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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]
Links to other databases:
Protein sequence:
MAMQMQLEANADTSVEEESFGPQPISRLEQCGINANDVKKLEEAGFHTVE
AVAYAPKKELINIKGISEAKADKILAEAAKLVPMGFTTATEFHQRRSEII
QITTGSKELDKLLQGGIETGSITEMFGEFRTGKTQICHTLAVTCQLPIDR
GGGEGKAMYIDTEGTFRPERLLAVAERYGLSGSDVLDNVAYARAFNTDHQ
TQLLYQASAMMVESRYALLIVDSATALYRTDYSGRGELSARQMHLARFLR
MLLRLADEFGVAVVITNQVVAQVDGAAMFAADPKKPIGGNIIAHASTTRL
YLRKGRGETRICKIYDSPCLPEAEAMFAINADGVGDAKD
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RAD51 (Homo sapiens) is able to recognize following damages:
RAD51 (Homo sapiens) belongs to following protein families:
References:
Title
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Authors
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Journal
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Cloning and sequence of the human RecA-like gene cDNA.
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Yoshimura Y, Morita T, Yamamoto A, Matsushiro A
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Nucleic Acids Res
April 11, 1993
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Cloning of human, mouse and fission yeast recombination genes homologous to RAD51 and recA.
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Shinohara A, Ogawa H, Matsuda Y, Ushio N, Ikeo K, Ogawa T
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Nat Genet
July 1, 1993
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Purification and characterization of the human Rad51 protein, an analogue of E. coli RecA.
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Benson FE, Stasiak A, West SC
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EMBO J
Dec. 1, 1994
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RAB22 and RAB163/mouse BRCA2: proteins that specifically interact with the RAD51 protein.
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Mizuta R, LaSalle JM, Cheng HL, Shinohara A, Ogawa H, Copeland N, Jenkins NA, Lalande M, Alt FW
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Proc Natl Acad Sci U S A
June 24, 1997
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Interaction of human recombination proteins Rad51 and Rad54.
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Golub EI, Kovalenko OV, Gupta RC, Ward DC, Radding CM
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Nucleic Acids Res
Oct. 15, 1997
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A novel nucleic acid-binding protein that interacts with human rad51 recombinase.
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Kovalenko OV, Golub EI, Bray-Ward P, Ward DC, Radding CM
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Nucleic Acids Res
Dec. 15, 1997
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The N-terminal domain of the human Rad51 protein binds DNA: structure and a DNA binding surface as revealed by NMR.
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Aihara H, Ito Y, Kurumizaka H, Yokoyama S, Shibata T
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J Mol Biol
July 9, 1999
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Characterization of the human Rad51 genomic locus and examination of tumors with 15q14-15 loss of heterozygosity (LOH).
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Schmutte C, Tombline G, Rhiem K, Sadoff MM, Schmutzler R, von Deimling A, Fishel R
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Cancer Res
Sept. 15, 1999
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Identification of Rad51 alteration in patients with bilateral breast cancer.
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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
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J Hum Genet
Jan. 1, 2000
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A novel human rad54 homologue, Rad54B, associates with Rad51.
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Tanaka K, Hiramoto T, Fukuda T, Miyagawa K
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J Biol Chem
Aug. 25, 2000
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A single nucleotide polymorphism in the 5' untranslated region of RAD51 and risk of cancer among BRCA1/2 mutation carriers.
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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
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Cancer Epidemiol Biomarkers Prev
Sept. 1, 2001
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Involvement of Rad51C in two distinct protein complexes of Rad51 paralogs in human cells.
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Liu N, Schild D, Thelen MP, Thompson LH
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Nucleic Acids Res
Jan. 15, 2002
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Homologous DNA pairing by human recombination factors Rad51 and Rad54.
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Sigurdsson S, Van Komen S, Petukhova G, Sung P
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J Biol Chem
Nov. 8, 2002
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Complex formation by the human Rad51B and Rad51C DNA repair proteins and their activities in vitro.
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Lio YC, Mazin AV, Kowalczykowski SC, Chen DJ
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J Biol Chem
Feb. 24, 2003
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Complete sequencing and characterization of 21,243 full-length human cDNAs.
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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
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Nat Genet
Feb. 1, 2004
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The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
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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
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Genome Res
Oct. 1, 2004
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The cell-cycle checkpoint kinase Chk1 is required for mammalian homologous recombination repair.
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Sorensen CS, Hansen LT, Dziegielewski J, Syljuasen RG, Lundin C, Bartek J, Helleday T
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Nat Cell Biol
Jan. 1, 2005
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RAD51AP2, a novel vertebrate- and meiotic-specific protein, shares a conserved RAD51-interacting C-terminal domain with RAD51AP1/PIR51.
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Kovalenko OV, Wiese C, Schild D
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Nucleic Acids Res
Jan. 1, 2006
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Single-stranded DNA-binding protein hSSB1 is critical for genomic stability.
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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
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Nature
May 1, 2008
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Last modification of this entry: June 19, 2013.
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