Atlas of Genetics and Cytogenetics in Oncology and Haematology


Home   Genes   Leukemias   Solid Tumours   Cancer-Prone   Deep Insight   Case Reports   Journals  Portal   Teaching   

X Y 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 NA

RAD51D (RAD51-like 3 (S. cerevisiae))

Identity

Other namesRAD51L3
HsTRAD
R51H3
RAD51D
Trad
HGNC (Hugo) RAD51D
LocusID (NCBI) 5892
Location 17q12
Location_base_pair Starts at 33426811 and ends at 33446888 bp from pter ( according to hg19-Feb_2009)
Note Of the five RAD51 paralog proteins, four come together to form the BCDX2 complex, which includes RAD51L1 (RAD51B; chromosome 14), RAD51L2 (RAD51C; chromosome 17), RAD51L3 (RAD51D; chromosome 17), and XRCC2 (chromosome 14). The protein complex is involved in homologous recombination repair of double-stranded breaks that result during DNA replication or from DNA-damaging agents, e.g., cisplatin (Masson et al., 2001).
The RAD51L3 protein directly interacts with RAD51L2 (RAD51C) and XRCC2. It does not directly interact with RAD51L1 (RAD51B) (Schild et al., 2000).

DNA/RNA

Note The human gene is composed of 10 exons. The study by Kawabata and Saeki (1999) describes alternative splicing of the human gene using a numbering scheme of 12 alternatively spliced exons. The exon alignment is illustrated below.
Further descriptions of mouse alternatively spliced variants are described in Gruver et al., 2009 and Kawabata et al., 2004.
 
  Human RAD51D alternative splicing. A. Exons 4 and 8 of the Kawabata and Saeki numbering scheme are considered "alternative exons" and not included in the reference sequence. B. Summary of splice variants and predicted translation products (for further details see the annexed document below).
Note [Annexed document]
  Annexe. RAD51L3 transcripts description.
Transcription The HsTRAD transcript is the predominant variant. It is the full-length transcript and is made up of 2418 base pairs. This transcript will be used as the reference for the information that follows. There are multiple splice variants for the RAD51L3 gene that translate into one of seven putative protein isoforms.

Protein

Note The Saccharomyces cerevisiae Rad51 protein is homologous to the RecA protein of Escherichia coli. The RecA protein is known to promote repair via ATP-dependent mechanisms and is responsible for pairing and strand transfer between homologous DNA sequences. This is similar to the actions of the RAD51 protein in repair pathways. There are 5 members of the RAD51 family that share similar roles in recombination and DNA repair. RAD51D is one of these RecA-like genes (Pittman et al., 1998; Cartwright et al., 1998).
The RAD51D gene is predicted to encode seven different protein isoforms through alternative splicing. Isoform 1 is the predominant protein and is translated from the HsTRAD transcript mentioned previously (Kawabata and Saeki, 1999). The diagram below is based on this predominant form.
 
