RAD51L3: Difference between revisions

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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''DNA repair protein RAD51 homolog 4''' is a [[protein]] that in humans is encoded by the ''RAD51L3'' [[gene]].<ref name="pmid9570954">{{cite journal | vauthors = Pittman DL, Weinberg LR, Schimenti JC | title = Identification, characterization, and genetic mapping of Rad51d, a new mouse and human RAD51/RecA-related gene | journal = Genomics | volume = 49 | issue = 1 | pages = 103–11  | date = June 1998 | pmid = 9570954 | pmc =  | doi = 10.1006/geno.1998.5226 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: RAD51L3 RAD51-like 3 (S. cerevisiae)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5892| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = RAD51-like 3 (S. cerevisiae)
| HGNCid = 9823
| Symbol = RAD51L3
| AltSymbols =; HsTRAD; R51H3; RAD51D; Trad
| OMIM = 602954
| ECnumber = 
| Homologene = 2156
| MGIid = 1261809
| GeneAtlas_image1 = PBB_GE_RAD51L3_37793_r_at_tn.png
| GeneAtlas_image2 = PBB_GE_RAD51L3_209965_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008094 |text = DNA-dependent ATPase activity}} {{GNF_GO|id=GO:0017111 |text = nucleoside-triphosphatase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006259 |text = DNA metabolic process}} {{GNF_GO|id=GO:0006284 |text = base-excision repair}} {{GNF_GO|id=GO:0007131 |text = meiotic recombination}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5892
    | Hs_Ensembl = ENSG00000185379
    | Hs_RefseqProtein = NP_002869
    | Hs_RefseqmRNA = NM_002878
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 17
    | Hs_GenLoc_start = 30450929
    | Hs_GenLoc_end = 30470948
    | Hs_Uniprot = O75771
    | Mm_EntrezGene = 19364
    | Mm_Ensembl = ENSMUSG00000018841
    | Mm_RefseqmRNA = XM_489738
    | Mm_RefseqProtein = XP_489738
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 82690902
    | Mm_GenLoc_end = 82706806
    | Mm_Uniprot = Q5SU85
  }}
}}
'''RAD51-like 3 (S. cerevisiae)''', also known as '''RAD51L3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RAD51L3 RAD51-like 3 (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5892| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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.<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: RAD51L3 RAD51-like 3 (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5892| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
RAD51L3 has been shown to [[Protein-protein interaction|interact]] with:
* [[Bloom syndrome protein]],<ref name = pmid12975363/>
* [[RAD51C]],<ref name = pmid11842113/><ref name = pmid11744692>{{cite journal | vauthors = Miller KA, Yoshikawa DM, McConnell IR, Clark R, Schild D, Albala JS | title = RAD51C interacts with RAD51B and is central to a larger protein complex in vivo exclusive of RAD51 | journal = J. Biol. Chem. | volume = 277 | issue = 10 | pages = 8406–11  | date = March 2002 | pmid = 11744692 | doi = 10.1074/jbc.M108306200 }}</ref> and
* [[XRCC2]].<ref name = pmid12975363>{{cite journal | vauthors = Braybrooke JP, Li JL, Wu L, Caple F, Benson FE, Hickson ID | title = Functional interaction between the Bloom's syndrome helicase and the RAD51 paralog, RAD51L3 (RAD51D) | journal = J. Biol. Chem. | volume = 278 | issue = 48 | pages = 48357–66  | date = November 2003 | pmid = 12975363 | doi = 10.1074/jbc.M308838200 }}</ref><ref name = pmid11842113>{{cite journal | vauthors = Liu N, Schild D, Thelen MP, Thompson LH | title = Involvement of Rad51C in two distinct protein complexes of Rad51 paralogs in human cells | journal = Nucleic Acids Res. | volume = 30 | issue = 4 | pages = 1009–15  | date = February 2002 | pmid = 11842113 | pmc = 100342 | doi =  10.1093/nar/30.4.1009}}</ref><ref name = pmid10749867>{{cite journal | vauthors = Schild D, Lio YC, Collins DW, Tsomondo T, Chen DJ | title = Evidence for simultaneous protein interactions between human Rad51 paralogs | journal = J. Biol. Chem. | volume = 275 | issue = 22 | pages = 16443–9  | date = June 2000 | pmid = 10749867 | doi = 10.1074/jbc.M001473200 }}</ref><ref name = pmid15115758>{{cite journal | vauthors = 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 | title = Direct interaction of FANCD2 with BRCA2 in DNA damage response pathways | journal = Hum. Mol. Genet. | volume = 13 | issue = 12 | pages = 1241–8  | date = June 2004 | pmid = 15115758 | doi = 10.1093/hmg/ddh135 }}</ref>
 
