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Protein FULL name: RAD18 homolog [Mus musculus].
Rad18 (Mus musculus) is product of expression of
Rad18
gene.
FUNCTION: E3 ubiquitin-protein ligase involved in postreplication
repair of UV-damaged DNA. Postreplication repair functions in gap-
filling of a daughter strand on replication of damaged DNA.
Associates to the E2 ubiquitin conjugating enzyme UBE2B to form
the UBE2B-RAD18 ubiquitin ligase complex involved in mono-
ubiquitination of DNA-associated PCNA on 'Lys-164'. Has ssDNA
binding activity.
PATHWAY: Protein modification; protein ubiquitination.
SUBUNIT: Interacts with UBE2A and UBE2B. Interacts with HLTF and
SHPRH (By similarity).
SUBCELLULAR LOCATION: Nucleus.
TISSUE SPECIFICITY: Expressed in thymus, spleen, brain, and ovary.
SIMILARITY: Belongs to the RAD18 family.
SIMILARITY: Contains 1 Rad18-type zinc finger.
SIMILARITY: Contains 1 RING-type zinc finger.
SIMILARITY: Contains 1 SAP domain.
Links to other databases:
Protein sequence:
MEVLAEPRCPPGLAVMKTIDDLLRCGICFEYFNIAVIIPQCSHNYCSLCI
RKFLSYKTQCPTCCVAVTEPDLRNNRLLDELVKSMNFARTHLLQFALESP
PISPVSSTSKKVVVKVHNADAAQHPVKQANRLMDKFLIRETGDCVFELLG
KENERKFSPQKELSTSAEIKETSLLGKPVLGLSDANGPVTPSTSTMKLDT
KVSCPVCGVSIPENHINKHLDSCLSREEKKESLRSSAHKRKPLPKTVYNL
LSDRDLKKKLKQYGLSVPGNKQQLIKRHQEFVHMYNAQCDALHPKSAAEI
VQEIESMEKTRMRLEASKLNENVMVFTKNQTEKEIEEVHSEYRKKHQNAF
QLLVDQAKKGYKKTGRVSQAAAMRTDEPAETLPSMRTDEPAETLPSMRTD
EPAETLPLMRADEPAETLPSECIAQEDNVSFSDTVSVTNHFPQPQLDSPG
PSEPERPDDSSSCTDILFSSDSDSCNRNDQNREVSPQQTRRTRASECVEI
EPRNKRNKN
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Rad18 (Mus musculus) belongs to following protein families:
References:
Title
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Authors
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Journal
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Characterization of mRAD18Sc, a mouse homolog of the yeast postreplication repair gene RAD18.
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van der Laan R, Roest HP, Hoogerbrugge JW, Smit EM, Slater R, Baarends WM, Hoeijmakers JH, Grootegoed JA
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Genomics
Oct. 1, 2000
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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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