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Q08297 (RAD51_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA repair protein RAD51 homolog 1
Alternative name(s):
RAD51 homolog A
Gene names
Name:Rad51
Synonyms:Rad51a, Reca
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Participates in a common DNA damage response pathway associated with the activation of homologous recombination and double-strand break repair. Binds to single and double-stranded DNA and exhibits DNA-dependent ATPase activity. Underwinds duplex DNA and forms helical nucleoprotein filaments. 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. Ref.6

Subunit structure

Forms linear homooligomers, giving rise to a RAD51 nucleoprotein filament, which is essential for strand-pairing reactions during DNA recombination. Interacts with BRCA1 and either directly or indirectly with p53. Interacts with XRCC3, RAD54L and RAD54B. Interacts with the BCDX2 subcomplex RAD51C:RAD51B. Interacts directly with PALB2 which may serve as a scaffold for a HR complex containing PALB2, BRCA2, RAD51C, RAD51 and XRCC3. Interacts with RAD51AP1 and RAD51AP2. Interacts with CHEK1, and this may require prior phosphorylation of CHEK1. Interacts with the MND1-PSMC3IP heterodimer. Found in a complex, at least composed of BLM, RAD51 and SPIDR; the complex formation is mediated by SPIDR. Interacts with SPIDR; the interaction is direct and recruits RAD51 to DNA damage sites. Interacts with FIGNL1 (via N-terminus one-half region); the interaction is direct. Interacts with RAD51AP1 (via C-terminus region); the interaction is direct. Interacts with NABP2, RPA1, PALB2 and RAD51. Interacts with SWI5/C9orf119, and at lower level with SFR1/MEIR5. Interacts with hyperphosphorylated RPA2; this interaction is necessary for efficient recruitment to chromatin in response to DNA damage. Interacts with SWSAP1; involved in homologous recombination repair. Interacts with PARPBP, BRCA2 and RECQL5; these interactions interfere with the formation of the RAD51-DNA homologous recombination structure. Ref.6 Ref.7

Subcellular location

Nucleus. Cytoplasm By similarity. Cytoplasmperinuclear region By similarity. Mitochondrion matrix By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Note: Colocalizes with RAD51AP1 and RPA2 to multiple nuclear foci upon induction of DNA damage. DNA damage induces an increase in nuclear levels. Together with FIGNL1, redistributed in discrete nuclear DNA damage-induced foci after ionizing radiation (IR) or camptothecin (CPT) treatment. Accumulated at sites of DNA damage in a SPIDR-dependent manner By similarity.

Tissue specificity

Expressed in ovary and testis. Expressed in the brain. Ref.8

Developmental stage

Expression in the brain is strongest at day E12, particularly in the cortical ventricular zone. In the cortex of newborn mice (P0), RAD51 is mainly present in the subplate and, in lesser amounts, in layer V. It is detected in a subpopulation of corticospinal axons at the pyramidal decussation in 2-day-old (P2) mice. Ref.8

Post-translational modification

Phosphorylated. Phosphorylation of Thr-309 by CHEK1 may enhance association with chromatin at sites of DNA damage and promote DNA repair by homologous recombination By similarity.

Miscellaneous

The nucleus of a mouse embryonic stem (ES) cells contains on average 4.7 x 105 molecules.

Sequence similarities

Belongs to the RecA family. RAD51 subfamily.

Contains 1 HhH domain.