  RAD51L3 protein structure. Isoform 1 (from full-length transcript).
Description The RAD51D protein contains regions necessary for interactions with other RAD51 paralogs as well as those that are required for proper function of the protein. RAD51D contains an ATP binding domain with highly conserved Walker A and B motifs (Pittman et al., 1998; Cartwright et al., 1998). Mutations targeting the conserved residues of glycine and lysine within the Walker A motif region resulted in a reduction in RAD51C binding ability and were shown to be required for DNA repair (Gruver et al., 2005). The Walker B motif contains a "GGQRE" sequence between residues 219-223 that is also required for DNA repair (Wiese et al., 2006). Furthermore, RAD51D-XRCC2 complex formation is significantly reduced with mutations targeting a highly conserved aspartate residue within the Walker B motif (Wiese et al., 2006).
A carboxyl terminal domain spanning amino acids 77-329 has been identified to be required for RAD51D to interact with RAD51C. In addition, the "linker region" located between residues 54-77 in the amino terminus is required for proper interactions with XRCC2. Together, these interactions aid in the repair of DNA damage (Miller et al., 2004; Gruver et al., 2009).
Expression According to the study by Kawabata and Saeki (1999), RAD51L3 transcripts are expressed to varying degrees in the colon, prostate, spleen, testis, ovaries, thymus, small intestine and leukocytes.
Localisation Located in the nucleus. Specifically, RAD51L3 localizes to the telomeres during both mitosis and meiosis (Tarsounas et al., 2004). There is evidence that RAD51L3 is found in the cytoplasm as well (Gruver et al., 2005).
Function RAD51D is one of five members of the RAD51 gene family that is known to participate in repair of double stranded DNA breaks via homologous recombination. Without repair, the DNA damage can result in cell death or chromosomal aberrations that can ultimately lead to cancer (Thacker, 2005). Knockout studies with mice have shown a dramatic increase in levels of chromosomal aberrations, most notably, chromatid and chromosome breaks that occur through unrepaired replication forks (Smiraldo et al., 2005; Hinz et al., 2006). Proteomic studies have identified an interaction between RAD51D with the SFPQ protein (Rajesh et al., 2011). Exposure of mouse RAD51D-deficient cells to a strong alkylating agent results in G2/M cell cycle arrest and ultimately apoptosis (Rajesh et al., 2010). RAD51D has recently been shown to play a diverse role in cellular processes through its interaction with proteins involved in cell division, embryo development, protein and carbohydrate metabolism, cellular trafficking, protein synthesis, modification or folding, and cellular structure (Rajesh et al., 2009).
RAD51L3 is directly associated with telomeres prevents their dysfunction (Tarsounas et al., 2004). In mouse studies, RAD51L3 foci were present at telomeres in both meiosis and mitosis. Knockout studies showed that "RAD51D-deficient" mice exhibited an increase in end-to-end fusion and telomere attrition (Smiraldo et al., 2005). In addition, human studies using RAD51D-deficient cells have shown repeated shortening of the telomeric DNA, leading to chromosomal instability. This suggests a role for "RAD51D" in telomere capping. Failure to provide this function can lead to chromosomal aberrations (Tarsounas and West, 2005).
Homology
Canis lupus familiaris
[Dog]
Official gene name:
RAD51-like 3 (S. cerevisiae)
Genomic location:
chromosome 9
Reference material:

no primary references found

Pan troglodytes
[Chimpanzee]
Official gene name:
RAD51-like 3 (S. cerevisiae)
Genomic location:
chromosome 17
Reference material:

no primary references found

Bos taurus
[Cow]
Official gene name:
RAD51-like 3 (S. cerevisiae)
Genomic location:
chromosome 19
Reference material:

Zimin et al., 2009

Gallus gallus
[Chicken]
Official gene name:
RAD51-like 3 (S. cerevisiae)
Genomic location:
chromosome 19
Reference material:

no primary references found

Rattus norvegicus
[Rat]
Official gene name:
RAD51-like 3 (S. cerevisiae)
Genomic location:
chromosome 10
Reference material:

Strausberg et al., 2002

Mus musculus
[Mouse]
Official gene name:
RAD51-like 3 (S. cerevisiae)
Genomic location:
chromosome 11
Reference material:
Pittman et al., 1998
Cartwright et al., 1998
Arabidopsis thaliana
[Thale cress]
Official gene name:
RAD51D (ARABIDOPSIS HOMOLOG OF RAD51D)
Genomic location:
chromosome 1
Reference material:

Durrant et al., 2007

Oryza sativa
[Rice]

