UniProt ID | TRPG_YEAST | |
---|---|---|
UniProt AC | P00937 | |
Protein Name | Multifunctional tryptophan biosynthesis protein | |
Gene Name | TRP3 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 484 | |
Subcellular Localization | ||
Protein Description | ||
Protein Sequence | MSVHAATNPINKHVVLIDNYDSFTWNVYEYLCQEGAKVSVYRNDAITVPEIAALNPDTLLISPGPGHPKTDSGISRDCIRYFTGKIPVFGICMGQQCMFDVFGGEVAYAGEIVHGKTSPISHDNCGIFKNVPQGIAVTRYHSLAGTESSLPSCLKVTASTENGIIMGVRHKKYTVEGVQFHPESILTEEGHLMIRNILNVSGGTWEENKSSPSNSILDRIYARRKIDVNEQSKIPGFTFQDLQSNYDLGLAPPLQDFYTVLSSSHKRAVVLAEVKRASPSKGPICLKAVAAEQALKYAEAGASAISVLTEPHWFHGSLQDLVNVRKILDLKFPPKERPCVLRKEFIFSKYQILEARLAGADTVLLIVKMLSQPLLKELYSYSKDLNMEPLVEVNSKEELQRALEIGAKVVGVNNRDLHSFNVDLNTTSNLVESIPKDVLLIALSGITTRDDAEKYKKEGVHGFLVGEALMKSTDVKKFIHELCE | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSVHAATNP ------CCCCCCCCC | 23.70 | 22369663 | |
7 | Phosphorylation | -MSVHAATNPINKHV -CCCCCCCCCCCCCE | 42.16 | 22369663 | |
117 | Phosphorylation | GEIVHGKTSPISHDN CEEECCCCCCCCCCC | 44.31 | 29136822 | |
118 | Phosphorylation | EIVHGKTSPISHDNC EEECCCCCCCCCCCC | 24.58 | 29136822 | |
121 | Phosphorylation | HGKTSPISHDNCGIF CCCCCCCCCCCCCCC | 28.33 | 29136822 | |
129 | Acetylation | HDNCGIFKNVPQGIA CCCCCCCCCCCCCEE | 55.93 | 22865919 | |
204 | Phosphorylation | ILNVSGGTWEENKSS EEECCCCCCCCCCCC | 32.98 | 22369663 | |
210 | Phosphorylation | GTWEENKSSPSNSIL CCCCCCCCCCCCHHH | 60.09 | 22369663 | |
211 | Phosphorylation | TWEENKSSPSNSILD CCCCCCCCCCCHHHH | 33.68 | 22369663 | |
213 | Phosphorylation | EENKSSPSNSILDRI CCCCCCCCCHHHHHH | 45.19 | 22369663 | |
215 | Phosphorylation | NKSSPSNSILDRIYA CCCCCCCHHHHHHHH | 28.94 | 22369663 | |
287 | Acetylation | SKGPICLKAVAAEQA CCCCCHHHHHHHHHH | 36.08 | 22865919 | |
343 | Acetylation | ERPCVLRKEFIFSKY CCCCEECCHHCCCHH | 53.46 | 22865919 | |
376 | Acetylation | MLSQPLLKELYSYSK HHCHHHHHHHHHHCC | 54.05 | 24489116 | |
380 | Phosphorylation | PLLKELYSYSKDLNM HHHHHHHHHCCCCCC | 35.24 | 19779198 | |
381 | Phosphorylation | LLKELYSYSKDLNME HHHHHHHHCCCCCCC | 13.24 | 19779198 | |
395 | Phosphorylation | EPLVEVNSKEELQRA CCCEECCCHHHHHHH | 46.77 | 19779198 | |
444 | Phosphorylation | DVLLIALSGITTRDD HHHHHHHCCCCCHHH | 21.08 | 28889911 |
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 TRPG_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TRPG_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 TRPG_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-2; SER-211 AND SER-444,AND MASS SPECTROMETRY. |