| UniProt ID | ODO2_YEAST | |
|---|---|---|
| UniProt AC | P19262 | |
| Protein Name | Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial | |
| Gene Name | KGD2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 463 | |
| Subcellular Localization | Mitochondrion. | |
| Protein Description | The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).. | |
| Protein Sequence | MLSRATRTAAAKSLVKSKVARNVMAASFVKRHASTSLFKQANKVESLGSIYLSGKKISVAANPFSITSNRFKSTSIEVPPMAESLTEGSLKEYTKNVGDFIKEDELLATIETDKIDIEVNSPVSGTVTKLNFKPEDTVTVGEELAQVEPGEAPAEGSGESKPEPTEQAEPSQGVAARENSSEETASKKEAAPKKEAAPKKEVTEPKKADQPKKTVSKAQEPPVASNSFTPFPRTETRVKMNRMRLRIAERLKESQNTAASLTTFNEVDMSALMEMRKLYKDEIIKKTGTKFGFMGLFSKACTLAAKDIPAVNGAIEGDQIVYRDYTDISVAVATPKGLVTPVVRNAESLSVLDIENEIVRLSHKARDGKLTLEDMTGGTFTISNGGVFGSLYGTPIINSPQTAVLGLHGVKERPVTVNGQIVSRPMMYLALTYDHRLLDGREAVTFLKTVKELIEDPRKMLLW | |
| 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 |
|---|---|---|---|---|---|
| 17 | Phosphorylation | AAKSLVKSKVARNVM HHHHHHHHHHHHHHH | 25.53 | 19823750 | |
| 27 | Phosphorylation | ARNVMAASFVKRHAS HHHHHHHHHHHHHHC | 22.49 | 19823750 | |
| 34 | Phosphorylation | SFVKRHASTSLFKQA HHHHHHHCCHHHHHH | 16.65 | 19823750 | |
| 35 | Phosphorylation | FVKRHASTSLFKQAN HHHHHHCCHHHHHHH | 30.17 | 19823750 | |
| 36 | Phosphorylation | VKRHASTSLFKQANK HHHHHCCHHHHHHHH | 29.34 | 19823750 | |
| 46 | Phosphorylation | KQANKVESLGSIYLS HHHHHCCCCCEEEEC | 40.81 | 28889911 | |
| 51 | Phosphorylation | VESLGSIYLSGKKIS CCCCCEEEECCCEEE | 9.12 | 28889911 | |
| 53 | Phosphorylation | SLGSIYLSGKKISVA CCCEEEECCCEEEEE | 31.43 | 28889911 | |
| 93 | Phosphorylation | TEGSLKEYTKNVGDF CCCCHHHHHCCHHHH | 22.79 | 27017623 | |
| 114 | N6-lipoyllysine | LATIETDKIDIEVNS EEEEECCEEEEEECC | 50.09 | - | |
| 114 | Lipoylation | LATIETDKIDIEVNS EEEEECCEEEEEECC | 50.09 | - | |
| 114 | Acetylation | LATIETDKIDIEVNS EEEEECCEEEEEECC | 50.09 | 25381059 | |
| 225 | Phosphorylation | AQEPPVASNSFTPFP CCCCCCCCCCCCCCC | 32.99 | 29734811 | |
| 227 | Phosphorylation | EPPVASNSFTPFPRT CCCCCCCCCCCCCCC | 28.18 | 27214570 | |
| 236 | Phosphorylation | TPFPRTETRVKMNRM CCCCCCCHHHHHHHH | 39.90 | 20377248 | |
| 277 | Acetylation | SALMEMRKLYKDEII HHHHHHHHHHHHHHH | 55.66 | 25381059 | |
| 280 | Acetylation | MEMRKLYKDEIIKKT HHHHHHHHHHHHHHH | 60.36 | 24489116 | |
| 280 | Succinylation | MEMRKLYKDEIIKKT HHHHHHHHHHHHHHH | 60.36 | 23954790 | |
| 285 | Acetylation | LYKDEIIKKTGTKFG HHHHHHHHHHCCCCC | 50.36 | 24489116 | |
| 285 | Succinylation | LYKDEIIKKTGTKFG HHHHHHHHHHCCCCC | 50.36 | 23954790 | |
| 290 | Acetylation | IIKKTGTKFGFMGLF HHHHHCCCCCHHHHH | 44.85 | 24489116 | |
| 336 | Succinylation | SVAVATPKGLVTPVV EEEEECCCCCCCHHC | 61.60 | 23954790 | |
| 340 | Phosphorylation | ATPKGLVTPVVRNAE ECCCCCCCHHCCCCC | 18.53 | 27214570 | |
| 448 | Acetylation | REAVTFLKTVKELIE HHHHHHHHHHHHHHH | 47.26 | 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 ODO2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ODO2_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 ODO2_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "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-340, AND MASSSPECTROMETRY. | |
