NAA38 is an auxiliary subunit of the N-terminal acetyltransferase C (NatC) complex, which catalyzes acetylation of N-terminal methionine residues on approximately 80% of human proteins 1. NAA38 functions alongside the catalytic subunit NAA30 and the large auxiliary subunit NAA35 to facilitate N-terminal acetylation, primarily through co-translational mechanisms at the ribosome 2. Structurally, NAA38 increases NatC thermostability and broadens substrate specificity by ordering an NAA35 segment and reorienting NAA30's peptide-binding loop for optimal catalysis 1. N-terminal acetylation mediated by the NatC complex protects proteins from ubiquitin-dependent degradation via the N-end rule pathway, thereby regulating protein stability and cellular function. NAA38 dysfunction has been implicated in multiple disease contexts. Genetic variation in NAA38 was identified as a novel type 1 diabetes susceptibility locus through immune cell transcriptomic analysis 3. NAA38 disruption affects ferroptosis sensitivity by regulating intracellular glutathione levels through NRF2-mediated transcription 4. Additionally, inhibition of the NatC complex (including NAA38) mitigates endoplasmic reticulum stress-induced muscle atrophy in cancer cachexia models 5. A chr17 deletion encompassing NAA38 was associated with congenital hearing loss and speech development delay 6, suggesting NAA38 relevance to neurodevelopmental and sensory function.