EC Number   |
General Information |
Reference |
|---|
   2.3.1.255 | malfunction |
Aenzyme knockdown significantly reduces dendritic extension in cultured Purkinje cells |
703852 |
| 2.3.1.255 | physiological function |
ARD1 is essential for viability in mammalian and insect-stage Trypanosoma brucei cells |
-, 740977 |
| 2.3.1.255 | metabolism |
ARD1 variants have different effects on hypoxia-inducible factor-1alpha stability and acetylation |
739977 |
| 2.3.1.255 | physiological function |
arrest defective 1 (ARD1), also known as N(alpha)-acetyltransferase 10 (NAA10) is originally identified as an N-terminal acetyltransferase (NAT) that catalyzes the acetylation of N-termini of newly synthesized peptides. Mammalian ARD1/NAA10 also plays a role as lysine acetyltransferase (KAT) that posttranslationally acetylates internal lysine residues of proteins. ARD1/NAA10 is the only enzyme with both NAT (EC 2.3.1.255) and KAT (EC 2.3.1.48) activities. NATs acetylate N-terminal residues of newly synthesized proteins from ribosomes in an irreversible manner. N-terminal acetylation is known to be closely related to protein stability, interaction, and localization. lysine acetylation catalyzed by KATs is reversibly regulated by lysine deacetyltransferases (KDACs) that remove acetyl groups from lysine residues in proteins. While acetylation neutralizes the positive charge on lysine residues, deacetylation recovers it, thereby causing a change in electronic and conformational properties of proteins. Acetylation and deacetylation of lysine residues serve as the switches that turn-on and turn-off the cellular signal pathways and regulate diverse biological events. Any unbalance between lysine acetylation and deacetylation results in the improper regulation of biological processes and may cause various types of human diseases such as cancer and neurodegeneration |
757723 |
| 2.3.1.255 | physiological function |
enzyme Daf-31 regulates the transcriptional activity of DAF-16, the FOXO transcription factor. Mutant daf-31(m655) leads to developmental larval arrest, fat accumulation, formation of dauer-like larvae under starvation conditions, and decreased lifespan, and the mutant lacks SDS-resistance and cannot resume development and reproduction after food re-providing |
-, 756675 |
| 2.3.1.255 | malfunction |
enzyme knockdown causes a phenotype with lethality, growth retardation, bent axis and tails, abnormal eyes, and less pigmentation |
756675 |
| 2.3.1.255 | malfunction |
enzyme mutants show phenotypes with pleiotropic oogenesis, aberrant mitosis, egg chamber encapsulation defects, and nurse cell chromatin dispersion defects |
756675 |
| 2.3.1.255 | physiological function |
enzyme variant ARD1131 has no influence on cyclin D1 expression and cell growth |
736273 |
| 2.3.1.255 | physiological function |
hNatA significantly enhances the catalytic efficiency of hNatE (EC 2.3.1.258). The hNatE complex comprises subunits Naa10 and Naa15 (NatA) and Naa50. HYPK binding to hNatE largely nullifies this effect |
757754 |
| 2.3.1.255 | malfunction |
HYPK is a negative regulator for hNatA acetylation activity |
757754 |
