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Literature summary for 3.5.1.98 extracted from

  • Luo, Y.; Jian, W.; Stavreva, D.; Fu, X.; Hager, G.; Bungert, J.; Huang, S.; Qiu, Y.
    Trans-regulation of histone deacetylase activities through acetylation (2009), J. Biol. Chem., 284, 34901-34910.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
K432R the HDAC1 mutant only partially loses acetylation modification Homo sapiens
R433K the HDAC2 mutant is only acetylated at low levels Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
acetylated histone deacetylase 1 the activity of HDAC2 is inhibited by acetylated HDAC1 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
acetylation HDAC, but not HDAC2 is acetylated by p300 Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-acetyl-lysine-histone H3 + H2O
-
Homo sapiens acetate + histone H3
-
?
N-acetyl-lysine-histone H4 + H2O
-
Homo sapiens acetate + histone H4
-
?

Synonyms

Synonyms Comment Organism
HDAC1
-
Homo sapiens
HDAC2
-
Homo sapiens

General Information

General Information Comment Organism
physiological function HDAC2 and HDAC1 are required for glucocorticoid receptor-mediated gene activation. HDAC2, however, is regulated through a different mechanism from that of HDAC1. Acetylated HDAC1 can trans-regulate HDAC2 through heterodimerization. Both HDAC1 and HDAC2 are required for mouse mammary tumor virus transcription Homo sapiens