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Literature summary extracted from

  • Iwamori, N.; Zhao, M.; Meistrich, M.L.; Matzuk, M.M.
    The testis-enriched histone demethylase, KDM4D, regulates methylation of histone H3 lysine 9 during spermatogenesis in the mouse but is dispensable for fertility (2011), Biol. Reprod., 84, 1225-1234 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.11.66 gene Kdm4d, expression analysis, recombinant expression in HeLa cells, di- and trimethylated H3K9 disappear from KDM4D-positive cells, whereas H3K9me1 were increased by KDM4D expression Mus musculus

Protein Variants

EC Number Protein Variants Comment Organism
1.14.11.66 additional information targeted disruption of KDM4D, a testis-enriched tridemethylase of H3K9. Kdm4d-null mice are viable and fertile and do not show any obvious phenotype, but H3K9me3 accumulates significantly in Kdm4d-null round spermatids, and the distribution of methylated H3K9 in germ cells is dramatically changed, overview. Lack of expression of Kdm4d in spermatogonia is consistent with lack of expression of Kdm4d in germline stem cells Mus musculus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.11.66 nucleus
-
 Mus musculus 5634
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.11.66 [histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2 Mus musculus
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 [histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
-
 ?
1.14.11.66 [histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2 Mus musculus
-
 [histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.11.66 Mus musculus Q3U2K5
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.11.66 spermatocyte
-
 Mus musculus
-
1.14.11.66 testis preferential expression of KDM4D (also known as JMJD2D), one of the tridemethylases of H3K9 in the testis Mus musculus
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.11.66 additional information KDM4D can demethylate H3K9me2 and H3K9me3 into H3K9me1 without significant effects on most of the other histone H3 methylation patterns Mus musculus ?
-
 ?
1.14.11.66 [histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
-
 Mus musculus [histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
-
 ?
1.14.11.66 [histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
-
 Mus musculus [histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.11.66 H3K9Me3 demethylase
-
 Mus musculus
1.14.11.66 JMJD2D
-
 Mus musculus
1.14.11.66 KDM4D
-
 Mus musculus
1.14.11.66 testis-enriched histone demethylase
-
 Mus musculus
1.14.11.66 tridemethylase of H3K9
-
 Mus musculus

General Information

EC Number General Information Comment Organism
1.14.11.66 malfunction Kdm4d-null mice are viable and fertile and do not show any obvious phenotype. But H3K9me3 accumulates significantly in Kdm4d-null round spermatids, and the distribution of methylated H3K9 in germ cells is dramatically changed. Nevertheless, the progression of spermatogenesis and the number of spermatozoa are normal, likely secondary to the earlier nuclear localization of another H3K9 tridemethylase, KDM4B, in Kdm4d-null elongating spermatids Mus musculus
1.14.11.66 physiological function the testis-enriched histone demethylase, KDM4D, regulates methylation of histone H3 lysine 9 during spermatogenesis in mouse but is dispensable for fertility. Among various methylations of histone H3, methylation of histone H3 lysine 9 (H3K9) by testis-enriched tridemethylase of H3K9 and its regulation are essential for spermatogenesis. Demethylation of H3K9me3 in round spermatids is dispensable for spermatogenesis, possible defects in Kdm4d-null elongating spermatids can be rescued by functional redundancy of the KDM4B demethylase. KDM4D can demethylate H3K9me2 and H3K9me3 into H3K9me1 without significant effects on most of the other histone H3 methylation patterns Mus musculus