{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["25(9)"],"submitter":["Graf JF"],"pubmed_abstract":["PPM1D is a p53-regulated protein phosphatase that modulates the DNA damage response (DDR) and is frequently altered in cancer. Here, we employed chemical inhibition of PPM1D and quantitative mass spectrometry-based phosphoproteomics to identify the substrates of PPM1D upon induction of DNA double-strand breaks (DSBs) by etoposide. We identified 73 putative PPM1D substrates that are involved in DNA repair, regulation of transcription, and RNA processing. One-third of DSB-induced S/TQ phosphorylation sites are dephosphorylated by PPM1D, demonstrating that PPM1D only partially counteracts ATM/ATR/DNA-PK signaling. PPM1D-targeted phosphorylation sites are found in a specific amino acid sequence motif that is characterized by glutamic acid residues, high intrinsic disorder, and poor evolutionar"],"journal":["iScience"],"pagination":["104892"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9436757"],"repository":["biostudies-literature"],"pubmed_title":["Substrate spectrum of PPM1D in the cellular response to DNA double-strand breaks."],"pmcid":["PMC9436757"],"pubmed_authors":["Mikicic I","Beli P","Graf JF","Ping X","Scalera C","Mayr K","Stelzl LS","Wagner SA"],"additional_accession":[]},"is_claimable":false,"name":"Substrate spectrum of PPM1D in the cellular response to DNA double-strand breaks.","description":"PPM1D is a p53-regulated protein phosphatase that modulates the DNA damage response (DDR) and is frequently altered in cancer. Here, we employed chemical inhibition of PPM1D and quantitative mass spectrometry-based phosphoproteomics to identify the substrates of PPM1D upon induction of DNA double-strand breaks (DSBs) by etoposide. We identified 73 putative PPM1D substrates that are involved in DNA repair, regulation of transcription, and RNA processing. One-third of DSB-induced S/TQ phosphorylation sites are dephosphorylated by PPM1D, demonstrating that PPM1D only partially counteracts ATM/ATR/DNA-PK signaling. PPM1D-targeted phosphorylation sites are found in a specific amino acid sequence motif that is characterized by glutamic acid residues, high intrinsic disorder, and poor evolutionar","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Sep","modification":"2026-05-10T05:13:52.863Z","creation":"2025-02-19T04:03:16.913Z"},"accession":"S-EPMC9436757","cross_references":{"pubmed":["36060052"],"doi":["10.1016/j.isci.2022.104892"]}}