ATP15/YPL271W Summary Help

Standard Name ATP15
Systematic Name YPL271W
Feature Type ORF, Verified
Description Epsilon 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 (1, 2, 3 and see Summary Paragraph)
Also known as: ATPEPSILON
Name Description ATP synthase
Chromosomal Location
ChrXVI:30079 to 30267 | ORF Map | GBrowse
Gene Ontology Annotations All ATP15 GO evidence and references
  View Computational GO annotations for ATP15
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 4 genes
Classical genetics
Large-scale survey
66 total interaction(s) for 58 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 9
  • Affinity Capture-RNA: 3
  • Co-purification: 5
  • Reconstituted Complex: 1

Genetic Interactions
  • Dosage Lethality: 1
  • Positive Genetic: 44
  • Synthetic Lethality: 3

Expression Summary
Length (a.a.) 62
Molecular Weight (Da) 6,743
Isoelectric Point (pI) 10.64
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXVI:30079 to 30267 | ORF Map | GBrowse
Last Update Coordinates: 1996-07-31 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..189 30079..30267 1996-07-31 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 SGDIDS000006192

ATP15 encodes the epsilon subunit of mitochondrial ATP synthase (1). The ATP synthase complex utilizes proton motive force to generate ATP from ADP and Pi (4). 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. F1 and F0 are connected, both functionally and physically, via two additional multi-subunit structures, the central stalk and the stator stalk. The epsilon subunit is a component of the central stalk, which, like a rotor shaft, transmits the movement of the F0 proton pump to the catalytic core of F1. Unlike many ATP synthase subunits, the mitochondrial epsilon subunit does not have a bacterial homolog. The bacterial subunit named "epsilon" is homologous to mitochondrial "delta" (Atp16p) (4 and 5 and references therein).

Although ATP15 is essential for ATP synthase function, it is not essential for life in yeast. Deletion of ATP15, 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 4 and 5. For a review that is specific to yeast, see reference 6).

Last updated: 2001-01-16 Contact SGD

References cited on this page View Complete Literature Guide for ATP15
1) Guelin E, et al.  (1993) ATP synthase of yeast mitochondria. Isolation and disruption of the ATP epsilon gene. J Biol Chem 268(1):161-7
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) Boyer PD  (1997) The ATP synthase--a splendid molecular machine. Annu Rev Biochem 66:717-49
5) Nakamoto RK, et al.  (1999) Rotational coupling in the F0F1 ATP synthase. Annu Rev Biophys Biomol Struct 28():205-34
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