RAD51L3

RAD51D
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2KZ3
Identifiers
Aliases	RAD51D, BROVCA4, R51H3, RAD51L3, TRAD, RAD51 paralog D
External IDs	MGI: 1261809 HomoloGene: 2156 GeneCards: RAD51D
Gene ontology Molecular function • DNA binding • nucleotide binding • DNA-dependent ATPase activity • recombinase activity • single-stranded DNA binding • protein binding • four-way junction DNA binding • gamma-tubulin binding • double-stranded DNA binding • endodeoxyribonuclease activity • ATP binding Cellular component • cytoplasm • centrosome • replication fork • nucleoplasm • chromosome • microtubule organizing center • chromosome, telomeric region • Rad51B-Rad51C-Rad51D-XRCC2 complex • cytoskeleton • nuclear chromosome, telomeric region • nucleus Biological process • strand invasion • response to ionizing radiation • nucleotide-excision repair • reciprocal meiotic recombination • DNA recombination • interstrand cross-link repair • chromosome organization • regulation of cell cycle • cellular response to DNA damage stimulus • mitotic recombination • telomere maintenance • DNA repair • meiotic DNA recombinase assembly • DNA synthesis involved in DNA repair • double-strand break repair via homologous recombination • strand displacement Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5892	19364
Ensembl	ENSG00000185379	ENSMUSG00000018841
UniProt	O75771	O55230
RefSeq (mRNA)	NM_001142571 NM_002878 NM_133627 NM_133628 NM_133629 NM_133630	NM_001277938 NM_001277939 NM_001277941 NM_001277942 NM_011235
RefSeq (protein)	NP_001136043.1 NP_002869.3 NP_598332.1	NP_035365.1
Location (UCSC)	Chr 17: 35.09 – 35.12 Mb	Chr 11: 82.88 – 82.89 Mb
PubMed search	[1]	[2]
Wikidata

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DNA repair protein RAD51 homolog 4 is a protein that in humans is encoded by the RAD51L3 gene.^[3][4]

Function

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, which are known to be involved in the homologous recombination and repair of DNA. This protein forms a complex with several other members of the RAD51 family, including RAD51L1, RAD51L2, and XRCC2. The protein complex formed with this protein has been shown to catalyze homologous pairing between single- and double-stranded DNA, and is thought to play a role in the early stage of recombinational repair of DNA. Several alternatively spliced transcript variants of this gene have been described, but the biological validity of some of them has not been determined.^[4]

Interactions

RAD51L3 has been shown to interact with:

• Bloom syndrome protein,^[5]
• RAD51C,^[6][7] and
• XRCC2.^[5][6][8][9]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Pittman DL, Weinberg LR, Schimenti JC (June 1998). "Identification, characterization, and genetic mapping of Rad51d, a new mouse and human RAD51/RecA-related gene". Genomics. 49 (1): 103–11. doi:10.1006/geno.1998.5226. PMID 9570954.
4. "Entrez Gene: RAD51L3 RAD51-like 3 (S. cerevisiae)".
5. Braybrooke JP, Li JL, Wu L, Caple F, Benson FE, Hickson ID (November 2003). "Functional interaction between the Bloom's syndrome helicase and the RAD51 paralog, RAD51L3 (RAD51D)". J. Biol. Chem. 278 (48): 48357–66. doi:10.1074/jbc.M308838200. PMID 12975363.
6. Liu N, Schild D, Thelen MP, Thompson LH (February 2002). "Involvement of Rad51C in two distinct protein complexes of Rad51 paralogs in human cells". Nucleic Acids Res. 30 (4): 1009–15. doi:10.1093/nar/30.4.1009. PMC 100342. PMID 11842113.
7. Miller KA, Yoshikawa DM, McConnell IR, Clark R, Schild D, Albala JS (March 2002). "RAD51C interacts with RAD51B and is central to a larger protein complex in vivo exclusive of RAD51". J. Biol. Chem. 277 (10): 8406–11. doi:10.1074/jbc.M108306200. PMID 11744692.
8. Schild D, Lio YC, Collins DW, Tsomondo T, Chen DJ (June 2000). "Evidence for simultaneous protein interactions between human Rad51 paralogs". J. Biol. Chem. 275 (22): 16443–9. doi:10.1074/jbc.M001473200. PMID 10749867.
9. Hussain S, Wilson JB, Medhurst AL, Hejna J, Witt E, Ananth S, Davies A, Masson JY, Moses R, West SC, de Winter JP, Ashworth A, Jones NJ, Mathew CG (June 2004). "Direct interaction of FANCD2 with BRCA2 in DNA damage response pathways". Hum. Mol. Genet. 13 (12): 1241–8. doi:10.1093/hmg/ddh135. PMID 15115758.

