REPAIRtoire - a database of DNA repair pathways

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Rad54l

Protein FULL name:

DNA repair and recombination protein RAD54-like [Mus musculus].


Rad54l (Mus musculus) is product of expression of Rad54l gene.






FUNCTION: Involved in DNA repair and mitotic recombination. Functions in the recombinational DNA repair (RAD52) pathway. Dissociates RAD51 from nucleoprotein filaments formed on dsDNA. Could be involved in the turnover of RAD51 protein-dsDNA filaments (By similarity). Deficient mice also show significantly shorter telomeres than wild-type controls, indicating that the protein activity plays an essential role in telomere length maintenance in mammals. Deficiency also resulted in an increased frequency of end-to-end chromosome fusions involving telomeres compared to the controls, suggesting a putative role in telomere capping. Non- homologous end joining (NHEJ) and homologous recombination (HR) represent the two major pathways of DNA double-strand break (DSB) repair in eukaryotic cells. LIG4 and RAD54L cooperate to support cellular proliferation, repair spontaneous DSBs, and prevent chromosome and single chromatid aberrations.

SUBUNIT: Interacts (via N-terminus) with RAD51 (By similarity).

SUBCELLULAR LOCATION: Nucleus (Probable).

TISSUE SPECIFICITY: Hardly detectable in most tissues. Dramatically increased in thymus, spleen and testis.

MISCELLANEOUS: The nucleus of a mouse embryonic stem (ES) cell contains on average 2.4 x 10(5) molecules.

SIMILARITY: Belongs to the SNF2/RAD54 helicase family.

SIMILARITY: Contains 1 helicase ATP-binding domain.

SIMILARITY: Contains 1 helicase C-terminal domain.


NCBI GenPept GI number(s): 171906595
Species: Mus musculus

Links to other databases:

Database ID Link
Uniprot P70270 P70270
PFAM: - P70270 (Link - using uniprot id)
InterPro: - P70270 (Link - using uniprot id)
CATH: - -
SCOP: - -
PDB: - -


Protein sequence:
MRRSLAPSQLARRKPEDRSSDDEDWQPGTVTPKKRKSSSETQVQECFLSP
FRKPLTQLLNRPPCLDSSQHEAFIRSILSKPFKVPIPNYQGPLGSRALGL
KRAGVRRALHDPLEEGALVLYEPPPLSAHDQLKLDKEKLPVHVVVDPILS
KVLRPHQREGVKFLWECVTSRRIPGSHGCIMADEMGLGKTLQCITLMWTL
LRQSPECKPEIEKAVVVSPSSLVKNWYNEVEKWLGGRIQPLAIDGGSKDE
IDRKLEGFMNQRGARVPSPILIISYETFRLHVGVLKKGNVGLVICDEGHR
LKNSENQTYQALDSLNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTA
HEFKKHFELPILKSRDAAASEADRQRGEERLRELIGIVNRCLIRRTSDIL
SKYLPVKIEQVVCCRLTPLQTELYKRFLRQAKPEEELREGKMSVSSLSSI
TSLKKLCNHPALIYDKCVAEEDGFEGTLGIFPPGYNSKAVEPQLSGKMLV
LDYILAVTRSRSSDKVVLVSNYTQTLDLFEKLCRVRRYLYVRLDGTMSIK
KRAKVVERFNSPSSPDFVFMLSSKAGGCGLNLIGANRLVMFDPDWNPAND
EQAMARVWRDGQKKICYIYRLLSAGTIEEKIFQRQSHKKALSSCVVDEEQ
DVERHFSLGELKELFTLDEASLSDTHDRLHCRRCVNNRQVWPPPDGSDCT
SDLAQWNHSTDKRGLQDEVLQAAWDASSTAITFVFHQRSHEEQRGLH

Rad54l (Mus musculus) belongs to following protein families:
References:

