| UniProt ID | DPH5_YEAST | |
|---|---|---|
| UniProt AC | P32469 | |
| Protein Name | Diphthine methyl ester synthase | |
| Gene Name | DPH5 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 300 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | S-adenosyl-L-methionine-dependent methyltransferase that catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester. The four successive methylation reactions represent the second step of diphthamide biosynthesis.. | |
| Protein Sequence | MLYLIGLGLSYKSDITVRGLEAIKKCSRVYLEHYTSILMAASQEELESYYGKEIILADRELVETGSKQILNNADKEDVAFLVVGDPFGATTHTDLVLRAKREAIPVEIIHNASVMNAVGACGLQLYNFGQTVSMVFFTDNWRPDSWYDKIWENRKIGLHTLVLLDIKVKEQSIENMARGRLIYEPPRYMSIAQCCEQLLEIEEKRGTKAYTPDTPAVAISRLGSSSQSFKSGTISELANYDSGEPLHSLVILGRQCHELELEYLLEFADDKEKFGKDVANDQEYFKPAAWVPPTEDDSDE | |
| 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 |
|---|---|---|---|---|---|
| 3 | Phosphorylation | -----MLYLIGLGLS -----CEEEEECCCC | 8.58 | 28889911 | |
| 169 | 2-Hydroxyisobutyrylation | VLLDIKVKEQSIENM EEEEEEECHHHHHHH | 45.06 | - | |
| 172 | Phosphorylation | DIKVKEQSIENMARG EEEECHHHHHHHHCC | 32.72 | 25752575 | |
| 208 | Ubiquitination | IEEKRGTKAYTPDTP HHHHHCCCCCCCCCC | 42.07 | 23749301 | |
| 211 | Phosphorylation | KRGTKAYTPDTPAVA HHCCCCCCCCCCCEE | 21.39 | 25752575 | |
| 224 | Phosphorylation | VAISRLGSSSQSFKS EEEHHCCCCCCCCCC | 31.26 | 22369663 | |
| 225 | Phosphorylation | AISRLGSSSQSFKSG EEHHCCCCCCCCCCC | 30.51 | 22369663 | |
| 226 | Phosphorylation | ISRLGSSSQSFKSGT EHHCCCCCCCCCCCC | 31.38 | 22369663 | |
| 228 | Phosphorylation | RLGSSSQSFKSGTIS HCCCCCCCCCCCCHH | 36.27 | 22369663 | |
| 284 | Phosphorylation | DVANDQEYFKPAAWV CCCCCCCCCCCCCCC | 15.98 | 22369663 | |
| 294 | Phosphorylation | PAAWVPPTEDDSDE- CCCCCCCCCCCCCC- | 46.07 | 22369663 | |
| 298 | Phosphorylation | VPPTEDDSDE----- CCCCCCCCCC----- | 56.83 | 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 DPH5_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DPH5_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 DPH5_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 SER-172 AND SER-298, ANDMASS SPECTROMETRY. | |
| "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-298, AND MASSSPECTROMETRY. | |
