| UniProt ID | ATO3_YEAST | |
|---|---|---|
| UniProt AC | Q12359 | |
| Protein Name | Ammonia transport outward protein 3 | |
| Gene Name | ATO3 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 275 | |
| Subcellular Localization |
Cell membrane Multi-pass membrane protein . Localizes to large detergent resistant patches of the cell membrane (DRM) enriched in ergosterol and sphingolipids. |
|
| Protein Description | Transporter protein required for ammonia export. Induced in rho(0) cells, probably to eliminate the excess ammonia that arises because of a potential defect in ammonia assimilation in those cells.. | |
| Protein Sequence | MTSSASSPQDLEKGVNTLENIETLPQQGSIAGVSQGFPNIQEIYSDRDFITLGSSTYRRRDLLNALDRGDGEEGNCAKYTPHQFANPVPLGLASFSLSCLVLSLINANVRGVTDGKWALSLFMFFGGAIELFAGLLCFVIGDTYAMTVFSSFGGFWICYGYGLTDTDNLVSGYTDPTMLNNVIGFFLAGWTVFTFLMLMCTLKSTWGLFLLLTFLDLTFLLLCIGTFIDNNNLKMAGGYFGILSSCCGWYSLYCSVVSPSNSYLAFRAHTMPNAP | |
| 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 | ------MTSSASSPQ ------CCCCCCCHH | 31.24 | 28152593 | |
| 3 | Phosphorylation | -----MTSSASSPQD -----CCCCCCCHHH | 23.70 | 19823750 | |
| 4 | Phosphorylation | ----MTSSASSPQDL ----CCCCCCCHHHH | 24.01 | 19823750 | |
| 6 | Phosphorylation | --MTSSASSPQDLEK --CCCCCCCHHHHHH | 44.49 | 19823750 | |
| 7 | Phosphorylation | -MTSSASSPQDLEKG -CCCCCCCHHHHHHH | 26.71 | 19823750 | |
| 23 | Phosphorylation | NTLENIETLPQQGSI HHHHHHHCCCCCCCC | 39.68 | 29688323 | |
| 29 | Phosphorylation | ETLPQQGSIAGVSQG HCCCCCCCCCCCCCC | 12.62 | 29734811 | |
| 34 | Phosphorylation | QGSIAGVSQGFPNIQ CCCCCCCCCCCCCHH | 24.54 | 27214570 | |
| 44 | Phosphorylation | FPNIQEIYSDRDFIT CCCHHHHHCCCCEEE | 12.08 | 29688323 | |
| 45 | Phosphorylation | PNIQEIYSDRDFITL CCHHHHHCCCCEEEC | 31.65 | 29688323 | |
| 54 | Phosphorylation | RDFITLGSSTYRRRD CCEEECCCCHHHHHH | 23.71 | 27214570 | |
| 55 | Phosphorylation | DFITLGSSTYRRRDL CEEECCCCHHHHHHH | 27.88 | 27214570 |
| 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 ATO3_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ATO3_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 ATO3_YEAST !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| KTR4_YEAST | KTR4 | physical | 16093310 | |
| FRE4_YEAST | FRE4 | physical | 16093310 | |
| TPO3_YEAST | TPO3 | physical | 16093310 | |
| RV161_YEAST | RVS161 | genetic | 20526336 | |
| CSG2_YEAST | CSG2 | genetic | 20526336 | |
| BRO1_YEAST | BRO1 | genetic | 20526336 | |
| PFD2_YEAST | GIM4 | genetic | 20526336 | |
| INP52_YEAST | INP52 | genetic | 20526336 | |
| GET1_YEAST | GET1 | genetic | 20526336 | |
| ATO3_YEAST | ATO3 | physical | 22579979 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-4 AND SER-6, ANDMASS SPECTROMETRY. | |
| "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; SER-4; SER-6 ANDSER-7, AND MASS SPECTROMETRY. | |
| "Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae."; Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.; Nat. Biotechnol. 20:301-305(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-6 AND SER-7, ANDMASS SPECTROMETRY. | |
