RAD51
entrez
5888
canonical
uniprot
Q06609
canonical
ensembl
ENSG00000051180
resolver
ensp
ENSP00000267868
resolver
ensp
ENSP00000372088
resolver
ensp
ENSP00000406602
resolver
ensp
ENSP00000433924
resolver
ensp
ENSP00000493712
resolver
ensp
ENSP00000582797
resolver
genesymbol
RAD51
resolver
genesymbol_syn
RAD51A
resolver
genesymbol_syn
RECA
resolver
hgnc
HGNC:9817
resolver
uniprot
B0FXP0
resolver
uniprot
B2R8T6
resolver
uniprot
Q6FHX9
resolver
uniprot
Q6ZNA8
resolver
uniprot
Q9BV60
resolver
uniprot_entry
RAD51_HUMAN
resolver
uniprot_sec
B0FXP0
resolver
uniprot_sec
B2R8T6
resolver
uniprot_sec
Q6FHX9
resolver
uniprot_sec
Q6ZNA8
resolver
uniprot_sec
Q9BV60
resolver
activity_regulation
ACTIVITY REGULATION: Acts as a self-inactivating ATPase, with rapid ATP hydrolysis and slow ADP dissociation (PubMed:15226506). Ca(2+) by reducing the ATPase activity preserves the nucleoprotein filament in its active state, thereby stimulating the DNA strand exchange activity of RAD51 (PubMed:15226506). {ECO:0000269|PubMed:15226506}.
uniprot
proteins
amino_acid_sequence
MAMQMQLEANADTSVEEESFGPQPISRLEQCGINANDVKKLEEAGFHTVEAVAYAPKKELINIKGISEAKADKILAEAAKLVPMGFTTATEFHQRRSEIIQITTGSKELDKLLQGGIETGSITEMFGEFRTGKTQICHTLAVTCQLPIDRGGGEGKAMYIDTEGTFRPERLLAVAERYGLSGSDVLDNVAYARAFNTDHQTQLLYQASAMMVESRYALLIVDSATALYRTDYSGRGELSARQMHLARFLRMLLRLADEFGVAVVITNQVVAQVDGAAMFAADPKKPIGGNIIAHASTTRLYLRKGRGETRICKIYDSPCLPEAEAMFAINADGVGDAKD
uniprot
proteins
disease_involvement
DISEASE: Breast cancer (BC) [MIM:114480]: A common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case. {ECO:0000269|PubMed:10807537, ECO:0000269|PubMed:25539919}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Mirror movements 2 (MRMV2) [MIM:614508]: A disorder characterized by contralateral involuntary movements that mirror voluntary ones. While mirror movements are occasionally found in young children, persistence beyond the age of 10 is abnormal. Mirror movements occur more commonly in the upper extremities. {ECO:0000269|PubMed:22305526, ECO:0000269|PubMed:30406765, ECO:0000269|PubMed:38314870}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Fanconi anemia, complementation group R (FANCR) [MIM:617244]: A disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair. {ECO:0000269|PubMed:26253028, ECO:0000269|PubMed:26681308}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.6.4.-
uniprot
proteins
function
FUNCTION: Homologous DNA recombinase that catalyzes strand exchange, a key step in DNA repair through homologous recombination (HR) (PubMed:12205100, PubMed:12442171, PubMed:15937124, PubMed:17515904, PubMed:17515903, PubMed:18417535, PubMed:19303847, PubMed:20231364, PubMed:20348101, PubMed:22325354, PubMed:23509288, PubMed:23754376, PubMed:24141787, PubMed:26681308, PubMed:27941124, PubMed:28575658, PubMed:32640219, PubMed:37499663, PubMed:38509361, PubMed:7988572). Binds to single-stranded DNA (ssDNA) in an ATP-dependent manner to form nucleoprotein filaments which are essential for the homology search and strand exchange (PubMed:12205100, PubMed:15937124, PubMed:17515904, PubMed:17515903, PubMed:18417535, PubMed:19303847, PubMed:15226506, PubMed:20231364, PubMed:20348101, PubMed:23509288, PubMed:23754376, PubMed:26681308, PubMed:28575658, PubMed:37499663, PubMed:39636933, PubMed:41166468, PubMed:38509361, PubMed:7988572). Catalyzes