| UniProt ID | DHAS_YEAST | |
|---|---|---|
| UniProt AC | P13663 | |
| Protein Name | Aspartate-semialdehyde dehydrogenase | |
| Gene Name | HOM2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 365 | |
| Subcellular Localization | ||
| Protein Description | Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.. | |
| Protein Sequence | MAGKKIAGVLGATGSVGQRFILLLANHPHFELKVLGASSRSAGKKYVDAVNWKQTDLLPESATDIIVSECKSEFFKECDIVFSGLDADYAGAIEKEFMEAGIAIVSNAKNYRREQDVPLIVPVVNPEHLDIVAQKLDTAKAQGKPRPGFIICISNCSTAGLVAPLKPLIEKFGPIDALTTTTLQAISGAGFSPGVPGIDILDNIIPYIGGEEDKMEWETKKILAPLAEDKTHVKLLTPEEIKVSAQCNRVAVSDGHTECISLRFKNRPAPSVEQVKTCLKEYVCDAYKLGCHSAPKQTIHVLEQPDRPQPRLDRNRDSGYGVSVGRIREDPLLDFKMVVLSHNTIIGAAGSGVLIAEILLARNLI | |
| 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 |
|---|---|---|---|---|---|
| 13 | Phosphorylation | IAGVLGATGSVGQRF CCHHHCCCCCHHHHH | 28.35 | 28889911 | |
| 15 | Phosphorylation | GVLGATGSVGQRFIL HHHCCCCCHHHHHHH | 20.79 | 19779198 | |
| 38 | Phosphorylation | ELKVLGASSRSAGKK EEEECCCCCCCCCCC | 25.20 | 22369663 | |
| 39 | Phosphorylation | LKVLGASSRSAGKKY EEECCCCCCCCCCCC | 29.71 | 22369663 | |
| 45 | Acetylation | SSRSAGKKYVDAVNW CCCCCCCCCCCCCCH | 49.98 | 24489116 | |
| 135 | Acetylation | HLDIVAQKLDTAKAQ HHHHHHHHHHHHHHC | 38.30 | 24489116 | |
| 135 | Ubiquitination | HLDIVAQKLDTAKAQ HHHHHHHHHHHHHHC | 38.30 | 24961812 | |
| 140 | Acetylation | AQKLDTAKAQGKPRP HHHHHHHHHCCCCCC | 43.25 | 25381059 | |
| 230 | Acetylation | LAPLAEDKTHVKLLT HHHHHCCCCEEEECC | 31.84 | 24489116 | |
| 234 | Acetylation | AEDKTHVKLLTPEEI HCCCCEEEECCHHHH | 30.12 | 24489116 | |
| 242 | Acetylation | LLTPEEIKVSAQCNR ECCHHHHHHEEECCE | 33.16 | 24489116 | |
| 242 | Ubiquitination | LLTPEEIKVSAQCNR ECCHHHHHHEEECCE | 33.16 | 23749301 | |
| 253 | Phosphorylation | QCNRVAVSDGHTECI ECCEEEEECCCCEEE | 28.30 | 23749301 | |
| 265 | Ubiquitination | ECISLRFKNRPAPSV EEEEEEECCCCCCCH | 45.68 | 23749301 | |
| 265 | Acetylation | ECISLRFKNRPAPSV EEEEEEECCCCCCCH | 45.68 | 22865919 | |
| 271 | Phosphorylation | FKNRPAPSVEQVKTC ECCCCCCCHHHHHHH | 40.15 | 23749301 | |
| 276 | Ubiquitination | APSVEQVKTCLKEYV CCCHHHHHHHHHHHH | 32.96 | 22817900 | |
| 276 | Acetylation | APSVEQVKTCLKEYV CCCHHHHHHHHHHHH | 32.96 | 25381059 | |
| 280 | Ubiquitination | EQVKTCLKEYVCDAY HHHHHHHHHHHHHHH | 49.50 | 22817900 | |
| 280 | Acetylation | EQVKTCLKEYVCDAY HHHHHHHHHHHHHHH | 49.50 | 24489116 | |
| 288 | Acetylation | EYVCDAYKLGCHSAP HHHHHHHHCCCCCCC | 39.87 | 24489116 | |
| 318 | Phosphorylation | RLDRNRDSGYGVSVG CCCCCCCCCCCCCCC | 30.58 | 22369663 | |
| 320 | Phosphorylation | DRNRDSGYGVSVGRI CCCCCCCCCCCCCCC | 20.50 | 22369663 | |
| 323 | Phosphorylation | RDSGYGVSVGRIRED CCCCCCCCCCCCCCC | 17.94 | 22890988 |
| 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 DHAS_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DHAS_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 DHAS_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-13; SER-318 AND TYR-320,AND MASS SPECTROMETRY. | |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-318, AND MASSSPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-318, AND MASSSPECTROMETRY. | |