Ontologies

Keywords
   Biological processDNA damage
DNA recombination
DNA repair
   Cellular componentCytoplasm
Cytoskeleton
Mitochondrion
Nucleus
   LigandATP-binding
DNA-binding
Nucleotide-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Traceable author statement PubMed 8816780. Source: UniProtKB

DNA unwinding involved in DNA replication

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to DNA damage stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to camptothecin

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to ionizing radiation

Inferred from sequence or structural similarity. Source: UniProtKB

double-strand break repair via homologous recombination

Inferred from direct assay PubMed 15359272. Source: MGI

meiotic nuclear division

Inferred from direct assay PubMed 10809667PubMed 12091911. Source: MGI

positive regulation of DNA ligation

Inferred from electronic annotation. Source: Ensembl

protein homooligomerization

Inferred from electronic annotation. Source: Ensembl

reciprocal meiotic recombination

Traceable author statement PubMed 8816780. Source: UniProtKB

regulation of double-strand break repair via homologous recombination

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentPML body

Inferred from electronic annotation. Source: Ensembl

condensed chromosome

Inferred from direct assay PubMed 10809667PubMed 12091911PubMed 12591952PubMed 12913077PubMed 17291760. Source: MGI

condensed nuclear chromosome

Inferred from direct assay PubMed 14668445PubMed 18283110PubMed 20551173PubMed 22164254PubMed 23555294. Source: MGI

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

lateral element

Inferred from direct assay PubMed 18694567PubMed 21743440. Source: MGI

mitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear chromosome

Inferred from sequence or structural similarity. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 8816780. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

synaptonemal complex

Traceable author statement PubMed 8816780. Source: UniProtKB

   Molecular_functionATP binding

Inferred from sequence orthology PubMed 16428451. Source: MGI

damaged DNA binding

Inferred from electronic annotation. Source: InterPro

double-stranded DNA binding

Inferred from electronic annotation. Source: Ensembl

single-stranded DNA binding

Inferred from electronic annotation. Source: Ensembl

single-stranded DNA-dependent ATPase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 339338DNA repair protein RAD51 homolog 1
PRO_0000122933

Regions

Domain48 – 7730HhH
Nucleotide binding127 – 1348ATP By similarity
Region184 – 25774Interaction with PALB2 By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue541Phosphotyrosine; by ABL1 By similarity
Modified residue3091Phosphothreonine; by CHEK1 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q08297 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: CE631E2C246BA481

FASTA33936,971
        10         20         30         40         50         60 
MAMQMQLEAS ADTSVEEESF GPQPISRLEQ CGINANDVKK LEEAGYHTVE AVAYAPKKEL 

        70         80         90        100        110        120 
INIKGISEAK ADKILTEAAK LVPMGFTTAT EFHQRRSEII QITTGSKELD KLLQGGIETG 

       130        140        150        160        170        180 
SITEMFGEFR TGKTQICHTL AVTCQLPIDR GGGEGKAMYI DTEGTFRPER LLAVAERYGL 

       190        200        210        220        230        240 
SGSDVLDNVA YARGFNTDHQ TQLLYQASAM MVESRYALLI VDSATALYRT DYSGRGELSA 

       250        260        270        280        290        300 
RQMHLARFLR MLLRLADEFG VAVVITNQVV AQVDGAAMFA ADPKKPIGGN IIAHASTTRL 

