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O15315

- RA51B_HUMAN

UniProt

O15315 - RA51B_HUMAN

Protein

DNA repair protein RAD51 homolog 2

Gene

RAD51B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 2 (07 Nov 2003)
      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. May promote the assembly of presynaptic RAD51 nucleoprotein filaments. Binds single-stranded DNA and double-stranded DNA 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. The BCDX2 subcomplex RAD51B:RAD51C exhibits single-stranded DNA-dependent ATPase activity suggesting an involvement in early stages of the HR pathway.6 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei252 – 2532Breakpoint for translocation to form HMGA2-RAD51B

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi108 – 1158ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA binding Source: ProtInc
    3. DNA-dependent ATPase activity Source: UniProtKB
    4. double-stranded DNA binding Source: UniProtKB
    5. protein binding Source: IntAct
    6. single-stranded DNA binding Source: UniProtKB

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. blood coagulation Source: Reactome
    3. DNA recombination Source: ProtInc
    4. DNA repair Source: ProtInc
    5. double-strand break repair via homologous recombination Source: UniProtKB
    6. positive regulation of G2/M transition of mitotic cell cycle Source: UniProtKB
    7. reciprocal meiotic recombination Source: ProtInc

    Keywords - Biological processi

    DNA damage, DNA recombination, DNA repair

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_24970. Factors involved in megakaryocyte development and platelet production.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA repair protein RAD51 homolog 2
    Short name:
    R51H2
    Alternative name(s):
    RAD51 homolog B
    Short name:
    Rad51B
    RAD51-like protein 1
    Gene namesi
    Name:RAD51B
    Synonyms:RAD51L1, REC2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:9822. RAD51B.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome
    2. nucleus Source: ProtInc
    3. Rad51B-Rad51C-Rad51D-XRCC2 complex Source: UniProtKB
    4. replication fork Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving RAD51B is found in pulmonary chondroid hamartoma. Translocation t(6;14)(p21;q23-24) with HMGA1.
    A chromosomal aberration involving RAD51B is found in uterine leiomyoma. Translocation t(12;14)(q15;q23-24) with HMGA2.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi326 – 3261P → L: Abolishs interaction with BCR-ABL SH3 domain. 1 Publication

    Organism-specific databases

    MIMi150699. phenotype.
    PharmGKBiPA34178.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 384384DNA repair protein RAD51 homolog 2PRO_0000122939Add
    BLAST

    Post-translational modificationi

    Phosphorylated on tyrosine residues by BCR-ALB.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO15315.
    PaxDbiO15315.
    PRIDEiO15315.

    PTM databases

    PhosphoSiteiO15315.

    Expressioni

    Tissue specificityi

    Expressed in a wide range of tissues.

    Gene expression databases

    ArrayExpressiO15315.
    BgeeiO15315.
    GenevestigatoriO15315.

    Organism-specific databases

    HPAiCAB016191.
    HPA051869.

    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. The BCDX2 subcomplex RAD51B:RAD51C interacts with RAD51. Interacts with SWSAP1; involved in homologous recombination repair.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RAD51CO4350210EBI-2824089,EBI-2267048
    RAD51DO757715EBI-2824089,EBI-1055693
    SWSAP1Q6NVH72EBI-2824089,EBI-5281637

    Protein-protein interaction databases

    BioGridi111827. 6 interactions.
    DIPiDIP-41246N.
    IntActiO15315. 6 interactions.
    MINTiMINT-224850.

