L3MBTL1

L3MBTL1 histone methyl-lysine binding protein is a polycomb group (PcG) protein that specifically recognizes and binds mono- and dimethyllysine residues on target proteins, therey acting as a 'reader' of a network of post-translational modifications. PcG proteins maintain the transcriptionally repressive state of genes: acts as a chromatin compaction factor by recognizing and binding mono- and dimethylated histone H1b/HIST1H1E at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condense chromatin and repress transcription. It recognizes and binds p53/TP53 monomethylated at 'Lys-382', leading to repress p53/TP53-target genes. It also recognizes and binds RB1/RB monomethylated at 'Lys-860'. It participates in the ETV6-mediated repression. It probably plays a role in cell proliferation. Overexpression of this protein induces multinucleated cells, suggesting that it is required to accomplish normal mitosis (By similarity).

Full Name

L3Mbtl1 Histone Methyl-Lysine Binding Protein

Function

Polycomb group (PcG) protein that specifically recognizes and binds mono- and dimethyllysine residues on target proteins, therey acting as a 'reader' of a network of post-translational modifications. PcG proteins maintain the transcriptionally repressive state of genes: acts as a chromatin compaction factor by recognizing and binding mono- and dimethylated histone H1b/H1-4 at 'Lys-26' (AC H1bK26me1 and AC H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condense chromatin and repress transcription. Recognizes and binds p53/TP53 monomethylated at 'Lys-382', leading to repress p53/TP53-target genes. Also recognizes and binds RB1/RB monomethylated at 'Lys-860'. Participates in the ETV6-mediated repression. Probably plays a role in cell proliferation. Overexpression induces multinucleated cells, suggesting that it is required to accomplish normal mitosis.

Biological Process

Chromatin organizationManual Assertion Based On ExperimentIDA:UniProtKB
HemopoiesisManual Assertion Based On ExperimentIEP:UniProtKB
Heterochromatin assemblyManual Assertion Based On ExperimentIDA:ComplexPortal
Negative regulation of transcription, DNA-templatedManual Assertion Based On ExperimentIDA:UniProtKB
Regulation of cell cycle1 PublicationNAS:UniProtKB
Regulation of megakaryocyte differentiationManual Assertion Based On ExperimentIDA:UniProtKB
Regulation of mitotic nuclear divisionManual Assertion Based On ExperimentIMP:UniProtKB

Cellular Location

Nucleus
Excluded from the nucleolus. Does not colocalizes with the PcG protein BMI1, suggesting that these two proteins do not belong to the same complex.

PTM

Ubiquitinated in a VCP/p97-dependent way following DNA damage, leading to its removal from DNA damage sites, promoting accessibility of H4K20me2 mark for DNA repair protein TP53BP1, which is then recruited to DNA damage sites.