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Q06609

- RAD51_HUMAN

UniProt

Q06609 - RAD51_HUMAN

Protein

DNA repair protein RAD51 homolog 1

Gene

RAD51

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    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 XRCC3.8 Publications

    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. DNA polymerase binding Source: UniProt
    4. double-stranded DNA binding Source: UniProtKB
    5. identical protein binding Source: IntAct
    6. protein binding Source: UniProtKB
    7. protein C-terminus binding Source: UniProtKB
    8. single-stranded DNA binding Source: UniProtKB
    9. single-stranded DNA-dependent ATPase activity Source: UniProtKB

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. cellular response to camptothecin Source: UniProtKB
    3. cellular response to DNA damage stimulus Source: UniProtKB
    4. cellular response to ionizing radiation Source: UniProtKB
    5. DNA recombinase assembly Source: Reactome
    6. DNA recombination Source: UniProtKB
    7. DNA repair Source: Reactome
    8. DNA unwinding involved in DNA replication Source: UniProtKB
    9. double-strand break repair Source: Reactome
    10. double-strand break repair via homologous recombination Source: UniProtKB
    11. meiotic nuclear division Source: UniProtKB
    12. mitotic recombination Source: ProtInc
    13. positive regulation of DNA ligation Source: UniProtKB
    14. protein homooligomerization Source: UniProtKB
    15. reciprocal meiotic recombination Source: ProtInc
    16. 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_2141. Assembly of the RAD51-ssDNA nucleoprotein complex.
    REACT_27271. Meiotic recombination.
    REACT_408. Presynaptic phase of homologous DNA pairing and strand exchange.
    SignaLinkiQ06609.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA repair protein RAD51 homolog 1
    Short name:
    HsRAD51
    Short name:
    hRAD51
    Alternative name(s):
    RAD51 homolog A
    Gene namesi
    Name:RAD51
    Synonyms:RAD51A, RECA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:9817. RAD51.

    Subcellular locationi

    Nucleus. Cytoplasm. Cytoplasmperinuclear region. Mitochondrion matrix. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome
    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.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Mitochondrion, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Breast cancer (BC) [MIM:114480]: A common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti150 – 1501R → Q in BC; familial. 1 Publication
    Corresponds to variant rs121917739 [ dbSNP | Ensembl ].
    VAR_010899
    Mirror movements 2 (MRMV2) [MIM:614508]: A disorder characterized by contralateral involuntary movements that mirror voluntary ones. While mirror movements are occasionally found in young children, persistence beyond the age of 10 is abnormal. Mirror movements occur more commonly in the upper extremities.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi86 – 861F → A: Loss of homooligomerization. 1 Publication
    Mutagenesisi89 – 891A → E: Loss of homooligomerization. 1 Publication
    Mutagenesisi309 – 3091T → A: Confers hypersensitivity to hydroxyurea. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi114480. phenotype.
    614508. phenotype.
    Orphaneti238722. Familial congenital mirror movements.
    145. Hereditary breast and ovarian cancer syndrome.
    PharmGKBiPA34176.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 339338DNA repair protein RAD51 homolog 1PRO_0000122932Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei54 – 541Phosphotyrosine; by ABL11 Publication
    Modified residuei309 – 3091Phosphothreonine; by CHEK11 Publication

    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. Phosphorylation by ABL1 inhibits function.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ06609.
    PaxDbiQ06609.
    PRIDEiQ06609.

    PTM databases

    PhosphoSiteiQ06609.

    Miscellaneous databases

    PMAP-CutDBQ06609.

    Expressioni

    Tissue specificityi

    Highly expressed in testis and thymus, followed by small intestine, placenta, colon, pancreas and ovary. Weakly expressed in breast.

    Inductioni

    Stress-induced increase in the mitochondrial levels is seen.1 Publication

    Gene expression databases

    ArrayExpressiQ06609.
    BgeeiQ06609.
    CleanExiHS_RAD51.
    GenevestigatoriQ06609.

    Organism-specific databases

    HPAiCAB010381.
    HPA039310.

