RAD51

gene
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Also known as HsRad51HsT16930BRCC5FANCR

Summary

RAD51 (RAD51 recombinase, HGNC:9817) is a protein-coding gene on chromosome 15q15.1, encoding DNA repair protein RAD51 homolog 1 (Q06609). Plays an important role in homologous strand exchange, a key step in DNA repair through homologous recombination (HR). It is a common-essential gene (DepMap: required in 97.3% of cancer cell lines).

The protein encoded by this gene is a member of the RAD51 protein family. RAD51 family members are highly similar to bacterial RecA and Saccharomyces cerevisiae Rad51, and are known to be involved in the homologous recombination and repair of DNA. This protein can interact with the ssDNA-binding protein RPA and RAD52, and it is thought to play roles in homologous pairing and strand transfer of DNA. This protein is also found to interact with BRCA1 and BRCA2, which may be important for the cellular response to DNA damage. BRCA2 is shown to regulate both the intracellular localization and DNA-binding ability of this protein. Loss of these controls following BRCA2 inactivation may be a key event leading to genomic instability and tumorigenesis. Multiple transcript variants encoding different isoforms have been found for this gene.

Source: NCBI Gene 5888 — RefSeq curated summary.

At a glance

  • Gene–disease (curated): mirror movements 2 (Strong, GenCC) — +4 more curated relationships
  • GWAS associations: 7
  • Clinical variants (ClinVar): 502 total — 5 pathogenic, 7 likely-pathogenic
  • Phenotypes (HPO): 143
  • Druggable target: yes
  • Cancer dependency (DepMap): dependent in 97.3% of screened cell lines (common-essential)
  • MANE Select transcript: NM_002875

Identifiers

Gene identifiers

FieldValue
HGNC IDHGNC:9817
Approved symbolRAD51
NameRAD51 recombinase
Location15q15.1
Locus typegene with protein product
StatusApproved
AliasesHsRad51, HsT16930, BRCC5, FANCR
Ensembl geneENSG00000051180
Ensembl biotypeprotein_coding
OMIM179617
Entrez5888

Gene structure

Transcript identifiers

Ensembl transcripts: 18 — 15 protein_coding, 3 nonsense_mediated_decay

ENST00000267868, ENST00000382643, ENST00000423169, ENST00000525066, ENST00000526763, ENST00000527860, ENST00000531277, ENST00000532743, ENST00000533741, ENST00000557850, ENST00000645673, ENST00000894385, ENST00000894386, ENST00000912735, ENST00000912736, ENST00000912737, ENST00000912738, ENST00000948778

RefSeq mRNA: 4 — MANE Select: NM_002875 NM_001164269, NM_001164270, NM_002875, NM_133487

CCDS: CCDS10062, CCDS53931, CCDS53932

Canonical transcript exons

ENST00000267868 — 10 exons

ExonStartEnd
ENSE000018757824073105540732340
ENSE000021723414069517440695425
ENSE000035402524072985340729974
ENSE000036118714070617740706294
ENSE000038425304069875740698845
ENSE000038443294072871140728824
ENSE000038461974070902540709116
ENSE000038469734071880540718899
ENSE000038471244070106440701201
ENSE000038494604072950540729634

Expression profiles

Bgee: expression breadth ubiquitous, 193 present calls, max score 91.67.

FANTOM5 (CAGE): breadth ubiquitous, TPM avg 8.3127 / max 105.4209, expressed in 1231 samples.

FANTOM5 promoters (3 alternative TSS)

Promoter IDTPM avgSamples expressed
1461257.36681198
1461260.9413561
1461270.00452

Top tissues by expression

285 total, by Bgee expression score (0-100, higher = more expressed):

TissueAnatomy IDExpression scoreQuality
primordial germ cell in gonadCL:0000670 ∩ UBERON:000099191.67gold quality
buccal mucosa cellCL:000233687.04gold quality
ventricular zoneUBERON:000305386.55gold quality
embryoUBERON:000092286.54gold quality
ganglionic eminenceUBERON:000402385.74gold quality
left testisUBERON:000453385.48gold quality
right testisUBERON:000453485.37gold quality
mucosa of transverse colonUBERON:000499184.95gold quality
testisUBERON:000047384.64gold quality
male germ line stem cell (sensu Vertebrata) in testisCL:0000089 ∩ UBERON:000047384.43gold quality
bone marrow cellCL:000209282.81gold quality
cervix squamous epitheliumUBERON:000692282.74silver quality
secondary oocyteCL:000065581.96gold quality
bone marrowUBERON:000237181.96gold quality
rectumUBERON:000105280.65gold quality
trabecular bone tissueUBERON:000248379.84gold quality
stromal cell of endometriumCL:000225579.51gold quality
spermCL:000001979.31gold quality
epithelium of nasopharynxUBERON:000195178.88silver quality
male germ cellCL:000001578.62gold quality
oocyteCL:000002377.23gold quality
vermiform appendixUBERON:000115476.42gold quality
placentaUBERON:000198776.32gold quality
amniotic fluidUBERON:000017376.03gold quality
squamous epitheliumUBERON:000691475.10silver quality
lymph nodeUBERON:000002974.73gold quality
esophagus mucosaUBERON:000246974.38gold quality
esophagus squamous epitheliumUBERON:000692073.54gold quality
caecumUBERON:000115373.28gold quality
epithelium of esophagusUBERON:000197672.99gold quality

Single-cell (SCXA)

Detected in 1 experiment(s), a significant marker in 1.

ExperimentMarker?Max mean expression
E-ANND-3yes5.21

Regulation

Is transcription factor: yes

Downstream targets (CollecTRI)

1 targets.

TargetRegulation
SP1Activation

Upstream regulators (CollecTRI, top): BRCA2, CREBBP, E2F1, E2F4, EGR1, EP300, ETS1, ETV4, FLT3, HR, HSF4, MEN1, MYC, PTEN, RBL2, STAT5A, STAT5B, TP53

miRNA regulators (miRDB)

43 targeting RAD51, top 30 by miRDB confidence (max_score; target_count = how many genes the miRNA targets in total — lower means more specific):

miRNAMax scoreAvg scoremiRNA target_count
HSA-MIR-499A-5P99.9870.791323
HSA-MIR-96-5P99.9572.802140
HSA-MIR-124-3P99.8973.743043
HSA-MIR-506-3P99.8973.553057
HSA-MIR-374C-5P99.8072.062910
HSA-MIR-655-3P99.8072.192909
HSA-MIR-4713-5P99.7867.801794
HSA-MIR-320A-3P99.7769.732107
HSA-MIR-320B99.7769.732107
HSA-MIR-320C99.7769.732107
HSA-MIR-320D99.7769.732107
HSA-MIR-442999.7769.622111
HSA-MIR-2681-5P99.7567.641655
HSA-MIR-366099.6867.331149
HSA-MIR-452699.6867.071136
HSA-MIR-5003-5P99.6169.131624
HSA-MIR-426199.5970.303415
HSA-MIR-6832-5P99.5864.821132
HSA-MIR-4762-5P99.5768.541424
HSA-MIR-510-3P99.5470.062965
HSA-MIR-888-3P99.5369.771057
HSA-MIR-766-3P99.4765.241811
HSA-MIR-57899.4668.361787
HSA-MIR-147B-5P99.4570.622432
HSA-MIR-20A-3P99.4469.101575
HSA-MIR-32-3P99.3668.202517
HSA-MIR-329-5P99.2768.111597
HSA-MIR-194-5P99.0169.651465
HSA-MIR-989899.0067.89500
HSA-MIR-480198.9669.422096

Functional genomics

DepMap (CRISPR cell-line fitness): dependent in 97.3% of screened cell lines, common-essential.

Literature-anchored findings (GeneRIF, showing 40)