Official gene name:
Os09g0104200
Genomic location:
chromosome 9
**Hypothetical protein**
Reference material:

no primary references found

Danio rerio
[Zebrafish]
Official gene name:
zgc:77165
Genomic location:
chromosome 5
Reference material:

no primary references found

** Protein alignments and protein sequences are available at the HomoloGene database.

Mutations

Note Single nucleotide polymorphisms have been identified in RAD51L3. However, only a small number of the major mutations occur in coding regions. The majority of the other mutations are present in various locations within the introns. Of the mutations affecting the gene, only one has an observed clinical association. It is observed that a mutation of the mRNA position 954 (SNP ID: rs28363284) results in an allele change to GGG (from the wild type GAG). This point mutation affects the 233rd amino acid as a glycine residue is observed in this particular mutation rather than the natural glutamic acid. This particular variation in amino acid sequence has been implicated as a precursor to breast cancer (see "Implicated In" section below). Another mutation observed in the coding region is at mRNA position 188 (SNP ID: rs1871892), resulting in a change in the sequence to TCA (from the wild type CCA). This particular substitution results in the insertion of proline at the 36th protein position rather than a serine. A third mutation observed is noted to occur at mRNA positions 810 (SNP ID: rs4796033). A mutation at this location results in a sequence of CAG (from the natural CGG). The effect of this substitution is the insertion of a glutamine residue at the 185th amino acid position rather than the arginine observed in the wild type gene. It is noted, that this particular mutation also occurs in 2 additional transcripts of the gene at the mRNA positions 750 and 414 affecting the 165th and 53rd amino acid residues respectively. Other mutations in the coding region include E237K (SNP ID: rs115031549), R252Q (SNP ID: rs28363283), A245T (SNP ID: rs28363282), A210T (SNP ID: rs80116829), E177D (SNP ID: rs55942401), and R24S (SNP ID: rs28363257).

Implicated in

Entity Cancer
Disease Cancer arises in part due to the accumulation of genetic damage. Furthermore, such damage has a greater tendency to be found in significant levels when genetic repair pathways such as DNA mismatch repair and homologous recombination (HR) are defective. Involved in the pathway of HR are numerous proteins that are known as the RAD51 paralogs (RAD51L1, RAD51L2, RAD51L3, XRCC2 and XRCC3). It is believed that the lack of genetic stability created from the loss of this pathway, HR, is significant in initiation and potentially the progression of cancer. In particular, defects in the HR pathway have been noted to be associated with breast and ovarian cancer (Thacker, 2005); however, it is plausible that such a defect could potentially lead to multiple forms of cancer due to the accumulation of genetic mutations (although it takes significant damage accumulation to lead to tumor formation). A RAD51L3 variant does have an association with increased familial breast cancer risk (Rodríguez-López et al., 2004).
  
Entity Breast cancer
Note Although conflicting data exist, the RAD51D-E233G variant allele has been identified as a potential precursor to breast cancers in women with high familial risk but do not possess a BRCA1/BRCA2 mutation (Rodríguez-López et al., 2004; Dowty et al., 2008).
Disease In an initial study that screened for possible breast cancer alleles, it was determined that the exon 8 mutation led to an increased frequency of breast cancer in a specific group of cases (familial cancer cases) versus the control group (Rodríguez-López et al., 2004). Additionally, individuals expressing the RAD51D-E233G variant have been shown to have higher proliferative indices and a less favorable clinical immunohistochemical pattern (Rodríguez-López et al., 2004). However, another study found no statistically significant evidence that this variant is associated with breast cancer risk. Yet, this study did find that it was plausible that the variable could lead to a small increase in the risk of breast cancer and that a small, yet insignificant, effect was made by the variant on the risk of breast cancer (approximately 30%) (Dowty et al., 2008).
Prognosis It has been noted that the RAD51D-E223G variant confers increased resistance to DNA damaging agents such as: mitomycin C, cisplatin, ultraviolet light, and methyl methane sulfonate, and taxol. This presents clinical implications as these are commonly utilized therapies. Furthermore, the variant has increased cellular proliferation and telomere maintenance compared to the wild-type and exhibits reduced interaction with the binding partner RAD51C but does not affect binding to XRCC2 (Nadkarni et al., 2009b).
  
