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Literature summary for 2.3.1.256 extracted from

  • Starheim, K.K.; Kalvik, T.V.; Bjoerkoey, G.; Arnesen, T.
    Depletion of the human N-terminal acetyltransferase hNaa30 disrupts Golgi integrity and ARFRP1 localization (2017), Biosci. Rep., 37, BSR20170066 .
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
additional information siRNA-mediated knockdown of hNAA30 gene expression in HeLa and CAL-62 cells, phenotypes, detailed overview Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
Golgi apparatus
-
 Homo sapiens 5794
-

Organism

Organism UniProt Comment Textmining
Homo sapiens Q147X3
-
-

Source Tissue

Source Tissue Comment Organism Textmining
CAL-62 cell
-
 Homo sapiens
-
HeLa cell
-
 Homo sapiens
-

Synonyms

Synonyms Comment Organism
hNaa30
-
 Homo sapiens
N-alpha-acetyltransferase 30
-
 Homo sapiens
N-terminal acetyltransferase
-
 Homo sapiens
NAA30
-
 Homo sapiens
NAT12 gene name, UniProt Homo sapiens
NatC
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
acetyl-CoA
-
 Homo sapiens

General Information

General Information Comment Organism
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 Homo sapiens
physiological function the human NatC complex (hNatC) is an evolutionarily conserved complex composed of the catalytic subunit hNaa30 (hMak3) and the auxiliary subunits hNaa35 (hMak10) and hNaa38 (hMak31). NatC Nt-acetylates Met-Leu-, Met-Ile-, Met-Phe-, Met-Trp-, Met-Val-, Met-Met-, Met-His-, and Met-Lys-N-termini. The NatC complex is one of several Nt-acetyltransferases (NATs) that perform Nt-acetylation in eukaryotes. Nt-acetylation or protein N-alpha-terminal acetylation, is the addition of an acetyl group on the Nalpha-amino group of proteins. It is one of the most abundant protein modifications in eukaryotes and displays a wide array of biological functions. The Golgi apparatus associated GTPase ADP ribosylation factor related protein 1 (ARFRP1) requires N-terminal acetylation for membrane association and based on its N-terminal sequence, it is likely to be a substrate of hNaa30. ARFRP1 is involved in endosome-to-trans-Golgi network (TGN) traffic Homo sapiens