  • molecular evolution (PMID:11580245)
  • reduces double-strand break-induced homologous recombination with overexpression in mammalian cells (PMID:11691922)
  • Elevated levels of Rad51 recombination protein in tumor cells. (PMID:11782381)
  • differential effects of overexpression on gene targeting and extrachromosomal homologous recombination in a human tumor cell line (PMID:11809887)
  • biochemical characterization by ATP hydrolysis (PMID:11839739)
  • binding and ATPPase inhibition by adenine nucleotides (PMID:11839740)
  • modulation of DNA binding by adenosine nucleotides (PMID:11839741)
  • TGFbeta can promote DNA instability through down-regulation of Rad51 and inhibition of DNA repair. (PMID:11867550)
  • autoantibody screening indicates Rad51 is a tumor-associated antigen in pancreatic adenocarcinoma (PMID:11935313)
  • involved in homologous DNA pairing (PMID:12205100)
  • association of oligomeric state with biochemical function (PMID:12226092)
  • interacts with FANCD2 in S phase cell lines (PMID:12239151)
  • physiological role for the WRN RecQ helicase protein in RAD51-dependent homologous recombination (PMID:12242278)
  • crystal structure of a complex between an evolutionarily conserved sequence in BRCA2 (the BRC repeat) and the RecA-homology domain of RAD51 (PMID:12442171)
  • S-phase RAD51 foci form normally in CAPAN-1 cells expressing truncated BRCA2. Moreover, we find that RAD51 specifically associates with chromatin at S phase in a reaction that is BRCA2-independent. (PMID:12606939)
  • In conclusion, effective and prompt IR-induced Rad51 focus formation is cell cycle-regulated and requires both ATM and c-Abl. (PMID:12650908)
  • study implies that the G/C polymorphism of the RAD51 gene may not be directly involved in the development and/or progression of breast cancer and so it may not be useful as an independent marker in this disease (PMID:12673366)
  • p53 interacts with hRAD51 and hRAD54, and directly modulates homologous recombination. (PMID:12750285)
  • Ectopic expression of the recombination protein Rad51 can protect cells from radiation-induced translocations. (PMID:12826751)
  • exogenous nuclease-defective FEN-1 causes repeat instability and aberrant DNA repair. Inefficient flap processing blocks the formation of Rad51/BRCA1 complexes but invokes repair by other pathways (PMID:12917330)
  • Rad51 is involved in the signalling and repair of DNA damage–REVIEW (PMID:14599770)
  • link between elevated Rad51 protein levels, genome instability, and tumor progression (PMID:14724582)
  • results establish a direct functional link between p53 and Rad51, and reveal that one of p53’s functions in genome stabilization may be to prevent detrimental genome rearrangements promoted by Rad51 (PMID:15095978)
  • ADP/ATP processing and strand exchange by hRAD51 is enhanced by hXRCC2 (PMID:15123651)
  • investigation of the role of tyrosine 315 by comparing the three-dimensional structures of human Rad51 and its prokaryotic homologue, Escherichia coli RecA (PMID:15165851)
  • a crucial role of the ATPase activity in regulation of DNA strand exchange activity of hRad51 protein. (PMID:15226506)
  • Mutational analyses of the human Rad51-Tyr315 residue indicates an important role of Tyr315 residue in ssDNA binding and DNA filament formation. (PMID:15330855)
  • Rad54 protein serves as a dsDNA gateway for the Rad51-ssDNA filament, promoting binding and an ATP hydrolysis-dependent translocation of dsDNA during the search for homologous sequences (PMID:15466868)
  • Rad51 binds at a promiscuous, highly electrostatic binding site in p53 (PMID:15611070)
  • FANCD2 mediates double strand DNA break repair independently of BRCA2- and Rad51-associated homologous recombination (PMID:15671039)
  • BLM collaborates with RAD51 to facilitate recombination repair and promotes the resistance of BCR/ABL-positive leukemia cells to DNA-damaging agents. (PMID:15750625)
  • purified hRad51 and hRad52 interact with each other as well as with Mini chromosome maintenance (MCM) proteins in HeLa cell extracts (PMID:15766559)
  • Rad51 forms regular stable filaments with extended double-stranded DNA in conditions that promote an efficient in vitro strand exchange reaction. (PMID:15944450)
  • Data show that JC polyomavirus T-antigen inhibits homologous recombination DNA repair by binding insulin receptor substrate 1, which then translocates to the nucleus and binds Rad51 at the site of damaged DNA. (PMID:15965906)
  • These results help us to model important mechanistic steps of hRad51 presynapsis on ssDNA templates. (PMID:16018971)
  • MDC1 functions in Rad51-mediated homologous recombination by retaining Rad51 in chromatin. (PMID:16186822)
  • We have made the unexpected observation that Rad51 degradation via the ubiquitin-mediated proteasome pathway occurs as a natural part of recombinational DNA repair. (PMID:16215984)
  • Because mutations in BRCA1 and BRCA2 may be directly linked with breast cancer, genetic variations in the BRCA2 and RAD51 genes may be believed to play a role in this disease. (PMID:16261408)
  • DNA-induced disassembly of higher-order forms of Rad51 and Rad52 proteins as steps that precede protein assembly during hRad51 presynapsis on DNA, in vitro. (PMID:16367760)
  • RAD51C ensures a tight regulation of RAD51 assembly during DSB repair and plays a direct role in repairing DSBs in vivo. (PMID:16395335)

Cross-species orthologs

5 orthologs

OrganismSymbolGene ID
danio_reriorad51ENSDARG00000041411
mus_musculusRad51ENSMUSG00000027323
rattus_norvegicusRad51ENSRNOG00000037302
drosophila_melanogasterspn-AFBGN0003479
caenorhabditis_elegansWBGENE00004297

Paralogs (6): DMC1 (ENSG00000100206), RAD51C (ENSG00000108384), XRCC3 (ENSG00000126215), RAD51B (ENSG00000182185), RAD51D (ENSG00000185379), XRCC2 (ENSG00000196584)

Protein

Protein identifiers

DNA repair protein RAD51 homolog 1Q06609 (reviewed: Q06609)

Alternative names: RAD51 homolog A

All UniProt accessions (6): Q06609, E9PI54, E9PJ30, E9PNT5, H0YD61, Q9NZG9

UniProt curated annotations — full annotation on UniProt →

Function. Plays an important role in homologous strand exchange, a key step in DNA repair through homologous recombination (HR). Binds to single-stranded DNA in an ATP-dependent manner to form nucleoprotein filaments which are essential for the homology search and strand exchange. 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. Recruited to resolve stalled replication forks during replication stress. Part of a PALB2-scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51C and XRCC3. Also involved in interstrand cross-link repair.

Subunit / interactions. Forms linear homooligomers, giving rise to a RAD51 nucleoprotein filament, which is essential for strand-pairing reactions during DNA recombination. Interacts with RAD54L; the interaction enhances RAD51-mediated homology search and strand invasion. Interacts with RAD54B; the interaction could enhance RAD51-mediated homology search and strand invasion. Interacts with BRCA1 and either directly or indirectly with p53. Interacts with XRCC3. Interacts with the BCDX2 subcomplex RAD51C:RAD51B. Component of the homologous recombination repair (HR) complex composed of ERCC5/XPG, BRCA2, PALB2, DSS1 and RAD51. Interacts directly with PALB2 which may serve as a scaffold for a HR complex containing PALB2, BRCA2, RAD51C, RAD51 and XRCC3. Interacts with RAD51AP1 and RAD51AP2. Interacts with CHEK1, and this may require prior phosphorylation of CHEK1. Interacts with the MND1-PSMC3IP heterodimer. Found in a complex, at least composed of BLM, RAD51 and SPIDR; the complex formation is mediated by SPIDR. Interacts with SPIDR; the interaction is direct and recruits RAD51 to DNA damage sites. Interacts with FIGNL1 (via N-terminal one-half region); the interaction is direct. Interacts with RAD51AP1 (via C-terminal region); the interaction is direct. Interacts with NABP2, RPA1, PALB2 and RAD51. Interacts with SWI5/C9orf119, and at lower level with SFR1/MEIR5. Interacts with hyperphosphorylated RPA2; this interaction is necessary for efficient recruitment to chromatin in response to DNA damage. Interacts with SWSAP1; involved in homologous recombination repair. Interacts with PARPBP, BRCA2 and RECQL5; these interactions interfere with the formation of the RAD51-DNA homologous recombination structure. Interacts with POLQ; POLQ acts as an inhibitor of homology-recombination repair (HR) pathway by limiting RAD51 accumulation at resected ends. Interacts with FBH1. Interacts with POLN. Interacts with RFWD3. Interacts with the MCM8-MCM9 complex; the interaction recruits RAD51 to DNA damage sites. Component of a multiprotein complex with MEIOB and SPATA22. Interacts with the complex BRME1:HSF2BP:BRCA2. Interacts with HELQ; stimulating HELQ DNA helicase activity and ability to unwing DNA. Interacts with MMS22L; the interaction is direct and promotes recruitment of RAD51 to sites of DNA damage. Interacts with the ATAD5 RFC-like complex. Within the ATAD5 RFC-like complex, interacts with ATAD5 (via N-terminus); the interaction is direct and enhanced under replication stress. Interacts with WDR48; the interaction is enhanced under replication stress. Interacts with DNA helicase ZGRF1; the interaction promotes RAD51 strand exchange activity. Interacts (when phosphorylated) with TOPBP1; interaction takes place following phosphorylation by CK2 and PLK1 and promotes recruitment to DNA damage sites. Interacts with GRB2; this interaction inhibits RAD51 ATPase activity to stabilize RAD51 on stalled replication forks.

Subcellular location. Nucleus. Cytoplasm. Perinuclear region. Mitochondrion matrix. Chromosome. Cytoskeleton. Microtubule organizing center. Centrosome.

Tissue specificity. Highly expressed in testis and thymus, followed by small intestine, placenta, colon, pancreas and ovary. Weakly expressed in breast.

Post-translational modifications. Ubiquitinated by the SCF(FBH1) E3 ubiquitin ligase complex, regulating RAD51 subcellular location and preventing its association with DNA. Ubiquitinated by RFWD3 in response to DNA damage: ubiquitination leads to degradation by the proteasome, promoting homologous recombination. Phosphorylation of Thr-309 by CHEK1 may enhance association with chromatin at sites of DNA damage and promote DNA repair by homologous recombination. 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. Phosphorylation by ABL1 inhibits function.

Disease relevance. 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. Disease susceptibility is associated with variants affecting the gene represented in this entry. 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. The disease is caused by variants affecting the gene represented in this entry. 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. The disease is caused by variants affecting the gene represented in this entry.

Activity regulation. Acts as a self-inactivating ATPase, with rapid ATP hydrolysis and slow ADP dissociation. Ca(2+) by reducing the ATPase activity preserves the nucleoprotein filament in its active state, thereby stimulating the DNA strand exchange activity of RAD51.

Domain organisation. The nuclear localization may reside in the C-terminus (between 259 and 339 AA).

Induction. Stress-induced increase in the mitochondrial levels is seen.

Miscellaneous. Mutagenesis of Arg-264 to Ala inhibits nuclear localization. Mutagenesis of Lys-264 to Gln inhibits nuclear localization. Deletion of 254-Arg-Lys-255 inhibits nuclear localization.

Similarity. Belongs to the RecA family. RAD51 subfamily.

Isoforms (4)

UniProt IDNamesCanonical?
Q06609-11yes
Q06609-22
Q06609-33
Q06609-44

RefSeq proteins (4): NP_001157741, NP_001157742, NP_002866, NP_597994 (=MANE)

Domains & families (InterPro)

IDNameType
IPR003593AAA+_ATPaseDomain
IPR010995DNA_repair_Rad51/TF_NusA_a-hlxHomologous_superfamily
IPR011941DNA_recomb/repair_Rad51Family
IPR013632Rad51_CDomain
IPR016467DNA_recomb/repair_RecA-likeFamily
IPR020587RecA_monomer-monomer_interfaceDomain
IPR020588RecA_ATP-bdDomain
IPR027417P-loop_NTPaseHomologous_superfamily

Pfam: PF08423, PF14520

Enzyme classification (BRENDA):

  • EC 3.6.4.B7 — (BRENDA: organisms, substrates, inhibitors, Km, kcat entries)

Catalyzed reactions (Rhea), 1 shown:

  • ATP + H2O = ADP + phosphate + H(+) (RHEA:13065)

UniProt features (77 total): strand 17, helix 16, binding site 11, mutagenesis site 8, sequence variant 6, modified residue 5, splice variant 4, cross-link 2, turn 2, initiator methionine 1, chain 1, domain 1, region of interest 1, short sequence motif 1, sequence conflict 1

Structure

Experimental structures (PDB)

52 structures, top 30 by resolution.

