DNA repair protein RAD51 homolog 1 - Homo sapiens (Human)

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

Alternative products

Sequence annotation (Features)

Sequences

References

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Secondary structure

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Reviewed, UniProtKB/Swiss-Prot Q06609 (RAD51_HUMAN)

Last modified November 25, 2008. Version 102. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Protein names

Recommended name:
    DNA repair protein RAD51 homolog 1
      Short name=hRAD51
      Short name=HsRAD51

Gene names

Name:	RAD51
Synonyms:	RAD51A, RECA

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

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Sequence length	339 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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Function	May participate in a common DNA damage response pathway associated with the activation of homologous recombination and double-strand break repair. Binds to single and double stranded DNA and exhibits DNA-dependent ATPase activity. Underwinds duplex DNA and forms helical nucleoprotein filaments.
Subunit structure	Interacts with BRCA1, BRCA2 and either directly or indirectly with p53. Interacts with XRCC3, RAD54L and RAD54B. Part of a complex with RAD51C and RAD51B. Interacts with RAD51AP1 and RAD51AP2. Interacts with CHEK1/CHK1, and this may require prior phosphorylation of CHEK1. Interacts with the MND1-PSMC3IP heterodimer By similarity. Interacts with OBFC2B.
Subcellular location	Nucleus. Note= Colocalizes with RAD51AP1 to multiple nuclear foci upon induction of DNA damage.
Tissue specificity	Highly expressed in testis and thymus, followed by small intestine, placenta, colon, pancreas and ovary. Weakly expressed in breast.
Post-translational modification	Phosphorylated. Phosphorylation of Thr-309 by CHEK1/CHK1 may enhance association with chromatin at sites of DNA damage and promote DNA repair by homologous recombination.
Involvement in disease	Defects in RAD51 are associated with breast cancer (BC) [MIM:114480].
Sequence similarities	Belongs to the recA family. RAD51 subfamily. Contains 1 HhH domain.

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Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Disease	Disease mutation
Ligand	ATP-binding DNA-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	DNA unwinding during replication Ref.8 Inferred from direct assay. Source: UniProtKB double-strand break repair via homologous recombination Ref.15 Traceable author statement. Source: UniProtKB mitotic recombination Ref.1 Traceable author statement. Source: ProtInc positive regulation of DNA ligation Inferred from direct assay. Source: UniProtKB protein homooligomerization Inferred from physical interaction. Source: UniProtKB reciprocal meiotic recombination Ref.1 Traceable author statement. Source: ProtInc
Cellular component	PML body Inferred from direct assay. Source: UniProtKB condensed nuclear chromosome Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	ATP binding Inferred from sequence or structural similarity. Source: UniProtKB damaged DNA binding Inferred from electronic annotation. Source: InterPro double-stranded DNA binding Ref.8 Inferred from direct assay. Source: UniProtKB identical protein binding Inferred from physical interaction. Source: IntAct protein C-terminus binding Inferred from physical interaction. Source: UniProtKB recombinase activity Inferred from sequence or structural similarity. Source: UniProtKB sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro single-stranded DNA binding Ref.8 Inferred from direct assay. Source: UniProtKB single-stranded DNA-dependent ATPase activity Ref.8 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

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With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-297202,EBI-297202
BRCA2	P51587	7	EBI-297202,EBI-79792
RAD51AP1	Q96B01-2	2	EBI-297202,EBI-1178743
RAD51AP1	Q96B01-3	3	EBI-297202,EBI-1178748
rhp51	P36601	2	EBI-297202,EBI-926960	From a different organism.
TP53	P04637	1	EBI-297202,EBI-366083

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Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Chain

1 – 339

339

DNA repair protein RAD51 homolog 1

PRO_0000122932

Domain

48 – 77

HhH

Nucleotide binding

127 – 134

ATP By similarity

Modified residue

309

Phosphothreonine; by CHK1

Alternative sequence

77 – 173

Missing in isoform 2.

VSP_005556

Natural variant

150

R → Q in BC; familial.

