| UniProt ID | RS15_YEAST | |
|---|---|---|
| UniProt AC | Q01855 | |
| Protein Name | 40S ribosomal protein S15 {ECO:0000303|PubMed:9559554} | |
| Gene Name | RPS15 {ECO:0000303|PubMed:9559554} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 142 | |
| 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. [PubMed: 22096102 uS19 is involved in the nuclear export of the small ribosomal subunit precursor. Has a role in the late stage of the assembly of pre-40S particles within the nucleus and controls their export to the cytoplasm] | |
| Protein Sequence | MSQAVNAKKRVFKTHSYRGVDLEKLLEMSTEDFVKLAPARVRRRFARGMTSKPAGFMKKLRAAKLAAPENEKPAPVRTHMRNMIIVPEMIGSVVGIYNGKAFNQVEIRPEMLGHYLGEFSITYTPVRHGRAGATTSRFIPLK | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MSQAVNAKK ------CCHHHHHHH | 27.18 | 27717283 | |
| 2 | Acetylation | ------MSQAVNAKK ------CCHHHHHHH | 27.18 | 10601260 | |
| 8 | 2-Hydroxyisobutyrylation | MSQAVNAKKRVFKTH CCHHHHHHHHHEECC | 35.59 | - | |
| 8 | Acetylation | MSQAVNAKKRVFKTH CCHHHHHHHHHEECC | 35.59 | 25381059 | |
| 8 | Ubiquitination | MSQAVNAKKRVFKTH CCHHHHHHHHHEECC | 35.59 | 22817900 | |
| 9 | Ubiquitination | SQAVNAKKRVFKTHS CHHHHHHHHHEECCC | 51.92 | 22817900 | |
| 13 | 2-Hydroxyisobutyrylation | NAKKRVFKTHSYRGV HHHHHHEECCCCCCC | 42.33 | - | |
| 13 | Acetylation | NAKKRVFKTHSYRGV HHHHHHEECCCCCCC | 42.33 | 24489116 | |
| 13 | Ubiquitination | NAKKRVFKTHSYRGV HHHHHHEECCCCCCC | 42.33 | 23749301 | |
| 14 | Phosphorylation | AKKRVFKTHSYRGVD HHHHHEECCCCCCCC | 12.46 | 28889911 | |
| 16 | Phosphorylation | KRVFKTHSYRGVDLE HHHEECCCCCCCCHH | 23.04 | 20377248 | |
| 17 | Phosphorylation | RVFKTHSYRGVDLEK HHEECCCCCCCCHHH | 12.09 | 29136822 | |
| 24 | Ubiquitination | YRGVDLEKLLEMSTE CCCCCHHHHHCCCHH | 66.71 | 23749301 | |
| 24 | Acetylation | YRGVDLEKLLEMSTE CCCCCHHHHHCCCHH | 66.71 | 24489116 | |
| 29 | Phosphorylation | LEKLLEMSTEDFVKL HHHHHCCCHHHHHHH | 21.19 | 22369663 | |
| 30 | Phosphorylation | EKLLEMSTEDFVKLA HHHHCCCHHHHHHHH | 37.96 | 22369663 | |
| 35 | Ubiquitination | MSTEDFVKLAPARVR CCHHHHHHHHHHHHH | 38.64 | 23749301 | |
| 35 | Acetylation | MSTEDFVKLAPARVR CCHHHHHHHHHHHHH | 38.64 | 24489116 | |
| 50 | Phosphorylation | RRFARGMTSKPAGFM HHHHCCCCCCCCHHH | 36.10 | 24909858 | |
| 51 | Phosphorylation | RFARGMTSKPAGFMK HHHCCCCCCCCHHHH | 27.96 | 24909858 | |
| 52 | Ubiquitination | FARGMTSKPAGFMKK HHCCCCCCCCHHHHH | 29.71 | 23749301 | |
| 58 | Ubiquitination | SKPAGFMKKLRAAKL CCCCHHHHHHHHHHH | 46.52 | 23749301 | |
| 59 | Ubiquitination | KPAGFMKKLRAAKLA CCCHHHHHHHHHHHC | 31.27 | 22817900 | |
| 64 | Ubiquitination | MKKLRAAKLAAPENE HHHHHHHHHCCCCCC | 37.36 | 23749301 | |
| 64 | Acetylation | MKKLRAAKLAAPENE HHHHHHHHHCCCCCC | 37.36 | 24489116 | |
| 64 | 2-Hydroxyisobutyrylation | MKKLRAAKLAAPENE HHHHHHHHHCCCCCC | 37.36 | - | |
| 72 | 2-Hydroxyisobutyrylation | LAAPENEKPAPVRTH HCCCCCCCCCCCCHH | 59.05 | - | |
| 72 | Succinylation | LAAPENEKPAPVRTH HCCCCCCCCCCCCHH | 59.05 | 23954790 | |
| 72 | Acetylation | LAAPENEKPAPVRTH HCCCCCCCCCCCCHH | 59.05 | 24489116 | |
| 72 | Ubiquitination | LAAPENEKPAPVRTH HCCCCCCCCCCCCHH | 59.05 | 23749301 | |
| 124 | Phosphorylation | GEFSITYTPVRHGRA CEEEEEEECCCCCCC | 13.47 | 28889911 | |
| 134 | Phosphorylation | RHGRAGATTSRFIPL CCCCCCCEECCCCCC | 25.12 | 21440633 | |
| 135 | Phosphorylation | HGRAGATTSRFIPLK CCCCCCEECCCCCCC | 19.85 | 22369663 | |
| 136 | Phosphorylation | GRAGATTSRFIPLK- CCCCCEECCCCCCC- | 22.34 | 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 RS15_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RS15_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 RS15_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "The action of N-terminal acetyltransferases on yeast ribosomalproteins."; Arnold R.J., Polevoda B., Reilly J.P., Sherman F.; J. Biol. Chem. 274:37035-37040(1999). Cited for: CLEAVAGE OF INITIATOR METHIONINE, AND ACETYLATION AT SER-2 BY NATA. | |
| 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 SER-16, AND MASSSPECTROMETRY. | |
| "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-124, AND MASSSPECTROMETRY. | |
