Cloned (Comment) | Organism |
---|---|
gene KAT2A, recombinant expression in HeLa cells, overexpressed Flag-KAT2A does not associate with SQSTM1 | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
autophagosome | - |
Homo sapiens | 5776 | - |
mitochondrion | - |
Saccharomyces cerevisiae | 5739 | - |
mitoplast | the Gcn5 protein is present inside mitoplasts | Saccharomyces cerevisiae | - |
- |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + [alpha-tubulin]-L-lysine | Saccharomyces cerevisiae | - |
CoA + [alpha-tubulin]-N6-acetyl-L-lysine | - |
? | |
acetyl-CoA + [alpha-tubulin]-L-lysine | Saccharomyces cerevisiae D273-10B/A1 | - |
CoA + [alpha-tubulin]-N6-acetyl-L-lysine | - |
? | |
acetyl-CoA + [alpha-tubulin]-L-lysine | Saccharomyces cerevisiae W303-1A | - |
CoA + [alpha-tubulin]-N6-acetyl-L-lysine | - |
? | |
acetyl-CoA + [alpha-tubulin]-L-lysine40 | Homo sapiens | - |
CoA + [alpha-tubulin]-N6-acetyl-L-lysine40 | - |
? | |
acetyl-CoA + [protein]-L-lysine | Saccharomyces cerevisiae | - |
CoA + [protein]-N6-acetyl-L-lysine | - |
? | |
acetyl-CoA + [protein]-L-lysine | Homo sapiens | - |
CoA + [protein]-N6-acetyl-L-lysine | - |
? | |
acetyl-CoA + [protein]-L-lysine | Saccharomyces cerevisiae D273-10B/A1 | - |
CoA + [protein]-N6-acetyl-L-lysine | - |
? | |
acetyl-CoA + [protein]-L-lysine | Saccharomyces cerevisiae W303-1A | - |
CoA + [protein]-N6-acetyl-L-lysine | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q92830 | - |
- |
Saccharomyces cerevisiae | - |
- |
- |
Saccharomyces cerevisiae D273-10B/A1 | - |
- |
- |
Saccharomyces cerevisiae W303-1A | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
additional information | the histone acetyltransferase KAT2A/GCN5 binds directly to the autophagosome protein MAP1LC3/LC3 (microtubule associated protein 1 light chain) via a conserved LC3-interacting region (LIR) domain. This interaction is required for KAT2A sequestration in autophagosomes and degradation by lysosomal acid hydrolases. Suppression of autophagy results in KAT2A accumulation. The LIR domain of KAT2A is required for KAT2A degradation | Homo sapiens |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
aortic smooth muscle cell | - |
Homo sapiens | - |
HeLa cell | - |
Homo sapiens | - |
smooth muscle cell | - |
Saccharomyces cerevisiae | - |
smooth muscle cell | - |
Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + [alpha-tubulin]-L-lysine | - |
Saccharomyces cerevisiae | CoA + [alpha-tubulin]-N6-acetyl-L-lysine | - |
? | |
acetyl-CoA + [alpha-tubulin]-L-lysine | - |
Saccharomyces cerevisiae D273-10B/A1 | CoA + [alpha-tubulin]-N6-acetyl-L-lysine | - |
? | |
acetyl-CoA + [alpha-tubulin]-L-lysine | - |
Saccharomyces cerevisiae W303-1A | CoA + [alpha-tubulin]-N6-acetyl-L-lysine | - |
? | |
acetyl-CoA + [alpha-tubulin]-L-lysine40 | - |
Homo sapiens | CoA + [alpha-tubulin]-N6-acetyl-L-lysine40 | - |
? | |
acetyl-CoA + [alpha-tubulin]-L-lysine40 | KAT2A acetylates Lys40 of TUBA | Homo sapiens | CoA + [alpha-tubulin]-N6-acetyl-L-lysine40 | - |
? | |
acetyl-CoA + [protein]-L-lysine | - |
Saccharomyces cerevisiae | CoA + [protein]-N6-acetyl-L-lysine | - |
? | |
acetyl-CoA + [protein]-L-lysine | - |
Homo sapiens | CoA + [protein]-N6-acetyl-L-lysine | - |
? | |
acetyl-CoA + [protein]-L-lysine | - |
Saccharomyces cerevisiae D273-10B/A1 | CoA + [protein]-N6-acetyl-L-lysine | - |
? | |
acetyl-CoA + [protein]-L-lysine | - |
Saccharomyces cerevisiae W303-1A | CoA + [protein]-N6-acetyl-L-lysine | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Gcn5 | - |
Saccharomyces cerevisiae |
Gcn5 | - |
Homo sapiens |
histone acetyltransferase | - |
Homo sapiens |
KAT2 | - |
Saccharomyces cerevisiae |
Kat2A | - |
Homo sapiens |
KAT2A/GCN5 | - |
Homo sapiens |
lysine acetyltransferase 2 | - |
Homo sapiens |
lysine-acetyltransferase | - |
Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
acetyl-CoA | - |
Saccharomyces cerevisiae | |
acetyl-CoA | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
malfunction | GCN5 deletion differently affects the growth of two strains, i.e. W303-1A and D273-10B/A1. The defective mitochondrial phenotype is related to a marked decrease in mtDNA content, which also involves the deletion of specific regions of the molecule. W303-1A cells deleted of the GCN5 gene show a thermosensitive phenotype. The ratio of mtDNA to nuclear DNA is strongly decreased (50 times) in the W303-1A mutant cells compared to wild-type cells. This defect is not observed in the D273-10B/1A cells. The different level of mtDNA in the two gcn5DELTA strains is consistent with their different phenotypes and with the higher respiratory competence of W303-1A compared to D273-10B/A1 cells. Deletion of GCN5 differently affects fermentative and respirative growth. The dynamics of mtDNA depletion during cell duplication indicates the loss of specific regions | Saccharomyces cerevisiae |
metabolism | in HeLa cells, ectopically overexpressed recombinant MYC-LC3 associates with endogenous KAT2A, but overexpressed Flag-KAT2A does not associate with SQSTM1. Gene silencing of SQSTM1 does not disrupt the association between KAT2A and LC3 in HeLa cells, suggesting that KAT2A physically interacts with LC3, and SQSTM1 is not involved in the interaction between KAT2A and LC3 | Homo sapiens |
physiological function | in Saccharomyces cerevisiae the lysine-acetyltransferase Gcn5 (KAT2) is part of the SAGA complex and is responsible for histone acetylation widely or at specific lysines. In wild-type mitochondria the Gcn5 protein is present in the mitoplasts, suggesting a distinct mitochondrial function for Gcn5 independent from the SAGA complex and possibly another function for this protein connecting epigenetics and metabolism, role of Gcn5 as a factor involved in respiratory metabolism, overview | Saccharomyces cerevisiae |
physiological function | the histone acetyltransferase KAT2A/GCN5 (lysine acetyltransferase 2) acetylates TUBA in vascular smooth muscle cells leading to microtubule instability and promotion of VSMC migration. Deacetylation of TUBA and perturbation of microtubule stability via selective autophagic degradation of KAT2A are essential for autophagy-promoting VSMC migration | Homo sapiens |