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O15315 (RA51B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA repair protein RAD51 homolog 2
Short name=R51H2
Alternative name(s):
RAD51 homolog B
Short name=Rad51B
RAD51-like protein 1
Gene names
Name:RAD51B
Synonyms:RAD51L1, REC2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length384 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. The RAD51B-RAD51C dimer exhibits single-stranded DNA-dependent ATPase activity. The BCDX2 complex binds single-stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA. Ref.11 Ref.12 Ref.13

Subunit structure

Interacts with RAD51C. Part of a BCDX2 complex consisting of RAD51B, RAD51C, RAD51D and XRCC2. Part of a complex consisting of RAD51B, RAD51C, RAD51D, XRCC2 and XRCC3. Part of a complex with RAD51C and RAD51. Interacts with SWSAP1; involved in homologous recombination repair. Ref.12

Subcellular location

Nucleus Probable.

Tissue specificity

Expressed in a wide range of tissues.

Involvement in disease

Note=A chromosomal aberration involving RAD51B is found in pulmonary chondroid hamartoma. Translocation t(6;14)(p21;q23-24) with HMGA1.

Note=A chromosomal aberration involving RAD51B is found in uterine leiomyoma. Translocation t(12;14)(q15;q23-24) with HMGA2.

Sequence similarities

Belongs to the RecA family. RAD51 subfamily.

Sequence caution

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.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O15315-3)

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.
Isoform 2 (identifier: O15315-1)

Also known as: RAD51L1a;

The sequence of this isoform differs from the canonical sequence as follows:
     346-384: ETTFCSVTQAELNWAPEILPPQPPEQLGLQMCHHTQLIF → AYGNS
Isoform 3 (identifier: O15315-2)

Also known as: RAD51L1b;

The sequence of this isoform differs from the canonical sequence as follows:
     346-384: ETTFCSVTQAELNWAPEILPPQPPEQLGLQMCHHTQLIF → GQEKP
Isoform 4 (identifier: O15315-4)

The sequence of this isoform differs from the canonical sequence as follows:
     347-384: TTFCSVTQAELNWAPEILPPQPPEQLGLQMCHHTQLIF → FWHICISGFSIQNRLKENES
Note: No experimental confirmation available.
Isoform 5 (identifier: O15315-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-119: Missing.
     346-384: ETTFCSVTQAELNWAPEILPPQPPEQLGLQMCHHTQLIF → GQEKP
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 384384DNA repair protein RAD51 homolog 2
PRO_0000122939

Regions

Nucleotide binding108 – 1158ATP Potential

Sites

Site252 – 2532Breakpoint for translocation to form HMGA2-RAD51B

Natural variations

Alternative sequence1 – 119119Missing in isoform 5.
VSP_008817
Alternative sequence346 – 38439ETTFC…TQLIF → AYGNS in isoform 2.
VSP_008819
Alternative sequence346 – 38439ETTFC…TQLIF → GQEKP in isoform 3 and isoform 5.
VSP_008818
Alternative sequence347 – 38438TTFCS…TQLIF → FWHICISGFSIQNRLKENES in isoform 4.
VSP_008820
Natural variant91V → M. Ref.5
Corresponds to variant rs34583846 [ dbSNP | Ensembl ].
VAR_025243
Natural variant821F → C. Ref.5
Corresponds to variant rs35282642 [ dbSNP | Ensembl ].
VAR_025244
Natural variant1721L → W. Ref.5
Corresponds to variant rs34094401 [ dbSNP | Ensembl ].
VAR_025245
Natural variant1801Y → C. Ref.5
Corresponds to variant rs28910275 [ dbSNP | Ensembl ].
VAR_025246
Natural variant2071V → L.
Corresponds to variant rs28908168 [ dbSNP | Ensembl ].
VAR_035437
Natural variant2431K → R. Ref.5
Corresponds to variant rs34594234 [ dbSNP | Ensembl ].
VAR_025247
Natural variant2501S → A. Ref.5
Corresponds to variant rs33929366 [ dbSNP | Ensembl ].
VAR_025248
Natural variant3651P → R.
Corresponds to variant rs28908468 [ dbSNP | Ensembl ].
VAR_051730

Experimental info

Sequence conflict2811S → P in AAN60542. Ref.9
Sequence conflict2811S → P in AAN60543. Ref.9
Sequence conflict2811S → P in AAN60544. Ref.9

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 7, 2003. Version 2.
Checksum: DB0B9AE82F44A52B

FASTA38442,196
        10         20         30         40         50         60 
MGSKKLKRVG LSQELCDRLS RHQILTCQDF LCLSPLELMK VTGLSYRGVH ELLCMVSRAC 

