| UniProt ID | RIO1_YEAST | |
|---|---|---|
| UniProt AC | Q12196 | |
| Protein Name | Serine/threonine-protein kinase RIO1 | |
| Gene Name | RIO1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 484 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | Required for the final endonucleolytic cleavage at site D converting 20S pre-rRNA into the mature 18S rRNA. Required for the final steps of cytoplasmic maturation of the 40S ribosomal subunit. The association with the very late 40S subunit intermediate seems to follow RIO2 association with precursors of the 40S subunit and may involve a translation-like checkpoint point cycle preceeding the binding to the 60S ribosomal subunit. Despite the protein kinase domain is proposed to act predominantly as an ATPase. The catalytic activity regulates its dynamic association with the 40S subunit. Has a role in the cell cycle where it is required for entrance into S-phase and in the control of the onset of anaphase. Appears to also be involved in the maintenance of chromosome stability and correct mitotic segregation.. | |
| Protein Sequence | MSLEDKFDSLSVSQGASDHINNQLLEKYSHKIKTDELSFSRAKTSKDKANRATVENVLDPRTMRFLKSMVTRGVIADLNGCLSTGKEANVYHAFAGTGKAPVIDEETGQYEVLETDGSRAEYAIKIYKTSILVFKDRERYVDGEFRFRNSRSQHNPRKMIKIWAEKEFRNLKRIYQSGVIPAPKPIEVKNNVLVMEFLSRGNGFASPKLKDYPYKNRDEIFHYYHTMVAYMRLLYQVCRLVHADLSEYNTIVHDDKLYMIDVSQSVEPEHPMSLDFLRMDIKNVNLYFEKMGISIFPERVIFQFVISETLEKFKGDYNNISALVAYIASNLPIKSTEQDEAEDEIFRSLHLVRSLGGLEERDFDRYTDGKFDLLKSLIAHDNERNFAASEQFEFDNADHECSSGTEEFSDDEEDGSSGSEEDDEEEGEYYDDDEPKVLKGKKHEDKDLKKLRKQEAKDAKREKRKTKVKKHIKKKLVKKTKSKK | |
| 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 | ------MSLEDKFDS ------CCHHHHCCC | 40.23 | 24961812 | |
| 38 | Phosphorylation | KIKTDELSFSRAKTS CCCCCCCCCCCCCCC | 21.09 | 23749301 | |
| 40 | Phosphorylation | KTDELSFSRAKTSKD CCCCCCCCCCCCCCH | 28.14 | 30377154 | |
| 226 | Phosphorylation | EIFHYYHTMVAYMRL HHHHHHHHHHHHHHH | 9.38 | 27017623 | |
| 230 | Phosphorylation | YYHTMVAYMRLLYQV HHHHHHHHHHHHHHH | 3.27 | 27017623 | |
| 246 | Phosphorylation | RLVHADLSEYNTIVH HHHCCCHHHCCEEEE | 38.28 | 27017623 | |
| 263 | Phosphorylation | KLYMIDVSQSVEPEH EEEEEECCCCCCCCC | 17.00 | 27017623 | |
| 273 | Phosphorylation | VEPEHPMSLDFLRMD CCCCCCCCCCEEECC | 29.27 | 27017623 | |
| 354 | Phosphorylation | RSLHLVRSLGGLEER HHHHHHHHCCCCCCC | 24.72 | 25752575 | |
| 402 | Phosphorylation | DNADHECSSGTEEFS CCCCCCCCCCCCCCC | 28.90 | 17725716 | |
| 403 | Phosphorylation | NADHECSSGTEEFSD CCCCCCCCCCCCCCC | 62.48 | 17725716 | |
| 409 | Phosphorylation | SSGTEEFSDDEEDGS CCCCCCCCCCCCCCC | 47.64 | 17725716 | |
| 416 | Phosphorylation | SDDEEDGSSGSEEDD CCCCCCCCCCCCCCC | 43.79 | 17725716 | |
| 417 | Phosphorylation | DDEEDGSSGSEEDDE CCCCCCCCCCCCCCC | 52.44 | 17725716 | |
| 419 | Phosphorylation | EEDGSSGSEEDDEEE CCCCCCCCCCCCCCC | 39.50 | 17725716 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 402 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| 402 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| 403 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| 403 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| 409 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| 409 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| 416 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| 416 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| 417 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| 417 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| 419 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| 419 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RIO1_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 RIO1_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-354, AND MASSSPECTROMETRY. | |
| "Protein kinase CK2 activates the atypical Rio1p kinase and promotesits cell-cycle phase-dependent degradation in yeast."; Angermayr M., Hochleitner E., Lottspeich F., Bandlow W.; FEBS J. 274:4654-4667(2007). Cited for: INTERACTION WITH CKA2, AND PHOSPHORYLATION AT SER-403; SER-403;SER-409; SER-416; SER-417 AND SER-419. | |