PDBMethodResolution (Å)
1N0WX-RAY DIFFRACTION1.7
9TRMELECTRON MICROSCOPY2.4
9SVYELECTRON MICROSCOPY2.6
8PBCELECTRON MICROSCOPY2.61
9Q29ELECTRON MICROSCOPY2.61
9SRZELECTRON MICROSCOPY2.61
9I62ELECTRON MICROSCOPY2.64
9Q2AELECTRON MICROSCOPY2.67
9SVXELECTRON MICROSCOPY2.7
8UVWX-RAY DIFFRACTION2.73
8PBDELECTRON MICROSCOPY2.83
9Q23ELECTRON MICROSCOPY2.84
9Q28ELECTRON MICROSCOPY2.84
8XBWELECTRON MICROSCOPY2.89
8BR2ELECTRON MICROSCOPY2.9
9SSLELECTRON MICROSCOPY2.9
9ZZRELECTRON MICROSCOPY2.95
7EJCELECTRON MICROSCOPY2.97
9QNCELECTRON MICROSCOPY2.98
9SW0ELECTRON MICROSCOPY3
9TRLELECTRON MICROSCOPY3
8C3JX-RAY DIFFRACTION3.02
8GYKELECTRON MICROSCOPY3.14
9QN8ELECTRON MICROSCOPY3.14
8R64ELECTRON MICROSCOPY3.2
8RCDELECTRON MICROSCOPY3.2
9Q2BELECTRON MICROSCOPY3.2
9TYYELECTRON MICROSCOPY3.2
9Q25ELECTRON MICROSCOPY3.24
9OMYELECTRON MICROSCOPY3.25

Predicted structure (AlphaFold)

ModelpLDDTFraction very-high
AF-Q06609-F191.590.89

Functional residue map

Curated UniProt residues grouped by drug-discovery relevance — catalytic, ligand-binding, modification, and mutation-validated positions. Source: UniProtKB sequence features.

Ligand- & substrate-binding residues (11): 135; 170; 222; 268; 319; 322; 130; 132; 133; 134; 134

Post-translational modifications (7): 2, 13, 14, 54, 309, 58, 64

Mutagenesis-validated functional residues (8):

PositionPhenotype
13abolished phosphorylation by ck2.
14abolished phosphorylation by plk1 and subsequent phosphorylation by ck2.
58impaired ubiquitination; when associated with r-64.
64impaired ubiquitination; when associated with r-58.
86loss of homooligomerization.
89loss of homooligomerization.
208–209disrupts interaction with brca2, no effect on homooligomerization, promotes interaction with xpo1 and cytoplasmic locali
309confers hypersensitivity to hydroxyurea.

Function

Pathways and Gene Ontology

Reactome pathways

13 pathways

IDPathway
R-HSA-5685938HDR through Single Strand Annealing (SSA)
R-HSA-5685942HDR through Homologous Recombination (HRR)
R-HSA-5693554Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA)
R-HSA-5693568Resolution of D-loop Structures through Holliday Junction Intermediates
R-HSA-5693579Homologous DNA Pairing and Strand Exchange
R-HSA-5693616Presynaptic phase of homologous DNA pairing and strand exchange
R-HSA-8953750Transcriptional Regulation by E2F6
R-HSA-912446Meiotic recombination
R-HSA-9701192Defective homologous recombination repair (HRR) due to BRCA1 loss of function
R-HSA-9704331Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function
R-HSA-9704646Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function
R-HSA-9709570Impaired BRCA2 binding to RAD51
R-HSA-9709603Impaired BRCA2 binding to PALB2

MSigDB gene sets: 720 (showing top): GOBP_DNA_TEMPLATED_DNA_REPLICATION_MAINTENANCE_OF_FIDELITY, GOBP_REGULATION_OF_DOUBLE_STRAND_BREAK_REPAIR, REACTOME_MEIOTIC_RECOMBINATION, E2F_Q4, GOBP_CHROMOSOME_ORGANIZATION, E2F_Q4_01, GOBP_RESPONSE_TO_NITROGEN_COMPOUND, GOBP_REGULATION_OF_DNA_RECOMBINATION, GOBP_REGULATION_OF_CELL_CYCLE_CHECKPOINT, GOBP_RESPONSE_TO_IONIZING_RADIATION, MULLIGHAN_NPM1_SIGNATURE_3_UP, BIOCARTA_ATM_PATHWAY, GOBP_CELL_CYCLE_DNA_REPLICATION, FISCHER_G1_S_CELL_CYCLE, GOBP_CELL_CYCLE_PHASE_TRANSITION

GO Biological Process (32): telomere maintenance via recombination (GO:0000722), double-strand break repair via homologous recombination (GO:0000724), DNA recombinase assembly (GO:0000730), DNA repair (GO:0006281), DNA recombination (GO:0006310), mitotic recombination (GO:0006312), DNA damage response (GO:0006974), reciprocal meiotic recombination (GO:0007131), response to xenobiotic stimulus (GO:0009410), response to toxic substance (GO:0009636), response to X-ray (GO:0010165), regulation of double-strand break repair via homologous recombination (GO:0010569), telomere maintenance via telomere lengthening (GO:0010833), replication fork processing (GO:0031297), interstrand cross-link repair (GO:0036297), DNA strand invasion (GO:0042148), meiotic cell cycle (GO:0051321), chromosome organization involved in meiotic cell cycle (GO:0070192), cellular response to ionizing radiation (GO:0071479), cellular response to gamma radiation (GO:0071480), cellular response to hydroxyurea (GO:0072711), cellular response to cisplatin (GO:0072719), cellular response to camptothecin (GO:0072757), response to glucoside (GO:1904631), replication-born double-strand break repair via sister chromatid exchange (GO:1990414), mitotic recombination-dependent replication fork processing (GO:1990426), double-strand break repair involved in meiotic recombination (GO:1990918), regulation of DNA damage checkpoint (GO:2000001), DNA metabolic process (GO:0006259), meiosis I (GO:0007127), telomere organization (GO:0032200), cellular response to alkaloid (GO:0071312)

GO Molecular Function (15): DNA strand exchange activity (GO:0000150), chromatin binding (GO:0003682), double-stranded DNA binding (GO:0003690), single-stranded DNA binding (GO:0003697), ATP binding (GO:0005524), ATP-dependent activity, acting on DNA (GO:0008094), single-stranded DNA helicase activity (GO:0017116), enzyme binding (GO:0019899), identical protein binding (GO:0042802), DNA polymerase binding (GO:0070182), ATP-dependent DNA damage sensor activity (GO:0140664), nucleotide binding (GO:0000166), DNA binding (GO:0003677), protein binding (GO:0005515), ATP hydrolysis activity (GO:0016887)

GO Cellular Component (24): nuclear ubiquitin ligase complex (GO:0000152), nuclear chromosome (GO:0000228), chromosome, telomeric region (GO:0000781), chromatin (GO:0000785), condensed chromosome (GO:0000793), condensed nuclear chromosome (GO:0000794), lateral element (GO:0000800), male germ cell nucleus (GO:0001673), nucleus (GO:0005634), nucleoplasm (GO:0005654), nucleolus (GO:0005730), cytoplasm (GO:0005737), mitochondrion (GO:0005739), mitochondrial matrix (GO:0005759), centrosome (GO:0005813), cytosol (GO:0005829), PML body (GO:0016605), protein-containing complex (GO:0032991), protein-DNA complex (GO:0032993), site of double-strand break (GO:0035861), perinuclear region of cytoplasm (GO:0048471), presynaptic intermediate filament cytoskeleton (GO:0099182), chromosome (GO:0005694), cytoskeleton (GO:0005856)

Reactome top-level categories

Rollup of top-9 pathways:

CategoryPathways
HDR through Homologous Recombination (HRR) or Single Strand Annealing (SSA)2
Resolution of D-Loop Structures2
Defective homologous recombination repair (HRR) due to PALB2 loss of function2
Defective homologous recombination repair (HRR) due to BRCA2 loss of function2
HDR through Homologous Recombination (HRR)1
Homologous DNA Pairing and Strand Exchange1
Generic Transcription Pathway1
Meiosis1
Diseases of DNA Double-Strand Break Repair1

GO top-level categories

Rollup of top GO terms by namespace:

CategoryTerms
cellular anatomical structure5
DNA metabolic process3
DNA recombination3
nucleus3
chromosome3
nuclear lumen3
telomere maintenance2
meiotic cell cycle process2
response to chemical2
response to ionizing radiation2
catalytic activity, acting on DNA2
binding2
DNA binding2
ATP-dependent activity2
protein binding2
intracellular membrane-bounded organelle2
cytoplasm2
mitotic recombination1
recombinational repair1
double-strand break repair1
double-strand break repair via synthesis-dependent strand annealing1
protein-DNA complex assembly1
DNA repair complex assembly1
DNA damage response1
cellular response to stress1
meiosis I1
reciprocal homologous recombination1
regulation of DNA recombination1
double-strand break repair via homologous recombination1
regulation of double-strand break repair1
DNA-templated DNA replication maintenance of fidelity1
DNA repair1
cell cycle1
sexual reproduction1
reproductive process1
meiotic nuclear division1
chromosome organization1
meiotic cell cycle1
cellular response to radiation1
response to gamma radiation1

Protein interactions and networks

STRING

5521 interactions, top by confidence (×1000):