       310        320        330 
YLRKGRGETR ICKIYDSPCL PEAEAMFAIN ADGVGDAKD 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of human, mouse and fission yeast recombination genes homologous to RAD51 and recA."
Shinohara A., Ogawa H., Matsuda Y., Ushio N., Ikeo K., Ogawa T.
Nat. Genet. 4:239-243(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"A mouse homolog of the Escherichia coli recA and Saccharomyces cerevisiae RAD51 genes."
Morita T., Yoshimura Y., Yamamoto A., Murata K., Mori M., Yamamoto H., Matsushiro A.
Proc. Natl. Acad. Sci. U.S.A. 90:6577-6580(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Bone marrow.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary gland.
[5]"Analysis of mouse Rad54 expression and its implications for homologous recombination."
Essers J., Hendriks R.W., Wesoly J., Beerens C.E.M.T., Smit B., Hoeijmakers J.H.J., Wyman C., Dronkert M.L.G., Kanaar R.
DNA Repair 1:779-793(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION.
[6]"The Hop2 and Mnd1 proteins act in concert with Rad51 and Dmc1 in meiotic recombination."
Petukhova G.V., Pezza R.J., Vanevski F., Ploquin M., Masson J.-Y., Camerini-Otero R.D.
Nat. Struct. Mol. Biol. 12:449-453(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MND1-PSMC3IP HETERODIMER.
[7]"Role for the mammalian Swi5-Sfr1 complex in DNA strand break repair through homologous recombination."
Akamatsu Y., Jasin M.
PLoS Genet. 6:E1001160-E1001160(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SWI5.
[8]"RAD51 haploinsufficiency causes congenital mirror movements in humans."
Depienne C., Bouteiller D., Meneret A., Billot S., Groppa S., Klebe S., Charbonnier-Beaupel F., Corvol J.C., Saraiva J.P., Brueggemann N., Bhatia K., Cincotta M., Brochard V., Flamand-Roze C., Carpentier W., Meunier S., Marie Y., Gaussen M. expand/collapse author list , Stevanin G., Wehrle R., Vidailhet M., Klein C., Dusart I., Brice A., Roze E.
Am. J. Hum. Genet. 90:301-307(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D13473 mRNA. Translation: BAA02718.1.
D13803 mRNA. Translation: BAA02961.1.
AK011242 mRNA. Translation: BAB27489.1.
AK076468 mRNA. Translation: BAC36357.1.
AK151157 mRNA. Translation: BAE30162.1.
AK151177 mRNA. Translation: BAE30179.1.
BC027384 mRNA. Translation: AAH27384.1.
PIRA48221.
RefSeqNP_035364.1. NM_011234.4.
UniGeneMm.330492.

3D structure databases

ProteinModelPortalQ08297.
SMRQ08297. Positions 16-339.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202564. 5 interactions.
IntActQ08297. 1 interaction.
MINTMINT-205669.

Chemistry

ChEMBLCHEMBL2034808.

PTM databases

PhosphoSiteQ08297.

Proteomic databases

PaxDbQ08297.
PRIDEQ08297.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028795; ENSMUSP00000028795; ENSMUSG00000027323.
GeneID19361.
KEGGmmu:19361.
UCSCuc008ltd.1. mouse.

Organism-specific databases

CTD5888.
MGIMGI:97890. Rad51.

Phylogenomic databases

eggNOGCOG0468.
GeneTreeENSGT00750000117750.
HOGENOMHOG000227426.
HOVERGENHBG001504.
InParanoidQ08297.
KOK04482.
OMAMMAESRY.
PhylomeDBQ08297.
TreeFamTF101218.

Enzyme and pathway databases

ReactomeREACT_198624. Meiosis.
REACT_27235. Meiotic Recombination.

Gene expression databases

ArrayExpressQ08297.
BgeeQ08297.
CleanExMM_RAD51.
GenevestigatorQ08297.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR011941. DNA_recomb/repair_Rad51.
IPR013632. DNA_recomb/repair_Rad51_C.
IPR016467. DNA_recomb/repair_RecA-like.
IPR010995. DNA_repair_Rad51/TF_NusA_a-hlx.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR027417. P-loop_NTPase.
IPR020588. RecA_ATP-bd.
IPR020587. RecA_monomer-monomer_interface.
[Graphical view]
PANTHERPTHR22942:SF12. PTHR22942:SF12. 1 hit.
PfamPF08423. Rad51. 1 hit.
[Graphical view]
PIRSFPIRSF005856. Rad51. 1 hit.
SMARTSM00382. AAA. 1 hit.
SM00278. HhH1. 1 hit.
[Graphical view]
SUPFAMSSF47794. SSF47794. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR02239. recomb_RAD51. 1 hit.
PROSITEPS50162. RECA_2. 1 hit.
PS50163. RECA_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio296421.
PROQ08297.
SOURCESearch...

Entry information

Entry nameRAD51_MOUSE
AccessionPrimary (citable) accession number: Q08297
Secondary accession number(s): Q3UAY5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: April 16, 2014
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot