U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

Naa10 N(alpha)-acetyltransferase 10, NatA catalytic subunit [ Mus musculus (house mouse) ]

Gene ID: 56292, updated on 27-Nov-2024

Summary

Go to the top of the page Help
Official Symbol
Naa10provided by MGI
Official Full Name
N(alpha)-acetyltransferase 10, NatA catalytic subunitprovided by MGI
Primary source
MGI:MGI:1915255
See related
Ensembl:ENSMUSG00000031388 AllianceGenome:MGI:1915255
Gene type
protein coding
RefSeq status
VALIDATED
Organism
Mus musculus
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as
Te2; Ard1; Ard1a; 2310039H09Rik
Summary
Enables N-acetyltransferase activity. Predicted to be involved in N-terminal protein amino acid acetylation and negative regulation of maintenance of mitotic sister chromatid cohesion, centromeric. Located in cytoplasm. Is expressed in several structures, including brain; genitourinary system; heart; liver; and submandibular gland primordium. Human ortholog(s) of this gene implicated in Ogden syndrome and syndromic microphthalmia 1. Orthologous to human NAA10 (N-alpha-acetyltransferase 10, NatA catalytic subunit). [provided by Alliance of Genome Resources, Nov 2024]
Expression
Ubiquitous expression in liver E14.5 (RPKM 30.5), large intestine adult (RPKM 29.1) and 27 other tissues See more
Orthologs
human all
NEW
Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help
See Naa10 in Genome Data Viewer
Location:
X A7.3; X 37.49 cM
Exon count:
8
Annotation release Status Assembly Chr Location
RS_2024_02 current GRCm39 (GCF_000001635.27) X NC_000086.8 (72960476..72965550, complement)
108.20200622 previous assembly GRCm38.p6 (GCF_000001635.26) X NC_000086.7 (73916870..73921944, complement)

Chromosome X - NC_000086.8Genomic Context describing neighboring genes Neighboring gene L1 cell adhesion molecule Neighboring gene Rho GTPase activating protein 4 Neighboring gene arginine vasopressin receptor 2 Neighboring gene CapStarr-seq enhancer MGSCv37_chrX:71157031-71157252 Neighboring gene STARR-seq mESC enhancer starr_47360 Neighboring gene renin binding protein Neighboring gene STARR-seq mESC enhancer starr_47361 Neighboring gene host cell factor C1 Neighboring gene STARR-seq mESC enhancer starr_47362

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to nucleotide: Graphics FASTA GenBank

Expression

Go to the top of the page Help
  • Project title: Mouse ENCODE transcriptome data
  • Description: RNA profiling data sets generated by the Mouse ENCODE project.
  • BioProject: PRJNA66167
  • Publication: PMID 25409824
  • Analysis date: n/a

Bibliography

Go to the top of the pageHelp

Related articles in PubMed

  1. Evaluating possible maternal effect lethality and genetic background effects in Naa10 knockout mice. Lyon GJ, et al. PLoS One, 2024. PMID 38713657, Free PMC Article
  2. The N-end rule pathway enzyme Naa10 supports epiblast specification in mouse embryonic stem cells by modulating FGF/MAPK. Takekoshi D, et al. In Vitro Cell Dev Biol Anim, 2019 May. PMID 30993557
  3. Characterization of ARD1 variants in mammalian cells. Kim SH, et al. Biochem Biophys Res Commun, 2006 Feb 10. PMID 16376303
  4. Differential regulation of splicing, localization and stability of mammalian ARD1235 and ARD1225 isoforms. Chun KH, et al. Biochem Biophys Res Commun, 2007 Feb 2. PMID 17161380
  5. N-acetyltransferase ARD1-NAT1 regulates neuronal dendritic development. Ohkawa N, et al. Genes Cells, 2008 Nov. PMID 19090811