Protein AProtein BPartner UniProtScore
RAD51RAD52P43351999
RAD51BRCA2P51587999
RAD51BRCA1P38398999
RAD51ATRXP46100998
RAD51PALB2Q86YC2997
RAD51TP53P04637995
RAD51BARD1Q99728994
RAD51FANCD2Q9BXW9993
RAD51RAD54BQ9Y620980
RAD51CHEK1O14757973
RAD51MND1Q9BWT6968
RAD51WRNQ14191966
RAD51ATMQ13315958
RAD51K7EN88K7EN88956
RAD51EXO1Q9UQ84954

IntAct

272 interactions, top by confidence:

ABTypeScore
BRCA2RAD51psi-mi:“MI:0915”(physical association)0.980
RAD51BRCA2psi-mi:“MI:0915”(physical association)0.980
BRCA2RAD51psi-mi:“MI:0407”(direct interaction)0.980
RAD51BRCA2psi-mi:“MI:0407”(direct interaction)0.980
BRCA2RAD51psi-mi:“MI:0403”(colocalization)0.980
BRCA2RAD51psi-mi:“MI:0914”(association)0.980
PALB2BRCA2psi-mi:“MI:0914”(association)0.970
IGBP1PPP6Cpsi-mi:“MI:0914”(association)0.940
RAD51RAD51psi-mi:“MI:0915”(physical association)0.920
RAD51RAD51psi-mi:“MI:0407”(direct interaction)0.920
RAD51RAD51psi-mi:“MI:0403”(colocalization)0.920

BioGRID (672): RAD51 (Two-hybrid), RAD51 (Affinity Capture-Western), RAD51 (Affinity Capture-MS), RAD51 (Affinity Capture-MS), RAD51 (Affinity Capture-Western), RAD51 (Affinity Capture-Western), RAD51 (Affinity Capture-Western), RAD51 (Affinity Capture-Western), RAD51 (Synthetic Growth Defect), RAD51 (Two-hybrid), RAD51AP1 (Two-hybrid), RAD51 (Two-hybrid), CDH13 (Two-hybrid), CST6 (Two-hybrid), FAM84B (Two-hybrid)

ESM2 similar proteins: A2SR54, A3CWU4, A4FWV5, A4YCN4, A5UMW0, A6VGG2, A8AB83, A9AA90, B8BM09, O27436, O42634, O73948, O77507, O93748, P0CW58, P0CW59, P25453, P37383, P37384, P50265, P70099, P94102, Q06609, Q08297, Q12UG7, Q14565, Q27297, Q2KJ94, Q2NE95, Q39009, Q40134, Q46A31, Q49593, Q4JAT5, Q61880, Q67EU8, Q6L126, Q7EAG4, Q7GBF7, Q7GBF8

Diamond homologs: A2SR54, A3CWU4, A3CXI2, A3MXX9, A4FWV5, A4WN87, A4YCN4, A5UMW0, A6VGG2, A8AB83, A9AA90, B0R7Y4, B1YC14, B8BM09, B8D610, C3MRI1, C3MY77, C3MZK6, C3N7M8, C3NFU5, C4KIT6, O27436, O29269, O42634, O58001, O73948, O74036, O77507, O93748, P0CW58, P0CW59, P0CW91, P0CW92, P25301, P25453, P25454, P36601, P37383, P37384, P50265

SIGNOR signaling

33 interactions.

AEffectBMechanism
CHEK1up-regulatesRAD51phosphorylation
PALB2up-regulatesRAD51binding
BRCA2“up-regulates activity”RAD51binding
ABL1“up-regulates activity”RAD51phosphorylation
RAD51AP1“up-regulates activity”RAD51binding
XRCC3“up-regulates quantity by stabilization”RAD51binding
RAD51“form complex”“BRCC ubiquitin ligase complex”binding
XRCC3“up-regulates activity”RAD51relocalization
“D1-D2-G-X3 complex”“up-regulates activity”RAD51relocalization
HDLBP“up-regulates activity”RAD51binding
BCR-ABL“up-regulates activity”RAD51phosphorylation
“Caspase 3 complex”“down-regulates quantity by destabilization”RAD51cleavage
CASP3“down-regulates quantity by destabilization”RAD51cleavage
PLK1“up-regulates activity”RAD51phosphorylation
RFWD3“up-regulates activity”RAD51ubiquitination
CDK2“down-regulates quantity by destabilization”RAD51phosphorylation
“SHU complex”“up-regulates activity”RAD51binding
ABL1down-regulatesRAD51phosphorylation
ABL1up-regulatesRAD51phosphorylation
FLT3“up-regulates quantity by expression”RAD51“transcriptional regulation”
STAT5A“up-regulates quantity by expression”RAD51“transcriptional regulation”
RAD51“up-regulates activity”SYCP3binding
RAD51“up-regulates activity”Synaptonemal_complexbinding
RAD51up-regulatesDNA_repair
FBH1“up-regulates activity”RAD51binding
“Cullin 1-RBX1-Skp1”“up-regulates activity”RAD51ubiquitination

Enriched among interaction partners

Reactome pathways and GO biological processes over-represented among this gene’s 160 IntAct physical interaction partners (hypergeometric vs the genome-wide background, BH-FDR, gene-set size 15–500, ranked by fold). A functional readout of the neighbourhood — distinct from this gene’s own memberships above, and biased toward well-studied / hub proteins, so read it as themes rather than proof.

Reactome pathways:

PathwayPartnersFoldFDR
Impaired BRCA2 binding to PALB2733.0×9e-08
Translesion synthesis by POLK532.7×1e-05
Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA)832.5×1e-08
Homologous DNA Pairing and Strand Exchange831.4×1e-08
Resolution of D-loop Structures through Holliday Junction Intermediates1031.0×1e-10
Defective homologous recombination repair (HRR) due to BRCA1 loss of function730.5×1e-07
Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function730.5×1e-07
Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function730.5×1e-07

GO biological processes:

GO termPartnersFoldFDR
regulation of double-strand break repair via homologous recombination646.8×3e-07
mitotic G2/M transition checkpoint531.6×4e-05
cellular response to ionizing radiation825.9×1e-07
mismatch repair525.5×1e-04
mitotic G2 DNA damage checkpoint signaling620.9×4e-05
double-strand break repair via homologous recombination1720.9×4e-15
DNA recombination718.6×1e-05
base-excision repair518.4×4e-04

Disease & clinical

Clinical variants and AI predictions

ClinVar

502 variants total. Per-class counts are floors (≥ shown; pagination cap):

ClassificationCount (floor)
Pathogenic5
Likely pathogenic7
Uncertain significance247
Likely benign194
Benign26

Top pathogenic / likely-pathogenic (12)

Variant IDHGVSClassification
29868NM_002875.5(RAD51):c.760C>T (p.Arg254Ter)Pathogenic
29869NM_002875.5(RAD51):c.855dup (p.Pro286fs)Pathogenic
471141NM_002875.5(RAD51):c.749G>A (p.Arg250Gln)Pathogenic
4770021NM_002875.5(RAD51):c.378T>G (p.Phe126Leu)Pathogenic
916731NM_002875.5(RAD51):c.391A>C (p.Thr131Pro)Pathogenic
2443994NM_002875.5(RAD51):c.871ATC[1] (p.Ile292del)Likely pathogenic
2500726NM_002875.5(RAD51):c.590C>T (p.Thr197Ile)Likely pathogenic
2636942NM_002875.5(RAD51):c.53_69delinsTATCTTCTT (p.Glu18fs)Likely pathogenic
3906887NM_002875.5(RAD51):c.881A>G (p.His294Arg)Likely pathogenic
4077458NM_002875.5(RAD51):c.388C>T (p.Arg130Ter)Likely pathogenic
449674NM_002875.5(RAD51):c.857C>T (p.Pro286Leu)Likely pathogenic
522859NM_002875.5(RAD51):c.772G>A (p.Glu258Lys)Likely pathogenic

SpliceAI

1643 predictions. Top by Δscore:

VariantEffectΔscore
15:40698752:TTCA:Tacceptor_loss1.0000
15:40698754:CA:Cacceptor_loss1.0000
15:40698755:A:ACacceptor_loss1.0000
15:40698755:A:AGacceptor_gain1.0000
15:40698756:G:GAacceptor_gain1.0000
15:40698756:GT:Gacceptor_gain1.0000
15:40698756:GTA:Gacceptor_gain1.0000
15:40698756:GTAA:Gacceptor_gain1.0000
15:40698756:GTAAT:Gacceptor_gain1.0000
15:40698758:A:AGacceptor_gain1.0000
15:40698843:GAG:Gdonor_gain1.0000
15:40698844:AGGTA:Adonor_loss1.0000
15:40698845:GGTA:Gdonor_loss1.0000
15:40698847:T:Gdonor_loss1.0000
15:40701056:A:AGacceptor_gain1.0000
15:40701057:T:Gacceptor_gain1.0000
15:40701060:GCA:Gacceptor_loss1.0000
15:40701062:A:ACacceptor_loss1.0000
15:40701062:A:AGacceptor_gain1.0000
15:40701063:G:GTacceptor_gain1.0000
15:40701063:GC:Gacceptor_gain1.0000
15:40701063:GCA:Gacceptor_gain1.0000
15:40701063:GCAGT:Gacceptor_gain1.0000
15:40701197:TTCTG:Tdonor_gain1.0000
15:40701198:TCTG:Tdonor_gain1.0000
15:40701199:CTG:Cdonor_gain1.0000
15:40701200:TG:Tdonor_gain1.0000
15:40701201:GG:Gdonor_gain1.0000
15:40701202:G:GGdonor_gain1.0000
15:40701202:GTAA:Gdonor_loss1.0000

AlphaMissense

2200 scored. Top likely-pathogenic:

VariantProtein changeam_pathogenicity
15:40701131:T:AV52D1.000
15:40706217:C:AA89E1.000
15:40709060:G:AG127R1.000
15:40709060:G:CG127R1.000
15:40709061:G:AG127E1.000
15:40709061:G:TG127V1.000
15:40709066:T:CF129L1.000
15:40709068:C:AF129L1.000
15:40709068:C:GF129L1.000
15:40709075:G:TG132W1.000
15:40709076:G:AG132E1.000
15:40709078:A:CK133Q1.000
15:40709082:C:TT134I1.000
15:40709092:T:GC137W1.000
15:40709113:C:GC144W1.000
15:40729525:A:TD222V1.000
15:40729527:A:CS223R1.000
15:40729529:T:AS223R1.000
15:40729529:T:GS223R1.000
15:40729546:G:CR229T1.000
15:40729546:G:TR229I1.000
15:40729547:A:CR229S1.000
15:40729547:A:TR229S1.000
15:40729561:G:AG234D1.000
15:40729573:T:AL238H1.000
15:40729573:T:CL238P1.000
15:40729582:G:CR241T1.000
15:40729582:G:TR241M1.000
15:40729583:G:CR241S1.000
15:40729583:G:TR241S1.000

dbSNP variants (sampled 300 via entrez): RS1000081593 (15:40695216 C>T), RS1000174544 (15:40703327 C>G), RS1000261225 (15:40716470 A>G), RS1000371561 (15:40709688 T>G), RS1000395200 (15:40703926 CAG>C), RS1000399033 (15:40692814 G>A), RS1000445147 (15:40709408 G>A), RS1000455513 (15:40697641 G>A,C,T), RS1000456563 (15:40716427 CATG>C), RS1000590205 (15:40716754 A>G), RS1000694873 (15:40703610 T>C), RS1000697370 (15:40722795 T>A,G), RS1000924527 (15:40692885 G>A), RS1000944769 (15:40728135 C>T), RS1000955023 (15:40705513 G>A)

Disease associations

OMIM: gene MIM:179617 | disease phenotypes: MIM:114480, MIM:614508, MIM:617244, MIM:167000

GenCC curated gene-disease

DiseaseClassificationInheritance
mirror movements 2StrongAutosomal dominant
Fanconi anemia complementation group RStrongAutosomal dominant
familial congenital mirror movementsSupportiveAutosomal dominant
Fanconi anemiaSupportiveAutosomal recessive
hereditary breast carcinomaLimitedAutosomal dominant

Mondo (7): hereditary breast carcinoma (MONDO:0016419), mirror movements 2 (MONDO:0013790), Fanconi anemia complementation group R (MONDO:0014986), ovarian cancer (MONDO:0008170), hereditary neoplastic syndrome (MONDO:0015356), familial congenital mirror movements (MONDO:0016558), Fanconi anemia (MONDO:0019391)

Orphanet (4): Hereditary breast cancer (Orphanet:227535), Familial congenital mirror movements (Orphanet:238722), Rare ovarian cancer (Orphanet:213500), Inherited cancer-predisposing syndrome (Orphanet:140162)

HPO phenotypes

143 total (30 of 143 shown, HPO-id order):

HPOTerm
HP:0000006Autosomal dominant inheritance
HP:0000010Recurrent urinary tract infections
HP:0000027Azoospermia
HP:0000028Cryptorchidism
HP:0000035Abnormal testis morphology
HP:0000044Hypogonadotropic hypogonadism
HP:0000047Hypospadias
HP:0000072Hydroureter
HP:0000079Abnormality of the urinary system
HP:0000083Renal insufficiency
HP:0000125Pelvic kidney
HP:0000130Abnormality of the uterus
HP:0000135Hypogonadism
HP:0000175Cleft palate
HP:0000218High palate
HP:0000238Hydrocephalus
HP:0000252Microcephaly
HP:0000268Dolichocephaly
HP:0000286Epicanthus
HP:0000316Hypertelorism
HP:0000324Facial asymmetry
HP:0000340Sloping forehead
HP:0000347Micrognathia
HP:0000364Hearing abnormality
HP:0000365Hearing impairment
HP:0000377Abnormal pinna morphology
HP:0000453Choanal atresia
HP:0000478Abnormality of the eye
HP:0000483Astigmatism
HP:0000486Strabismus

GWAS associations

7 associations (top):

StudyTraitp-value
GCST008559_8Anxiety and stress-related disorders7.000000e-07
GCST010002_167Refractive error3.000000e-11
GCST010725_23Malaria2.000000e-06
GCST010725_38Malaria3.000000e-06
GCST010725_80Malaria7.000000e-06
GCST012227_283Hip circumference adjusted for BMI7.000000e-09
GCST90002397_252Mean spheric corpuscular volume6.000000e-22

EFO canonical traits (2, from GWAS)

EFO IDTrait name
EFO:0010098stress-related disorder
EFO:0008039BMI-adjusted hip circumference

MeSH disease descriptors (4)

DescriptorNameTree numbers
D005199Fanconi AnemiaC15.378.050.085.080.280; C15.378.190.223.500.500.280; C16.320.077.280; C18.452.284.280
D009386Neoplastic Syndromes, HereditaryC04.700; C16.320.700
D010051Ovarian NeoplasmsC04.588.322.455; C12.050.351.500.056.630.705; C12.050.351.937.418.685; C12.100.250.056.630.705; C12.900.418.685; C19.344.410; C19.391.630.705
C562840Breast Cancer, Familial (supp.)

Drugs & pharmacology

Drug and pharmacology data

Is drug target: yes

ChEMBL targets (1): CHEMBL2034807 (SINGLE PROTEIN)

PharmGKB: 1 entry (VIP=true, CPIC=false)

PharmGKB variants

3 variants.

VariantGenesLevelScore#Clin annotsDrugs
rs1801320RAD510.000
rs7180135RAD510.000
rs12593359RAD510.000

Binding affinities (BindingDB)

147 measured of 151 human assays (165 total across all organisms); most potent 50 below. Values come from heterogeneous assays and are not directly comparable.

LigandMeasureValue
MLS000697664IC501560 nM
1,1,3-Trimethyl-2-[3-(1,3,3-trimethyl-1,3-dihydro-indol-2-ylidene)-propenyl]-1H-benzo[e]indoliumIC5010600 nM
(3-methyl-4-pyrrolidino-phenyl)amine;hydrochlorideEC5013700 nM
(6-chloranyl-2-phenyl-chromen-4-ylidene)-(2,2,6,6-tetramethylpiperidin-4-yl)azanium;tetrafluoroborateIC5014700 nM
2-chloranyl-N1,N4-bis[4-(4,5-dihydro-1H-imidazol-2-yl)phenyl]benzene-1,4-dicarboxamideIC5016400 nM
3-[(8,9-dimethoxy-2-phenyl-[1,2,4]triazolo[1,5-c]quinazolin-5-yl)amino]propyl-diethyl-amineIC5021100 nM
(2Z)-3-ethyl-2-[(E)-3-(3-ethyl-1,3-benzothiazol-3-ium-2-yl)-2-methyl-prop-2-enylidene]-1,3-benzothiazole;iodideEC5022400 nM
9-Methoxy-5,11-dimethyl-6H-pyrido[4,3-b]carbazoleIC5024700 nM
6-formyl-4,7-dihydroxy-9-keto-5H-phenazine-1-carboxylic acid methyl esterIC5024800 nM
N-cyclopentyl-2-((5-((2-oxobenzo[d]thiazol-3(2H)-yl)methyl)-4-phenpropyl-4H-1,2,4-triazol-3-yl)thio)acetamideEC5025000 nM
2-amino-4,6-dimethyl-3-oxo-1-N,9-N-bis[(3R,6S,7R,10S,16S)-7,11,14-trimethyl-2,5,9,12,15-pentaoxo-3,10-di(propan-2-yl)-8-oxa-1,4,11,14-tetrazabicyclo[14.3.0]nonadecan-6-yl]phenoxazine-1,9-dicarboxamideIC5032100 nM
3-(phenylmethyl)-2-[(E)-2-(3-pyridinyl)ethenyl]-4-quinazolinoneIC5037000 nM
6,7,12,15,15-pentamethyl-3,10-diazatetracyclo[10.2.1.02,11.04,9]pentadeca-2(11),3,5,7,9-pentaene-1-carboxylic acidIC5037100 nM
3-[(2Z)-2-(3-formyl-4-oxo-1-cyclohexa-2,5-dienylidene)hydrazinyl]benzoic acidIC5042500 nM
cid_649572IC5042500 nM
4-[morpholin-4-yl(2,2,3,3-tetrafluoropropoxy)phosphoryl]morpholineIC5042500 nM
methyl 2-azanyl-5-phenyl-1,3-thiazole-4-carboxylateIC5042500 nM
MLS000082684IC5042500 nM
MLS000054855IC5042500 nM
cid_3237774IC5042500 nM
MLS000051428IC5042500 nM
SMR000074755IC5042500 nM
2-(4-quinazolinylamino)hexanoic acidIC5042500 nM
1,1,4,4-tetraketo-N,6-diphenyl-2,3-dihydro-1,4-dithiin-5-carboxamideEC5043900 nM
2N-(3,3-aminoiminopropyl)-4-[4-(4-formamido-1-methyl-1H-2-pyrrolylcarboxamido)-1-methyl-1H-2-pyrrolylcarboxamido]-1-methyl-1H-2-pyrrolecarboxamideIC5047000 nM
3-[[8,9-dimethoxy-2-(3-pyridyl)-[1,2,4]triazolo[1,5-c]quinazolin-5-yl]amino]propyl-diethyl-amineIC5049900 nM
MLS000050598IC5053000 nM
4-[4-(4-methoxyphenyl)piperazin-1-yl]carbonyl-2,9-dimethyl-pyrido[3,4-b]indol-1-oneIC5053000 nM
2-[(2,5-dichlorophenyl)hydrazinylidene]-2-(2,6-dimethyl-4-morpholinyl)acetic acid ethyl esterIC5053000 nM
(E)-3-[2-[N-acetyl-3-(trifluoromethyl)anilino]-1,3-thiazol-4-yl]prop-2-enoic acidIC5053000 nM
Acid, 24IC5053000 nM
(E)-3-(1-benzyl-3-pyridin-3-ylpyrazol-4-yl)prop-2-enoic acidIC5053000 nM
1-benzyl-N-(2-fluorobenzyl)-3,5-dimethyl-pyrazole-4-carboxamideIC5053000 nM
2-[(2-chlorophenyl)hydrazo]-2-(2-oxolanylmethylimino)acetic acid ethyl esterIC5053000 nM
3-[1,3-bis(oxidanylidene)isoindol-2-yl]-N-(4,5-dihydro-1,3-thiazol-2-yl)benzamideIC5053000 nM
3-cyclopentylpropanoic acid [2-[[(tert-butylamino)-oxomethyl]amino]-2-oxoethyl] esterIC5053000 nM
6-diazanyl-N,N-di(propan-2-yl)pyridine-3-sulfonamideIC5053000 nM
2-[1-[(4-methyl-1,3-thiazol-2-yl)sulfanyl]ethyl]-5-phenyl-3H-thieno[2,3-d]pyrimidin-4-oneIC5053000 nM
(E)-1-[4-(4-hydroxyphenyl)-1-piperazinyl]-3-thiophen-2-yl-2-propen-1-oneIC5053000 nM
4-(2-furanylmethylsulfamoyl)-N-methyl-N-(thiophen-2-ylmethyl)benzamideIC5053000 nM
2-[4-(4-methylphenyl)-2-(2-pyridinyl)-5-thiazolyl]acetic acidIC5053000 nM
3-[(4-chlorophenyl)sulfonylamino]propanoic acid [2-(4-methoxyanilino)-2-oxoethyl] esterIC5053000 nM
2-[(veratroylhydrazono)methyl]benzoic acidIC5053000 nM
MLS000761278IC5053000 nM
4-ethoxy-N-[(6-fluoro-1,1-diketo-2,3-dihydrothiochromen-4-ylidene)amino]benzenesulfonamideIC5053000 nM
2-[ethyl-[(4-keto-1H-quinazolin-2-yl)methyl]amino]-N-[2-(4-fluorophenyl)ethyl]acetamideIC5053000 nM
2-[[4-(4-methoxyphenyl)-1,2,4-triazol-3-yl]sulfanyl]-N-(5-methyl-1,2-oxazol-3-yl)acetamideIC5053000 nM
Glycopeptide, 2IC5053000 nM
4-[7-[4-[diethyl(methyl)ammonio]butoxy]-9-keto-fluoren-2-yl]oxybutyl-diethyl-methyl-ammonium;iodideIC5053000 nM
2-(aminocarbonylamino)-N-[4-[(4-methoxyphenyl)sulfamoyl]phenyl]-4-methylsulfanyl-butanamideIC5053000 nM

