|SwissProt ID Link
||Catalytic subunit of the N-terminal acetyltransferase A (NatA) complex which displays alpha (N-terminal) acetyltransferase activity. The NAT activity may be important for vascular, hematopoietic and neuronal growth and development. Without NAA15, displays epsilon (internal) acetyltransferase activity towards HIF1A, thereby promoting its degradation. Represses MYLK kinase activity by acetylation, and thus represses tumor cell migration. Acetylates, and stabilizes TSC2, thereby repressing mTOR activity and suppressing cancer development.
||Cytoplasm. Nucleus. According to PubMed:12464182 it is cytoplasmic. According to PubMed:15496142, it is nuclear and cytoplasmic. Also present in the free cytosolic and cytoskeleton-bound polysomes.
|Involvement in Disease
||N-terminal acetyltransferase deficiency: An enzymatic deficiency resulting in postnatal growth failure with severe delays and dysmorphic features. It is clinically characterized by wrinkled forehead, prominent eyes, widely opened anterior and posterior fontanels, downsloping palpebral fissures, thickened lids, large ears, flared nares, hypoplastic alae, short columella, protruding upper lip, and microretrognathia. There are also delayed closing of fontanels and broad great toes. Skin is characterized by redundancy or laxity with minimal subcutaneous fat, cutaneous capillary malformations, and very fine hair and eyebrows. Death results from cardiogenic shock following arrhythmia. The disease is caused by mutations affecting the gene represented in this entry.
Microphthalmia, syndromic, 1: A rare syndrome defined by the canonical features of unilateral or bilateral microphthalmia or anophthalmia and defects in the skeletal and genitourinary systems. Microphthalmia is a disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues
. In many cases, microphthalmia/anophthalmia occurs in association with syndromes that include non-ocular abnormalities. Anomalies of the digits, teeth, and ears are hallmarks of MCOPS1. Intellectual disability ranges from mild to severe, with self-mutilating behaviors and seizures in severely affected MCOPS1 individuals. The disease is caused by mutations affecting the gene represented in this entry.
||Cleaved by caspases during apoptosis.Phosphorylation by IKBKB/IKKB at Ser-209 promotes its proteasome-mediated degradation.
||Component of the N-terminal acetyltransferase A (NatA) complex composed of NAA10 and NAA15 or NAA16. Interacts with HIF1A (via its ODD domain); the interaction increases HIF1A protein stability during normoxia, an down-regulates it when induced by hypoxia. Interacts with NAA50 and with the ribosome. Binds to MYLK. Associates with HYPK when in complex with NAA15. Interacts (via its C-terminal domain) with TSC2, leading to its acetylation.
||Belongs to the acetyltransferase family. ARD1 subfamily.
Contains 1 N-acetyltransferase domain.