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Validated All-in-One™ qPCR Primer for KDM4A(NM_014663.2) Search again
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Summary
This gene is a member of the Jumonji domain 2 (JMJD2) family and encodes a protein with a JmjN domain, a JmjC domain, a JD2H domain, two TUDOR domains, and two PHD-type zinc fingers. This nuclear protein functions as a trimethylation-specific demethylase, converting specific trimethylated histone residues to the dimethylated form, and as a transcriptional repressor. [provided by RefSeq].
Gene References into function
- The ability of JMJD2A to associate with retinoblastoma proteins and histone deacetylase 1 implies an important role for this protein in cell proliferation and oncogenesis.
- JMJD2A selectively represses the expression of the achaete scute-like homologue 2 (ASCL2) gene but not other imprinted genes in the same imprinted locus in HeLa cells
- crystal structure of the double tudor domain of JMJD2A both in the presence and absence of a trimethylated H3-K4 peptide
- JHDM3A may function in euchromatin to remove histone methylation marks that are associated with active transcription
- identified two related histone demethylases, JMJD2A and JMJD2D
- how human JMJD2A, which is selective towards tri- and dimethylated histone H3 lysyl residues 9 and 36 (H3K9me3/me2 and H3K36me3/me2), discriminates between methylation states and achieves sequence selectivity for H3K9
- Crystal structures of the JMJD2A catalytic domain in complex with H3K9me3, H3K36me2 and H3K36me3 peptides are presented.
- Human JMJD2A was expressed in undifferentiated and differentiated ES cells.
- JMJD2A has the unique property of binding trimethylated peptides from two different histone sequences.
