| UniProt ID | RIO2_YEAST | |
|---|---|---|
| UniProt AC | P40160 | |
| Protein Name | Serine/threonine-protein kinase RIO2 | |
| Gene Name | RIO2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 425 | |
| Subcellular Localization | Cytoplasm. Nucleus. Predominantly cytoplasmic. | |
| Protein Description | Required for the final endonucleolytic cleavage of 20S pre-rRNA at site D in the cytoplasm, converting it into the mature 18S rRNA. Involved in normal export of the pre-40S particles from the nucleus to the cytoplasm. No longer associates with pre-40S subunits in RPS19 disruptions, suggesting it acts after the ribosomal protein in 18S rRNA maturation.. | |
| Protein Sequence | MKLDTSHMRYLTTDDFRVLQAVEQGSRSHEVVPTPLIHQISGMRSQSGTNRAISDLAKLSLISKMRNVKYDGYRLTYNGIDYLALKTMLNRDTVYSVGNTIGVGKESDIYKVSDKNGNPRVMKIHRLGRTSFHSVRNNRDYLKKSNQGANWMHLSRLAANKEYQFMSMLYSKGFKVPEPFDNSRHIVVMELIEGYPMRRLRKHKNIPKLYSDLMCFIVDLANSGLIHCDFNEFNIMIKDKLEDENDCGFVVIDFPQCISIQHQDADYYFQRDVDCIRRFFKKKLKYEPKPDSSMLDTEGFGDGYKYAYPDFKRDVKRTDNLDELVQASGFSKKHPGDRGLETAVESMRNAVYNSDDDMSNDEAEEENGEGDYSEEDEYYDSELDNESSEDDSEDAQEEENERIIEALSSGVENLKMDKLGNYILE | |
| 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 |
|---|---|---|---|---|---|
| 34 | Phosphorylation | RSHEVVPTPLIHQIS CCCCCCCCHHHHHHH | 21.08 | 28889911 | |
| 54 | Phosphorylation | SGTNRAISDLAKLSL CCCHHHHHHHHHHHH | 26.11 | 30377154 | |
| 58 | Acetylation | RAISDLAKLSLISKM HHHHHHHHHHHHHHH | 46.00 | 24489116 | |
| 58 | Ubiquitination | RAISDLAKLSLISKM HHHHHHHHHHHHHHH | 46.00 | 24961812 | |
| 69 | Acetylation | ISKMRNVKYDGYRLT HHHHCCCCCCCEEEE | 40.97 | 22865919 | |
| 86 | Ubiquitination | GIDYLALKTMLNRDT CCCHHHHHHHCCCCC | 26.70 | 23749301 | |
| 145 | Phosphorylation | NRDYLKKSNQGANWM CHHHHHHCCCCCCHH | 32.57 | 28889911 | |
| 161 | Ubiquitination | LSRLAANKEYQFMSM HHHHHCCHHHHHHHH | 53.74 | 22817900 | |
| 170 | Phosphorylation | YQFMSMLYSKGFKVP HHHHHHHHHCCCCCC | 10.33 | 28889911 | |
| 175 | Ubiquitination | MLYSKGFKVPEPFDN HHHHCCCCCCCCCCC | 66.60 | 23749301 | |
| 285 | Acetylation | RFFKKKLKYEPKPDS HHHHHHCCCCCCCCC | 57.35 | 24489116 | |
| 292 | Phosphorylation | KYEPKPDSSMLDTEG CCCCCCCCCCCCCCC | 26.61 | 28889911 | |
| 293 | Phosphorylation | YEPKPDSSMLDTEGF CCCCCCCCCCCCCCC | 30.64 | 21440633 | |
| 297 | Phosphorylation | PDSSMLDTEGFGDGY CCCCCCCCCCCCCCC | 33.76 | 28889911 | |
| 304 | Phosphorylation | TEGFGDGYKYAYPDF CCCCCCCCCCCCCCH | 12.93 | 28889911 | |
| 332 | Acetylation | VQASGFSKKHPGDRG HHHCCCCCCCCCCCH | 53.49 | 24489116 | |
| 346 | Phosphorylation | GLETAVESMRNAVYN HHHHHHHHHHHHHHC | 19.22 | 22369663 | |
| 408 | Phosphorylation | ERIIEALSSGVENLK HHHHHHHHHCHHHHC | 31.90 | 28889911 | |
| 409 | Phosphorylation | RIIEALSSGVENLKM HHHHHHHHCHHHHCH | 47.94 | 25752575 | |
| 415 | Ubiquitination | SSGVENLKMDKLGNY HHCHHHHCHHHHHCC | 57.54 | 23749301 | |
| 418 | Ubiquitination | VENLKMDKLGNYILE HHHHCHHHHHCCCCC | 55.59 | 23749301 | |
| 418 | Acetylation | VENLKMDKLGNYILE HHHHCHHHHHCCCCC | 55.59 | 22865919 |
| 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 RIO2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RIO2_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 RIO2_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-346 AND SER-409, ANDMASS SPECTROMETRY. | |
