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Protein FULL name: ubiquitin-conjugating enzyme E2B, RAD6 homology [Mus musculus].
Ube2b (Mus musculus) is product of expression of
Ube2b
gene.
FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
proteins. Required for postreplication repair of UV-damaged DNA.
Associates to the E3 ligase RAD18 to form the UBE2B-RAD18
ubiquitin ligase complex involved in mono-ubiquitination of DNA-
associated PCNA on 'Lys-164'. May be involved in neurite outgrowth
(By similarity).
CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP +
diphosphate + protein N-ubiquityllysine.
PATHWAY: Protein modification; protein ubiquitination.
SUBUNIT: Interacts with RAD18 and UBR2.
SUBCELLULAR LOCATION: Cell membrane (By similarity). Nucleus (By
similarity). Note=In peripheral neurons, expressed both at the
plasma membrane and in nuclei (By similarity).
SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
Links to other databases:
Protein sequence:
MSTPARERLMRDFKRLQEDPPVGVSGAPSENNIMQWNAVIFGPEGTPFED
GTFKLVIEFSEEYPNKPPTVRFLSKMFHPNVYADGSICLDILQNRWSPTY
DVSSILTSIQSLLDEPNPNSPANSQAAQLYQENKREYEKRVSAIVEQSWN
DS
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Ube2b (Mus musculus) belongs to following protein families:
References:
Title
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Authors
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Journal
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Inactivation of the HR6B ubiquitin-conjugating DNA repair enzyme in mice causes male sterility associated with chromatin modification.
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Roest HP, van Klaveren J, de Wit J, van Gurp CG, Koken MH, Vermey M, van Roijen JH, Hoogerbrugge JW, Vreeburg JT, Baarends WM, Bootsma D, Grootegoed JA, Hoeijmakers JH
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Cell
Sept. 6, 1996
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Female lethality and apoptosis of spermatocytes in mice lacking the UBR2 ubiquitin ligase of the N-end rule pathway.
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Kwon YT, Xia Z, An JY, Tasaki T, Davydov IV, Seo JW, Sheng J, Xie Y, Varshavsky A
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Mol Cell Biol
Nov. 1, 2003
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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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