脱ユビキチン化酵素
(Deubiquitinating Enzyme から転送)
出典: フリー百科事典『ウィキペディア（Wikipedia）』 (2021/04/30 15:45 UTC 版)
脱ユビキチン化酵素（だつユビキチンかこうそ、英: deubiquitinating enzyme、略称: DUB）は、タンパク質からユビキチンを切断除去するプロテアーゼのグループである[1][2]。他にdeubiquitinating peptidase、deubiquitinating isopeptidase、deubiquitinase、ubiquitin protease、ubiquitin hydrolase、ubiquitin isopeptidaseなどとも呼ばれる。ユビキチンは、プロテアソームとリソソームを介したタンパク質分解の調節や、タンパク質の細胞内局在の調整、タンパク質の活性化や不活性化、タンパク質間相互作用の調節のためにタンパク質に付加される[3][4][5]。DUBはユビキチンと基質の間のペプチド結合またはイソペプチド結合を切断することで、ユビキチン化による効果を逆転させる。ヒトには約100種類のDUBの遺伝子が存在し、システインプロテアーゼとメタロプロテアーゼという2つの主要なクラスに分類される。システインプロテアーゼグループのDUBは、USP（ubiquitin-specific protease）、UCH（ubiquitin C-terminal hydrolase）、MJD（Machado-Josephin domain protease）、OTU（ovarian tumour protease）ファミリーなどからなる。メタロプロテアーゼグループのDUBは、JAMM（Jab1/Mov34/Mpr1 Pad1 N-terminal+）ドメインプロテアーゼのみが含まれる[2]。
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[続きの解説]
「脱ユビキチン化酵素」の続きの解説一覧
- 1 脱ユビキチン化酵素とは
- 2 脱ユビキチン化酵素の概要
- 3 ドメイン
- 4 疾患における役割
- 脱ユビキチン化酵素のページへのリンク