== References ==
{{reflist}}
{{Clear}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Cartwright R, Dunn AM, Simpson PJ, Tambini CE, Thacker J | title = Isolation of novel human and mouse genes of the recA/RAD51 recombination-repair gene family | journal = Nucleic Acids Res. | volume = 26 | issue = 7 | pages = 1653–9 | year = 1998 | pmid = 9512535 | pmc = 147465 | doi = 10.1093/nar/26.7.1653 }}
| citations =
* {{cite journal | vauthors = Kawabata M, Saeki K | title = Multiple alternative transcripts of the human homologue of the mouse TRAD/R51H3/RAD51D gene, a member of the rec A/RAD51 gene family | journal = Biochem. Biophys. Res. Commun. | volume = 257 | issue = 1 | pages = 156–62 | year = 1999 | pmid = 10092526 | doi = 10.1006/bbrc.1999.0413 }}
*{{cite journal | author=Cartwright R, Dunn AM, Simpson PJ, ''et al.'' |title=Isolation of novel human and mouse genes of the recA/RAD51 recombination-repair gene family. |journal=Nucleic Acids Res. |volume=26 |issue= 7 |pages= 1653-9 |year= 1998 |pmid= 9512535 |doi= }}
* {{cite journal | vauthors = Schild D, Lio YC, Collins DW, Tsomondo T, Chen DJ | title = Evidence for simultaneous protein interactions between human Rad51 paralogs | journal = J. Biol. Chem. | volume = 275 | issue = 22 | pages = 16443–9 | year = 2000 | pmid = 10749867 | doi = 10.1074/jbc.M001473200 }}
*{{cite journal | author=Pittman DL, Weinberg LR, Schimenti JC |title=Identification, characterization, and genetic mapping of Rad51d, a new mouse and human RAD51/RecA-related gene. |journal=Genomics |volume=49 |issue= 1 |pages= 103-11 |year= 1998 |pmid= 9570954 |doi= 10.1006/geno.1998.5226 }}
* {{cite journal | vauthors = Braybrooke JP, Spink KG, Thacker J, Hickson ID | title = The RAD51 family member, RAD51L3, is a DNA-stimulated ATPase that forms a complex with XRCC2 | journal = J. Biol. Chem. | volume = 275 | issue = 37 | pages = 29100–6 | year = 2000 | pmid = 10871607 | doi = 10.1074/jbc.M002075200 }}
*{{cite journal | author=Kawabata M, Saeki K |title=Multiple alternative transcripts of the human homologue of the mouse TRAD/R51H3/RAD51D gene, a member of the rec A/RAD51 gene family. |journal=Biochem. Biophys. Res. Commun. |volume=257 |issue= 1 |pages= 156-62 |year= 1999 |pmid= 10092526 |doi= 10.1006/bbrc.1999.0413 }}
* {{cite journal | vauthors = Miller KA, Yoshikawa DM, McConnell IR, Clark R, Schild D, Albala JS | title = RAD51C interacts with RAD51B and is central to a larger protein complex in vivo exclusive of RAD51 | journal = J. Biol. Chem. | volume = 277 | issue = 10 | pages = 8406–11 | year = 2002 | pmid = 11744692 | doi = 10.1074/jbc.M108306200 }}
*{{cite journal | author=Schild D, Lio YC, Collins DW, ''et al.'' |title=Evidence for simultaneous protein interactions between human Rad51 paralogs. |journal=J. Biol. Chem. |volume=275 |issue= 22 |pages= 16443-9 |year= 2000 |pmid= 10749867 |doi= 10.1074/jbc.M001473200 }}
* {{cite journal | vauthors = Masson JY, Tarsounas MC, Stasiak AZ, Stasiak A, Shah R, McIlwraith MJ, Benson FE, West SC | title = Identification and purification of two distinct complexes containing the five RAD51 paralogs | journal = Genes Dev. | volume = 15 | issue = 24 | pages = 3296–307 | year = 2001 | pmid = 11751635 | pmc = 312846 | doi = 10.1101/gad.947001 }}
*{{cite journal | author=Braybrooke JP, Spink KG, Thacker J, Hickson ID |title=The RAD51 family member, RAD51L3, is a DNA-stimulated ATPase that forms a complex with XRCC2. |journal=J. Biol. Chem. |volume=275 |issue= 37 |pages= 29100-6 |year= 2000 |pmid= 10871607 |doi= 10.1074/jbc.M002075200 }}
* {{cite journal | vauthors = Sigurdsson S, Van Komen S, Bussen W, Schild D, Albala JS, Sung P | title = Mediator function of the human Rad51B-Rad51C complex in Rad51/RPA-catalyzed DNA strand exchange | journal = Genes Dev. | volume = 15 | issue = 24 | pages = 3308–18 | year = 2001 | pmid = 11751636 | pmc = 312844 | doi = 10.1101/gad.935501 }}
