UniProt ID | AK_YEAST | |
---|---|---|
UniProt AC | P10869 | |
Protein Name | Aspartokinase | |
Gene Name | HOM3 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 527 | |
Subcellular Localization | ||
Protein Description | ||
Protein Sequence | MPMDFQPTSSHSNWVVQKFGGTSVGKFPVQIVDDIVKHYSKPDGPNNNVAVVCSARSSYTKAEGTTSRLLKCCDLASQESEFQDIIEVIRQDHIDNADRFILNPALQAKLVDDTNKELELVKKYLNASKVLGEVSSRTVDLVMSCGEKLSCLFMTALCNDRGCKAKYVDLSHIVPSDFSASALDNSFYTFLVQALKEKLAPFVSAKERIVPVFTGFFGLVPTGLLNGVGRGYTDLCAALIAVAVNADELQVWKEVDGIFTADPRKVPEARLLDSVTPEEASELTYYGSEVIHPFTMEQVIRAKIPIRIKNVQNPLGNGTIIYPDNVAKKGESTPPHPPENLSSSFYEKRKRGATAITTKNDIFVINIHSNKKTLSHGFLAQIFTILDKYKLVVDLISTSEVHVSMALPIPDADSLKSLRQAEEKLRILGSVDITKKLSIVSLVGKHMKQYIGIAGTMFTTLAEEGINIEMISQGANEINISCVINESDSIKALQCIHAKLLSERTNTSNQFEHAIDERLEQLKRLGI | |
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 |
---|---|---|---|---|---|
18 | Ubiquitination | HSNWVVQKFGGTSVG CCCEEEEECCCCCCC | 34.07 | 17644757 | |
22 | Phosphorylation | VVQKFGGTSVGKFPV EEEECCCCCCCCCCE | 22.18 | 22369663 | |
23 | Phosphorylation | VQKFGGTSVGKFPVQ EEECCCCCCCCCCEE | 31.95 | 21440633 | |
26 | Acetylation | FGGTSVGKFPVQIVD CCCCCCCCCCEEEHH | 44.32 | 24489116 | |
26 | Ubiquitination | FGGTSVGKFPVQIVD CCCCCCCCCCEEEHH | 44.32 | 22817900 | |
37 | Ubiquitination | QIVDDIVKHYSKPDG EEHHHHHHHCCCCCC | 36.84 | 17644757 | |
61 | Ubiquitination | SARSSYTKAEGTTSR EECCCCCCCCCCHHH | 35.89 | 23749301 | |
67 | Phosphorylation | TKAEGTTSRLLKCCD CCCCCCHHHHHHHHH | 22.29 | 30377154 | |
109 | Acetylation | LNPALQAKLVDDTNK CCHHHHHHCCCCCHH | 35.76 | 22865919 | |
116 | Acetylation | KLVDDTNKELELVKK HCCCCCHHHHHHHHH | 66.81 | 24489116 | |
309 | Ubiquitination | AKIPIRIKNVQNPLG CCCCEEEECCCCCCC | 41.01 | 17644757 | |
328 | Ubiquitination | IYPDNVAKKGESTPP ECCCCCCCCCCCCCC | 57.96 | 17644757 | |
329 | Ubiquitination | YPDNVAKKGESTPPH CCCCCCCCCCCCCCC | 59.16 | 17644757 | |
332 | Phosphorylation | NVAKKGESTPPHPPE CCCCCCCCCCCCCCC | 55.68 | 22369663 | |
333 | Phosphorylation | VAKKGESTPPHPPEN CCCCCCCCCCCCCCC | 36.22 | 22369663 | |
342 | Phosphorylation | PHPPENLSSSFYEKR CCCCCCCCHHHHHHH | 35.20 | 22369663 | |
343 | Phosphorylation | HPPENLSSSFYEKRK CCCCCCCHHHHHHHH | 27.86 | 22369663 | |
344 | Phosphorylation | PPENLSSSFYEKRKR CCCCCCHHHHHHHHC | 28.59 | 22369663 | |
346 | Phosphorylation | ENLSSSFYEKRKRGA CCCCHHHHHHHHCCC | 23.61 | 22369663 | |
348 | Acetylation | LSSSFYEKRKRGATA CCHHHHHHHHCCCCE | 52.41 | 24489116 | |
354 | Phosphorylation | EKRKRGATAITTKND HHHHCCCCEEECCCC | 22.78 | 28889911 | |
357 | Phosphorylation | KRGATAITTKNDIFV HCCCCEEECCCCEEE | 29.29 | 28889911 | |
369 | Phosphorylation | IFVINIHSNKKTLSH EEEEEECCCCCEECH | 46.69 | 28889911 | |
373 | Phosphorylation | NIHSNKKTLSHGFLA EECCCCCEECHHHHH | 34.79 | 19823750 | |
375 | Phosphorylation | HSNKKTLSHGFLAQI CCCCCEECHHHHHHH | 27.13 | 19823750 | |
384 | Phosphorylation | GFLAQIFTILDKYKL HHHHHHHHHHHHHCH | 23.43 | 19823750 | |
435 | Acetylation | LGSVDITKKLSIVSL HCCCCCCCCCCHHHH | 52.64 | 24489116 | |
441 | Phosphorylation | TKKLSIVSLVGKHMK CCCCCHHHHHHHHHH | 18.70 | 28889911 | |
499 | Acetylation | ALQCIHAKLLSERTN HHHHHHHHHHHCCCC | 35.48 | 24489116 | |
502 | Phosphorylation | CIHAKLLSERTNTSN HHHHHHHHCCCCCCH | 35.15 | 21440633 | |
505 | Phosphorylation | AKLLSERTNTSNQFE HHHHHCCCCCCHHHH | 38.50 | 22369663 | |
507 | Phosphorylation | LLSERTNTSNQFEHA HHHCCCCCCHHHHHH | 28.57 | 22369663 | |
508 | Phosphorylation | LSERTNTSNQFEHAI HHCCCCCCHHHHHHH | 30.61 | 22369663 |
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 AK_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AK_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 AK_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 THR-333 AND SER-441, ANDMASS SPECTROMETRY. | |
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333, 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 THR-333, AND MASSSPECTROMETRY. |