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FLASH GENE
Symbol NAT10 contributors: mct - updated : 01-06-2022
HGNC name N-acetyltransferase 10
HGNC id 29830
DNA
TYPE functioning gene
STRUCTURE 41.28 kb     29 Exon(s)
MAPPING cloned Y linked N status provisional
RNA
TRANSCRIPTS type messenger
identificationnb exonstypebpproduct
ProteinkDaAAspecific expressionYearPubmed
29 - 3973 115 1025 - 2021 33723305
28 - 3758 - 953 - 2021 33723305
EXPRESSION
Type ubiquitous
   expressed in (based on citations)
organ(s)
SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
Digestivemouthtongue  highly
Lymphoid/Immunespleen   highly
Reproductivefemale systemuteruscervix  
tissue
SystemTissueTissue level 1Tissue level 2LevelPubmedSpeciesStageRna symbol
Blood / hematopoieticbone marrow   
cell lineage
cell lines
fluid/secretion
at STAGE
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • an N-acetyltransferase domain
  • an ATP/GTP-binding motif
  • an ATPase domain
  • HOMOLOGY
    Homologene
    FAMILY
  • putative ATPase family
  • CATEGORY adaptor , enzyme , RNA associated
    SUBCELLULAR LOCALIZATION     intracellular
    intracellular,nucleus,nucleoplasm
    intracellular,nucleus,chromatin/chromosome,telomere
    intracellular,nucleus,nucleolus
    text
  • localizes mainly in the nucleolus, which has a known role in maintaining nuclear shape
  • is not only predominantly distributed in the nucleolus in interphase, but is also concentrated in the mitotic midbody during telophase
  • basic FUNCTION
  • influences the activity of histone acetylation and could up-regulate telomerase activity through transactivation of TERT promoter
  • may play an important role in cell division through facilitating reformation of the nucleolus and midbody in the late phase of cell mitosis, and stabilization of microtubules
  • lysine acetyltransferase that targets microtubules and histones and plays an important role in cell division
  • is an ATP-dependent RNA acetyltransferase responsible for formation of N(4)-acetylcytidine (ac(4)C) at position 1842 in the terminal helix of mammalian 18 S rRNA
  • RNA cytosine acetyltransferases with, surprisingly, specificity toward both 18S rRNA and tRNAs
  • effects of NAT10 on laminopathic cells are due to reduced ribosome biogenesis or function
  • NAT10 plays a critical role in TP53 activation via acetylating TP53 and counteracting MDM2 action, providing a novel pathway by which nucleolar protein activates TP53 as a cellular stress sensor
  • plays a role in the transition between rRNA biogenesis and autophagy
  • participates in different maturation events, such as acetylation and processing of 18S rRNA, and assembly of the 40S ribosomal subunit
  • role of human NAT10 in Hutchinson-Gilford progeria syndrome
  • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    a component
    INTERACTION
    DNA
    RNA
    small molecule
    protein
  • interacting with TERT
  • is a novel regulator for TP53 activation
  • THUMPD1 is a specific adaptor protein that modulates tRNA acetylation through interaction with NAT10
  • upon energy stress, NAT10 is deacetylated by SIRT1, leading to suppression of NAT10-activated rRNA biogenesis
  • cell & other
    REGULATION
    Other acetylation of K426 in NAT10 is required for its function in activating rRNA transcription, and this new post-translational modification on NAT10 which regulates its function
    ASSOCIATED DISORDERS
    corresponding disease(s)
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    tumoral       gain of function
    in acute myeloid leukemia
    Susceptibility
    Variant & Polymorphism
    Candidate gene
    Marker
  • potential prognostic and therapeutic biomarker for AML
  • Therapy target
    SystemTypeDisorderPubmed
    neuromuscular  
    small molecule inhibitors of NAT10 may thus provide additional ways to study laminopathy-associated processes with spatial and temporal resolution, as well as opportunities for alleviating dystrophic and premature-ageing diseases
    ANIMAL & CELL MODELS