| UniProt ID | DHE2_YEAST | |
|---|---|---|
| UniProt AC | P33327 | |
| Protein Name | NAD-specific glutamate dehydrogenase | |
| Gene Name | GDH2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1092 | |
| Subcellular Localization | ||
| Protein Description | NAD(+)-dependent glutamate dehydrogenase which degrades glutamate to ammonia and alpha-ketoglutarate.. | |
| Protein Sequence | MLFDNKNRGALNSLNTPDIASLSISSMSDYHVFDFPGKDLQREEVIDLLDQQGFIPDDLIEQEVDWFYNSLGIDDLFFSRESPQLISNIIHSLYASKLDFFAKSKFNGIQPRLFSIKNKIITNDNHAIFMESNTGVSISDSQQKNFKFASDAVGNDTLEHGKDTIKKNRIEMDDSCPPYELDSEIDDLFLDNKSQKNCRLVSFWAPESELKLTFVYESVYPNDDPAGVDISSQDLLKGDIESISDKTMYKVSSNENKKLYGLLLKLVKEREGPVIKTTRSVENKDEIRLLVAYKRFTTKRYYSALNSLFHYYKLKPSKFYLESFNVKDDDIIIFSVYLNENQQLEDVLLHDVEAALKQVEREASLLYAIPNNSFHEVYQRRQFSPKEAIYAHIGAIFINHFVNRLGSDYQNLLSQITIKRNDTTLLEIVENLKRKLRNETLTQQTIINIMSKHYTIISKLYKNFAQIHYYHNSTKDMEKTLSFQRLEKVEPFKNDQEFEAYLNKFIPNDSPDLLILKTLNIFNKSILKTNFFITRKVAISFRLDPSLVMTKFEYPETPYGIFFVVGNTFKGFHIRFRDIARGGIRIVCSRNQDIYDLNSKNVIDENYQLASTQQRKNKDIPEGGSKGVILLNPGLVEHDQTFVAFSQYVDAMIDILINDPLKENYVNLLPKEEILFFGPDEGTAGFVDWATNHARVRNCPWWKSFLTGKSPSLGGIPHDEYGMTSLGVRAYVNKIYETLNLTNSTVYKFQTGGPDGDLGSNEILLSSPNECYLAILDGSGVLCDPKGLDKDELCRLAHERKMISDFDTSKLSNNGFFVSVDAMDIMLPNGTIVANGTTFRNTFHTQIFKFVDHVDIFVPCGGRPNSITLNNLHYFVDEKTGKCKIPYIVEGANLFITQPAKNALEEHGCILFKDASANKGGVTSSSMEVLASLALNDNDFVHKFIGDVSGERSALYKSYVVEVQSRIQKNAELEFGQLWNLNQLNGTHISEISNQLSFTINKLNDDLVASQELWLNDLKLRNYLLLDKIIPKILIDVAGPQSVLENIPESYLKVLLSSYLSSTFVYQNGIDVNIGKFLEFIGGLKREAEASA | |
| 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 |
|---|---|---|---|---|---|
| 13 | Phosphorylation | KNRGALNSLNTPDIA CCCCCHHCCCCCCCE | 24.68 | 22369663 | |
| 16 | Phosphorylation | GALNSLNTPDIASLS CCHHCCCCCCCEEEE | 27.86 | 22369663 | |
| 21 | Phosphorylation | LNTPDIASLSISSMS CCCCCCEEEEEHHCC | 24.00 | 22369663 | |
| 23 | Phosphorylation | TPDIASLSISSMSDY CCCCEEEEEHHCCCC | 20.23 | 22369663 | |
| 25 | Phosphorylation | DIASLSISSMSDYHV CCEEEEEHHCCCCEE | 19.33 | 22369663 | |
| 26 | Phosphorylation | IASLSISSMSDYHVF CEEEEEHHCCCCEEE | 22.19 | 22369663 | |
| 28 | Phosphorylation | SLSISSMSDYHVFDF EEEEHHCCCCEEECC | 36.64 | 22369663 | |
| 30 | Phosphorylation | SISSMSDYHVFDFPG EEHHCCCCEEECCCC | 7.80 | 25371407 | |
| 157 | Phosphorylation | SDAVGNDTLEHGKDT CCCCCCCCHHCCCCC | 37.74 | 25371407 | |
| 162 | Acetylation | NDTLEHGKDTIKKNR CCCHHCCCCCHHHCC | 54.31 | 25381059 | |
| 242 | Phosphorylation | LLKGDIESISDKTMY HHCCCHHHCCCCEEE | 27.94 | 27214570 | |
| 276 | Acetylation | EREGPVIKTTRSVEN HCCCCEEEEECCCCC | 44.04 | 25381059 | |
| 480 | Phosphorylation | STKDMEKTLSFQRLE CCCCHHHHHHHHHHH | 17.83 | 22369663 | |
| 482 | Phosphorylation | KDMEKTLSFQRLEKV CCHHHHHHHHHHHCC | 25.27 | 22369663 | |
| 546 | Phosphorylation | ISFRLDPSLVMTKFE EEEECCHHHEEEEEE | 33.01 | 27017623 | |
| 710 | Phosphorylation | KSFLTGKSPSLGGIP HHHHHCCCCCCCCCC | 22.52 | 27017623 | |
| 712 | Phosphorylation | FLTGKSPSLGGIPHD HHHCCCCCCCCCCCC | 46.89 | 27017623 | |
| 725 | Phosphorylation | HDEYGMTSLGVRAYV CCCCCCCCHHHHHHH | 17.77 | 27017623 | |
| 736 | Phosphorylation | RAYVNKIYETLNLTN HHHHHHHHHHHCCCC | 12.41 | 27017623 | |
| 742 | Phosphorylation | IYETLNLTNSTVYKF HHHHHCCCCCEEEEE | 26.50 | 27017623 | |
| 747 | Phosphorylation | NLTNSTVYKFQTGGP CCCCCEEEEEECCCC | 13.23 | 27017623 | |
| 1023 | Phosphorylation | NDLKLRNYLLLDKII HHHHHHHHHHHHCHH | 7.72 | 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 DHE2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DHE2_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 DHE2_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-25; SER-28 AND SER-242,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-482, AND MASSSPECTROMETRY. | |