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Literature summary for 2.3.1.48 extracted from

  • Li, Y.; Jaramillo-Lambert, A.N.; Yang, Y.; Williams, R.; Lee, N.H.; Zhu, W.
    And-1 is required for the stability of histone acetyltransferase Gcn5 (2012), Oncogene, 31, 643-652.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
medicine high mobility group domain-containing protein And-1 forms a complex with both histone H3 and isoform Gcn5. And-1 expression is increased in cancer cells in a manner correlating with increase in Gcn5 and acetylation of H3K9 and H3K56 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
-

Source Tissue

Source Tissue Comment Organism Textmining
HEK-293T cell
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Homo sapiens
-

Subunits

Subunits Comment Organism
More high mobility group domain-containing protein And-1 forms a complex with both histone H3 and isoform Gcn5. Downregulation of And-1 results in Gcn5 degradation, leading to the reduction of histone H3K9 and H3K56 acetylation. And-1 overexpression stabilizes Gcn5 through protein-protein interactions in vivo Homo sapiens

Synonyms

Synonyms Comment Organism
Gcn5
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Homo sapiens

General Information

General Information Comment Organism
metabolism high mobility group domain-containing protein And-1 overexpression stabilizes Gcn5 through protein-protein interactions in vivo Homo sapiens
physiological function high mobility group domain-containing protein And-1 forms a complex with both histone H3 and isoform Gcn5. Downregulation of And-1 results in Gcn5 degradation, leading to the reduction of histone H3K9 and H3K56 acetylation. And-1 overexpression stabilizes Gcn5 through protein-protein interactions in vivo. And-1 expression is increased in cancer cells in a manner correlating with increase in Gcn5 and acetylation of H3K9 and H3K56 Homo sapiens