| UniProt ID | DLD3_YEAST | |
|---|---|---|
| UniProt AC | P39976 | |
| Protein Name | D-2-hydroxyglutarate--pyruvate transhydrogenase DLD3 {ECO:0000305} | |
| Gene Name | DLD3 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 496 | |
| Subcellular Localization | Cytoplasm . | |
| 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.. | |
| Protein Sequence | MTAAHPVAQLTAEAYPKVKRNPNFKVLDSEDLAYFRSILSNDEILNSQAPEELASFNQDWMKKYRGQSNLILLPNSTDKVSKIMKYCNDKKLAVVPQGGNTDLVGASVPVFDEIVLSLRNMNKVRDFDPVSGTFKCDAGVVMRDAHQFLHDHDHIFPLDLPSRNNCQVGGVVSTNAGGLNFLRYGSLHGNVLGLEVVLPNGEIISNINALRKDNTGYDLKQLFIGAEGTIGVVTGVSIVAAAKPKALNAVFFGIENFDTVQKLFVKAKSELSEILSAFEFMDRGSIECTIEYLKDLPFPLENQHNFYVLIETSGSNKRHDDEKLTAFLKDTTDSKLISEGMMAKDKADFDRLWTWRKSVPTACNSYGGMYKYDMSLQLKDLYSVSAAVTERLNAAGLIGDAPKPVVKSCGYGHVGDGNIHLNIAVREFTKQIEDLLEPFVYEYIASKKGSISAEHGIGFHKKGKLHYTRSDIEIRFMKDIKNHYDPNGILNPYKYI | |
| 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 |
|---|---|---|---|---|---|
| 11 | Phosphorylation | AHPVAQLTAEAYPKV CCHHHHHHHHHCCHH | 15.46 | 30377154 | |
| 15 | Phosphorylation | AQLTAEAYPKVKRNP HHHHHHHCCHHCCCC | 8.62 | 30377154 | |
| 17 | Ubiquitination | LTAEAYPKVKRNPNF HHHHHCCHHCCCCCC | 47.95 | 12872131 | |
| 25 | Ubiquitination | VKRNPNFKVLDSEDL HCCCCCCCCCCHHHH | 48.83 | 17644757 | |
| 29 | Phosphorylation | PNFKVLDSEDLAYFR CCCCCCCHHHHHHHH | 28.93 | 22369663 | |
| 34 | Phosphorylation | LDSEDLAYFRSILSN CCHHHHHHHHHHHCC | 13.56 | 22369663 | |
| 55 | Phosphorylation | QAPEELASFNQDWMK CCHHHHHHCCHHHHH | 37.04 | 30377154 | |
| 62 | Acetylation | SFNQDWMKKYRGQSN HCCHHHHHHHCCCCC | 42.26 | 24489116 | |
| 63 | Ubiquitination | FNQDWMKKYRGQSNL CCHHHHHHHCCCCCE | 24.87 | 17644757 | |
| 64 | Phosphorylation | NQDWMKKYRGQSNLI CHHHHHHHCCCCCEE | 17.92 | 19795423 | |
| 68 | Phosphorylation | MKKYRGQSNLILLPN HHHHCCCCCEEECCC | 36.11 | 22369663 | |
| 76 | Phosphorylation | NLILLPNSTDKVSKI CEEECCCCHHHHHHH | 35.72 | 22369663 | |
| 77 | Phosphorylation | LILLPNSTDKVSKIM EEECCCCHHHHHHHH | 46.62 | 22369663 | |
| 79 | Ubiquitination | LLPNSTDKVSKIMKY ECCCCHHHHHHHHHH | 48.79 | 17644757 | |
| 85 | Acetylation | DKVSKIMKYCNDKKL HHHHHHHHHCCCCCE | 50.56 | 25381059 | |
| 90 | Ubiquitination | IMKYCNDKKLAVVPQ HHHHCCCCCEEEECC | 35.38 | 17644757 | |
| 91 | Ubiquitination | MKYCNDKKLAVVPQG HHHCCCCCEEEECCC | 44.54 | 17644757 | |
| 107 | Phosphorylation | NTDLVGASVPVFDEI CCCCCCCCCCCHHHH | 22.48 | 25005228 | |
| 117 | Phosphorylation | VFDEIVLSLRNMNKV CHHHHHHHHCCCCCC | 17.87 | 25005228 | |
| 123 | Ubiquitination | LSLRNMNKVRDFDPV HHHCCCCCCCCCCCC | 28.07 | 17644757 | |
| 135 | Ubiquitination | DPVSGTFKCDAGVVM CCCCCEEEECCEEEE | 30.92 | 24961812 | |
| 212 | Ubiquitination | SNINALRKDNTGYDL ECHHHHCCCCCCCCH | 57.06 | 17644757 | |
| 215 | Phosphorylation | NALRKDNTGYDLKQL HHHCCCCCCCCHHHH | 47.45 | 27214570 | |
| 245 | Ubiquitination | IVAAAKPKALNAVFF HHHCCCCHHHHEEEE | 65.87 | 17644757 | |
| 262 | Ubiquitination | ENFDTVQKLFVKAKS CCHHHHHHHHHHHHH | 39.29 | 17644757 | |
| 323 | Acetylation | NKRHDDEKLTAFLKD CCCCCHHHHHHHHHH | 59.12 | 24489116 | |
| 323 | Ubiquitination | NKRHDDEKLTAFLKD CCCCCHHHHHHHHHH | 59.12 | 17644757 | |
| 329 | Ubiquitination | EKLTAFLKDTTDSKL HHHHHHHHHCCCHHH | 46.72 | 17644757 | |
| 329 | Acetylation | EKLTAFLKDTTDSKL HHHHHHHHHCCCHHH | 46.72 | 24489116 | |
| 329 | Succinylation | EKLTAFLKDTTDSKL HHHHHHHHHCCCHHH | 46.72 | 23954790 | |
