NAA35 is an auxiliary subunit of the N-terminal acetyltransferase C (NatC) complex, which catalyzes acetylation of N-terminal methionine residues on approximately 20% of human proteins 1. NAA35 functions as a large auxiliary component that enhances NatC thermostability and broadens substrate specificity by ordering an N-terminal segment and optimizing the catalytic environment 2. N-terminal acetylation by NatC protects proteins from ubiquitin-mediated degradation via the N-end rule pathway and is essential for proper protein localization to the Golgi apparatus, inner nuclear membrane, and mitochondria 3. NAA35 plays important roles in regulating smooth muscle cell apoptosis and proliferation. Clinically, NAA35 dysfunction has been implicated in cerebral palsy as a candidate disease gene identified through whole-exome sequencing 4. Additionally, NAA35 upregulation contributes to muscle wasting in cancer cachexia through endoplasmic reticulum stress pathways; NAA35 inhibition reduces cathepsin K-mediated proteolysis and preserves muscle mass and strength in cancer-bearing mice 5. NAA35 has also been identified as a molecular signature associated with keloid formation 6, and GOLM1-NAA35 chimeric RNA in salivary exosomes shows promise as a noninvasive biomarker for esophageal squamous cell carcinoma detection and treatment monitoring 7.