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Protein

DNA repair protein RAD51 homolog 1

Gene

Rad51

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 XRCC3.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi127 – 1348ATPBy similarity

GO - Molecular functioni

GO - Biological processi

  • cellular response to alkaloid Source: MGI
  • cellular response to camptothecin Source: UniProtKB
  • cellular response to DNA damage stimulus Source: UniProtKB
  • cellular response to hydroxyurea Source: MGI
  • cellular response to ionizing radiation Source: UniProtKB
  • chromosome organization involved in meiosis Source: MGI
  • DNA repair Source: UniProtKB
  • DNA unwinding involved in DNA replication Source: UniProtKB
  • double-strand break repair via homologous recombination Source: MGI
  • meiotic nuclear division Source: MGI
  • positive regulation of DNA ligation Source: MGI
  • protein homooligomerization Source: MGI
  • reciprocal meiotic recombination Source: UniProtKB
  • regulation of double-strand break repair via homologous recombination Source: UniProtKB
  • regulation of protein phosphorylation Source: MGI
  • replication-born double-strand break repair via sister chromatid exchange Source: MGI
  • replication fork processing Source: MGI
  • telomere organization Source: MGI
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_27235. Meiotic Recombination.
REACT_298118. Assembly of the RAD51-ssDNA nucleoprotein complex.
REACT_301691. Presynaptic phase of homologous DNA pairing and strand exchange.
REACT_309945. Meiotic recombination.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA repair protein RAD51 homolog 1
Alternative name(s):
RAD51 homolog A
Gene namesi
Name:Rad51
Synonyms:Rad51a, Reca
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:97890. Rad51.

Subcellular locationi

GO - Cellular componenti

  • condensed chromosome Source: MGI
  • condensed nuclear chromosome Source: MGI
  • cytoplasm Source: UniProtKB
  • lateral element Source: MGI
  • microtubule organizing center Source: UniProtKB-SubCell
  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
  • nuclear chromosome Source: UniProtKB
  • nucleolus Source: MGI
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • PML body Source: MGI
  • synaptonemal complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 339338DNA repair protein RAD51 homolog 1PRO_0000122933Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei54 – 541Phosphotyrosine; by ABL1By similarity
Modified residuei309 – 3091Phosphothreonine; by CHEK1By similarity

Post-translational modificationi

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).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ08297.
PaxDbiQ08297.
PRIDEiQ08297.

PTM databases

PhosphoSiteiQ08297.

Expressioni

Tissue specificityi

Expressed in ovary and testis. Expressed in the brain.1 Publication

Developmental stagei

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.1 Publication

Gene expression databases

BgeeiQ08297.
CleanExiMM_RAD51.
ExpressionAtlasiQ08297. baseline and differential.
GenevisibleiQ08297. MM.

Interactioni

Subunit structurei

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 (By similarity). Interacts with the MND1-PSMC3IP heterodimer (PubMed:15834424). 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-terminal one-half region); the interaction is direct. Interacts with RAD51AP1 (via C-terminal region); the interaction is direct (By similarity). Interacts with NABP2, RPA1, PALB2 and RAD51. Interacts with SWI5/C9orf119, and at lower level with SFR1/MEIR5 (PubMed:20976249). 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. Interacts with POLQ; POLQ acts as an inhibitor of homology-recombination repair (HR) pathway by limiting RAD51 accumulation at resected ends (By similarity).By similarity2 Publications

Protein-protein interaction databases

BioGridi202564. 5 interactions.
IntActiQ08297. 1 interaction.
MINTiMINT-205669.
STRINGi10090.ENSMUSP00000028795.

Structurei

3D structure databases

ProteinModelPortaliQ08297.
SMRiQ08297. Positions 16-339.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini48 – 7730HhHAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni184 – 25774Interaction with PALB2By similarityAdd
BLAST

Sequence similaritiesi

Belongs to the RecA family. RAD51 subfamily.Curated
Contains 1 HhH domain.Curated

