RAD51_MOUSE
ID RAD51_MOUSE Reviewed; 339 AA.
AC Q08297; Q3UAY5;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=DNA repair protein RAD51 homolog 1 {ECO:0000305};
DE AltName: Full=RAD51 homolog A;
GN Name=Rad51 {ECO:0000312|MGI:MGI:97890}; Synonyms=Rad51a, Reca;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8358431; DOI=10.1038/ng0793-239;
RA Shinohara A., Ogawa H., Matsuda Y., Ushio N., Ikeo K., Ogawa T.;
RT "Cloning of human, mouse and fission yeast recombination genes homologous
RT to RAD51 and recA.";
RL Nat. Genet. 4:239-243(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=8341671; DOI=10.1073/pnas.90.14.6577;
RA Morita T., Yoshimura Y., Yamamoto A., Murata K., Mori M., Yamamoto H.,
RA Matsushiro A.;
RT "A mouse homolog of the Escherichia coli recA and Saccharomyces cerevisiae
RT RAD51 genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:6577-6580(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION.
RX PubMed=12531026; DOI=10.1016/s1568-7864(02)00110-6;
RA Essers J., Hendriks R.W., Wesoly J., Beerens C.E.M.T., Smit B.,
RA Hoeijmakers J.H.J., Wyman C., Dronkert M.L.G., Kanaar R.;
RT "Analysis of mouse Rad54 expression and its implications for homologous
RT recombination.";
RL DNA Repair 1:779-793(2002).
RN [6]
RP FUNCTION, AND INTERACTION WITH MND1-PSMC3IP HETERODIMER.
RX PubMed=15834424; DOI=10.1038/nsmb923;
RA Petukhova G.V., Pezza R.J., Vanevski F., Ploquin M., Masson J.-Y.,
RA Camerini-Otero R.D.;
RT "The Hop2 and Mnd1 proteins act in concert with Rad51 and Dmc1 in meiotic
RT recombination.";
RL Nat. Struct. Mol. Biol. 12:449-453(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP INTERACTION WITH SWI5.
RX PubMed=20976249; DOI=10.1371/journal.pgen.1001160;
RA Akamatsu Y., Jasin M.;
RT "Role for the mammalian Swi5-Sfr1 complex in DNA strand break repair
RT through homologous recombination.";
RL PLoS Genet. 6:E1001160-E1001160(2010).
RN [9]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=22305526; DOI=10.1016/j.ajhg.2011.12.002;
RA Depienne C., Bouteiller D., Meneret A., Billot S., Groppa S., Klebe S.,
RA Charbonnier-Beaupel F., Corvol J.C., Saraiva J.P., Brueggemann N.,
RA Bhatia K., Cincotta M., Brochard V., Flamand-Roze C., Carpentier W.,
RA Meunier S., Marie Y., Gaussen M., Stevanin G., Wehrle R., Vidailhet M.,
RA Klein C., Dusart I., Brice A., Roze E.;
RT "RAD51 haploinsufficiency causes congenital mirror movements in humans.";
RL Am. J. Hum. Genet. 90:301-307(2012).
RN [10]
RP INTERACTION WITH FBH1.
RX PubMed=24108124; DOI=10.1074/jbc.m113.484493;
RA Simandlova J., Zagelbaum J., Payne M.J., Chu W.K., Shevelev I., Hanada K.,
RA Chatterjee S., Reid D.A., Liu Y., Janscak P., Rothenberg E., Hickson I.D.;
RT "FBH1 helicase disrupts RAD51 filaments in vitro and modulates homologous
RT recombination in mammalian cells.";
RL J. Biol. Chem. 288:34168-34180(2013).
RN [11]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH BRCA2.
RX PubMed=30760716; DOI=10.1038/s41467-019-08676-2;
RA Zhang J., Fujiwara Y., Yamamoto S., Shibuya H.;
RT "A meiosis-specific BRCA2 binding protein recruits recombinases to DNA
RT double-strand breaks to ensure homologous recombination.";
RL Nat. Commun. 10:722-722(2019).
RN [12]
RP INTERACTION WITH BRCA2.