the recognition of homology and strand exchange between homologous DNA partners to form a joint molecule between a processed DNA break and the repair template (PubMed:12205100, PubMed:18417535, PubMed:19303847, PubMed:20231364, PubMed:20348101, PubMed:23509288, PubMed:23754376, PubMed:26681308, PubMed:28575658, PubMed:38459011). RAD51 targeting to ssDNA promotes removal of replication protein-A (RPA) from ssDNA and stabilization of RAD51-ssDNA filaments by blocking ATP hydrolysis (PubMed:20729859). Nucleosomal DNA is peeled from the histone surface by the RAD51 filament (PubMed:38509361). Recruited to resolve stalled replication forks during replication stress (PubMed:27797818, PubMed:31844045). Also required for homologous recombination during meiosis by acting as an non-catalytic accessory factor for DMC1 recombinase, enabling proper chromosome pairing and crossing over (By similarity). Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51C and XRCC3 (PubMed:20413593). Also involved in interstrand cross-link repair (PubMed:26253028). {ECO:0000250|UniProtKB:Q08297, ECO:0000269|PubMed:12205100, ECO:0000269|PubMed:12442171, ECO:0000269|PubMed:15226506, ECO:0000269|PubMed:15937124, ECO:0000269|PubMed:17515903, ECO:0000269|PubMed:17515904, ECO:0000269|PubMed:18417535, ECO:0000269|PubMed:19303847, ECO:0000269|PubMed:20231364, ECO:0000269|PubMed:20348101, ECO:0000269|PubMed:20413593, ECO:0000269|PubMed:20729859, ECO:0000269|PubMed:22325354, ECO:0000269|PubMed:23509288, ECO:0000269|PubMed:23754376, ECO:0000269|PubMed:24141787, ECO:0000269|PubMed:26253028, ECO:0000269|PubMed:26681308, ECO:0000269|PubMed:27797818, ECO:0000269|PubMed:27941124, ECO:0000269|PubMed:28575658, ECO:0000269|PubMed:31844045, ECO:0000269|PubMed:32640219, ECO:0000269|PubMed:37499663, ECO:0000269|PubMed:38459011, ECO:0000269|PubMed:38509361, ECO:0000269|PubMed:39636933, ECO:0000269|PubMed:41166468, ECO:0000269|PubMed:7988572}.
uniprot
proteins
mass_dalton
36966
uniprot
proteins
mutagenesis
MUTAGEN 13; /note="T->A: Abolished phosphorylation by CK2."; /evidence="ECO:0000269|PubMed:22325354"; MUTAGEN 14; /note="S->A: Abolished phosphorylation by PLK1 and subsequent phosphorylation by CK2."; /evidence="ECO:0000269|PubMed:22325354, ECO:0000269|PubMed:26811421"; MUTAGEN 57..64; /note="KKELINIK->RRELINIR: In 3KR mutant; abolished deubiquitination by UCHL3."; /evidence="ECO:0000269|PubMed:27941124"; MUTAGEN 58; /note="K->R: Impaired ubiquitination; when associated with R-64."; /evidence="ECO:0000269|PubMed:23393192"; MUTAGEN 59; /note="E->R: Decreased nucleosome-binding."; /evidence="ECO:0000269|PubMed:38509361"; MUTAGEN 64; /note="K->A: Impaired DNA-binding."; /evidence="ECO:0000269|PubMed:38509361"; MUTAGEN 64; /note="K->R: Impaired ubiquitination; when associated with R-58."; /evidence="ECO:0000269|PubMed:23393192"; MUTAGEN 67; /note="S->E: Mimics phosphorylation; increased formation of filament."; /evidence="ECO:0000269|PubMed:38509361"; MUTAGEN 70; /note="K->A: Impaired DNA-binding."; /evidence="ECO:0000269|PubMed:38509361"; MUTAGEN 86; /note="F->A: Loss of homooligomerization."; /evidence="ECO:0000269|PubMed:12442171"; MUTAGEN 86; /note="F->E: Impaired ability to form homooligomers."; /evidence="ECO:0000269|PubMed:17515904"; MUTAGEN 89; /note="A->E: Loss of