| UniProt ID | MDHC_YEAST | |
|---|---|---|
| UniProt AC | P22133 | |
| Protein Name | Malate dehydrogenase, cytoplasmic | |
| Gene Name | MDH2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 377 | |
| Subcellular Localization | Cytoplasm. | |
| Protein Description | The isoenzyme MDH2 may function primarily in the glyoxylate cycle.. | |
| Protein Sequence | MPHSVTPSIEQDSLKIAILGAAGGIGQSLSLLLKAQLQYQLKESNRSVTHIHLALYDVNQEAINGVTADLSHIDTPISVSSHSPAGGIENCLHNASIVVIPAGVPRKPGMTRDDLFNVNAGIISQLGDSIAECCDLSKVFVLVISNPVNSLVPVMVSNILKNHPQSRNSGIERRIMGVTKLDIVRASTFLREINIESGLTPRVNSMPDVPVIGGHSGETIIPLFSQSNFLSRLNEDQLKYLIHRVQYGGDEVVKAKNGKGSATLSMAHAGYKCVVQFVSLLLGNIEQIHGTYYVPLKDANNFPIAPGADQLLPLVDGADYFAIPLTITTKGVSYVDYDIVNRMNDMERNQMLPICVSQLKKNIDKGLEFVASRSASS | |
| 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 |
|---|---|---|---|---|---|
| 4 | Phosphorylation | ----MPHSVTPSIEQ ----CCCCCCCCCCH | 23.09 | 22369663 | |
| 6 | Phosphorylation | --MPHSVTPSIEQDS --CCCCCCCCCCHHH | 17.84 | 22369663 | |
| 8 | Phosphorylation | MPHSVTPSIEQDSLK CCCCCCCCCCHHHHH | 29.41 | 22369663 | |
| 13 | Phosphorylation | TPSIEQDSLKIAILG CCCCCHHHHHHEEHH | 31.12 | 22369663 | |
| 15 | Ubiquitination | SIEQDSLKIAILGAA CCCHHHHHHEEHHHC | 33.76 | 17644757 | |
| 34 | Ubiquitination | QSLSLLLKAQLQYQL HHHHHHHHHHHHHHH | 33.77 | 17644757 | |
| 42 | Ubiquitination | AQLQYQLKESNRSVT HHHHHHHHHCCCCCE | 43.50 | 23749301 | |
| 180 | Ubiquitination | RRIMGVTKLDIVRAS HHHCCCCHHHHHHHH | 41.58 | 23749301 | |
| 180 | Acetylation | RRIMGVTKLDIVRAS HHHCCCCHHHHHHHH | 41.58 | 24489116 | |
| 197 | Phosphorylation | LREINIESGLTPRVN HHHHCCCCCCCCCCC | 34.99 | 30377154 | |
| 200 | Phosphorylation | INIESGLTPRVNSMP HCCCCCCCCCCCCCC | 16.75 | 29734811 | |
| 239 | Ubiquitination | RLNEDQLKYLIHRVQ HCCHHHHHHHHHHHC | 32.17 | 15699485 | |
| 239 | Acetylation | RLNEDQLKYLIHRVQ HCCHHHHHHHHHHHC | 32.17 | 24489116 | |
| 254 | Ubiquitination | YGGDEVVKAKNGKGS CCCCEEEECCCCCCE | 59.84 | 23749301 | |
| 256 | Ubiquitination | GDEVVKAKNGKGSAT CCEEEECCCCCCEEE | 61.59 | 15699485 | |
| 259 | Ubiquitination | VVKAKNGKGSATLSM EEECCCCCCEEEHHH | 60.11 | 23749301 | |
| 272 | Ubiquitination | SMAHAGYKCVVQFVS HHHCCCHHHHHHHHH | 21.45 | 15699485 | |
| 330 | Ubiquitination | IPLTITTKGVSYVDY EEEEEECCCCCEECH | 48.98 | 15699485 | |
| 360 | Ubiquitination | PICVSQLKKNIDKGL HHHHHHHHHHHHHHH | 35.82 | 17644757 | |
| 361 | Ubiquitination | ICVSQLKKNIDKGLE HHHHHHHHHHHHHHH | 68.66 | 17644757 | |
| 365 | Acetylation | QLKKNIDKGLEFVAS HHHHHHHHHHHHHHH | 62.69 | 24489116 | |
| 365 | Ubiquitination | QLKKNIDKGLEFVAS HHHHHHHHHHHHHHH | 62.69 | 15699485 | |
| 372 | Phosphorylation | KGLEFVASRSASS-- HHHHHHHHCCCCC-- | 22.82 | 27214570 | |
| 374 | Phosphorylation | LEFVASRSASS---- HHHHHHCCCCC---- | 29.97 | 27017623 |
| 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 MDHC_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MDHC_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 MDHC_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 THR-6, AND MASSSPECTROMETRY. | |