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Protein FULL name: DNA repair protein RAD51 homolog 2 [Mus musculus].
Rad51l1 (Mus musculus) is product of expression of
Rad51l1
gene.
FUNCTION: Involved in the homologous recombination repair (HRR)
pathway of double-stranded DNA breaks arising during DNA
replication or induced by DNA-damaging agents. May promote the
assembly of presynaptic RAD51 nucleoprotein filaments. The RAD51B-
RAD51C dimer exhibits single-stranded DNA-dependent ATPase
activity. The BCDX2 complex binds single-stranded DNA, single-
stranded gaps in duplex DNA and specifically to nicks in duplex
DNA (By similarity).
SUBUNIT: Interacts with RAD51C. Part of a BCDX2 complex consisting
of RAD51B, RAD51C, RAD51D and XRCC2. Part of a complex consisting
of RAD51B, RAD51C, RAD51D, XRCC2 and XRCC3. Part of a complex with
RAD51C and RAD51 (By similarity).
SUBCELLULAR LOCATION: Nucleus (Probable).
TISSUE SPECIFICITY: Expressed in a wide range of tissues.
SIMILARITY: Belongs to the recA family. RAD51 subfamily.
Links to other databases:
Protein sequence:
MSSKKLRRVGLSPELCDRLSRYQIVNCQHFLSLSPLELMKVTGLSYRGVH
ELLHTVSKACAPQMQTAYELKTRRSAHLSPAFLSTTLCALDEALHGGVPC
GSLTEITGPPGCGKTQFCIMMSVLATLPTSLGGLEGAVVYIDTESAFTAE
RLVEIAESRFPQYFNTEEKLLLTSSRVHLCRELTCEGLLQRLESLEEEII
SKGVKLVIVDSIASVVRKEFDPKLQGNIKERNKFLGKGASLLKYLAGEFS
IPVILTNQITTHLSGALPSQADLVSPADDLSLSEGTSGSSCLVAALGNTW
GHCVNTRLILQYLDSERRQILIAKSPLAAFTSFVYTIKGEGLVLQGHERP
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Rad51l1 (Mus musculus) belongs to following protein families:
References:
Title
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Authors
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Journal
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Isolation of human and mouse genes based on homology to REC2, a recombinational repair gene from the fungus Ustilago maydis.
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Rice MC, Smith ST, Bullrich F, Havre P, Kmiec EB
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Proc Natl Acad Sci U S A
July 8, 1997
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The transcriptional landscape of the mammalian genome.
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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
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Science
Sept. 2, 2005
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Last modification of this entry: Oct. 6, 2010.
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