| UniProt ID | ATPN_YEAST | |
|---|---|---|
| UniProt AC | Q12233 | |
| Protein Name | ATP synthase subunit g, mitochondrial | |
| Gene Name | ATP20 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 115 | |
| Subcellular Localization | Mitochondrion membrane. | |
| Protein Description | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane.. | |
| Protein Sequence | MLSRIQNYTSGLVSKANLLSSKALYYGKVGAEISKQIYLKEGLQPPTVAQFKSVYSNLYKQSLNFALKPTEVLSCLKNIQKNELLKYGAYGIQLIGFYSVGEIIGRRKLVGYKHH | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MLSRIQNY -------CCHHHHHH | 7.47 | 17761666 | |
| 3 | Phosphorylation | -----MLSRIQNYTS -----CCHHHHHHHH | 26.49 | 28889911 | |
| 14 | Phosphorylation | NYTSGLVSKANLLSS HHHHHHHHHHHHHCC | 30.97 | 27214570 | |
| 40 | Acetylation | ISKQIYLKEGLQPPT HHCHHHHCCCCCCCC | 32.53 | 24489116 | |
| 62 | Phosphorylation | YSNLYKQSLNFALKP HHHHHHHHHCCCCCH | 22.56 | 28889911 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of ATPN_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 62 | S | Phosphorylation |
| 17761666 |
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of ATPN_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Profiling phosphoproteins of yeast mitochondria reveals a role ofphosphorylation in assembly of the ATP synthase."; Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.; Mol. Cell. Proteomics 6:1896-1906(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-62,MUTAGENESIS OF SER-62, AND MASS SPECTROMETRY. | |
