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Literature summary extracted from

  • Joshi, P.; Carrington, E.A.; Wang, L.; Ketel, C.S.; Miller, E.L.; Jones, R.S.; Simon, J.A.
    Dominant alleles identify SET domain residues required for histone methyltransferase of Polycomb repressive complex 2 (2008), J. Biol. Chem., 283, 27757-27766.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.356 F679Y the mutant is tolerated with about 2fold reduction compared with wild type Drosophila melanogaster
2.1.1.356 F679Y the mutant retains the capacity to produce trimethylated histone H3(K27) Drosophila melanogaster
2.1.1.356 F681Y the mutation dramatically reduces PRC2 HMTase Drosophila melanogaster
2.1.1.356 additional information each SET domain mutation disrupts PRC2 histone methyltransferase, based on known SET domain structures, the mutations likely affect either the lysine-substrate binding pocket, the binding site for the adenosylmethionine methyl donor, or a critical tyrosine predicted to interact with the substrate lysine epsilon-amino group. The CXC mutant retains catalytic activity, Lys-27 specificity, and trimethylation capacity. Drosophila melanogaster

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.356 Drosophila melanogaster
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-
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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) di- and trimethylation at histone H3(K27) Drosophila melanogaster ?
-
?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.356 histone lysine methyltransferase
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Drosophila melanogaster
2.1.1.356 HMTase
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Drosophila melanogaster
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