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Literature summary for 2.1.1.367 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
Search for more literature for 2.1.1.367

Localization

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + a [histone H3]-L-lysine9 Mus musculus
-
 S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine9
-
 ?
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

Organism UniProt Comment Textmining
Mus musculus A2A935
-
-
Mus musculus A2A935 isoform Prdm16
-
Mus musculus P14404
-
-
Mus musculus P14404 isoform Prdm3
-

Purification (Commentary)

Purification (Comment) Organism
-
 Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
fibroblast embryonic fibroblast Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + a [histone H3]-L-lysine9
-
 Mus musculus S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine9
-
 ?
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
-
 ?
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

Synonyms Comment Organism
Mecom
-
 Mus musculus
PRDM16
-
 Mus musculus
PRDM3
-
 Mus musculus

General Information

General Information Comment Organism
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
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