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JMJD5 catalyzes stereoselective C-3 hydroxylation of arginine residues in sequences from human RCCD1 and ribosomal protein S6.
Here, we report that JMJD5, a Jumonji C (JmjC) domain-containing protein, is a Cathepsin L-type protease that mediates histone H3 N-tail proteolytic cleavage under stress conditions that cause a DNA damage response.
The protease activities of JMJD5 and JMJD7 represent a mechanism for removal of histone tails bearing methylated arginine residues and define a potential mechanism of transcription regulation.
JMJD5 depletion increases the susceptibility of cancer cells to microtubule-destabilizing agents.
JMJD5 is a tumor suppressor gene in HCC pathogenesis, and the epigenetic silencing of JMJD5 promotes HCC cell proliferation by directly down-regulating CDKN1A transcription.
Data suggest that JMJD5 partially accumulates on mitotic spindles during mitosis; depletion of JMJD5 results in significant mitotic arrest, spindle assembly defects, and sustained activation of spindle assembly checkpoint.
These results suggest that direct interaction of JMJD5 with HBx facilitates hepatitis B virus replication through the hydroxylase activity of JMJD5.
Suggest JMJD5 as a potential oncogene in colon carcinogenesis.
results reveal that JMJD5 is a novel binding partner of p53 and it functions as a positive modulator of cell cycle and cell proliferation mainly through the repression of p53 pathway.
we provide genetic and biochemical evidence that the JMJD5/CDKN1A (p21) axis is essential to maintaining the short G1 phase which is critical for pluripotency in human embryonic stem cells
RCCD1 and KDM8 form a histone demethylase complex.
These results reveal that the N-terminal domain is essential for the nuclear localization of JMJD5 and its normal enzymatic function towards substrates in the nucleus
Comparison of the structure of JMJD5 with that of FIH, a well characterized protein hydroxylase, reveals that human JMJD5 might function as a protein hydroxylase.
JMJD5 has a role in regulating PKM2 nuclear translocation and reprogramming HIF-1alpha-mediated glucose metabolism
The study reports high-resolution crystal structures of the human JMJD5 catalytic domain in complex with the substrate 2-oxoglutarate (2-OG) and the inhibitor N-oxalylglycine (NOG).
JMJD5 is a post-translational co-repressor for NFATc1 that attenuates osteoclastogenesis.
Data show that both Arabidopsis jmjd5 mutant seedlings and mammalian cell cultures deficient for the human ortholog of this gene have similar fast-running circadian oscillations compared with WT.
show that JMJD5 (now renamed KDM8), demethylates H3K36me2 and is required for cell cycle progression.
Identifies five novel candidate tumor suppressor genes in mouse, including Pou2f2, Hivep3, Jmjd5, Fbxl10 and a protein similar to human N4BP3.
Jmjd5 is involved in the transcriptional regulation of a subset of p53-regulated genes, possibly through the control of p53 recruitment at the gene loci.
Data suggest that Jmjd5 partially accumulates on mitotic spindles during mitosis; depletion of Jmjd5 results in significant mitotic arrest, spindle assembly defects, and sustained activation of spindle assembly checkpoint.
Collectively, these data indicate that JMJD5 is essential during embryonal development and a repressor of p53 expression. The latter suggests that JMJD5 has oncogenic activity and accordingly JMJD5 is upregulated in leukemias and breast cancer.
Results suggest that Jmjd5 physiologically moderates embryonic cell proliferation through the epigenetic control of Cdkn1a expression.
This gene likely encodes a histone lysine demethylase. Studies of a similar protein in mouse indicate a potential role for this protein as a tumor suppressor. Alternatively spliced transcript variants have been described.
jumonji domain containing 5
, JmjC domain-containing protein 5
, Jumonji domain-containing protein 5
, lysine-specific demethylase 8
, jmjC domain-containing protein 5
, jumonji domain-containing protein 5