UniProt ID | RL2B_YEAST | |
---|---|---|
UniProt AC | P0CX46 | |
Protein Name | 60S ribosomal protein L2-B {ECO:0000303|PubMed:9559554} | |
Gene Name | RPL2B {ECO:0000303|PubMed:9559554} | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 254 | |
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 | MGRVIRNQRKGAGSIFTSHTRLRQGAAKLRTLDYAERHGYIRGIVKQIVHDSGRGAPLAKVVFRDPYKYRLREEIFIANEGVHTGQFIYAGKKASLNVGNVLPLGSVPEGTIVSNVEEKPGDRGALARASGNYVIIIGHNPDENKTRVRLPSGAKKVISSDARGVIGVIAGGGRVDKPLLKAGRAFHKYRLKRNSWPKTRGVAMNPVDHPHGGGNHQHIGKASTISRGAVSGQKAGLIAARRTGLLRGSQKTQD | |
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 |
---|---|---|---|---|---|
10 | Ubiquitination | RVIRNQRKGAGSIFT CCCCCCCCCCCCCCC | 43.26 | 23749301 | |
14 | Phosphorylation | NQRKGAGSIFTSHTR CCCCCCCCCCCCHHH | 17.62 | 22369663 | |
17 | Phosphorylation | KGAGSIFTSHTRLRQ CCCCCCCCCHHHHHH | 20.23 | 22369663 | |
18 | Phosphorylation | GAGSIFTSHTRLRQG CCCCCCCCHHHHHHH | 16.47 | 23749301 | |
20 | Phosphorylation | GSIFTSHTRLRQGAA CCCCCCHHHHHHHHH | 31.03 | 22369663 | |
28 | Ubiquitination | RLRQGAAKLRTLDYA HHHHHHHHHHCCCHH | 37.66 | 15699485 | |
31 | Phosphorylation | QGAAKLRTLDYAERH HHHHHHHCCCHHHHH | 34.12 | 17563356 | |
46 | Ubiquitination | GYIRGIVKQIVHDSG CCHHHHHHHHHCCCC | 32.18 | 23749301 | |
52 | Phosphorylation | VKQIVHDSGRGAPLA HHHHHCCCCCCCCCE | 18.60 | 17287358 | |
60 | Ubiquitination | GRGAPLAKVVFRDPY CCCCCCEEEEECCCC | 46.76 | 22817900 | |
67 | Phosphorylation | KVVFRDPYKYRLREE EEEECCCCCCCCCCE | 25.58 | 27017623 | |
68 | Ubiquitination | VVFRDPYKYRLREEI EEECCCCCCCCCCEE | 29.31 | 22106047 | |
84 | Phosphorylation | IANEGVHTGQFIYAG EEECCCCCCCEEECC | 30.21 | 17287358 | |
92 | Ubiquitination | GQFIYAGKKASLNVG CCEEECCCCEEEECC | 36.67 | 23793018 | |
93 | Ubiquitination | QFIYAGKKASLNVGN CEEECCCCEEEECCC | 42.14 | 23749301 | |
95 | Phosphorylation | IYAGKKASLNVGNVL EECCCCEEEECCCCE | 29.38 | 22369663 | |
106 | Phosphorylation | GNVLPLGSVPEGTIV CCCEECCCCCCCEEE | 42.03 | 21440633 | |
111 | Phosphorylation | LGSVPEGTIVSNVEE CCCCCCCEEEECCCC | 19.28 | 22369663 | |
114 | Phosphorylation | VPEGTIVSNVEEKPG CCCCEEEECCCCCCC | 31.16 | 22369663 | |
119 | Ubiquitination | IVSNVEEKPGDRGAL EEECCCCCCCCCCHH | 40.57 | 23749301 | |
133 | Phosphorylation | LARASGNYVIIIGHN HHHCCCCEEEEEECC | 9.13 | 23749301 | |
145 | Ubiquitination | GHNPDENKTRVRLPS ECCCCCCCEEEECCC | 35.34 | 23749301 | |
155 | Ubiquitination | VRLPSGAKKVISSDA EECCCCCCEEECCCC | 51.61 | 22817900 | |
156 | Ubiquitination | RLPSGAKKVISSDAR ECCCCCCEEECCCCC | 44.24 | 23749301 | |
159 | Phosphorylation | SGAKKVISSDARGVI CCCCEEECCCCCCEE | 25.75 | 17287358 | |
160 | Phosphorylation | GAKKVISSDARGVIG CCCEEECCCCCCEEE | 24.94 | 17287358 | |
177 | Ubiquitination | AGGGRVDKPLLKAGR ECCCCCCHHHHHHHH | 34.41 | 23749301 | |
181 | Ubiquitination | RVDKPLLKAGRAFHK CCCHHHHHHHHHHHH | 57.38 | 23749301 | |
195 | Phosphorylation | KYRLKRNSWPKTRGV HHHCCCCCCCCCCCE | 49.11 | 21440633 | |
198 | Ubiquitination | LKRNSWPKTRGVAMN CCCCCCCCCCCEECC | 44.59 | 23749301 | |
221 | Ubiquitination | GNHQHIGKASTISRG CCCCCCCEEEEEECC | 38.26 | 23749301 | |
223 | Phosphorylation | HQHIGKASTISRGAV CCCCCEEEEEECCCC | 29.74 | 21440633 | |
224 | Phosphorylation | QHIGKASTISRGAVS CCCCEEEEEECCCCC | 28.03 | 21440633 | |
226 | Phosphorylation | IGKASTISRGAVSGQ CCEEEEEECCCCCCC | 25.42 | 21440633 | |
231 | Phosphorylation | TISRGAVSGQKAGLI EEECCCCCCCHHHHH | 34.67 | 19823750 | |
234 | Ubiquitination | RGAVSGQKAGLIAAR CCCCCCCHHHHHHHH | 48.20 | 23749301 | |
243 | Phosphorylation | GLIAARRTGLLRGSQ HHHHHHHHCCCCCCC | 26.99 | 17287358 | |
249 | Phosphorylation | RTGLLRGSQKTQD-- HHCCCCCCCCCCC-- | 23.28 | 17287358 |
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 RL2B_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RL2B_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 RL2B_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"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 THR-20; SER-52; THR-84;SER-159; SER-160; THR-243 AND SER-249, AND MASS SPECTROMETRY. |