Entity Bloom's syndrome
Disease Bloom's syndrome is an autosomal recessive disorder of rare occurrence. Characteristics include short stature, immunodeficiency, fertility defects, and increased risk for the development of various types of cancer. Cells associated with this disorder are noted for their genomic instability. They exhibit an increase in sister chromatid and homologous chromosome exchanges. In normal, healthy cells, BLM, a helicase of the RecQ family, interacts with the RAD51L3 portion of the RAD51L3-XRCC2 heteromeric complex. Upon joining with the complex, BLM disrupts synthetic 4-way junctions that resemble Holliday junctions suggesting an important role for the protein-protein interaction in DNA repair. The mutated form of the gene encoding for this protein, which occurs in Bloom's syndrome, results in the inability for BLM to bind to RAD51L3. Absence of normal BLM function leads to the characteristic elevation in recombination events seen in Bloom's syndrome (Braybrooke et al., 2003).
  

External links

Nomenclature
HGNC (Hugo)RAD51D   9823
Cards
AtlasRAD51L3ID347ch17q12
Entrez_Gene (NCBI)RAD51D  5892  RAD51 paralog D
GeneCards (Weizmann)RAD51D
Ensembl (Hinxton)ENSG00000185379 [Gene_View]  chr17:33426811-33446888 [Contig_View]  RAD51D [Vega]
ICGC DataPortalENSG00000185379
AceView (NCBI)RAD51D
Genatlas (Paris)RAD51D
WikiGenes5892
SOURCE (Princeton)NM_001142571 NM_002878 NM_133627 NM_133628 NM_133629 NM_133630
Genomic and cartography
GoldenPath (UCSC)RAD51D  -  17q12   chr17:33426811-33446888 -  17q11   [Description]    (hg19-Feb_2009)
EnsemblRAD51D - 17q11 [CytoView]
Mapping of homologs : NCBIRAD51D [Mapview]
OMIM602954   614291   
Gene and transcription
Genbank (Entrez)AB013341 AB016223 AB016224 AB016225 AB018360
RefSeq transcript (Entrez)NM_001142571 NM_002878 NM_133627 NM_133628 NM_133629 NM_133630
RefSeq genomic (Entrez)AC_000149 NC_000017 NC_018928 NG_031858 NT_010783 NW_001838432 NW_004929407
Consensus coding sequences : CCDS (NCBI)RAD51D
Cluster EST : UnigeneHs.631757 [ NCBI ]
CGAP (NCI)Hs.631757
Alternative Splicing : Fast-db (Paris)GSHG0013266
Alternative Splicing GalleryENSG00000185379
Gene ExpressionRAD51D [ NCBI-GEO ]     RAD51D [ SEEK ]   RAD51D [ MEM ]
Protein : pattern, domain, 3D structure
UniProt/SwissProtO75771 (Uniprot)
NextProtO75771  [Medical]
With graphics : InterProO75771
Splice isoforms : SwissVarO75771 (Swissvar)
Domaine pattern : Prosite (Expaxy)RECA_2 (PS50162)   
Domains : Interpro (EBI)AAA+_ATPase    DNA_recomb/repair_Rad51_C    DNA_recomb/repair_RecA-like    P-loop_NTPase    RecA_ATP-bd   
Related proteins : CluSTrO75771
Domain families : Pfam (Sanger)Rad51 (PF08423)   
Domain families : Pfam (NCBI)pfam08423   
Domain families : Smart (EMBL)AAA (SM00382)  
DMDM Disease mutations5892
Blocks (Seattle)O75771
PDB (SRS)2KZ3   
PDB (PDBSum)2KZ3   
PDB (IMB)2KZ3   
PDB (RSDB)2KZ3   
Human Protein AtlasENSG00000185379
Peptide AtlasO75771
HPRD04261
IPIIPI00291454   IPI00411326   IPI00216381   IPI00216382   IPI00216383   IPI00216384   IPI00216386   IPI00910911   IPI01026311   IPI00791891   IPI00795140   
Protein Interaction databases
DIP (DOE-UCLA)O75771
IntAct (EBI)O75771
FunCoupENSG00000185379
BioGRIDRAD51D
IntegromeDBRAD51D
STRING (EMBL)RAD51D
Ontologies - Pathways
QuickGOO75771
Ontology : AmiGOfour-way junction DNA binding  telomere maintenance  double-strand break repair via homologous recombination  chromosome, telomeric region  DNA binding  single-stranded DNA binding  protein binding  ATP binding  nucleus  replication fork  cytoplasm  centrosome  ATP catabolic process  ATP catabolic process  DNA repair  reciprocal meiotic recombination  DNA-dependent ATPase activity  Rad51B-Rad51C-Rad51D-XRCC2 complex  strand invasion  gamma-tubulin binding  
Ontology : EGO-EBIfour-way junction DNA binding  telomere maintenance  double-strand break repair via homologous recombination  chromosome, telomeric region  DNA binding  single-stranded DNA binding  protein binding  ATP binding  nucleus  replication fork  cytoplasm  centrosome  ATP catabolic process  ATP catabolic process  DNA repair  reciprocal meiotic recombination  DNA-dependent ATPase activity  Rad51B-Rad51C-Rad51D-XRCC2 complex  strand invasion  gamma-tubulin binding  
Pathways : KEGGHomologous recombination   
Protein Interaction DatabaseRAD51D
Wikipedia pathwaysRAD51D
Gene fusion - rearrangments
Polymorphisms : SNP, mutations, diseases
SNP Single Nucleotide Polymorphism (NCBI)RAD51D
SNP (GeneSNP Utah)RAD51D
SNP : HGBaseRAD51D
Genetic variants : HAPMAPRAD51D
1000_GenomesRAD51D 
ICGC programENSG00000185379 
CONAN: Copy Number AnalysisRAD51D 
Somatic Mutations in Cancer : COSMICRAD51D 
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
DECIPHER (Syndromes)17:33426811-33446888
Mutations and Diseases : HGMDRAD51D
OMIM602954    614291   
MedgenRAD51D
GENETestsRAD51D
Disease Genetic AssociationRAD51D
Huge Navigator RAD51D [HugePedia]  RAD51D [HugeCancerGEM]
Genomic VariantsRAD51D  RAD51D [DGVbeta]
Exome VariantRAD51D
dbVarRAD51D
ClinVarRAD51D
snp3D : Map Gene to Disease5892
General knowledge
Homologs : HomoloGeneRAD51D
Homology/Alignments : Family Browser (UCSC)RAD51D
Phylogenetic Trees/Animal Genes : TreeFamRAD51D
Chemical/Protein Interactions : CTD5892
Chemical/Pharm GKB GenePA34179
Clinical trialRAD51D
Cancer Resource (Charite)ENSG00000185379
Other databases
Probes
Litterature
PubMed43 Pubmed reference(s) in Entrez
CoreMineRAD51D
GoPubMedRAD51D
iHOPRAD51D

