{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kanno SI"],"funding":["Naito Foundation","Princess Takamatsu Cancer Research Fund","Takeda Science Foundation","Japan Proteomics Co., Ltd"],"pagination":["gkaf150"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11904782"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["53(5)"],"pubmed_abstract":["The SWI/SNF chromatin-remodeling complex that comprises multiple subunits orchestrates diverse cellular processes, including gene expression, DNA repair, and DNA replication, by sliding and releasing nucleosomes. AT-interacting domain-rich protein 1A (ARID1A) and ARID1B (ARID1A/B), a pivotal subunit, have significant relevance in cancer management because they are frequently mutated in a broad range of cancer types. To delineate the protein network involving ARID1A/B, we investigated the interactions of this with other proteins under physiological conditions. The ARID domain of ARID1A/B interacts with proteins involved in transcription and DNA/RNA metabolism. Several proteins are responsible for genome integrity maintenance, including DNA-dependent protein kinase catalytic subunit (DNA-PKc"],"journal":["Nucleic acids research"],"pubmed_title":["Armadillo domain of ARID1A directly interacts with DNA-PKcs to couple chromatin remodeling with nonhomologous end joining (NHEJ) pathway."],"pmcid":["PMC11904782"],"funding_grant_id":["15-24705"],"pubmed_authors":["Kanno SI","Kobayashi T","Kurimasa A","Yasui A","Tanaka K","Watanabe R","Ui A"],"additional_accession":[]},"is_claimable":false,"name":"Armadillo domain of ARID1A directly interacts with DNA-PKcs to couple chromatin remodeling with nonhomologous end joining (NHEJ) pathway.","description":"The SWI/SNF chromatin-remodeling complex that comprises multiple subunits orchestrates diverse cellular processes, including gene expression, DNA repair, and DNA replication, by sliding and releasing nucleosomes. AT-interacting domain-rich protein 1A (ARID1A) and ARID1B (ARID1A/B), a pivotal subunit, have significant relevance in cancer management because they are frequently mutated in a broad range of cancer types. To delineate the protein network involving ARID1A/B, we investigated the interactions of this with other proteins under physiological conditions. The ARID domain of ARID1A/B interacts with proteins involved in transcription and DNA/RNA metabolism. Several proteins are responsible for genome integrity maintenance, including DNA-dependent protein kinase catalytic subunit (DNA-PKc","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Feb","modification":"2026-04-23T03:12:37.867Z","creation":"2025-04-04T00:32:11.08Z"},"accession":"S-EPMC11904782","cross_references":{"pubmed":["40087883"],"doi":["10.1093/nar/gkaf150"]}}