UniProt ID | IDI1_YEAST | |
---|---|---|
UniProt AC | P15496 | |
Protein Name | Isopentenyl-diphosphate Delta-isomerase | |
Gene Name | IDI1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 288 | |
Subcellular Localization | Cytoplasm. | |
Protein Description | Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).. | |
Protein Sequence | MTADNNSMPHGAVSSYAKLVQNQTPEDILEEFPEIIPLQQRPNTRSSETSNDESGETCFSGHDEEQIKLMNENCIVLDWDDNAIGAGTKKVCHLMENIEKGLLHRAFSVFIFNEQGELLLQQRATEKITFPDLWTNTCCSHPLCIDDELGLKGKLDDKIKGAITAAVRKLDHELGIPEDETKTRGKFHFLNRIHYMAPSNEPWGEHEIDYILFYKINAKENLTVNPNVNEVRDFKWVSPNDLKTMFADPSYKFTPWFKIICENYLFNWWEQLDDLSEVENDRQIHRML | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MTADNNSMP ------CCCCCCCCC | 42.59 | 22369663 | |
7 | Phosphorylation | -MTADNNSMPHGAVS -CCCCCCCCCCCHHH | 39.69 | 22369663 | |
14 | Phosphorylation | SMPHGAVSSYAKLVQ CCCCCHHHHHHHHHC | 19.66 | 22369663 | |
15 | Phosphorylation | MPHGAVSSYAKLVQN CCCCHHHHHHHHHCC | 23.63 | 22369663 | |
16 | Phosphorylation | PHGAVSSYAKLVQNQ CCCHHHHHHHHHCCC | 10.55 | 22369663 | |
24 | Phosphorylation | AKLVQNQTPEDILEE HHHHCCCCHHHHHHH | 35.87 | 17563356 | |
46 | Phosphorylation | QQRPNTRSSETSNDE CCCCCCCCCCCCCCC | 30.41 | 19779198 | |
49 | Phosphorylation | PNTRSSETSNDESGE CCCCCCCCCCCCCCC | 34.47 | 28889911 | |
50 | Phosphorylation | NTRSSETSNDESGET CCCCCCCCCCCCCCC | 37.93 | 17330950 | |
57 | Phosphorylation | SNDESGETCFSGHDE CCCCCCCCCCCCCCH | 23.52 | 28889911 | |
60 | Phosphorylation | ESGETCFSGHDEEQI CCCCCCCCCCCHHHH | 37.05 | 25315811 | |
100 | Acetylation | HLMENIEKGLLHRAF HHHHHHHHCHHHHHH | 51.57 | 24489116 | |
169 | Ubiquitination | AITAAVRKLDHELGI HHHHHHHHHHHHHCC | 52.23 | 23749301 | |
169 | Acetylation | AITAAVRKLDHELGI HHHHHHHHHHHHHCC | 52.23 | 24489116 | |
182 | Acetylation | GIPEDETKTRGKFHF CCCCCCCCCCCCEEE | 33.89 | 24489116 | |
186 | Acetylation | DETKTRGKFHFLNRI CCCCCCCCEEECCCE | 32.16 | 24489116 | |
219 | Ubiquitination | LFYKINAKENLTVNP EEEEECCCCCEEECC | 42.52 | 23749301 | |
235 | Acetylation | VNEVRDFKWVSPNDL CCCCEECEEECHHHH | 51.48 | 24489116 | |
243 | Ubiquitination | WVSPNDLKTMFADPS EECHHHHHHHCCCCC | 40.58 | 23749301 | |
243 | Acetylation | WVSPNDLKTMFADPS EECHHHHHHHCCCCC | 40.58 | 24489116 | |
252 | Ubiquitination | MFADPSYKFTPWFKI HCCCCCCCCCHHHHH | 47.28 | 23749301 | |
252 | Acetylation | MFADPSYKFTPWFKI HCCCCCCCCCHHHHH | 47.28 | 24489116 |
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 IDI1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of IDI1_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 IDI1_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-7, AND MASSSPECTROMETRY. | |
"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 THR-24, AND MASSSPECTROMETRY. |