homooligomerization."; /evidence="ECO:0000269|PubMed:12442171, ECO:0000269|PubMed:17515904"; MUTAGEN 208..209; /note="SA->LE: Disrupts interaction with BRCA2, no effect on homooligomerization, promotes interaction with XPO1 and cytoplasmic localization."; /evidence="ECO:0000269|PubMed:14580352, ECO:0000269|PubMed:24013206"; MUTAGEN 309; /note="T->A: Confers hypersensitivity to hydroxyurea."; /evidence="ECO:0000269|PubMed:15665856"; MUTAGEN Q06609-3:264..266; /note="Missing: Inhibits nuclear localization."; /evidence="ECO:0000269|PubMed:18417535"; MUTAGEN Q06609-3:264; /note="R->A: Inhibits nuclear localization."; /evidence="ECO:0000269|PubMed:18417535"; MUTAGEN Q06609-3:265; /note="K->Q: Inhibits nuclear localization."; /evidence="ECO:0000269|PubMed:18417535
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated by the SCF(FBH1) E3 ubiquitin ligase complex, regulating RAD51 subcellular location and preventing its association with DNA (PubMed:23393192). Ubiquitinated by RFWD3 in response to DNA damage: ubiquitination leads to degradation by the proteasome, promoting homologous recombination (PubMed:28575658). Deubiquitinated at Lys-57, Lys-58 and Lys-64 by UCHL3 in response to DNA damage, promoting interaction with BRCA2 and formation of nucleoprotein filaments (PubMed:27941124). {ECO:0000269|PubMed:23393192, ECO:0000269|PubMed:27941124, ECO:0000269|PubMed:28575658}.; PTM: Phosphorylation of Thr-309 by CHEK1 may enhance association with chromatin at sites of DNA damage and promote DNA repair by homologous recombination (PubMed:15665856). Phosphorylated at Ser-14 by PLK1, triggering phosphorylation at Thr-13 by CK2, thereby promoting interaction with TOPBP1 and recruitment to DNA damage sites during S-phase (PubMed:22325354, PubMed:26811421). Phosphorylation by ABL1 inhibits function (PubMed:9461559). Phosphorylation at Ser-67 stimulates the formation of RAD51 nucleoprotein filament (PubMed:38509361). {ECO:0000269|PubMed:15665856, ECO:0000269|PubMed:22325354, ECO:0000269|PubMed:26811421, ECO:0000269|PubMed:38509361, ECO:0000269|PubMed:9461559}.
uniprot
proteins
protein_family
RAD51 subfamily
uniprot
proteins
protein_family
RecA family
uniprot
proteins
pubmed
10390347
uniprot
proteins
pubmed
10493508
uniprot
proteins
pubmed
10807537
uniprot
proteins
pubmed
10851248
uniprot
proteins
pubmed
11535547
uniprot
proteins
pubmed
11842113
uniprot
proteins
pubmed
11884632
uniprot
proteins
pubmed
12205100
uniprot
proteins
pubmed
12427746
uniprot
proteins
pubmed
12442171
uniprot
proteins
pubmed
14580352
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15226506
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15665856
uniprot
proteins
pubmed
15937124
uniprot
proteins
pubmed
16215984
uniprot
proteins
pubmed
16428451
uniprot
proteins
pubmed
16572171
uniprot
proteins
pubmed
16990250
uniprot
proteins
pubmed
17515903
uniprot
proteins
pubmed
17515904
uniprot
proteins
pubmed
18417535
uniprot
proteins
pubmed
18449195
uniprot
proteins
pubmed
19303847
uniprot
proteins
pubmed
19783859
uniprot
proteins
pubmed
19995904
uniprot
proteins
pubmed
20154705
uniprot
proteins
pubmed
20231364
uniprot
proteins
pubmed
20348101
uniprot
proteins
pubmed
20413593
uniprot
proteins
pubmed
20705237
uniprot
proteins
pubmed
20729859
uniprot
proteins
pubmed
20871615
uniprot
proteins
pubmed
21252223
uniprot
proteins
pubmed
21276791
