Description of target: Plays an important role in homologous strand exchange, a key step in DNA repair through homologous recombination. Binds to single and double-stranded DNA and exhibits DNA-dependent ATPase activity. 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. Binds to single-stranded DNA in an ATP-dependent manner to form nucleoprotein filaments which are essential for the homology search and strand exchange (PubMed:26681308). 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 XRCC3.9 Publications
 <p>Manually curated information for which there is published experimental evidence.</p>
 
 
 <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment iniRef.5"Identification of a novel human Rad51 variant that promotes DNA strand exchange."_x005F_x005F_x000D_Park J.Y., Yoo H.W., Kim B.R., Park R., Choi S.Y., Kim Y._x005F_x005F_x000D_Nucleic Acids Res. 36:3226-3234(2008) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION OF ISOFORMS 1 AND 3, TISSUE SPECIFICITY (ISOFORMS 1 AND 3), SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), MUTAGENESIS (ISOFORM 3).Ref.18"Homologous DNA pairing by human recombination factors Rad51 and Rad54."_x005F_x005F_x000D_Sigurdsson S., Van Komen S., Petukhova G., Sung P._x005F_x005F_x000D_J. Biol. Chem. 277:42790-42794(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION.Ref.27"Physical interaction of RECQ5 helicase with RAD51 facilitates its anti-recombinase activity."_x005F_x005F_x000D_Schwendener S., Raynard S., Paliwal S., Cheng A., Kanagaraj R., Shevelev I., Stark J.M., Sung P., Janscak P._x005F_x005F_x000D_J. Biol. Chem. 285:15739-15745(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RECQL5, FUNCTION.Ref.28"Discovery of a novel function for human Rad51: maintenance of the mitochondrial genome."_x005F_x005F_x000D_Sage J.M., Gildemeister O.S., Knight K.L._x005F_x005F_x000D_J. Biol. Chem. 285:18984-18990(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION.Ref.30"RecQL5 promotes genome stabilization through two parallel mechanisms--interacting with RNA polymerase II and acting as a helicase."_x005F_x005F_x000D_Islam M.N., Fox D. III, Guo R., Enomoto T., Wang W._x005F_x005F_x000D_Mol. Cell. Biol. 30:2460-2472(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RECQL5, FUNCTION.Ref.42"FIGNL1-containing protein complex is required for efficient homologous recombination repair."_x005F_x005F_x000D_Yuan J., Chen J._x005F_x005F_x000D_Proc. Natl. Acad. Sci. U.S.A. 110:10640-10645(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH FIGNL1; RAD51AP1 AND SWI5, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.Ref.43"Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome helicase with homologous recombination repair."_x005F_x005F_x000D_Wan L., Han J., Liu T., Dong S., Xie F., Chen H., Huang J._x005F_x005F_x000D_Proc. Natl. Acad. Sci. U.S.A. 110:10646-10651(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH BLM AND SPIDR, INTERACTION WITH SPIDR, SUBCELLULAR LOCATION.Ref.46"Insights into DNA recombination from the structure of a RAD51-BRCA2 complex."_x005F_x005F_x000D_Pellegrini L., Yu D.S., Lo T., Anand S., Lee M., Blundell T.L., Venkitaraman A.R._x005F_x005F_x000D_Nature 420:287-293(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 97-339 IN COMPLEX WITH BRCA2, FUNCTION, SUBUNIT, MUTAGENESIS OF PHE-86 AND ALA-89, SUBCELLULAR LOCATION, INTERACTION WITH BRCA2.Ref.48"A novel Fanconi anaemia subtype associated with a dominant-negative mutation in RAD51."_x005F_x005F_x000D_Ameziane N., May P., Haitjema A., van de Vrugt H.J., van Rossum-Fikkert S.E., Ristic D., Williams G.J., Balk J., Rockx D., Li H., Rooimans M.A., Oostra A.B., Velleuer E., Dietrich R., Bleijerveld O.B., Maarten Altelaar A.F., Meijers-Heijboer H., Joenje H. , Glusman G., Roach J., Hood L., Galas D., Wyman C., Balling R., den Dunnen J., de Winter J.P., Kanaar R., Gelinas R., Dorsman J.C._x005F_x005F_x000D_Nat. Commun. 6:8829-8829(2015) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT THR-293, CHARACTERIZATION OF VARIANT THR-293, FUNCTION, SUBCELLULAR LOCATION. ;Species reactivity: Human;Application: ELISA;Assay info: Assay Methodology: Quantitative Sandwich Immunoassay;Sensitivity: < 0.118 ng/mL
4886.78RON
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Număr Catalog 247-OKCD01086CategorieAfaceri și industrie > Știință și laboratorFurnizorAviva Systems BiologyGentaurDimensiune96 WellsTipsingle
