| UniProt ID | RS3_YEAST | |
|---|---|---|
| UniProt AC | P05750 | |
| Protein Name | 40S ribosomal protein S3 {ECO:0000303|PubMed:9559554} | |
| Gene Name | RPS3 {ECO:0000303|PubMed:9559554} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 240 | |
| 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 | MVALISKKRKLVADGVFYAELNEFFTRELAEEGYSGVEVRVTPTKTEVIIRATRTQDVLGENGRRINELTLLVQKRFKYAPGTIVLYAERVQDRGLSAVAQAESMKFKLLNGLAIRRAAYGVVRYVMESGAKGCEVVVSGKLRAARAKAMKFADGFLIHSGQPVNDFIDTATRHVLMRQGVLGIKVKIMRDPAKSRTGPKALPDAVTIIEPKEEEPILAPSVKDYRPAEETEAQAEPVEA | |
| 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 | 2-Hydroxyisobutyrylation | -MVALISKKRKLVAD -CCEEECCCCCHHCC | 49.99 | - | |
| 7 | Succinylation | -MVALISKKRKLVAD -CCEEECCCCCHHCC | 49.99 | 23954790 | |
| 10 | Ubiquitination | ALISKKRKLVADGVF EEECCCCCHHCCCCC | 57.08 | 17644757 | |
| 35 | Phosphorylation | ELAEEGYSGVEVRVT HHHHCCCCCEEEEEC | 47.41 | 27214570 | |
| 44 | Phosphorylation | VEVRVTPTKTEVIIR EEEEECCCCCEEEEE | 41.03 | 28889911 | |
| 45 | Ubiquitination | EVRVTPTKTEVIIRA EEEECCCCCEEEEEE | 43.84 | 23749301 | |
| 45 | Acetylation | EVRVTPTKTEVIIRA EEEECCCCCEEEEEE | 43.84 | 24489116 | |
| 45 | Succinylation | EVRVTPTKTEVIIRA EEEECCCCCEEEEEE | 43.84 | 23954790 | |
| 53 | Phosphorylation | TEVIIRATRTQDVLG CEEEEEEEECCCCCC | 25.13 | 17287358 | |
| 55 | Phosphorylation | VIIRATRTQDVLGEN EEEEEEECCCCCCCC | 25.43 | 28889911 | |
| 70 | Phosphorylation | GRRINELTLLVQKRF CCCHHHHHHHHHHHH | 16.33 | 17287358 | |
| 75 | 2-Hydroxyisobutyrylation | ELTLLVQKRFKYAPG HHHHHHHHHHCCCCC | 52.93 | - | |
| 75 | Ubiquitination | ELTLLVQKRFKYAPG HHHHHHHHHHCCCCC | 52.93 | 23749301 | |
| 75 | Acetylation | ELTLLVQKRFKYAPG HHHHHHHHHHCCCCC | 52.93 | 24489116 | |
| 78 | Ubiquitination | LLVQKRFKYAPGTIV HHHHHHHCCCCCEEE | 44.53 | 24961812 | |
| 78 | Acetylation | LLVQKRFKYAPGTIV HHHHHHHCCCCCEEE | 44.53 | 24489116 | |
| 97 | Phosphorylation | RVQDRGLSAVAQAES EHHHCCHHHHHCHHH | 24.42 | 25752575 | |
| 104 | Phosphorylation | SAVAQAESMKFKLLN HHHHCHHHHHHHHHH | 30.23 | 27214570 | |
| 106 | Acetylation | VAQAESMKFKLLNGL HHCHHHHHHHHHHHH | 48.93 | 24489116 | |
| 106 | 2-Hydroxyisobutyrylation | VAQAESMKFKLLNGL HHCHHHHHHHHHHHH | 48.93 | - | |
| 106 | Ubiquitination | VAQAESMKFKLLNGL HHCHHHHHHHHHHHH | 48.93 | 23749301 | |
| 108 | Ubiquitination | QAESMKFKLLNGLAI CHHHHHHHHHHHHHH | 46.69 | 23749301 | |
| 108 | Acetylation | QAESMKFKLLNGLAI CHHHHHHHHHHHHHH | 46.69 | 24489116 | |
| 129 | Phosphorylation | VVRYVMESGAKGCEV HHHHHHHCCCCCCEE | 26.42 | 17287358 | |
| 132 | Ubiquitination | YVMESGAKGCEVVVS HHHHCCCCCCEEEEC | 68.56 | 23749301 | |
| 141 | Acetylation | CEVVVSGKLRAARAK CEEEECCCHHHHHHH | 27.56 | 24489116 | |
