Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q08297

- RAD51_MOUSE

UniProt

Q08297 - RAD51_MOUSE

Protein

DNA repair protein RAD51 homolog 1

Gene

Rad51

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 1 (01 Oct 1994)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    1. ATP binding Source: MGI
    2. damaged DNA binding Source: InterPro
    3. double-stranded DNA binding Source: Ensembl
    4. protein binding Source: UniProtKB
    5. single-stranded DNA binding Source: Ensembl
    6. single-stranded DNA-dependent ATPase activity Source: Ensembl

    GO - Biological processi

    1. cellular response to camptothecin Source: UniProtKB
    2. cellular response to DNA damage stimulus Source: UniProtKB
    3. cellular response to ionizing radiation Source: UniProtKB
    4. DNA repair Source: UniProtKB
    5. DNA unwinding involved in DNA replication Source: UniProtKB
    6. double-strand break repair via homologous recombination Source: MGI
    7. meiotic nuclear division Source: MGI
    8. positive regulation of DNA ligation Source: Ensembl
    9. protein homooligomerization Source: Ensembl
    10. reciprocal meiotic recombination Source: UniProtKB
    11. regulation of double-strand break repair via homologous recombination Source: UniProtKB

    Keywords - Biological processi

    DNA damage, DNA recombination, DNA repair

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_198629. Meiotic recombination.
    REACT_27235. 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: Chromosome 2

    Organism-specific databases

    MGIiMGI:97890. Rad51.

    Subcellular locationi

    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.By similarity

    GO - Cellular componenti

    1. condensed chromosome Source: MGI
    2. condensed nuclear chromosome Source: MGI
    3. cytoplasm Source: UniProtKB
    4. lateral element Source: MGI
    5. microtubule organizing center Source: UniProtKB-SubCell
    6. mitochondrial matrix Source: UniProtKB-SubCell
    7. nuclear chromosome Source: UniProtKB
    8. nucleoplasm Source: Reactome
    9. nucleus Source: UniProtKB
    10. perinuclear region of cytoplasm Source: UniProtKB
    11. PML body Source: Ensembl
    12. synaptonemal complex Source: UniProtKB

    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

    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

    ArrayExpressiQ08297.
    BgeeiQ08297.
    CleanExiMM_RAD51.
    GenevestigatoriQ08297.

    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. 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-terminal one-half region); the interaction is direct. Interacts with RAD51AP1 (via C-terminal 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.2 Publications

    Protein-protein interaction databases

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

    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.
    GeneTreeiENSGT00750000117750.
    HOGENOMiHOG000227426.
    HOVERGENiHBG001504.
    InParanoidiQ08297.
    KOiK04482.
    OMAiMMAESRY.
    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

    MAMQMQLEAS ADTSVEEESF GPQPISRLEQ CGINANDVKK LEEAGYHTVE    50
    AVAYAPKKEL INIKGISEAK ADKILTEAAK LVPMGFTTAT EFHQRRSEII 100
    QITTGSKELD KLLQGGIETG SITEMFGEFR TGKTQICHTL AVTCQLPIDR 150
    GGGEGKAMYI DTEGTFRPER LLAVAERYGL SGSDVLDNVA YARGFNTDHQ 200
    TQLLYQASAM MVESRYALLI VDSATALYRT DYSGRGELSA RQMHLARFLR 250
    MLLRLADEFG VAVVITNQVV AQVDGAAMFA ADPKKPIGGN IIAHASTTRL 300
    YLRKGRGETR ICKIYDSPCL PEAEAMFAIN ADGVGDAKD 339
    Length:339
    Mass (Da):36,971
    Last modified:October 1, 1994 - v1
    Checksum:iCE631E2C246BA481
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS16590.1.
    PIRi A48221.
    RefSeqi NP_035364.1. NM_011234.4.
    UniGenei Mm.330492.

    3D structure databases

    ProteinModelPortali Q08297.
    SMRi Q08297. Positions 16-339.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202564. 5 interactions.
    IntActi Q08297. 1 interaction.
    MINTi MINT-205669.

    Chemistry

    ChEMBLi CHEMBL2034808.

    PTM databases

    PhosphoSitei Q08297.

    Proteomic databases

    PaxDbi Q08297.
    PRIDEi Q08297.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000028795 ; ENSMUSP00000028795 ; ENSMUSG00000027323 .
    GeneIDi 19361.
    KEGGi mmu:19361.
    UCSCi uc008ltd.1. mouse.

    Organism-specific databases

    CTDi 5888.
    MGIi MGI:97890. Rad51.

    Phylogenomic databases

    eggNOGi COG0468.
    GeneTreei ENSGT00750000117750.
    HOGENOMi HOG000227426.
    HOVERGENi HBG001504.
    InParanoidi Q08297.
    KOi K04482.
    OMAi MMAESRY.
    PhylomeDBi Q08297.
    TreeFami TF101218.

    Enzyme and pathway databases

    Reactomei REACT_198629. Meiotic recombination.
    REACT_27235. Meiotic Recombination.

    Miscellaneous databases

    NextBioi 296421.
    PROi Q08297.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q08297.
    Bgeei Q08297.
    CleanExi MM_RAD51.
    Genevestigatori Q08297.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR003593. 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 ]
    Pfami PF08423. Rad51. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005856. Rad51. 1 hit.
    SMARTi SM00382. AAA. 1 hit.
    SM00278. HhH1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47794. SSF47794. 1 hit.
    SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR02239. recomb_RAD51. 1 hit.
    PROSITEi PS50162. RECA_2. 1 hit.
    PS50163. RECA_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 146 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