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NAT1 peptide alpha-N-acetyltransferase complex A subunit NAT1 [ Saccharomyces cerevisiae S288C ]

Gene ID: 851521, updated on 13-Apr-2024

Summary

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Gene symbol
NAT1
Gene description
peptide alpha-N-acetyltransferase complex A subunit NAT1
Primary source
SGD:S000002198
Locus tag
YDL040C
See related
AllianceGenome:SGD:S000002198
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Saccharomyces cerevisiae S288C (strain: S288C)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as
AAA1; NAA15
Summary
Enables ribosome binding activity. Contributes to peptide alpha-N-acetyltransferase activity. Involved in N-terminal protein amino acid acetylation. Located in mitochondrion. Part of NatA complex. Used to study autism spectrum disorder; congenital heart disease; and intellectual disability. Human ortholog(s) of this gene implicated in autosomal dominant mental retardation 50. Orthologous to human NAA15 (N-alpha-acetyltransferase 15, NatA auxiliary subunit) and NAA16 (N-alpha-acetyltransferase 16, NatA auxiliary subunit). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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Location:
chromosome: IV
Exon count:
1
Sequence:
Chromosome: IV; NC_001136.10 (378874..381438, complement)

Chromosome IV - NC_001136.10Genomic Context describing neighboring genes Neighboring gene Prp11p Neighboring gene NAD-dependent histone deacetylase SIR2 Neighboring gene pheromone-regulated protein PRM7 Neighboring gene Bsc1p

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_001136.10

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Analysis of the Structural Mechanism of ATP Inhibition at the AAA1 Subunit of Cytoplasmic Dynein-1 Using a Chemical "Toolkit". Tati S, et al. Int J Mol Sci, 2021 Jul 19. PMID 34299323, Free PMC Article
  2. Rapid Identification of Major QTL(S) Associated With Near- Freezing Temperature Tolerance in Saccharomyces cerevisiae. Feng L, et al. Front Microbiol, 2018. PMID 30254614, Free PMC Article
  3. N(α)-Acetylation of yeast ribosomal proteins and its effect on protein synthesis. Kamita M, et al. J Proteomics, 2011 Apr 1. PMID 21184851
  4. Sequence requirements for Nalpha-terminal acetylation of yeast proteins by NatA. Perrot M, et al. Yeast, 2008 Jul. PMID 18615858
  5. N alpha acetylation is required for normal growth and mating of Saccharomyces cerevisiae. Lee FJ, et al. J Bacteriol, 1989 Nov. PMID 2681143, Free PMC Article

See all (86) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Structure and mechanism of acetylation by the N-terminal dual enzyme NatA/Naa50 complex has been reported.
    Title: Structure and Mechanism of Acetylation by the N-Terminal Dual Enzyme NatA/Naa50 Complex.
  2. NatA from humans and yeast have identical or nearly identical specificities
    Title: Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humans.
  3. NatA null strains are specifically impaired in establishing the translation termination defect that normally accompanies Sup35 incorporation into prion complexes.
    Title: The NatA acetyltransferase couples Sup35 prion complexes to the [PSI+] phenotype.
Submit: New GeneRIF Correction

Pathways from PubChem

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Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Homology

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables ribosome binding IDA
Inferred from Direct Assay
more info
 PubMed 
Process Evidence Code Pubs
involved_in N-terminal peptidyl-methionine acetylation IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in N-terminal protein amino acid acetylation IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in N-terminal protein amino acid acetylation IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
part_of NatA complex IBA
Inferred from Biological aspect of Ancestor
more info
  
part_of NatA complex IDA
Inferred from Direct Assay
more info
 PubMed 
is_active_in cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
located_in mitochondrion HDA PubMed 

General protein information

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Preferred Names
peptide alpha-N-acetyltransferase complex A subunit NAT1
NP_010244.1
  • Subunit of protein N-terminal acetyltransferase NatA; NatA comprised of Nat1p, Ard1p, and Nat5p; N-terminally acetylates many proteins to influence multiple processes such as cell cycle progression, heat-shock resistance, mating, sporulation, telomeric silencing and early stages of mitophagy; orthologous to human NAA15; expression of both human NAA10 and NAA15 functionally complements ard1 nat1 double mutant although single mutations are not complemented by their orthologs

NCBI Reference Sequences (RefSeq)

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Genome Annotation

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

Reference assembly

Genomic

  1. NC_001136.10 Reference assembly

    Range
    378874..381438 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001180099.1 → NP_010244.1  TPA: peptide alpha-N-acetyltransferase complex A subunit NAT1 [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_010244.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6VRV5, P12945
    UniProtKB/TrEMBL
    A0A8H8UMP0, A6ZXT4, C8Z4N0, G2WCC0, N1PAA6
    Conserved Domains (3) summary
    COG4783
    Location:1 → 191
    YfgC; Putative Zn-dependent protease, contains TPR repeats [General function prediction only]
    sd00006
    Location:24 → 48
    TPR; TPR repeat [structural motif]
    pfam12569
    Location:199 → 736
    NARP1; NMDA receptor-regulated protein 1
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
6HD5_t.1
P12945.2

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