ChEMBL bioactivities

68 potent at pChembl≥5 of 178 total, top 50 by pChembl (potency: 10 = 0.1 nM, 6 = 1 µM).

pChemblTypeValueUnitMolecule
8.03Kd9.24nMCHEMBL6174717
7.46IC5035nMCHEMBL6174717
7.40Kd40.12nMCHEMBL6162630
7.25Kd56.71nMCHEMBL6134638
6.89Kd128.3nMCHEMBL6149072
6.84Kd145.1nMCHEMBL6147824
6.63Kd236.5nMCHEMBL6152887
6.60IC50250nMCHEMBL2316725
6.45Kd355nMCHEMBL5527941
6.44Ki366nMCHEMBL5527941
6.44Kd365.5nMCHEMBL5527941
6.43IC50370nMCHEMBL2316724
6.22Kd602.4nMCHEMBL6176383
6.14IC50720nMCHEMBL6175342
6.12IC50750nMCHEMBL133930
6.12Ki750nMCHEMBL1215819
6.09IC50810nMCHEMBL2316723
6.05IC50900nMCHEMBL133930
6.03IC50930nMCHEMBL2316722
6.02EC50950nMCHEMBL4516566
5.98IC501050nMCHEMBL1215819
5.89Kd1300nMCHEMBL3427781
5.89IC501300nMCHEMBL5280045
5.85IC501400nMCHEMBL2316721
5.85Kd1400nMCHEMBL6175342
5.82IC501500nMCHEMBL1215819
5.75Ki1800nMCHEMBL1215817
5.70EC502000nMCHEMBL4468829
5.70IC502000nMCHEMBL1215817
5.68IC502100nMCHEMBL1215810
5.67IC502140nMCHEMBL2316720
5.64IC502300nMCHEMBL5287027
5.60IC502500nMCHEMBL1215817
5.58IC502600nMCHEMBL1215818
5.57IC502700nMCHEMBL1215815
5.52Kd3000nMCHEMBL3427780
5.52IC503000nMCHEMBL3823105
5.52IC503000nMCHEMBL5277728
5.51IC503100nMCHEMBL2316738
5.46IC503500nMCHEMBL1215811
5.42IC503800nMCHEMBL5287027
5.40EC504000nMCHEMBL5561822
5.38Ki4200nMCHEMBL1215818
5.37IC504300nMCHEMBL6168507
5.31IC504900nMCHEMBL5280045
5.30IC505000nMCHEMBL1215818
5.28IC505290nMCHEMBL2316739
5.25Kd5600nMCHEMBL1567670
5.22IC506000nMCHEMBL1567670
5.22IC506000nMCHEMBL1215813

PubChem BioAssay actives

56 with measured affinity, of 541 total; 39 most potent distinct compounds. Largely complementary to BindingDB; screening values are coarse (µM, 4 dp), so sub-nM hits tie at the floor.

