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Literature summary extracted from

  • Pinheiro, I.; Margueron, R.; Shukeir, N.; Eisold, M.; Fritzsch, C.; Richter, F.M.; Mittler, G.; Genoud, C.; Goyama, S.; Kurokawa, M.; Son, J.; Reinberg, D.; Lachner, M.; Jenuwein, T.
    Prdm3 and Prdm16 are H3K9me1 methyltransferases required for mammalian heterochromatin integrity (2012), Cell, 150, 948-960 .
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.1.1.367 cytoplasm
-
 Mus musculus 5737
-
2.1.1.367 nucleus
-
 Mus musculus 5634
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.355 S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine9 Mus musculus
-
 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
-
 ?
2.1.1.355 S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine9 Mus musculus
-
 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine9
-
 ?
2.1.1.367 S-adenosyl-L-methionine + a [histone H3]-L-lysine9 Mus musculus
-
 S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine9
-
 ?
2.1.1.367 S-adenosyl-L-methionine + histone H3 peptide Mus musculus amino acids 6-11 of histone H3 S-adenosyl-L-homocysteine + [histone H3 peptide]-N6-methyl-L-lysine9
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.355 Mus musculus O54864
-
-
2.1.1.367 Mus musculus A2A935
-
-
2.1.1.367 Mus musculus A2A935 isoform Prdm16
-
2.1.1.367 Mus musculus P14404
-
-
2.1.1.367 Mus musculus P14404 isoform Prdm3
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.367
-
 Mus musculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.1.1.355 fibroblast embryonic fibrobast Mus musculus
-
2.1.1.367 fibroblast embryonic fibroblast Mus musculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.355 S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine9
-
 Mus musculus S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
-
 ?
2.1.1.355 S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine9
-
 Mus musculus S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine9
-
 ?
2.1.1.367 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
-
 Mus musculus S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine9
-
 ?
2.1.1.367 S-adenosyl-L-methionine + histone H3 peptide amino acids 6-11 of histone H3 Mus musculus S-adenosyl-L-homocysteine + [histone H3 peptide]-N6-methyl-L-lysine9
-
 ?
2.1.1.367 S-adenosyl-L-methionine + [histone H3 peptide 6-11]-L-lysine9
-
 Mus musculus S-adenosyl-L-homocysteine + a [histone H3 peptide 6-11]-N6-methyl-L-lysine9
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.355 SUV39H1
-
 Mus musculus
2.1.1.367 Mecom
-
 Mus musculus
2.1.1.367 PRDM16
-
 Mus musculus
2.1.1.367 PRDM3
-
 Mus musculus

General Information

EC Number General Information Comment Organism
2.1.1.355 physiological function Prdm3 and Prdm16 are redundant histone H3K9me1-specific methyltransferases that direct cytoplasmic H3K9me1 methylation. H3K9me1 is converted in the nucleus to H3K9me3 by the Suv39h enzyme to reinforce heterochromatin. Suv39h double null immortalized mouse embryonic fibroblasts are depleted for nuclear H3K9me3. Simultaneous depletion of Prdm3 and Prdm16 abrogates H3K9me1 methylation, prevents Suv39h-dependent H3K9me3 trimethylation, and derepresses major satellite transcription Mus musculus
2.1.1.367 physiological function Prdm3 and Prdm16 are redundant histone H3K9me1-specific methyltransferases that direct cytoplasmic H3K9me1 methylation. The H3K9me1 is converted in the nucleus to H3K9me3 by the Suv39h enzymes to reinforce heterochromatin. Simultaneous depletion of Prdm3 and Prdm16 abrogates H3K9me1 methylation, prevents Suv39h-dependent H3K9me3 trimethylation, and derepresses major satellite transcription. Combined impairment of Prdm3 and Prdm16 results in disintegration of heterochromatic foci and disruption of the nuclear lamina Mus musculus
2.1.1.367 physiological function simultaneous depletion of Prdm3 and Prdm16 abrogates H3K9me1 methylation, prevents Suv39h-dependent H3K9me3 trimethylation, and derepresses major satellite transcription. Combined impairment of Prdm3 and Prdm16 results in disintegration of heterochromatic foci and disruption of the nuclear lamina Mus musculus