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UniProtKB/Swiss-Prot entry O15315


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RA51B_HUMAN
Primary accession number O15315
Secondary accession numbers O60914 O75210 Q3Y4F8 Q86SY3 Q86SY4 Q86TR0 Q86U92 Q86U93 Q86U94 Q8N6H4 Q9UPL5
Integrated into Swiss-Prot on December 15, 1998
Sequence was last modified on November 7, 2003 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 81)
Name and origin of the protein
Protein name DNA repair protein RAD51 homolog 2
Synonyms R51H2
RAD51-like protein 1
Rad51B
Gene name
Name: RAD51L1
Synonyms: RAD51B, REC2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
DOI=10.1073/pnas.94.14.7417; PubMed=9207106 [NCBI, ExPASy, EBI, Israel, Japan]
Rice M.C., Smith S.T., Bullrich F., Havre P., Kmiec E.B.;
"Isolation of human and mouse genes based on homology to REC2, a recombinational repair gene from the fungus Ustilago maydis.";
Proc. Natl. Acad. Sci. U.S.A. 94:7417-7422(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
DOI=10.1006/geno.1997.5062; PubMed=9441753 [NCBI, ExPASy, EBI, Israel, Japan]
Albala J.S., Thelen M.P., Prange C.K., Fan W., Christensen M., Thompson L.H., Lennon G.G.;
"Identification of a novel human RAD51 homolog, RAD51B.";
Genomics 46:476-479(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
DOI=10.1093/nar/26.7.1653; PubMed=9512535 [NCBI, ExPASy, EBI, Israel, Japan]
Cartwright R., Dunn A.M., Simpson P.J., Tambini C.E., Thacker J.;
"Isolation of novel human and mouse genes of the recA/RAD51 recombination-repair gene family.";
Nucleic Acids Res. 26:1653-1659(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4 AND 5).
TISSUE=Neuroblastoma;
Li W.B., Gruber C., Jessee J., Polayes D.;
"Full-length cDNA libraries and normalization.";
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-9; CYS-82; TRP-172; CYS-180; ARG-243 AND ALA-250.
NIEHS SNPs program;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature01348; PubMed=12508121 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 253-310, AND CHROMOSOMAL TRANSLOCATION WITH HMGA2.
PubMed=12649198 [NCBI, ExPASy, EBI, Israel, Japan]
Quade B.J., Weremowicz S., Neskey D.M., Vanni R., Ladd C., Dal Cin P., Morton C.C.;
"Fusion transcripts involving HMGA2 are not a common molecular mechanism in uterine leiomyomata with rearrangements in 12q15.";
Cancer Res. 63:1351-1358(2003).
[9]
FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH RAD51C; RAD51D AND XRCC2.
DOI=10.1101/gad.947001; PubMed=11751635 [NCBI, ExPASy, EBI, Israel, Japan]
Masson J.Y., Tarsounas M.C., Stasiak A.Z., Stasiak A., Shah R., McIlwraith M.J., Benson F.E., West S.C.;
"Identification and purification of two distinct complexes containing the five RAD51 paralogs.";
Genes Dev. 15:3296-3307(2001).
[10]
FUNCTION, AND INTERACTION WITH RAD51C.
DOI=10.1101/gad.935501; PubMed=11751636 [NCBI, ExPASy, EBI, Israel, Japan]
Sigurdsson S., Van Komen S., Bussen W., Schild D., Albala J.S., Sung P.;
"Mediator function of the human Rad51B-Rad51C complex in Rad51/RPA-catalyzed DNA strand exchange.";
Genes Dev. 15:3308-3318(2001).
[11]
FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH RAD51C; RAD51D AND XRCC2.
DOI=10.1093/nar/30.4.1009; PubMed=11842113 [NCBI, ExPASy, EBI, Israel, Japan]
Liu N., Schild D., Thelen M.P., Thompson L.H.;
"Involvement of Rad51C in two distinct protein complexes of Rad51 paralogs in human cells.";
Nucleic Acids Res. 30:1009-1015(2002).
[12]
IDENTIFICATION IN A COMPLEX WITH RAD51C; RAD51D; XRCC2 AND XRCC3.
