Liu Q, Jin C, Liao X, Shen Z, Chen D J, Chen Y
Division of Immunology, Beckman Research Institute of the City of Hope, Duarte, California 91010, USA.
J Biol Chem. 1999 Jun 11;274(24):16979-87. doi: 10.1074/jbc.274.24.16979.
Human UBC9 is a member of the E2 (ubiquitin conjugation enzyme) family of proteins. Instead of conjugating to ubiquitin, it conjugates with a ubiquitin homologue UBL1 (also known as SUMO-1, GMP1, SMTP3, PIC1, and sentrin). UBC9 has been shown to be involved in cell cycle regulation, DNA repair, and p53-dependent processes. The binding interfaces of the UBC9 and UBL1 complex have been determined by chemical shift perturbation using nuclear magnetic resonance spectroscopy. The binding site of UBL1 resides on the ubiquitin domain, and the binding site of UBC9 is located on a structurally conserved region of E2. Because the UBC9-UBL1 system shares many similarities with the ubiquitin system in structures and in conjugation with each other and with target proteins, the observed binding interfaces may be conserved in E2-ubiquitin interactions in general.
人UBC9是E2（泛素缀合酶）蛋白家族的成员。它不是与泛素缀合，而是与泛素同源物UBL1（也称为SUMO-1、GMP1、SMTP3、PIC1和sentrin）缀合。已证明UBC9参与细胞周期调控、DNA修复和p53依赖性过程。UBC9与UBL1复合物的结合界面已通过使用核磁共振光谱的化学位移扰动来确定。UBL1的结合位点位于泛素结构域上，而UBC9的结合位点位于E2的结构保守区域。由于UBC9-UBL1系统在结构上以及彼此之间和与靶蛋白的缀合方面与泛素系统有许多相似之处，因此观察到的结合界面可能在一般的E2-泛素相互作用中是保守的。
