| UniProt ID | ACS2_YEAST | |
|---|---|---|
| UniProt AC | P52910 | |
| Protein Name | Acetyl-coenzyme A synthetase 2 | |
| Gene Name | ACS2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 683 | |
| Subcellular Localization | Cytoplasm. Nucleus. Predominantly nuclear. | |
| Protein Description | Catalyzes the production of acetyl-CoA. Provides the acetyl-CoA source for histone acetylation in the nucleus. "Anaerobic" isozyme of acetyl-coenzyme A synthetase, which is required for growth on fermentable carbon sources such as glucose. May be involved in the PDH (pyruvate dehydrogenase complex) bypass.. | |
| Protein Sequence | MTIKEHKVVYEAHNVKALKAPQHFYNSQPGKGYVTDMQHYQEMYQQSINEPEKFFDKMAKEYLHWDAPYTKVQSGSLNNGDVAWFLNGKLNASYNCVDRHAFANPDKPALIYEADDESDNKIITFGELLRKVSQIAGVLKSWGVKKGDTVAIYLPMIPEAVIAMLAVARIGAIHSVVFAGFSAGSLKDRVVDANSKVVITCDEGKRGGKTINTKKIVDEGLNGVDLVSRILVFQRTGTEGIPMKAGRDYWWHEEAAKQRTYLPPVSCDAEDPLFLLYTSGSTGSPKGVVHTTGGYLLGAALTTRYVFDIHPEDVLFTAGDVGWITGHTYALYGPLTLGTASIIFESTPAYPDYGRYWRIIQRHKATHFYVAPTALRLIKRVGEAEIAKYDTSSLRVLGSVGEPISPDLWEWYHEKVGNKNCVICDTMWQTESGSHLIAPLAGAVPTKPGSATVPFFGINACIIDPVTGVELEGNDVEGVLAVKSPWPSMARSVWNHHDRYMDTYLKPYPGHYFTGDGAGRDHDGYYWIRGRVDDVVNVSGHRLSTSEIEASISNHENVSEAAVVGIPDELTGQTVVAYVSLKDGYLQNNATEGDAEHITPDNLRRELILQVRGEIGPFASPKTIILVRDLPRTRSGKIMRRVLRKVASNEAEQLGDLTTLANPEVVPAIISAVENQFFSQKKK | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
|
|
||
* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 7 | Ubiquitination | -MTIKEHKVVYEAHN -CCCCCCEEEEEECC | 34.19 | 17644757 | |
| 7 | Acetylation | -MTIKEHKVVYEAHN -CCCCCCEEEEEECC | 34.19 | 22865919 | |
| 16 | Acetylation | VYEAHNVKALKAPQH EEEECCCCEECCCCC | 54.01 | 22865919 | |
| 16 | Ubiquitination | VYEAHNVKALKAPQH EEEECCCCEECCCCC | 54.01 | 17644757 | |
| 19 | Acetylation | AHNVKALKAPQHFYN ECCCCEECCCCCCCC | 63.98 | 24489116 | |
| 19 | Ubiquitination | AHNVKALKAPQHFYN ECCCCEECCCCCCCC | 63.98 | 17644757 | |
| 27 | Phosphorylation | APQHFYNSQPGKGYV CCCCCCCCCCCCCCC | 26.77 | 21440633 | |
| 31 | Ubiquitination | FYNSQPGKGYVTDMQ CCCCCCCCCCCCCHH | 54.47 | 17644757 | |
| 33 | Phosphorylation | NSQPGKGYVTDMQHY CCCCCCCCCCCHHHH | 12.03 | 27017623 | |
| 35 | Phosphorylation | QPGKGYVTDMQHYQE CCCCCCCCCHHHHHH | 19.78 | 27017623 | |
| 44 | Phosphorylation | MQHYQEMYQQSINEP HHHHHHHHHHHCCCH | 11.57 | 27017623 | |
| 53 | Ubiquitination | QSINEPEKFFDKMAK HHCCCHHHHHHHHHH | 63.14 | 17644757 | |
