| UniProt ID | MCK1_YEAST | |
|---|---|---|
| UniProt AC | P21965 | |
| Protein Name | Protein kinase MCK1 | |
| Gene Name | MCK1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 375 | |
| Subcellular Localization | ||
| Protein Description | May be an autophosphorylating tyrosine kinase, a bifunctional (serine/tyrosine-specific) protein kinase, or a serine kinase that is a substrate for an associated tyrosine kinase. MCK1 is a transcriptional activator of IME1, it stimulates spore maturation, and play a positive regulatory role in both mitotic centromere function and activation of early meiotic gene expression.. | |
| Protein Sequence | MSTEEQNGVPLQRGSEFIADDVTSNKSNNTRRMLVKEYRKIGRGAFGTVVQAYLTQDKKNWLGPFAIKKVPAHTEYKSRELQILRIADHPNIVKLQYFFTHLSPQDNKVYQHLAMECLPETLQIEINRYVTNKLEMPLKHIRLYTYQIARGMLYLHGLGVCHRDIKPSNVLVDPETGVLKICDFGSAKKLEHNQPSISYICSRFYRAPELIIGCTQYTTQIDIWGLGCVMGEMLIGKAIFQGQEPLLQLREIAKLLGPPDKRFIFFSNPAYDGPLFSKPLFSGSSQQRFEKYFGHSGPDGIDLLMKILVYEPQQRLSPRRILAHQFFNELRNDDTFLPRGFTEPIKLPNLFDFNDFELQILGEFADKIKPTKVAE | |
| 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 | Acetylation | ------MSTEEQNGV ------CCHHHHCCC | 44.52 | 22814378 | |
| 2 | Phosphorylation | ------MSTEEQNGV ------CCHHHHCCC | 44.52 | 28152593 | |
| 3 | Phosphorylation | -----MSTEEQNGVP -----CCHHHHCCCC | 42.09 | 28132839 | |
| 15 | Phosphorylation | GVPLQRGSEFIADDV CCCCCCCCCEECCCC | 31.36 | 29136822 | |
| 23 | Phosphorylation | EFIADDVTSNKSNNT CEECCCCCCCCCCCH | 33.31 | 22369663 | |
| 24 | Phosphorylation | FIADDVTSNKSNNTR EECCCCCCCCCCCHH | 41.95 | 22369663 | |
| 27 | Phosphorylation | DDVTSNKSNNTRRML CCCCCCCCCCHHHHH | 39.29 | 29136822 | |
| 30 | Phosphorylation | TSNKSNNTRRMLVKE CCCCCCCHHHHHHHH | 24.73 | 29136822 | |
| 36 | Acetylation | NTRRMLVKEYRKIGR CHHHHHHHHHHHHCC | 45.10 | 22865919 | |
| 48 | Phosphorylation | IGRGAFGTVVQAYLT HCCCCHHHHHHHHHC | 15.85 | 17563356 | |
| 58 | Acetylation | QAYLTQDKKNWLGPF HHHHCCCCCCCCCCC | 37.88 | 24489116 | |
| 94 | Acetylation | ADHPNIVKLQYFFTH CCCCCEEEEEEEECC | 26.52 | 24489116 | |
| 100 | Phosphorylation | VKLQYFFTHLSPQDN EEEEEEECCCCCCCC | 16.41 | 21440633 | |
| 103 | Phosphorylation | QYFFTHLSPQDNKVY EEEECCCCCCCCHHH | 16.95 | 28152593 | |
| 133 | Acetylation | INRYVTNKLEMPLKH HHHHHHCCCCCCCHH | 36.14 | 24489116 | |
| 166 | Ubiquitination | GVCHRDIKPSNVLVD CEECCCCCCCCEEEC | 46.84 | 23749301 | |
| 196 | Phosphorylation | KLEHNQPSISYICSR CCCCCCCCHHHHHHH | 17.88 | 22369663 | |
| 198 | Phosphorylation | EHNQPSISYICSRFY CCCCCCHHHHHHHHH | 16.87 | 22369663 | |
| 199 | Phosphorylation | HNQPSISYICSRFYR CCCCCHHHHHHHHHC | 12.32 | 22369663 | |
| 202 | Phosphorylation | PSISYICSRFYRAPE CCHHHHHHHHHCCCH | 18.83 | 22369663 | |
| 254 | Acetylation | LQLREIAKLLGPPDK HHHHHHHHHHCCCCC | 50.32 | 24489116 | |
| 282 | Phosphorylation | LFSKPLFSGSSQQRF CCCCCCCCCCCHHHH | 45.51 | 22369663 | |
| 284 | Phosphorylation | SKPLFSGSSQQRFEK CCCCCCCCCHHHHHH | 24.63 | 22369663 | |
| 285 | Phosphorylation | KPLFSGSSQQRFEKY CCCCCCCCHHHHHHH | 33.58 | 22369663 | |
| 291 | Acetylation | SSQQRFEKYFGHSGP CCHHHHHHHHCCCCC | 43.07 | 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 MCK1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MCK1_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 MCK1_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-24; SER-27; SER-196;SER-198; TYR-199 AND SER-202, 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-24; THR-48 AND SER-198,AND MASS 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 TYR-199, AND MASSSPECTROMETRY. | |
| "A proteomics approach to understanding protein ubiquitination."; Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.; Nat. Biotechnol. 21:921-926(2003). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-199, AND MASSSPECTROMETRY. | |
