| UniProt ID | ODP2_YEAST | |
|---|---|---|
| UniProt AC | P12695 | |
| Protein Name | Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial | |
| Gene Name | LAT1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 482 | |
| Subcellular Localization | Mitochondrion matrix . | |
| Protein Description | The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).. | |
| Protein Sequence | MSAFVRVVPRISRSSVLTRSLRLQLRCYASYPEHTIIGMPALSPTMTQGNLAAWTKKEGDQLSPGEVIAEIETDKAQMDFEFQEDGYLAKILVPEGTKDIPVNKPIAVYVEDKADVPAFKDFKLEDSGSDSKTSTKAQPAEPQAEKKQEAPAEETKTSAPEAKKSDVAAPQGRIFASPLAKTIALEKGISLKDVHGTGPRGRITKADIESYLEKSSKQSSQTSGAAAATPAAATSSTTAGSAPSPSSTASYEDVPISTMRSIIGERLLQSTQGIPSYIVSSKISISKLLKLRQSLNATANDKYKLSINDLLVKAITVAAKRVPDANAYWLPNENVIRKFKNVDVSVAVATPTGLLTPIVKNCEAKGLSQISNEIKELVKRARINKLAPEEFQGGTICISNMGMNNAVNMFTSIINPPQSTILAIATVERVAVEDAAAENGFSFDNQVTITGTFDHRTIDGAKGAEFMKELKTVIENPLEMLL | |
| 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 |
|---|---|---|---|---|---|
| 18 | Phosphorylation | ISRSSVLTRSLRLQL CCHHHHHHHHHHHHH | 18.96 | 28889911 | |
| 75 | N6-lipoyllysine | IAEIETDKAQMDFEF EEEEECCCCCCCEEE | 48.19 | - | |
| 75 | Lipoylation | IAEIETDKAQMDFEF EEEEECCCCCCCEEE | 48.19 | 3050999 | |
| 97 | Phosphorylation | KILVPEGTKDIPVNK EEECCCCCCCCCCCC | 24.71 | 21440633 | |
| 98 | Acetylation | ILVPEGTKDIPVNKP EECCCCCCCCCCCCC | 65.60 | 24489116 | |
| 104 | Acetylation | TKDIPVNKPIAVYVE CCCCCCCCCEEEEEE | 37.73 | 24489116 | |
| 113 | Acetylation | IAVYVEDKADVPAFK EEEEEECCCCCCCCC | 32.74 | 24489116 | |
| 120 | Acetylation | KADVPAFKDFKLEDS CCCCCCCCCEECCCC | 65.45 | 24489116 | |
| 120 | Succinylation | KADVPAFKDFKLEDS CCCCCCCCCEECCCC | 65.45 | 23954790 | |
| 123 | Acetylation | VPAFKDFKLEDSGSD CCCCCCEECCCCCCC | 62.19 | 24489116 | |
| 127 | Phosphorylation | KDFKLEDSGSDSKTS CCEECCCCCCCCCCC | 30.71 | 28889911 | |
| 129 | Phosphorylation | FKLEDSGSDSKTSTK EECCCCCCCCCCCCC | 42.54 | 24961812 | |
| 131 | Phosphorylation | LEDSGSDSKTSTKAQ CCCCCCCCCCCCCCC | 39.26 | 24961812 | |
| 132 | 2-Hydroxyisobutyrylation | EDSGSDSKTSTKAQP CCCCCCCCCCCCCCC | 52.03 | - | |
| 133 | Phosphorylation | DSGSDSKTSTKAQPA CCCCCCCCCCCCCCC | 45.65 | 28889911 | |
| 135 | Phosphorylation | GSDSKTSTKAQPAEP CCCCCCCCCCCCCCC | 35.31 | 23749301 | |
| 146 | Acetylation | PAEPQAEKKQEAPAE CCCCHHHHHCCCCHH | 63.87 | 25381059 | |
| 156 | Acetylation | EAPAEETKTSAPEAK CCCHHHHCCCCCHHH | 43.70 | 22865919 | |
