EC Number |
Protein Variants |
Reference |
---|
1.14.11.27 | H188A |
inactive |
764639 |
1.14.11.27 | H211A |
inactive mutant |
700374 |
1.14.11.27 | H212A |
inactive mutant |
-, 726260 |
1.14.11.27 | H212A |
mutation completely abolishes the enzymatic activity |
662947 |
1.14.11.27 | H305A |
more than 90% loss of activity |
688966 |
1.14.11.27 | H305A |
mutation completely abolishes the enzymatic activity |
662947 |
1.14.11.27 | H319A |
a catalytically inactive mutant |
724815 |
1.14.11.27 | more |
enzyme engineering and swapping of the C-terminus region containing the distal Tudor domain between isozymes KDM4C and KDM4A. Chimera5, which encodes the first 934 amino acids of KDM4C fused with the last 129 amino acid containing the distal Tudor domain of KDM4A, is excluded from mitotic chromatin. On the other hand, chimera6 that encodes the first 954 amino acids of KDM4A fused to 101 amino acids of KDM4C, which includes its distal Tudor domain, remains excluded from chromatin. The C-terminus of KDM4C containing the distal Tudor domain is essential but not sufficient for its mitotic chromatin localization |
745919 |
1.14.11.27 | more |
enzyme engineering and swapping of the C-terminus region containing the distal Tudor domain between isozymes KDM4C and KDM4A. Chimera5, which encodes the first 934 amino acids of KDM4C fused with the last 129 amino acid containing the distal Tudor domain of KDM4A, is excluded from mitotic chromatin. On the other hand, chimera6 that encodes the first 954 amino acids of KDM4A fused to 101 amino acids of KDM4C, which includes its distal Tudor domain, remains excluded from chromatin. The C-terminus of KDM4C containing the distal Tudor domain is essential but not sufficient for its mitotic chromatin localization. EGFP-KDM4CRDTF/DNLY mutant is excluded from mitotic chromatin. For isozyme knockout, U2OS cells are transfected with KDM4B-C siRNA sequences |
745919 |
1.14.11.27 | more |
expression of histone demthylase Ndy1 in mouse embryo fibroblast results in immortalization in absence of replicative senescence via a JmjC domain-dependent process that targets the Rb and p53 pathways. Knockdown of endogenous Ndy1 or expression of JmjC domain mutants of Ndy1 promote senescence, suggesting that Ndy1 is a physiological inhibitor of senescence in dividing cells and that inhibition of senescence depends on histone H3 demethylation |
689797 |