Bibliography

Isolation of novel human and mouse genes of the recA/RAD51 recombination-repair gene family.
Cartwright R, Dunn AM, Simpson PJ, Tambini CE, Thacker J.
Nucleic Acids Res. 1998 Apr 1;26(7):1653-9.
PMID 9512535
 
Identification, characterization, and genetic mapping of Rad51d, a new mouse and human RAD51/RecA-related gene.
Pittman DL, Weinberg LR, Schimenti JC.
Genomics. 1998 Apr 1;49(1):103-11.
PMID 9570954
 
Multiple alternative transcripts of the human homologue of the mouse TRAD/R51H3/RAD51D gene, a member of the rec A/RAD51 gene family.
Kawabata M, Saeki K.
Biochem Biophys Res Commun. 1999 Apr 2;257(1):156-62.
PMID 10092526
 
Evidence for simultaneous protein interactions between human Rad51 paralogs.
Schild D, Lio YC, Collins DW, Tsomondo T, Chen DJ.
J Biol Chem. 2000 Jun 2;275(22):16443-9.
PMID 10749867
 
Identification and purification of two distinct complexes containing the five RAD51 paralogs.
Masson JY, Tarsounas MC, Stasiak AZ, Stasiak A, Shah R, McIlwraith MJ, Benson FE, West SC.
Genes Dev. 2001 Dec 15;15(24):3296-307.
PMID 11751635
 
Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.
Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA; Mammalian Gene Collection Program Team.
Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11.
PMID 12477932
 
