Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O15315

- RA51B_HUMAN

UniProt

O15315 - RA51B_HUMAN

(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)

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

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. 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
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_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
Complete GO annotation...

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

BgeeiO15315.
ExpressionAtlasiO15315. baseline and differential.
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.
GeneTreeiENSGT00760000119278.
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

        10         20         30         40         50
MGSKKLKRVG LSQELCDRLS RHQILTCQDF LCLSPLELMK VTGLSYRGVH
60 70 80 90 100
ELLCMVSRAC APKMQTAYGI KAQRSADFSP AFLSTTLSAL DEALHGGVAC
110 120 130 140 150
GSLTEITGPP GCGKTQFCIM MSILATLPTN MGGLEGAVVY IDTESAFSAE
160 170 180 190 200
RLVEIAESRF PRYFNTEEKL LLTSSKVHLY RELTCDEVLQ RIESLEEEII
210 220 230 240 250
SKGIKLVILD SVASVVRKEF DAQLQGNLKE RNKFLAREAS SLKYLAEEFS
260 270 280 290 300
IPVILTNQIT THLSGALASQ ADLVSPADDL SLSEGTSGSS CVIAALGNTW
310 320 330 340 350
SHSVNTRLIL QYLDSERRQI LIAKSPLAPF TSFVYTIKEE GLVLQETTFC
360 370 380
SVTQAELNWA PEILPPQPPE QLGLQMCHHT QLIF
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

EnsembliENST00000471583; 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 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.
GeneTreei ENSGT00760000119278.
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

Bgeei O15315.
ExpressionAtlasi O15315. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 128 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