DOI=10.1074/jbc.M108306200; PubMed=11744692 [NCBI, ExPASy, EBI, Israel, Japan]
Miller K.A., Yoshikawa D.M., McConnell I.R., Clark R., Schild D., Albala J.S.;
"RAD51C interacts with RAD51B and is central to a larger protein complex in vivo exclusive of RAD51.";
J. Biol. Chem. 277:8406-8411(2002).
[13]
IDENTIFICATION IN A COMPLEX WITH RAD51C; RAD51D AND XRCC2.
DOI=10.1093/nar/30.4.1001; PubMed=11842112 [NCBI, ExPASy, EBI, Israel, Japan]
Wiese C., Collins D.W., Albala J.S., Thompson L.H., Kronenberg A., Schild D.;
"Interactions involving the Rad51 paralogs Rad51C and XRCC3 in human cells.";
Nucleic Acids Res. 30:1001-1008(2002).
[14]
IDENTIFICATION IN A COMPLEX WITH RAD51 AND RAD51C.
DOI=10.1074/jbc.M211038200; PubMed=12427746 [NCBI, ExPASy, EBI, Israel, Japan]
Lio Y.-C., Mazin A.V., Kowalczykowski S.C., Chen D.J.;
"Complex formation by the human Rad51B and Rad51C DNA repair proteins and their activities in vitro.";
J. Biol. Chem. 278:2469-2478(2003).
[15]
CHROMOSOMAL TRANSLOCATION WITH HMGA2.
PubMed=9892177 [NCBI, ExPASy, EBI, Israel, Japan]
Schoenmakers E.F.P.M., Huysmans C., Van de Ven W.J.M.;
"Allelic knockout of novel splice variants of human recombination repair gene RAD51B in t(12;14) uterine leiomyomas.";
Cancer Res. 59:19-23(1999).
[16]
CHROMOSOMAL TRANSLOCATION WITH HMGA1.
PubMed=11978964 [NCBI, ExPASy, EBI, Israel, Japan]
Blank C., Schoenmakers E.F.P.M., Rogalla P., Huys E.H., van Rijk A.A., Drieschner N., Bullerdiek J.;
"Intragenic breakpoint within RAD51L1 in a t(6;14)(p21.3;q24) of a pulmonary chondroid hamartoma.";
Cytogenet. Cell Genet. 95:17-19(2001).
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.
  • SUBUNIT: 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.
  • SUBCELLULAR LOCATION: Nucleus (Probable).
  • ALTERNATIVE PRODUCTS: 5 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDO15315-3
    This is the isoform sequence displayed in this entry.
    Name2
    SynonymsRAD51L1a
    Isoform IDO15315-1
    Features which should be applied to build the isoform sequence: VSP_008819.
    Name3
    SynonymsRAD51L1b
    Isoform IDO15315-2
    Features which should be applied to build the isoform sequence: VSP_008818.
    Name4
    Isoform IDO15315-4
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_008820.
    Name5
    Isoform IDO15315-5
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_008817, VSP_008818.
  • TISSUE SPECIFICITY: Expressed in a wide range of tissues.
  • DISEASE: A chromosomal aberration involving RAD51L1 is found in pulmonary chondroid hamartoma. Translocation t(6;14)(p21;q23-24) with HMGA1.
  • DISEASE: A chromosomal aberration involving RAD51L1 is found in uterine leiomyoma (UL) [MIM:150699]. Translocation t(12;14)(q15;q23-24) with HMGA2.
  • SIMILARITY: Belongs to the recA family. RAD51 subfamily.
  • WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/rad51l1/";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U92074; AAB63358.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U84138; AAC39723.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y15571; CAA75680.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BX161515; CAD61950.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BX248061; CAD62357.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BX248766; CAD66573.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ160197; AAZ85144.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC004518; AAC32426.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC004518; AAC32425.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC030219; AAH30219.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY138857; AAN60542.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY138858; AAN60543.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY138859; AAN60544.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00006105; -.
IPI00220523; -.
IPI00386489; -.
IPI00386490; -.
IPI00395987; -.
RefSeq NP_002868.1; -.
NP_598193.2; -.
NP_598194.1; -.
