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RAD54L |
Protein FULL name:
RAD54-like protein [Homo sapiens].
RAD54L (Homo sapiens) 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). May play also an essential role in telomere length maintenance and telomere capping in mammalian cells.
SUBUNIT: Interacts (via N-terminus) with RAD51.
SUBCELLULAR LOCATION: Nucleus.
INDUCTION: Expression increases approximately 3-fold in late G1 phase compared to other phases of the cell cycle.
SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
SIMILARITY: Contains 1 helicase ATP-binding domain.
SIMILARITY: Contains 1 helicase C-terminal domain.
WEB RESOURCE: Name=NIEHS-SNPs; [LINK]
| NCBI GenPept GI number(s): |
4506397 |
| Species: | Homo sapiens |
Links to other databases:
| Database | ID | Link |
| Uniprot | Q92698 |
Q92698 |
| PFAM: | - |
Q92698 (Link - using uniprot id) |
| InterPro: | - |
Q92698 (Link - using uniprot id) |
| CATH: | - | - |
| SCOP: | - | - |
| PDB: | - | - |
Protein sequence:
|
MRRSLAPSQLAKRKPEGRSCDDEDWQPGLVTPRKRKSSSETQIQECFLSP FRKPLSQLTNQPPCLDSSQHEAFIRSILSKPFKVPIPNYQGPLGSRALGL KRAGVRRALHDPLEKDALVLYEPPPLSAHDQLKLDKEKLPVHVVVDPILS KVLRPHQREGVKFLWECVTSRRIPGSHGCIMADEMGLGKTLQCITLMWTL LRQSPECKPEIDKAVVVSPSSLVKNWYNEVGKWLGGRIQPLAIDGGSKDE IDQKLEGFMNQRGARVSSPILIISYETFRLHVGVLQKGSVGLVICDEGHR LKNSENQTYQALDSLNTSRRVLISGTPIQNDLLEYFSLVHFVNSGILGTA HEFKKHFELPILKGRDAAASEADRQLGEERLRELTSIVNRCLIRRTSDIL SKYLPVKIEQVVCCRLTPLQTELYKRFLRQAKPAEELLEGKMSVSSLSSI TSLKKLCNHPALIYDKCVEEEDGFVGALDLFPPGYSSKALEPQLSGKMLV LDYILAVTRSRSSDKVVLVSNYTQTLDLFEKLCRARRYLYVRLDGTMSIK KRAKVVERFNSPSSPDFVFMLSSKAGGCGLNLIGANRLVMFDPDWNPAND EQAMARVWRDGQKKTCYIYRLLSAGTIEEKIFQRQSHKKALSSCVVDEEQ DVERHFSLGELKELFILDEASLSDTHDRLHCRRCVNSRQIRPPPDGSDCT SDLAGWNHCTDKWGLRDEVLQAAWDAASTAITFVFHQHSHEEQRGLR |
RAD54L (Homo sapiens) is able to recognize following damages:
RAD54L (Homo sapiens) 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 |
| Characterization of the human homologue of RAD54: a gene located on chromosome 1p32 at a region of high loss of heterozygosity in breast tumors. | Rasio D, Murakumo Y, Robbins D, Roth T, Silver A, Negrini M, Schmidt C, Burczak J, Fishel R, Croce CM | Cancer Res June 15, 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 |
| The human RAD54 recombinational DNA repair protein is a double-stranded DNA-dependent ATPase. | Swagemakers SM, Essers J, de Wit J, Hoeijmakers JH, Kanaar R | J Biol Chem Oct. 23, 1998 |
| Mutations in the RAD54 recombination gene in primary cancers. | Matsuda M, Miyagawa K, Takahashi M, Fukuda T, Kataoka T, Asahara T, Inui H, Watatani M, Yasutomi M, Kamada N, Dohi K, Kamiya K | Oncogene June 3, 1999 |
| Analysis of the RAD54 gene on chromosome 1p as a potential tumor-suppressor gene in parathyroid adenomas. | Carling T, Imanishi Y, Gaz RD, Arnold A | Int J Cancer Sept. 24, 1999 |
| The architecture of the human Rad54-DNA complex provides evidence for protein translocation along DNA. | Ristic D, Wyman C, Paulusma C, Kanaar R | Proc Natl Acad Sci U S A July 17, 2001 |
| 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 |
| 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 DNA sequence and biological annotation of human chromosome 1. | Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E | Nature May 18, 2006 |
Last modification of this entry: Oct. 11, 2010.
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