uniprot
proteins
pubmed
21965664
uniprot
proteins
pubmed
22153967
uniprot
proteins
pubmed
22305526
uniprot
proteins
pubmed
22325354
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23393192
uniprot
proteins
pubmed
23401855
uniprot
proteins
pubmed
23509288
uniprot
proteins
pubmed
23754376
uniprot
proteins
pubmed
24013206
uniprot
proteins
pubmed
24141787
uniprot
proteins
pubmed
25539919
uniprot
proteins
pubmed
25642963
uniprot
proteins
pubmed
26253028
uniprot
proteins
pubmed
26681308
uniprot
proteins
pubmed
26811421
uniprot
proteins
pubmed
26833090
uniprot
proteins
pubmed
27797818
uniprot
proteins
pubmed
27941124
uniprot
proteins
pubmed
28575658
uniprot
proteins
pubmed
29507080
uniprot
proteins
pubmed
30406765
uniprot
proteins
pubmed
31844045
uniprot
proteins
pubmed
32640219
uniprot
proteins
pubmed
34937945
uniprot
proteins
pubmed
37499663
uniprot
proteins
pubmed
38314870
uniprot
proteins
pubmed
38459011
uniprot
proteins
pubmed
38509361
uniprot
proteins
pubmed
39636933
uniprot
proteins
pubmed
41166468
uniprot
proteins
pubmed
7988572
uniprot
proteins
pubmed
8358431
uniprot
proteins
pubmed
8479919
uniprot
proteins
pubmed
9192668
uniprot
proteins
pubmed
9321665
uniprot
proteins
pubmed
9396801
uniprot
proteins
pubmed
9461559
uniprot
proteins
sequence_length
339
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:19303847, ECO:0000269|PubMed:22325354, ECO:0000269|PubMed:23401855, ECO:0000269|PubMed:26811421, ECO:0000269|PubMed:27797818, ECO:0000269|PubMed:27941124, ECO:0000269|PubMed:31844045, ECO:0000269|PubMed:37499663}. Nucleus {ECO:0000269|PubMed:12442171, ECO:0000269|PubMed:15665856, ECO:0000269|PubMed:18417535, ECO:0000269|PubMed:19783859, ECO:0000269|PubMed:23401855, ECO:0000269|PubMed:23509288, ECO:0000269|PubMed:26681308, ECO:0000269|PubMed:26833090, ECO:0000269|PubMed:9192668}. Cytoplasm {ECO:0000269|PubMed:16215984, ECO:0000269|PubMed:26681308}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16215984}. Mitochondrion matrix {ECO:0000269|PubMed:20413593}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:21276791}. Note=Colocalizes with RAD51AP1 and RPA2 to multiple nuclear foci upon induction of DNA damage (PubMed:20154705). DNA damage induces an increase in nuclear levels (PubMed:20154705). Together with FIGNL1, redistributed in discrete nuclear DNA damage-induced foci after ionizing radiation (IR) or camptothecin (CPT) treatment (PubMed:23754376). Accumulated at sites of DNA damage in a SPIDR-dependent manner (PubMed:23509288). Recruited at sites of DNA damage in a MCM9-MCM8-dependent manner (PubMed:23401855). Recruited at sites of DNA damage following interaction with TOPBP1 in S-phase (PubMed:26811421). Colocalizes with ERCC5/XPG to nuclear foci in S phase (PubMed:26833090). Recruited to stalled replication forks during replication stress by the TONSL-MMS22L complex, as well as ATAD5 and WDR48 in an ATR-dependent manner (PubMed:27797818, PubMed:31844045). In germ cells, during meiotic prcess, binds single-stranded DNA (ssDNA) away from the break site (By similarity). {ECO:0000250|UniProtKB:Q08297, ECO:0000269|PubMed:20154705, ECO:0000269|PubMed:23401855, ECO:0000269|PubMed:23509288, ECO:0000269|PubMed:23754376, ECO:0000269|PubMed:26811421, ECO:0000269|PubMed:26833090, ECO:0000269|PubMed:27797818, ECO:0000269|PubMed:31844045}.
uniprot
proteins