| UniProt ID | G6PD_YEAST | |
|---|---|---|
| UniProt AC | P11412 | |
| Protein Name | Glucose-6-phosphate 1-dehydrogenase | |
| Gene Name | ZWF1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 505 | |
| Subcellular Localization | ||
| Protein Description | Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis (By similarity).. | |
| Protein Sequence | MSEGPVKFEKNTVISVFGASGDLAKKKTFPALFGLFREGYLDPSTKIFGYARSKLSMEEDLKSRVLPHLKKPHGEADDSKVEQFFKMVSYISGNYDTDEGFDELRTQIEKFEKSANVDVPHRLFYLALPPSVFLTVAKQIKSRVYAENGITRVIVEKPFGHDLASARELQKNLGPLFKEEELYRIDHYLGKELVKNLLVLRFGNQFLNASWNRDNIQSVQISFKERFGTEGRGGYFDSIGIIRDVMQNHLLQIMTLLTMERPVSFDPESIRDEKVKVLKAVAPIDTDDVLLGQYGKSEDGSKPAYVDDDTVDKDSKCVTFAAMTFNIENERWEGVPIMMRAGKALNESKVEIRLQYKAVASGVFKDIPNNELVIRVQPDAAVYLKFNAKTPGLSNATQVTDLNLTYASRYQDFWIPEAYEVLIRDALLGDHSNFVRDDELDISWGIFTPLLKHIERPDGPTPEIYPYGSRGPKGLKEYMQKHKYVMPEKHPYAWPVTKPEDTKDN | |
| 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 | Acetylation | ------MSEGPVKFE ------CCCCCCCCC | 51.79 | 2040308 | |
| 15 | Phosphorylation | FEKNTVISVFGASGD CCCCEEEEEEECCCH | 13.68 | 24961812 | |
| 20 | Phosphorylation | VISVFGASGDLAKKK EEEEEECCCHHHHCC | 32.97 | 24961812 | |
| 25 | Acetylation | GASGDLAKKKTFPAL ECCCHHHHCCHHHHH | 63.20 | 24489116 | |
| 26 | Acetylation | ASGDLAKKKTFPALF CCCHHHHCCHHHHHH | 51.98 | 24489116 | |
| 27 | Acetylation | SGDLAKKKTFPALFG CCHHHHCCHHHHHHH | 55.48 | 24489116 | |
| 46 | Ubiquitination | GYLDPSTKIFGYARS CCCCCCHHHHHHHHH | 40.13 | 24961812 | |
| 54 | Acetylation | IFGYARSKLSMEEDL HHHHHHHCCCCCHHH | 38.74 | 24489116 | |
| 62 | Succinylation | LSMEEDLKSRVLPHL CCCCHHHHHCCHHHC | 48.84 | 23954790 | |
| 80 | Acetylation | HGEADDSKVEQFFKM CCCCCHHHHHHHHHH | 57.70 | 24489116 | |
| 110 | Acetylation | ELRTQIEKFEKSANV HHHHHHHHHHHHCCC | 61.52 | 22865919 | |
| 113 | Acetylation | TQIEKFEKSANVDVP HHHHHHHHHCCCCCC | 58.98 | 24489116 | |
| 113 | Ubiquitination | TQIEKFEKSANVDVP HHHHHHHHHCCCCCC | 58.98 | 17644757 | |
| 125 | Phosphorylation | DVPHRLFYLALPPSV CCCCHHHHHHCCHHH | 8.82 | 22369663 | |
| 131 | Phosphorylation | FYLALPPSVFLTVAK HHHHCCHHHHHHHHH | 24.46 | 22369663 | |
| 135 | Phosphorylation | LPPSVFLTVAKQIKS CCHHHHHHHHHHHHH | 13.62 | 22369663 | |
| 141 | Ubiquitination | LTVAKQIKSRVYAEN HHHHHHHHHHHHHHC | 29.71 | 17644757 | |
| 142 | Phosphorylation | TVAKQIKSRVYAENG HHHHHHHHHHHHHCC | 28.71 | 17330950 | |
| 145 | Phosphorylation | KQIKSRVYAENGITR HHHHHHHHHHCCCEE | 13.69 | 17330950 | |
| 157 | Ubiquitination | ITRVIVEKPFGHDLA CEEEEEECCCCCCHH | 34.45 | 23749301 | |
