GPMDB00205OtherHalim VA, et al.InstrumentNot AvailableNot availableHuman, Human_adenovirus_54, Human_adenovirus_a, Human_adenovirus_b, Human_adenovirus_c, Human_adenovirus_d, Human_adenovirus_e, Human_adenovirus_f, Human_adenovirus_g, Human_astrovirus, Human_bocavirus, Human_bocavirus_2, Human_bocavirus_3, Human_bocavirus_4, Human_coronavirus_229e, Human_coronavirus_hku1, Human_coronavirus_nl63, Human_coronavirus_oc43, Human_cosavirus_a, Human_cosavirus_b, Human_cosavirus_d, Human_cosavirus_e, Human_enteric_coronavirus_4408, Human_enterovirus_100, Human_enterovirus_a, Human_enterovirus_b, Human_enterovirus_c, Human_enterovirus_d, Human_erythrovirus_v9, Human_herpesvirus_1, Human_herpesvirus_2, Human_herpesvirus_3, Human_herpesvirus_4_type_1, Human_herpesvirus_4_type_2, Human_herpesvirus_5, Human_herpesvirus_6a, Human_herpesvirus_6b, Human_herpesvirus_7, Human_herpesvirus_8_type_p, Human_immunodeficiency_virus_1, Human_immunodeficiency_virus_2, Human_metapneumovirus, Human_papillomavirus_fa75_ki88_03, Human_papillomavirus_rtrx7, Human_papillomavirus_type_10, Human_papillomavirus_type_100, Human_papillomavirus_type_101, Human_papillomavirus_type_103, Human_papillomavirus_type_104, Human_papillomavirus_type_105, Human_papillomavirus_type_108, Human_papillomavirus_type_109, Human_papillomavirus_type_112, Human_papillomavirus_type_113, Human_papillomavirus_type_16, Human_papillomavirus_type_24, Human_papillomavirus_type_26, Human_papillomavirus_type_32, Human_papillomavirus_type_34, Human_papillomavirus_type_4, Human_papillomavirus_type_41, Human_papillomavirus_type_48, Human_papillomavirus_type_49, Human_papillomavirus_type_5, Human_papillomavirus_type_50, Human_papillomavirus_type_53, Human_papillomavirus_type_60, Human_papillomavirus_type_63, Human_papillomavirus_type_6b, Human_papillomavirus_type_7, Human_papillomavirus_type_71, Human_papillomavirus_type_88, Human_papillomavirus_type_9, Human_papillomavirus_type_92, Human_papillomavirus_type_96, Human_papillomavirus_type_98, Human_papillomavirus_type_99, Human_papillomavirus___1, Human_papillomavirus___18, Human_papillomavirus___2, Human_papillomavirus___54, Human_papillomavirus___61, Human_papillomavirus___cand90, Human_parainfluenza_virus_1, Human_parainfluenza_virus_2, Human_parainfluenza_virus_3, Human_parechovirus, Human_parvovirus_4, Human_parvovirus_b19, Human_picobirnavirus, Human_respiratory_syncytial_virus, Human_rhinovirus_a, Human_rhinovirus_b, Human_rhinovirus_c, Human_tmev_like_cardiovirus, Human_t_lymphotropic_virus_1, Human_t_lymphotropic_virus_2, 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9http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210016918Department of Medical Oncology and Cancer Genomics Center, University Medical Center UtrechNot availableGPMDBHow cells recover from a DNA damage-induced arrest is currently poorly understood. We performed large-scale quantitative phosphoproteomics to identify changes in protein phosphorylation that occurred during recovery from arrest in the G2 phase of the cell cycle caused by DNA damage. We identified 154 proteins that were differentially phosphorylated, and systematic depletion of each of these differentially phosphorylated proteins by small interfering RNA (siRNA) identified at least 10 potential regulators of recovery. Astrin, a protein associated with the mitotic spindle, was among the potential regulators of recovery. We found that astrin controlled the abundance of the cell cycle regulator p53 during DNA damage-induced arrest. Cells in which astrin was depleted had decreased murine double minute 2 (MDM2) abundance and increased p53 at the later stages of the DNA damage response. Astrin was required for continued expression of genes encoding proteins that promote cell cycle progression in arrested cells. Thus, by controlling p53 abundance in cells recovering from DNA damage, astrin maintains the cells in a state competent to resume the cell cycle.Comparative phosphoproteomic analysis of checkpoint recovery identifies new regulators of the DNA damage response.Halim Vincentius A VA,Alvarez-Fernández Mónica M,Xu Yan Juan YJ,Aprelia Melinda M,van den Toorn Henk W P HW,Heck Albert J R AJ,Mohammed Shabaz S,Medema René H RH,Halim Vincentius A VA, Alvarez-Fernández Mónica M, Xu Yan