ACC1/YNR016C Summary Help

Standard Name ACC1 1
Systematic Name YNR016C
Alias ABP2 , FAS3 , MTR7 2
Feature Type ORF, Verified
Description Acetyl-CoA carboxylase, biotin containing enzyme; catalyzes carboxylation of cytosolic acetyl-CoA to form malonyl-CoA and regulates histone acetylation by regulating the availablity of acetyl-CoA; required for de novo biosynthesis of long-chain fatty acids; ACC1 has a paralog, HFA1, that arose from the whole genome duplication (1, 3, 4, 5 and see Summary Paragraph)
Name Description Acetyl-CoA Carboxylase 1
Chromosomal Location
ChrXIV:661374 to 654673 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gene Ontology Annotations All ACC1 GO evidence and references
  View Computational GO annotations for ACC1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 4 genes
Classical genetics
reduction of function
Large-scale survey
reduction of function
85 total interaction(s) for 72 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 47
  • Affinity Capture-RNA: 6
  • Co-crystal Structure: 1
  • Two-hybrid: 10

Genetic Interactions
  • Negative Genetic: 8
  • Phenotypic Suppression: 1
  • Positive Genetic: 7
  • Synthetic Growth Defect: 1
  • Synthetic Lethality: 1
  • Synthetic Rescue: 3

Expression Summary
Length (a.a.) 2,233
Molecular Weight (Da) 250,351
Isoelectric Point (pI) 6.22
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXIV:661374 to 654673 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Last Update Coordinates: 2011-02-03 | Sequence: 1997-01-28
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..6702 661374..654673 2011-02-03 1997-01-28
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 SGDIDS000005299

ACC1 encodes acetyl-CoA carboxylase (6, 7), a biotin-containing enzyme that catalyzes the first step in de novo fatty acid biosynthesis (8). Acc1p is essential (3); a mutant allele of ACC1 called mtr7 is defective in mRNA export from the nucleus, and shows altered nuclear envelope morphology (9). The mtr7 allele and a cold-sensitive acc1 allele are both synthetically lethal with an hpr1 null mutant; the hpr1 single mutant has a hyperrecombination phenotype. The acc1 hpr1 double mutant phenotype may reflect changes in nucleocytoplasmic transport or the structure of the nucleolus (8). Transcription of ACC1 is repressed in the presence of the phospholipid precursors inositol and choline, and is regulated by the transcription factors Ino2p, and Ino4p, and the negative regualtor Opi1p (3, 10). Enzymes with similar amino acid sequences have been identified in chicken and rat (7).

Last updated: 1999-11-02 Contact SGD

References cited on this page View Complete Literature Guide for ACC1
1) Roggenkamp R, et al.  (1980) Fatty acid-requiring mutant of Saccharomyces cerevisiae defective in acetyl-CoA carboxylase. Proc Natl Acad Sci U S A 77(4):1814-7
2) Kadowaki T, et al.  (1994) Isolation and characterization of Saccharomyces cerevisiae mRNA transport-defective (mtr) mutants. J Cell Biol 126(3):649-59
3) Hasslacher M, et al.  (1993) Acetyl-CoA carboxylase from yeast is an essential enzyme and is regulated by factors that control phospholipid metabolism. J Biol Chem 268(15):10946-52
4) Byrne KP and Wolfe KH  (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61
5) Galdieri L and Vancura A  (2012) Acetyl-CoA carboxylase regulates global histone acetylation. J Biol Chem 287(28):23865-76
6) Mishina M, et al.  (1980) Yeast mutants defective in acetyl-coenzyme A carboxylase and biotin: apocarboxylase ligase. Eur J Biochem 111(1):79-87
7) Al-Feel W, et al.  (1992) Cloning of the yeast FAS3 gene and primary structure of yeast acetyl-CoA carboxylase. Proc Natl Acad Sci U S A 89(10):4534-8
8) Schneiter R, et al.  (1999) The Saccharomyces cerevisiae hyperrecombination mutant hpr1Delta is synthetically lethal with two conditional alleles of the acetyl coenzyme A carboxylase gene and causes a defect in nuclear export of polyadenylated RNA. Mol Cell Biol 19(5):3415-22
9) Fabre E and Hurt E  (1997) Yeast genetics to dissect the nuclear pore complex and nucleocytoplasmic trafficking. Annu Rev Genet 31:277-313
10) Chirala SS, et al.  (1994) Analysis of FAS3/ACC regulatory region of Saccharomyces cerevisiae: identification of a functional UASINO and sequences responsible for fatty acid mediated repression. Nucleic Acids Res 22(3):412-8