| UniProt ID | ODP21_ARATH | |
|---|---|---|
| UniProt AC | Q0WQF7 | |
| Protein Name | Dihydrolipoyllysine-residue acetyltransferase component 1 of pyruvate dehydrogenase complex, mitochondrial | |
| Gene Name | LTA3 | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 637 | |
| Subcellular Localization | Mitochondrion matrix . | |
| Protein Description | The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).. | |
| Protein Sequence | MVLPLFRRAAIARTSSLLRARLFAPASEFHSRFSNGLYHLDDKISSSNGVRSASIDLITRMDDSSPKPILRFGVQNFSSTGPISQTVLAMPALSPTMSHGNVVKWMKKEGDKVEVGDVLCEIETDKATVEFESQEEGFLAKILVTEGSKDIPVNEPIAIMVEEEDDIKNVPATIEGGRDGKEETSAHQVMKPDESTQQKSSIQPDASDLPPHVVLEMPALSPTMNQGNIAKWWKKEGDKIEVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSKDVAVGKPIALIVEDAESIEAIKSSSAGSSEVDTVKEVPDSVVDKPTERKAGFTKISPAAKLLILEHGLEASSIEASGPYGTLLKSDVVAAIASGKASKSSASTKKKQPSKETPSKSSSTSKPSVTQSDNNYEDFPNSQIRKIIAKRLLESKQKIPHLYLQSDVVLDPLLAFRKELQENHGVKVSVNDIVIKAVAVALRNVRQANAFWDAEKGDIVMCDSVDISIAVATEKGLMTPIIKNADQKSISAISLEVKELAQKARSGKLAPHEFQGGTFSISNLGMYPVDNFCAIINPPQAGILAVGRGNKVVEPVIGLDGIEKPSVVTKMNVTLSADHRIFDGQVGASFMSELRSNFEDVRRLLL | |
| 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 |
|---|---|---|---|---|---|
| 59 | Phosphorylation | SASIDLITRMDDSSP EEEEEEEEECCCCCC | 29654922 | ||
| 126 | N6-lipoyllysine | LCEIETDKATVEFES EEEEECCCCEEEEEE | - | ||
| 126 | Lipoylation | LCEIETDKATVEFES EEEEECCCCEEEEEE | - | ||
| 126 | Lipoylation | LCEIETDKATVEFES EEEEECCCCEEEEEE | - | ||
| 253 | N6-lipoyllysine | IGEIETDKATLEFES EEEEECCCCEEEEEE | - | ||
| 253 | Lipoylation | IGEIETDKATLEFES EEEEECCCCEEEEEE | - | ||
| 253 | Lipoylation | IGEIETDKATLEFES EEEEECCCCEEEEEE | - | ||
| 275 | Phosphorylation | KILIPEGSKDVAVGK EEECCCCCCCCCCCC | 24243849 | ||
| 495 | Phosphorylation | GDIVMCDSVDISIAV CCEEEECCCCEEEEE | 25368622 | ||
| 499 | Phosphorylation | MCDSVDISIAVATEK EECCCCEEEEEECCC | 25368622 | ||
| 520 | Phosphorylation | IKNADQKSISAISLE ECCCCCCCEEEEEHH | 19880383 | ||
| 522 | Phosphorylation | NADQKSISAISLEVK CCCCCCEEEEEHHHH | 19880383 | ||
| 529 | Acetylation | SAISLEVKELAQKAR EEEEHHHHHHHHHHH | 24727099 |
| 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 ODP21_ARATH !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ODP21_ARATH !! | ||||||
* 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 ODP21_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| SUMO3_ARATH | SUMO3 | physical | 20855607 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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