Ontology highlight
ABSTRACT:
SUBMITTER: Wang F
PROVIDER: S-EPMC3965384 | biostudies-literature | 2014 Mar
REPOSITORIES: biostudies-literature
Wang Feng F He Lin L Huangyang Peiwei P Liang Jing J Si Wenzhe W Yan Ruorong R Han Xiao X Liu Shumeng S Gui Bin B Li Wanjin W Miao Di D Jing Chao C Liu Zhihua Z Pei Fei F Sun Luyang L Shang Yongfeng Y
PLoS biology 20140325 3
Jumonji domain-containing 6 (JMJD6) is a member of the Jumonji C domain-containing family of proteins. Compared to other members of the family, the cellular activity of JMJD6 is still not clearly defined and its biological function is still largely unexplored. Here we report that JMJD6 is physically associated with the tumor suppressor p53. We demonstrated that JMJD6 acts as an α-ketoglutarate- and Fe(II)-dependent lysyl hydroxylase to catalyze p53 hydroxylation. We found that p53 indeed exists ...[more]