    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.22 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself5EBI-297202,EBI-297202
    BRCA2P5158736EBI-297202,EBI-79792
    CHEK1O147573EBI-297202,EBI-974488
    PALB2Q86YC25EBI-297202,EBI-1222653
    RAD51AP1Q96B01-24EBI-297202,EBI-1178743
    RAD51AP1Q96B01-35EBI-297202,EBI-1178748
    RAD51CO435026EBI-297202,EBI-2267048
    RAD52P433513EBI-297202,EBI-706448
    SWSAP1Q6NVH72EBI-297202,EBI-5281637
    TP53P046372EBI-297202,EBI-366083
    XRCC3O435423EBI-297202,EBI-2849976

    Protein-protein interaction databases

    BioGridi111825. 60 interactions.
    DIPiDIP-462N.
    IntActiQ06609. 37 interactions.
    MINTiMINT-1374477.
    STRINGi9606.ENSP00000267868.

    Structurei

    Secondary structure

    1
    339
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi25 – 306
    Helixi35 – 428
    Helixi49 – 513
    Beta strandi54 – 563
    Helixi57 – 615
    Turni62 – 654
    Helixi70 – 8112
    Helixi107 – 1126
    Turni113 – 1153
    Beta strandi116 – 1183
    Beta strandi121 – 1266
    Helixi133 – 14311
    Helixi148 – 1503
    Beta strandi154 – 16411
    Helixi168 – 17710
    Helixi182 – 1876
    Beta strandi189 – 1935
    Helixi197 – 21317
    Beta strandi216 – 2227
    Helixi226 – 2283
    Helixi238 – 25922
    Beta strandi262 – 2676
    Beta strandi298 – 3047
    Beta strandi309 – 3146
    Beta strandi323 – 3308
    Beta strandi333 – 3353

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B22NMR-A1-114[»]
    1N0WX-ray1.70A97-339[»]
    ProteinModelPortaliQ06609.
    SMRiQ06609. Positions 16-339.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ06609.

    Family & Domainsi

    Domains and Repeats

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

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni184 – 25774Interaction with PALB2Add
    BLAST

    Domaini

    The nuclear localization may reside in the C-terminus (between 259 and 339 AA).

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0468.
    HOGENOMiHOG000227426.
    HOVERGENiHBG001504.
    KOiK04482.
    OMAiMMAESRY.
    PhylomeDBiQ06609.
    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]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q06609-1) [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

    MAMQMQLEAN ADTSVEEESF GPQPISRLEQ CGINANDVKK LEEAGFHTVE    50
    AVAYAPKKEL INIKGISEAK ADKILAEAAK LVPMGFTTAT EFHQRRSEII 100
    QITTGSKELD KLLQGGIETG SITEMFGEFR TGKTQICHTL AVTCQLPIDR 150
    GGGEGKAMYI DTEGTFRPER LLAVAERYGL SGSDVLDNVA YARAFNTDHQ 200
    TQLLYQASAM MVESRYALLI VDSATALYRT DYSGRGELSA RQMHLARFLR 250
    MLLRLADEFG VAVVITNQVV AQVDGAAMFA ADPKKPIGGN IIAHASTTRL 300
    YLRKGRGETR ICKIYDSPCL PEAEAMFAIN ADGVGDAKD 339
    Length:339
    Mass (Da):36,966
    Last modified:June 1, 1994 - v1
    Checksum:i26578E6206DEDEDA
    GO
    Isoform 2 (identifier: Q06609-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         77-173: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:242
    Mass (Da):26,351
    Checksum:iDFA9E12DC8429CA2
    GO
    Isoform 3 (identifier: Q06609-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         259-284: FGVAVVITNQVVAQVDGAAMFAADPK → IVSEERKRGNQNLQNLRLSLSS
         285-339: Missing.

    Note: Mutagenesis of Arg-264 to Ala inhibits nuclear localization. Mutagenesis of Lys-264 to Gln inhibits nuclear localization. Deletion of 254-Arg-Lys-255 inhibits nuclear localization.

    Show »
    Length:280
    Mass (Da):31,001
    Checksum:i1DFA22F6C0926FC2
    GO
    Isoform 4 (identifier: Q06609-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         76-114: AEAAKLVPMG...GSKELDKLLQ → TESRSVARLE...ASASRVVGTT

    Note: No experimental confirmation available.

