| UniProt ID | NHX1_YEAST | |
|---|---|---|
| UniProt AC | Q04121 | |
| Protein Name | Endosomal/prevacuolar sodium/hydrogen exchanger | |
| Gene Name | NHX1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 633 | |
| Subcellular Localization |
Endosome membrane Multi-pass membrane protein. Prevacuolar compartment membrane Multi-pass membrane protein. |
|
| Protein Description | Endosomal/prevacuolar electroneutral Na(+)/H(+) exchanger which mediates intracellular sequestration of Na(+) cations, regulates vacuolar pH and contributes to osmotolerance following sudden exposure to hyperosmotic media. Contributes also to the postdiauxic/stationary phase resistance to osmotic stress and allows for the continued growth of cells until the acquired osmotolerance response can occur. Involved in hygromycin resistance probably through its influence on the electrochemical proton gradient affecting secondarily the entrance of hygromycin. Mediates pH-dependent vesicle trafficking out of the endosome. Contributes to K(+) sequestration and homeostasis.. | |
| Protein Sequence | MLSKVLLNIAFKVLLTTAKRAVDPDDDDELLPSPDLPGSDDPIAGDPDVDLNPVTEEMFSSWALFIMLLLLISALWSSYYLTQKRIRAVHETVLSIFYGMVIGLIIRMSPGHYIQDTVTFNSSYFFNVLLPPIILNSGYELNQVNFFNNMLSILIFAIPGTFISAVVIGIILYIWTFLGLESIDISFADAMSVGATLSATDPVTILSIFNAYKVDPKLYTIIFGESLLNDAISIVMFETCQKFHGQPATFSSVFEGAGLFLMTFSVSLLIGVLIGILVALLLKHTHIRRYPQIESCLILLIAYESYFFSNGCHMSGIVSLLFCGITLKHYAYYNMSRRSQITIKYIFQLLARLSENFIFIYLGLELFTEVELVYKPLLIIVAAISICVARWCAVFPLSQFVNWIYRVKTIRSMSGITGENISVPDEIPYNYQMMTFWAGLRGAVGVALALGIQGEYKFTLLATVLVVVVLTVIIFGGTTAGMLEVLNIKTGCISEEDTSDDEFDIEAPRAINLLNGSSIQTDLGPYSDNNSPDISIDQFAVSSNKNLPNNISTTGGNTFGGLNETENTSPNPARSSMDKRNLRDKLGTIFNSDSQWFQNFDEQVLKPVFLDNVSPSLQDSATQSPADFSSQNH | |
| 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 |
|---|---|---|---|---|---|
| 417 | Phosphorylation | IRSMSGITGENISVP HHHHCCCCCCCCCCC | 41.80 | 30377154 | |
| 420 | N-linked_Glycosylation | MSGITGENISVPDEI HCCCCCCCCCCCCCC | 32.93 | - | |
| 429 | Phosphorylation | SVPDEIPYNYQMMTF CCCCCCCCCHHHHHH | 31.96 | 30377154 | |
| 431 | Phosphorylation | PDEIPYNYQMMTFWA CCCCCCCHHHHHHHH | 7.61 | 30377154 | |
| 435 | Phosphorylation | PYNYQMMTFWAGLRG CCCHHHHHHHHHHHH | 15.64 | 30377154 | |
| 490 | Phosphorylation | LEVLNIKTGCISEED HHHHCCCCCCCCCCC | 33.23 | 22369663 | |
| 494 | Phosphorylation | NIKTGCISEEDTSDD CCCCCCCCCCCCCCC | 38.72 | 22369663 | |
| 498 | Phosphorylation | GCISEEDTSDDEFDI CCCCCCCCCCCCCCC | 37.02 | 22369663 | |
| 499 | Phosphorylation | CISEEDTSDDEFDIE CCCCCCCCCCCCCCC | 56.22 | 22369663 | |
| 515 | N-linked_Glycosylation | PRAINLLNGSSIQTD HHHHHCCCCCCCCCC | 52.01 | 11036065 | |
| 531 | Phosphorylation | GPYSDNNSPDISIDQ CCCCCCCCCCCCHHH | 30.15 | 28889911 | |
| 550 | N-linked_Glycosylation | SNKNLPNNISTTGGN CCCCCCCCCEECCCC | 27.87 | 11036065 | |
| 552 | Phosphorylation | KNLPNNISTTGGNTF CCCCCCCEECCCCCC | 23.26 | 22369663 | |
| 553 | Phosphorylation | NLPNNISTTGGNTFG CCCCCCEECCCCCCC | 26.18 | 21440633 | |
| 554 | Phosphorylation | LPNNISTTGGNTFGG CCCCCEECCCCCCCC | 35.98 | 20377248 | |
| 558 | Phosphorylation | ISTTGGNTFGGLNET CEECCCCCCCCCCCC | 27.25 | 25521595 | |
| 563 | N-linked_Glycosylation | GNTFGGLNETENTSP CCCCCCCCCCCCCCC | 58.37 | 11036065 | |
| 565 | Phosphorylation | TFGGLNETENTSPNP CCCCCCCCCCCCCCC | 33.20 | 22369663 | |
| 568 | Phosphorylation | GLNETENTSPNPARS CCCCCCCCCCCCCCC | 39.05 | 20377248 | |
| 569 | Phosphorylation | LNETENTSPNPARSS CCCCCCCCCCCCCCC | 33.97 | 22369663 | |
| 575 | Phosphorylation | TSPNPARSSMDKRNL CCCCCCCCCCCCCCH | 31.92 | 22369663 | |
| 576 | Phosphorylation | SPNPARSSMDKRNLR CCCCCCCCCCCCCHH | 26.00 | 25521595 | |
| 614 | Phosphorylation | PVFLDNVSPSLQDSA HHHHHCCCHHHCCCC | 18.28 | 28889911 | |
| 616 | Phosphorylation | FLDNVSPSLQDSATQ HHHCCCHHHCCCCCC | 31.02 | 28889911 | |
| 624 | Phosphorylation | LQDSATQSPADFSSQ HCCCCCCCCCHHCCC | 20.08 | 21551504 |
| 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 NHX1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NHX1_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 NHX1_YEAST !! | ||||||
| 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-499; SER-531; THR-554;SER-569; SER-614 AND SER-616, AND MASS SPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, AND MASSSPECTROMETRY. | |