| 53 | Acetylation | QSINEPEKFFDKMAK HHCCCHHHHHHHHHH | 63.14 | 24489116 | |
| 57 | Ubiquitination | EPEKFFDKMAKEYLH CHHHHHHHHHHHHHC | 35.28 | 17644757 | |
| 57 | Acetylation | EPEKFFDKMAKEYLH CHHHHHHHHHHHHHC | 35.28 | 24489116 | |
| 60 | Ubiquitination | KFFDKMAKEYLHWDA HHHHHHHHHHHCCCC | 43.31 | 17644757 | |
| 60 | Acetylation | KFFDKMAKEYLHWDA HHHHHHHHHHHCCCC | 43.31 | 24489116 | |
| 71 | Ubiquitination | HWDAPYTKVQSGSLN CCCCCCCCCCCCCCC | 32.22 | 17644757 | |
| 89 | Ubiquitination | VAWFLNGKLNASYNC EEEEECCEECCCEEC | 37.18 | 17644757 | |
| 107 | Acetylation | HAFANPDKPALIYEA HHHCCCCCCEEEEEC | 33.19 | 22865919 | |
| 107 | Ubiquitination | HAFANPDKPALIYEA HHHCCCCCCEEEEEC | 33.19 | 17644757 | |
| 121 | Ubiquitination | ADDESDNKIITFGEL CCCCCCCCEEEHHHH | 40.24 | 17644757 | |
| 131 | Ubiquitination | TFGELLRKVSQIAGV EHHHHHHHHHHHHHH | 46.32 | 17644757 | |
| 140 | Ubiquitination | SQIAGVLKSWGVKKG HHHHHHHHHCCCCCC | 41.58 | 17644757 | |
| 153 | Phosphorylation | KGDTVAIYLPMIPEA CCCEEEEECCCCHHH | 8.60 | 24909858 | |
| 187 | Ubiquitination | GFSAGSLKDRVVDAN CCCCCCHHHCEECCC | 45.23 | 17644757 | |
| 196 | Ubiquitination | RVVDANSKVVITCDE CEECCCCCEEEECCC | 40.09 | 17644757 | |
| 205 | Ubiquitination | VITCDEGKRGGKTIN EEECCCCCCCCEEEC | 45.91 | 23749301 | |
| 205 | Acetylation | VITCDEGKRGGKTIN EEECCCCCCCCEEEC | 45.91 | 22865919 | |
| 209 | Ubiquitination | DEGKRGGKTINTKKI CCCCCCCEEECHHHH | 49.40 | 22817900 | |
| 209 | 2-Hydroxyisobutyrylation | DEGKRGGKTINTKKI CCCCCCCEEECHHHH | 49.40 | - | |
| 214 | Ubiquitination | GGKTINTKKIVDEGL CCEEECHHHHHCCCC | 35.69 | 17644757 | |
| 214 | 2-Hydroxyisobutyrylation | GGKTINTKKIVDEGL CCEEECHHHHHCCCC | 35.69 | - | |
| 215 | Ubiquitination | GKTINTKKIVDEGLN CEEECHHHHHCCCCC | 46.02 | 17644757 | |
| 215 | Acetylation | GKTINTKKIVDEGLN CEEECHHHHHCCCCC | 46.02 | 24489116 | |
| 236 | Phosphorylation | RILVFQRTGTEGIPM EEEEEECCCCCCCCC | 37.36 | 22369663 | |
| 238 | Phosphorylation | LVFQRTGTEGIPMKA EEEECCCCCCCCCCC | 30.35 | 22369663 | |
| 244 | Ubiquitination | GTEGIPMKAGRDYWW CCCCCCCCCCCCCCC | 42.19 | 17644757 | |
| 257 | Acetylation | WWHEEAAKQRTYLPP CCCHHHHHCCCCCCC | 47.57 | 24489116 | |
| 257 | Ubiquitination | WWHEEAAKQRTYLPP CCCHHHHHCCCCCCC | 47.57 | 17644757 | |
| 284 | Phosphorylation | YTSGSTGSPKGVVHT EECCCCCCCCCEEEE | 24.43 | 21440633 | |
| 286 | Ubiquitination | SGSTGSPKGVVHTTG CCCCCCCCCEEEECC | 67.06 | 17644757 | |