RX PubMed=32345962; DOI=10.1038/s41467-020-15954-x;
RA Zhang J., Gurusaran M., Fujiwara Y., Zhang K., Echbarthi M., Vorontsov E.,
RA Guo R., Pendlebury D.F., Alam I., Livera G., Emmanuelle M., Wang P.J.,
RA Nandakumar J., Davies O.R., Shibuya H.;
RT "The BRCA2-MEILB2-BRME1 complex governs meiotic recombination and impairs
RT the mitotic BRCA2-RAD51 function in cancer cells.";
RL Nat. Commun. 11:2055-2055(2020).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=30272023; DOI=10.1038/s42003-018-0154-z;
RA Zhang Q., Shao J., Fan H.Y., Yu C.;
RT "Evolutionarily-conserved MZIP2 is essential for crossover formation in
RT mammalian meiosis.";
RL Commun. Biol. 1:147-147(2018).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=30949703; DOI=10.1093/nar/gkz226;
RA Liu H., Huang T., Li M., Li M., Zhang C., Jiang J., Yu X., Yin Y.,
RA Zhang F., Lu G., Luo M.C., Zhang L.R., Li J., Liu K., Chen Z.J.;
RT "SCRE serves as a unique synaptonemal complex fastener and is essential for
RT progression of meiosis prophase I in mice.";
RL Nucleic Acids Res. 47:5670-5683(2019).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=30746471; DOI=10.1126/sciadv.aau9780;
RA Zhang Q., Ji S.Y., Busayavalasa K., Yu C.;
RT "SPO16 binds SHOC1 to promote homologous recombination and crossing-over in
RT meiotic prophase I.";
RL Sci. Adv. 5:eaau9780-eaau9780(2019).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=32463460; DOI=10.1093/nar/gkaa406;
RA Shang Y., Huang T., Liu H., Liu Y., Liang H., Yu X., Li M., Zhai B.,
RA Yang X., Wei Y., Wang G., Chen Z., Wang S., Zhang L.;
RT "MEIOK21: a new component of meiotic recombination bridges required for
RT spermatogenesis.";
RL Nucleic Acids Res. 48:6624-6639(2020).
CC -!- FUNCTION: Plays an important role in homologous strand exchange, a key
CC step in DNA repair through homologous recombination (HR)
CC (PubMed:15834424). Binds to single-stranded DNA in an ATP-dependent
CC manner to form nucleoprotein filaments which are essential for the
CC homology search and strand exchange. Catalyzes the recognition of
CC homology and strand exchange between homologous DNA partners to form a
CC joint molecule between a processed DNA break and the repair template.
CC Recruited to resolve stalled replication forks during replication
CC stress. Part of a PALB2-scaffolded HR complex containing BRCA2 and
CC RAD51C and which is thought to play a role in DNA repair by HR. Plays a
CC role in regulating mitochondrial DNA copy number under conditions of
CC oxidative stress in the presence of RAD51C and XRCC3. Also involved in
CC interstrand cross-link repair (By similarity).
CC {ECO:0000250|UniProtKB:Q06609, ECO:0000269|PubMed:15834424}.
CC -!- SUBUNIT: Forms linear homooligomers, giving rise to a RAD51
CC nucleoprotein filament, which is essential for strand-pairing reactions
CC during DNA recombination. Interacts with BRCA1 and either directly or
CC indirectly with p53. Interacts with XRCC3, RAD54L and RAD54B. Interacts
CC with the BCDX2 subcomplex RAD51C:RAD51B. Component of the homologous
CC recombination repair (HR) complex composed of ERCC5/XPG, BRCA2, PALB2,
CC DSS1 and RAD51 (By similarity). Interacts directly with PALB2 which may
CC serve as a scaffold for a HR complex containing PALB2, BRCA2, RAD51C,
CC RAD51 and XRCC3. Interacts with RAD51AP1 and RAD51AP2. Interacts with
CC CHEK1, and this may require prior phosphorylation of CHEK1 (By
CC similarity). Interacts with the MND1-PSMC3IP heterodimer
CC (PubMed:15834424). Found in a complex, at least composed of BLM, RAD51
CC and SPIDR; the complex formation is mediated by SPIDR. Interacts with
CC SPIDR; the interaction is direct and recruits RAD51 to DNA damage
CC sites. Interacts with FIGNL1 (via N-terminal one-half region); the
CC interaction is direct. Interacts with RAD51AP1 (via C-terminal region);
CC the interaction is direct (By similarity). Interacts with NABP2, RPA1,
CC PALB2 and RAD51. Interacts with SWI5/C9orf119, and at lower level with
CC SFR1/MEIR5 (PubMed:20976249). Interacts with hyperphosphorylated RPA2;
CC this interaction is necessary for efficient recruitment to chromatin in
CC response to DNA damage. Interacts with SWSAP1; involved in homologous
CC recombination repair. Interacts with PARPBP, BRCA2 and RECQL5; these
CC interactions interfere with the formation of the RAD51-DNA homologous
CC recombination structure. Interacts with POLQ; POLQ acts as an inhibitor
CC of homology-recombination repair (HR) pathway by limiting RAD51
CC accumulation at resected ends. Interacts with POLN (By similarity).
