{"database":"GPMDB","file_versions":[],"scores":{"citationCount":0,"reanalysisCount":0,"viewCount":31,"searchCount":3},"additional":{"omics_type":["Other"],"submitter":["Dan Lu, et al."],"instrument_platform":["Instrument"],"disease":["Not Available"],"brenda_tissue":["Not available"],"species":["Homo_sapiens_viruses, Human_female"],"submitter_mail":["danlu_pku@126.com"],"publication":["Not available"],"submitter_affiliation":["Peking University Health Science Center"],"model":["http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310025099"],"cell_type":["Not available"],"repository":["GPMDB"],"description_synonyms":["measuring, 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, Controlled"],"name_synonyms":["PAC-1, ADMIO, 1110034C02Rik, AW109958., PAC1, Aprf, APRF, HIES"],"view_count":["31"],"citation_count":["0"],"full_dataset_link":["http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310025099"],"search_count":["3"],"search_domains":["dbgap_ncbi~0","patentfamilies~0","rfam~0","merops~0","complex-portal~0","uniprot~0","wormbaseparasite~0","embl-covid19~0","reactome~0","emdb~0","wgs_masters~0","ebiweb_resources~0","opentargets_genetics~0","biomodels_all~0","ipd-mhc~0","ebiweb_teams~0","taxonomy~0","genome_assembly~0","sc-experiments~0","ebiweb_people~0","enzymeportal_enzymes~0","ipd-nhkir~0","cellosaurus~0","pdbe~0","chebi~0","patentproteins~0","interpro7~0","uniref~0","chembl~0","pdbekb~0","gpcrdb~0","hgnc~0","sc-genes~0","intact~0","rhea~0","ebiweb_training~0","alphafold~0","imgt-hla~0","patentnucleotides~0","ensemblroot~0","eva_studies~0","non-coding~0","europepmc~0","identifiers_registry~0","pdbechem~0","hpa-covid19~0","eva-variants-covid19~0","biosamples~0","gwas_catalog~0","biotools~0","tls_masters~0","mesh~0","coding~0","sra~0","opentargets~0","efo~0","embl-pathogen~0","project~0","pride~1","human_diseases~0","geo_datasets~0","embl~0","treefam~0","uniparc~0","ols~0","dgva~0","intenz~0","go~0","tsa_masters~0","biosamples-covid19~0","ebiweb_corporate~0","omim~0","lrg~0","earlycause-molecular-sequences~0","ipd-kir~0","empiar~0","rnacentral~0","orcid_data_claims~0","gpmdb~1","lineage-covid19~0","metagenomics~0","pfam~0","pride archive~1","varsite~0"],"reanalysis_count":["0"],"submitter_keywords":["Resource Reanalysis"],"citation_count_scaled":["0.0"],"reanalysis_count_scaled":["0.0"],"view_count_scaled":["0.009561998766193708"],"download_count_scaled":["0.0"],"normalized_connections":["1.0"],"additional_accession":[]},"is_claimable":false,"name":"DUSP2 dephosphorylates STAT3 at Y705 and S727 residues","description":"Data 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}}","dates":{"submission":"2015-10-13"},"accession":"GPM32310025099","cross_references":{"Pride":["PXD002743"],"pride":[],"Pride Archive":["PXD002743"]}}