VAR_010899

Mutagenesis

309

T → A: Confers hypersensitivity to hydroxyurea

Sequence conflict

313

K → Q in BAA02962. Ref.1

339

Helix Strand Turn

Details...

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Sequence		Length	Mass (Da)
Isoform 1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 26578E6206DEDEDA Show »	FASTA	339	36,966
10 20 30 40 50 60 MAMQMQLEAN ADTSVEEESF GPQPISRLEQ CGINANDVKK LEEAGFHTVE AVAYAPKKEL 70 80 90 100 110 120 INIKGISEAK ADKILAEAAK LVPMGFTTAT EFHQRRSEII QITTGSKELD KLLQGGIETG 130 140 150 160 170 180 SITEMFGEFR TGKTQICHTL AVTCQLPIDR GGGEGKAMYI DTEGTFRPER LLAVAERYGL 190 200 210 220 230 240 SGSDVLDNVA YARAFNTDHQ TQLLYQASAM MVESRYALLI VDSATALYRT DYSGRGELSA 250 260 270 280 290 300 RQMHLARFLR MLLRLADEFG VAVVITNQVV AQVDGAAMFA ADPKKPIGGN IIAHASTTRL 310 320 330 YLRKGRGETR ICKIYDSPCL PEAEAMFAIN ADGVGDAKD « Hide
Isoform 2 [UniParc]. Checksum: DFA9E12DC8429CA2 Show »		242	26,351
10 20 30 40 50 60 MAMQMQLEAN ADTSVEEESF GPQPISRLEQ CGINANDVKK LEEAGFHTVE AVAYAPKKEL 70 80 90 100 110 120 INIKGISEAK ADKILAVAER YGLSGSDVLD NVAYARAFNT DHQTQLLYQA SAMMVESRYA 130 140 150 160 170 180 LLIVDSATAL YRTDYSGRGE LSARQMHLAR FLRMLLRLAD EFGVAVVITN QVVAQVDGAA 190 200 210 220 230 240 MFAADPKKPI GGNIIAHAST TRLYLRKGRG ETRICKIYDS PCLPEAEAMF AINADGVGDA KD « Hide

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This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q06609-1)

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: Q06609-2)

The sequence of this isoform differs from the canonical sequence as follows:
77-173: Missing.

Notes: No experimental confirmation available.

