UniProt ID | PURA_YEAST | |
---|---|---|
UniProt AC | P80210 | |
Protein Name | Adenylosuccinate synthetase {ECO:0000255|HAMAP-Rule:MF_03125} | |
Gene Name | ADE12 {ECO:0000255|HAMAP-Rule:MF_03125} | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 433 | |
Subcellular Localization | Cytoplasm . | |
Protein Description | Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.. | |
Protein Sequence | MVNVVLGSQWGDEGKGKLVDLLVGKYDIVARCAGGNNAGHTIVVDGVKYDFHMLPSGLVNPNCQNLLGNGVVIHVPSFFKELETLEAKGLKNARSRLFVSSRAHLVFDFHQVTDKLRELELSGRSKDGKNIGTTGKGIGPTYSTKASRSGLRVHHLVNDQPGAWEEFVARYKRLLETRRQRYGDFEYDFEAKLAEYKKLREQLKPFVVDSVVFMHNAIEAKKKILVEGANALMLDIDFGTYPYVTSSNTGIGGVLTGLGIPPRTIDEIYGVVKAYTTRVGEGPFPTEQLNENGEKLQTIGAEFGVTTGRKRRCGWLDLVVLKYSTLINGYTSLNITKLDVLDTFKEIPVGISYSIQGKKLDLFPEDLNILGKVEVEYKVLPGWDQDITKITKYEDLPENAKKYLKYIEDFVGVPVEWVGTGPARESMLHKEIK | |
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 |
---|---|---|---|---|---|
17 | Acetylation | WGDEGKGKLVDLLVG CCCCCCCHHHHHHCC | 49.15 | 24489116 | |
25 | Acetylation | LVDLLVGKYDIVARC HHHHHCCCCEEEEEE | 32.07 | 24489116 | |
88 | Acetylation | ELETLEAKGLKNARS HHHHHHHCCCCCHHH | 56.23 | 24489116 | |
115 | Acetylation | DFHQVTDKLRELELS EHHHHHHHHHHHHHC | 39.83 | 24489116 | |
122 | Phosphorylation | KLRELELSGRSKDGK HHHHHHHCCCCCCCC | 23.84 | 28889911 | |
125 | Phosphorylation | ELELSGRSKDGKNIG HHHHCCCCCCCCCCC | 38.33 | 24961812 | |
141 | Phosphorylation | TGKGIGPTYSTKASR CCCCCCCCCCCCCCC | 25.54 | 21126336 | |
143 | Phosphorylation | KGIGPTYSTKASRSG CCCCCCCCCCCCCCC | 26.38 | 27214570 | |
145 | 2-Hydroxyisobutyrylation | IGPTYSTKASRSGLR CCCCCCCCCCCCCCE | 38.12 | - | |
197 | 2-Hydroxyisobutyrylation | EAKLAEYKKLREQLK HHHHHHHHHHHHHHC | 36.52 | - | |
275 | Phosphorylation | IYGVVKAYTTRVGEG HHHHHHHHCCCCCCC | 11.70 | 23607784 | |
276 | Phosphorylation | YGVVKAYTTRVGEGP HHHHHHHCCCCCCCC | 17.00 | 23607784 | |
277 | Phosphorylation | GVVKAYTTRVGEGPF HHHHHHCCCCCCCCC | 15.64 | 23607784 | |
286 | Phosphorylation | VGEGPFPTEQLNENG CCCCCCCHHHCCCCC | 36.42 | 23607784 | |
358 | 2-Hydroxyisobutyrylation | ISYSIQGKKLDLFPE EEEEECCEEEECCHH | 33.51 | - | |
378 | Acetylation | GKVEVEYKVLPGWDQ CEEEEEEEECCCCCC | 24.64 | 24489116 | |
389 | Acetylation | GWDQDITKITKYEDL CCCCCHHHHCCHHHC | 49.03 | 24489116 | |
392 | Acetylation | QDITKITKYEDLPEN CCHHHHCCHHHCCHH | 50.55 | 22865919 | |
392 | 2-Hydroxyisobutyrylation | QDITKITKYEDLPEN CCHHHHCCHHHCCHH | 50.55 | - | |
426 | Phosphorylation | GTGPARESMLHKEIK CCCCHHHHHHCHHCC | 22.53 | 21440633 |
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 PURA_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PURA_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 PURA_YEAST !! |
Kegg Drug | ||||||
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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-122 AND SER-143, ANDMASS SPECTROMETRY. |