RA51B_MOUSE
ID RA51B_MOUSE Reviewed; 350 AA.
AC O35719; Q8BSH6; Q9D555;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=DNA repair protein RAD51 homolog 2;
DE Short=R51H2;
DE AltName: Full=RAD51 homolog B;
DE AltName: Full=RAD51-like protein 1;
GN Name=Rad51b; Synonyms=Rad51l1, Rec2;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=9207106; DOI=10.1073/pnas.94.14.7417;
RA Rice M.C., Smith S.T., Bullrich F., Havre P., Kmiec E.B.;
RT "Isolation of human and mouse genes based on homology to REC2, a
RT recombinational repair gene from the fungus Ustilago maydis.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:7417-7422(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Mesonephros;
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).
CC -!- FUNCTION: Involved in the homologous recombination repair (HRR) pathway
CC of double-stranded DNA breaks arising during DNA replication or induced
CC by DNA-damaging agents. May promote the assembly of presynaptic RAD51
CC nucleoprotein filaments. Binds single-stranded DNA and double-stranded
CC DNA and has DNA-dependent ATPase activity. Part of the RAD51 paralog
CC protein complex BCDX2 which acts in the BRCA1-BRCA2-dependent HR
CC pathway. Upon DNA damage, BCDX2 acts downstream of BRCA2 recruitment
CC and upstream of RAD51 recruitment. BCDX2 binds predominantly to the
CC intersection of the four duplex arms of the Holliday junction and to
CC junction of replication forks. The BCDX2 complex was originally
CC reported to bind single-stranded DNA, single-stranded gaps in duplex
CC DNA and specifically to nicks in duplex DNA. The BCDX2 subcomplex
CC RAD51B:RAD51C exhibits single-stranded DNA-dependent ATPase activity
CC suggesting an involvement in early stages of the HR pathway.
CC {ECO:0000250|UniProtKB:O15315}.
CC -!- SUBUNIT: Part of the BCDX2 complex consisting of RAD51B, RAD51C, RAD51D
CC and XRCC2; the complex has a ring-like structure arranged into a flat
CC disc around a central channel. The BCDX2 subcomplex RAD51B:RAD51C
CC interacts with RAD51. Interacts with SWSAP1; involved in homologous
CC recombination repair. Interacts with HELQ.
CC {ECO:0000250|UniProtKB:O15315}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O15315}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O35719-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O35719-2; Sequence=VSP_008869, VSP_008870;
CC -!- TISSUE SPECIFICITY: Expressed in a wide range of tissues.
CC {ECO:0000269|PubMed:9207106}.
CC -!- PTM: Phosphorylated on tyrosine residues by BCR-ABL.
CC {ECO:0000250|UniProtKB:O15315}.
CC -!- SIMILARITY: Belongs to the RecA family. RAD51 subfamily. {ECO:0000305}.
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DR EMBL; U92068; AAB63359.1; -; mRNA.
DR EMBL; AK015771; BAB29970.1; -; mRNA.
DR EMBL; AK032913; BAC28084.1; -; mRNA.
DR CCDS; CCDS56845.1; -. [O35719-2]
DR CCDS; CCDS88360.1; -. [O35719-1]
DR RefSeq; NP_001239491.1; NM_001252562.1. [O35719-2]
DR RefSeq; NP_033040.2; NM_009014.3. [O35719-1]
DR RefSeq; XP_011242347.1; XM_011244045.1.
DR AlphaFoldDB; O35719; -.
DR SMR; O35719; -.
DR BioGRID; 202566; 6.
DR STRING; 10090.ENSMUSP00000078490; -.
DR PhosphoSitePlus; O35719; -.
DR EPD; O35719; -.
DR MaxQB; O35719; -.
DR PaxDb; O35719; -.
DR PeptideAtlas; O35719; -.
DR PRIDE; O35719; -.
