| UniProt ID | IDH2_YEAST | |
|---|---|---|
| UniProt AC | P28241 | |
| Protein Name | Isocitrate dehydrogenase [NAD] subunit 2, mitochondrial | |
| Gene Name | IDH2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 369 | |
| Subcellular Localization | Mitochondrion matrix . | |
| Protein Description | Performs an essential role in the oxidative function of the citric acid cycle. Also binds RNA; specifically to the 5'-untranslated leaders of mitochondrial mRNAs.. | |
| Protein Sequence | MLRNTFFRNTSRRFLATVKQPSIGRYTGKPNPSTGKYTVSFIEGDGIGPEISKSVKKIFSAANVPIEWESCDVSPIFVNGLTTIPDPAVQSITKNLVALKGPLATPIGKGHRSLNLTLRKTFGLFANVRPAKSIEGFKTTYENVDLVLIRENTEGEYSGIEHIVCPGVVQSIKLITRDASERVIRYAFEYARAIGRPRVIVVHKSTIQRLADGLFVNVAKELSKEYPDLTLETELIDNSVLKVVTNPSAYTDAVSVCPNLYGDILSDLNSGLSAGSLGLTPSANIGHKISIFEAVHGSAPDIAGQDKANPTALLLSSVMMLNHMGLTNHADQIQNAVLSTIASGPENRTGDLAGTATTSSFTEAVIKRL | |
| 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 |
|---|---|---|---|---|---|
| 22 | Phosphorylation | LATVKQPSIGRYTGK EEEEECCCCCEECCC | 34.87 | 19823750 | |
| 26 | Phosphorylation | KQPSIGRYTGKPNPS ECCCCCEECCCCCCC | 18.03 | 19823750 | |
| 27 | Phosphorylation | QPSIGRYTGKPNPST CCCCCEECCCCCCCC | 37.05 | 19823750 | |
| 29 | Acetylation | SIGRYTGKPNPSTGK CCCEECCCCCCCCCE | 33.55 | 24489116 | |
| 33 | Phosphorylation | YTGKPNPSTGKYTVS ECCCCCCCCCEEEEE | 57.33 | 19823750 | |
| 34 | Phosphorylation | TGKPNPSTGKYTVSF CCCCCCCCCEEEEEE | 38.66 | 19823750 | |
| 36 | Acetylation | KPNPSTGKYTVSFIE CCCCCCCEEEEEEEE | 37.52 | 24489116 | |
| 38 | Phosphorylation | NPSTGKYTVSFIEGD CCCCCEEEEEEEECC | 17.11 | 30377154 | |
| 40 | Phosphorylation | STGKYTVSFIEGDGI CCCEEEEEEEECCCC | 16.83 | 28889911 | |
| 53 | Acetylation | GIGPEISKSVKKIFS CCCHHHHHHHHHHHH | 66.00 | 24489116 | |
| 100 | Acetylation | TKNLVALKGPLATPI HCCHHHHCCCCCCCC | 49.06 | 24489116 | |
| 105 | Phosphorylation | ALKGPLATPIGKGHR HHCCCCCCCCCCCCC | 24.11 | 22369663 | |
| 113 | Phosphorylation | PIGKGHRSLNLTLRK CCCCCCCCCCCCHHH | 18.88 | 22369663 | |
| 117 | Phosphorylation | GHRSLNLTLRKTFGL CCCCCCCCHHHHHCE | 24.36 | 22369663 | |
| 121 | Phosphorylation | LNLTLRKTFGLFANV CCCCHHHHHCEECCC | 19.26 | 25521595 | |
| 132 | Acetylation | FANVRPAKSIEGFKT ECCCCCCCCCCCCEE | 55.43 | 24489116 | |
| 133 | Phosphorylation | ANVRPAKSIEGFKTT CCCCCCCCCCCCEEC | 28.16 | 21440633 | |
| 153 | Phosphorylation | LVLIRENTEGEYSGI EEEEECCCCCCCCCC | 40.38 | 22369663 | |
| 158 | Phosphorylation | ENTEGEYSGIEHIVC CCCCCCCCCCCEEEC | 29.06 | 19779198 | |
| 165 | Glutathionylation | SGIEHIVCPGVVQSI CCCCEEECCHHHHEE | 2.10 | 22833525 | |
| 220 | Succinylation | GLFVNVAKELSKEYP CCHHHHHHHHHHHCC | 55.71 | 23954790 | |
| 220 | Acetylation | GLFVNVAKELSKEYP CCHHHHHHHHHHHCC | 55.71 | 24489116 | |
| 224 | Acetylation | NVAKELSKEYPDLTL HHHHHHHHHCCCCEE | 74.10 | 24489116 | |
| 298 | Phosphorylation | IFEAVHGSAPDIAGQ EEEHHHCCCCCCCCC | 23.04 | 21440633 | |
| 311 | Phosphorylation | GQDKANPTALLLSSV CCCCCCHHHHHHHHH | 29.73 | 19779198 | |
| 327 | Phosphorylation | MLNHMGLTNHADQIQ HHHHCCCCCCHHHHH | 21.16 | 19779198 | |
| 339 | Phosphorylation | QIQNAVLSTIASGPE HHHHHHHHHHHCCCC | 15.92 | 19779198 | |
| 340 | Phosphorylation | IQNAVLSTIASGPEN HHHHHHHHHHCCCCC | 19.19 | 28889911 | |
| 343 | Phosphorylation | AVLSTIASGPENRTG HHHHHHHCCCCCCCC | 51.54 | 27017623 | |
| 349 | Phosphorylation | ASGPENRTGDLAGTA HCCCCCCCCCCCCCC | 46.78 | 28889911 | |
| 358 | Phosphorylation | DLAGTATTSSFTEAV CCCCCCCCCHHHHHH | 21.65 | 30377154 | |
| 359 | Phosphorylation | LAGTATTSSFTEAVI CCCCCCCCHHHHHHH | 21.06 | 27214570 | |
| 360 | Phosphorylation | AGTATTSSFTEAVIK CCCCCCCHHHHHHHH | 33.81 | 25752575 | |
| 362 | Phosphorylation | TATTSSFTEAVIKRL CCCCCHHHHHHHHHC | 25.61 | 30377154 |
| 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 IDH2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of IDH2_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 IDH2_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 THR-105; THR-153 ANDSER-360, AND MASS 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 THR-349, AND MASSSPECTROMETRY. | |