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O55230

- RA51D_MOUSE

UniProt

O55230 - RA51D_MOUSE

Protein

DNA repair protein RAD51 homolog 4

Gene

Rad51d

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
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    Functioni

    Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. Bind to single-stranded DNA (ssDNA) and has DNA-dependent ATPase activity. Part of the Rad21 paralog protein complex BCDX2 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 acts downstream of BRCA2 recruitment and upstream of RAD51 recruitment. BCDX2 binds predominantly to the intersection of the four duplex arms of the Holliday junction and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA. Involved in telomere maintenance. The BCDX2 subcomplex XRCC2:RAD51D can stimulate Holliday junction resolution by BLM By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi107 – 1148ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA-dependent ATPase activity Source: UniProtKB
    3. gamma-tubulin binding Source: UniProtKB
    4. single-stranded DNA binding Source: UniProtKB

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. double-strand break repair via homologous recombination Source: UniProtKB
    3. strand invasion Source: UniProtKB
    4. telomere maintenance Source: UniProtKB

    Keywords - Biological processi

    DNA damage, DNA recombination, DNA repair

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA repair protein RAD51 homolog 4
    Alternative name(s):
    R51H3
    RAD51 homolog D
    RAD51-like protein 3
    Gene namesi
    Name:Rad51d
    Synonyms:R51h3, Rad51l3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:1261809. Rad51d.

    Subcellular locationi

    Nucleus By similarity. Chromosometelomere 1 Publication

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. chromosome, telomeric region Source: UniProtKB
    3. Rad51B-Rad51C-Rad51D-XRCC2 complex Source: UniProtKB
    4. replication fork Source: UniProtKB

    Keywords - Cellular componenti

    Chromosome, Nucleus, Telomere

    Pathology & Biotechi

    Disruption phenotypei

    Midgestation lethal.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 329329DNA repair protein RAD51 homolog 4PRO_0000122943Add
    BLAST

    Proteomic databases

    PRIDEiO55230.

    PTM databases

    PhosphoSiteiO55230.

    Expressioni

    Tissue specificityi

    Highly expressed in brain followed by testis. Also expressed in heart, liver, kidney, spleen, lung and skeletal muscle.

    Gene expression databases

    ArrayExpressiO55230.
    BgeeiO55230.
    CleanExiMM_RAD51L3.
    GenevestigatoriO55230.

    Interactioni

    Subunit structurei

    Part of the BCDX2 complex consisting of RAD51B, RAD51C, RAD51D and XRCC2; the complex has a ring-like structure arranged into a flat disc around a central channel. In the absence of DNA, the BCDX2 subcomplex XRCC2:RAD51D formed a multimeric ring structure; in the presence of single-stranded DNA it formed a filamentous structure with the ssDNA. Interacts with SWSAP1 and ZSWIM7; involved in homologous recombination repair. Interacts with BLM; required for stimulation of BLM activity by the BCDX2 subcomplex XRCC2:RAD51D By similarity.By similarity

    Protein-protein interaction databases

    IntActiO55230. 1 interaction.
    MINTiMINT-415416.

    Structurei

    3D structure databases

    ProteinModelPortaliO55230.
    SMRiO55230. Positions 1-319.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 8383Preferencially binds ssDNABy similarityAdd
    BLAST
    Regioni4 – 7774Interaction with XRCC2Add
    BLAST
    Regioni77 – 328252Interaction with RAD51CAdd
    BLAST

    Sequence similaritiesi

    Belongs to the RecA family. RAD51 subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG0468.
    HOGENOMiHOG000049134.
    HOVERGENiHBG057455.
    InParanoidiO55230.
    KOiK10871.
    OMAiCSLSYKA.
    PhylomeDBiO55230.
    TreeFamiTF101219.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR003593. AAA+_ATPase.
    IPR013632. DNA_recomb/repair_Rad51_C.
    IPR016467. DNA_recomb/repair_RecA-like.
    IPR027417. P-loop_NTPase.
    IPR020588. RecA_ATP-bd.
    [Graphical view]
    PfamiPF08423. Rad51. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005856. Rad51. 1 hit.
    SMARTiSM00382. AAA. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS50162. RECA_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    This entry describes 1 isoform i produced by alternative splicing. Align

    Note: At least 2 isoforms are produced.

