{"metadata":{"accession":"PF17659","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR061920","hierarchy":null,"name":{"name":"RPA-related protein RADX N-terminal domain","short":"RADX"},"description":[{"text":"<p>This entry represents the N-terminal domain of a family of proteins that includes RPA-related protein RADX from animals, the human member is also known as CXorf57. High-throughput sequencing used to identify genes driving tumorigenesis in Avian leukosis virus (ALV)-induced B-cell lymphomas, showed CXorf57 as the 10th most frequently targeted common integration site by ALV. ALV induces B-cell lymphoma and other neoplasms in chickens by integrating within or near cancer genes and perturbing their expression [[cite:PUB00138338]]. RADX is a replication factor A protein-like (RPA-like), single-stranded DNA binding protein recruited to replication forks to maintain genome stability [[cite:PUB00091321]]. It also modulates stalled fork protection by antagonising RAD51 [[cite:PUB00091322]]. These proteins consist of four tandem OB fold domains.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00138338":{"PMID":26670384,"ISBN":null,"volume":"6","issue":"6","year":2015,"title":"Common Viral Integration Sites Identified in Avian Leukosis Virus-Induced B-Cell Lymphomas.","URL":null,"raw_pages":"e01863-15","medline_journal":"mBio","ISO_journal":"mBio","authors":["Justice JF 4th","Morgan RW","Beemon KL."],"DOI_URL":null},"PUB00091322":{"PMID":30021152,"ISBN":null,"volume":"24","issue":"3","year":2018,"title":"RADX Modulates RAD51 Activity to Control Replication Fork Protection.","URL":null,"raw_pages":"538-545","medline_journal":"Cell Rep","ISO_journal":"Cell Rep","authors":["Bhat KP","Krishnamoorthy A","Dungrawala H","Garcin EB","Modesti M","Cortez D."],"DOI_URL":"https://doi.org/10.1016/j.celrep.2018.06.061"},"PUB00091321":{"PMID":28735897,"ISBN":null,"volume":"67","issue":"3","year":2017,"title":"RADX Promotes Genome Stability and Modulates Chemosensitivity by Regulating RAD51 at Replication Forks.","URL":null,"raw_pages":"374-386.e5","medline_journal":"Mol Cell","ISO_journal":"Mol. Cell","authors":["Dungrawala H","Bhat KP","Le Meur R","Chazin WJ","Ding X","Sharan SK","Wessel SR","Sathe AA","Zhao R","Cortez D."],"DOI_URL":"https://doi.org/10.1016/j.molcel.2017.06.023"}},"set_info":{"accession":"CL0021","name":"OB"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":23,"interactions":0,"matches":615,"pathways":0,"proteins":614,"proteomes":402,"sets":1,"structural_models":{"alphafold":534},"structures":2,"taxa":1399},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":7,"alignment:full":474},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}