Reviewed, UniProtKB/Swiss-Prot O15315 (RA51B_HUMAN)

Names and origin

Protein names

Recommended name:
    DNA repair protein RAD51 homolog 2
      Short name=R51H2
Alternative name(s):
    RAD51-like protein 1
    Rad51B

Gene names

Name:	RAD51L1
Synonyms:	RAD51B, REC2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	384 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.12
Subcellular location	Nucleus Probable.
Tissue specificity	Expressed in a wide range of tissues.
Involvement in disease	A chromosomal aberration involving RAD51L1 is found in pulmonary chondroid hamartoma. Translocation t(6;14)(p21;q23-24) with HMGA1. A chromosomal aberration involving RAD51L1 is found in uterine leiomyoma (UL) [MIM:150699]. Translocation t(12;14)(q15;q23-24) with HMGA2.
Sequence similarities	Belongs to the recA family. RAD51 subfamily.

Ontologies

Keywords
Biological process	DNA damage DNA recombination DNA repair
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Ligand	ATP-binding DNA-binding Nucleotide-binding
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	DNA repair Ref.3 Traceable author statement. Source: ProtInc reciprocal meiotic recombination Ref.2 Traceable author statement. Source: ProtInc
Cellular component	nucleus Ref.3 Traceable author statement. Source: ProtInc
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Ref.3 Traceable author statement. Source: ProtInc DNA-dependent ATPase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 384	384	DNA repair protein RAD51 homolog 2		PRO_0000122939
Regions
	Nucleotide binding	108 – 115	8	ATP Potential
Sites
	Site	252 – 253	2	Breakpoint for translocation to form HMGA2-RAD51L1
Natural variations
	Alternative sequence	1 – 119	119	Missing in isoform 5.		VSP_008817
	Alternative sequence	346 – 384	39	ETTFC…TQLIF → AYGNS in isoform 2.		VSP_008819
	Alternative sequence	346 – 384	39	ETTFC…TQLIF → GQEKP in isoform 3 and isoform 5.		VSP_008818
	Alternative sequence	347 – 384	38	TTFCS…TQLIF → FWHICISGFSIQNRLKENES in isoform 4.		VSP_008820
	Natural variant	9	1	V → M: dbSNP rs34583846. Ref.5		VAR_025243
	Natural variant	82	1	F → C: dbSNP rs35282642. Ref.5		VAR_025244
	Natural variant	172	1	L → W: dbSNP rs34094401. Ref.5		VAR_025245
	Natural variant	180	1	Y → C: dbSNP rs28910275. Ref.5		VAR_025246
	Natural variant	207	1	V → L: dbSNP rs28908168.		VAR_035437
	Natural variant	243	1	K → R: dbSNP rs34594234. Ref.5		VAR_025247
	Natural variant	250	1	S → A: dbSNP rs33929366. Ref.5		VAR_025248
	Natural variant	365	1	P → R: dbSNP rs28908468.		VAR_051730
Experimental info
	Sequence conflict	281	1	S → P in AAN60542. Ref.9
	Sequence conflict	281	1	S → P in AAN60543. Ref.9
	Sequence conflict	281	1	S → P in AAN60544. Ref.9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 7, 2003. Version 2. Checksum: DB0B9AE82F44A52B	FASTA	384	42,196
	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
	Isoform 2 (RAD51L1a). Checksum: CEA992DDC394F3B0	FASTA	350	38,257
	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 SHSVNTRLIL QYLDSERRQI LIAKSPLAPF TSFVYTIKEE GLVLQAYGNS
	Isoform 3 (RAD51L1b). Checksum: CC7EE1B04634F3B0	FASTA	350	38,304
	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 SHSVNTRLIL QYLDSERRQI LIAKSPLAPF TSFVYTIKEE GLVLQGQEKP
	Isoform 4. Checksum: 790D20F0E8EB791A	FASTA	366	40,284
	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 GLVLQEFWHI CISGFSIQNR LKENES
	Isoform 5. Checksum: 2EAE6E210C8E74B6	FASTA	231	25,527
	10 20 30 40 50 60 MMSILATLPT NMGGLEGAVV YIDTESAFSA ERLVEIAESR FPRYFNTEEK LLLTSSKVHL 70 80 90 100 110 120 YRELTCDEVL QRIESLEEEI ISKGIKLVIL DSVASVVRKE FDAQLQGNLK ERNKFLAREA 130 140 150 160 170 180 SSLKYLAEEF SIPVILTNQI TTHLSGALAS QADLVSPADD LSLSEGTSGS SCVIAALGNT 190 200 210 220 230 WSHSVNTRLI LQYLDSERRQ ILIAKSPLAP FTSFVYTIKE EGLVLQGQEK P

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
+	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.
IPI	IPI00006105. IPI00220523. IPI00386489. IPI00386490. IPI00395987.
RefSeq	NP_002868.1. NP_598193.2. NP_598194.1.
UniGene	Hs.172587
3D structure databases
SMR	O15315. Positions 4-343.
ModBase	Search...
Protein-protein interaction databases
STRING	O15315.
Genome annotation databases
Ensembl	ENST00000402498; ENSP00000385485; ENSG00000182185; Homo sapiens. [Genome view] ENST00000487270; ENSP00000419471; ENSG00000182185; Homo sapiens. [Genome view]
GeneID	5890.
KEGG	hsa:5890.
NMPDR	fig|9606.3.peg.9776.
UCSC	uc001xkd.1. human. uc001xkf.1. human. uc001xkg.1. human.
Organism-specific databases
CTD	5890.
GeneCards	GC14P067356.
H-InvDB	HIX0022466.
HGNC	HGNC:9822. RAD51L1.
HPA	CAB016191.
MIM	150699. phenotype. 602948. gene.
PharmGKB	PA34178.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG16975.
HOVERGEN	O15315.
InParanoid	O15315.
OMA	RKEFDTQ.
PhylomeDB	O15315.
Gene expression databases
ArrayExpress	O15315.
Bgee	O15315.
Genevestigator	O15315.
Family and domain databases
InterPro	IPR003593. ATPase_AAA+_core. IPR013632. DNA_recomb/repair_Rad51_C. IPR016467. DNA_recomb/repair_RecA-like. IPR020588. DNA_recomb_RecA/RadB_ATP-bd. [Graphical view]
Pfam	PF08423. Rad51. 1 hit. [Graphical view]
PIRSF	PIRSF005856. Rad51. 1 hit.
SMART	SM00382. AAA. 1 hit. [Graphical view]
PROSITE	PS50162. RECA_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	22908.
SOURCE	Search...

Entry information

Entry name

RA51B_HUMAN

Accession

Primary (citable) accession number: O15315
Secondary accession number(s): O60914 , 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 19, 2010
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.