Further reading

• Cartwright R, Dunn AM, Simpson PJ, Tambini CE, Thacker J (1998). "Isolation of novel human and mouse genes of the recA/RAD51 recombination-repair gene family". Nucleic Acids Res. 26 (7): 1653–9. doi:10.1093/nar/26.7.1653. PMC 147465. PMID 9512535.
• Kawabata M, Saeki K (1999). "Multiple alternative transcripts of the human homologue of the mouse TRAD/R51H3/RAD51D gene, a member of the rec A/RAD51 gene family". Biochem. Biophys. Res. Commun. 257 (1): 156–62. doi:10.1006/bbrc.1999.0413. PMID 10092526.
• Schild D, Lio YC, Collins DW, Tsomondo T, Chen DJ (2000). "Evidence for simultaneous protein interactions between human Rad51 paralogs". J. Biol. Chem. 275 (22): 16443–9. doi:10.1074/jbc.M001473200. PMID 10749867.
• Braybrooke JP, Spink KG, Thacker J, Hickson ID (2000). "The RAD51 family member, RAD51L3, is a DNA-stimulated ATPase that forms a complex with XRCC2". J. Biol. Chem. 275 (37): 29100–6. doi:10.1074/jbc.M002075200. PMID 10871607.
• Miller KA, Yoshikawa DM, McConnell IR, Clark R, Schild D, Albala JS (2002). "RAD51C interacts with RAD51B and is central to a larger protein complex in vivo exclusive of RAD51". J. Biol. Chem. 277 (10): 8406–11. doi:10.1074/jbc.M108306200. PMID 11744692.
• Masson JY, Tarsounas MC, Stasiak AZ, Stasiak A, Shah R, McIlwraith MJ, Benson FE, West SC (2001). "Identification and purification of two distinct complexes containing the five RAD51 paralogs". Genes Dev. 15 (24): 3296–307. doi:10.1101/gad.947001. PMC 312846. PMID 11751635.
• Sigurdsson S, Van Komen S, Bussen W, Schild D, Albala JS, Sung P (2001). "Mediator function of the human Rad51B-Rad51C complex in Rad51/RPA-catalyzed DNA strand exchange". Genes Dev. 15 (24): 3308–18. doi:10.1101/gad.935501. PMC 312844. PMID 11751636.
• Kurumizaka H, Ikawa S, Nakada M, Enomoto R, Kagawa W, Kinebuchi T, Yamazoe M, Yokoyama S, Shibata T (2002). "Homologous pairing and ring and filament structure formation activities of the human Xrcc2*Rad51D complex". J. Biol. Chem. 277 (16): 14315–20. doi:10.1074/jbc.M105719200. PMID 11834724.
• Wiese C, Collins DW, Albala JS, Thompson LH, Kronenberg A, Schild D (2002). "Interactions involving the Rad51 paralogs Rad51C and XRCC3 in human cells". Nucleic Acids Res. 30 (4): 1001–8. doi:10.1093/nar/30.4.1001. PMC 100332. PMID 11842112.
• Liu N, Schild D, Thelen MP, Thompson LH (2002). "Involvement of Rad51C in two distinct protein complexes of Rad51 paralogs in human cells". Nucleic Acids Res. 30 (4): 1009–15. doi:10.1093/nar/30.4.1009. PMC 100342. PMID 11842113.
• Godthelp BC, Artwert F, Joenje H, Zdzienicka MZ (2002). "Impaired DNA damage-induced nuclear Rad51 foci formation uniquely characterizes Fanconi anemia group D1". Oncogene. 21 (32): 5002–5. doi:10.1038/sj.onc.1205656. PMID 12118380.
• Braybrooke JP, Li JL, Wu L, Caple F, Benson FE, Hickson ID (2003). "Functional interaction between the Bloom's syndrome helicase and the RAD51 paralog, RAD51L3 (RAD51D)". J. Biol. Chem. 278 (48): 48357–66. doi:10.1074/jbc.M308838200. PMID 12975363.
• Hillman RT, Green RE, Brenner SE (2004). "An unappreciated role for RNA surveillance". Genome Biol. 5 (2): R8. doi:10.1186/gb-2004-5-2-r8. PMC 395752. PMID 14759258.
• Tarsounas M, Davies AA, West SC (2004). "RAD51 localization and activation following DNA damage". Philos. Trans. R. Soc. Lond., B, Biol. Sci. 359 (1441): 87–93. doi:10.1098/rstb.2003.1368. PMC 1693300. PMID 15065660.
• Tarsounas M, Muñoz P, Claas A, Smiraldo PG, Pittman DL, Blasco MA, West SC (2004). "Telomere maintenance requires the RAD51D recombination/repair protein". Cell. 117 (3): 337–47. doi:10.1016/S0092-8674(04)00337-X. PMID 15109494.
• Hussain S, Wilson JB, Medhurst AL, Hejna J, Witt E, Ananth S, Davies A, Masson JY, Moses R, West SC, de Winter JP, Ashworth A, Jones NJ, Mathew CG (2004). "Direct interaction of FANCD2 with BRCA2 in DNA damage response pathways". Hum. Mol. Genet. 13 (12): 1241–8. doi:10.1093/hmg/ddh135. PMID 15115758.
• Rodríguez-López R, Osorio A, Ribas G, Pollán M, Sánchez-Pulido L, de la Hoya M, Ruibal A, Zamora P, Arias JI, Salazar R, Vega A, Martínez JI, Esteban-Cardeñosa E, Alonso C, Letón R, Urioste Azcorra M, Miner C, Armengod ME, Carracedo A, González-Sarmiento R, Caldés T, Díez O, Benítez J (2004). "The variant E233G of the RAD51D gene could be a low-penetrance allele in high-risk breast cancer families without BRCA1/2 mutations". Int. J. Cancer. 110 (6): 845–9. doi:10.1002/ijc.20169. PMID 15170666.
• Loveday C, Turnbull C, Ramsay E, Hughes D, Ruark E, Frankum JR, Bowden G, Kalmyrzaev B, Warren-Perry M, Snape K, Adlard JW, Barwell J, Berg J, Brady AF, Brewer C, Brice G, Chapman C, Cook J, Davidson R, Donaldson A, Douglas F, Greenhalgh L, Henderson A, Izatt L, Kumar A, Lalloo F, Miedzybrodzka Z, Morrison PJ, Paterson J, Porteous M, Rogers MT, Shanley S, Walker L, Eccles D, Evans DG, Renwick A, Seal S, Lord CJ, Ashworth A, Reis-Filho JS, Antoniou AC, Rahman N (2011-08-07). "Germline mutations in RAD51D confer susceptibility to ovarian cancer". Nat. Genet. 43 (9): 879–82. doi:10.1038/ng.893. PMID 21822267.