNOTTED1-like homeobox gene 5, Zystein, susceptibility, Hydrogen, Sulfhydryl Compound, 2-amino-3-sulfanylpropanoic acid, Post Translational Protein Processing, HIF1-ALPHA, prophylaxis, anon-WO0118547.315, AGAMOUS-like 32, L-2-Amino-3-mercaptopropionic acid, (R)-2-amino-3-mercaptopropanoic acid, MYH-Associated Polyposis, metal ion regulated core promoter proximal region sequence-specific binding, copper ion regulated core promoter proximal region sequence-specific binding, 2-Amino-3-mercaptopropionic acid, F10N7.150, primary structure of sequence macromolecule, post-translational amino acid modification, signalling, Protein Gene Products, Gene Proteins, HIF1alpha, Post Translational Protein Modification, EGF, Epidermal, signalling process, Compound, Mercapto, control, Isolation of Nuclei TAgged in specific Cell Types, Nomads, Modern Man, Post-Translational Protein Processing, E920, MAP syndrome, regulation, bHLHe78, assay, 2900024F02Rik, RWDD5, FAP2, colorectal adenomatous polyposis0PXD015907falseSite-specific mapping and quantification of protein S-sulphenylation in cells<p><a href="http://www.nature.com/ncomms/2014/140901/ncomms5776/abs/ncomms5776.html" target="_blank">Jing Yang, Vinayak Gupta, Kate S. Carroll, & Daniel C. Liebler, (2014) Nature Communications 5, 4776, doi:10.1038/ncomms5776</a></p><p>Cysteine S-sulphenylation provides redox regulation of protein functions, but the global cellular impact of this transient post-translational modification remains unexplored. We describe a chemoproteomic workflow to map and quantify over 1,000 S-sulphenylation sites on more than 700 proteins in intact cells. Quantitative analysis of human cells stimulated with hydrogen peroxide or epidermal growth factor measured hundreds of site selective redox changes. Different cysteines in the same proteins displayed dramatic differences in susceptibility to S-sulphenylation. Newly discovered S-sulphenylations provided mechanistic support for proposed cysteine redox reactions and suggested novel redox mechanisms, including S-sulphenyl-mediated redox regulation of the transcription factor HIF1A by SIRT6. S-sulphenylation is favored at solvent-exposed protein surfaces and is associated with sequence motifs that are distinct from those for other thiol modifications. S-sulphenylations affect regulators of phosphorylation, acetylation and ubiquitylation, which suggest regulatory crosstalk between redox control and signalling pathways.</p><ul><li>Dataset imported into MassIVE from <a href="https://cptac-data-portal.georgetown.edu/cptac/s/S024">https://cptac-data-portal.georgetown.edu/cptac/s/S024</a> on 08/28/19</li></ul>Wed Aug 28 14:03:00 BST 2019MSV00008424425175731