| UniProt ID | MAK11_YEAST | |
|---|---|---|
| UniProt AC | P20484 | |
| Protein Name | Protein MAK11 | |
| Gene Name | MAK11 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 414 | |
| Subcellular Localization |
Nucleus, nucleolus . Nucleus membrane Peripheral membrane protein . Membrane associated. |
|
| Protein Description | Essential for cell growth. Plays a role in assembly of 60S pre-ribosomal particles in the nucleolus. Also required for replication of the M1 double-stranded RNA of the L-A virus. This latter function may reflect an enhanced requirement for free 60S ribosomal particles for the translation of viral mRNAs which lack poly-A tails.. | |
| Protein Sequence | MSAIGDKNQFRIIVGSYEHNILCLSLDIPNQKENDAAKTPHFMPIFHFQAHSLSIKCLAVSRRYLVSGSNDEHIRIYDLQKRKELGTLLSHQGSITALQFSHPASSSEDAAVSKGSKNSKWLLSASEDHKIMVWRVKDWETVGTLKGHTARVNDVDIHPTNRIAISVSDDHSIRLWNLMTLRNAAVLKLRKYNTNGTCVRWLGAKGDYFAVGLRDRVLIYETGSAKVFKEIVFQRKTLMHIETHILPFDNKEYLSVGISDGNVHFYPCEELFEKVEENEKQEDDDDKEDISPAFSLLGHTNRIKDFKFYTNEFGTYLVTIGSDGKIVVWDMSTKEQVAVYDCGERLNCLTLCDESIEKYNTMKKRDAETADIGDQSEVESDTEELKKIMFGEKKKLNKKKRKQLKKSKVSVELE | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
|
|
||
* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MSAIGDKNQ ------CCCCCCCCC | 5.19 | 22814378 | |
| 35 | Phosphorylation | IPNQKENDAAKTPHF CCCCCCCCCCCCCCC | 35.65 | 19823750 | |
| 69 | Phosphorylation | RRYLVSGSNDEHIRI EEEEECCCCCCCEEE | 17.69 | 30377154 | |
| 137 | Acetylation | KIMVWRVKDWETVGT CEEEEEECCCEEEEE | 65.41 | 24489116 | |
| 280 | Acetylation | EKVEENEKQEDDDDK HHHHHHHCCCCCCCC | 50.32 | 24489116 | |
| 369 | Phosphorylation | MKKRDAETADIGDQS CCCCCCCCCCCCCHH | 21.00 | 22890988 | |
| 376 | Phosphorylation | TADIGDQSEVESDTE CCCCCCHHHCCCCHH | 39.06 | 22369663 | |
| 380 | Phosphorylation | GDQSEVESDTEELKK CCHHHCCCCHHHHHH | 3.55 | 22369663 | |
| 382 | Phosphorylation | QSEVESDTEELKKIM HHHCCCCHHHHHHHH | 4.01 | 22369663 | |
| 407 | Phosphorylation | KRKQLKKSKVSVELE HHHHHHHHCCCEECC | 56.65 | 24961812 | |
| 410 | Phosphorylation | QLKKSKVSVELE--- HHHHHCCCEECC--- | 5.08 | 24961812 | |
| 423 | Phosphorylation | ---------------- ---------------- | 31.20 | 15665377 | |
| 430 | Phosphorylation | ----------------------- ----------------------- | 48.64 | 22369663 | |
| 434 | Phosphorylation | --------------------------- --------------------------- | 55.82 | 22369663 | |
| 436 | Phosphorylation | ----------------------------- ----------------------------- | 40.41 | 25521595 | |
| 464 | Phosphorylation | --------------------------------------------------------- --------------------------------------------------------- | 17.38 | 24961812 |
| 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 MAK11_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MAK11_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 MAK11_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| 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-430; SER-434 ANDTHR-436, 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-430 AND SER-434, 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-430 AND SER-434, ANDMASS SPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-423 AND SER-430, ANDMASS SPECTROMETRY. | |
