| Standard Name | ATP20 (see Nomenclature conflict Note) |
|---|---|
| Systematic Name | YPR020W |
| Feature Type | ORF, Verified |
| Description | Subunit g of the mitochondrial F1F0 ATP synthase; reversibly phosphorylated on two residues; unphosphorylated form is required for dimerization of the ATP synthase complex, which in turn determines oligomerization of the complex and the shape of inner membrane cristae (1, 2, 3 and see Summary Paragraph) |
| Name Description | ATP synthase |
| Chromosomal Location | |
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| View Computational GO annotations for ATP20 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated | |
| High-throughput |
| Classical genetics | |
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| null | |
| repressible | |
| Large-scale survey | |
| null | |
| overexpression | |
| Resources |
| 61 total interaction(s) for 45 unique genes/features. | |
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| Resources |
| Localization | |
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| Phosphorylation | PhosphoGRID | PhosphoPep Database |
| Structure | |
| Homologs |
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| Last Update | Coordinates: 2011-02-03 | Sequence: 1996-07-31 | ||||||||||||
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| S288C only | |
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| 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 |
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| Primary SGDID | S000006224 |
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NOMENCLATURE CONFLICT NOTE
| Name | Relevance | Description |
|---|---|---|
| ATP19 | Nomenclature conflict | Both ATP19/YOL077W-A, subunit k of mitochondrial ATP synthase, and ATP20/YPR020W, subunit g of mitochondrial ATP synthase, have been referred to as ATP19. |
ATP20 encodes subunit g of mitochondrial ATP synthase (4). 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). Subunit g, like subunit e (Tim11p), is not essential for the basic function or assembly of the F1/F0 ATP synthase complex, but is required for complex dimerization and maximal enzyme stability. Deletion of ATP20 reduces the mitochondrial concentration of ATP synthase, but does not alter enzyme activity (1).
General ATP synthase structure and function are reviewed in references 5 and 7. For a review that is specific to yeast, see reference 6.
| 1) | Arnold I, et al. (1998) Yeast mitochondrial F1F0-ATP synthase exists as a dimer: identification of three dimer-specific subunits. EMBO J 17(24):7170-8 |
| 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) | Davies KM, et al. (2012) Structure of the yeast F1Fo-ATP synthase dimer and its role in shaping the mitochondrial cristae. Proc Natl Acad Sci U S A 109(34):13602-7 |
| 4) | Boyle GM, et al. (1999) Identification of subunit g of yeast mitochondrial F1F0-ATP synthase, a protein required for maximal activity of cytochrome c oxidase. Eur J Biochem 262(2):315-23 |
| 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) | Nakamoto RK, et al. (1999) Rotational coupling in the F0F1 ATP synthase. Annu Rev Biophys Biomol Struct 28:205-34 |





