NAA35

Last update 08 May 2025

Basic Info

Synonyms

bA379P1.1, EGAP, Embryonic growth-associated protein homolog

+ [6]

Introduction

Auxillary component of the N-terminal acetyltransferase C (NatC) complex which catalyzes acetylation of N-terminal methionine residues (PubMed:19398576, PubMed:37891180). N-terminal acetylation protects proteins from ubiquitination and degradation by the N-end rule pathway (PubMed:37891180). Involved in regulation of apoptosis and proliferation of smooth muscle cells (PubMed:19398576).

100 Clinical Results associated with NAA35

100 Translational Medicine associated with NAA35

0 Patents (Medical) associated with NAA35

Literatures (Medical) associated with NAA35

30 Sep 2024·African Journal of Reproductive Health

Association between genetic polymorphisms in chromosome region 9q21 and pelvic organ prolapse in Northwestern Chinese women

Article

Author: Wang, Jian ; Mao, Baohong ; Lu, Yongli ; Tao, Chengbing ; Wei, Ying ; Liu, Xiyun ; Liu, Qing ; Xu, Wenjing ; Sheng, Yannan

This study aimed to explore the association between genetic polymorphisms in the chromosome region 9q21 and the risk of pelvic organ prolapse (POP) in Northwestern Chinese women. A case-control study was conducted with 241 POP patients and 268 healthy controls, analyzing ten single nucleotide polymorphisms (SNPs) across five genes using PCR amplification and Sequenom MassArray. The results revealed significant associations between three SNPs—rs2297002 in GOLM1, rs7450 in MAK10, and rs3814535 in TLE1—and POP. Specifically, the TC genotype of rs2297002, the GA genotype of rs7450, and the AA genotype of rs3814535 were linked to an increased or decreased risk of POP. The study suggests that these genetic variants might contribute to the pathogenesis of POP in this population, offering potential markers for early diagnosis and further investigation into the molecular mechanisms underlying POP.

01 Sep 2023·American journal of medical genetics. Part A

A nonsense variant in the N-terminal acetyltransferase NAA30 may be associated with global developmental delay and tracheal cleft.

Author: Arnesen, Thomas ; Brønstad, Kirsten Marie ; Varland, Sylvia ; Skinner, Stephanie J

Most human proteins are N-terminally acetylated by N-terminal acetyltransferases (NATs), which play crucial roles in many cellular functions. The NatC complex, comprising the catalytic subunit NAA30 and the auxiliary subunits NAA35 and NAA38, is estimated to acetylate up to 20% of the human proteome in a co-translational manner. Several NAT enzymes have been linked to rare genetic diseases, causing developmental delay, intellectual disability, and heart disease. Here, we report a de novo heterozygous NAA30 nonsense variant c.244C>T (p.Q82*) (NM_001011713.2), which was identified by whole exome sequencing in a 5-year-old boy presenting with global development delay, autism spectrum disorder, hypotonia, tracheal cleft, and recurrent respiratory infections. Biochemical studies were performed to assess the functional impact of the premature stop codon on NAA30's catalytic activity. We find that NAA30-Q82* completely disrupts the N-terminal acetyltransferase activity toward a classical NatC substrate using an in vitro acetylation assay. This finding corresponds with structural modeling showing that the truncated NAA30 variant lacks the entire GNAT domain, which is required for catalytic activity. This study suggests that defective NatC-mediated N-terminal acetylation can cause disease, thus expanding the spectrum of NAT variants linked to genetic disease.

01 Feb 2023·Structure

Molecular role of NAA38 in thermostability and catalytic activity of the human NatC N-terminal acetyltransferase

Article

Author: Pan, Buyan ; Deng, Sunbin ; Gottlieb, Leah ; Gardner, Sarah M ; Marmorstein, Ronen ; Petersson, E James

N-terminal acetylation occurs on over 80% of human proteins and is catalyzed by a family of N-terminal acetyltransferases (NATs). All NATs contain a small catalytic subunit, while some also contain a large auxiliary subunit that facilitates catalysis and ribosome targeting for co-translational acetylation. NatC is one of the major NATs containing an NAA30 catalytic subunit, but uniquely contains two auxiliary subunits, large NAA35 and small NAA38. Here, we report the cryo-EM structures of human NatC (hNatC) complexes with and without NAA38, together with biochemical studies, to reveal that NAA38 increases the thermostability and broadens the substrate-specificity profile of NatC by ordering an N-terminal segment of NAA35 and reorienting an NAA30 N-terminal peptide binding loop for optimal catalysis, respectively. We also note important differences in engagement with a stabilizing inositol hexaphosphate molecule between human and yeast NatC. These studies provide new insights for the function and evolution of the NatC complex.

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NAA35

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