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Literature summary for 2.1.1.366 extracted from

  • Yang, L.; Xia, L.; Wu, D.Y.; Wang, H.; Chansky, H.A.; Schubach, W.H.; Hickstein, D.D.; Zhang, Y.
    Molecular cloning of ESET, a novel histone H3-specific methyltransferase that interacts with ERG transcription factor (2002), Oncogene, 21, 148-152 .
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
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 Mus musculus

Protein Variants

Protein Variants Comment Organism
C1242T highly conserved cysteine residues, mutant has lost histone methyltransferase activity Mus musculus
C798L highly conserved cysteine residues, mutant has lost histone methyltransferase activity Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus O88974
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information ESET can specifically methylate histone H3 while inactive toward histone H2A, H2B and H4 Mus musculus ?
-
-

Subunits

Subunits Comment Organism
? x * 145000, calculated from sequence, x * 180000, SDS-PAGE of recombinant protein Mus musculus

Synonyms

Synonyms Comment Organism
ERG-associated protein with SET domain
-
 Mus musculus
ESET
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 Mus musculus
SETDB1
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 Mus musculus

General Information

General Information Comment Organism
physiological function ESET interacts with transcription factor EST Mus musculus