    Structurei

    3D structure databases

    ProteinModelPortaliO15315.
    SMRiO15315. Positions 10-342.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 7575Interaction with RAD51CAdd
    BLAST

    Sequence similaritiesi

    Belongs to the RecA family. RAD51 subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG0468.
    HOVERGENiHBG061476.
    InParanoidiO15315.
    KOiK10869.
    OMAiCIMMSVL.
    PhylomeDBiO15315.
    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]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O15315-3) [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

    MGSKKLKRVG LSQELCDRLS RHQILTCQDF LCLSPLELMK VTGLSYRGVH    50
    ELLCMVSRAC APKMQTAYGI KAQRSADFSP AFLSTTLSAL DEALHGGVAC 100
    GSLTEITGPP GCGKTQFCIM MSILATLPTN MGGLEGAVVY IDTESAFSAE 150
    RLVEIAESRF PRYFNTEEKL LLTSSKVHLY RELTCDEVLQ RIESLEEEII 200
    SKGIKLVILD SVASVVRKEF DAQLQGNLKE RNKFLAREAS SLKYLAEEFS 250
    IPVILTNQIT THLSGALASQ ADLVSPADDL SLSEGTSGSS CVIAALGNTW 300
    SHSVNTRLIL QYLDSERRQI LIAKSPLAPF TSFVYTIKEE GLVLQETTFC 350
    SVTQAELNWA PEILPPQPPE QLGLQMCHHT QLIF 384
    Length:384
    Mass (Da):42,196
    Last modified:November 7, 2003 - v2
    Checksum:iDB0B9AE82F44A52B
    GO
    Isoform 2 (identifier: O15315-1) [UniParc]FASTAAdd to Basket

    Also known as: RAD51L1a

    The sequence of this isoform differs from the canonical sequence as follows:
         346-384: ETTFCSVTQAELNWAPEILPPQPPEQLGLQMCHHTQLIF → AYGNS

    Show »
    Length:350
    Mass (Da):38,257
    Checksum:iCEA992DDC394F3B0
    GO
    Isoform 3 (identifier: O15315-2) [UniParc]FASTAAdd to Basket

    Also known as: RAD51L1b

    The sequence of this isoform differs from the canonical sequence as follows:
         346-384: ETTFCSVTQAELNWAPEILPPQPPEQLGLQMCHHTQLIF → GQEKP

    Show »
    Length:350
    Mass (Da):38,304
    Checksum:iCC7EE1B04634F3B0
    GO
    Isoform 4 (identifier: O15315-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         347-384: TTFCSVTQAELNWAPEILPPQPPEQLGLQMCHHTQLIF → FWHICISGFSIQNRLKENES

    Note: No experimental confirmation available.

    Show »
    Length:366
    Mass (Da):40,284
    Checksum:i790D20F0E8EB791A
    GO
    Isoform 5 (identifier: O15315-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-119: Missing.
         346-384: ETTFCSVTQAELNWAPEILPPQPPEQLGLQMCHHTQLIF → GQEKP

    Note: No experimental confirmation available.

    Show »
    Length:231
    Mass (Da):25,527
    Checksum:i2EAE6E210C8E74B6
    GO

    Sequence cautioni

    The sequence CAD62357.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAD66573.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti281 – 2811S → P in AAN60542. (PubMed:15489334)Curated
    Sequence conflicti281 – 2811S → P in AAN60543. (PubMed:15489334)Curated
    Sequence conflicti281 – 2811S → P in AAN60544. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti9 – 91V → M.1 Publication
    Corresponds to variant rs34583846 [ dbSNP | Ensembl ].
    VAR_025243
    Natural varianti82 – 821F → C.1 Publication
    Corresponds to variant rs35282642 [ dbSNP | Ensembl ].
    VAR_025244
    Natural varianti172 – 1721L → W.1 Publication
    Corresponds to variant rs34094401 [ dbSNP | Ensembl ].
    VAR_025245
    Natural varianti180 – 1801Y → C.1 Publication
    Corresponds to variant rs28910275 [ dbSNP | Ensembl ].
    VAR_025246
    Natural varianti207 – 2071V → L.
    Corresponds to variant rs28908168 [ dbSNP | Ensembl ].
    VAR_035437
    Natural varianti243 – 2431K → R.1 Publication
    Corresponds to variant rs34594234 [ dbSNP | Ensembl ].
    VAR_025247
    Natural varianti250 – 2501S → A.1 Publication
    Corresponds to variant rs33929366 [ dbSNP | Ensembl ].
    VAR_025248
    Natural varianti365 – 3651P → R.
    Corresponds to variant rs28908468 [ dbSNP | Ensembl ].
    VAR_051730