Phylogenomic databases

eggNOGiCOG0468.
GeneTreeiENSGT00770000120539.
HOGENOMiHOG000227426.
HOVERGENiHBG001504.
InParanoidiQ08297.
KOiK04482.
OMAiCQLPIDQ.
PhylomeDBiQ08297.
TreeFamiTF101218.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. 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]
PfamiPF08423. Rad51. 1 hit.
[Graphical view]
PIRSFiPIRSF005856. Rad51. 1 hit.
SMARTiSM00382. AAA. 1 hit.
SM00278. HhH1. 1 hit.
[Graphical view]
SUPFAMiSSF47794. SSF47794. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR02239. recomb_RAD51. 1 hit.
PROSITEiPS50162. RECA_2. 1 hit.
PS50163. RECA_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q08297-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMQMQLEAS ADTSVEEESF GPQPISRLEQ CGINANDVKK LEEAGYHTVE
60 70 80 90 100
AVAYAPKKEL INIKGISEAK ADKILTEAAK LVPMGFTTAT EFHQRRSEII
110 120 130 140 150
QITTGSKELD KLLQGGIETG SITEMFGEFR TGKTQICHTL AVTCQLPIDR
160 170 180 190 200
GGGEGKAMYI DTEGTFRPER LLAVAERYGL SGSDVLDNVA YARGFNTDHQ
210 220 230 240 250
TQLLYQASAM MVESRYALLI VDSATALYRT DYSGRGELSA RQMHLARFLR
260 270 280 290 300
MLLRLADEFG VAVVITNQVV AQVDGAAMFA ADPKKPIGGN IIAHASTTRL
310 320 330
YLRKGRGETR ICKIYDSPCL PEAEAMFAIN ADGVGDAKD
Length:339
Mass (Da):36,971
Last modified:October 1, 1994 - v1
Checksum:iCE631E2C246BA481
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS16590.1.
PIRiA48221.
RefSeqiNP_035364.1. NM_011234.4.
UniGeneiMm.330492.

Genome annotation databases

EnsembliENSMUST00000028795; ENSMUSP00000028795; ENSMUSG00000027323.
GeneIDi19361.
KEGGimmu:19361.
UCSCiuc008ltd.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS16590.1.
PIRiA48221.
RefSeqiNP_035364.1. NM_011234.4.
UniGeneiMm.330492.

3D structure databases

ProteinModelPortaliQ08297.
SMRiQ08297. Positions 16-339.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202564. 5 interactions.
IntActiQ08297. 1 interaction.
MINTiMINT-205669.
STRINGi10090.ENSMUSP00000028795.

Chemistry

ChEMBLiCHEMBL2034808.

PTM databases

PhosphoSiteiQ08297.

Proteomic databases

MaxQBiQ08297.
PaxDbiQ08297.
PRIDEiQ08297.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028795; ENSMUSP00000028795; ENSMUSG00000027323.
GeneIDi19361.
KEGGimmu:19361.
UCSCiuc008ltd.1. mouse.

Organism-specific databases

CTDi5888.
MGIiMGI:97890. Rad51.

Phylogenomic databases

eggNOGiCOG0468.
GeneTreeiENSGT00770000120539.
HOGENOMiHOG000227426.
HOVERGENiHBG001504.
InParanoidiQ08297.
KOiK04482.
OMAiCQLPIDQ.
PhylomeDBiQ08297.
TreeFamiTF101218.

Enzyme and pathway databases

ReactomeiREACT_27235. Meiotic Recombination.
REACT_298118. Assembly of the RAD51-ssDNA nucleoprotein complex.
REACT_301691. Presynaptic phase of homologous DNA pairing and strand exchange.
REACT_309945. Meiotic recombination.

Miscellaneous databases

NextBioi296421.
PROiQ08297.
SOURCEiSearch...

Gene expression databases

BgeeiQ08297.
CleanExiMM_RAD51.
ExpressionAtlasiQ08297. baseline and differential.
GenevisibleiQ08297. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. 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]
PfamiPF08423. Rad51. 1 hit.
[Graphical view]
PIRSFiPIRSF005856. Rad51. 1 hit.
SMARTiSM00382. AAA. 1 hit.
SM00278. HhH1. 1 hit.
[Graphical view]
SUPFAMiSSF47794. SSF47794. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR02239. recomb_RAD51. 1 hit.
PROSITEiPS50162. RECA_2. 1 hit.
PS50163. RECA_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiRAD51_MOUSE
AccessioniPrimary (citable) accession number: Q08297
Secondary accession number(s): Q3UAY5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: June 24, 2015
This is version 154 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.