| UniProt ID | DLD2_YEAST | |
|---|---|---|
| UniProt AC | P46681 | |
| Protein Name | D-2-hydroxyglutarate--pyruvate transhydrogenase DLD2 {ECO:0000305} | |
| Gene Name | DLD2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 530 | |
| Subcellular Localization | Mitochondrion matrix . | |
| Protein Description | Catalyzes the reversible oxidation of (R)-2-hydroxyglutarate to 2-oxoglutarate coupled to reduction of pyruvate to (R)-lactate. Can also use oxaloacetate as electron acceptor instead of pyruvate producing (R)-malate. [PubMed: 26774271 In addition to its enzymatic role it could play an important role in the yeast cell morphology] | |
| Protein Sequence | MLRNILVRSTGSNFKFAGRYMKSSALLGYYRRVNYYSTKIQTRLTSENYPDVHRDPRFKKLTSDDLNYFKSILSEQEILRASESEDLSFYNEDWMRKYKGQSKLVLRPKSVEKVSLILNYCNDEKIAVVPQGGNTGLVGGSVPIFDELILSLANLNKIRDFDPVSGILKCDAGVILENANNYVMEQNYMFPLDLGAKGSCHVGGVVATNAGGLRLLRYGSLHGSVLGLEVVMPNGQIVNSMHSMRKDNTGYDLKQLFIGSEGTIGIITGVSILTVPKPKAFNVSYLSVESFEDVQKVFVRARQELSEILSAFEFMDAKSQVLAKSQLKDAAFPLEDEHPFYILIETSGSNKDHDDSKLETFLENVMEEGIVTDGVVAQDETELQNLWKWREMIPEASQANGGVYKYDVSLPLKDLYSLVEATNARLSEAELVGDSPKPVVGAIGYGHVGDGNLHLNVAVREYNKNIEKTLEPFVYEFVSSKHGSVSAEHGLGFQKKNYIGYSKSPEEVKMMKDLKVHYDPNGILNPYKYI | |
| 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 |
|---|---|---|---|---|---|
| 249 | Phosphorylation | HSMRKDNTGYDLKQL HHCCCCCCCCCHHHE | 47.45 | 27214570 | |
| 319 | Phosphorylation | FEFMDAKSQVLAKSQ HHHCCHHHHHHHHHH | 27.52 | 19823750 | |
| 325 | Phosphorylation | KSQVLAKSQLKDAAF HHHHHHHHHHCCCCC | 34.83 | 19823750 | |
| 468 | Acetylation | EYNKNIEKTLEPFVY HHHHCHHHHHHHHHH | 55.39 | 24489116 | |
| 503 | Acetylation | KNYIGYSKSPEEVKM CCCCCCCCCHHHHHH | 62.64 | 25381059 | |
| 509 | Acetylation | SKSPEEVKMMKDLKV CCCHHHHHHHHCCEE | 36.23 | 25381059 |
| 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 DLD2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DLD2_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 DLD2_YEAST !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| ACT_YEAST | ACT1 | physical | 15249227 | |
| ACT_YEAST | ACT1 | physical | 15158445 | |
| ACT_YEAST | ACT1 | physical | 15351742 | |
| RV167_YEAST | RVS167 | genetic | 20093466 | |
| ZRT1_YEAST | ZRT1 | genetic | 20093466 | |
| MKS1_YEAST | MKS1 | genetic | 20093466 | |
| MED9_YEAST | CSE2 | genetic | 20093466 | |
| BUD21_YEAST | BUD21 | genetic | 20093466 | |
| LGE1_YEAST | LGE1 | genetic | 20093466 | |
| CSG2_YEAST | CSG2 | genetic | 21623372 | |
| QCR8_YEAST | QCR8 | genetic | 21623372 | |
| LCB5_YEAST | LCB5 | genetic | 21623372 | |
| MRM2_YEAST | MRM2 | genetic | 27708008 | |
| CSN12_YEAST | YJR084W | genetic | 27708008 | |
| RV161_YEAST | RVS161 | genetic | 27708008 | |
| MSH3_YEAST | MSH3 | genetic | 27708008 | |
| HNT2_YEAST | HNT2 | genetic | 27708008 | |
| RLA4_YEAST | RPP2B | genetic | 27708008 | |
| RV167_YEAST | RVS167 | genetic | 27708008 | |
| SMF2_YEAST | SMF2 | genetic | 27708008 | |
| UBX2_YEAST | UBX2 | genetic | 27708008 | |
| MKS1_YEAST | MKS1 | genetic | 27708008 | |
| SIN3_YEAST | SIN3 | genetic | 27708008 | |
| IDH2_YEAST | IDH2 | genetic | 27708008 | |
| RS10A_YEAST | RPS10A | genetic | 27708008 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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