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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.366
-
 Mus musculus

Protein Variants

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

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.366 Mus musculus O88974
-
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

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

General Information

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