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O15315 (RA51B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. 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·Interactions·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) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. 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. Ref.11 Ref.12 Ref.13 Ref.19 Ref.23 Ref.24

Subunit structure

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. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.20 Ref.22

Subcellular location

Nucleus Probable.

Tissue specificity

Expressed in a wide range of tissues.

Post-translational modification

Phosphorylated on tyrosine residues by BCR-ALB. Ref.21

Involvement in disease

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.

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.

Ontologies

Keywords
   Biological processDNA damage
DNA recombination
DNA repair
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   LigandATP-binding
DNA-binding
Nucleotide-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.19. Source: GOC

DNA recombination

Traceable author statement Ref.3. Source: ProtInc

DNA repair

Traceable author statement Ref.3. Source: ProtInc

blood coagulation

Traceable author statement. Source: Reactome

double-strand break repair via homologous recombination

Inferred from mutant phenotype Ref.24. Source: UniProtKB

positive regulation of G2/M transition of mitotic cell cycle

Inferred from mutant phenotype Ref.23. Source: UniProtKB

reciprocal meiotic recombination

Traceable author statement Ref.2. Source: ProtInc

   Cellular_componentRad51B-Rad51C-Rad51D-XRCC2 complex

Inferred from direct assay Ref.11. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Traceable author statement Ref.3. Source: ProtInc

replication fork

Inferred from direct assay Ref.25. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Traceable author statement Ref.3. Source: ProtInc

DNA-dependent ATPase activity

Inferred from direct assay Ref.19. Source: UniProtKB

double-stranded DNA binding

Inferred from direct assay Ref.19. Source: UniProtKB

single-stranded DNA binding

Inferred from direct assay Ref.19. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SWSAP1Q6NVH72EBI-2824089,EBI-5281637

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
Region1 – 7575Interaction with RAD51C

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

Mutagenesis3261P → L: Abolishs interaction with BCR-ABL SH3 domain. Ref.21
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] [Europe PMC] [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] [Europe PMC] [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] [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. 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] [Europe PMC] [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] [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.
+Additional computationally mapped references.

Web resources

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.
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 10-342.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111827. 6 interactions.
DIPDIP-41246N.
IntActO15315. 3 interactions.
MINTMINT-224850.

PTM databases

PhosphoSiteO15315.

Proteomic databases

PaxDbO15315.
PRIDEO15315.

Protocols and materials databases

DNASU5890.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000390683; ENSP00000375101; ENSG00000182185. [O15315-4]
ENST00000471583; ENSP00000418859; ENSG00000182185. [O15315-2]
ENST00000487270; ENSP00000419471; ENSG00000182185. [O15315-3]
ENST00000488612; ENSP00000420061; ENSG00000182185. [O15315-4]
GeneID5890.
KEGGhsa:5890.
UCSCuc001xkd.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

CTD5890.
GeneCardsGC14P068287.
H-InvDBHIX0022466.
HGNCHGNC:9822. RAD51B.
HPACAB016191.
HPA051869.
MIM150699. phenotype.
602948. gene.
neXtProtNX_O15315.
PharmGKBPA34178.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0468.
HOVERGENHBG061476.
InParanoidO15315.
KOK10869.
OMACIMMSVL.
PhylomeDBO15315.
TreeFamTF101219.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressO15315.
BgeeO15315.
GenevestigatorO15315.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR013632. DNA_recomb/repair_Rad51_C.
IPR016467. DNA_recomb/repair_RecA-like.
IPR027417. P-loop_NTPase.
IPR020588. RecA_ATP-bd.
[Graphical view]
PfamPF08423. Rad51. 1 hit.
[Graphical view]
PIRSFPIRSF005856. Rad51. 1 hit.
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS50162. RECA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRAD51B. human.
GeneWikiRAD51L1.
GenomeRNAi5890.
NextBio22908.
PROO15315.
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: April 16, 2014
This is version 122 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

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

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