UniGene Hs.172587
3D structure databases
HSSP Q06609; 1N0W. [HSSP ENTRY / PDB]
ModBase O15315.
Organism-specific databases
GeneCards GC14P067356; -.
H-InvDB HIX0022466; -.
HGNC HGNC:9822; RAD51L1.
GenAtlas RAD51L1.
HPA CAB016191; -.
MIM 150699; phenotype. [NCBI / EBI]
602948; gene. [NCBI / EBI]
PharmGKB PA34178; -.
Gene expression databases
ArrayExpress O15315; -.
Bgee O15315; -.
Ontologies
GO
GO:0005634; Cellular component: nucleus (traceable author statement from ProtInc).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003677; Molecular function: DNA binding (traceable author statement from ProtInc).
GO:0008094; Molecular function: DNA-dependent ATPase activity (inferred from electronic annotation from InterPro).
GO:0006281; Biological process: DNA repair (traceable author statement from ProtInc).
GO:0007131; Biological process: reciprocal meiotic recombination (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR003593; ATPase_AAA+_core.
IPR016467; DNA_repair_recomb_RecA-like.
IPR013632; Rad51_C.
IPR001553; RecA_bac.
Graphical view of domain structure.
Pfam PF08423; Rad51; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF005856; Rad51; 1.
SMART SM00382; AAA; 1.
SMART graphical view of domain structure.
PROSITE PS50162; RECA_2; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
Ensembl ENSG00000182185; Homo sapiens. [Contig view]
GeneID 5890; -.
KEGG hsa:5890; -.
NMPDR fig|9606.3.peg.9776; -.
Phylogenomic databases
HOVERGEN O15315; -.
OMA O15315; YIDTESA.
Other
NextBio 22908; -.
SOURCE RAD51L1; Homo sapiens.
ProtoNet O15315.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; ATP-binding; Chromosomal rearrangement; DNA damage; DNA recombination; DNA repair; DNA-binding; Nucleotide-binding; Nucleus; Polymorphism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   384  384     DNA repair protein RAD51 homolog 2. PRO_0000122939
NP_BIND   108   115  8     ATP (Potential). 
SITE   252   253  2     Breakpoint for translocation to form HMGA2-RAD51L1. 
VAR_SEQ   1   119        Missing (in isoform 5). VSP_008817
VAR_SEQ   346   384        ETTFCSVTQAELNWAPEILPPQPPEQLGLQMCHHTQLIF -> AYGNS (in isoform 2). VSP_008819
VAR_SEQ   346   384        ETTFCSVTQAELNWAPEILPPQPPEQLGLQMCHHTQLIF -> GQEKP (in isoform 3 and isoform 5). VSP_008818
VAR_SEQ   347   384        TTFCSVTQAELNWAPEILPPQPPEQLGLQMCHHTQLIF -> FWHICISGFSIQNRLKENES (in isoform 4). VSP_008820
VARIANT   9     9  1     V -> M (in dbSNP:rs34583846 [NCBI]). VAR_025243 
VARIANT   82    82  1     F -> C (in dbSNP:rs35282642 [NCBI]). VAR_025244 
VARIANT   172   172  1     L -> W (in dbSNP:rs34094401 [NCBI]). VAR_025245 
VARIANT   180   180  1     Y -> C (in dbSNP:rs28910275 [NCBI]). VAR_025246 
VARIANT   207   207  1     V -> L (in dbSNP:rs28908168 [NCBI]). VAR_035437 
VARIANT   243   243  1     K -> R (in dbSNP:rs34594234 [NCBI]). VAR_025247 
VARIANT   250   250  1     S -> A (in dbSNP:rs33929366 [NCBI]). VAR_025248 
VARIANT   365   365  1     P -> R (in dbSNP:rs28908468 [NCBI]). VAR_051730 
CONFLICT   281   281        S -> P (in Ref. 7; AAN60542/AAN60543/AAN60544). 
Sequence information
Length: 384 AA [This is the length of the unprocessed precursor] Molecular weight: 42196 Da [This is the MW of the unprocessed precursor] CRC64: DB0B9AE82F44A52B [This is a checksum on the sequence]
        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 

O15315 in FASTA format

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