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N-alpha-acetyltransferase 11, NatA catalytic subunit (NAA11)

Target
NAA11
Molecular classification
Enzyme, N-terminal acetyltransferase, N(alpha)-acetyltransferase subunit, Protein modifying enzyme
01

Overview

N-alpha-acetyltransferase 11, NatA catalytic subunit (NAA11), also known as ARD1B or ARD2, is an enzyme and alternative catalytic subunit of the NatA N-terminal acetyltransferase complex, homologous to the ubiquitously expressed NAA10(ARD1)[1][3]. NAA11 catalyzes the N-terminal acetylation of proteins, a common and evolutionarily conserved post-translational modification essential for regulating protein stability, localization, and interactions[1]. It is predominantly expressed in testicular and placental tissues, with expression tightly controlled by DNA methylation, and is typically absent in most other tissues and cancer lines due to CpG island hypermethylation at its promoter[1]. NAA11 and NAA10 likely serve nonredundant, tissue-specific roles in the human NatA complex[1]. Animal model and cancer studies suggest a functional role for NAA11 in regulating cell-specific processes but its direct association with substantial cancer biology or therapeutic targeting remains underexplored[1][3]. No approved drugs are currently known to act specifically on NAA11 nor are there established clinical biomarkers or safety concerns for this target[1][2][3][4]. Key information: - Human protein-coding gene, belongs to the N(alpha)-acetyltransferase subunit family[1]. - Localized mainly to the Golgi apparatus, centrosome, and nucleoplasm[1]. - Expression pattern is distinct from NAA10 and largely restricted to reproductive tissues, regulated by promoter methylation[1]. - The potential role in cancer, particularly related to loss of heterozygosity and methylation status, needs further research[1]. - Known by several alternative names/aliases, commonly NAA11, ARD1B, ARD2, and hARD2[1].

Other names
ARD1BARD2hARD2HARD2NAA11ARD1 homolog BN-terminal acetyltransferase complex ARD1 subunit homolog Bhuman arrest defective 2
02

Biological functions

Protein N-terminal acetylationRegulation of protein stabilityRegulation of protein–protein interactionsRegulation of protein localization
03

Disease associations

Cancer (noted in loss of heterozygosity studies and epigenetic regulation in cancer tissues)Other (possible tissue- or cancer-specific regulatory roles)

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