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Literature summary for 2.1.1.356 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
Search for more literature for 2.1.1.356

Protein Variants

Protein Variants Comment Organism
F679Y the mutant is tolerated with about 2fold reduction compared with wild type Drosophila melanogaster
F679Y the mutant retains the capacity to produce trimethylated histone H3(K27) Drosophila melanogaster
F681Y the mutation dramatically reduces PRC2 HMTase Drosophila melanogaster
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

Organism UniProt Comment Textmining
Drosophila melanogaster
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + histone H3(K27) di- and trimethylation at histone H3(K27) Drosophila melanogaster ?
-
 ?

Synonyms

Synonyms Comment Organism
histone lysine methyltransferase
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 Drosophila melanogaster
HMTase
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 Drosophila melanogaster
Polycomb repressive complex 2
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 Drosophila melanogaster
PRC2
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 Drosophila melanogaster