        70         80         90        100        110        120 
APKMQTAYGI KAQRSADFSP AFLSTTLSAL DEALHGGVAC GSLTEITGPP GCGKTQFCIM 

       130        140        150        160        170        180 
MSILATLPTN MGGLEGAVVY IDTESAFSAE RLVEIAESRF PRYFNTEEKL LLTSSKVHLY 

       190        200        210        220        230        240 
RELTCDEVLQ RIESLEEEII SKGIKLVILD SVASVVRKEF DAQLQGNLKE RNKFLAREAS 

       250        260        270        280        290        300 
SLKYLAEEFS IPVILTNQIT THLSGALASQ ADLVSPADDL SLSEGTSGSS CVIAALGNTW 

       310        320        330        340        350        360 
SHSVNTRLIL QYLDSERRQI LIAKSPLAPF TSFVYTIKEE GLVLQETTFC SVTQAELNWA 

       370        380 
PEILPPQPPE QLGLQMCHHT QLIF

« Hide

Isoform 2 (RAD51L1a) [UniParc].

Checksum: CEA992DDC394F3B0
Show »

FASTA35038,257
Isoform 3 (RAD51L1b) [UniParc].

Checksum: CC7EE1B04634F3B0
Show »

FASTA35038,304
Isoform 4 [UniParc].

Checksum: 790D20F0E8EB791A
Show »

FASTA36640,284
Isoform 5 [UniParc].

Checksum: 2EAE6E210C8E74B6
Show »

FASTA23125,527

References

« Hide 'large scale' references
[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: 9207106] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"Identification of a novel human RAD51 homolog, RAD51B."
Albala J.S., Thelen M.P., Prange C.K., Fan W., Christensen M., Thompson L.H., Lennon G.G.
Genomics 46:476-479(1997) [PubMed: 9441753] [Abstract]
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: 9512535] [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. expand/collapse author list , 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: 12508121] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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: 15489334] [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: 12649198] [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: 11751635] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A 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: 11751636] [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: 11842113] [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: 11744692] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH RAD51C; RAD51D; XRCC2 AND XRCC3.
[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: 11842112] [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: 12427746] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX 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: 9892177] [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: 11978964] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH HMGA1.
[19]"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: 21965664] [Abstract]
Cited for: INTERACTION WITH SWSAP1.
+Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00006105.
IPI00220523.
IPI00386489.
IPI00386490.
IPI00395987.
RefSeqNP_002868.1. NM_002877.5.
NP_598193.2. NM_133509.3.
NP_598194.1. NM_133510.3.
UniGeneHs.172587.

3D structure databases

ProteinModelPortalO15315.
SMRO15315. Positions 1-343.
ModBaseSearch...

Protein-protein interaction databases

IntActO15315. 2 interactions.
MINTMINT-224850.
STRINGO15315.

Proteomic databases

PRIDEO15315.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000402498; ENSP00000385485; ENSG00000182185.
ENST00000487270; ENSP00000419471; ENSG00000182185.
GeneID5890.
KEGGhsa:5890.
NMPDRfig|9606.3.peg.9776.
UCSCuc001xkd.1. human.
uc001xkf.1. human.
uc001xkg.1. human.

Organism-specific databases

CTD5890.
GeneCardsGC14P068287.
HGNCHGNC:9822. RAD51B.
HPACAB016191.
MIM150699. phenotype.
602948. gene.
neXtProtNX_O15315.
PharmGKBPA34178.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG16975.
GeneTreeENSGT00550000074609.
HOVERGENHBG061476.
InParanoidO15315.
OMAPLELMKM.
PhylomeDBO15315.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressO15315.
BgeeO15315.
GenevestigatorO15315.

Family and domain databases

InterProIPR003593. ATPase_AAA+_core.
IPR013632. DNA_recomb/repair_Rad51_C.
IPR016467. DNA_recomb/repair_RecA-like.
IPR020588. DNA_recomb_RecA/RadB_ATP-bd.
[Graphical view]
KOK10869.
PfamPF08423. Rad51. 1 hit.
[Graphical view]
PIRSFPIRSF005856. Rad51. 1 hit.
SMARTSM00382. AAA. 1 hit.
[Graphical view]
PROSITEPS50162. RECA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio22908.
SOURCESearch...

Entry information

Entry nameRA51B_HUMAN
AccessionPrimary (citable) accession number: O15315
Secondary accession number(s): O60914 expand/collapse secondary AC list , O75210, Q3Y4F8, Q6FHX8, Q86SY3, Q86SY4, Q86TR0, Q86U92, Q86U93, Q86U94, Q8N6H4, Q9UPL5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 7, 2003
Last modified: January 25, 2012
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents