| UniProt ID | DLDH_YEAST | |
|---|---|---|
| UniProt AC | P09624 | |
| Protein Name | Dihydrolipoyl dehydrogenase, mitochondrial | |
| Gene Name | LPD1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 499 | |
| Subcellular Localization | Mitochondrion matrix. | |
| Protein Description | Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes. This includes the pyruvate dehydrogenase complex, which catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). Acts also as component of the glycine cleavage system (glycine decarboxylase complex), which catalyzes the degradation of glycine.. | |
| Protein Sequence | MLRIRSLLNNKRAFSSTVRTLTINKSHDVVIIGGGPAGYVAAIKAAQLGFNTACVEKRGKLGGTCLNVGCIPSKALLNNSHLFHQMHTEAQKRGIDVNGDIKINVANFQKAKDDAVKQLTGGIELLFKKNKVTYYKGNGSFEDETKIRVTPVDGLEGTVKEDHILDVKNIIVATGSEVTPFPGIEIDEEKIVSSTGALSLKEIPKRLTIIGGGIIGLEMGSVYSRLGSKVTVVEFQPQIGASMDGEVAKATQKFLKKQGLDFKLSTKVISAKRNDDKNVVEIVVEDTKTNKQENLEAEVLLVAVGRRPYIAGLGAEKIGLEVDKRGRLVIDDQFNSKFPHIKVVGDVTFGPMLAHKAEEEGIAAVEMLKTGHGHVNYNNIPSVMYSHPEVAWVGKTEEQLKEAGIDYKIGKFPFAANSRAKTNQDTEGFVKILIDSKTERILGAHIIGPNAGEMIAEAGLALEYGASAEDVARVCHAHPTLSEAFKEANMAAYDKAIHC | |
| 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 |
|---|---|---|---|---|---|
| 57 | Acetylation | FNTACVEKRGKLGGT CCCHHHHCCCCCCCE | 46.16 | 24489116 | |
| 110 | Acetylation | INVANFQKAKDDAVK EEECCHHHHCHHHHH | 53.95 | 24489116 | |
| 117 | Acetylation | KAKDDAVKQLTGGIE HHCHHHHHHHCCCEE | 41.11 | 24489116 | |
| 128 | Acetylation | GGIELLFKKNKVTYY CCEEEEEEECCEEEE | 56.24 | 24489116 | |
| 136 | Acetylation | KNKVTYYKGNGSFED ECCEEEECCCCCCCC | 35.17 | 24489116 | |
| 136 | Succinylation | KNKVTYYKGNGSFED ECCEEEECCCCCCCC | 35.17 | 23954790 | |
| 146 | Acetylation | GSFEDETKIRVTPVD CCCCCCCEEEEEECC | 26.85 | 24489116 | |
| 160 | Acetylation | DGLEGTVKEDHILDV CCCCCCCCCCEEEEC | 58.21 | 24489116 | |
| 160 | Succinylation | DGLEGTVKEDHILDV CCCCCCCCCCEEEEC | 58.21 | 23954790 | |
| 193 | Phosphorylation | IDEEKIVSSTGALSL CCHHHCCCCCCCCCH | 26.17 | 22369663 | |
| 194 | Phosphorylation | DEEKIVSSTGALSLK CHHHCCCCCCCCCHH | 21.70 | 22369663 | |
| 195 | Phosphorylation | EEKIVSSTGALSLKE HHHCCCCCCCCCHHH | 20.97 | 22369663 | |
| 199 | Phosphorylation | VSSTGALSLKEIPKR CCCCCCCCHHHCCCC | 36.54 | 22369663 | |
| 201 | Acetylation | STGALSLKEIPKRLT CCCCCCHHHCCCCEE | 50.66 | 24489116 | |
| 249 | Acetylation | SMDGEVAKATQKFLK CCCHHHHHHHHHHHH | 58.08 | 24489116 | |
| 253 | Acetylation | EVAKATQKFLKKQGL HHHHHHHHHHHHCCC | 48.59 | 24489116 | |
| 263 | Acetylation | KKQGLDFKLSTKVIS HHCCCCCEEEEEEEE | 40.99 | 24489116 | |
| 267 | 2-Hydroxyisobutyrylation | LDFKLSTKVISAKRN CCCEEEEEEEEEECC | 33.91 | - | |
| 272 | 2-Hydroxyisobutyrylation | STKVISAKRNDDKNV EEEEEEEECCCCCCE | 44.97 | - | |
| 277 | Acetylation | SAKRNDDKNVVEIVV EEECCCCCCEEEEEE | 55.28 | 24489116 | |
| 324 | Acetylation | KIGLEVDKRGRLVID HCCCEECCCCCEEEC | 63.03 | 24489116 | |
| 337 | Acetylation | IDDQFNSKFPHIKVV ECCCCCCCCCCEEEE | 65.11 | 24489116 | |
| 401 | Succinylation | GKTEEQLKEAGIDYK CCCHHHHHHCCCCCE | 45.25 | 23954790 | |
| 401 | 2-Hydroxyisobutyrylation | GKTEEQLKEAGIDYK CCCHHHHHHCCCCCE | 45.25 | - | |
| 401 | Acetylation | GKTEEQLKEAGIDYK CCCHHHHHHCCCCCE | 45.25 | 24489116 | |
| 408 | Acetylation | KEAGIDYKIGKFPFA HHCCCCCEECCCCCC | 41.03 | 24489116 | |
| 411 | Acetylation | GIDYKIGKFPFAANS CCCCEECCCCCCCCC | 54.02 | 24489116 | |
| 418 | Phosphorylation | KFPFAANSRAKTNQD CCCCCCCCCCCCCCC | 28.96 | 22369663 | |
| 436 | Phosphorylation | FVKILIDSKTERILG CEEEEEECCCCEEEE | 34.19 | 22369663 | |
| 437 | Acetylation | VKILIDSKTERILGA EEEEEECCCCEEEEC | 51.13 | 24489116 | |
| 437 | 2-Hydroxyisobutyrylation | VKILIDSKTERILGA EEEEEECCCCEEEEC | 51.13 | - | |
| 437 | Succinylation | VKILIDSKTERILGA EEEEEECCCCEEEEC | 51.13 | 23954790 | |
| 438 | Phosphorylation | KILIDSKTERILGAH EEEEECCCCEEEECE | 34.15 | 22369663 |
| 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 DLDH_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DLDH_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 DLDH_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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