ATP1/YBL099W Summary Help

Standard Name ATP1
Systematic Name YBL099W
Feature Type ORF, Verified
Description Alpha subunit of the F1 sector of mitochondrial F1F0 ATP synthase; which is a large, evolutionarily conserved enzyme complex required for ATP synthesis; F1 translationally regulates ATP6 and ATP8 expression to achieve a balanced output of ATP synthase genes encoded in nucleus and mitochondria; phosphorylated; N-terminally propionylated in vivo (1, 2, 3, 4 and see Summary Paragraph)
Name Description ATP synthase
Chromosomal Location
ChrII:37053 to 38690 | ORF Map | GBrowse
Gene Ontology Annotations All ATP1 GO evidence and references
  View Computational GO annotations for ATP1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 4 genes
Classical genetics
gain of function
Large-scale survey
122 total interaction(s) for 93 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 41
  • Affinity Capture-RNA: 3
  • Affinity Capture-Western: 8
  • Co-fractionation: 1
  • Co-purification: 6
  • Reconstituted Complex: 1
  • Two-hybrid: 1

Genetic Interactions
  • Dosage Rescue: 2
  • Negative Genetic: 24
  • Phenotypic Suppression: 1
  • Positive Genetic: 15
  • Synthetic Growth Defect: 7
  • Synthetic Lethality: 9
  • Synthetic Rescue: 3

Expression Summary
Length (a.a.) 545
Molecular Weight (Da) 58,608
Isoelectric Point (pI) 9.5
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrII:37053 to 38690 | ORF Map | GBrowse
Last Update Coordinates: 2011-02-03 | Sequence: 2011-02-03
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1638 37053..38690 2011-02-03 2011-02-03
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 SGDIDS000000195

ATP1 encodes the alpha subunit of mitochondrial ATP synthase (1). The ATP synthase complex utilizes proton motive force to generate ATP from ADP and Pi (5). The structure of this enzyme complex is highly conserved among diverse organisms and consists of two major components, soluble F1 and membrane-bound F0, each of which contains many subunits (6). The catalytic core of the enzyme resides in the F1 component and consists of a hexamer of alternating alpha and beta (Atp2p) subunits(7, 8). These three alpha-beta dimers each provide one of ATP synthase's three catalytic sites. Both alpha and beta subunits are thought to contribute to nucleotide binding and catalysis (5).

Although ATP1 is essential for ATP synthase function, it is not essential for life in yeast. Deletion of ATP1, like deletions in many genes necessary for the function or maintenance of mitochondria, leads to a "petite" phenotype that is slow-growing and unable to survive on nonfermentable carbon sources (1).

General ATP synthase structure and function are reviewed in references 5 and 9. For a review that is specific to yeast, see reference 6.

Last updated: 2000-12-28 Contact SGD

References cited on this page View Complete Literature Guide for ATP1
1) Takeda M, et al.  (1986) Nuclear genes encoding the yeast mitochondrial ATPase complex. Analysis of ATP1 coding the F1-ATPase alpha-subunit and its assembly. J Biol Chem 261(32):15126-33
2) Reinders J, et al.  (2007) Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase. Mol Cell Proteomics 6(11):1896-906
3) Rak M and Tzagoloff A  (2009) F1-dependent translation of mitochondrially encoded Atp6p and Atp8p subunits of yeast ATP synthase. Proc Natl Acad Sci U S A 106(44):18509-14
4) Foyn H, et al.  (2013) Protein N-terminal acetyltransferases act as N-terminal propionyltransferases in vitro and in vivo. Mol Cell Proteomics 12(1):42-54
5) Boyer PD  (1997) The ATP synthase--a splendid molecular machine. Annu Rev Biochem 66:717-49
6) Devenish RJ, et al.  (2000) Insights into ATP synthase assembly and function through the molecular genetic manipulation of subunits of the yeast mitochondrial enzyme complex. Biochim Biophys Acta 1458(2-3):428-42
7) Abrahams JP, et al.  (1993) Inherent asymmetry of the structure of F1-ATPase from bovine heart mitochondria at 6.5 A resolution. EMBO J 12(5):1775-80
8) Abrahams JP, et al.  (1994) Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria. Nature 370(6491):621-8
9) Nakamoto RK, et al.  (1999) Rotational coupling in the F0F1 ATP synthase. Annu Rev Biophys Biomol Struct 28():205-34