    Show »
    Length:340
    Mass (Da):36,780
    Checksum:iD8E2AAD35400FB04
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti313 – 3131K → Q in BAA02962. (PubMed:8358431)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti150 – 1501R → Q in BC; familial. 1 Publication
    Corresponds to variant rs121917739 [ dbSNP | Ensembl ].
    VAR_010899

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei76 – 11439AEAAK…DKLLQ → TESRSVARLECNSVILVYCT LRLSGSSDSPASASRVVGTT in isoform 4. 1 PublicationVSP_043655Add
    BLAST
    Alternative sequencei77 – 17397Missing in isoform 2. 1 PublicationVSP_005556Add
    BLAST
    Alternative sequencei259 – 28426FGVAV…AADPK → IVSEERKRGNQNLQNLRLSL SS in isoform 3. 1 PublicationVSP_041724Add
    BLAST
    Alternative sequencei285 – 33955Missing in isoform 3. 1 PublicationVSP_041725Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D13804 mRNA. Translation: BAA02962.1.
    D14134 mRNA. Translation: BAA03189.1.
    AF165094
    , AF165088, AF165089, AF165090, AF165091, AF165092, AF165093 Genomic DNA. Translation: AAD49705.1.
    AF233744
    , AF233740, AF233741, AF233742, AF236021, AF233743 Genomic DNA. Translation: AAF69145.1.
    EU362635 mRNA. Translation: ABY59731.1.
    AY196785 Genomic DNA. Translation: AAN87149.1.
    AK131299 mRNA. Translation: BAD18467.1.
    AK291969 mRNA. Translation: BAF84658.1.
    AK313503 mRNA. Translation: BAG36283.1.
    CR536559 mRNA. Translation: CAG38796.1.
    AC012476 Genomic DNA. No translation available.
    AC022405 Genomic DNA. No translation available.
    CH471125 Genomic DNA. Translation: EAW92434.1.
    CH471125 Genomic DNA. Translation: EAW92432.1.
    CH471125 Genomic DNA. Translation: EAW92435.1.
    BC001459 mRNA. Translation: AAH01459.1.
    CCDSiCCDS10062.1. [Q06609-1]
    CCDS53931.1. [Q06609-4]
    CCDS53932.1. [Q06609-3]
    PIRiI58295.
    RefSeqiNP_001157741.1. NM_001164269.1. [Q06609-4]
    NP_001157742.1. NM_001164270.1. [Q06609-3]
    NP_002866.2. NM_002875.4. [Q06609-1]
    NP_597994.3. NM_133487.3. [Q06609-4]
    XP_006720689.1. XM_006720626.1. [Q06609-1]
    UniGeneiHs.631709.

    Genome annotation databases

    EnsembliENST00000267868; ENSP00000267868; ENSG00000051180. [Q06609-1]
    ENST00000382643; ENSP00000372088; ENSG00000051180. [Q06609-4]
    ENST00000423169; ENSP00000406602; ENSG00000051180. [Q06609-3]
    ENST00000532743; ENSP00000433924; ENSG00000051180. [Q06609-4]
    ENST00000557850; ENSP00000454176; ENSG00000051180. [Q06609-2]
    GeneIDi5888.
    KEGGihsa:5888.
    UCSCiuc001zmi.4. human. [Q06609-1]
    uc001zml.4. human. [Q06609-4]
    uc010bbw.3. human. [Q06609-3]

    Polymorphism databases

    DMDMi548663.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D13804 mRNA. Translation: BAA02962.1 .
    D14134 mRNA. Translation: BAA03189.1 .
    AF165094
    , AF165088 , AF165089 , AF165090 , AF165091 , AF165092 , AF165093 Genomic DNA. Translation: AAD49705.1 .
    AF233744
    , AF233740 , AF233741 , AF233742 , AF236021 , AF233743 Genomic DNA. Translation: AAF69145.1 .
    EU362635 mRNA. Translation: ABY59731.1 .
    AY196785 Genomic DNA. Translation: AAN87149.1 .
    AK131299 mRNA. Translation: BAD18467.1 .
    AK291969 mRNA. Translation: BAF84658.1 .
    AK313503 mRNA. Translation: BAG36283.1 .
    CR536559 mRNA. Translation: CAG38796.1 .
    AC012476 Genomic DNA. No translation available.
    AC022405 Genomic DNA. No translation available.
    CH471125 Genomic DNA. Translation: EAW92434.1 .
    CH471125 Genomic DNA. Translation: EAW92432.1 .
    CH471125 Genomic DNA. Translation: EAW92435.1 .
    BC001459 mRNA. Translation: AAH01459.1 .
    CCDSi CCDS10062.1. [Q06609-1 ]
    CCDS53931.1. [Q06609-4 ]
    CCDS53932.1. [Q06609-3 ]
    PIRi I58295.
    RefSeqi NP_001157741.1. NM_001164269.1. [Q06609-4 ]
    NP_001157742.1. NM_001164270.1. [Q06609-3 ]
    NP_002866.2. NM_002875.4. [Q06609-1 ]
    NP_597994.3. NM_133487.3. [Q06609-4 ]
    XP_006720689.1. XM_006720626.1. [Q06609-1 ]
    UniGenei Hs.631709.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B22 NMR - A 1-114 [» ]
    1N0W X-ray 1.70 A 97-339 [» ]
    ProteinModelPortali Q06609.
    SMRi Q06609. Positions 16-339.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111825. 60 interactions.
    DIPi DIP-462N.
    IntActi Q06609. 37 interactions.
    MINTi MINT-1374477.
    STRINGi 9606.ENSP00000267868.