Functional interaction between the Bloom's syndrome helicase and the RAD51 paralog, RAD51L3 (RAD51D).
Braybrooke JP, Li JL, Wu L, Caple F, Benson FE, Hickson ID.
J Biol Chem. 2003 Nov 28;278(48):48357-66. Epub 2003 Sep 15.
PMID 12975363
 
Genomic structure and multiple alternative transcripts of the mouse TRAD/RAD51L3/RAD51D gene, a member of the recA/RAD51 gene family.
Kawabata M, Akiyama K, Kawabata T.
Biochim Biophys Acta. 2004 Aug 12;1679(2):107-16.
PMID 15297144
 
Domain mapping of the Rad51 paralog protein complexes.
Miller KA, Sawicka D, Barsky D, Albala JS.
Nucleic Acids Res. 2004 Jan 2;32(1):169-78. Print 2004.
PMID 14704354
 
The variant E233G of the RAD51D gene could be a low-penetrance allele in high-risk breast cancer families without BRCA1/2 mutations.
Rodriguez-Lopez R, Osorio A, Ribas G, Pollan M, Sanchez-Pulido L, de la Hoya M, Ruibal A, Zamora P, Arias JI, Salazar R, Vega A, Martinez JI, Esteban-Cardenosa E, Alonso C, Leton R, Urioste Azcorra M, Miner C, Armengod ME, Carracedo A, Gonzalez-Sarmiento R, Caldes T, Diez O, Benitez J.
Int J Cancer. 2004 Jul 20;110(6):845-9.
PMID 15170666
 
Recombination repair pathway in the maintenance of chromosomal integrity against DNA interstrand crosslinks.
Sasaki MS, Takata M, Sonoda E, Tachibana A, Takeda S.
Cytogenet Genome Res. 2004;104(1-4):28-34.
PMID 15162012
 
Telomere maintenance requires the RAD51D recombination/repair protein.
Tarsounas M, Munoz P, Claas A, Smiraldo PG, Pittman DL, Blasco MA, West SC.
Cell. 2004 Apr 30;117(3):337-47.
PMID 15109494
 
The ATPase motif in RAD51D is required for resistance to DNA interstrand crosslinking agents and interaction with RAD51C.
Gruver AM, Miller KA, Rajesh C, Smiraldo PG, Kaliyaperumal S, Balder R, Stiles KM, Albala JS, Pittman DL.
Mutagenesis. 2005 Nov;20(6):433-40. Epub 2005 Oct 19.
PMID 16236763
 
Extensive chromosomal instability in Rad51d-deficient mouse cells.
Smiraldo PG, Gruver AM, Osborn JC, Pittman DL.
Cancer Res. 2005 Mar 15;65(6):2089-96.
PMID 15781618
 
Recombination at mammalian telomeres: an alternative mechanism for telomere protection and elongation.
Tarsounas M, West SC.
Cell Cycle. 2005 May;4(5):672-4. Epub 2005 May 25. (REVIEW)
PMID 15846103
 
The RAD51 gene family, genetic instability and cancer.
Thacker J.
Cancer Lett. 2005 Mar 10;219(2):125-35. (REVIEW)
PMID 15723711
 
Repression of mutagenesis by Rad51D-mediated homologous recombination.
Hinz JM, Tebbs RS, Wilson PF, Nham PB, Salazar EP, Nagasawa H, Urbin SS, Bedford JS, Thompson LH.
Nucleic Acids Res. 2006 Mar 6;34(5):1358-68. Print 2006.
PMID 16522646
 
Disparate requirements for the Walker A and B ATPase motifs of human RAD51D in homologous recombination.
Wiese C, Hinz JM, Tebbs RS, Nham PB, Urbin SS, Collins DW, Thompson LH, Schild D.
Nucleic Acids Res. 2006 May 22;34(9):2833-43. Print 2006.
PMID 16717288
 
