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RAD51

Protein FULL name:

DNA repair protein RAD51 homolog 1 isoform 1 [Homo sapiens].


RAD51 (Homo sapiens) is product of expression of RAD51 gene.

Human diseases related to this protein:

RAD51 is involved in:

HRR in Homo sapiens

Keywords:



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: 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.

INTERACTION: Self; NbExp=1; IntAct=EBI-297202, EBI-297202; P51587:BRCA2; NbExp=7; IntAct=EBI-297202, EBI-79792; Q9Y376:CAB39; NbExp=1; IntAct=EBI-297202, EBI-306905; P41214:LGTN; NbExp=1; IntAct=EBI-297202, EBI-1055793; Q9BQ15:OBFC2B; NbExp=1; IntAct=EBI-297202, EBI-2120336; Q96B01-2:RAD51AP1; NbExp=2; IntAct=EBI-297202, EBI-1178743; Q96B01-3:RAD51AP1; NbExp=3; IntAct=EBI-297202, EBI-1178748; P36601:rhp51 (xeno); NbExp=2; IntAct=EBI-297202, EBI-926960; Q9Y5L4:TIMM13; NbExp=1; IntAct=EBI-297202, EBI-1057344; P04637:TP53; NbExp=1; IntAct=EBI-297202, EBI-366083;

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.

PTM: 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.

DISEASE: Defects in RAD51 are a cause of susceptibility to breast cancer (BC) [MIM:114480]. A common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case.

SIMILARITY: Belongs to the recA family. RAD51 subfamily.

SIMILARITY: Contains 1 HhH domain.

WEB RESOURCE: Name=NIEHS-SNPs; [LINK]


NCBI GenPept GI number(s): 19924133
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot Q06609 Q06609
PFAM: - Q06609 (Link - using uniprot id)
InterPro: - Q06609 (Link - using uniprot id)
CATH: None  
SCOP: None  
PDB: - -


Protein sequence:
MAMQMQLEANADTSVEEESFGPQPISRLEQCGINANDVKKLEEAGFHTVE
AVAYAPKKELINIKGISEAKADKILAEAAKLVPMGFTTATEFHQRRSEII
QITTGSKELDKLLQGGIETGSITEMFGEFRTGKTQICHTLAVTCQLPIDR
GGGEGKAMYIDTEGTFRPERLLAVAERYGLSGSDVLDNVAYARAFNTDHQ
TQLLYQASAMMVESRYALLIVDSATALYRTDYSGRGELSARQMHLARFLR
MLLRLADEFGVAVVITNQVVAQVDGAAMFAADPKKPIGGNIIAHASTTRL
YLRKGRGETRICKIYDSPCLPEAEAMFAINADGVGDAKD

RAD51 (Homo sapiens) is able to recognize following damages:
RAD51 (Homo sapiens) belongs to following protein families:
References:

Title Authors Journal
Cloning and sequence of the human RecA-like gene cDNA. Yoshimura Y, Morita T, Yamamoto A, Matsushiro A Nucleic Acids Res April 11, 1993
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 July 1, 1993
Purification and characterization of the human Rad51 protein, an analogue of E. coli RecA. Benson FE, Stasiak A, West SC EMBO J Dec. 1, 1994
RAB22 and RAB163/mouse BRCA2: proteins that specifically interact with the RAD51 protein. Mizuta R, LaSalle JM, Cheng HL, Shinohara A, Ogawa H, Copeland N, Jenkins NA, Lalande M, Alt FW Proc Natl Acad Sci U S A June 24, 1997
Interaction of human recombination proteins Rad51 and Rad54. Golub EI, Kovalenko OV, Gupta RC, Ward DC, Radding CM Nucleic Acids Res Oct. 15, 1997
A novel nucleic acid-binding protein that interacts with human rad51 recombinase. Kovalenko OV, Golub EI, Bray-Ward P, Ward DC, Radding CM Nucleic Acids Res Dec. 15, 1997
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 July 9, 1999
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 MM, Schmutzler R, von Deimling A, Fishel R Cancer Res Sept. 15, 1999
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 Jan. 1, 2000
A novel human rad54 homologue, Rad54B, associates with Rad51. Tanaka K, Hiramoto T, Fukuda T, Miyagawa K J Biol Chem Aug. 25, 2000
A single nucleotide polymorphism in the 5' untranslated region of RAD51 and risk of cancer among BRCA1/2 mutation carriers. Wang WW, Spurdle AB, Kolachana P, Bove B, Modan B, Ebbers SM, Suthers G, Tucker MA, Kaufman DJ, Doody MM, Tarone RE, Daly M, Levavi H, Pierce H, Chetrit A, Yechezkel GH, Chenevix-Trench G, Offit K, Godwin AK, Struewing JP Cancer Epidemiol Biomarkers Prev Sept. 1, 2001
Involvement of Rad51C in two distinct protein complexes of Rad51 paralogs in human cells. Liu N, Schild D, Thelen MP, Thompson LH Nucleic Acids Res Jan. 15, 2002
Homologous DNA pairing by human recombination factors Rad51 and Rad54. Sigurdsson S, Van Komen S, Petukhova G, Sung P J Biol Chem Nov. 8, 2002
Complex formation by the human Rad51B and Rad51C DNA repair proteins and their activities in vitro. Lio YC, Mazin AV, Kowalczykowski SC, Chen DJ J Biol Chem Feb. 24, 2003
Complete sequencing and characterization of 21,243 full-length human cDNAs. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S Nat Genet Feb. 1, 2004
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J Genome Res Oct. 1, 2004
The cell-cycle checkpoint kinase Chk1 is required for mammalian homologous recombination repair. Sorensen CS, Hansen LT, Dziegielewski J, Syljuasen RG, Lundin C, Bartek J, Helleday T Nat Cell Biol Jan. 1, 2005
RAD51AP2, a novel vertebrate- and meiotic-specific protein, shares a conserved RAD51-interacting C-terminal domain with RAD51AP1/PIR51. Kovalenko OV, Wiese C, Schild D Nucleic Acids Res Jan. 1, 2006
Single-stranded DNA-binding protein hSSB1 is critical for genomic stability. Richard DJ, Bolderson E, Cubeddu L, Wadsworth RI, Savage K, Sharma GG, Nicolette ML, Tsvetanov S, McIlwraith MJ, Pandita RK, Takeda S, Hay RT, Gautier J, West SC, Paull TT, Pandita TK, White MF, Khanna KK Nature May 1, 2008


Last modification of this entry: June 19, 2013.

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