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 119119Missing in isoform 5. 1 PublicationVSP_008817Add
    BLAST
    Alternative sequencei346 – 38439ETTFC…TQLIF → AYGNS in isoform 2. 3 PublicationsVSP_008819Add
    BLAST
    Alternative sequencei346 – 38439ETTFC…TQLIF → GQEKP in isoform 3 and isoform 5. 2 PublicationsVSP_008818Add
    BLAST
    Alternative sequencei347 – 38438TTFCS…TQLIF → FWHICISGFSIQNRLKENES in isoform 4. 1 PublicationVSP_008820Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U92074 mRNA. Translation: AAB63358.1.
    U84138 mRNA. Translation: AAC39723.1.
    Y15571 mRNA. Translation: CAA75680.1.
    BX161515 mRNA. Translation: CAD61950.1.
    BX248061 mRNA. Translation: CAD62357.1. Different initiation.
    BX248766 mRNA. Translation: CAD66573.1. Different initiation.
    DQ160197 Genomic DNA. Translation: AAZ85144.1.
    AC004518 Genomic DNA. Translation: AAC32426.1.
    AC004518 Genomic DNA. Translation: AAC32425.1.
    CR536560 mRNA. Translation: CAG38797.1.
    CH471061 Genomic DNA. Translation: EAW80957.1.
    BC030219 mRNA. Translation: AAH30219.1.
    AY138857 mRNA. Translation: AAN60542.1.
    AY138858 mRNA. Translation: AAN60543.1.
    AY138859 mRNA. Translation: AAN60544.1.
    CCDSiCCDS9789.1. [O15315-3]
    CCDS9790.1. [O15315-2]
    RefSeqiNP_002868.1. NM_002877.5. [O15315-1]
    NP_598193.2. NM_133509.3. [O15315-3]
    NP_598194.1. NM_133510.3. [O15315-2]
    UniGeneiHs.172587.

    Genome annotation databases

    EnsembliENST00000390683; ENSP00000375101; ENSG00000182185. [O15315-4]
    ENST00000471583; ENSP00000418859; ENSG00000182185. [O15315-2]
    ENST00000487270; ENSP00000419471; ENSG00000182185. [O15315-3]
    ENST00000488612; ENSP00000420061; ENSG00000182185. [O15315-4]
    GeneIDi5890.
    KEGGihsa:5890.
    UCSCiuc001xkd.3. human. [O15315-2]
    uc001xke.3. human. [O15315-1]
    uc001xkf.2. human. [O15315-3]
    uc001xkg.2. human. [O15315-4]
    uc010aqr.3. human. [O15315-5]

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U92074 mRNA. Translation: AAB63358.1 .
    U84138 mRNA. Translation: AAC39723.1 .
    Y15571 mRNA. Translation: CAA75680.1 .
    BX161515 mRNA. Translation: CAD61950.1 .
    BX248061 mRNA. Translation: CAD62357.1 . Different initiation.
    BX248766 mRNA. Translation: CAD66573.1 . Different initiation.
    DQ160197 Genomic DNA. Translation: AAZ85144.1 .
    AC004518 Genomic DNA. Translation: AAC32426.1 .
    AC004518 Genomic DNA. Translation: AAC32425.1 .
    CR536560 mRNA. Translation: CAG38797.1 .
    CH471061 Genomic DNA. Translation: EAW80957.1 .
    BC030219 mRNA. Translation: AAH30219.1 .
    AY138857 mRNA. Translation: AAN60542.1 .
    AY138858 mRNA. Translation: AAN60543.1 .
    AY138859 mRNA. Translation: AAN60544.1 .
    CCDSi CCDS9789.1. [O15315-3 ]
    CCDS9790.1. [O15315-2 ]
    RefSeqi NP_002868.1. NM_002877.5. [O15315-1 ]
    NP_598193.2. NM_133509.3. [O15315-3 ]
    NP_598194.1. NM_133510.3. [O15315-2 ]
    UniGenei Hs.172587.

