Ontology highlight
ABSTRACT:
SUBMITTER: Han Z
PROVIDER: S-EPMC5836141 | biostudies-literature | 2018 Mar
REPOSITORIES: biostudies-literature
Han Zhen Z Wu Hong H Kim Sunjoo S Yang Xiangkun X Li Qianjin Q Huang He H Cai Houjian H Bartlett Michael G MG Dong Aiping A Zeng Hong H Brown Peter J PJ Yang Xiang-Jiao XJ Arrowsmith Cheryl H CH Zhao Yingming Y Zheng Y George YG
The Journal of biological chemistry 20180110 9
Short-chain acylation of lysine residues has recently emerged as a group of reversible posttranslational modifications in mammalian cells. The diversity of acylation further broadens the landscape and complexity of the proteome. Identification of regulatory enzymes and effector proteins for lysine acylation is critical to understand functions of these novel modifications at the molecular level. Here, we report that the MYST family of lysine acetyltransferases (KATs) possesses strong propionyltra ...[more]