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Literature summary extracted from

  • Stepanik, V.A.; Harte, P.J.
    A mutation in the E(Z) methyltransferase that increases trimethylation of histone H3 lysine 27 and causes inappropriate silencing of active Polycomb target genes (2012), Dev. Biol., 364, 249-258.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.356 additional information the E(z)Trm mutation increases the histone H3 (K27) trimethylation efficiency of catalytic subunit E(Z) of Polycomb Repressive Complex 2 Drosophila melanogaster

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.356 Drosophila melanogaster
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-
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Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.1.1.356 embryo
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Drosophila melanogaster
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.356 S-adenosyl-L-methionine + histone H3(K27) Drosophila Polycomb Repressive Complex 2 is a lysine methyltransferase that trimethylates histone H3 (K27) Drosophila melanogaster ?
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?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.356 Polycomb repressive complex 2
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Drosophila melanogaster
2.1.1.356 PRC2
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Drosophila melanogaster

General Information

EC Number General Information Comment Organism
2.1.1.356 malfunction mutations in the catalytic subunit E(Z) that abolish methyltransferase activity disrupt Polycomb silencing, causing derepression of Polycomb target genes in cells where they are normally silenced. Increased histone H3(K27) trimethylation activity of mutant E(Z)Trm causes the premature accumulation of trimethylated histone H3(K27) in early embryogenesis, predestining initially active Polycomb target genes to silencing once Polycomb silencing is initiated Drosophila melanogaster