    3D structure databases

    ProteinModelPortali O15315.
    SMRi O15315. Positions 10-342.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111827. 6 interactions.
    DIPi DIP-41246N.
    IntActi O15315. 6 interactions.
    MINTi MINT-224850.

    PTM databases

    PhosphoSitei O15315.

    Proteomic databases

    MaxQBi O15315.
    PaxDbi O15315.
    PRIDEi O15315.

    Protocols and materials databases

    DNASUi 5890.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000390683 ; ENSP00000375101 ; ENSG00000182185 . [O15315-4 ]
    ENST00000471583 ; ENSP00000418859 ; ENSG00000182185 . [O15315-2 ]
    ENST00000487270 ; ENSP00000419471 ; ENSG00000182185 . [O15315-3 ]
    ENST00000488612 ; ENSP00000420061 ; ENSG00000182185 . [O15315-4 ]
    GeneIDi 5890.
    KEGGi hsa:5890.
    UCSCi uc001xkd.3. human. [O15315-2 ]
    uc001xke.3. human. [O15315-1 ]
    uc001xkf.2. human. [O15315-3 ]
    uc001xkg.2. human. [O15315-4 ]
    uc010aqr.3. human. [O15315-5 ]

    Organism-specific databases

    CTDi 5890.
    GeneCardsi GC14P068287.
    H-InvDB HIX0022466.
    HGNCi HGNC:9822. RAD51B.
    HPAi CAB016191.
    HPA051869.
    MIMi 150699. phenotype.
    602948. gene.
    neXtProti NX_O15315.
    PharmGKBi PA34178.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0468.
    HOVERGENi HBG061476.
    InParanoidi O15315.
    KOi K10869.
    OMAi CIMMSVL.
    PhylomeDBi O15315.
    TreeFami TF101219.

    Enzyme and pathway databases

    Reactomei REACT_24970. Factors involved in megakaryocyte development and platelet production.

    Miscellaneous databases

    ChiTaRSi RAD51B. human.
    GeneWikii RAD51L1.
    GenomeRNAii 5890.
    NextBioi 22908.
    PROi O15315.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O15315.
    Bgeei O15315.
    Genevestigatori O15315.