Juan YJ, Aprelia Melinda M, van den Toorn Henk W P HW, Heck Albert J R AJ, Mohammed Shabaz S, Medema René H RHassay, DNA damage response, cellular DNA damage response, response to DNA damage stimulus, determination, chemical analysis, response to genotoxic stress.big, APR, data, scale tissue, Genotoxic Stresses, small interfering RNA, LRP, Gap Phase 2, peltate hair, Proteins, number, Phases, APOER, Gene, electronic data file, DNA Damages, presence, Damage, Cell, Division Cycles, Damages, Gap Phases, Stresses, protein amino acid phosphorylation, polypeptide, large, count in organism, Experiment, CD91, count, Cycle, Protein, Gene Products, computer data file, TGFBR5, scales, Gap, Second Gap Phases, Cell Division Cycles, Cycles, DNA Injury, Genotoxic Stress, Phase, DNA Injuries, G2 Phases, Injury, Gap Phase, scale, Division Cycle, G2, NOXA, plant peltate hair, Cell Division Cycle, expanded, cell-division cycle, Cell Division, proteins, Second Gap, Phase 2, INSDC_feature:ncRNA., INSDC_feature:ncRNA, Injuries, Protein Gene Products, INSDC_qualifier:siRNA, Gene Proteins, Second Gap Phase, Genotoxic, A2MR, enlarged, great, Cell Cycles, Stress, LRP1A, Second, quantitative, DNA, IGFBP3R, presence or absence in organismassay, DNA damage response, cellular DNA damage response, response to DNA damage stimulus, determination, chemical analysis, response to genotoxic stress.big, Astrin, scale tissue, Materials, Genotoxic Stresses, tumor suppressor, antigen NY-CO-13, ACTFS, Gap Phase 2, peltate hair, p53, number, Phases, Gene, Mitotic spindle-associated protein p126, DNA Damages, LFS1, Damage, presence, supernumerary, Tp53, Damages, Stresses, Gap Phases, protein amino acid phosphorylation, large, cell cycle regulator, reduced, subnumerary, 1700007J15Rik, bbl, Cycle, Gene Products, tumor suppressor p53, present in fewer numbers in organism, TP53, Cell Division Cycles, Cycles, increased, G2 Phases, Injury, cellular DNA damage response, Gap Phase, Genetic, reference sample, BCC7, plant peltate hair, Cell Division Cycle, hdm2, cell-division cycle, min, Cell Division, proteins, decreased number, Phase 2, INSDC_feature:ncRNA, response to genotoxic stress, INSDC_qualifier:siRNA, Trp53, Second Gap Phase, decreased, MAP126, control of cell cycle progression, regulation of progression through cell cycle, regulation of cell cycle progression, great, Cell Cycles, phosphoprotein p53, TRP53, associated, Controlled, cell cycle modulation, Controlling, DNA damage response, HDMX, small interfering RNA, Proteins, incomplete, response to DNA damage stimulus, Cistrons, Cell, Division Cycles, polypeptide, abolished, count in organism, count, Protein, modulation of cell cycle progression, Genetic Materials, bfy, scales, Gap, Genetic Material, Deepest, Second Gap Phases, DNA Injury, Genotoxic Stress, DNA Injuries, Phase, scale, Division Cycle, G2, increased number, expanded, AA415488, Second Gap, Mdm-2, Cell Cycles., Injuries, Protein Gene Products, Gene Proteins, present in greater numbers in organism, Genotoxic, enlarged, Material, Stress, P53, p44, bhy, Cistron, Second, DNA, quantitative, cell cycle regulation, accessory, presence or absence in organism2005http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210016883dbgap_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~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~2lineage-covid19~0metagenomics~0pfam~0pride archive~1varsite~00Resource Reanalysis0.00.00.0061690314620604570.01.0falseComparative phosphoproteomic analysis of checkpoint recovery identifies new regulators of the DNA damage response.Data from ProteomeXchange, PXD ID: PXD000222. Experiment: 080918_PLKinh4, data file: 080918_PLKinh4_F28.mzXML. Data published as part of Sci Signal. 2013 Apr 23;6(272):rs9 . From th Abstract: {{i}} We performed large-scale quantitative phosphoproteomics to identify changes in protein phosphorylation that occurred during recovery from arrest in the G2 phase of the cell cycle caused by DNA damage. We identified 154 proteins that were differentially phosphorylated, and systematic depletion of each of these differentially phosphorylated proteins by small interfering RNA (siRNA) identified at least 10 potential regulators of recovery ...{{/i}}2013-05-05GPM1121001688323612710PXD000222PXD000222