UniProt ID | ADY2_YEAST | |
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UniProt AC | P25613 | |
Protein Name | Accumulation of dyads protein 2 | |
Gene Name | ADY2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 283 | |
Subcellular Localization |
Cell membrane Multi-pass membrane protein . Vacuole membrane Multi-pass membrane protein . Localizes to large detergent resistant patches of the cell membrane (DRM) enriched in ergosterol and sphingolipids (PubMed:17395151). |
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Protein Description | Transporter protein required for ammonia export and acetate uptake and resistance. Necessary for up-regulation and down-regulation of meiotic plaque (MP) component levels in a dependency on external acetate. Has a role in ascus formation.. | |
Protein Sequence | MSDKEQTSGNTDLENAPAGYYSSHDNDVNGVAEDERPSHDSLGKIYTGGDNNEYIYIGRQKFLKSDLYQAFGGTLNPGLAPAPVHKFANPAPLGLSAFALTTFVLSMFNARAQGITVPNVVVGCAMFYGGLVQLIAGIWEIALENTFGGTALCSYGGFWLSFAAIYIPWFGILEAYEDNESDLNNALGFYLLGWAIFTFGLTVCTMKSTVMFFLLFFLLALTFLLLSIGHFANRLGVTRAGGVLGVVVAFIAWYNAYAGVATKQNSYVLARPFPLPSTERVIF | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSDKEQTSG ------CCHHHCCCC | 58.34 | 30377154 | |
7 | Phosphorylation | -MSDKEQTSGNTDLE -CCHHHCCCCCCCCC | 39.43 | 29136822 | |
8 | Phosphorylation | MSDKEQTSGNTDLEN CCHHHCCCCCCCCCC | 29.73 | 29136822 | |
11 | Phosphorylation | KEQTSGNTDLENAPA HHCCCCCCCCCCCCC | 45.55 | 29136822 | |
20 | Phosphorylation | LENAPAGYYSSHDND CCCCCCCCCCCCCCC | 11.41 | 29136822 | |
21 | Phosphorylation | ENAPAGYYSSHDNDV CCCCCCCCCCCCCCC | 11.63 | 29136822 | |
22 | Phosphorylation | NAPAGYYSSHDNDVN CCCCCCCCCCCCCCC | 16.83 | 27214570 | |
23 | Phosphorylation | APAGYYSSHDNDVNG CCCCCCCCCCCCCCC | 20.81 | 29136822 | |
38 | Phosphorylation | VAEDERPSHDSLGKI CCCCCCCCCCCCCCE | 46.26 | 27214570 | |
41 | Phosphorylation | DERPSHDSLGKIYTG CCCCCCCCCCCEECC | 33.33 | 27214570 | |
46 | Phosphorylation | HDSLGKIYTGGDNNE CCCCCCEECCCCCCC | 11.65 | 27214570 | |
47 | Phosphorylation | DSLGKIYTGGDNNEY CCCCCEECCCCCCCE | 37.86 | 25005228 | |
65 | Phosphorylation | GRQKFLKSDLYQAFG CCHHHHCCCHHHHHC | 34.69 | 27214570 | |
277 | Phosphorylation | ARPFPLPSTERVIF- EECCCCCCCCCCCC- | 51.05 | 27214570 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of ADY2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of ADY2_YEAST !! |
* 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 ADY2_YEAST !! |
Kegg Drug | ||||||
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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 THR-47, AND MASSSPECTROMETRY. |