| UniProt ID | RL15A_YEAST | |
|---|---|---|
| UniProt AC | P05748 | |
| Protein Name | 60S ribosomal protein L15-A {ECO:0000303|PubMed:9559554} | |
| Gene Name | RPL15A {ECO:0000303|PubMed:9559554} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 204 | |
| 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 | MGAYKYLEELQRKKQSDVLRFLQRVRVWEYRQKNVIHRAARPTRPDKARRLGYKAKQGFVIYRVRVRRGNRKRPVPKGATYGKPTNQGVNELKYQRSLRATAEERVGRRAANLRVLNSYWVNQDSTYKYFEVILVDPQHKAIRRDARYNWICDPVHKHREARGLTATGKKSRGINKGHKFNNTKAGRRKTWKRQNTLSLWRYRK | |
| 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 | ---MGAYKYLEELQR ---CCHHHHHHHHHH | 42.71 | 24961812 | |
| 5 | Succinylation | ---MGAYKYLEELQR ---CCHHHHHHHHHH | 42.71 | 23954790 | |
| 13 | Ubiquitination | YLEELQRKKQSDVLR HHHHHHHHHHHHHHH | 42.05 | 22817900 | |
| 14 | 2-Hydroxyisobutyrylation | LEELQRKKQSDVLRF HHHHHHHHHHHHHHH | 58.17 | - | |
| 14 | Ubiquitination | LEELQRKKQSDVLRF HHHHHHHHHHHHHHH | 58.17 | 22817900 | |
| 33 | 2-Hydroxyisobutyrylation | RVWEYRQKNVIHRAA HHHHHHHCCHHHHHC | 44.15 | - | |
| 33 | Ubiquitination | RVWEYRQKNVIHRAA HHHHHHHCCHHHHHC | 44.15 | 22817900 | |
| 54 | Ubiquitination | KARRLGYKAKQGFVI HHHHHCCEECCCEEE | 47.51 | 22817900 | |
| 56 | Acetylation | RRLGYKAKQGFVIYR HHHCCEECCCEEEEE | 46.96 | 22865919 | |
| 56 | Ubiquitination | RRLGYKAKQGFVIYR HHHCCEECCCEEEEE | 46.96 | 23749301 | |
| 56 | 2-Hydroxyisobutyrylation | RRLGYKAKQGFVIYR HHHCCEECCCEEEEE | 46.96 | - | |
| 72 | Ubiquitination | RVRRGNRKRPVPKGA EEECCCCCCCCCCCC | 66.12 | 22817900 | |
| 77 | Ubiquitination | NRKRPVPKGATYGKP CCCCCCCCCCCCCCC | 62.50 | 22817900 | |
| 80 | Phosphorylation | RPVPKGATYGKPTNQ CCCCCCCCCCCCCCC | 41.28 | 21440633 | |
| 81 | Phosphorylation | PVPKGATYGKPTNQG CCCCCCCCCCCCCCC | 23.71 | 28889911 | |
| 83 | Ubiquitination | PKGATYGKPTNQGVN CCCCCCCCCCCCCHH | 37.95 | 23749301 | |
| 83 | Acetylation | PKGATYGKPTNQGVN CCCCCCCCCCCCCHH | 37.95 | 24489116 | |
| 85 | Phosphorylation | GATYGKPTNQGVNEL CCCCCCCCCCCHHHH | 43.59 | 21440633 | |
| 93 | 2-Hydroxyisobutyrylation | NQGVNELKYQRSLRA CCCHHHHHHHHHHHH | 32.91 | - | |
| 93 | Ubiquitination | NQGVNELKYQRSLRA CCCHHHHHHHHHHHH | 32.91 | 23749301 | |
| 93 | Acetylation | NQGVNELKYQRSLRA CCCHHHHHHHHHHHH | 32.91 | 24489116 | |
| 118 | Phosphorylation | ANLRVLNSYWVNQDS HCCEEEEEEEECCCC | 19.06 | 28152593 | |
| 126 | Phosphorylation | YWVNQDSTYKYFEVI EEECCCCCCEEEEEE | 32.11 | 30377154 | |
| 128 | Ubiquitination | VNQDSTYKYFEVILV ECCCCCCEEEEEEEE | 43.48 | 23749301 | |
| 140 | Succinylation | ILVDPQHKAIRRDAR EEECCCCHHHHHHHC | 40.02 | 23954790 | |
| 140 | Acetylation | ILVDPQHKAIRRDAR EEECCCCHHHHHHHC | 40.02 | 24489116 | |
| 140 | Ubiquitination | ILVDPQHKAIRRDAR EEECCCCHHHHHHHC | 40.02 | 23749301 | |
| 157 | Acetylation | WICDPVHKHREARGL CCCCHHHHCHHHHCC | 44.59 | 24489116 | |
| 157 | Ubiquitination | WICDPVHKHREARGL CCCCHHHHCHHHHCC | 44.59 | 23749301 | |
| 169 | Succinylation | RGLTATGKKSRGINK HCCCCCCCCCCCCCC | 43.13 | 23954790 | |
| 170 | Ubiquitination | GLTATGKKSRGINKG CCCCCCCCCCCCCCC | 46.89 | 17644757 | |
| 171 | Phosphorylation | LTATGKKSRGINKGH CCCCCCCCCCCCCCC | 38.94 | 19795423 | |
| 176 | 2-Hydroxyisobutyrylation | KKSRGINKGHKFNNT CCCCCCCCCCCCCCC | 61.54 | - | |
| 176 | Ubiquitination | KKSRGINKGHKFNNT CCCCCCCCCCCCCCC | 61.54 | 17644757 | |
| 176 | Acetylation | KKSRGINKGHKFNNT CCCCCCCCCCCCCCC | 61.54 | 25381059 | |
| 179 | Ubiquitination | RGINKGHKFNNTKAG CCCCCCCCCCCCHHC | 59.46 | 22817900 | |
| 179 | Acetylation | RGINKGHKFNNTKAG CCCCCCCCCCCCHHC | 59.46 | 25381059 | |
| 184 | 2-Hydroxyisobutyrylation | GHKFNNTKAGRRKTW CCCCCCCHHCCCCCH | 51.47 | - | |
| 184 | Ubiquitination | GHKFNNTKAGRRKTW CCCCCCCHHCCCCCH | 51.47 | 22817900 | |
| 184 | Acetylation | GHKFNNTKAGRRKTW CCCCCCCHHCCCCCH | 51.47 | 25381059 | |
| 184 | Succinylation | GHKFNNTKAGRRKTW CCCCCCCHHCCCCCH | 51.47 | 23954790 | |
| 189 | Ubiquitination | NTKAGRRKTWKRQNT CCHHCCCCCHHHHCC | 58.33 | 22817900 | |
| 192 | Ubiquitination | AGRRKTWKRQNTLSL HCCCCCHHHHCCHHH | 49.70 | 17644757 | |
| 196 | Phosphorylation | KTWKRQNTLSLWRYR CCHHHHCCHHHEEEC | 14.91 | 23749301 | |
| 198 | Phosphorylation | WKRQNTLSLWRYRK- HHHHCCHHHEEECC- | 24.69 | 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 RL15A_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RL15A_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 RL15A_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| 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 SER-198, AND MASSSPECTROMETRY. | |