DR ProteomicsDB; 300285; -. [O35719-1]
DR ProteomicsDB; 300286; -. [O35719-2]
DR Antibodypedia; 4257; 301 antibodies from 36 providers.
DR DNASU; 19363; -.
DR Ensembl; ENSMUST00000079533; ENSMUSP00000078490; ENSMUSG00000059060. [O35719-2]
DR Ensembl; ENSMUST00000171210; ENSMUSP00000128357; ENSMUSG00000059060. [O35719-1]
DR Ensembl; ENSMUST00000218039; ENSMUSP00000152105; ENSMUSG00000059060. [O35719-1]
DR GeneID; 19363; -.
DR KEGG; mmu:19363; -.
DR UCSC; uc007oai.1; mouse. [O35719-1]
DR UCSC; uc007oaj.1; mouse. [O35719-2]
DR CTD; 5890; -.
DR MGI; MGI:1099436; Rad51b.
DR VEuPathDB; HostDB:ENSMUSG00000059060; -.
DR eggNOG; KOG1433; Eukaryota.
DR GeneTree; ENSGT00940000160169; -.
DR InParanoid; O35719; -.
DR OMA; QLQGNMK; -.
DR OrthoDB; 1345899at2759; -.
DR PhylomeDB; O35719; -.
DR TreeFam; TF101219; -.
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 Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 19363; 3 hits in 109 CRISPR screens.
DR ChiTaRS; Rad51b; mouse.
DR PRO; PR:O35719; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; O35719; protein.
DR Bgee; ENSMUSG00000059060; Expressed in animal zygote and 98 other tissues.
DR Genevisible; O35719; MM.
DR GO; GO:0033063; C:Rad51B-Rad51C-Rad51D-XRCC2 complex; ISS:UniProtKB.
DR GO; GO:0005657; C:replication fork; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISO:MGI.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0000400; F:four-way junction DNA binding; ISO:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0001832; P:blastocyst growth; IMP:MGI.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0061053; P:somite development; IMP:MGI.
DR CDD; cd01123; Rad51_DMC1_radA; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013632; DNA_recomb/repair_Rad51_C.
DR InterPro; IPR016467; DNA_recomb/repair_RecA-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033925; Rad51_DMC1_RadA.
DR InterPro; IPR030548; RAD51B.
DR InterPro; IPR020588; RecA_ATP-bd.
DR PANTHER; PTHR46456; PTHR46456; 1.
DR Pfam; PF08423; Rad51; 1.
DR PIRSF; PIRSF005856; Rad51; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50162; RECA_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; DNA damage; DNA recombination;
KW DNA repair; DNA-binding; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..350
FT /note="DNA repair protein RAD51 homolog 2"
FT /id="PRO_0000122940"
FT REGION 1..75
FT /note="Interaction with RAD51C"
FT /evidence="ECO:0000250"
FT BINDING 108..115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 254..258
FT /note="ILTNQ -> TFQPI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008869"
FT VAR_SEQ 259..350
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008870"
FT CONFLICT 23
FT /note="Q -> L (in Ref. 1; AAB63359)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 350 AA; 38152 MW; 2DB79F8D60C0529D CRC64;
MSSKKLRRVG LSPELCDRLS RYQIVNCQHF LSLSPLELMK VTGLSYRGVH ELLHTVSKAC
APQMQTAYEL KTRRSAHLSP AFLSTTLCAL DEALHGGVPC GSLTEITGPP GCGKTQFCIM
MSVLATLPTS LGGLEGAVVY IDTESAFTAE RLVEIAESRF PQYFNTEEKL LLTSSRVHLC
RELTCEGLLQ RLESLEEEII SKGVKLVIVD SIASVVRKEF DPKLQGNIKE RNKFLGKGAS
LLKYLAGEFS IPVILTNQIT THLSGALPSQ ADLVSPADDL SLSEGTSGSS CLVAALGNTW
GHCVNTRLIL QYLDSERRQI LIAKSPLAAF TSFVYTIKGE GLVLQGHERP