CC Interacts with FBH1 (PubMed:24108124). Interacts with RFWD3 (By
CC similarity). Interacts with the MCM8-MCM9 complex; the interaction
CC recruits RAD51 to DNA damage sites (By similarity). Component of a
CC multiprotein complex with MEIOB and SPATA22. Interacts with the complex
CC BRME1:HSF2BP:BRCA2 (PubMed:32345962, PubMed:30760716). Interacts with
CC HELQ; stimulating HELQ DNA helicase activity and ability to unwing DNA
CC (By similarity). Interacts with MMS22L; the interaction is direct and
CC promotes recruitment of RAD51 to sites of DNA damage (By similarity).
CC Interacts with the ATAD5 RFC-like complex (By similarity). Within the
CC ATAD5 RFC-like complex, interacts with ATAD5 (via N-terminus); the
CC interaction is direct and enhanced under replication stress (By
CC similarity). Interacts with WDR48; the interaction is enhanced under
CC replication stress (By similarity). {ECO:0000250|UniProtKB:Q06609,
CC ECO:0000269|PubMed:15834424, ECO:0000269|PubMed:20976249,
CC ECO:0000269|PubMed:24108124, ECO:0000269|PubMed:30760716,
CC ECO:0000269|PubMed:32345962}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q06609}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q06609}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q06609}. Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q06609}. Chromosome
CC {ECO:0000269|PubMed:30272023, ECO:0000269|PubMed:30746471,
CC ECO:0000269|PubMed:30760716, ECO:0000269|PubMed:30949703,
CC ECO:0000269|PubMed:32463460}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q06609}.
CC Note=Colocalizes with RAD51AP1 and RPA2 to multiple nuclear foci upon
CC induction of DNA damage. DNA damage induces an increase in nuclear
CC levels. Together with FIGNL1, redistributed in discrete nuclear DNA
CC damage-induced foci after ionizing radiation (IR) or camptothecin (CPT)
CC treatment. Accumulated at sites of DNA damage in a SPIDR-dependent
CC manner. Recruited at sites of DNA damage in a MCM9-MCM8-dependent
CC manner. Colocalizes with ERCC5/XPG to nuclear foci in S phase.
CC Recruited to stalled replication forks during replication stress by the
CC TONSL-MMS22L complex, as well as ATAD5 and WDR48 in an ATR-dependent
CC manner. {ECO:0000250|UniProtKB:Q06609}.
CC -!- TISSUE SPECIFICITY: Expressed in ovary and testis. Expressed in the
CC brain. {ECO:0000269|PubMed:22305526}.
CC -!- DEVELOPMENTAL STAGE: Expression in the brain is strongest at day 12
CC dpc, particularly in the cortical ventricular zone. In the cortex of
CC newborn mice (P0), RAD51 is mainly present in the subplate and, in
CC lesser amounts, in layer V. It is detected in a subpopulation of
CC corticospinal axons at the pyramidal decussation in 2-day-old (P2)
CC mice. {ECO:0000269|PubMed:22305526}.
CC -!- PTM: Ubiquitinated by the SCF(FBH1) E3 ubiquitin ligase complex,
CC regulating RAD51 subcellular location and preventing its association
CC with DNA. Ubiquitinated by RFWD3 in response to DNA damage:
CC ubiquitination leads to degradation by the proteasome, promoting
CC homologous recombination. {ECO:0000250|UniProtKB:Q06609}.