*{{cite journal | author=Miller KA, Yoshikawa DM, McConnell IR, ''et al.'' |title=RAD51C interacts with RAD51B and is central to a larger protein complex in vivo exclusive of RAD51. |journal=J. Biol. Chem. |volume=277 |issue= 10 |pages= 8406-11 |year= 2002 |pmid= 11744692 |doi= 10.1074/jbc.M108306200 }}
* {{cite journal | vauthors = Kurumizaka H, Ikawa S, Nakada M, Enomoto R, Kagawa W, Kinebuchi T, Yamazoe M, Yokoyama S, Shibata T | title = Homologous pairing and ring and filament structure formation activities of the human Xrcc2*Rad51D complex | journal = J. Biol. Chem. | volume = 277 | issue = 16 | pages = 14315–20 | year = 2002 | pmid = 11834724 | doi = 10.1074/jbc.M105719200 }}
*{{cite journal | author=Masson JY, Tarsounas MC, Stasiak AZ, ''et al.'' |title=Identification and purification of two distinct complexes containing the five RAD51 paralogs. |journal=Genes Dev. |volume=15 |issue= 24 |pages= 3296-307 |year= 2002 |pmid= 11751635 |doi= 10.1101/gad.947001 }}
* {{cite journal | vauthors = Wiese C, Collins DW, Albala JS, Thompson LH, Kronenberg A, Schild D | title = Interactions involving the Rad51 paralogs Rad51C and XRCC3 in human cells | journal = Nucleic Acids Res. | volume = 30 | issue = 4 | pages = 1001–8 | year = 2002 | pmid = 11842112 | pmc = 100332 | doi = 10.1093/nar/30.4.1001 }}
*{{cite journal | author=Sigurdsson S, Van Komen S, Bussen W, ''et al.'' |title=Mediator function of the human Rad51B-Rad51C complex in Rad51/RPA-catalyzed DNA strand exchange. |journal=Genes Dev. |volume=15 |issue= 24 |pages= 3308-18 |year= 2002 |pmid= 11751636 |doi= 10.1101/gad.935501 }}
* {{cite journal | vauthors = Liu N, Schild D, Thelen MP, Thompson LH | title = Involvement of Rad51C in two distinct protein complexes of Rad51 paralogs in human cells | journal = Nucleic Acids Res. | volume = 30 | issue = 4 | pages = 1009–15 | year = 2002 | pmid = 11842113 | pmc = 100342 | doi = 10.1093/nar/30.4.1009 }}
*{{cite journal | author=Kurumizaka H, Ikawa S, Nakada M, ''et al.'' |title=Homologous pairing and ring and filament structure formation activities of the human Xrcc2*Rad51D complex. |journal=J. Biol. Chem. |volume=277 |issue= 16 |pages= 14315-20 |year= 2002 |pmid= 11834724 |doi= 10.1074/jbc.M105719200 }}
* {{cite journal | vauthors = Godthelp BC, Artwert F, Joenje H, Zdzienicka MZ | title = Impaired DNA damage-induced nuclear Rad51 foci formation uniquely characterizes Fanconi anemia group D1 | journal = Oncogene | volume = 21 | issue = 32 | pages = 5002–5 | year = 2002 | pmid = 12118380 | doi = 10.1038/sj.onc.1205656 }}
*{{cite journal | author=Wiese C, Collins DW, Albala JS, ''et al.'' |title=Interactions involving the Rad51 paralogs Rad51C and XRCC3 in human cells. |journal=Nucleic Acids Res. |volume=30 |issue= 4 |pages= 1001-8 |year= 2002 |pmid= 11842112 |doi= }}
* {{cite journal | vauthors = Braybrooke JP, Li JL, Wu L, Caple F, Benson FE, Hickson ID | title = Functional interaction between the Bloom's syndrome helicase and the RAD51 paralog, RAD51L3 (RAD51D) | journal = J. Biol. Chem. | volume = 278 | issue = 48 | pages = 48357–66 | year = 2003 | pmid = 12975363 | doi = 10.1074/jbc.M308838200 }}
*{{cite journal | author=Liu N, Schild D, Thelen MP, Thompson LH |title=Involvement of Rad51C in two distinct protein complexes of Rad51 paralogs in human cells. |journal=Nucleic Acids Res. |volume=30 |issue= 4 |pages= 1009-15 |year= 2002 |pmid= 11842113 |doi= }}
* {{cite journal | vauthors = Hillman RT, Green RE, Brenner SE | title = An unappreciated role for RNA surveillance | journal = Genome Biol. | volume = 5 | issue = 2 | pages = R8 | year = 2004 | pmid = 14759258 | pmc = 395752 | doi = 10.1186/gb-2004-5-2-r8 }}
*{{cite journal | author=Godthelp BC, Artwert F, Joenje H, Zdzienicka MZ |title=Impaired DNA damage-induced nuclear Rad51 foci formation uniquely characterizes Fanconi anemia group D1. |journal=Oncogene |volume=21 |issue= 32 |pages= 5002-5 |year= 2002 |pmid= 12118380 |doi= 10.1038/sj.onc.1205656 }}
