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Rad50

Protein FULL name:

DNA repair protein RAD50 [Mus musculus].


Rad50 (Mus musculus) is product of expression of Rad50 gene.






FUNCTION: Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis. The complex possesses single-strand endonuclease activity and double-strand- specific 3'-5' exonuclease activity, which are provided by MRE11A. RAD50 may be required to bind DNA ends and hold them in close proximity. This could facilitate searches for short or long regions of sequence homology in the recombining DNA templates, and may also stimulate the activity of DNA ligases and/or restrict the nuclease activity of MRE11A to prevent nucleolytic degradation past a given point. The complex may also be required for DNA damage signaling via activation of the ATM kinase. In telomeres the MRN complex may modulate t-loop formation (By similarity).

COFACTOR: Binds 1 zinc ion per homodimer (By similarity).

SUBUNIT: Component of the MRN complex composed of two heterodimers RAD50/MRE11A associated with a single NBN. Component of the BASC complex, at least composed of BRCA1, MSH2, MSH6, MLH1, ATM, BLM, RAD50, MRE11A and NBN. Found in a complex with TERF2. Interacts with RINT1. Interacts with BRCA1 via its N-terminal domain. Interacts with DCLRE1C/Artemis (By similarity).

SUBCELLULAR LOCATION: Nucleus (By similarity). Telomere (By similarity). Note=Localizes to discrete nuclear foci after treatment with genotoxic agents (By similarity).

TISSUE SPECIFICITY: In adult, it is expressed at very low level in most tissues, except in heart, lung and aorta. Expressed at high level in testis.

DEVELOPMENTAL STAGE: Widely expressed. Expressed at higher level in heart, liver and thymus from E18. By neonatal day 1.5, it decreases in brain, liver, gut and skin, while it is expressed in spleen.

DOMAIN: The zinc-hook, which separates the large intramolecular coiled coil regions, contains 2 Cys residues that coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc- hook of another RAD50 molecule, thereby forming a V-shaped homodimer. The two heads of the homodimer, which constitute the ATP-binding domain, interact with the MRE11A homodimer (By similarity).

PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.

DISRUPTION PHENOTYPE: Defects cause embryonic stem cell lethality, abnormal embryonic development and sensitivity to ionizing radiation.

SIMILARITY: Belongs to the SMC family. RAD50 subfamily.

SIMILARITY: Contains 1 zinc-hook domain.


NCBI GenPept GI number(s): 153945822
Species: Mus musculus

Links to other databases:

Database ID Link
Uniprot P70388 P70388
PFAM: - P70388 (Link - using uniprot id)
InterPro: - P70388 (Link - using uniprot id)
CATH: - -
SCOP: - -
PDB: - -


Protein sequence:
MSRIEKMSILGVRSFGIEDKDKQIISFFSPLTILVGPNGAGKTTIIECLK
YICTGDFPPGTKGNTFVHDPKVAQETDVRAQIRLQFRDVNGEMVAVHRSM
LCSQKNKKTEFKTLEGVITRMKHGEKVSLSSKCAEIDREMISCLGVSKSV
LNNVIFCHQEDSNWPLSEGKALKQKFDEIFSATRYIKALDTLRQVRQTQG
QKVKECQTELKYLKQNKEKACEIRDQITSKEAQLASSQEIVRSYEDELEP
LKNRLKEIEHNLSKIMKLDNEIKALESRKKQMEKDNSELEQKMEKVFQGT
DEQLNDLYHNHQRTVREKERRLVDCQRELEKLNKEARLLNQEKAELLVEQ
GRLQLQADRHQEHIRARDSLIQSLATHLELDGFERGPFSERQIKNFHELV
KERQEREAKTASQLLSDLTDKEALKQRQLDELRDRKSGLGRTIELKTEIL
TKKQSELRHVRSELQQLEGSSDRILELDQELTKAERELSKAEKNSSIETL
KAEVMSLQNEKADLDRSLRKLDQEMEQLNHHTTTRTQMEMLTKDKTDKDE
QIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKE
LASAEQNKNHINNELKKKEEQLSSYEDKLFDVCGSQDLESDLGRLKEEIE
KSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEVISD
LQSKLRLAPDKLKSTESELKKKERRRDEMLGLVPVRQSIIDLKEKEIPEL
RNRLQSVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQM
ELKDVERKIAQQAAKLQGVDLDRTVQQVNQEKQEKQHRLDTVTSKIELNR
KLIQDQQEQIQHLKSKTNELKSEKLQIATNLQRRQQMEEQSVELSTEVQS
LNREIKDAKEQISPLETALEKLQQEKEELIHRKHTSNKMAQDKINDIKEK
VKNIHGYMKDIENYIQDGKDDYKKQKETELNGVAVQLNECEKHREKINKD
MGTMRQDIDTQKIQERWLQDNLTLRKRRDELKEVEEERKQHLKEMGQMQV
LQMKNEHQKLEENIDTIKRNHSLALGRQKGYEDEILHFKKELREPQFRDA
EEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMKMEEINKIIRDL
WRSTYRGQDIEYIEIRSDADENVSASDKRRNYNYRVVMLKGDTALDMRGR
CSAGQKVLASLIIRLALAETFCLNCGILALDEPTTNLDRENIESLAHALV
EIIKSRSQQRNFQLLVITHDEDFVELLGRSEYVEKFYRVKKNMDQCSEIV
KCSISSLGSYVH

Rad50 (Mus musculus) belongs to following protein families:
References:

Title Authors Journal
Mouse RAD50 has limited epitopic homology to p53 and is expressed in the adult myocardium. Kim KK, Daud AI, Wong SC, Pajak L, Tsai SC, Wang H, Henzel WJ, Field LJ J Biol Chem Nov. 15, 1996
Disruption of mRad50 causes embryonic stem cell lethality, abnormal embryonic development, and sensitivity to ionizing radiation. Luo G, Yao MS, Bender CF, Mills M, Bladl AR, Bradley A, Petrini JH Proc Natl Acad Sci U S A June 22, 1999
Cancer predisposition and hematopoietic failure in Rad50(S/S) mice. Bender CF, Sikes ML, Sullivan R, Huye LE, Le Beau MM, Roth DB, Mirzoeva OK, Oltz EM, Petrini JH Genes Dev Sept. 1, 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 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
ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ Science May 25, 2007


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

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