Title Authors Journal
Human and mouse homologs of the Saccharomyces cerevisiae RAD54 DNA repair gene: evidence for functional conservation. Kanaar R, Troelstra C, Swagemakers SM, Essers J, Smit B, Franssen JH, Pastink A, Bezzubova OY, Buerstedde JM, Clever B, Heyer WD, Hoeijmakers JH Curr Biol July 1, 1996
Disruption of mouse RAD54 reduces ionizing radiation resistance and homologous recombination. Essers J, Hendriks RW, Swagemakers SM, Troelstra C, de Wit J, Bootsma D, Hoeijmakers JH, Kanaar R Cell April 18, 1997
Mouse Rad54 affects DNA conformation and DNA-damage-induced Rad51 foci formation. Tan TL, Essers J, Citterio E, Swagemakers SM, de Wit J, Benson FE, Hoeijmakers JH, Kanaar R Curr Biol March 25, 1999
Mouse RAD54 affects DNA double-strand break repair and sister chromatid exchange. Dronkert ML, Beverloo HB, Johnson RD, Hoeijmakers JH, Jasin M, Kanaar R Mol Cell Biol May 1, 2000
Gene conversion-like sequence transfers between transgenic antibody V genes are independent of RAD54. D'Avirro N, Truong D, Luong M, Kanaar R, Selsing E J Immunol Sept. 15, 2002
Analysis of mouse Rad54 expression and its implications for homologous recombination. Essers J, Hendriks RW, Wesoly J, Beerens CE, Smit B, Hoeijmakers JH, Wyman C, Dronkert ML, Kanaar R DNA Repair (Amst) Oct. 1, 2002
Somatic hypermutation does not require Rad54 and Rad54B-mediated homologous recombination. Bross L, Wesoly J, Buerstedde JM, Kanaar R, Jacobs H Eur J Immunol Jan. 1, 2003
Role of mammalian Rad54 in telomere length maintenance. Jaco I, Munoz P, Goytisolo F, Wesoly J, Bailey S, Taccioli G, Blasco MA Mol Cell Biol Aug. 1, 2003
Rad54 and DNA Ligase IV cooperate to maintain mammalian chromatid stability. Mills KD, Ferguson DO, Essers J, Eckersdorff M, Kanaar R, Alt FW Genes Dev June 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 transcriptional landscape of the mammalian genome. Carninci P, Kasukawa T, Katayama S, Gough J, Frith MC, Maeda N, Oyama R, Ravasi T, Lenhard B, Wells C, Kodzius R, Shimokawa K, Bajic VB, Brenner SE, Batalov S, Forrest AR, Zavolan M, Davis MJ, Wilming LG, Aidinis V, Allen JE, Ambesi-Impiombato A, Apweiler R, Aturaliya RN, Bailey TL, Bansal M, Baxter L, Beisel KW, Bersano T, Bono H, Chalk AM, Chiu KP, Choudhary V, Christoffels A, Clutterbuck DR, Crowe ML, Dalla E, Dalrymple BP, de Bono B, Della Gatta G, di Bernardo D, Down T, Engstrom P, Fagiolini M, Faulkner G, Fletcher CF, Fukushima T, Furuno M, Futaki S, Gariboldi M, Georgii-Hemming P, Gingeras TR, Gojobori T, Green RE, Gustincich S, Harbers M, Hayashi Y, Hensch TK, Hirokawa N, Hill D, Huminiecki L, Iacono M, Ikeo K, Iwama A, Ishikawa T, Jakt M, Kanapin A, Katoh M, Kawasawa Y, Kelso J, Kitamura H, Kitano H, Kollias G, Krishnan SP, Kruger A, Kummerfeld SK, Kurochkin IV, Lareau LF, Lazarevic D, Lipovich L, Liu J, Liuni S, McWilliam S, Madan Babu M, Madera M, Marchionni L, Matsuda H, Matsuzawa S, Miki H, Mignone F, Miyake S, Morris K, Mottagui-Tabar S, Mulder N, Nakano N, Nakauchi H, Ng P, Nilsson R, Nishiguchi S, Nishikawa S, Nori F, Ohara O, Okazaki Y, Orlando V, Pang KC, Pavan WJ, Pavesi G, Pesole G, Petrovsky N, Piazza S, Reed J, Reid JF, Ring BZ, Ringwald M, Rost B, Ruan Y, Salzberg SL, Sandelin A, Schneider C, Schonbach C, Sekiguchi K, Semple CA, Seno S, Sessa L, Sheng Y, Shibata Y, Shimada H, Shimada K, Silva D, Sinclair B, Sperling S, Stupka E, Sugiura K, Sultana R, Takenaka Y, Taki K, Tammoja K, Tan SL, Tang S, Taylor MS, Tegner J, Teichmann SA, Ueda HR, van Nimwegen E, Verardo R, Wei CL, Yagi K, Yamanishi H, Zabarovsky E, Zhu S, Zimmer A, Hide W, Bult C, Grimmond SM, Teasdale RD, Liu ET, Brusic V, Quackenbush J, Wahlestedt C, Mattick JS, Hume DA, Kai C, Sasaki D, Tomaru Y, Fukuda S, Kanamori-Katayama M, Suzuki M, Aoki J, Arakawa T, Iida J, Imamura K, Itoh M, Kato T, Kawaji H, Kawagashira N, Kawashima T, Kojima M, Kondo S, Konno H, Nakano K, Ninomiya N, Nishio T, Okada M, Plessy C, Shibata K, Shiraki T, Suzuki S, Tagami M, Waki K, Watahiki A, Okamura-Oho Y, Suzuki H, Kawai J, Hayashizaki Y Science Sept. 2, 2005


Last modification of this entry: Oct. 6, 2010.

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