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Literature summary for 2.1.1.369 extracted from

  • Zhao, X.; Wang, Y.; Wang, Y.; Liu, Y.; Gao, S.
    Histone methyltransferase TXR1 is required for both H3 and H3.3 lysine 27 methylation in the well-known ciliated protist Tetrahymena thermophila (2017), Sci. China Life Sci., 60, 264-270 .
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Tetrahymena thermophila
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information K27Q mutation in variant H3.3 further aggravates the replication stress phenotype of K27Q mutation in canonical H3. H3.3 is a physiologically relevant substrate of TXR1 Tetrahymena thermophila ?
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S-adenosyl-L-methionine + [histone H3.3]-L-lysine27
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Tetrahymena thermophila S-adenosyl-L-homocysteine + [histone H3.3]-N6-methyl-L-lysine27
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?
S-adenosyl-L-methionine + [histone H3]-L-lysine27
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Tetrahymena thermophila S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine27
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?

Synonyms

Synonyms Comment Organism
Tetrahymena Trithorax related protein 1
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Tetrahymena thermophila
TXR1
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Tetrahymena thermophila