    Chemistry

    BindingDBi Q06609.
    ChEMBLi CHEMBL2034807.

    PTM databases

    PhosphoSitei Q06609.

    Polymorphism databases

    DMDMi 548663.

    Proteomic databases

    MaxQBi Q06609.
    PaxDbi Q06609.
    PRIDEi Q06609.

    Protocols and materials databases

    DNASUi 5888.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000267868 ; ENSP00000267868 ; ENSG00000051180 . [Q06609-1 ]
    ENST00000382643 ; ENSP00000372088 ; ENSG00000051180 . [Q06609-4 ]
    ENST00000423169 ; ENSP00000406602 ; ENSG00000051180 . [Q06609-3 ]
    ENST00000532743 ; ENSP00000433924 ; ENSG00000051180 . [Q06609-4 ]
    ENST00000557850 ; ENSP00000454176 ; ENSG00000051180 . [Q06609-2 ]
    GeneIDi 5888.
    KEGGi hsa:5888.
    UCSCi uc001zmi.4. human. [Q06609-1 ]
    uc001zml.4. human. [Q06609-4 ]
    uc010bbw.3. human. [Q06609-3 ]

    Organism-specific databases

    CTDi 5888.
    GeneCardsi GC15P040987.
    HGNCi HGNC:9817. RAD51.
    HPAi CAB010381.
    HPA039310.
    MIMi 114480. phenotype.
    179617. gene.
    614508. phenotype.
    neXtProti NX_Q06609.
    Orphaneti 238722. Familial congenital mirror movements.
    145. Hereditary breast and ovarian cancer syndrome.
    PharmGKBi PA34176.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0468.
    HOGENOMi HOG000227426.
    HOVERGENi HBG001504.
    KOi K04482.
    OMAi MMAESRY.
    PhylomeDBi Q06609.
    TreeFami TF101218.

    Enzyme and pathway databases

    Reactomei REACT_2141. Assembly of the RAD51-ssDNA nucleoprotein complex.
    REACT_27271. Meiotic recombination.
    REACT_408. Presynaptic phase of homologous DNA pairing and strand exchange.
    SignaLinki Q06609.

    Miscellaneous databases

    ChiTaRSi RAD51. human.
    EvolutionaryTracei Q06609.
    GeneWikii RAD51.
    GenomeRNAii 5888.
    NextBioi 22896.
    PMAP-CutDB Q06609.
    PROi Q06609.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q06609.
    Bgeei Q06609.
    CleanExi HS_RAD51.
    Genevestigatori Q06609.