CC -!- PTM: Phosphorylated. Phosphorylation of Thr-309 by CHEK1 may enhance
CC association with chromatin at sites of DNA damage and promote DNA
CC repair by homologous recombination. Phosphorylation by ABL1 inhibits
CC function. {ECO:0000250|UniProtKB:Q06609}.
CC -!- MISCELLANEOUS: The nucleus of a mouse embryonic stem (ES) cells
CC contains on average 4.7 x 10(5) molecules.
CC -!- SIMILARITY: Belongs to the RecA family. RAD51 subfamily. {ECO:0000305}.
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DR EMBL; D13473; BAA02718.1; -; mRNA.
DR EMBL; D13803; BAA02961.1; -; mRNA.
DR EMBL; AK011242; BAB27489.1; -; mRNA.
DR EMBL; AK076468; BAC36357.1; -; mRNA.
DR EMBL; AK151157; BAE30162.1; -; mRNA.
DR EMBL; AK151177; BAE30179.1; -; mRNA.
DR EMBL; BC027384; AAH27384.1; -; mRNA.
DR CCDS; CCDS16590.1; -.
DR PIR; A48221; A48221.
DR RefSeq; NP_035364.1; NM_011234.4.
DR AlphaFoldDB; Q08297; -.
DR BMRB; Q08297; -.
DR SMR; Q08297; -.
DR BioGRID; 202564; 15.
DR ComplexPortal; CPX-972; BRCC ubiquitin ligase complex.
DR CORUM; Q08297; -.
DR IntAct; Q08297; 1.
DR MINT; Q08297; -.
DR STRING; 10090.ENSMUSP00000028795; -.
DR ChEMBL; CHEMBL2034808; -.
DR iPTMnet; Q08297; -.
DR PhosphoSitePlus; Q08297; -.
DR EPD; Q08297; -.
DR MaxQB; Q08297; -.
DR PaxDb; Q08297; -.
DR PRIDE; Q08297; -.
DR ProteomicsDB; 300305; -.
DR Antibodypedia; 4162; 970 antibodies from 45 providers.
DR DNASU; 19361; -.
DR Ensembl; ENSMUST00000028795; ENSMUSP00000028795; ENSMUSG00000027323.
DR GeneID; 19361; -.
DR KEGG; mmu:19361; -.
DR UCSC; uc008ltd.1; mouse.
DR CTD; 5888; -.
DR MGI; MGI:97890; Rad51.
DR VEuPathDB; HostDB:ENSMUSG00000027323; -.
DR eggNOG; KOG1433; Eukaryota.
DR GeneTree; ENSGT00940000156157; -.
DR HOGENOM; CLU_041732_0_2_1; -.
DR InParanoid; Q08297; -.
DR OMA; TFRIYLR; -.
DR OrthoDB; 877394at2759; -.
DR PhylomeDB; Q08297; -.
DR TreeFam; TF101218; -.
DR Reactome; R-MMU-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-MMU-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-MMU-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR Reactome; R-MMU-5693579; Homologous DNA Pairing and Strand Exchange.
DR Reactome; R-MMU-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR BioGRID-ORCS; 19361; 36 hits in 110 CRISPR screens.
DR ChiTaRS; Xrcc2; mouse.
DR PRO; PR:Q08297; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q08297; protein.
DR Bgee; ENSMUSG00000027323; Expressed in otic placode and 186 other tissues.
DR ExpressionAtlas; Q08297; baseline and differential.
DR Genevisible; Q08297; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL.
DR GO; GO:0000793; C:condensed chromosome; IDA:MGI.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0000800; C:lateral element; IDA:MGI.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0000228; C:nuclear chromosome; ISS:UniProtKB.
DR GO; GO:0000152; C:nuclear ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0016605; C:PML body; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0035861; C:site of double-strand break; ISO:MGI.
DR GO; GO:0000795; C:synaptonemal complex; TAS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0070182; F:DNA polymerase binding; ISO:MGI.
DR GO; GO:0000150; F:DNA strand exchange activity; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:MGI.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0071312; P:cellular response to alkaloid; IMP:MGI.
DR GO; GO:0072757; P:cellular response to camptothecin; ISS:UniProtKB.
