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Protein FULL name: ribonucleoside-diphosphate reductase subunit M2 B [Mus musculus].
Rrm2b (Mus musculus) is product of expression of
Rrm2b
gene.
FUNCTION: Plays a pivotal role in cell survival by repairing
damaged DNA in a p53/TP53-dependent manner. Supplies
deoxyribonucleotides for DNA repair in cells arrested at G1 or G2.
Contains an iron-tyrosyl free radical center required for
catalysis. Forms an active ribonucleotide reductase (RNR) complex
with RRM1 which is expressed both in resting and proliferating
cells in response to DNA damage.
CATALYTIC ACTIVITY: 2'-deoxyribonucleoside diphosphate +
thioredoxin disulfide + H(2)O = ribonucleoside diphosphate +
thioredoxin.
COFACTOR: Binds 2 iron ions per subunit (By similarity).
PATHWAY: Genetic information processing; DNA replication.
SUBUNIT: Heterotetramer with large (RRM1) subunit. Interacts with
p53/TP53. Interacts with RRM1 in response to DNA damage (By
similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
similarity). Note=Translocates from cytoplasm to nucleus in
response to DNA damage (By similarity).
DISRUPTION PHENOTYPE: Mice develop normally until they are weaned
but from then on exhibit growth retardation and early mortality.
Pathological examination indicates that multiple organs fail and
that they die from severe renal failure by the age of 14 weeks.
SIMILARITY: Belongs to the ribonucleoside diphosphate reductase
small chain family.
Links to other databases:
Protein sequence:
MGDPERPEAARPEKGEQLCSETEENVVRSNEEPLLRKSSRRFVIFPIQYP
DIWRMYKQAQASFWTAEEVDLSKDLPHWNKLKSDEKYFISHILAFFAASD
GIVNENLVERFSQEVQVPEARCFYGFQILIENVHSEMYSLLIDTYIRDPK
KREFLFNAIETMPYVKKKADWALRWIADRKSTFGERVVAFAAVEGIFFSG
SFAAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFQYLVNKPSEDR
VREIIADAVQIEQEFLTEALPVGLIGMNCVLMKQYIEFVADRLLGELGFS
KIFQAENPFDFMENISLEGKTNFFEKRVSEYQRFAVMAETTDNVFTLDAD
F
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Rrm2b (Mus musculus) belongs to following protein families:
References:
Title
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Authors
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Journal
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Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells.
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Guittet O, Hakansson P, Voevodskaya N, Fridd S, Graslund A, Arakawa H, Nakamura Y, Thelander L
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J Biol Chem
Nov. 2, 2001
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Impaired function of p53R2 in Rrm2b-null mice causes severe renal failure through attenuation of dNTP pools.
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Kimura T, Takeda S, Sagiya Y, Gotoh M, Nakamura Y, Arakawa H
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Nat Genet
Aug. 1, 2003
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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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Genome Res
Oct. 1, 2004
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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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