GPMDB00143OtherYang J, et al.InstrumentNot AvailableNot availableHomo_sapiens_viruses, Human_femaleNot available25175731http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320005167http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320005178http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320005177http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320005166http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320005165http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320005176http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320005175http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320005164http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320005159http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320005169http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320005168http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320005179http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320005170http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320005181http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320005180http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320005174http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320005163http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320005162http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320005173http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320005161http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320005172http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320005160http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320005182Department of Biochemistry, Vanderbilt University School of Medicine,Not availableGPMDBCysteine 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 DC,Yang Jing J, Gupta Vinayak V, Carroll Kate S KS, Liebler Daniel C DCCell., Vitamin K Dependent, Cofactor Protein S, Vitamin K-Dependent Protein S, Vitamin K Dependent Protein S, Protein S, Vitamin K-Dependent, CofactorNat, NAT, EGF receptor binding, posttranslational modification, D17H6S113E, Cysteine Hydrochloride, PLXN5, Slf, Somatomedin-C, Nl1, L-Zystein, TGF-alpha receptor binding, Gene, FPH2, PLEXIN-B1, L-cysteine, FSH, SeP, CEH, AI790464, Gene Products, NEPII, NL1, Cell., NL2, Half-Cystine, SEH, Vitamin K Dependent Protein S, Work Flow, epidermal growth factor, MAP, RCB1872, SEP, C, rabGAPLP, Vitamin K Dependent, transforming growth factor alpha receptor ligand, posttranslational amino acid modification, Vitamin K-Dependent Protein S, epidermal growth factor receptor ligand, URG, L Cysteine, EGFR binding, somatomedin-C, SF, RabGAP-5, Kitl, proteins, Ring3, posttranslational protein modification, Mast cell growth factor, sEP, transforming growth factor alpha receptor binding, HOMG4, CYSTEINE, IGF1, RUSC3, transient structure, EGF receptor ligand, Mechano growth factor, SELP, FREE CYSTEINE, C3H7NO2S, Soluble KIT ligand, Half Cystine, (2R)-2-amino-3-mercaptopropanoic acid, Sl, IGF-I, data, steel factor, MUTYH-Associated Polyposis, Zinc Cysteinate, Cofactor, hematopoietic growth factor KL, Proteins, somatomedin, Mell1, Cys, sKITLG, Fsrg1, polypeptide, Workflows, Experiment, RING3, Cofactor Protein S, transforming growth factor alpha, MMEL2, mechano growth factor, AW228947, FSRG1, Protein, A-431, A431, mKIAA4005, Igf-1, (2R)-2-amino-3-sulfanylpropanoic acid, Urogastrone, RUTBC3, SHEP7, D6S113E, PTM, mast cell growth factor, Stem cell factor, RNF3, Rnf3, Frg-1, Epidermal growth factor, L-2-Amino-3-mercaptopropionic acid, L-Cysteine, (R)-2-amino-3-mercaptopropanoic acid, STAT5, MYH-Associated Polyposis, L-Cystein, post-translational amino acid modification, RABGAP5, Protein Gene Products, Gene Proteins, stem cell factor, EGF, KL-1, post-translational modification, MGF, c-Kit ligand, KITLG, E920, Eph2, regulation, SCF, Protein S, RCB0202, E430016J11Rik, TGFalpha receptor binding, Fsrg-1, Vitamin K-Dependent, RWDD5, Work Flows, NEP2Cell., Vitamin K Dependent, Cofactor Protein S, Vitamin K-Dependent Protein S, Vitamin K Dependent Protein S, Protein S, Vitamin K-Dependent, Cofactorbis(hydridooxygen)(O--O), HOOH, transcription factor, T-cell leukemia, EGF receptor binding, biological signaling, posttranslational modification, Cysteine Hydrochloride, human being, determination, H2O2, number, L-Zystein, Oxydol, TGF-alpha receptor binding, Gene, L-cysteine, Homo sapiense, Hydrogen Peroxide (H2O2), Transcription Factor, presence, dihydrogen dioxide, AI043036, AA959795, phosphorylation, Homo spaiens, beta-Urogastrone, Homo sapien, zinc ion regulated core promoter proximal region sequence-specific DNA binding, MOP1, Human Urinary Gastric Inhibitor, SIR2L6, Homo sapians, RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity, Gene Products, Mood, Growth Factor, Half-Cystine, sequence-specific DNA binding, Work Flow, InChI=1/H2O2/c1-2/h1-2H, epidermal