GPMDB00313OtherDan Lu, et al.InstrumentNot AvailableNot availableHomo_sapiens_viruses, Human_femaledanlu_pku@126.comNot availablePeking University Health Science Centerhttp://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310025099Not availableGPMDBmeasuring, p-nitrophenylphosphatase activity, data, ADMIO, CDF, Controlling, nitrophenyl phosphatase activity, PNPPase activity, determination, para-nitrophenyl phosphatase activity, Il-6, B-cell hybridoma growth factor, NPPase activity, Proteins, PAC-1, Gene, interferon beta-2, HSF, buffer, Cell, B-cell stimulatory factor 2, BSF2, polypeptide, any method, Polypeptides, HGF, IFN-beta-2, IL-6, Protein, Interferon beta-2, Gene Products, BSF-2, Hybridoma growth factor, 4-nitrophenylphosphate phosphohydrolase activity, CTL differentiation factor, APRF, study, reference sample, HIES, ecto-p-nitrophenyl phosphatase activity, Interleukin HP-1, chemical analysis., phosphoric monoester hydrolase activity, proteins, 4-nitrophenylphosphatase activity, K-pNPPase activity, PAC1, study assay, Aprf, AW109958, hybridoma growth factor, Protein Gene Products, Gene Proteins, IFNB2, interleukin-6 receptor ligand, 1110034C02Rik, scientific observation, IL6, interleukin HP-1, assay, p-nitrophenylphosphate phosphohydrolase activity, phosphatase, ControlledPAC-1, ADMIO, 1110034C02Rik, AW109958., PAC1, Aprf, APRF, HIES310http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM323100250993dbgap_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~0identifiers_registry~0pdbechem~0hpa-covid19~0eva-variants-covid19~0biosamples~0gwas_catalog~0biotools~0tls_masters~0mesh~0coding~0sra~0opentargets~0efo~0embl-pathogen~0project~0pride~1human_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~1lineage-covid19~0metagenomics~0pfam~0pride archive~1varsite~00Resource Reanalysis0.00.00.0095619987661937080.01.0falseDUSP2 dephosphorylates STAT3 at Y705 and S727 residuesData from ProteomeXchange, PXD ID: PXD002743. File: DUSP2.mzml. From ProteomeXchange: {{i}} In the related study, to determine whether DUSP2 definitively served as a phosphatase for STAT3, an in vitro phosphatase assay was used. Using S-tag beads, p-STAT3 was pulled down from IL-6 stimulated HEK293T cells transfected with STAT3-S-Tag. DUSP2 or control protein, which was purified from HEK293T cells transfected with DUSP2-FLAG or empty vector through extraction with anti-FLAG beads and elution with FLAG peptides, were incubated with p-STAT3-S-Tag-beads in phosphatase buffer. Then bound proteins were eluted and subjected to MS analysis ... {{/i}}2015-10-13GPM32310025099PXD002743PXD002743