| 157 | Acetylation | ITRVIVEKPFGHDLA CEEEEEECCCCCCHH | 34.45 | 24489116 | |
| 171 | Acetylation | ASARELQKNLGPLFK HHHHHHHHHHHHCCC | 67.76 | 24489116 | |
| 178 | Acetylation | KNLGPLFKEEELYRI HHHHHCCCHHHHHHH | 72.41 | 24489116 | |
| 191 | Acetylation | RIDHYLGKELVKNLL HHHHHCCHHHHHHHH | 45.33 | 24489116 | |
| 195 | Ubiquitination | YLGKELVKNLLVLRF HCCHHHHHHHHHHHC | 55.28 | 24961812 | |
| 224 | Acetylation | QSVQISFKERFGTEG EEEEEEEHHHHCCCC | 40.98 | 24489116 | |
| 238 | Phosphorylation | GRGGYFDSIGIIRDV CCCCCHHHHHHHHHH | 16.89 | 28889911 | |
| 297 | Phosphorylation | LLGQYGKSEDGSKPA EECCCCCCCCCCCCC | 36.24 | 22369663 | |
| 301 | Phosphorylation | YGKSEDGSKPAYVDD CCCCCCCCCCCCCCC | 48.03 | 22369663 | |
| 349 | Ubiquitination | GKALNESKVEIRLQY CHHCCCCCCEEEEEH | 37.39 | 23749301 | |
| 349 | Acetylation | GKALNESKVEIRLQY CHHCCCCCCEEEEEH | 37.39 | 24489116 | |
| 365 | Acetylation | AVASGVFKDIPNNEL HHHCCCCCCCCCCCE | 52.95 | 24489116 | |
| 365 | Ubiquitination | AVASGVFKDIPNNEL HHHCCCCCCCCCCCE | 52.95 | 24961812 | |
| 385 | Acetylation | PDAAVYLKFNAKTPG CCCEEEEEEECCCCC | 20.91 | 24489116 | |
| 389 | Ubiquitination | VYLKFNAKTPGLSNA EEEEEECCCCCCCCC | 57.25 | 23749301 | |
| 390 | Phosphorylation | YLKFNAKTPGLSNAT EEEEECCCCCCCCCE | 21.85 | 27017623 | |
| 394 | Phosphorylation | NAKTPGLSNATQVTD ECCCCCCCCCEEEEE | 30.27 | 27017623 | |
| 461 | Phosphorylation | IERPDGPTPEIYPYG CCCCCCCCCCCCCCC | 38.80 | 24961812 | |
| 484 | Phosphorylation | EYMQKHKYVMPEKHP HHHHHCCCCCCCCCC | 11.16 | 28889911 | |
| 489 | Acetylation | HKYVMPEKHPYAWPV CCCCCCCCCCCCCCC | 43.97 | 24489116 | |
| 492 | Phosphorylation | VMPEKHPYAWPVTKP CCCCCCCCCCCCCCC | 22.48 | 28889911 | |
| 498 | Acetylation | PYAWPVTKPEDTKDN CCCCCCCCCCCCCCC | 46.79 | 24489116 | |
| 503 | Acetylation | VTKPEDTKDN----- CCCCCCCCCC----- | 68.54 | 24489116 |
| 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 G6PD_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of G6PD_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 G6PD_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Functionally important regions of glucose-6-phosphate dehydrogenasedefined by the Saccharomyces cerevisiae enzyme and its differencesfrom the mammalian and insect forms."; Persson B., Joernvall H., Wood I., Jeffery J.; Eur. J. Biochem. 198:485-491(1991). Cited for: PROTEIN SEQUENCE OF 2-505. | |
| Phosphorylation | |
| Reference | PubMed |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142 AND TYR-145, ANDMASS SPECTROMETRY. | |