See all (36) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Evaluating possible maternal effect lethality and genetic background effects in Naa10 knockout mice.
    Title: Evaluating possible maternal effect lethality and genetic background effects in Naa10 knockout mice.
  2. Naa12 compensates for Naa10 in mice in the amino-terminal acetylation pathway.
    Title: Naa12 compensates for Naa10 in mice in the amino-terminal acetylation pathway.
  3. Naa10p-mediated N-terminal acetylation of Pgc1alpha downregulates thermogenic gene expression in beige adipocytes.
    Title: Naa10p Inhibits Beige Adipocyte-Mediated Thermogenesis through N-α-acetylation of Pgc1α.
  4. we established Naa10 knockout mESCs to test this hypothesis. We found that Naa10 deficiency attenuated differentiation towards the epiblast lineage, deviating towards primitive endoderm.
    Title: The N-end rule pathway enzyme Naa10 supports epiblast specification in mouse embryonic stem cells by modulating FGF/MAPK.
  5. Negative regulation of Naa10 towards NTN1 and its receptor UNC5B were also detected upon treatment of all-trans retinoid acid, which was often used to induce morphological differentiation.
    Title: Unc-5 homolog B (UNC5B) is one of the key downstream targets of N-α-Acetyltransferase 10 (Naa10).
  6. The lethal Ogden syndrome-associated mutation of Naa10p disrupts its binding to the imprinting control region of H19 and Dnmt1 recruitment.
    Title: The Role of N-α-acetyltransferase 10 Protein in DNA Methylation and Genomic Imprinting.
  7. NAA10 acts as a guard ensuring balanced osteogenesis by fine-tuning Runx2 signalling in a feedback manner.
    Title: NAA10 controls osteoblast differentiation and bone formation as a feedback regulator of Runx2.
  8. ARD1 has a crucial role in the cellular response to oxidative stress as a bona fide regulator of MSRA.
    Title: Arrest defective 1 regulates the oxidative stress response in human cells and mice by acetylating methionine sulfoxide reductase A.
  9. mARD1A(225) may be a novel upstream target that blocks VEGFA expression and tumor-related angiogenesis.
    Title: Roles of arrest-defective protein 1(225) and hypoxia-inducible factor 1alpha in tumor growth and metastasis.
  10. Biochemical analysis demonstrated that mNAT1 and its evolutionarily conserved co-subunit, mARD1, assemble to form a functional acetyltransferase.
    Title: An evolutionarily conserved N-terminal acetyltransferase complex associated with neuronal development.
Submit: New GeneRIF Correction See all GeneRIFs (12)

Variation

Go to the top of the page Help

Alleles

Alleles of this type are documented at Mouse Genome Informatics  (MGI)
  • Endonuclease-mediated (6) 
  • Targeted (3)  1 citation

Interactions

Go to the top of the page Help
Products Interactant Other Gene Complex Source Pubs Description

General gene information

Go to the top of the page Help

Markers

Homology

Gene Ontology Provided by MGI

Function Evidence Code Pubs
enables N-acetyltransferase activity IDA
Inferred from Direct Assay
more info
 PubMed 
contributes_to acetyltransferase activity ISO
Inferred from Sequence Orthology
more info
  
contributes_to peptide alpha-N-acetyltransferase activity ISO
Inferred from Sequence Orthology
more info
  
enables peptide alpha-N-acetyltransferase activity ISO
Inferred from Sequence Orthology
more info
  
enables peptide alpha-N-acetyltransferase activity ISS
Inferred from Sequence or Structural Similarity
more info
  
enables peptide-alanine-alpha-N-acetyltransferase activity IEA
Inferred from Electronic Annotation
more info
  
enables peptide-glutamate-alpha-N-acetyltransferase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables peptide-serine-alpha-N-acetyltransferase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables peptide-serine-alpha-N-acetyltransferase activity IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables ribosome binding IEA
Inferred from Electronic Annotation
more info
  
contributes_to ribosome binding ISO
Inferred from Sequence Orthology
more info
  
Process Evidence Code Pubs
involved_in N-terminal protein amino acid acetylation ISO
Inferred from Sequence Orthology
more info
  
involved_in N-terminal protein amino acid acetylation ISS
Inferred from Sequence or Structural Similarity
more info
  
involved_in negative regulation of maintenance of mitotic sister chromatid cohesion, centromeric ISO
Inferred from Sequence Orthology
more info
  
involved_in negative regulation of maintenance of mitotic sister chromatid cohesion, centromeric ISS
Inferred from Sequence or Structural Similarity
more info
  
involved_in protein acetylation ISO
Inferred from Sequence Orthology
more info
  
Component Evidence Code Pubs
part_of NatA complex IBA
Inferred from Biological aspect of Ancestor
more info
  
part_of NatA complex IEA
Inferred from Electronic Annotation
more info
  
part_of NatA complex ISO
Inferred from Sequence Orthology
more info
  
located_in cytoplasm IDA
Inferred from Direct Assay
more info
 PubMed 
located_in cytoplasm ISO
Inferred from Sequence Orthology
more info
  
