NAA10/ARD1 Protein, Human (sf9)

NAA10, the catalytic subunit of N-terminal acetyltransferase complexes, exhibits alpha (N-terminal) acetyltransferase activity, playing a crucial role in acetylating amino termini lacking initiator methionine. This activity holds significance in processes related to vascular, hematopoietic, and neuronal growth and development. In conjunction with NAA15, NAA10 displays epsilon (internal) acetyltransferase activity towards HIF1A, leading to its degradation and impacting cellular responses. Notably, NAA10 has diverse roles, repressing MYLK kinase activity through acetylation to inhibit tumor cell migration and stabilizing TSC2, thereby suppressing mTOR activity and impeding cancer development. Furthermore, NAA10 acetylates HSPA1A and HSPA1B at 'Lys-77,' enhancing their chaperone activity and promoting preferential binding to co-chaperone HOPX. Additional substrates include HIST1H4A, indicating a broad impact on cellular processes. Intriguingly, NAA10 acts as a negative regulator of sister chromatid cohesion during mitosis, underscoring its multifunctional role in cellular homeostasis.