Arabidopsis SNI1 and RAD51D regulate both gene transcription and DNA recombination during the defense response.
Durrant WE, Wang S, Dong X.
Proc Natl Acad Sci U S A. 2007 Mar 6;104(10):4223-7. Epub 2007 Feb 21.
PMID 17360504
 
The RAD51D E233G variant and breast cancer risk: population-based and clinic-based family studies of Australian women.
Dowty JG, Lose F, Jenkins MA, Chang JH, Chen X, Beesley J, Dite GS, Southey MC, Byrnes GB, Tesoriero A, Giles GG, Hopper JL, Spurdle AB; kConFab Investigators; Australian Breast Cancer Family Study (ABCFS).
Breast Cancer Res Treat. 2008 Nov;112(1):35-9. Epub 2007 Dec 4.
PMID 18058226
 
Functional characterization and identification of mouse Rad51d splice variants.
Gruver AM, Yard BD, McInnes C, Rajesh C, Pittman DL.
BMC Mol Biol. 2009 Mar 27;10:27.
PMID 19327148
 
Functional characterization of the RAD51D E233G genetic variant.
Nadkarni A, Furda A, Rajesh C, McInnes C, Ruch RJ, Pittman DL.
Pharmacogenet Genomics. 2009a Feb;19(2):153-60.
PMID 19033885
 
Cisplatin resistance conferred by the RAD51D (E233G) genetic variant is dependent upon p53 status in human breast carcinoma cell lines.
Nadkarni A, Rajesh P, Ruch RJ, Pittman DL.
Mol Carcinog. 2009b Jul;48(7):586-91.
PMID 19347880
 
The interaction profile of homologous recombination repair proteins RAD51C, RAD51D and XRCC2 as determined by proteomic analysis.
Rajesh C, Gruver AM, Basrur V, Pittman DL.
Proteomics. 2009 Aug;9(16):4071-86.
PMID 19658102
 
A whole-genome assembly of the domestic cow, Bos taurus.
Zimin AV, Delcher AL, Florea L, Kelley DR, Schatz MC, Puiu D, Hanrahan F, Pertea G, Van Tassell CP, Sonstegard TS, Marcais G, Roberts M, Subramanian P, Yorke JA, Salzberg SL.
Genome Biol. 2009;10(4):R42. Epub 2009 Apr 24.
PMID 19393038
 
RAD51D protects against MLH1-dependent cytotoxic responses to O(6)-methylguanine.
Rajesh P, Rajesh C, Wyatt MD, Pittman DL.
DNA Repair (Amst). 2010 Apr 4;9(4):458-67. Epub 2010 Feb 4.
PMID 20133210
 
The splicing-factor related protein SFPQ/PSF interacts with RAD51D and is necessary for homology-directed repair and sister chromatid cohesion.
Rajesh C, Baker DK, Pierce AJ, Pittman DL.
Nucleic Acids Res. 2011 Jan 1;39(1):132-45. Epub 2010 Sep 2.
PMID 20813759
 
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

Search in all EBI   NCBI

Contributor(s)

Written12-2010Mary K Taylor, Michael K Bedenbaugh, Susan M Brown, Brian D Yard, Douglas L Pittman
South Carolina College of Pharmacy, University of South Carolina, Coker Life Sciences Building, 715 Sumter Street, Columbia, SC 29208, USA

Citation

This paper should be referenced as such :
Taylor, MK ; Bedenbaugh, MK ; Brown, SM ; Yard, BD ; Pittman, DL. RAD51L3 (RAD51-like 3 (S
cerevisiae))
Atlas Genet Cytogenet Oncol Haematol. 2011;15(8):632-636.
Free online version   Free pdf version   [Bibliographic record ]
URL : http://AtlasGeneticsOncology.org/Genes/RAD51L3ID347ch17q12.html

© Atlas of Genetics and Cytogenetics in Oncology and Haematology
indexed on : Sat Nov 8 17:03:54 CET 2014

Home   Genes   Leukemias   Solid Tumours   Cancer-Prone   Deep Insight   Case Reports   Journals  Portal   Teaching   

For comments and suggestions or contributions, please contact us

jlhuret@AtlasGeneticsOncology.org.