DR GO; GO:0072719; P:cellular response to cisplatin; IEA:Ensembl.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0071480; P:cellular response to gamma radiation; IEA:Ensembl.
DR GO; GO:0072711; P:cellular response to hydroxyurea; IMP:MGI.
DR GO; GO:0071479; P:cellular response to ionizing radiation; ISS:UniProtKB.
DR GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IMP:MGI.
DR GO; GO:0000730; P:DNA recombinase assembly; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; TAS:UniProtKB.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; ISS:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:MGI.
DR GO; GO:0035518; P:histone H2A monoubiquitination; IC:ComplexPortal.
DR GO; GO:0036297; P:interstrand cross-link repair; ISS:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IDA:MGI.
DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
DR GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; IEA:InterPro.
DR GO; GO:0051106; P:positive regulation of DNA ligation; ISO:MGI.
DR GO; GO:0051865; P:protein autoubiquitination; IC:ComplexPortal.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
DR GO; GO:2000001; P:regulation of DNA damage checkpoint; IC:ComplexPortal.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IMP:MGI.
DR GO; GO:0031297; P:replication fork processing; IMP:MGI.
DR GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IMP:MGI.
DR GO; GO:1904631; P:response to glucoside; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR GO; GO:0010165; P:response to X-ray; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0042148; P:strand invasion; IBA:GO_Central.
DR GO; GO:0000722; P:telomere maintenance via recombination; IGI:BHF-UCL.
DR GO; GO:0010833; P:telomere maintenance via telomere lengthening; IGI:BHF-UCL.
DR GO; GO:0032200; P:telomere organization; IMP:MGI.
DR CDD; cd01123; Rad51_DMC1_radA; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011941; DNA_recomb/repair_Rad51.
DR InterPro; IPR013632; DNA_recomb/repair_Rad51_C.
DR InterPro; IPR016467; DNA_recomb/repair_RecA-like.
DR InterPro; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033925; Rad51_DMC1_RadA.
DR InterPro; IPR020588; RecA_ATP-bd.
DR InterPro; IPR020587; RecA_monomer-monomer_interface.
DR Pfam; PF08423; Rad51; 1.
DR PIRSF; PIRSF005856; Rad51; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF47794; SSF47794; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02239; recomb_RAD51; 1.
DR PROSITE; PS50162; RECA_2; 1.
DR PROSITE; PS50163; RECA_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Chromosome; Cytoplasm; Cytoskeleton; DNA damage;
KW DNA recombination; DNA repair; DNA-binding; Isopeptide bond; Mitochondrion;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q06609"
FT CHAIN 2..339
FT /note="DNA repair protein RAD51 homolog 1"
FT /id="PRO_0000122933"
FT DOMAIN 48..77
FT /note="HhH"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..257
FT /note="Interaction with PALB2"
FT /evidence="ECO:0000250"
FT MOTIF 245..260
FT /note="Nuclear export signal; masked by the interaction
FT with BRCA2"
FT /evidence="ECO:0000250|UniProtKB:Q06609"
FT BINDING 127..134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q06609"
FT MOD_RES 54
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000250|UniProtKB:Q06609"
FT MOD_RES 309
FT /note="Phosphothreonine; by CHEK1"
FT /evidence="ECO:0000250|UniProtKB:Q06609"
FT CROSSLNK 58
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q06609"
FT CROSSLNK 64
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q06609"
SQ SEQUENCE 339 AA; 36971 MW; CE631E2C246BA481 CRC64;
MAMQMQLEAS ADTSVEEESF GPQPISRLEQ CGINANDVKK LEEAGYHTVE AVAYAPKKEL
INIKGISEAK ADKILTEAAK LVPMGFTTAT EFHQRRSEII QITTGSKELD KLLQGGIETG
SITEMFGEFR TGKTQICHTL AVTCQLPIDR GGGEGKAMYI DTEGTFRPER LLAVAERYGL
SGSDVLDNVA YARGFNTDHQ TQLLYQASAM MVESRYALLI VDSATALYRT DYSGRGELSA
RQMHLARFLR MLLRLADEFG VAVVITNQVV AQVDGAAMFA ADPKKPIGGN IIAHASTTRL
YLRKGRGETR ICKIYDSPCL PEAEAMFAIN ADGVGDAKD
