| UniProt ID | ACH1_YEAST | |
|---|---|---|
| UniProt AC | P32316 | |
| Protein Name | Acetyl-CoA hydrolase | |
| Gene Name | ACH1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 526 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | Presumably involved in regulating the intracellular acetyl-CoA pool for fatty acid and cholesterol synthesis and fatty acid oxidation. It may be involved in overall regulation of acetylation during melatonin synthesis.. | |
| Protein Sequence | MTISNLLKQRVRYAPYLKKVKEAHELIPLFKNGQYLGWSGFTGVGTPKAVPEALIDHVEKNNLQGKLRFNLFVGASAGPEENRWAEHDMIIKRAPHQVGKPIAKAINQGRIEFFDKHLSMFPQDLTYGFYTRERKDNKILDYTIIEATAIKEDGSIVPGPSVGGSPEFITVSDKVIIEVNTATPSFEGIHDIDMPVNPPFRKPYPYLKVDDKCGVDSIPVDPEKVVAIVESTMRDQVPPNTPSDDMSRAIAGHLVEFFRNEVKHGRLPENLLPLQSGIGNIANAVIEGLAGAQFKHLTVWTEVLQDSFLDLFENGSLDYATATSVRLTEKGFDRAFANWENFKHRLCLRSQVVSNNPEMIRRLGVIAMNTPVEVDIYAHANSTNVNGSRMLNGLGGSADFLRNAKLSIMHAPSARPTKVDPTGISTIVPMASHVDQTEHDLDILVTDQGLADLRGLSPKERAREIINKCAHPDYQALLTDYLDRAEHYAKKHNCLHEPHMLKNAFKFHTNLAEKGTMKVDSWEPVD | |
| 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 |
|---|---|---|---|---|---|
| 2 | Blocked amino end (Thr) | ------MTISNLLKQ ------CCHHHHHHH | 32.87 | - | |
| 2 | Acetylation | ------MTISNLLKQ ------CCHHHHHHH | 32.87 | 1970569 | |
| 100 | Acetylation | RAPHQVGKPIAKAIN CCCHHCCHHHHHHHH | 34.10 | 25381059 | |
| 104 | Acetylation | QVGKPIAKAINQGRI HCCHHHHHHHHCCCC | 50.98 | 25381059 | |
| 241 | Phosphorylation | RDQVPPNTPSDDMSR CCCCCCCCCCHHHHH | 29.91 | 27214570 | |
| 263 | Acetylation | EFFRNEVKHGRLPEN HHHHHHHHCCCCCCC | 33.88 | 25381059 | |
| 298 | Phosphorylation | GAQFKHLTVWTEVLQ CCCCCCHHHHHHHHH | 17.45 | 29688323 | |
| 301 | Phosphorylation | FKHLTVWTEVLQDSF CCCHHHHHHHHHHHH | 16.33 | 29688323 | |
| 307 | Phosphorylation | WTEVLQDSFLDLFEN HHHHHHHHHHHHHHC | 18.10 | 29688323 | |
| 316 | Phosphorylation | LDLFENGSLDYATAT HHHHHCCCCCEEEEE | 29.64 | 29688323 | |
| 319 | Phosphorylation | FENGSLDYATATSVR HHCCCCCEEEEEEEE | 15.90 | 29688323 | |
| 321 | Phosphorylation | NGSLDYATATSVRLT CCCCCEEEEEEEECC | 25.00 | 29688323 | |
| 323 | Phosphorylation | SLDYATATSVRLTEK CCCEEEEEEEECCCC | 24.33 | 29688323 | |
| 324 | Phosphorylation | LDYATATSVRLTEKG CCEEEEEEEECCCCC | 11.63 | 29688323 | |
| 343 | Acetylation | FANWENFKHRLCLRS HCCHHHCCCHHHHHH | 39.12 | 24489116 | |
| 350 | Phosphorylation | KHRLCLRSQVVSNNP CCHHHHHHHHHHCCH | 17.87 | 28889911 | |
| 370 | Phosphorylation | LGVIAMNTPVEVDIY HCEEEECCCEEEEEE | 18.67 | 22369663 | |
| 377 | Phosphorylation | TPVEVDIYAHANSTN CCEEEEEEECCCCCC | 6.46 | 22369663 | |
| 382 | Phosphorylation | DIYAHANSTNVNGSR EEEECCCCCCCCCHH | 23.34 | 22369663 | |
| 383 | Phosphorylation | IYAHANSTNVNGSRM EEECCCCCCCCCHHC | 42.89 | 22369663 | |
| 388 | Phosphorylation | NSTNVNGSRMLNGLG CCCCCCCHHCCCCCC | 14.87 | 22369663 | |
| 459 | 2-Hydroxyisobutyrylation | DLRGLSPKERAREII HHCCCCHHHHHHHHH | 57.36 | - |
| 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 ACH1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ACH1_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 ACH1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Profiling phosphoproteins of yeast mitochondria reveals a role ofphosphorylation in assembly of the ATP synthase."; Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.; Mol. Cell. Proteomics 6:1896-1906(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, AND MASSSPECTROMETRY. | |