| UniProt ID | PMM_YEAST | |
|---|---|---|
| UniProt AC | P07283 | |
| Protein Name | Phosphomannomutase | |
| Gene Name | SEC53 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 254 | |
| Subcellular Localization | Cytoplasm. | |
| Protein Description | Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.. | |
| Protein Sequence | MSIAEFAYKEKPETLVLFDVDGTLTPARLTVSEEVRKTLAKLRNKCCIGFVGGSDLSKQLEQLGPNVLDEFDYSFSENGLTAYRLGKELASQSFINWLGEEKYNKLAVFILRYLSEIDLPKRRGTFLEFRNGMINVSPIGRNASTEERNEFERYDKEHQIRAKFVEALKKEFPDYGLTFSIGGQISFDVFPAGWDKTYCLQHVEKDGFKEIHFFGDKTMVGGNDYEIFVDERTIGHSVQSPDDTVKILTELFNL | |
| 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 | ------MSIAEFAYK ------CCHHHHCCC | 30.42 | 22369663 | |
| 8 | Phosphorylation | MSIAEFAYKEKPETL CCHHHHCCCCCCCEE | 25.63 | 22369663 | |
| 23 | Phosphorylation | VLFDVDGTLTPARLT EEEECCCCCCCEEEE | 24.01 | 29136822 | |
| 25 | Phosphorylation | FDVDGTLTPARLTVS EECCCCCCCEEEECC | 18.10 | 27214570 | |
| 32 | Phosphorylation | TPARLTVSEEVRKTL CCEEEECCHHHHHHH | 23.86 | 27214570 | |
| 45 | Ubiquitination | TLAKLRNKCCIGFVG HHHHHHHCCEEEEEC | 24.85 | 23749301 | |
| 54 | Phosphorylation | CIGFVGGSDLSKQLE EEEEECHHHHHHHHH | 29.47 | 28152593 | |
| 57 | Phosphorylation | FVGGSDLSKQLEQLG EECHHHHHHHHHHHC | 24.28 | 27017623 | |
| 87 | Acetylation | LTAYRLGKELASQSF CCHHHHHHHHHHHHH | 54.89 | 24489116 | |
| 91 | Phosphorylation | RLGKELASQSFINWL HHHHHHHHHHHHHHH | 38.69 | 27017623 | |
| 102 | Acetylation | INWLGEEKYNKLAVF HHHHCHHHHHHHHHH | 50.23 | 24489116 | |
| 105 | Acetylation | LGEEKYNKLAVFILR HCHHHHHHHHHHHHH | 34.43 | 24489116 | |
| 115 | Phosphorylation | VFILRYLSEIDLPKR HHHHHHHHHCCCCCC | 24.46 | 27214570 | |
| 121 | Acetylation | LSEIDLPKRRGTFLE HHHCCCCCCCCCCEE | 63.12 | 24489116 | |
| 125 | Phosphorylation | DLPKRRGTFLEFRNG CCCCCCCCCEEECCC | 24.20 | 27214570 | |
| 137 | Phosphorylation | RNGMINVSPIGRNAS CCCEEEECCCCCCCC | 13.30 | 27214570 | |
| 156 | Acetylation | NEFERYDKEHQIRAK HHHHHHCHHHHHHHH | 48.43 | 24489116 | |
| 163 | Acetylation | KEHQIRAKFVEALKK HHHHHHHHHHHHHHH | 39.84 | 24489116 | |
| 169 | Succinylation | AKFVEALKKEFPDYG HHHHHHHHHHCCCCC | 58.25 | 23954790 | |
| 205 | Acetylation | YCLQHVEKDGFKEIH EEEHHHHHCCCEEEE | 63.16 | 24489116 | |
| 209 | Acetylation | HVEKDGFKEIHFFGD HHHHCCCEEEEEECC | 62.38 | 24489116 | |
| 225 | Phosphorylation | TMVGGNDYEIFVDER EEECCCEEEEEEECC | 18.22 | 21440633 | |
| 233 | Phosphorylation | EIFVDERTIGHSVQS EEEEECCCCCCCCCC | 29.30 | 21440633 | |
| 237 | Phosphorylation | DERTIGHSVQSPDDT ECCCCCCCCCCHHHH | 19.35 | 22369663 | |
| 240 | Phosphorylation | TIGHSVQSPDDTVKI CCCCCCCCHHHHHHH | 28.30 | 22369663 | |
| 244 | Phosphorylation | SVQSPDDTVKILTEL CCCCHHHHHHHHHHH | 30.95 | 22369663 | |
| 246 | Ubiquitination | QSPDDTVKILTELFN CCHHHHHHHHHHHHC | 33.81 | 23749301 |
| 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 PMM_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PMM_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 PMM_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-2; SER-54 AND SER-240,AND MASS SPECTROMETRY. | |
| "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 SER-240, 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 SER-240, AND MASSSPECTROMETRY. | |
