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Official Full Name
N(alpha)-acetyltransferase 10, NatA catalytic subunit
N-alpha-acetylation is among the most common post-translational protein modifications in eukaryotic cells. This process involves the transfer of an acetyl group from acetyl-coenzyme A to the alpha-amino group on a nascent polypeptide and is essential for normal cell function. This gene encodes an N-terminal acetyltransferase that functions as the catalytic subunit of the major amino-terminal acetyltransferase A complex. Mutations in this gene are the cause of Ogden syndrome. Alternate splicing results in multiple transcript variants.
TE2; ARD1; ARD1A; DXS707; MGC71248; N-alpha-acetyltransferase 10, NatA catalytic subunit; OTTHUMP00000026001; OTTHUMP00000026002; OTTHUMP00000064808; OTTHUMP00000064809; OTTHUMP00000180622; OTTHUMP00000180623; ARD1 homolog, N-acetyltransferase; ARD1 homolog A, N-acetyltransferase; N-acetyltransferase ARD1, human homolog of; N-terminal acetyltransferase complex ARD1 subunit homolog A; NAA10; NATD; N(alpha)-acetyltransferase 10, NatA catalytic subunit; N-alpha-acetyltransferase 10; EC; TE2, ARD1, NATD, ARD1A, DXS707; zgc:63981; hm:zeh0223; wu:fc66b08

Nα-terminal acetylation (NTA) is one of the most common protein modifications that occur during protein synthesis and involves the transfer of an acetyl group from acetyl-coenzyme A to the protein alpha-amino group in many biologic processes. N-terminal acetyltransferase A (NatA) consists of the catalytic subunit Naa10 and the auxiliary subunit Naa15 and acetylates small side chains such as Ser, Ala, Thr, Gly, Val and Cys after the initiator methionine has been cleaved by methionine aminopeptidases.

N-alpha-acetyltransferase 10 (NAA10) is a catalytic subunit of the NatA complex which shows alpha (N-terminal) acetyltransferase activity [1]. The subcellular location of NAA10 is cytoplasm and nucleus. The alpha (N-terminal) acetyltransferase activity may play an important role in vascular, hematopoietic and neuronal growth and development [2].

Gene Function

  • Without NAA15, NAA10 shows epsilon (internal) acetyltransferase activity towards HIF1A, thereby promoting its degradation [3].
  • NAA10 represses MYLK kinase activity by acetylation, and thus represses tumor cell migration [4].
  • NAA10 acetylates, and stabilizes TSC2, thereby repressing mTOR activity and suppressing cancer development [5].
  • NAA10 acetylates HSPA1A and HSPA1B at 'Lys-77' which enhances its chaperone activity and leads to preferential binding to co-chaperone HOPX [1].
  • NAA10 acts as a negative regulator of sister chromatid cohesion during mitosis [6].

Fig.1. Multiple functions of Naa10 [7].

The relationships between gene and major human diseases

The relationships between NAA10 and diseases in humans are only recently emerging. For example, many studies combine NAA10 to neurodegenerative disorders, such as Alzheimer’s, Parkinson’s and Huntington’s disease, where abnormal manifestations of single proteins are believed to contribute to disease. Recently, several studies identified mutations of NAA10 in human patients with discrete symptoms, including a craniofacial anomalies, aged appearance, developmental delay, hypotonia, growth retardation and Lenz microphthalmia syndrome. However, the small phenotypic overlap between these patients suggests that different substrates or functions of NAA10 might be affected.

  • Alzheimer’s disease (AD)

Study has shown that Naa10 binds the cytoplasmic domain of the type I membrane protein β-amyloid precursor protein (APP) and colocalizes with it by its 50 C-terminal amino acids in HEK293 cells [8]. In AD, APP gets processed into beta-amyloid (Aβ) fragments that accumulate into plaques of abnormally folded proteins in the brain. Overexpression of the NatA complex (Naa10 wild type/Naa15 wild type) in HEK293 cells decreases endocytosis of APP and suppresses Aβ40 secretion, whereas the expression of an enzymatic-dead NatA (Naa10 R82A or G85A/Naa15 wild type) attenuated this suppression [8]. However, the mechanism by which NatA regulates Aβ production remains unclear.

  • N-terminal acetyltransferase deficiency (NATD)

NATD is an enzymatic deficiency disease resulting in postnatal growth failure with severe delays and dysmorphic features. Popp et al proposed that N-terminal acetyltransferase deficiency is clinically heterogeneous with the overall catalytic activity determining the phenotypic severity. Casey et al. identified a hemizygous missense mutation in the NAA10 gene [9, 10].

  • Lenz microphthalmia syndrome (LMS)

A rare syndrome defined by the canonical features of unilateral or bilateral microphthalmia or anophthalmia and defects in the skeletal and genitourinary systems. The study identified that the NAA10 mutation is the cause of LMS in the diseased family, likely through the dysregulation of the retinoic acid signaling pathway [11].


Most studies have paid attention to the N-terminal activity of NAA10, whereas some findings have been connected to lysine activity and the independent role of NAA10. The goal of future studies will be to elaborate on the cellular/molecular specific activity and distinct pathways of NAA10. Above all, in vivo studies are essential to analyze the definite biological effects of NAA10.


  1. Seo, J.H., et al., ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation. Nat Commun, 2016. 7: p. 12882.
  2. Arnesen, T., et al., Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humans. Proc Natl Acad Sci U S A, 2009. 106(20): p. 8157-62.
  3. Jeong, J.W., et al., Regulation and destabilization of HIF-1alpha by ARD1-mediated acetylation. Cell, 2002. 111(5): p. 709-20.
  4. Shin, D.H., et al., Arrest defective-1 controls tumor cell behavior by acetylating myosin light chain kinase. PLoS One, 2009. 4(10): p. e7451.
  5. Kuo, H.P., et al., ARD1 stabilization of TSC2 suppresses tumorigenesis through the mTOR signaling pathway. Sci Signal, 2010. 3(108): p. ra9.
  6. Rong, Z., et al., Opposing Functions of the N-terminal Acetyltransferases Naa50 and NatA in Sister-chromatid Cohesion. J Biol Chem, 2016. 291(36): p. 19079-91.
  7. Dorfel, M.J. and G.J. Lyon, The biological functions of Naa10 - From amino-terminal acetylation to human disease. Gene, 2015. 567(2): p. 103-31.
  8. Asaumi, M., et al., Interaction of N-terminal acetyltransferase with the cytoplasmic domain of beta-amyloid precursor protein and its effect on A beta secretion. J Biochem, 2005. 137(2): p. 147-55.
  9. Casey, J.P., et al., NAA10 mutation causing a novel intellectual disability syndrome with Long QT due to N-terminal acetyltransferase impairment. Sci Rep, 2015. 5: p. 16022.
  10. Myklebust, L.M., et al., Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt-acetylation defects. Hum Mol Genet, 2015. 24(7): p. 1956-76.
  11. Esmailpour, T., et al., A splice donor mutation in NAA10 results in the dysregulation of the retinoic acid signalling pathway and causes Lenz microphthalmia syndrome. J Med Genet, 2014. 51(3): p. 185-96.