CompoundAssayTypeValueUnit
1-(3,4-dichlorophenyl)-3-iodo-4-morpholin-4-ylpyrrole-2,5-dione724821: Inhibition of human RAD51 binding to single stranded DNA by fluorescence polarization assayic500.2500uM
N-[2-[(2S,4R)-2-[[(1S)-1-(2-chloro-4-methoxyphenyl)ethyl]carbamoyl]-4-hydroxypyrrolidin-1-yl]-2-oxoethyl]-6-fluoroquinoline-2-carboxamide2066591: Binding affinity to RAD51 (unknown origin) assessed as dissociation constant by fluorescence polarization assaykd0.3550uM
3-bromo-1-(3,4-dichlorophenyl)-4-morpholin-4-ylpyrrole-2,5-dione724821: Inhibition of human RAD51 binding to single stranded DNA by fluorescence polarization assayic500.3700uM
(4S)-4-[[(2S)-6-amino-2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-6-amino-2-[[2-[[(2S)-2-[[(2S)-2-[[(2S,3R)-2-[[(2S)-2-[[(2S)-2-[(2-aminoacetyl)amino]-3-phenylpropanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-3-hydroxybutanoyl]amino]propanoyl]amino]-3-hydroxypropanoyl]amino]acetyl]amino]hexanoyl]amino]hexanoyl]amino]-3-methylbutanoyl]amino]hexanoyl]amino]-3-methylpentanoyl]amino]-3-hydroxypropanoyl]amino]hexanoyl]amino]-5-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-6-amino-1-[[(2S)-1-[[(2S)-6-amino-1-[[(2S)-4-amino-1-[[(2S)-1-[[(1S)-1-carboxy-2-phenylethyl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-1,4-dioxobutan-2-yl]amino]-1-oxohexan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-1-oxohexan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-5-oxopentanoic acid499540: Inhibition of human RAD51 assessed as concentration required for half dissociation of protein/single-stranded DNA complex formation by fluorescence polarimetryki0.7500uM
disodium;5-isothiocyanato-2-[(E)-2-(4-isothiocyanato-2-sulfonatophenyl)ethenyl]benzenesulfonate1954698: Inhibition of RAD51 (unknown origin) assessed as reduction in novel 58/33-dsDNA formation incubated for 1 hr by electrophoresis based DNA strand exchange assayic500.7500uM
3-chloro-1-(3,4-dichlorophenyl)-4-[4-(trifluoromethyl)phenyl]pyrrole-2,5-dione724821: Inhibition of human RAD51 binding to single stranded DNA by fluorescence polarization assayic500.8100uM
3-chloro-1-(3,4-dichlorophenyl)-4-phenylpyrrole-2,5-dione724821: Inhibition of human RAD51 binding to single stranded DNA by fluorescence polarization assayic500.9300uM
3-[2-acetyl-3-(1-propylindazol-5-yl)-3,4-dihydropyrazol-5-yl]-6-chloro-4-phenyl-1H-quinolin-2-one1605279: Inhibition of biotinylated BRC4 peptide binding to His-tagged human RAD51 expressed in Escherichia coli Rosetta(DE3) pLysS cells assessed as BRC4-RAD51 protein -protein interaction by competitive ELISAec500.9500uM
4-bromo-5-chloro-N-[2-(1H-indol-3-yl)ethyl]thiophene-2-sulfonamide1207141: Binding affinity to RAD51 (unknown origin) by isothermal calorimetrykd1.3000uM
disodium;5-cyano-2-[(E)-2-(4-cyano-2-sulfonatophenyl)ethenyl]benzenesulfonate1954698: Inhibition of RAD51 (unknown origin) assessed as reduction in novel 58/33-dsDNA formation incubated for 1 hr by electrophoresis based DNA strand exchange assayic501.3000uM
3-(4-aminophenyl)-4-chloro-1-(3,4-dichlorophenyl)pyrrole-2,5-dione724821: Inhibition of human RAD51 binding to single stranded DNA by fluorescence polarization assayic501.4000uM
(4S)-4-[[(2S)-6-amino-2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-6-amino-2-[[2-[[(2S)-2-[[(2S)-2-[[(2S,3R)-2-[[(2S)-2-[[(2S)-2-[(2-aminoacetyl)amino]-3-phenylpropanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]amino]-3-hydroxybutanoyl]amino]propanoyl]amino]-3-hydroxypropanoyl]amino]acetyl]amino]hexanoyl]amino]hexanoyl]amino]-3-methylbutanoyl]amino]hexanoyl]amino]-3-methylpentanoyl]amino]-3-hydroxypropanoyl]amino]hexanoyl]amino]-5-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-6-amino-1-[[(2S)-1-[[(2S)-6-amino-1-[[(2S)-4-amino-1-[[(2S)-1-[[(1S)-1-carboxy-2-phenylethyl]amino]-4-methyl-1-oxopentan-2-yl]amino]-1,4-dioxobutan-2-yl]amino]-1-oxohexan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-1-oxohexan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-5-oxopentanoic acid499540: Inhibition of human RAD51 assessed as concentration required for half dissociation of protein/single-stranded DNA complex formation by fluorescence polarimetryki1.8000uM
4-[5-(6-chloro-2-oxo-4-phenyl-1H-quinolin-3-yl)-3-(1-methylindol-5-yl)-3,4-dihydropyrazol-2-yl]-4-oxobutanoic acid1605279: Inhibition of biotinylated BRC4 peptide binding to His-tagged human RAD51 expressed in Escherichia coli Rosetta(DE3) pLysS cells assessed as BRC4-RAD51 protein -protein interaction by competitive ELISAec502.0000uM
(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-4-amino-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-6-amino-2-[[2-[[(2S)-2-[[(2S)-2-[[(2S,3R)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-[[(2S)-2-amino-4-methylpentanoyl]amino]-4-methylpentanoyl]amino]acetyl]amino]-3-phenylpropanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]amino]-3-hydroxybutanoyl]amino]propanoyl]amino]-3-hydroxypropanoyl]amino]acetyl]amino]hexanoyl]amino]hexanoyl]amino]-3-methylbutanoyl]amino]hexanoyl]amino]-3-methylpentanoyl]amino]propanoyl]amino]hexanoyl]amino]-4-carboxybutanoyl]amino]-3-hydroxypropanoyl]amino]-4-methylpentanoyl]amino]-3-carboxypropanoyl]amino]hexanoyl]amino]-3-methylbutanoyl]amino]hexanoyl]amino]-4-oxobutanoyl]amino]-4-methylpentanoyl]amino]-3-phenylpropanoyl]amino]-3-carboxypropanoyl]amino]pentanedioic acid499542: Inhibition of human RAD51 assessed as dissociation of protein/single-stranded DNA complex formation by fluorescence polarimetryic502.1000uM
3-chloro-1-(3,4-dichlorophenyl)-4-(3,4-dimethoxyphenyl)pyrrole-2,5-dione724821: Inhibition of human RAD51 binding to single stranded DNA by fluorescence polarization assayic502.1400uM
disodium;5-(phenoxycarbonylamino)-2-[(E)-2-[4-(phenoxycarbonylamino)-2-sulfonatophenyl]ethenyl]benzenesulfonate1954699: Inhibition of RAD51 (unknown origin) using labeled 100-ss DNA as substrate assessed as reduction in DNA D-loop formation by [gamma-32P]ATP based scintillation counter methodic502.3000uM
(4S)-4-[[(2S)-6-amino-2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-6-amino-2-[[2-[[(2S)-2-[[(2S)-2-[[(2S,3R)-2-[[(2S)-2-[[(2S)-2-[(2-aminoacetyl)amino]-3-phenylpropanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]amino]-3-hydroxybutanoyl]amino]propanoyl]amino]-3-hydroxypropanoyl]amino]acetyl]amino]hexanoyl]amino]hexanoyl]amino]-3-methylbutanoyl]amino]hexanoyl]amino]-3-methylpentanoyl]amino]propanoyl]amino]hexanoyl]amino]-5-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-6-amino-1-[[(2S)-1-[[(2S)-6-amino-1-[[(2S)-4-amino-1-[[(2S)-1-[[(1S)-1-carboxy-2-phenylethyl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-1,4-dioxobutan-2-yl]amino]-1-oxohexan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-1-oxohexan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-5-oxopentanoic acid499544: Inhibition of human RAD51 assessed as dissociation of protein/single-stranded oligo(AGT)12 complex formation by fluorescence polarimetryic502.6000uM
(4S)-4-[[(2S)-6-amino-2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-6-amino-2-[[2-[[(2S)-2-[[(2S)-2-[[(2S,3R)-2-[[(2S)-2-[[(2S)-2-[(2-aminoacetyl)amino]-3-phenylpropanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-3-hydroxybutanoyl]amino]propanoyl]amino]-3-hydroxypropanoyl]amino]acetyl]amino]hexanoyl]amino]hexanoyl]amino]-3-methylbutanoyl]amino]hexanoyl]amino]-3-methylpentanoyl]amino]propanoyl]amino]hexanoyl]amino]-5-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-6-amino-1-[[(2S)-1-[[(2S)-6-amino-1-[[(2S)-4-amino-1-[[(2S)-1-[[(1S)-1-carboxy-2-phenylethyl]amino]-4-methyl-1-oxopentan-2-yl]amino]-1,4-dioxobutan-2-yl]amino]-1-oxohexan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-1-oxohexan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-5-oxopentanoic acid499544: Inhibition of human RAD51 assessed as dissociation of protein/single-stranded oligo(AGT)12 complex formation by fluorescence polarimetryic502.7000uM
2-phenylethyl (2S)-2-benzamido-3-(1H-indol-3-yl)propanoate1207141: Binding affinity to RAD51 (unknown origin) by isothermal calorimetrykd3.0000uM
N-ethyl-4-pyrrolo[1,2-a]quinoxalin-4-ylaniline1309725: Inhibition of RAD51-mediated homologous recombination in human HEK293-DR-GFP cells transfected with pCBASce expressing I-Sce-I after 24 hrs following transfection by 7-aminoactinomycin D staining based flow cytometryic503.0000uM
disodium;5-[(4-methoxybenzoyl)amino]-2-[(E)-2-[4-[(4-methoxybenzoyl)amino]-2-sulfonatophenyl]ethenyl]benzenesulfonate1954698: Inhibition of RAD51 (unknown origin) assessed as reduction in novel 58/33-dsDNA formation incubated for 1 hr by electrophoresis based DNA strand exchange assayic503.0000uM
1-(4-bromo-3-chlorophenyl)-3-chloro-4-morpholin-4-ylpyrrole-2,5-dione724821: Inhibition of human RAD51 binding to single stranded DNA by fluorescence polarization assayic503.1000uM
(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-4-amino-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-6-amino-2-[[2-[[(2S)-2-[[(2S)-2-[[(2S,3R)-2-[[(2S)-2-[[(2S)-2-[(2-aminoacetyl)amino]-3-phenylpropanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]amino]-3-hydroxybutanoyl]amino]propanoyl]amino]-3-hydroxypropanoyl]amino]acetyl]amino]hexanoyl]amino]hexanoyl]amino]-3-methylbutanoyl]amino]hexanoyl]amino]-3-methylpentanoyl]amino]propanoyl]amino]hexanoyl]amino]-4-carboxybutanoyl]amino]-3-hydroxypropanoyl]amino]-4-methylpentanoyl]amino]-3-carboxypropanoyl]amino]hexanoyl]amino]-3-methylbutanoyl]amino]hexanoyl]amino]-4-oxobutanoyl]amino]-4-methylpentanoyl]amino]-3-phenylpropanoyl]amino]-3-carboxypropanoyl]amino]pentanedioic acid499542: Inhibition of human RAD51 assessed as dissociation of protein/single-stranded DNA complex formation by fluorescence polarimetryic503.5000uM
3-benzyl-5-(trifluoromethyl)-6H-triazolo[4,5-d]pyrimidin-7-one2080013: Displacement of BRC4-biotinylated peptide from human RAD51 by competitive ELISAec504.0000uM
3-chloro-1-(3,4-dichlorophenyl)-4-(4-methoxyphenyl)pyrrole-2,5-dione724821: Inhibition of human RAD51 binding to single stranded DNA by fluorescence polarization assayic505.2900uM
3-benzyl-2-[(E)-2-pyridin-3-ylethenyl]quinazolin-4-one664765: Binding affinity to human RAD51 in absence of ATP by SPR methodkd5.6000uM
(4S)-4-[[(2S)-6-amino-2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-6-amino-2-[[2-[[(2S)-2-[[(2S)-2-[[(2S,3R)-2-[[(2S)-2-[[(2S)-2-[(2-aminoacetyl)amino]-3-phenylpropanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]amino]-3-hydroxybutanoyl]amino]propanoyl]amino]-3-hydroxypropanoyl]amino]acetyl]amino]hexanoyl]amino]hexanoyl]amino]-3-methylbutanoyl]amino]hexanoyl]amino]-3-methylpentanoyl]amino]propanoyl]amino]hexanoyl]amino]-5-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-6-amino-1-[[(2S)-1-[[(2S)-6-amino-1-[[(2S)-4-amino-1-[[(2S)-1-[[(1S)-1-carboxy-2-phenylethyl]amino]-4-methyl-1-oxopentan-2-yl]amino]-1,4-dioxobutan-2-yl]amino]-1-oxohexan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-1-oxohexan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-5-oxopentanoic acid499544: Inhibition of human RAD51 assessed as dissociation of protein/single-stranded oligo(AGT)12 complex formation by fluorescence polarimetryic506.0000uM
3-chloro-1-(3,4-dichlorophenyl)-4-(4-methylpiperazin-1-yl)pyrrole-2,5-dione724821: Inhibition of human RAD51 binding to single stranded DNA by fluorescence polarization assayic506.4300uM
3-chloro-1-(3,4-dichlorophenyl)-4-morpholin-4-ylpyrrole-2,5-dione724821: Inhibition of human RAD51 binding to single stranded DNA by fluorescence polarization assayic506.8200uM
3-chloro-1-(4-chloro-3-fluorophenyl)-4-morpholin-4-ylpyrrole-2,5-dione724821: Inhibition of human RAD51 binding to single stranded DNA by fluorescence polarization assayic507.9100uM
6-chloro-3-[3-(4-chlorophenyl)-2-propanoyl-3,4-dihydropyrazol-5-yl]-4-phenyl-1H-quinolin-2-one1605279: Inhibition of biotinylated BRC4 peptide binding to His-tagged human RAD51 expressed in Escherichia coli Rosetta(DE3) pLysS cells assessed as BRC4-RAD51 protein -protein interaction by competitive ELISAec508.0000uM
N-cyclohexyl-2-[[5-[(2-oxo-1,3-benzothiazol-3-yl)methyl]-4-(3-phenylpropyl)-1,2,4-triazol-3-yl]sulfanyl]acetamide1638125: Displacement of N-terminal biotinylated-BRC4 from recombinant human Rad51 expressed in Escherichia coli by ELISAec508.0000uM
3-chloro-1-(3-chloro-4-fluorophenyl)-4-morpholin-4-ylpyrrole-2,5-dione724821: Inhibition of human RAD51 binding to single stranded DNA by fluorescence polarization assayic508.3200uM
4-(4-aminophenyl)pyrrolo[1,2-a]quinoxalin-7-ol1309721: Inhibition of human N-terminal 6-histidine/Avi-tagged recombinant RAD51 expressed in Escherichia coli BL21(DE3) assessed as D-loop formation using 5’-32P-labeled 90-mer ssDNA as substrate preincubated for 10 mins followed by substrate addition with subsequent incubation with substrate for 5 mins measured after 20 mins in presence of supercoiled pRS306 dsDNA by agarose gel electrophoresisic508.4000uM
4-[4-(dimethylamino)phenyl]pyrrolo[1,2-a]quinoxalin-7-ol1309721: Inhibition of human N-terminal 6-histidine/Avi-tagged recombinant RAD51 expressed in Escherichia coli BL21(DE3) assessed as D-loop formation using 5’-32P-labeled 90-mer ssDNA as substrate preincubated for 10 mins followed by substrate addition with subsequent incubation with substrate for 5 mins measured after 20 mins in presence of supercoiled pRS306 dsDNA by agarose gel electrophoresisic509.8000uM
1-(3-bromo-4-chlorophenyl)-3-chloro-4-morpholin-4-ylpyrrole-2,5-dione724821: Inhibition of human RAD51 binding to single stranded DNA by fluorescence polarization assayic509.9400uM
4-[5-(6-chloro-2-oxo-4-phenyl-1H-quinolin-3-yl)-3-(1-ethylindol-5-yl)-3,4-dihydropyrazol-2-yl]-4-oxobutanoic acid1605279: Inhibition of biotinylated BRC4 peptide binding to His-tagged human RAD51 expressed in Escherichia coli Rosetta(DE3) pLysS cells assessed as BRC4-RAD51 protein -protein interaction by competitive ELISAec5010.0000uM
3-[2-acetyl-3-(4-chlorophenyl)-3,4-dihydropyrazol-5-yl]-6-chloro-4-phenyl-1H-quinolin-2-one1605279: Inhibition of biotinylated BRC4 peptide binding to His-tagged human RAD51 expressed in Escherichia coli Rosetta(DE3) pLysS cells assessed as BRC4-RAD51 protein -protein interaction by competitive ELISAec5010.0000uM
disodium;5-azido-2-[(E)-2-(4-azido-2-sulfonatophenyl)ethenyl]benzenesulfonate1954698: Inhibition of RAD51 (unknown origin) assessed as reduction in novel 58/33-dsDNA formation incubated for 1 hr by electrophoresis based DNA strand exchange assayic5010.0000uM