    Isoform 1 (identifier: O55230-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGMLRAGLCP GLTEETVQLL RGRKIKTVAD LAAADLEEVA QKCGLSYKAL    50
    VALRRVLLAQ FSAFPLNGAD LYEELKTSTA ILSTGIGSLD KLLDAGLYTG 100
    EVTEIVGGPG SGKTQVCLCV AANVAHSLQQ NVLYVDSNGG MTASRLLQLL 150
    QARTQDEEKQ ASALQRIQVV RSFDIFRMLD MLQDLRGTIA QQEATSSGAV 200
    KVVIVDSVTA VVAPLLGGQQ REGLALMMQL ARELKILARD LGVAVVVTNH 250
    LTRDWDGRRF KPALGRSWSF VPSTRILLDV TEGAGTLGSS QRTVCLTKSP 300
    RQPTGLQEMI DIGTLGTEEQ SPELPGKQT 329
    Length:329
    Mass (Da):35,260
    Last modified:June 1, 1998 - v1
    Checksum:i6E463822408EF484
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB007040 mRNA. Translation: BAA24010.1.
    AF034955 mRNA. Translation: AAC40093.1.
    Y15570 mRNA. Translation: CAA75679.1.
    AK017835 mRNA. Translation: BAB30965.1.
    BC049136 mRNA. Translation: AAH49136.1.
    CCDSiCCDS36250.1. [O55230-1]
    RefSeqiNP_035365.1. NM_011235.4. [O55230-1]
    UniGeneiMm.441571.
    Mm.9286.

    Genome annotation databases

    EnsembliENSMUST00000018985; ENSMUSP00000018985; ENSMUSG00000018841. [O55230-1]
    GeneIDi19364.
    KEGGimmu:19364.
    UCSCiuc007knm.1. mouse. [O55230-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB007040 mRNA. Translation: BAA24010.1 .
    AF034955 mRNA. Translation: AAC40093.1 .
    Y15570 mRNA. Translation: CAA75679.1 .
    AK017835 mRNA. Translation: BAB30965.1 .
    BC049136 mRNA. Translation: AAH49136.1 .
    CCDSi CCDS36250.1. [O55230-1 ]
    RefSeqi NP_035365.1. NM_011235.4. [O55230-1 ]
    UniGenei Mm.441571.
    Mm.9286.

    3D structure databases

    ProteinModelPortali O55230.
    SMRi O55230. Positions 1-319.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O55230. 1 interaction.
    MINTi MINT-415416.

    PTM databases

    PhosphoSitei O55230.

    Proteomic databases

    PRIDEi O55230.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000018985 ; ENSMUSP00000018985 ; ENSMUSG00000018841 . [O55230-1 ]
    GeneIDi 19364.
    KEGGi mmu:19364.
    UCSCi uc007knm.1. mouse. [O55230-1 ]

    Organism-specific databases

    CTDi 5892.
    MGIi MGI:1261809. Rad51d.

    Phylogenomic databases

    eggNOGi COG0468.
    HOGENOMi HOG000049134.
    HOVERGENi HBG057455.
    InParanoidi O55230.
    KOi K10871.
    OMAi CSLSYKA.
    PhylomeDBi O55230.
    TreeFami TF101219.

    Miscellaneous databases

    NextBioi 296433.
    PROi O55230.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O55230.
    Bgeei O55230.
    CleanExi MM_RAD51L3.
    Genevestigatori O55230.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR003593. AAA+_ATPase.
    IPR013632. DNA_recomb/repair_Rad51_C.
    IPR016467. DNA_recomb/repair_RecA-like.
    IPR027417. P-loop_NTPase.
    IPR020588. RecA_ATP-bd.
    [Graphical view ]
    Pfami PF08423. Rad51. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005856. Rad51. 1 hit.
    SMARTi SM00382. AAA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    PROSITEi PS50162. RECA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification, characterization, and genetic mapping of Rad51d, a new mouse and human RAD51/RecA-related gene."
      Pittman D.L., Weinberg L.R., Schimenti J.C.
      Genomics 49:103-111(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
    2. "Isolation of novel human and mouse genes of the recA/RAD51 recombination-repair gene family."
      Cartwright R., Dunn A.M., Simpson P.J., Tambini C.E., Thacker J.
      Nucleic Acids Res. 26:1653-1659(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. Kawabata M.
      Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "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.
    5. "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: C57BL/6.
      Tissue: Brain.
    6. "Midgestation lethality in mice deficient for the RecA-related gene, Rad51d/Rad51l3."
      Pittman D.L., Schimenti J.C.
      Genesis 26:167-173(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    7. "Telomere maintenance requires the RAD51D recombination/repair protein."
      Tarsounas M., Munoz P., Claas A., Smiraldo P.G., Pittman D.L., Blasco M.A., West S.C.
      Cell 117:337-347(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    8. "Domain mapping of the Rad51 paralog protein complexes."
      Miller K.A., Sawicka D., Barsky D., Albala J.S.
      Nucleic Acids Res. 32:169-178(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAD51C AND XRCC2.

    Entry informationi

    Entry nameiRA51D_MOUSE
    AccessioniPrimary (citable) accession number: O55230
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 114 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    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