    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. "Isolation of human and mouse genes based on homology to REC2, a recombinational repair gene from the fungus Ustilago maydis."
      Rice M.C., Smith S.T., Bullrich F., Havre P., Kmiec E.B.
      Proc. Natl. Acad. Sci. U.S.A. 94:7417-7422(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    3. "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] (ISOFORM 3).
    4. "Full-length cDNA libraries and normalization."
      Li W.B., Gruber C., Jessee J., Polayes D.
      Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4 AND 5).
      Tissue: Neuroblastoma.
    5. NIEHS SNPs program
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS MET-9; CYS-82; TRP-172; CYS-180; ARG-243 AND ALA-250.
    6. "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 2).
    7. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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 1).
      Tissue: Lung.
    10. "Fusion transcripts involving HMGA2 are not a common molecular mechanism in uterine leiomyomata with rearrangements in 12q15."
      Quade B.J., Weremowicz S., Neskey D.M., Vanni R., Ladd C., Dal Cin P., Morton C.C.
      Cancer Res. 63:1351-1358(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 253-310, CHROMOSOMAL TRANSLOCATION WITH HMGA2.
    11. "Identification and purification of two distinct complexes containing the five RAD51 paralogs."
      Masson J.Y., Tarsounas M.C., Stasiak A.Z., Stasiak A., Shah R., McIlwraith M.J., Benson F.E., West S.C.
      Genes Dev. 15:3296-3307(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE BCDX2 COMPLEX WITH RAD51C; RAD51D AND XRCC2.
    12. "Mediator function of the human Rad51B-Rad51C complex in Rad51/RPA-catalyzed DNA strand exchange."
      Sigurdsson S., Van Komen S., Bussen W., Schild D., Albala J.S., Sung P.
      Genes Dev. 15:3308-3318(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RAD51C.
    13. "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: FUNCTION, IDENTIFICATION IN A COMPLEX WITH RAD51C; RAD51D AND XRCC2.
    14. "RAD51C interacts with RAD51B and is central to a larger protein complex in vivo exclusive of RAD51."
      Miller K.A., Yoshikawa D.M., McConnell I.R., Clark R., Schild D., Albala J.S.
      J. Biol. Chem. 277:8406-8411(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAD51C, SUBUNIT.
    15. "Interactions involving the Rad51 paralogs Rad51C and XRCC3 in human cells."
      Wiese C., Collins D.W., Albala J.S., Thompson L.H., Kronenberg A., Schild D.
      Nucleic Acids Res. 30:1001-1008(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH RAD51C; RAD51D AND XRCC2.
    16. "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 RAD51 AND RAD51C.
    17. "Allelic knockout of novel splice variants of human recombination repair gene RAD51B in t(12;14) uterine leiomyomas."
      Schoenmakers E.F.P.M., Huysmans C., Van de Ven W.J.M.
      Cancer Res. 59:19-23(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH HMGA2.
    18. "Intragenic breakpoint within RAD51L1 in a t(6;14)(p21.3;q24) of a pulmonary chondroid hamartoma."
      Blank C., Schoenmakers E.F.P.M., Rogalla P., Huys E.H., van Rijk A.A., Drieschner N., Bullerdiek J.
      Cytogenet. Cell Genet. 95:17-19(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH HMGA1.
    19. "Holliday junction binding activity of the human Rad51B protein."
      Yokoyama H., Kurumizaka H., Ikawa S., Yokoyama S., Shibata T.
      J. Biol. Chem. 278:2767-2772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    20. "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.
    21. "BCR/ABL kinase interacts with and phosphorylates the RAD51 paralog, RAD51B."
      Slupianek A., Jozwiakowski S.K., Gurdek E., Skorski T.
      Leukemia 23:2308-2310(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY BCR-ABL, MUTAGENESIS OF PRO-326.
    22. "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.
    23. "The RAD51 paralogs ensure cellular protection against mitotic defects and aneuploidy."
      Rodrigue A., Coulombe Y., Jacquet K., Gagne J.P., Roques C., Gobeil S., Poirier G., Masson J.Y.
      J. Cell Sci. 126:348-359(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MITOTIC CELL PROGRESSION.
    24. "Rad51 paralog complexes BCDX2 and CX3 act at different stages in the BRCA1-BRCA2-dependent homologous recombination pathway."
      Chun J., Buechelmaier E.S., Powell S.N.
      Mol. Cell. Biol. 33:387-395(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE BCDX2 COMPLEX.
    25. "Ring-shaped Rad51 paralog protein complexes bind Holliday junctions and replication forks as visualized by electron microscopy."
      Compton S.A., Ozgur S., Griffith J.D.
      J. Biol. Chem. 285:13349-13356(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ELECTRON MICROSCOPY OF THE BCDX2 COMPLEX, DNA-BINDING OF THE BCDX2 COMPLEX.

    Entry informationi

    Entry nameiRA51B_HUMAN
    AccessioniPrimary (citable) accession number: O15315
    Secondary accession number(s): O60914
    , O75210, Q3Y4F8, Q6FHX8, Q86SY3, Q86SY4, Q86TR0, Q86U92, Q86U93, Q86U94, Q8N6H4, Q9UPL5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: November 7, 2003
    Last modified: October 1, 2014
    This is version 127 of the entry and version 2 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3