CTD chemical–gene interactions

151 total (human), top 30 by PubMed support.

ChemicalActions (top 5)PubMed papers
Cisplatindecreases expression, decreases reaction, increases expression, affects reaction, affects cotreatment (+1 more)7
chromium hexavalent ionaffects expression, affects phosphorylation, decreases expression, decreases localization, affects localization (+2 more)5
sodium arsenitedecreases expression, increases expression4
zinc chromateaffects reaction, increases abundance, affects expression, affects phosphorylation, decreases expression (+2 more)4
Benzo(a)pyreneaffects methylation, decreases expression, increases expression, affects cotreatment4
Doxorubicinaffects expression, decreases expression, increases expression, increases reaction, affects reaction (+1 more)4
Oxygendecreases expression4
Tobacco Smoke Pollutionaffects expression, decreases expression, increases expression4
4-biphenylaminedecreases expression, decreases reaction3
bisphenol Adecreases expression, increases expression3
Resveratrolaffects cotreatment, increases expression, decreases expression3
lasiocarpinedecreases expression, increases expression2
potassium chromate(VI)affects cotreatment, decreases expression2
SB 203580decreases expression, decreases reaction2
N-(oxo-5,6-dihydrophenanthridin-2-yl)-N,N-dimethylacetamide hydrochloridedecreases expression2
(+)-JQ1 compounddecreases reaction, increases response to substance, increases cleavage, decreases expression, affects binding (+2 more)2
Leflunomidedecreases expression2
Arsenicaffects methylation, decreases methylation, increases abundance2
Camptothecindecreases expression2
Estradiolincreases expression2
Mustard Gasaffects localization, decreases reaction, decreases expression, decreases response to substance2
Testosteronedecreases expression, increases expression, affects cotreatment2
Aflatoxin B1increases expression, affects cotreatment, increases response to substance2
Sodium Selenitedecreases expression2
Cadmium Chloridedecreases expression, increases expression2
Particulate Matterdecreases expression, increases abundance2
tetrachlorobenzoquinonedecreases reaction, decreases response to substance, affects expression, increases reaction, decreases expression (+3 more)1
GSK-J4decreases expression1
afuresertibdecreases expression1
INCB054329decreases expression, affects cotreatment1

ChEMBL screening assays

124 unique, capped per target: 116 binding, 8 admet

Representative assays (with source publication via chembl_document):

Assay IDTypeDescriptionSource paper
CHEMBL1219278BindingInhibition of human RAD51 assessed as concentration required for half dissociation of protein/single-stranded DNA complex formation by fluorescence polarimetryDesign of potent inhibitors of human RAD51 recombinase based on BRC motifs of BRCA2 protein: modeling and experimental validation of a chimera peptide. — J Med Chem
CHEMBL3824500ADMETInhibition of Escherichia coli BL21(DE3) expressing human N-terminal 6-histidine/Avi-tagged RAD51 binding to 5’-Alexa488-oligo-dT45 ssDNA preincubated for 40 mins followed by substrate addition measured after 40 mins by fluorescence polarizDevelopment of Small Molecules that Specifically Inhibit the D-loop Activity of RAD51. — J Med Chem

Cellosaurus cell lines

1 cell lines: 1 cancer cell line

First 10 cell lines (id-ordered, not curated):

CellosaurusNameCategorySex
CVCL_9U92Delta-Rad51+hRad51-DT40Cancer cell lineFemale

Clinical trials (associated diseases)

385 trials via MONDO — disease-level, not drug-specific.

TrialPhaseStatusTitle
NCT00190697PHASE4COMPLETEDA Study of LY353381 (Arzoxifene) for Patients Who Benefitted From This Drug in Other Oncology Trials and Wished to Continue Treatment
NCT00277160PHASE4COMPLETEDA Study of Primary Prophylaxis With Neulasta (Pegfilgrastim) Versus Secondary Prophylaxis After Chemotherapy in Elderly Subjects (>/= 65 Years Old) With Cancer
NCT00727961PHASE4COMPLETEDA Study to Evaluate Efficacy and Tolerance of Caelyx in Patients With Epithelial Ovarian Cancer. (Study P04072)(COMPLETED)
NCT00740116PHASE4COMPLETEDTranexamic Acid in Surgery of Advanced Ovarian Cancer
NCT00817479PHASE4COMPLETEDTumor Gene Expression in Women With Ovarian Cancer
NCT01432015PHASE4COMPLETEDFosaprepitant Versus Aprepitant in the Prevention of Chemotherapy Induced Nausea and Vomiting
NCT01706120PHASE4UNKNOWNStudy of Clinical and Biological Prognostic Factors in Patients With Ovarian Cancer Receiving Carboplatin +Paclitaxel With Bevacizumab
NCT01932125PHASE4COMPLETEDAn Interventional Study of Avastin (Bevacizumab) in Patients With Advanced/Metastatic Epithelial Ovarian Cancer, Fallopian Tube Cancer or Primary Peritoneal Cancer
NCT01953107PHASE4COMPLETEDOral Iron vs. Placebo in Newly Diagnosed Gynecologic Oncology Patients Who Are Surgical Candidates.
NCT02035345PHASE4TERMINATEDSlowed Carboplatin Infusion for Ovarian Cancer Patients Receiving Carboplatin Re-Treatment
NCT02243059PHASE4WITHDRAWNMagnetic Resonance Imaging for Lymph Node Staging in Ovarian Cancer
NCT03164980PHASE4TERMINATEDQoL-Comparison Between Trabectedin/PLD and Pt-based Therapy in Patients With Pt-sensitive Recurrent Ovarian Cancer
NCT03384511PHASE4COMPLETEDThe Use of 18F-ALF-NOTA-PRGD2 PET/CT Scan to Predict the Efficacy and Adverse Events of Apatinib in Malignancies.
NCT03543462PHASE4COMPLETEDDiaphragmatic Resection And Gynecological Ovarian Neoplasm
NCT03752216PHASE4COMPLETEDNIraparib and Quality of LifE is a Longitudinal Study Evaluating in Real Life the Tolerability of Niraparib.
NCT03858166PHASE4TERMINATEDEfficacy and Safety of PEG-rhG-CSF Secondary Prophylaxis vs. Therapeutic Administration in Patients With Ovarian Cancer
NCT04024254PHASE4COMPLETEDA Study of Serum Folate Levels in Patients Treated With Olaparib
NCT04330040PHASE4COMPLETEDProspective Multicentre Phase-IV Clinical Trial of Olaparib in Indian Patients With Ovarian and Metastatic Breast Cancer
NCT04352439PHASE4COMPLETEDAspirin for Prevention of Venous Thromboembolism Among Ovarian Cancer Patients Receiving Neoadjuvant Chemotherapy
NCT05187208PHASE4UNKNOWNPARP Inhibitor Oral Maintenance in Low-Risk Ovarian Cancer
NCT05606692PHASE4RECRUITINGInfluences of Propofol and Sevoflurane Anesthesia in Ovarian Cancer (Anesthetics)
NCT05926336PHASE4RECRUITINGThe Effects of Using Different Anesthetics on the Prognosis of Primary Tumors and Its Mechanism of Action
NCT06412120PHASE4RECRUITINGStudy Evaluating Safety, Tolerability, and Metabolism of Niraparib
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