* {{cite journal | vauthors = Tarsounas M, Davies AA, West SC | title = RAD51 localization and activation following DNA damage | journal = Philos. Trans. R. Soc. Lond. B Biol. Sci. | volume = 359 | issue = 1441 | pages = 87–93 | year = 2004 | pmid = 15065660 | pmc = 1693300 | doi = 10.1098/rstb.2003.1368 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{cite journal | vauthors = Tarsounas M, Muñoz P, Claas A, Smiraldo PG, Pittman DL, Blasco MA, West SC | title = Telomere maintenance requires the RAD51D recombination/repair protein | journal = Cell | volume = 117 | issue = 3 | pages = 337–47 | year = 2004 | pmid = 15109494 | doi = 10.1016/S0092-8674(04)00337-X }}
*{{cite journal | author=Braybrooke JP, Li JL, Wu L, ''et al.'' |title=Functional interaction between the Bloom's syndrome helicase and the RAD51 paralog, RAD51L3 (RAD51D). |journal=J. Biol. Chem. |volume=278 |issue= 48 |pages= 48357-66 |year= 2004 |pmid= 12975363 |doi= 10.1074/jbc.M308838200 }}
* {{cite journal | vauthors = 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 | title = Direct interaction of FANCD2 with BRCA2 in DNA damage response pathways | journal = Hum. Mol. Genet. | volume = 13 | issue = 12 | pages = 1241–8 | year = 2004 | pmid = 15115758 | doi = 10.1093/hmg/ddh135 }}
*{{cite journal | author=Hillman RT, Green RE, Brenner SE |title=An unappreciated role for RNA surveillance. |journal=Genome Biol. |volume=5 |issue= 2 |pages= R8 |year= 2005 |pmid= 14759258 |doi= 10.1186/gb-2004-5-2-r8 }}
* {{cite journal | vauthors = 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 | title = The variant E233G of the RAD51D gene could be a low-penetrance allele in high-risk breast cancer families without BRCA1/2 mutations | journal = Int. J. Cancer | volume = 110 | issue = 6 | pages = 845–9 | year = 2004 | pmid = 15170666 | doi = 10.1002/ijc.20169 }}
*{{cite journal | author=Tarsounas M, Davies AA, West SC |title=RAD51 localization and activation following DNA damage. |journal=Philos. Trans. R. Soc. Lond., B, Biol. Sci. |volume=359 |issue= 1441 |pages= 87-93 |year= 2004 |pmid= 15065660 |doi= 10.1098/rstb.2003.1368 }}
* {{cite journal | vauthors = 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 | title = Germline mutations in RAD51D confer susceptibility to ovarian cancer | journal = Nat. Genet. | volume = 43 | issue = 9 | pages = 879–82 | date = 2011-08-07 | pmid = 21822267 | doi = 10.1038/ng.893 }}
*{{cite journal | author=Tarsounas M, Muñoz P, Claas A, ''et al.'' |title=Telomere maintenance requires the RAD51D recombination/repair protein. |journal=Cell |volume=117 |issue= 3 |pages= 337-47 |year= 2004 |pmid= 15109494 |doi= }}
*{{cite journal | author=Hussain S, Wilson JB, Medhurst AL, ''et al.'' |title=Direct interaction of FANCD2 with BRCA2 in DNA damage response pathways. |journal=Hum. Mol. Genet. |volume=13 |issue= 12 |pages= 1241-8 |year= 2004 |pmid= 15115758 |doi= 10.1093/hmg/ddh135 }}
*{{cite journal  | author=Rodríguez-López R, Osorio A, Ribas G, ''et al.'' |title=The variant E233G of the RAD51D gene could be a low-penetrance allele in high-risk breast cancer families without BRCA1/2 mutations. |journal=Int. J. Cancer |volume=110 |issue= 6 |pages= 845-9 |year= 2004 |pmid= 15170666 |doi= 10.1002/ijc.20169 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
}}
{{refend}}
{{refend}}


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Revision as of 05:09, 25 November 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

DNA repair protein RAD51 homolog 4 is a protein that in humans is encoded by the RAD51L3 gene.[1][2]

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.[2]

Interactions

RAD51L3 has been shown to interact with:

References

  1. ↑ 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.
  2. ↑ 2.0 2.1 "Entrez Gene: RAD51L3 RAD51-like 3 (S. cerevisiae)".
  3. ↑ 3.0 3.1 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.
  4. ↑ 4.0 4.1 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.
  5. ↑ 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.
  6. ↑ 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.
  7. ↑ 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


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