growth factor, MAP, H(2)O(2), C, rabGAPLP, Transcription, posttranslational amino acid modification, transforming growth factor alpha receptor ligand, Homo sapients, Ubiquitylation, Hydroperoxide, reference sample, epidermal growth factor receptor ligand, L Cysteine, HIF1, Moods, EGFR binding, Acetylations, RabGAP-5, Peroxide, proteins, Growth Factor-Urogastrone, posttranslational protein modification, dihydrogen peroxide, man, RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity, Sir2l6, 2810449N18Rik, InChIKey=MHAJPDPJQMAIIY-UHFFFAOYAL, Epidermal Growth Factor-Urogastrone, transforming growth factor alpha receptor binding, extruding from, HIF-1alpha, CYSTEINE, Homo sapience, RNA polymerase II proximal promoter sequence-specific DNA binding, RUSC3, Homo sampiens, signaling process, transient structure, [OH(OH)], copper ion regulated proximal promoter sequence-specific DNA binding, EGF receptor ligand, FREE CYSTEINE, C3H7NO2S, 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, (2R)-2-amino-3-mercaptopropanoic acid, associated, Home sapiens, single organism signaling., Controlled, RNA polymerase II distal enhancer sequence-specific binding, distinct from, RNA polymerase II core promoter proximal region sequence-specific binding, Controlling, MUTYH-Associated Polyposis, Zinc Cysteinate, exits through, Affects, Proteins, dihydrogen(peroxide), acetylation, Phosphorylations, zinc ion regulated core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, homeobox 1, Factor, metal ion regulated sequence-specific DNA binding RNA polymerase II transcription factor activity, HIF-1A, Cys, Cell, transcription factor activity, polypeptide, count in organism, Workflows, transforming growth factor alpha, count, Perhydrol, Homo sapian, beta Urogastrone, Protein, chemical analysis, RNA polymerase II transcription factor activity, sequence, sequence-specific distal enhancer binding RNA polymerase II transcription factor activity, Homo sapeins, (2R)-2-amino-3-sulfanylpropanoic acid, metal ion regulated core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, Urogastrone, RUTBC3, susceptibility, Hydrogen, Superoxol, Factors, PTM, Hydrogen peroxide (H2O2), dioxidane, HIF1-ALPHA, Humo sapiens, Epidermal growth factor, L-2-Amino-3-mercaptopropionic acid, L-Cysteine, (R)-2-amino-3-mercaptopropanoic acid, sequence-specific DNA binding RNA polymerase II transcription factor activity, MYH-Associated Polyposis, metal ion regulated core promoter proximal region sequence-specific binding, exposed, copper ion regulated core promoter proximal region sequence-specific binding, Homo sapines, [H]OO[H], Transcription factor, human, primary structure of sequence macromolecule, L-Cystein, post-translational amino acid modification, signalling, RABGAP5, Protein Gene Products, Gene Proteins, HIF1alpha, Homo spiens, EGF, "human" EXACT genbank_common_name [], Epidermal, signalling process, post-translational modification, copper ion regulated core promoter proximal region sequence-specific DNA binding RNA polymerase II transcription factor activity, PASD8, E920, regulation, bHLHe78, assay, quantitative, E430016J11Rik, TGFalpha receptor binding, metal ion regulated sequence-specific DNA binding, RWDD5, Work Flows, metal ion regulated proximal promoter sequence-specific DNA binding, presence or absence in organism, sequence-specific transcription regulatory region DNA binding1403http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320005182dbgap_ncbi~0patentfamilies~0rfam~0merops~0complex-portal~0uniprot~0wormbaseparasite~0embl-covid19~0reactome~0emdb~0wgs_masters~0ebiweb_resources~0opentargets_genetics~0biomodels_all~0ipd-mhc~0ebiweb_teams~0taxonomy~0genome_assembly~0sc-experiments~0ebiweb_people~0enzymeportal_enzymes~0ipd-nhkir~0cellosaurus~0pdbe~0chebi~0patentproteins~0interpro7~0uniref~0chembl~0pdbekb~0gpcrdb~0hgnc~0sc-genes~0intact~0rhea~0ebiweb_training~0alphafold~0imgt-hla~0patentnucleotides~0ensemblroot~0eva_studies~0non-coding~0europepmc~0pubmed~1identifiers_registry~0pdbechem~0hpa-covid19~0eva-variants-covid19~0biosamples~0gwas_catalog~0biotools~0tls_masters~0mesh~0coding~0sra~0opentargets~0efo~0embl-pathogen~0project~0human_diseases~0geo_datasets~0embl~0treefam~0uniparc~0ols~0dgva~0intenz~0go~0tsa_masters~0biosamples-covid19~0ebiweb_corporate~0omim~0lrg~0earlycause-molecular-sequences~0ipd-kir~0empiar~0rnacentral~0orcid_data_claims~0gpmdb~2lineage-covid19~0metagenomics~0pfam~0varsite~00.00.00.004318322023442320.001.0falseSite-specific mapping and quantification of protein S-sulphenylation in cells.Data from CPTAC Portal. Experiment: Protein S-sulfenylation SulfenQ mzML_data A431, file: SulfenQ_A431_EGF_LH_B3.mgf. Published as part of Nat Commun. 2014 Sep 1;5:4776 . From the Abstract: {{i}} 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 ...{{/i}}2014-12-02GPM3232000518225175731