| 158 | Phosphorylation | PAEETKTSAPEAKKS CHHHHCCCCCHHHHH | 43.30 | 23749301 | |
| 163 | Acetylation | KTSAPEAKKSDVAAP CCCCCHHHHHCCCCC | 51.66 | 25381059 | |
| 165 | Phosphorylation | SAPEAKKSDVAAPQG CCCHHHHHCCCCCCC | 36.29 | 28889911 | |
| 177 | Phosphorylation | PQGRIFASPLAKTIA CCCCCCCCHHHHHHH | 15.08 | 24961812 | |
| 181 | Acetylation | IFASPLAKTIALEKG CCCCHHHHHHHHHCC | 48.42 | 24489116 | |
| 187 | Acetylation | AKTIALEKGISLKDV HHHHHHHCCCCCCCC | 63.49 | 24489116 | |
| 187 | 2-Hydroxyisobutyrylation | AKTIALEKGISLKDV HHHHHHHCCCCCCCC | 63.49 | - | |
| 192 | Succinylation | LEKGISLKDVHGTGP HHCCCCCCCCCCCCC | 51.41 | 23954790 | |
| 192 | Acetylation | LEKGISLKDVHGTGP HHCCCCCCCCCCCCC | 51.41 | 22865919 | |
| 205 | Acetylation | GPRGRITKADIESYL CCCCCCCHHHHHHHH | 41.51 | 24489116 | |
| 214 | Acetylation | DIESYLEKSSKQSSQ HHHHHHHHHCCCCCC | 58.39 | 24489116 | |
| 214 | Succinylation | DIESYLEKSSKQSSQ HHHHHHHHHCCCCCC | 58.39 | 23954790 | |
| 280 | Phosphorylation | GIPSYIVSSKISISK CCCHHHHCCCCCHHH | 19.16 | 28889911 | |
| 281 | Phosphorylation | IPSYIVSSKISISKL CCHHHHCCCCCHHHH | 24.10 | 28889911 | |
| 287 | Acetylation | SSKISISKLLKLRQS CCCCCHHHHHHHHHH | 57.05 | 24489116 | |
| 302 | 2-Hydroxyisobutyrylation | LNATANDKYKLSIND HCCCCCCCCCCCHHH | 44.06 | - | |
| 302 | Acetylation | LNATANDKYKLSIND HCCCCCCCCCCCHHH | 44.06 | 24489116 | |
| 304 | Acetylation | ATANDKYKLSINDLL CCCCCCCCCCHHHHH | 41.31 | 24489116 | |
| 360 | Ubiquitination | GLLTPIVKNCEAKGL CCCHHHHHCCHHCCH | 57.51 | 22817900 | |
| 365 | Ubiquitination | IVKNCEAKGLSQISN HHHCCHHCCHHHHHH | 37.78 | 23749301 | |
| 365 | Acetylation | IVKNCEAKGLSQISN HHHCCHHCCHHHHHH | 37.78 | 25381059 | |
| 368 | Phosphorylation | NCEAKGLSQISNEIK CCHHCCHHHHHHHHH | 33.85 | 25752575 | |
| 375 | Acetylation | SQISNEIKELVKRAR HHHHHHHHHHHHHHH | 38.52 | 24489116 | |
| 462 | Acetylation | HRTIDGAKGAEFMKE CCCCCCHHHHHHHHH | 65.27 | 24489116 | |
| 462 | Succinylation | HRTIDGAKGAEFMKE CCCCCCHHHHHHHHH | 65.27 | 23954790 | |
| 468 | Acetylation | AKGAEFMKELKTVIE HHHHHHHHHHHHHHH | 66.28 | 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 ODP2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ODP2_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 ODP2_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-280 AND SER-281, ANDMASS SPECTROMETRY. | |