    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] (ISOFORM 1).
    2. "Cloning and sequence of the human RecA-like gene cDNA."
      Yoshimura Y., Morita T., Yamamoto A., Matsushiro A.
      Nucleic Acids Res. 21:1665-1665(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Testis.
    3. "Characterization of the human Rad51 genomic locus and examination of tumors with 15q14-15 loss of heterozygosity (LOH)."
      Schmutte C., Tombline G., Rhiem K., Sadoff M.M., Schmutzler R., von Deimling A., Fishel R.
      Cancer Res. 59:4564-4569(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "A single nucleotide polymorphism in the 5' untranslated region of RAD51 and risk of cancer among BRCA1/2 mutation carriers."
      Wang W.W., Spurdle A.B., Kolachana P., Bove B., Modan B., Ebbers S.M., Suthers G., Tucker M.A., Kaufman D.J., Doody M.M., Tarone R.E., Daly M., Levavi H., Pierce H., Chetrit A., Yechezkel G.H., Chenevix-Trench G., Offit K., Godwin A.K., Struewing J.P.
      Cancer Epidemiol. Biomarkers Prev. 10:955-960(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Identification of a novel human Rad51 variant that promotes DNA strand exchange."
      Park J.Y., Yoo H.W., Kim B.R., Park R., Choi S.Y., Kim Y.
      Nucleic Acids Res. 36:3226-3234(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION OF ISOFORMS 1 AND 3, TISSUE SPECIFICITY (ISOFORMS 1 AND 3), SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), MUTAGENESIS (ISOFORM 3).
    6. NIEHS SNPs program
      Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
      Tissue: Brain.
    8. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    9. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "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] (ISOFORM 2).
      Tissue: Placenta.
    12. "Purification and characterization of the human Rad51 protein, an analogue of E. coli RecA."
      Benson F.E., Stasiak A., West S.C.
      EMBO J. 13:5764-5771(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    13. "Interaction of human recombination proteins Rad51 and Rad54."
      Golub E.I., Kovalenko O.V., Gupta R.C., Ward D.C., Radding C.M.
      Nucleic Acids Res. 25:4106-4110(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAD54L.
    14. "A novel nucleic acid-binding protein that interacts with human rad51 recombinase."
      Kovalenko O.V., Golub E.I., Bray-Ward P., Ward D.C., Radding C.M.
      Nucleic Acids Res. 25:4946-4953(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAD51AP1.
    15. "RAB22 and RAB163/mouse BRCA2: proteins that specifically interact with the RAD51 protein."
      Mizuta R., LaSalle J.M., Cheng H.-L., Shinohara A., Ogawa H., Copeland N.G., Jenkins N.A., Lalande M., Alt F.W.
      Proc. Natl. Acad. Sci. U.S.A. 94:6927-6932(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAD51AP1, SUBCELLULAR LOCATION.
    16. Cited for: INTERACTION WITH ABL1, PHOSPHORYLATION AT TYR-54.
    17. "A novel human Rad54 homologue, Rad54B, associates with Rad51."
      Tanaka K., Hiramoto T., Fukuda T., Miyagawa K.
      J. Biol. Chem. 275:26316-26321(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAD54B.
    18. "Homologous DNA pairing by human recombination factors Rad51 and Rad54."
      Sigurdsson S., Van Komen S., Petukhova G., Sung P.
      J. Biol. Chem. 277:42790-42794(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "Involvement of Rad51C in two distinct protein complexes of Rad51 paralogs in human cells."
      Liu N., Schild D., Thelen M.P., Thompson L.H.
      Nucleic Acids Res. 30:1009-1015(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH XRCC3.
    20. "Complex formation by the human Rad51B and Rad51C DNA repair proteins and their activities in vitro."
      Lio Y.-C., Mazin A.V., Kowalczykowski S.C., Chen D.J.
      J. Biol. Chem. 278:2469-2478(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAD51B AND RAD51C.
    21. "Cellular localization of human Rad51C and regulation of ubiquitin-mediated proteolysis of Rad51."
      Bennett B.T., Knight K.L.
      J. Cell. Biochem. 96:1095-1109(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    22. "The cell-cycle checkpoint kinase Chk1 is required for mammalian homologous recombination repair."
      Soerensen C.S., Hansen L.T., Dziegielewski J., Syljuaesen R.G., Lundin C., Bartek J., Helleday T.
      Nat. Cell Biol. 7:195-201(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CHEK1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-309, MUTAGENESIS OF THR-309.
    23. "RAD51AP2, a novel vertebrate- and meiotic-specific protein, shares a conserved RAD51-interacting C-terminal domain with RAD51AP1/PIR51."
      Kovalenko O.V., Wiese C., Schild D.
      Nucleic Acids Res. 34:5081-5092(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAD51AP2.
    24. Cited for: INTERACTION WITH NABP2.
    25. "Cellular redistribution of Rad51 in response to DNA damage: novel role for Rad51C."
      Gildemeister O.S., Sage J.M., Knight K.L.
