| UniProt ID | MPIP_YEAST | |
|---|---|---|
| UniProt AC | P23748 | |
| Protein Name | M-phase inducer phosphatase | |
| Gene Name | MIH1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 554 | |
| Subcellular Localization | ||
| Protein Description | Terminates the cell cycle delay. Reverses the CDC28 phosphorylation catalyzed by SWE1.. | |
| Protein Sequence | MNNIFHGTEDECANEDVLSFQKISLKSPFGKKKNIFRNVQTFFKSKSKHSNVDDDLINKENLAFDKSPLLTNHRSKEIDGPSPNIKQLGHRDELDENENENDDIVLSMHFASQTLQSPTRNSSRRSLTNNRDNDLLSRIKYPGSPQRSSSFSRSRSLSRKPSMNSSSNSSRRVQRQDGKIPRSSRKSSQKFSNITQNTLNFTSASSSPLAPNSVGVKCFESCLAKTQIPYYYDDRNSNDFFPRISPETLKNILQNNMCESFYNSCRIIDCRFEYEYTGGHIINSVNIHSRDELEYEFIHKVLHSDTSNNNTLPTLLIIHCEFSSHRGPSLASHLRNCDRIINQDHYPKLFYPDILILDGGYKAVFDNFPELCYPRQYVGMNSQENLLNCEQEMDKFRRESKRFATKNNSFRKLASPSNPNFFYRDSHQSSTTMASSALSFRFEPPPKLSLNHRRVSSGSSLNSSESTGDENFFPILSKSSMSSNSNLSTSHMLLMDGLDTPSYFSFEDERGNHQQVSGDEEQDGDFTFVGSDREDLPRPARRSLFPSLETEDKK | |
| 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 |
|---|---|---|---|---|---|
| 26 | Acetylation | SFQKISLKSPFGKKK CEEEEECCCCCCCCC | 49.66 | 22865919 | |
| 27 | Phosphorylation | FQKISLKSPFGKKKN EEEEECCCCCCCCCH | 30.65 | 21440633 | |
| 75 | Phosphorylation | PLLTNHRSKEIDGPS CCHHCCCCCCCCCCC | 27.39 | 21440633 | |
| 82 | Phosphorylation | SKEIDGPSPNIKQLG CCCCCCCCCCHHHCC | 35.79 | 28152593 | |
| 126 | Phosphorylation | TRNSSRRSLTNNRDN CCCCCCHHCCCCCCC | 38.13 | 22369663 | |
| 128 | Phosphorylation | NSSRRSLTNNRDNDL CCCCHHCCCCCCCCH | 31.52 | 22369663 | |
| 144 | Phosphorylation | SRIKYPGSPQRSSSF HHCCCCCCCCCCCCC | 17.23 | 21440633 | |
| 150 | Phosphorylation | GSPQRSSSFSRSRSL CCCCCCCCCCCCCCC | 28.61 | 21440633 | |
| 162 | Phosphorylation | RSLSRKPSMNSSSNS CCCCCCCCCCCCCCH | 33.36 | 30377154 | |
| 165 | Phosphorylation | SRKPSMNSSSNSSRR CCCCCCCCCCCHHHH | 26.88 | 30377154 | |
| 166 | Phosphorylation | RKPSMNSSSNSSRRV CCCCCCCCCCHHHHH | 28.65 | 30377154 | |
| 167 | Phosphorylation | KPSMNSSSNSSRRVQ CCCCCCCCCHHHHHH | 40.32 | 30377154 | |
| 169 | Phosphorylation | SMNSSSNSSRRVQRQ CCCCCCCHHHHHHHH | 27.46 | 30377154 | |
| 203 | Phosphorylation | QNTLNFTSASSSPLA HHCCCCCCCCCCCCC | 23.24 | 21440633 | |
| 205 | Phosphorylation | TLNFTSASSSPLAPN CCCCCCCCCCCCCCC | 30.99 | 21440633 | |
| 206 | Phosphorylation | LNFTSASSSPLAPNS CCCCCCCCCCCCCCC | 35.37 | 21440633 | |
| 207 | Phosphorylation | NFTSASSSPLAPNSV CCCCCCCCCCCCCCC | 22.80 | 21440633 | |
| 348 | Ubiquitination | INQDHYPKLFYPDIL CCCCCCCHHHCCCEE | 44.02 | 17644757 | |
| 362 | Ubiquitination | LILDGGYKAVFDNFP EEECCCHHHHHCCCH | 41.15 | 17644757 | |
| 377 | Phosphorylation | ELCYPRQYVGMNSQE HHCCCHHHCCCCCHH | 10.55 | 28889911 | |
| 382 | Phosphorylation | RQYVGMNSQENLLNC HHHCCCCCHHHHHCH | 29.94 | 20377248 | |
| 406 | Ubiquitination | ESKRFATKNNSFRKL HHHHHHCCCCHHHHC | 51.18 | 23749301 | |
| 409 | Phosphorylation | RFATKNNSFRKLASP HHHCCCCHHHHCCCC | 35.50 | 23749301 | |
| 412 | Ubiquitination | TKNNSFRKLASPSNP CCCCHHHHCCCCCCC | 46.52 | 23749301 | |
| 415 | Phosphorylation | NSFRKLASPSNPNFF CHHHHCCCCCCCCCC | 39.02 | 29136822 | |
| 417 | Phosphorylation | FRKLASPSNPNFFYR HHHCCCCCCCCCCCC | 63.52 | 24930733 | |
| 429 | Phosphorylation | FYRDSHQSSTTMASS CCCCCCCCCCCCCCC | 24.99 | 28889911 | |
| 457 | Phosphorylation | LNHRRVSSGSSLNSS CCCCCCCCCCCCCCC | 39.58 | 19779198 | |
| 459 | Phosphorylation | HRRVSSGSSLNSSES CCCCCCCCCCCCCCC | 33.33 | 28889911 | |
| 464 | Phosphorylation | SGSSLNSSESTGDEN CCCCCCCCCCCCCCC | 34.20 | 28889911 | |
| 466 | Phosphorylation | SSLNSSESTGDENFF CCCCCCCCCCCCCCH | 39.37 | 28889911 | |
| 517 | Phosphorylation | RGNHQQVSGDEEQDG CCCCCCCCCCCCCCC | 35.87 | 28889911 | |
| 531 | Phosphorylation | GDFTFVGSDREDLPR CCEEEECCCHHHCCC | 28.35 | 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 MPIP_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MPIP_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 MPIP_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-382 AND SER-417, ANDMASS 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-417, AND MASSSPECTROMETRY. | |