| 141 | Ubiquitination | CEVVVSGKLRAARAK CEEEECCCHHHHHHH | 27.56 | 23749301 | |
| 146 | Methylation | SGKLRAARAKAMKFA CCCHHHHHHHHHHHC | 35.32 | 22650761 | |
| 151 | Ubiquitination | AARAKAMKFADGFLI HHHHHHHHHCCCEEE | 42.11 | 23749301 | |
| 151 | Acetylation | AARAKAMKFADGFLI HHHHHHHHHCCCEEE | 42.11 | 24489116 | |
| 160 | Phosphorylation | ADGFLIHSGQPVNDF CCCEEECCCCCHHHH | 31.93 | 21440633 | |
| 172 | Phosphorylation | NDFIDTATRHVLMRQ HHHHHHHHHHHHHHC | 24.33 | 28889911 | |
| 185 | Ubiquitination | RQGVLGIKVKIMRDP HCCCCEEEEEEECCC | 35.36 | 23749301 | |
| 185 | Acetylation | RQGVLGIKVKIMRDP HCCCCEEEEEEECCC | 35.36 | 24489116 | |
| 194 | 2-Hydroxyisobutyrylation | KIMRDPAKSRTGPKA EEECCCCCCCCCCCC | 45.95 | - | |
| 194 | Acetylation | KIMRDPAKSRTGPKA EEECCCCCCCCCCCC | 45.95 | 24489116 | |
| 200 | Ubiquitination | AKSRTGPKALPDAVT CCCCCCCCCCCCCEE | 64.99 | 23749301 | |
| 200 | Acetylation | AKSRTGPKALPDAVT CCCCCCCCCCCCCEE | 64.99 | 24489116 | |
| 200 | Succinylation | AKSRTGPKALPDAVT CCCCCCCCCCCCCEE | 64.99 | 23954790 | |
| 207 | Phosphorylation | KALPDAVTIIEPKEE CCCCCCEEEECCCCC | 20.25 | 22369663 | |
| 212 | Ubiquitination | AVTIIEPKEEEPILA CEEEECCCCCCCCCC | 66.04 | 23749301 | |
| 212 | Sumoylation | AVTIIEPKEEEPILA CEEEECCCCCCCCCC | 66.04 | - | |
| 212 | Succinylation | AVTIIEPKEEEPILA CEEEECCCCCCCCCC | 66.04 | 23954790 | |
| 212 | Acetylation | AVTIIEPKEEEPILA CEEEECCCCCCCCCC | 66.04 | 24489116 | |
| 221 | Phosphorylation | EEPILAPSVKDYRPA CCCCCCCCHHCCCCH | 35.87 | 22369663 | |
| 223 | Ubiquitination | PILAPSVKDYRPAEE CCCCCCHHCCCCHHH | 54.07 | 23749301 | |
| 225 | Phosphorylation | LAPSVKDYRPAEETE CCCCHHCCCCHHHCH | 16.87 | 19795423 | |
| 231 | Phosphorylation | DYRPAEETEAQAEPV CCCCHHHCHHHCCCC | 28.29 | 21082442 |
| 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 RS3_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RS3_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 RS3_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 THR-44; SER-97; THR-207 ANDSER-221, AND MASS SPECTROMETRY. | |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, 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 THR-53; THR-70; SER-129 ANDSER-221, AND MASS SPECTROMETRY. | |
| "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-221, AND MASSSPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-207; SER-221 ANDTHR-231, AND MASS SPECTROMETRY. | |
| Ubiquitylation | |
| Reference | PubMed |
| "A proteomics approach to understanding protein ubiquitination."; Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.; Nat. Biotechnol. 21:921-926(2003). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-212, AND MASSSPECTROMETRY. | |
