ARD1/YHR013C Summary Help

Standard Name ARD1 1
Systematic Name YHR013C
Alias NAA10 2
Feature Type ORF, Verified
Description Subunit of protein N-terminal acetyltransferase NatA; NatA is comprised of Nat1p, Ard1p, and Nat5p; acetylates many proteins and thus affects telomeric silencing, cell cycle, heat-shock resistance, mating, and sporulation; human Ard1p levels are elevated in cancer cells; protein abundance increases in response to DNA replication stress (3, 4, 5, 6, 7, 8 and see Summary Paragraph)
Name Description ARrest Defective 1
Chromosomal Location
ChrVIII:131446 to 130730 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Genetic position: 10 cM
Gene Ontology Annotations All ARD1 GO evidence and references
  View Computational GO annotations for ARD1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 3 genes
Classical genetics
Large-scale survey
408 total interaction(s) for 317 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 27
  • Affinity Capture-RNA: 2
  • Affinity Capture-Western: 12
  • Co-fractionation: 2

Genetic Interactions
  • Dosage Rescue: 2
  • Negative Genetic: 83
  • Phenotypic Enhancement: 1
  • Phenotypic Suppression: 1
  • Positive Genetic: 36
  • Synthetic Growth Defect: 211
  • Synthetic Haploinsufficiency: 1
  • Synthetic Lethality: 23
  • Synthetic Rescue: 7

Expression Summary
Length (a.a.) 238
Molecular Weight (Da) 27,603
Isoelectric Point (pI) 4.61
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrVIII:131446 to 130730 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Genetic position: 10 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..717 131446..130730 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 | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000001055

Ard1p is part of an N-terminal acetyl transferase; it acts in a complex with Nat1p to catalyze the cotranslational N-terminal acetylation of many yeast proteins (3,4). Three N-terminal acetyl transferases have been identified in yeast: Nat1p/Ard1p, Nat3p, and Mak3p (9). These enzymes are responsible for the N-terminal modification of more than half of yeast proteins (9). Nat1p/Ard1p transfers an acetyl group from acetyl coenzyme A to the alpha-amino group of Ser, Ala, Gly, or Thr N-terminal residues (9, 10). Because Ard1p, Nat3p, and Mak3p share significant sequence similarity, it has recently been suggested that Ard1p may be the catalytic subunit of the Nat1p/Ard1p complex (9).

Mutations in ARD1 cause slow growth, failure to enter stationary phase, and defects in sporulation (4). Cells lacking Nat1p or Ard1p show derepression of silent mating type loci; overexpression of Sir1p, a silent information regulator, can suppress this derepression phenotype (4, 11, 12). ARD1 is also a modifier of position effect at telomeres; in ard1 mutants transcriptional repression is no longer seen near telomeres (13). These mutant phenotypes suggest that the Nat1p/Ard1p complex may modify proteins important for silenced chromatin structure and function.

The human gene (TE2), whose product shows 40% identity to Ard1p, has been identified on the X chromosome .

Last updated: 2005-07-01 Contact SGD

References cited on this page View Complete Literature Guide for ARD1
1) Whiteway M and Szostak JW  (1985) The ARD1 gene of yeast functions in the switch between the mitotic cell cycle and alternative developmental pathways. Cell 43(2 Pt 1):483-92
2) Polevoda B, et al.  (2009) A synopsis of eukaryotic Nalpha-terminal acetyltransferases: nomenclature, subunits and substrates. BMC Proc 3 Suppl 6:S2
3) 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
4) 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
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) Yu M, et al.  (2009) Immunohistochemical analysis of human arrest-defective-1 expressed in cancers in vivo. Oncol Rep 21(4):909-15
8) Tkach JM, et al.  (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
9) Polevoda B, et al.  (1999) Identification and specificities of N-terminal acetyltransferases from Saccharomyces cerevisiae. EMBO J 18(21):6155-68
10) Lee FJ, et al.  (1989) N alpha acetylation is required for normal growth and mating of Saccharomyces cerevisiae. J Bacteriol 171(11):5795-802
11) 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
12) Whiteway M, et al.  (1987) The yeast ARD1 gene product is required for repression of cryptic mating-type information at the HML locus. Mol Cell Biol 7(10):3713-22
13) 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