EC Number   |
General Information |
Reference |
|---|
   2.3.1.256 | evolution |
enzyme Naa30 belongs to the GNAT superfamily of acetyltransferases characterized by the highly conserved GNAT fold, which promotes Ac-CoA binding and substrate recognition |
756860 |
| 2.3.1.256 | malfunction |
depletion of the human N-terminal acetyltransferase hNaa30 disrupts Golgi integrity and Golgi-associated GTPase ADP ribosylation factor related protein 1 (ARFRP1) localization. Depletion of the hNatC catalytic subunit hNaa30 leads to disassembly of the Golgi apparatus and trans-Golgi network (TGN). ARFRP1 shifts from a predominantly cis-Golgi and TGN localization to localizing both Golgi and non-Golgi vesicular structures in hNaa30-depleted cells (smaller vesicle-like membranous compartments). Loss of membrane association of ARFRP1 is not observed. hNaa30 depletion induces Golgi scattering and induces aberrant ARFRP1 Golgi localization. Knockdown of each of the hNatC subunits in HeLa cells leads to p53-dependent apoptosis. Naa30 depletion severely disrupts mitochondrial organization. Knockdown phenotypes are specific for hNaa30 depletion and not a result of si-hNAA30-independent effects. Phenotypes, detailed overview |
756225 |
| 2.3.1.256 | malfunction |
enzyme depletion results in severe cell growth defects and embryonic lethality |
673107 |
| 2.3.1.256 | malfunction |
knockdown of Naa30 induces the loss of mitochondrial membrane potential and fragmentation of mitochondria |
741001 |
| 2.3.1.256 | malfunction |
knockdown of Nalpha-terminal acetyltransferase complex C leads to p53-dependent apoptosis and aberrant Arf-like GTPase Arl8b localization |
740993 |
| 2.3.1.256 | malfunction |
overexpression of full-length Naa30 increases cell viability via inhibition of apoptosis. In contrast, Naa30288 does not exert an anti-apoptotic effect |
756860 |
| 2.3.1.256 | more |
homology structure modeling of Naa30 using the crystal structure of human Naa50 (PDB ID 3TFY) as template |
756860 |
| 2.3.1.256 | more |
Trypanosoma cruzi NatC protein complex consists of one catalytic subunit TcNaa30 and one predicted auxiliary subunit TcNaa35. TcNatC and TcNatA (EC 2.3.1.255) complex subunits interact in vivo and in vitro |
-, 757472 |
| 2.3.1.256 | physiological function |
MAK3 is required for the N-terminal acetylation of the killer viral major coat protein, Gag |
740668 |
| 2.3.1.256 | physiological function |
MAK3 N-acetyltransferase modifies the L-A gag NH2 terminus which in turn is necessary for virus particle assembly |
740650 |
