Q08297 (RAD51_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA repair protein RAD51 homolog 1

Alternative name(s):
RAD51 homolog A

Gene names

Name:	Rad51
Synonyms:	Rad51a, Reca

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	339 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51C and XRCC3 By similarity. Ref.6
Subunit structure	Interacts with BRCA1, BRCA2 and either directly or indirectly with p53. Interacts with XRCC3, RAD54L and RAD54B. Part of a complex with RAD51C and RAD51B. Interacts with RAD51AP1 and RAD51AP2. Interacts with CHEK1, and this may require prior phosphorylation of CHEK1 By similarity. Interacts with the MND1-PSMC3IP heterodimer. Interacts with NABP2 By similarity. Interacts with RPA1, PALB2 and RAD51 By similarity. Interacts with hyperphosphorylated RPA2; this interaction is necessary for efficient recruitment to chromatin in response to DNA damage By similarity. Interacts with SWSAP1; involved in homologous recombination repair. Interacts with PARPBP; interfering with the formation of the RAD51-DNA homologous recombination structure By similarity. Interacts with SWI5/SAE3, and at lower level with SFR1/MEIR5. Ref.6 Ref.7
Subcellular location	Nucleus By similarity. Cytoplasm By similarity. Cytoplasm › perinuclear region By similarity. Mitochondrion matrix 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 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 process	DNA damage DNA recombination DNA repair
Cellular component	Cytoplasm Mitochondrion Nucleus
Ligand	ATP-binding DNA-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA unwinding involved in replication Inferred from sequence or structural similarity. Source: UniProtKB double-strand break repair via homologous recombination Inferred from direct assay PubMed 15359272. Source: MGI positive regulation of DNA ligation Inferred from electronic annotation. Source: Compara protein homooligomerization Inferred from electronic annotation. Source: Compara reciprocal meiotic recombination Traceable author statement PubMed 8816780. Source: UniProtKB
Cellular_component	PML body Inferred from electronic annotation. Source: Compara lateral element Inferred from direct assay PubMed 18694567PubMed 21743440. Source: MGI mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Traceable author statement. Source: Reactome perinuclear region of cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP 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: Compara single-stranded DNA binding Inferred from electronic annotation. Source: Compara single-stranded DNA-dependent ATPase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 339	339	DNA repair protein RAD51 homolog 1		PRO_0000122933
Regions
	Domain	48 – 77	30	HhH
	Nucleotide binding	127 – 134	8	ATP By similarity
	Region	184 – 257	74	Interaction with PALB2 By similarity
Amino acid modifications
	Modified residue	54	1	Phosphotyrosine; by ABL1 By similarity
	Modified residue	309	1	Phosphothreonine; by CHEK1 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q08297 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: CE631E2C246BA481	FASTA	339	36,971
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI00118524.
PIR	A48221.
RefSeq	NP_035364.1. NM_011234.4.
UniGene	Mm.330492.
3D structure databases
ProteinModelPortal	Q08297.
SMR	Q08297. Positions 16-339.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q08297. 1 interaction.
MINT	MINT-205669.
PTM databases
PhosphoSite	Q08297.
Proteomic databases
PaxDb	Q08297.
PRIDE	Q08297.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000028795; ENSMUSP00000028795; ENSMUSG00000027323.
GeneID	19361.
KEGG	mmu:19361.
Organism-specific databases
CTD	5888.
MGI	MGI:97890. Rad51.
Phylogenomic databases
eggNOG	COG0468.
GeneTree	ENSGT00550000074609.
HOGENOM	HOG000227426.
HOVERGEN	HBG001504.
InParanoid	Q08297.
KO	K04482.
OMA	MMAESRY.
OrthoDB	EOG47H5QB.
Enzyme and pathway databases
Reactome	REACT_120463. Meiosis. REACT_27235. Meiotic Recombination (mouse).
Gene expression databases
ArrayExpress	Q08297.
Bgee	Q08297.
CleanEx	MM_RAD51.
Genevestigator	Q08297.
GermOnline	ENSMUSG00000027323. Mus musculus.
Family and domain databases
InterPro	IPR003593. AAA+_ATPase. IPR011941. DNA_recomb/repair_Rad51. IPR013632. DNA_recomb/repair_Rad51_C. IPR016467. DNA_recomb/repair_RecA-like. IPR020588. DNA_recomb_RecA/RadB_ATP-bd. IPR010995. DNA_repair_Rad51/TF_NusA_a-hlx. IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif. IPR020587. RecA_monomer-monomer_interface. [Graphical view]
PANTHER	PTHR22942:SF12. PTHR22942:SF12. 1 hit.
Pfam	PF08423. Rad51. 1 hit. [Graphical view]
PIRSF	PIRSF005856. Rad51. 1 hit.
SMART	SM00382. AAA. 1 hit. SM00278. HhH1. 1 hit. [Graphical view]
SUPFAM	SSF47794. Rad51_N. 1 hit.
TIGRFAMs	TIGR02239. recomb_RAD51. 1 hit.
PROSITE	PS50162. RECA_2. 1 hit. PS50163. RECA_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	296421.
SOURCE	Search...

Entry information

Entry name

RAD51_MOUSE

Accession

Primary (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 3, 2013
This is version 131 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program