Extended PHD finger (ePHD) found in Jumonji domain-containing protein 2A (JMJD2A)
The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. This model includes the ePHD finger of JMJD2A. JMJD2A, also termed lysine-specific demethylase 4A (KDM4A), or JmjC domain-containing histone demethylation protein 3A (JHDM3A), catalyzes the demethylation of di- and trimethylated H3K9 and H3K36. It is involved in carcinogenesis and functions as a transcription regulator that may either stimulate or repress gene transcription. It associates with nuclear receptor co-repressor complex or histone deacetylases. Moreover, JMJD2A forms complexes with both the androgen and estrogen receptor (ER) and plays an essential role in growth of both ER-positive and -negative breast tumors. It is also involved in prostate, colon, and lung cancer progression. JMJD2A contains jmjN and jmjC domains in the N-terminal region, followed by a canonical PHD finger, this non-canonical ePHD finger, and a Tudor domain.
Conserved feature residue pattern:C C H C C C C C H C C H
Evidence:
Comment:based on the structure evidence that human Borjeson-Forssman-Lehmann syndrome-associated protein PHF6 (PDB 4NN2) binds three Zn2+ ions through its ePHD finger
Comment:The extended PHD finger is characterized by Cys2HisCys5HisCys2His.
Jiyao W et al.(2023). "The conserved domain database in 2023.",