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Updated: Dec 1, 2025

Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark
Published on: January 26, 2018
The methyltransferase SETD3-mediated histidine methylation: Biological functions and potential implications in
1Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Cancer Center of Renmin Hospital of Wuhan University, Wuhan University, Wuhan 430072, China.
Abstract:
SETD3 belongs to a family of SET-domain containing proteins. Recently, SETD3 was found as the first and so-far the only known metazoan histidine methyltransferase that catalyzes actin histidine 73 (His73) methylation, a pervasive modification which was discovered more than 50 years ago. In this review, we summarize some recent advances in SETD3 research, focusing on structural properties, substrate-recognition features, and physiological functions. We particularly highlight potential pathological relevance of SETD3 in human cancers and raise some questions to promote discussion about this novel histidine methyltransferase.
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