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of human, mouse and fission yeast recombination genes homologous to RAD51 and recA." Shinohara A., Ogawa H., Matsuda Y., Ushio N., Ikeo K., Ogawa T. Nat. Genet. 4:239-243(1993) [PubMed: 8358431] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Cloning and sequence of the human RecA-like gene cDNA." Yoshimura Y., Morita T., Yamamoto A., Matsushiro A. Nucleic Acids Res. 21:1665-1665(1993) [PubMed: 8479919] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Testis.
[3]	"Characterization of the human Rad51 genomic locus and examination of tumors with 15q14-15 loss of heterozygosity (LOH)." Schmutte C., Tombline G., Rhiem K., Sadoff M.M., Schmutzler R., von Deimling A., Fishel R. Cancer Res. 59:4564-4569(1999) [PubMed: 10493508] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"A single nucleotide polymorphism in the 5' untranslated region of RAD51 and risk of cancer among BRCA1/2 mutation carriers." Wang W.W., Spurdle A.B., Kolachana P., Bove B., Modan B., Ebbers S.M., Suthers G., Tucker M.A., Kaufman D.J., Doody M.M., Tarone R.E., Daly M., Levavi H., Pierce H., Chetrit A., Yechezkel G.H., Chenevix-Trench G., Offit K., Godwin A.K., Struewing J.P. Cancer Epidemiol. Biomarkers Prev. 10:955-960(2001) [PubMed: 11535547] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)." Rieder M.J., Livingston R.J., Daniels M.R., Montoya M.A., Chung M.-W., Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A. Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	"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 2). Tissue: Placenta.
[7]	"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 1).
[8]	"Purification and characterization of the human Rad51 protein, an analogue of E. coli RecA." Benson F.E., Stasiak A., West S.C. EMBO J. 13:5764-5771(1994) [PubMed: 7988572] [Abstract] Cited for: CHARACTERIZATION.
[9]	"Interaction of human recombination proteins Rad51 and Rad54." Golub E.I., Kovalenko O.V., Gupta R.C., Ward D.C., Radding C.M. Nucleic Acids Res. 25:4106-4110(1997) [PubMed: 9321665] [Abstract] Cited for: INTERACTION WITH RAD54L.
[10]	"A novel nucleic acid-binding protein that interacts with human rad51 recombinase." Kovalenko O.V., Golub E.I., Bray-Ward P., Ward D.C., Radding C.M. Nucleic Acids Res. 25:4946-4953(1997) [PubMed: 9396801] [Abstract] Cited for: INTERACTION WITH RAD51AP1.
[11]	"RAB22 and RAB163/mouse BRCA2: proteins that specifically interact with the RAD51 protein." Mizuta R., LaSalle J.M., Cheng H.-L., Shinohara A., Ogawa H., Copeland N.G., Jenkins N.A., Lalande M., Alt F.W. Proc. Natl. Acad. Sci. U.S.A. 94:6927-6932(1997) [PubMed: 9192668] [Abstract] Cited for: INTERACTION WITH RAD51AP1, SUBCELLULAR LOCATION.
[12]	"A novel human Rad54 homologue, Rad54B, associates with Rad51." Tanaka K., Hiramoto T., Fukuda T., Miyagawa K. J. Biol. Chem. 275:26316-26321(2000) [PubMed: 10851248] [Abstract] Cited for: INTERACTION WITH RAD54B.
[13]	"Homologous DNA pairing by human recombination factors Rad51 and Rad54." Sigurdsson S., Van Komen S., Petukhova G., Sung P. J. Biol. Chem. 277:42790-42794(2002) [PubMed: 12205100] [Abstract] Cited for: FUNCTION.
[14]	"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: INTERACTION WITH XRCC3.
[15]	"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 RAD51B AND RAD51C.
[16]	"The cell-cycle checkpoint kinase Chk1 is required for mammalian homologous recombination repair." Soerensen C.S., Hansen L.T., Dziegielewski J., Syljuaesen R.G., Lundin C., Bartek J., Helleday T. Nat. Cell Biol. 7:195-201(2005) [PubMed: 15665856] [Abstract] Cited for: INTERACTION WITH CHEK1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-309, MUTAGENESIS OF THR-309.
[17]	"RAD51AP2, a novel vertebrate- and meiotic-specific protein, shares a conserved RAD51-interacting C-terminal domain with RAD51AP1/PIR51." Kovalenko O.V., Wiese C., Schild D. Nucleic Acids Res. 34:5081-5092(2006) [PubMed: 16990250] [Abstract] Cited for: INTERACTION WITH RAD51AP2.
[18]	"Single-stranded DNA-binding protein hSSB1 is critical for genomic stability." Richard D.J., Bolderson E., Cubeddu L., Wadsworth R.I.M., Savage K., Sharma G.G., Nicolette M.L., Tsvetanov S., McIlwraith M.J., Pandita R.K., Takeda S., Hay R.T., Gautier J., West S.C., Paull T.T., Pandita T.K., White M.F., Khanna K.K. Nature 453:677-681(2008) [PubMed: 18449195] [Abstract] Cited for: INTERACTION WITH OBFC2B.
[19]	"The N-terminal domain of the human Rad51 protein binds DNA: structure and a DNA binding surface as revealed by NMR." Aihara H., Ito Y., Kurumizaka H., Yokoyama S., Shibata T. J. Mol. Biol. 290:495-504(1999) [PubMed: 10390347] [Abstract] Cited for: STRUCTURE BY NMR OF 1-114.
[20]	"Identification of Rad51 alteration in patients with bilateral breast cancer." Kato M., Yano K., Matsuo F., Saito H., Katagiri T., Kurumizaka H., Yoshimoto M., Kasumi F., Akiyama F., Sakamoto G., Nagawa H., Nakamura Y., Miki Y. J. Hum. Genet. 45:133-137(2000) [PubMed: 10807537] [Abstract] Cited for: VARIANT BC GLN-150.
+	Additional computationally mapped references.