ADE13/YLR359W Summary Help

Standard Name ADE13 1
Systematic Name YLR359W
Alias BRA1 2 , BRA8 2
Feature Type ORF, Verified
Description Adenylosuccinate lyase; catalyzes two steps in the 'de novo' purine nucleotide biosynthetic pathway; expression is repressed by adenine and activated by Bas1p and Pho2p; mutations in human ortholog ADSL cause adenylosuccinase deficiency (3, 4, 5 and see Summary Paragraph)
Name Description ADEnine requiring
Chromosomal Location
ChrXII:844282 to 845730 | ORF Map | GBrowse
Gene Ontology Annotations All ADE13 GO evidence and references
  View Computational GO annotations for ADE13
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 9 genes
Classical genetics
reduction of function
Large-scale survey
reduction of function
56 total interaction(s) for 50 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 10
  • Affinity Capture-RNA: 3
  • Affinity Capture-Western: 3
  • Two-hybrid: 1

Genetic Interactions
  • Dosage Lethality: 1
  • Negative Genetic: 22
  • Positive Genetic: 10
  • Synthetic Haploinsufficiency: 1
  • Synthetic Lethality: 4
  • Synthetic Rescue: 1

Expression Summary
Length (a.a.) 482
Molecular Weight (Da) 54,510
Isoelectric Point (pI) 6.4
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXII:844282 to 845730 | ORF Map | GBrowse
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1449 844282..845730 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 SGDIDS000004351

ADE13 encodes adenylosuccinate lyase (1), which is involved in catalysis of two reactions in the purine nucleotide biosynthetic pathway: the first in the de novo pathway leading to formation of inosine monophosphate (IMP), and the second in the interconversion of IMP to adenosine monophosphate (AMP) (see pathway diagram).

Expression of ADE13 and most of the other purine biosynthetic genes is repressed by adenine and activated by transcription factors Bas1p and Pho2p (6, 3). Reduction- or loss-of-function mutations in ADE13 relieve the transcriptional repression of the ADE genes by adenine, suggesting that AMP plays a role in mediating adenine repression (2). Only the most severe ade13 mutations also cause adenine auxotrophy, indicating that low levels of Ade13p activity are sufficient for growth in the absence of adenine (2).

Ade13p is a widely conserved protein, and orthologs have been described in bacteria, chicken, and humans (2). Mutations in the human gene ADSL cause adenylosuccinase deficiency, a rare autosomal recessive disease that causes severe mental retardation, and in some cases convulsions, autism, and growth retardation (reviewed in 5).

Last updated: 2007-03-28 Contact SGD

References cited on this page View Complete Literature Guide for ADE13
1) Dorfman BZ  (1969) The isolation of adenylosuccinate synthetase mutants in yeast by selection for constitutive behavior in pigmented strains. Genetics 61(2):377-89
2) Guetsova ML, et al.  (1997) The isolation and characterization of Saccharomyces cerevisiae mutants that constitutively express purine biosynthetic genes. Genetics 147(2):383-97
3) Denis V, et al.  (1998) Role of the myb-like protein bas1p in Saccharomyces cerevisiae: a proteome analysis. Mol Microbiol 30(3):557-66
4) Jones EW and Fink GR  (1982) "Regulation of amino acid and nucleotide biosynthesis in yeast." Pp.181-299 in The Molecular Biology of the Yeast Saccharomyces: Metabolism and Gene Expression, edited by Strathern JN, Jones EW and Broach JR. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
5) Van den Berghe G, et al.  (1997) Inborn errors of the purine nucleotide cycle: adenylosuccinase deficiency. J Inherit Metab Dis 20(2):193-202
6) Daignan-Fornier B and Fink GR  (1992) Coregulation of purine and histidine biosynthesis by the transcriptional activators BAS1 and BAS2. Proc Natl Acad Sci U S A 89(15):6746-50