      J. Biol. Chem. 284:31945-31952(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    26. "Physical interaction of RECQ5 helicase with RAD51 facilitates its anti-recombinase activity."
      Schwendener S., Raynard S., Paliwal S., Cheng A., Kanagaraj R., Shevelev I., Stark J.M., Sung P., Janscak P.
      J. Biol. Chem. 285:15739-15745(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RECQL5, FUNCTION.
    27. "Discovery of a novel function for human Rad51: maintenance of the mitochondrial genome."
      Sage J.M., Gildemeister O.S., Knight K.L.
      J. Biol. Chem. 285:18984-18990(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
    28. "Regulation of DNA repair through desumoylation and sumoylation of replication protein A complex."
      Dou H., Huang C., Singh M., Carpenter P.B., Yeh E.T.
      Mol. Cell 39:333-345(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RPA1.
    29. "RecQL5 promotes genome stabilization through two parallel mechanisms--interacting with RNA polymerase II and acting as a helicase."
      Islam M.N., Fox D. III, Guo R., Enomoto T., Wang W.
      Mol. Cell. Biol. 30:2460-2472(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RECQL5, FUNCTION.
    30. "A PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA repair via homologous recombination."
      Lee D.H., Pan Y., Kanner S., Sung P., Borowiec J.A., Chowdhury D.
      Nat. Struct. Mol. Biol. 17:365-372(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RPA2, SUBCELLULAR LOCATION.
    31. "Cooperation of breast cancer proteins PALB2 and piccolo BRCA2 in stimulating homologous recombination."
      Buisson R., Dion-Cote A.M., Coulombe Y., Launay H., Cai H., Stasiak A.Z., Stasiak A., Xia B., Masson J.Y.
      Nat. Struct. Mol. Biol. 17:1247-1254(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PALB2.
    32. "Homologous recombination proteins are associated with centrosomes and are required for mitotic stability."
      Cappelli E., Townsend S., Griffin C., Thacker J.
      Exp. Cell Res. 317:1203-1213(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    33. "The role of human SWI5-MEI5 complex in homologous recombination repair."
      Yuan J., Chen J.
      J. Biol. Chem. 286:9888-9893(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SWI5 AND SFR1.
    34. "hSWS1.SWSAP1 is an evolutionarily conserved complex required for efficient homologous recombination repair."
      Liu T., Wan L., Wu Y., Chen J., Huang J.
      J. Biol. Chem. 286:41758-41766(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SWSAP1.
    35. Cited for: INVOLVEMENT IN MRMV2.
    36. "Inhibition of homologous recombination by the PCNA-interacting protein PARI."
      Moldovan G.L., Dejsuphong D., Petalcorin M.I., Hofmann K., Takeda S., Boulton S.J., D'Andrea A.D.
      Mol. Cell 45:75-86(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PARPBP.
    37. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    38. "Breast cancer-associated missense mutants of the PALB2 WD40 domain, which directly binds RAD51C, RAD51 and BRCA2, disrupt DNA repair."
      Park J.Y., Singh T.R., Nassar N., Zhang F., Freund M., Hanenberg H., Meetei A.R., Andreassen P.R.
      Oncogene 0:0-0(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PALB2, IDENTIFICATION IN A PALB2-CONTAINING HR COMPLEX.
    39. "FIGNL1-containing protein complex is required for efficient homologous recombination repair."
      Yuan J., Chen J.
      Proc. Natl. Acad. Sci. U.S.A. 110:10640-10645(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FIGNL1; RAD51AP1 AND SWI5, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    40. "Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome helicase with homologous recombination repair."
      Wan L., Han J., Liu T., Dong S., Xie F., Chen H., Huang J.
      Proc. Natl. Acad. Sci. U.S.A. 110:10646-10651(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH BLM AND SPIDR, INTERACTION WITH SPIDR, SUBCELLULAR LOCATION.
    41. "The N-terminal domain of the human Rad51 protein binds DNA: structure and a DNA binding surface as revealed by NMR."
      Aihara H., Ito Y., Kurumizaka H., Yokoyama S., Shibata T.
      J. Mol. Biol. 290:495-504(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-114.
    42. "Insights into DNA recombination from the structure of a RAD51-BRCA2 complex."
      Pellegrini L., Yu D.S., Lo T., Anand S., Lee M., Blundell T.L., Venkitaraman A.R.
      Nature 420:287-293(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 97-339 IN COMPLEX WITH BRCA2, FUNCTION, SUBUNIT, MUTAGENESIS OF PHE-86 AND ALA-89, SUBCELLULAR LOCATION, INTERACTION WITH BRCA2.
    43. Cited for: VARIANT BC GLN-150.

    Entry informationi

    Entry nameiRAD51_HUMAN
    AccessioniPrimary (citable) accession number: Q06609
    Secondary accession number(s): B0FXP0
    , B2R8T6, Q6FHX9, Q6ZNA8, Q9BV60
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 166 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3