Gene Ontology annotation based on Enzyme Commission mapping
Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
TreeGrafter-generated GO annotations
Combined Automated Annotation using Multiple IEA Methods
Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases.
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JMJD2 family members, including JMJD2C, are trimethyl-specific H3K9 demethylases.
"subfamily members also functioned as trimethylation-specific demethylases"
Cooperative demethylation by JMJD2C and LSD1 promotes androgen receptor-dependent gene expression.
Structural and evolutionary basis for the dual substrate selectivity of human KDM4 histone demethylase family.
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KDM4A-C form a vertebrate-conserved subclass that demethylates both H3K9 and H3K36, preferring H3K9me3; the KDM4C catalytic-domain structure coordinates the metal through the conserved HX(E/D)...H motif.
"KDM4A–C, which are highly conserved in all vertebrates, and demethylate both H3K9 and H3K36"
Potent and Selective KDM5 Inhibitor Stops Cellular Demethylation of H3K4me3 at Transcription Start Sites and Proliferation of MM1S Myeloma Cells.
UniProt record for donkey KDM4C (A0A9L0K3L6)
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The donkey protein is assigned to the JHDM3 histone demethylase family.
"Belongs to the JHDM3 histone demethylase family."
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The donkey protein is classified in the KDM4C PANTHER subfamily.
"PTHR10694:SF104; LYSINE-SPECIFIC DEMETHYLASE 4C"
UniProt record for human KDM4C (Q9H3R0)
KDM4C: donkey-human sequence comparison
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Donkey KDM4C conserves all JmjC cofactor- and substrate-binding residues.
"All human 2-oxoglutarate-binding residues (Y134, N200, K208, K243), catalytic Fe-binding residues (H190, E192, H278) and Zn-binding residues (C236, H242, C308, C310) of the JmjC domain are conserved"