{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q92878","secondaryAccessions":["B9EGF5","O43254","Q6GMT7","Q6P5X3","Q9UP86"],"uniProtkbId":"RAD50_HUMAN","entryAudit":{"firstPublicDate":"2005-02-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1997-02-01","entryVersion":218,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"DNA repair protein RAD50"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9590181"}],"value":"hRAD50"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27889449"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9651580"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"15790808"}],"value":"3.6.-.-"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8756642"},{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:9816"}],"value":"RAD50"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9X1X1"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10888888"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11741547"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12805565"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15064416"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15790808"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16622404"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21757780"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27889449"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28134932"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28867292"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31537797"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9590181"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9651580"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9705271"}],"value":"Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis (PubMed:15064416, PubMed:21757780, PubMed:27889449, PubMed:28134932, PubMed:28867292, PubMed:9590181, PubMed:9651580, PubMed:9705271). The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases (PubMed:15064416, PubMed:21757780, PubMed:27889449, PubMed:28867292, PubMed:9590181, PubMed:9651580, PubMed:9705271). The complex (1) mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is (2) required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage (PubMed:15064416, PubMed:27889449, PubMed:28867292, PubMed:9590181, PubMed:9651580, PubMed:9705271). The MRN complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11, to initiate end resection, which is required for single-strand invasion and recombination (PubMed:11741547, PubMed:9590181, PubMed:9651580, PubMed:9705271). Within the complex, RAD50 is both required to bind DNA ends and hold them in close proximity and regulate the activity of MRE11 (PubMed:11741547, PubMed:12805565, PubMed:28134932). RAD50 provides an ATP-dependent control of MRE11 by positioning DNA ends into the MRE11 active site: ATP-binding induces a large structural change from an open form with accessible MRE11 nuclease sites into a closed form (By similarity). The MRN complex is also required for DNA damage signaling via activation of the ATM and ATR kinases: the nuclease activity of MRE11 is not required to activate ATM and ATR (PubMed:15064416, PubMed:15790808, PubMed:16622404). The MRN complex is also required for the processing of R-loops (PubMed:31537797). In telomeres the MRN complex may modulate t-loop formation (PubMed:10888888)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27889449"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9651580"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"15790808"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28134932"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28134932"}],"value":"Binds 1 zinc ion per homodimer."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P70388"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10426999"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10783165"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10839544"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10888888"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11096100"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15456891"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15723659"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26215093"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27568553"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28867292"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31353207"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36577401"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8756642"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9590181"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9705271"}],"value":"Component of the MRN complex composed of two heterodimers RAD50 and MRE11 associated with a single NBN (PubMed:10839544, PubMed:26215093, PubMed:28867292, PubMed:36577401, PubMed:8756642, PubMed:9590181, PubMed:9705271). The MRN complexes dimerize on DNA to form joined MRN-MRN oligomers required for DNA double-strand break repair (PubMed:36577401). As part of the MRN complex, interacts with MCM8 and MCM9; the interaction recruits the complex to DNA repair sites (PubMed:26215093). Component of the BASC complex, at least composed of BRCA1, MSH2, MSH6, MLH1, ATM, BLM, RAD50, MRE11 and NBN (PubMed:10783165). Found in a complex with TERF2 (PubMed:10888888). Interacts with RINT1 (PubMed:11096100). Interacts with BRCA1 via its N-terminal domain (PubMed:10426999). Interacts with DCLRE1C/Artemis (PubMed:15456891, PubMed:15723659). Interacts with MRNIP (PubMed:27568553). Interacts with CYREN (via XLF motif) (By similarity). Interacts with C1QBP and MRE11; interaction takes place in absence of DNA damage to form the MRC (MRE11-RAD50-C1QBP) complex that inhibits the activity of MRE11 (PubMed:31353207)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20943970"}],"value":"(Microbial infection) Interacts with herpes simplex virus 1 protein UL12 (PubMed:20943970)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q92878","intActId":"EBI-495494"},"interactantTwo":{"uniProtKBAccession":"P46100","geneName":"ATRX","intActId":"EBI-396461"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q92878","intActId":"EBI-495494"},"interactantTwo":{"uniProtKBAccession":"O75943","geneName":"RAD17","intActId":"EBI-968231"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q92878","intActId":"EBI-495494"},"interactantTwo":{"uniProtKBAccession":"Q92878","geneName":"RAD50","intActId":"EBI-495494"},"numberOfExperiments":5,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10783165"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15916964"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21757780"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26215093"}],"value":"Localizes to discrete nuclear foci after treatment with genotoxic agents (PubMed:10783165, PubMed:26215093). Localizes to DNA double-strand breaks (DSBs) (PubMed:15916964, PubMed:21757780)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10783165"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15916964"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26215093"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10888888"}],"value":"Chromosome, telomere","id":"SL-0276"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21757780"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26215093"}],"value":"Chromosome","id":"SL-0468"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"synonyms":[{"value":"RAD50-1"},{"value":"RAD50-2"}],"isoformIds":["Q92878-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["Q92878-2"],"sequenceIds":["VSP_012591"],"isoformSequenceStatus":"Described"},{"name":{"value":"3"},"synonyms":[{"value":"RAD50-3"}],"isoformIds":["Q92878-3"],"sequenceIds":["VSP_012590"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8756642"}],"value":"Expressed at very low level in most tissues, except in testis where it is expressed at higher level. Expressed in fibroblasts"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P58301"}],"value":"The zinc-hook, which separates the large intramolecular coiled coil regions, contains 2 Cys residues that coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another RAD50 molecule, thereby forming a V-shaped homodimer. The two heads of the homodimer, which constitute the ATP-binding domain, interact with the MRE11 homodimer"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21757780"}],"value":"Phosphorylation at Ser-635 by ATM in response to DNA damage is required for double-strand break (DSB) repair"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Nijmegen breakage syndrome-like disorder","diseaseAccession":"DI-02806","acronym":"NBSLD","description":"A disorder similar to Nijmegen breakage syndrome and characterized by chromosomal instability, radiation sensitivity, microcephaly, growth retardation, short stature and bird-like face. Immunodeficiency is absent.","diseaseCrossReference":{"database":"MIM","id":"613078"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19409520"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32212377"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the SMC family. RAD50 subfamily"}],"commentType":"SIMILARITY"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Miscellaneous discrepancy","sequence":"AAH62603.1","note":"Contaminating sequence. 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