located_in cytosol IEA
Inferred from Electronic Annotation
more info
  
located_in cytosol ISO
Inferred from Sequence Orthology
more info
  
located_in nucleolus IEA
Inferred from Electronic Annotation
more info
  
located_in nucleolus ISO
Inferred from Sequence Orthology
more info
  
located_in nucleus ISO
Inferred from Sequence Orthology
more info
  
located_in nucleus ISS
Inferred from Sequence or Structural Similarity
more info
  

General protein information

Go to the top of the page Help
Preferred Names
N-alpha-acetyltransferase 10
Names
ARD1 homolog A, N-acetyltransferase
N(alpha)-acetyltransferase 10, NatA catalytic subunitNalpha acetyltransferase 10
N-terminal acetyltransferase complex ARD1 subunit homolog A
Nalpha acetyltransferase 10
alpha-N-acetyltransferase 1A
natA catalytic subunit Naa10
NP_001171436.1
NP_001297467.1
NP_063923.1
XP_036017930.1
XP_036017931.1
XP_036017932.1

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

  1. NM_001177965.1 → NP_001171436.1  N-alpha-acetyltransferase 10 isoform 2

    See identical proteins and their annotated locations for NP_001171436.1

    Status: VALIDATED

    Description
    Transcript Variant: This variant (2) uses an alternate splice site in the 3' coding region, which results in a frameshift, compared to variant 1. The resulting protein (isoform 2) has a shorter and distinct C-terminus compared to isoform 1.
    Source sequence(s)
    AK003806, AL672002, BY101790
    Consensus CDS
    CCDS53102.1
    UniProtKB/TrEMBL
    Q3V4D5, Q8R2U5
    Related
    ENSMUSP00000110031.4, ENSMUST00000114389.10
    Conserved Domains (2) summary
    COG0456
    Location:1 → 149
    RimI; Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis]
    pfam00583
    Location:47 → 122
    Acetyltransf_1; Acetyltransferase (GNAT) family

  2. NM_001310538.1 → NP_001297467.1  N-alpha-acetyltransferase 10 isoform 3

    Status: VALIDATED

    Description
    Transcript Variant: This variant (3) uses an alternate splice site in the 3' coding region, which results in a frameshift, compared to variant 1. The resulting protein (isoform 3) has a shorter and distinct C-terminus compared to isoform 1.
    Source sequence(s)
    AK003806, BY101790, CN666135
    Consensus CDS
    CCDS81139.1
    UniProtKB/TrEMBL
    B1AUY9
    Related
    ENSMUSP00000110029.2, ENSMUST00000114387.8
    Conserved Domains (1) summary
    COG0456
    Location:1 → 149
    RimI; Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis]

  3. NM_019870.3 → NP_063923.1  N-alpha-acetyltransferase 10 isoform 1

    See identical proteins and their annotated locations for NP_063923.1

    Status: VALIDATED

    Description
    Transcript Variant: This variant (1) represents the shortest transcript but encodes the longest isoform (1).
    Source sequence(s)
    AL672002
    Consensus CDS
    CCDS30217.1
    UniProtKB/Swiss-Prot
    Q9QY36
    UniProtKB/TrEMBL
    B1AUY7, Q540H0
    Related
    ENSMUSP00000033763.9, ENSMUST00000033763.15
    Conserved Domains (1) summary
    COG0456
    Location:1 → 149
    RimI; Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis]

RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCm39 C57BL/6J

Genomic

  1. NC_000086.8 Reference GRCm39 C57BL/6J

    Range
    72960476..72965550 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_036162037.1 → XP_036017930.1  N-alpha-acetyltransferase 10 isoform X1

    UniProtKB/TrEMBL
    Q684Q8
    Conserved Domains (1) summary
    COG0456
    Location:15 → 138
    RimI; Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis]

  2. XM_036162039.1 → XP_036017932.1  N-alpha-acetyltransferase 10 isoform X3

    Conserved Domains (1) summary
    COG0456
    Location:15 → 138
    RimI; Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis]

  3. XM_036162038.1 → XP_036017931.1  N-alpha-acetyltransferase 10 isoform X2

    UniProtKB/TrEMBL
    Q8R2U5
    Conserved Domains (1) summary
    COG0456
    Location:15 → 138
    RimI; Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis]

RNA

  1. XR_004940354.1 RNA Sequence

  2. XR_003953017.2 RNA Sequence

Nucleotide Protein Strain
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
Q9QY36.1 GenPept UniProtKB/Swiss-Prot:Q9QY36

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

Chemical Information
Molecular Biology Databases
Research Materials
Tools