| 335 | Ubiquitination | LKDTTDSKLISEGMM HHHCCCHHHHHCCCC | 53.29 | 24961812 | |
| 335 | Acetylation | LKDTTDSKLISEGMM HHHCCCHHHHHCCCC | 53.29 | 22865919 | |
| 344 | Acetylation | ISEGMMAKDKADFDR HHCCCCCCCHHHHHH | 41.69 | 25381059 | |
| 357 | Ubiquitination | DRLWTWRKSVPTACN HHHHHHHHCCCCHHH | 47.57 | 23749301 | |
| 358 | Phosphorylation | RLWTWRKSVPTACNS HHHHHHHCCCCHHHH | 25.42 | 19779198 | |
| 372 | Phosphorylation | SYGGMYKYDMSLQLK HCCCEEEEEEEEEHH | 10.21 | 25533186 | |
| 403 | Ubiquitination | GLIGDAPKPVVKSCG CCCCCCCCCCEEECC | 52.76 | 24961812 | |
| 407 | Ubiquitination | DAPKPVVKSCGYGHV CCCCCCEEECCCCCC | 40.02 | 17644757 | |
| 408 | Phosphorylation | APKPVVKSCGYGHVG CCCCCEEECCCCCCC | 10.93 | 28889911 | |
| 411 | Phosphorylation | PVVKSCGYGHVGDGN CCEEECCCCCCCCCC | 14.37 | 25533186 | |
| 430 | Ubiquitination | IAVREFTKQIEDLLE EEHHHHHHHHHHHHH | 55.38 | 17644757 | |
| 447 | Ubiquitination | VYEYIASKKGSISAE HHHHHHHCCCCCEEE | 52.73 | 17644757 | |
| 448 | Ubiquitination | YEYIASKKGSISAEH HHHHHHCCCCCEEEC | 56.23 | 17644757 | |
| 450 | Phosphorylation | YIASKKGSISAEHGI HHHHCCCCCEEECCC | 23.42 | 24961812 | |
| 452 | Phosphorylation | ASKKGSISAEHGIGF HHCCCCCEEECCCEE | 29.33 | 24961812 | |
| 461 | Ubiquitination | EHGIGFHKKGKLHYT ECCCEEEECCCEEEE | 62.04 | 17644757 | |
| 461 | Acetylation | EHGIGFHKKGKLHYT ECCCEEEECCCEEEE | 62.04 | 22865919 | |
| 462 | Ubiquitination | HGIGFHKKGKLHYTR CCCEEEECCCEEEEC | 53.35 | 17644757 | |
| 467 | Phosphorylation | HKKGKLHYTRSDIEI EECCCEEEECHHHEE | 17.81 | 22369663 | |
| 468 | Phosphorylation | KKGKLHYTRSDIEIR ECCCEEEECHHHEEE | 16.98 | 22369663 | |
| 470 | Phosphorylation | GKLHYTRSDIEIRFM CCEEEECHHHEEEEE | 34.83 | 22369663 | |
| 481 | Acetylation | IRFMKDIKNHYDPNG EEEEHHHHHCCCCCC | 48.05 | 22865919 | |
| 481 | Ubiquitination | IRFMKDIKNHYDPNG EEEEHHHHHCCCCCC | 48.05 | 24961812 |
| 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 DLD3_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DLD3_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 DLD3_YEAST !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| LSP1_YEAST | LSP1 | physical | 18467557 | |
| HSP71_YEAST | SSA1 | physical | 19536198 | |
| SSB1_YEAST | SSB1 | physical | 19536198 | |
| HRT3_YEAST | HRT3 | physical | 26297823 | |
| PRP9_YEAST | PRP9 | genetic | 27708008 | |
| KTHY_YEAST | CDC8 | genetic | 27708008 | |
| PSA7_YEAST | PRE10 | genetic | 27708008 | |
| RLA1_YEAST | RPP1A | genetic | 27708008 | |
| GCS1_YEAST | GCS1 | genetic | 27708008 | |
| SNF6_YEAST | SNF6 | genetic | 27708008 | |
| FLX1_YEAST | FLX1 | genetic | 27708008 | |
| MDM35_YEAST | MDM35 | genetic | 27708008 | |
| ERG3_YEAST | ERG3 | genetic | 27708008 | |
| EIF3J_YEAST | HCR1 | genetic | 27708008 | |
| UPS1_YEAST | UPS1 | genetic | 27708008 | |
| PUS7_YEAST | PUS7 | genetic | 27708008 | |
| VPH1_YEAST | VPH1 | genetic | 27708008 | |
| MSC6_YEAST | MSC6 | genetic | 27708008 | |
| GGPPS_YEAST | BTS1 | genetic | 27708008 | |
| YME1_YEAST | YME1 | genetic | 27708008 | |
| MD1L1_HUMAN | MAD1L1 | physical | 27107014 |
| 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-470, AND MASSSPECTROMETRY. | |
| Ubiquitylation | |
| Reference | PubMed |
| "A proteomics approach to understanding protein ubiquitination."; Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.; Nat. Biotechnol. 21:921-926(2003). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-17, AND MASSSPECTROMETRY. | |