| UniProt ID | RLA0_YEAST | |
|---|---|---|
| UniProt AC | P05317 | |
| Protein Name | 60S acidic ribosomal protein P0 {ECO:0000303|PubMed:9559554} | |
| Gene Name | RPP0 {ECO:0000303|PubMed:9559554} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 312 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. uL10 forms part of the P stalk that participates in recruiting G proteins to the ribosome.. | |
| Protein Sequence | MGGIREKKAEYFAKLREYLEEYKSLFVVGVDNVSSQQMHEVRKELRGRAVVLMGKNTMVRRAIRGFLSDLPDFEKLLPFVKGNVGFVFTNEPLTEIKNVIVSNRVAAPARAGAVAPEDIWVRAVNTGMEPGKTSFFQALGVPTKIARGTIEIVSDVKVVDAGNKVGQSEASLLNLLNISPFTFGLTVVQVYDNGQVFPSSILDITDEELVSHFVSAVSTIASISLAIGYPTLPSVGHTLINNYKDLLAVAIAASYHYPEIEDLVDRIENPEKYAAAAPAATSAASGDAAPAEEAAAEEEEESDDDMGFGLFD | |
| 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 |
|---|---|---|---|---|---|
| 7 | Acetylation | -MGGIREKKAEYFAK -CCCHHHHHHHHHHH | 47.65 | 25381059 | |
| 8 | 2-Hydroxyisobutyrylation | MGGIREKKAEYFAKL CCCHHHHHHHHHHHH | 41.52 | - | |
| 8 | Ubiquitination | MGGIREKKAEYFAKL CCCHHHHHHHHHHHH | 41.52 | 24961812 | |
| 14 | 2-Hydroxyisobutyrylation | KKAEYFAKLREYLEE HHHHHHHHHHHHHHH | 37.87 | - | |
| 14 | Acetylation | KKAEYFAKLREYLEE HHHHHHHHHHHHHHH | 37.87 | 24489116 | |
| 14 | Ubiquitination | KKAEYFAKLREYLEE HHHHHHHHHHHHHHH | 37.87 | 23749301 | |
| 34 | Phosphorylation | VVGVDNVSSQQMHEV EEECCCCCHHHHHHH | 28.78 | 17287358 | |
| 55 | Acetylation | RAVVLMGKNTMVRRA CEEEEECCCHHHHHH | 34.97 | 24489116 | |
| 55 | 2-Hydroxyisobutyrylation | RAVVLMGKNTMVRRA CEEEEECCCHHHHHH | 34.97 | - | |
| 55 | Ubiquitination | RAVVLMGKNTMVRRA CEEEEECCCHHHHHH | 34.97 | 23749301 | |
| 68 | Phosphorylation | RAIRGFLSDLPDFEK HHHHHHHHCCCCHHH | 34.54 | 22369663 | |
| 75 | Ubiquitination | SDLPDFEKLLPFVKG HCCCCHHHHHHHHCC | 56.15 | 23749301 | |
| 81 | Ubiquitination | EKLLPFVKGNVGFVF HHHHHHHCCCEEEEE | 45.18 | 23749301 | |
| 89 | Phosphorylation | GNVGFVFTNEPLTEI CCEEEEEECCCCHHE | 33.11 | 28132839 | |
| 97 | Ubiquitination | NEPLTEIKNVIVSNR CCCCHHEEEEEECCC | 38.64 | 23749301 | |
| 102 | Phosphorylation | EIKNVIVSNRVAAPA HEEEEEECCCCCCCC | 14.06 | 21440633 | |
| 126 | Phosphorylation | IWVRAVNTGMEPGKT HEEEECCCCCCCCCC | 31.16 | 28889911 | |
| 132 | Ubiquitination | NTGMEPGKTSFFQAL CCCCCCCCCCHHHHC | 52.27 | 23749301 | |
| 132 | Acetylation | NTGMEPGKTSFFQAL CCCCCCCCCCHHHHC | 52.27 | 24489116 | |
| 133 | Phosphorylation | TGMEPGKTSFFQALG CCCCCCCCCHHHHCC | 36.36 | 22369663 | |
| 134 | Phosphorylation | GMEPGKTSFFQALGV CCCCCCCCHHHHCCC | 27.78 | 22369663 | |
| 143 | Phosphorylation | FQALGVPTKIARGTI HHHCCCCCEECCCEE | 32.45 | 22369663 | |
| 144 | Ubiquitination | QALGVPTKIARGTIE HHCCCCCEECCCEEE | 28.44 | 23749301 | |
| 144 | Acetylation | QALGVPTKIARGTIE HHCCCCCEECCCEEE | 28.44 | 24489116 | |
| 149 | Phosphorylation | PTKIARGTIEIVSDV CCEECCCEEEEECCE | 15.19 | 27717283 | |
| 154 | Phosphorylation | RGTIEIVSDVKVVDA CCEEEEECCEEEEEC | 42.20 | 27717283 | |
| 157 | Ubiquitination | IEIVSDVKVVDAGNK EEEECCEEEEECCCC | 41.34 | 24961812 | |
| 157 | Acetylation | IEIVSDVKVVDAGNK EEEECCEEEEECCCC | 41.34 | 24489116 | |
| 273 | Phosphorylation | RIENPEKYAAAAPAA HCCCHHHHHHHHHHH | 10.38 | 29688323 | |
| 281 | Phosphorylation | AAAAPAATSAASGDA HHHHHHHHHHHCCCC | 22.47 | 28152593 | |
| 282 | Phosphorylation | AAAPAATSAASGDAA HHHHHHHHHHCCCCC | 19.67 | 21440633 | |
| 285 | Phosphorylation | PAATSAASGDAAPAE HHHHHHHCCCCCCHH | 36.60 | 28152593 | |
| 302 | Phosphorylation | AAEEEEESDDDMGFG HHHHHHHCCCCCCCC | 50.01 | 25521595 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 302 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| 302 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RLA0_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 RLA0_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-302, AND MASSSPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, AND MASSSPECTROMETRY. | |
| "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-302, AND MASSSPECTROMETRY. | |
| "Phosphorylation of ribosomal protein P0 is not essential for ribosomefunction but can affect translation."; Rodriguez-Gabriel M.A., Remacha M., Ballesta J.P.G.; Biochemistry 37:16620-16626(1998). Cited for: PHOSPHORYLATION AT SER-302. | |
