KMT5A

The protein encoded by this gene is a protein-lysine N-methyltransferase that can monomethylate Lys-20 of histone H4 to effect transcriptional repression of some genes. The encoded protein is required for cell proliferation and plays a role in chromatin condensation.

Lysine Methyltransferase 5A

Protein-lysine N-methyltransferase that monomethylates both histones and non-histone proteins. Specifically monomethylates 'Lys-20' of histone H4 (H4K20me1). H4K20me1 is enriched during mitosis and represents a specific tag for epigenetic transcriptional repression. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. Required for cell proliferation, probably by contributing to the maintenance of proper higher-order structure of DNA during mitosis. Involved in chromosome condensation and proper cytokinesis. Nucleosomes are preferred as substrate compared to free histones. Mediates monomethylation of p53/TP53 at 'Lys-382', leading to repress p53/TP53-target genes. Plays a negative role in TGF-beta response regulation and a positive role in cell migration.

Cell divisionIEA:UniProtKB-KW
Chromatin organizationIEA:UniProtKB-KW
Mitotic chromosome condensationTAS:Reactome
Negative regulation of transcription by RNA polymerase IIManual Assertion Based On ExperimentIMP:UniProtKB
Negative regulation of transcription, DNA-templatedManual Assertion Based On ExperimentIDA:UniProtKB
Peptidyl-lysine monomethylationManual Assertion Based On ExperimentIDA:UniProtKB
Regulation of DNA damage response, signal transduction by p53 class mediatorManual Assertion Based On ExperimentIMP:UniProtKB
Regulation of signal transduction by p53 class mediatorTAS:Reactome

Nucleus
Chromosome
Specifically localizes to mitotic chromosomes. Colocalized with SIRT2 at mitotic foci. Associates with chromosomes during mitosis; association is increased in a H(2)O(2)-induced oxidative stress-dependent manner. Associates with silent chromatin on euchromatic arms. Not associated with constitutive heterochromatin.

Acetylated at Lys-172; does not change methyltransferase activity. Deacetylated at Lys-172 by SIRT2; does not change methyltransferase activity.
Ubiquitinated and degraded by the DCX(DTL) complex.