RAD50
entrez
10111
canonical
uniprot
Q92878
canonical
ensembl
ENSG00000113522
resolver
ensp
ENSP00000368100
resolver
genesymbol
RAD50
resolver
hgnc
HGNC:9816
resolver
uniprot
A5D6Y3
resolver
uniprot
B9EGF5
resolver
uniprot
O43254
resolver
uniprot
Q6GMT7
resolver
uniprot
Q6P5X3
resolver
uniprot
Q9UP86
resolver
uniprot_entry
A5D6Y3_HUMAN
resolver
uniprot_entry
RAD50_HUMAN
resolver
uniprot_sec
B9EGF5
resolver
uniprot_sec
O43254
resolver
uniprot_sec
Q6GMT7
resolver
uniprot_sec
Q6P5X3
resolver
uniprot_sec
Q9UP86
resolver
amino_acid_sequence
MSRIEKMSILGVRSFGIEDKDKQIITFFSPLTILVGPNGAGKTTIIECLKYICTGDFPPGTKGNTFVHDPKVAQETDVRAQIRLQFRDVNGELIAVQRSMVCTQKSKKTEFKTLEGVITRTKHGEKVSLSSKCAEIDREMISSLGVSKAVLNNVIFCHQEDSNWPLSEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVKEYQMELKYLKQYKEKACEIRDQITSKEAQLTSSKEIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALDSRKKQMEKDNSELEEKMEKVFQGTDEQLNDLYHNHQRTVREKERKLVDCHRELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQEHIRARDSLIQSLATQLELDGFERGPFSERQIKNFHKLVRERQEGEAKTANQLMNDFAEKETLKQKQIDEIRDKKTGLGRIIELKSEILSKKQNELKNVKYELQQLEGSSDRILELDQELIKAERELSKAEKNSNVETLKMEVISLQNEKADLDRTLRKLDQEMEQLNHHTTTRTQMEMLTKDKADKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEDKLFDVCGSQDFESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGIDLDRTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNELKSEKLQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELINKKNTSNKIAQDKLNDIKEKVKNIHGYMKDIENYIQDGKDDYKKQKETELNKVIAQLSECEKHKEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRNEELKEVEEERKQHLKEMGQMQVLQMKSEHQKLEENIDNIKRNHNLALGRQKGYEEEIIHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMKMEEINKIIRDLWRSTYRGQDIEYIEIRSDADENVSASDKRRNYNYRVVMLKGDTALDMRGRCSAGQKVLASLIIRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIIKSRSQQRNFQLLVITHDEDFVELLGRSEYVEKFYRIKKNIDQCSEIVKCSVSSLGFNVH
uniprot
proteins
disease_involvement
DISEASE: Nijmegen breakage syndrome-like disorder (NBSLD) [MIM:613078]: 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. {ECO:0000269|PubMed:19409520, ECO:0000269|PubMed:32212377}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.6.-.-
uniprot
proteins
function
FUNCTION: 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). {ECO:0000250|UniProtKB:Q9X1X1, ECO:0000269|PubMed:10888888, ECO:0000269|PubMed:11741547, ECO:0000269|PubMed:12805565, ECO:0000269|PubMed:15064416, ECO:0000269|PubMed:15790808, ECO:0000269|PubMed:16622404, ECO:0000269|PubMed:21757780, ECO:0000269|PubMed:27889449, ECO:0000269|PubMed:28134932, ECO:0000269|PubMed:28867292, ECO:0000269|PubMed:31537797, ECO:0000269|PubMed:9590181, ECO:0000269|PubMed:9651580, ECO:0000269|PubMed:9705271}.
uniprot
proteins
mass_dalton
153892
uniprot
proteins
mutagenesis
MUTAGEN 42; /note="K->N: Abolishes ability to degrade ATP."; /evidence="ECO:0000269|PubMed:9651580"; MUTAGEN 635; /note="S->G: Abolished phosphorylation by ATM, leading to impaired ability to mediate DNA repair."; /evidence="ECO:0000269|PubMed:21757780"; MUTAGEN 675..679; /note="DENQS->AAAAA: Decreased ability to mediate DNA repair due to impaired MRN oligomers formation."; /evidence="ECO:0000269|PubMed:36577401"; MUTAGEN 1202; /note="S->R: Abolished ATPase activity and ability and activate ATM."; /evidence="ECO:0000269|PubMed:15790808, ECO:0000269|PubMed:16622404"; MUTAGEN 1231; /note="D->A: Abolishes ability to degrade ATP."; /evidence="ECO:0000269|PubMed:9651580
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-635 by ATM in response to DNA damage is required for double-strand break (DSB) repair. {ECO:0000269|PubMed:21757780}.
uniprot
proteins
protein_family
RAD50 subfamily
uniprot
proteins
protein_family
SMC family
uniprot
proteins
pubmed
10415333
uniprot
proteins
pubmed
10426999
uniprot
proteins
pubmed
10783165
uniprot
proteins
pubmed
10839544
uniprot
proteins
pubmed
10888888
uniprot
proteins
pubmed
11096100
uniprot
proteins
pubmed
11741547
uniprot
proteins
pubmed
12384589
uniprot
proteins
pubmed
12805565
uniprot
proteins
pubmed
14684699
uniprot
proteins
pubmed
15064416
uniprot
proteins
pubmed
15372022
uniprot
proteins
pubmed
15456891
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15723659
uniprot
proteins
pubmed
15790808
uniprot
proteins
pubmed
15916964
uniprot
proteins
pubmed
16622404
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19409520
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20943970
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21757780
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26215093
uniprot
proteins
pubmed
27568553
uniprot
proteins
pubmed
27889449
uniprot
proteins
pubmed
28134932
uniprot
proteins
pubmed
28867292
uniprot
proteins
pubmed
31353207
uniprot
proteins
pubmed
31537797
uniprot
proteins
pubmed
32212377
uniprot
proteins
pubmed
36577401
uniprot
proteins
pubmed
8756642
uniprot
proteins
pubmed
9590181
uniprot
proteins
pubmed
9651580
uniprot
proteins
pubmed
9705271
uniprot
proteins
sequence_length
1312
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10783165, ECO:0000269|PubMed:15916964, ECO:0000269|PubMed:26215093}. Chromosome, telomere {ECO:0000269|PubMed:10888888}. Chromosome {ECO:0000269|PubMed:21757780, ECO:0000269|PubMed:26215093}. Note=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). {ECO:0000269|PubMed:10783165, ECO:0000269|PubMed:15916964, ECO:0000269|PubMed:21757780, ECO:0000269|PubMed:26215093}.
uniprot
proteins