NAT1/YDL040C Summary Help

Standard Name NAT1 1
Systematic Name YDL040C
Alias AAA1 2 , NAA15 3
Feature Type ORF, Verified
Description Subunit of protein N-terminal acetyltransferase NatA; NatA is comprised of Nat1p, Ard1p, and Nat5p; N-terminally acetylates many proteins, which influences multiple processes such as the cell cycle, heat-shock resistance, mating, sporulation, and telomeric silencing (1, 4, 5, 6 and see Summary Paragraph)
Name Description N-terminal AcetylTransferase 1
Chromosomal Location
ChrIV:381438 to 378874 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Genetic position: -14.93 cM
Gene Ontology Annotations All NAT1 GO evidence and references
  View Computational GO annotations for NAT1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 4 genes
Classical genetics
Large-scale survey
277 total interaction(s) for 228 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 39
  • Affinity Capture-RNA: 3
  • Affinity Capture-Western: 5

Genetic Interactions
  • Dosage Rescue: 2
  • Phenotypic Enhancement: 2
  • Synthetic Growth Defect: 203
  • Synthetic Lethality: 21
  • Synthetic Rescue: 2

Expression Summary
Length (a.a.) 854
Molecular Weight (Da) 98,904
Isoelectric Point (pI) 9.45
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrIV:381438 to 378874 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Genetic position: -14.93 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..2565 381438..378874 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000002198

Nat1p is part of an N-terminal acetyl transferase; it acts in a complex with Ard1p to catalyze the cotranslational N-terminal acetylation of many yeast proteins (4, 1). Three N-terminal acetyl transferases have been identified in yeast: Nat1p/Ard1p, Nat3p, and Mak3p (7). These enzymes are responsible for the N-terminal modification of more than half of yeast proteins (7). Nat1p/Ard1p transfers an acetyl group from acetyl coenzyme A to the alpha-amino group of Ser, Ala, Gly, or Thr N-terminal residues (7, 8).

Deletion of NAT1 causes slow growth, failure to enter stationary phase, and defects in sporulation (1, 8). Cells lacking Nat1p or Ard1p show derepression of silent mating type loci; overexpression of Sir1p, a silent information regulator, can suppress this derepression phenotype (1, 9). NAT1 is also a modifier of position effect at telomeres; in nat1 mutants transcriptional repression is no longer seen near telomeres 10. Overexpression or deletion of NAT1 can lead to chromosomal instability (11). These mutant phenotypes suggest that the Nat1p/Ard1p complex may modify proteins important for chromatin structure and function.

Last updated: 1999-12-31 Contact SGD

References cited on this page View Complete Literature Guide for NAT1
1) Mullen JR, et al.  (1989) Identification and characterization of genes and mutants for an N-terminal acetyltransferase from yeast. EMBO J 8(7):2067-75
2) Lee FJ, et al.  (1989) Molecular cloning and sequencing of a cDNA encoding N alpha-acetyltransferase from Saccharomyces cerevisiae. J Biol Chem 264(21):12339-43
3) Polevoda B, et al.  (2009) A synopsis of eukaryotic Nalpha-terminal acetyltransferases: nomenclature, subunits and substrates. BMC Proc 3 Suppl 6:S2
4) Park EC and Szostak JW  (1992) ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity. EMBO J 11(6):2087-93
5) Polevoda B and Sherman F  (2003) Composition and function of the eukaryotic N-terminal acetyltransferase subunits. Biochem Biophys Res Commun 308(1):1-11
6) Gautschi M, et al.  (2003) The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides. Mol Cell Biol 23(20):7403-14
7) Polevoda B, et al.  (1999) Identification and specificities of N-terminal acetyltransferases from Saccharomyces cerevisiae. EMBO J 18(21):6155-68
8) Lee FJ, et al.  (1989) N alpha acetylation is required for normal growth and mating of Saccharomyces cerevisiae. J Bacteriol 171(11):5795-802
9) Stone EM, et al.  (1991) The SIR1 gene of Saccharomyces cerevisiae and its role as an extragenic suppressor of several mating-defective mutants. Mol Cell Biol 11(4):2253-62
10) Aparicio OM, et al.  (1991) Modifiers of position effect are shared between telomeric and silent mating-type loci in S. cerevisiae. Cell 66(6):1279-87
11) Ouspenski II, et al.  (1999) New yeast genes important for chromosome integrity and segregation identified by dosage effects on genome stability. Nucleic Acids Res 27(15):3001-8