Jumonji domain-containing protein: Difference between revisions
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== Function == | == Function == | ||
'''Jumonji domain-containing protein 2A''' (Jmjd2a) catalyzes the demethylation of trimethylated histone at lysine residues 9 and 36 producing the | '''Jumonji domain-containing protein 2A''' (Jmjd2a) catalyzes the demethylation of trimethylated histone at lysine residues 9 and 36 producing the demethylated form. Jmjd2a domains contain: N-terminal, catalytic core (residues 1-350), 2 TUDOR domains which recognize dimethylated Arg (residues 895-1011) , 2 PHD-type zinc fingers and C-terminal domain. Jmjd2a is Fe+2 and α-ketoglutarate dependent. Methylation of histones in the chromatin is involved in regulation of gene activity, chromatin structure and epigenetic memory. | ||
== Disease == | == Disease == |
Revision as of 11:36, 4 April 2016
FunctionJumonji domain-containing protein 2A (Jmjd2a) catalyzes the demethylation of trimethylated histone at lysine residues 9 and 36 producing the demethylated form. Jmjd2a domains contain: N-terminal, catalytic core (residues 1-350), 2 TUDOR domains which recognize dimethylated Arg (residues 895-1011) , 2 PHD-type zinc fingers and C-terminal domain. Jmjd2a is Fe+2 and α-ketoglutarate dependent. Methylation of histones in the chromatin is involved in regulation of gene activity, chromatin structure and epigenetic memory. DiseaseRelevanceStructural highlights |
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3D structures of jumonji domain-containing protein 2A3D structures of jumonji domain-containing protein 2A
Updated on 04-April-2016