| UniProt ID | RL20B_YEAST | |
|---|---|---|
| UniProt AC | P0CX24 | |
| Protein Name | 60S ribosomal protein L20-B {ECO:0000303|PubMed:9559554} | |
| Gene Name | RPL20B {ECO:0000303|PubMed:9559554} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 172 | |
| 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.. | |
| Protein Sequence | MAHFKEYQVIGRRLPTESVPEPKLFRMRIFASNEVIAKSRYWYFLQKLHKVKKASGEIVSINQINEAHPTKVKNFGVWVRYDSRSGTHNMYKEIRDVSRVAAVETLYQDMAARHRARFRSIHILKVAEIEKTADVKRQYVKQFLTKDLKFPLPHRVQKSTKTFSYKRPSTFY | |
| 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 |
|---|---|---|---|---|---|
| 5 | Ubiquitination | ---MAHFKEYQVIGR ---CCCCCEEEEECC | 45.72 | 15699485 | |
| 16 | Phosphorylation | VIGRRLPTESVPEPK EECCCCCCCCCCCCC | 45.55 | 22369663 | |
| 18 | Phosphorylation | GRRLPTESVPEPKLF CCCCCCCCCCCCCEE | 45.51 | 22369663 | |
| 23 | Ubiquitination | TESVPEPKLFRMRIF CCCCCCCCEEEEEEE | 59.60 | 24961812 | |
| 32 | Phosphorylation | FRMRIFASNEVIAKS EEEEEECCCCHHHHH | 23.83 | 17287358 | |
| 38 | Ubiquitination | ASNEVIAKSRYWYFL CCCCHHHHHHHHHHH | 25.09 | 23749301 | |
| 39 | Phosphorylation | SNEVIAKSRYWYFLQ CCCHHHHHHHHHHHH | 22.91 | 21440633 | |
| 41 | Phosphorylation | EVIAKSRYWYFLQKL CHHHHHHHHHHHHHH | 16.14 | 21440633 | |
| 47 | Ubiquitination | RYWYFLQKLHKVKKA HHHHHHHHHHHHHHC | 55.49 | 17644757 | |
| 52 | Ubiquitination | LQKLHKVKKASGEIV HHHHHHHHHCCCCEE | 47.64 | 17644757 | |
| 53 | Ubiquitination | QKLHKVKKASGEIVS HHHHHHHHCCCCEEE | 51.26 | 17644757 | |
| 55 | Phosphorylation | LHKVKKASGEIVSIN HHHHHHCCCCEEEEE | 45.93 | 27214570 | |
| 60 | Phosphorylation | KASGEIVSINQINEA HCCCCEEEEEECCCC | 22.83 | 24961812 | |
| 71 | Ubiquitination | INEAHPTKVKNFGVW CCCCCCCCCCEEEEE | 56.51 | 22817900 | |
| 73 | Ubiquitination | EAHPTKVKNFGVWVR CCCCCCCCEEEEEEE | 48.38 | 23749301 | |
| 85 | Phosphorylation | WVRYDSRSGTHNMYK EEEEECCCCCCHHHH | 52.58 | 28889911 | |
| 92 | Ubiquitination | SGTHNMYKEIRDVSR CCCCHHHHHHHHHHH | 35.58 | 23749301 | |
| 120 | Phosphorylation | RHRARFRSIHILKVA HHHHHHHEEEEEEEE | 18.79 | 23749301 | |
| 125 | Ubiquitination | FRSIHILKVAEIEKT HHEEEEEEEEEEECC | 38.50 | 23749301 | |
| 131 | Ubiquitination | LKVAEIEKTADVKRQ EEEEEEECCHHHHHH | 55.46 | 23749301 | |
| 136 | Ubiquitination | IEKTADVKRQYVKQF EECCHHHHHHHHHHH | 34.04 | 22817900 | |
| 141 | Ubiquitination | DVKRQYVKQFLTKDL HHHHHHHHHHHHCCC | 30.33 | 23749301 | |
| 146 | Ubiquitination | YVKQFLTKDLKFPLP HHHHHHHCCCCCCCC | 64.31 | 23749301 | |
| 149 | Ubiquitination | QFLTKDLKFPLPHRV HHHHCCCCCCCCCCC | 55.88 | 23749301 | |
| 158 | Ubiquitination | PLPHRVQKSTKTFSY CCCCCCCCCCCEECC | 58.18 | 22817900 | |
| 159 | Phosphorylation | LPHRVQKSTKTFSYK CCCCCCCCCCEECCC | 20.32 | 21440633 | |
| 161 | Ubiquitination | HRVQKSTKTFSYKRP CCCCCCCCEECCCCC | 55.45 | 23749301 | |
| 162 | Phosphorylation | RVQKSTKTFSYKRPS CCCCCCCEECCCCCC | 20.22 | 21440633 | |
| 164 | Phosphorylation | QKSTKTFSYKRPSTF CCCCCEECCCCCCCC | 34.67 | 23749301 | |
| 165 | Phosphorylation | KSTKTFSYKRPSTFY CCCCEECCCCCCCCC | 13.56 | 21440633 | |
| 166 | Ubiquitination | STKTFSYKRPSTFY- CCCEECCCCCCCCC- | 57.54 | 23749301 | |
| 169 | Phosphorylation | TFSYKRPSTFY---- EECCCCCCCCC---- | 34.87 | 22369663 | |
| 170 | Phosphorylation | FSYKRPSTFY----- ECCCCCCCCC----- | 29.63 | 22369663 | |
| 172 | Phosphorylation | YKRPSTFY------- CCCCCCCC------- | 20.10 | 22369663 |
| 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 RL20B_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RL20B_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 RL20B_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-32, 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-32, AND MASSSPECTROMETRY. | |
