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 | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
HEK-293T cell | - |
Homo sapiens | - |
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 | Comment | Organism |
---|---|---|
Gcn5 | - |
Homo sapiens |
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 |