| 291 | Phosphorylation | SPKGVVHTTGGYLLG CCCCEEEECCCHHHC | 18.61 | 25371407 | |
| 292 | Phosphorylation | PKGVVHTTGGYLLGA CCCEEEECCCHHHCH | 17.46 | 25371407 | |
| 364 | 2-Hydroxyisobutyrylation | WRIIQRHKATHFYVA HHHHHHCCCCCEEEC | 58.11 | - | |
| 364 | Ubiquitination | WRIIQRHKATHFYVA HHHHHHCCCCCEEEC | 58.11 | 17644757 | |
| 379 | Ubiquitination | PTALRLIKRVGEAEI HHHHHHHHHHCHHHH | 45.69 | 17644757 | |
| 388 | Ubiquitination | VGEAEIAKYDTSSLR HCHHHHEEECCCCCE | 49.69 | 23749301 | |
| 388 | Acetylation | VGEAEIAKYDTSSLR HCHHHHEEECCCCCE | 49.69 | 24489116 | |
| 415 | Ubiquitination | LWEWYHEKVGNKNCV HHHHHHHHHCCCCEE | 41.97 | 17644757 | |
| 488 | Phosphorylation | AVKSPWPSMARSVWN EEECCCHHHHHHHHH | 22.62 | 28889911 | |
| 500 | Phosphorylation | VWNHHDRYMDTYLKP HHHCHHHHHHCCCCC | 12.85 | 28889911 | |
| 504 | Phosphorylation | HDRYMDTYLKPYPGH HHHHHHCCCCCCCCC | 14.41 | 28889911 | |
| 506 | Acetylation | RYMDTYLKPYPGHYF HHHHCCCCCCCCCEE | 31.90 | 24489116 | |
| 506 | Ubiquitination | RYMDTYLKPYPGHYF HHHHCCCCCCCCCEE | 31.90 | 17644757 | |
| 539 | Phosphorylation | VDDVVNVSGHRLSTS ECCEEEECCCCCCHH | 24.55 | 27214570 | |
| 582 | Ubiquitination | VVAYVSLKDGYLQNN EEEEEEECCCCCCCC | 41.42 | 17644757 | |
| 599 | Phosphorylation | EGDAEHITPDNLRRE CCCHHHCCCCHHHHH | 26.88 | 28889911 | |
| 620 | Phosphorylation | GEIGPFASPKTIILV CCCCCCCCCCEEEEE | 27.58 | 22369663 | |
| 622 | Ubiquitination | IGPFASPKTIILVRD CCCCCCCCEEEEEEC | 50.27 | 17644757 | |
| 622 | Acetylation | IGPFASPKTIILVRD CCCCCCCCEEEEEEC | 50.27 | 24489116 | |
| 645 | Ubiquitination | IMRRVLRKVASNEAE HHHHHHHHHHCCHHH | 37.68 | 17644757 | |
| 648 | Phosphorylation | RVLRKVASNEAEQLG HHHHHHHCCHHHHHC | 37.88 | 27214570 | |
| 679 | Phosphorylation | AVENQFFSQKKK--- HHHHHHHHCCCC--- | 42.24 | 20190278 | |
| 681 | Ubiquitination | ENQFFSQKKK----- HHHHHHCCCC----- | 62.42 | 17644757 | |
| 682 | Ubiquitination | NQFFSQKKK------ HHHHHCCCC------ | 56.96 | 17644757 |
| 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 ACS2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ACS2_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 ACS2_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| 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-620 AND SER-679, ANDMASS SPECTROMETRY. | |
| 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-506, AND MASSSPECTROMETRY. | |
