Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Autoacetylation of NAT10 is critical for its function in rRNA transcription activation.

Biochemical and biophysical research communications - 29 Jan 2017

Cai Shiying, Liu Xiaofeng, Zhang Chunfeng, Xing Baocai, Du Xiaojuan

Abstract excerpt

NAT10, an important member of GNAT family, harbors histone acetyltransferase and participates in many cellular processes such as ribosome production and cell cycle. Here, we report that NAT10 is acetylated in vivo and autoacetylated in vitro. The lysine residue at 426 (K426) is the acetylation site of NAT10. K426R mutant of NAT10 fails to activate rRNA transcription. NAT10 K426R loses its capability of...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Lysine
Share to Acetylation
Share to HCT116 Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HeLa Cells

Share to Protein Processing, Post-Translational

Share to RNA Polymerase I

Share to RNA, Ribosomal

Share to Transcriptional Activation

Source

Identifiers

PMID: 27993683
DOI: 10.1016/j.bbrc.2016.12.092

Genes

NAT10

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Autoacetylation of NAT10 is critical for its function in rRNA transcription activation.PMID 27993683Read ↗

Biological Function and Mechanism of NAT10 in CancerSemantic proximity Read ↗

Research progress on NAT10-mediated acetylation in normal development and diseaseSemantic proximity Read ↗

Cellular effects of NAT-mediated histone N-terminal acetylationSemantic proximity Read ↗

The biological functions of Naa10 – from amino-terminal acetylation to human diseaseSemantic proximity Read ↗

NAA10 p.(D10G) and NAA10 p.(L11R) Variants Hamper Formation of the NatA N-Terminal Acetyltransferase Complex.Semantic proximity Read ↗

NAT10‐mediated mRNA N4‐acetylcytidine modification promotes bladder cancer progressionSemantic proximity Read ↗

Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt-acetylation defects.Semantic proximity Read ↗

Emerging role of N-acetyltransferase 10 in diseases: RNA ac4C modification and beyondSemantic proximity Read ↗

NATs at a glanceSemantic proximity Read ↗

A novel human NatA Nα-terminal acetyltransferase complex: hNaa16p-hNaa10p (hNat2-hArd1)Semantic proximity Read ↗

A novel NAA10 variant with impaired acetyltransferase activity causes developmental delay, intellectual disability, and hypertrophic cardiomyopathy.Semantic proximity Read ↗

Missense NAA20 variantsimpairing the NatB protein N-terminal acetyltransferase cause autosomal recessivedevelopmental delay, intellectual disability, and microcephalySemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.