| UniProt ID | RL10_YEAST | |
|---|---|---|
| UniProt AC | P41805 | |
| Protein Name | 60S ribosomal protein L10 {ECO:0000303|PubMed:9559554} | |
| Gene Name | RPL10 {ECO:0000303|PubMed:9559554} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 221 | |
| 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 | MARRPARCYRYQKNKPYPKSRYNRAVPDSKIRIYDLGKKKATVDEFPLCVHLVSNELEQLSSEALEAARICANKYMTTVSGRDAFHLRVRVHPFHVLRINKMLSCAGADRLQQGMRGAWGKPHGLAARVDIGQIIFSVRTKDSNKDVVVEGLRRARYKFPGQQKIILSKKWGFTNLDRPEYLKKREAGEVKDDGAFVKFLSKKGSLENNIREFPEYFAAQA | |
| 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 |
|---|---|---|---|---|---|
| 13 | Ubiquitination | ARCYRYQKNKPYPKS CHHCCCCCCCCCCCH | 58.99 | 23749301 | |
| 15 | Acetylation | CYRYQKNKPYPKSRY HCCCCCCCCCCCHHC | 53.62 | 25381059 | |
| 15 | Ubiquitination | CYRYQKNKPYPKSRY HCCCCCCCCCCCHHC | 53.62 | 22817900 | |
| 19 | Ubiquitination | QKNKPYPKSRYNRAV CCCCCCCCHHCCCCC | 41.54 | 23749301 | |
| 20 | Phosphorylation | KNKPYPKSRYNRAVP CCCCCCCHHCCCCCC | 35.18 | 21440633 | |
| 30 | 2-Hydroxyisobutyrylation | NRAVPDSKIRIYDLG CCCCCCCCEEEEECC | 43.30 | - | |
| 30 | Ubiquitination | NRAVPDSKIRIYDLG CCCCCCCCEEEEECC | 43.30 | 23749301 | |
| 30 | Acetylation | NRAVPDSKIRIYDLG CCCCCCCCEEEEECC | 43.30 | 24489116 | |
| 38 | Ubiquitination | IRIYDLGKKKATVDE EEEEECCCCCCCCCC | 59.40 | 23749301 | |
| 39 | Ubiquitination | RIYDLGKKKATVDEF EEEECCCCCCCCCCC | 45.93 | 22817900 | |
| 40 | Ubiquitination | IYDLGKKKATVDEFP EEECCCCCCCCCCCH | 53.42 | 23749301 | |
| 61 | Phosphorylation | SNELEQLSSEALEAA HHHHHHHCHHHHHHH | 26.31 | 27214570 | |
| 62 | Phosphorylation | NELEQLSSEALEAAR HHHHHHCHHHHHHHH | 35.17 | 27214570 | |
| 74 | Acetylation | AARICANKYMTTVSG HHHHHCHHCCEEECC | 20.20 | 24489116 | |
| 74 | Ubiquitination | AARICANKYMTTVSG HHHHHCHHCCEEECC | 20.20 | 23749301 | |
| 75 | Phosphorylation | ARICANKYMTTVSGR HHHHCHHCCEEECCC | 10.25 | 27017623 | |
| 77 | Phosphorylation | ICANKYMTTVSGRDA HHCHHCCEEECCCCC | 22.43 | 27017623 | |
| 78 | Phosphorylation | CANKYMTTVSGRDAF HCHHCCEEECCCCCE | 8.99 | 27017623 | |
| 80 | Phosphorylation | NKYMTTVSGRDAFHL HHCCEEECCCCCEEE | 26.47 | 21440633 | |
| 101 | Acetylation | FHVLRINKMLSCAGA HHHHHHHHCHHHCCH | 38.56 | 22865919 | |
| 101 | Ubiquitination | FHVLRINKMLSCAGA HHHHHHHHCHHHCCH | 38.56 | 23749301 | |
| 104 | Phosphorylation | LRINKMLSCAGADRL HHHHHCHHHCCHHHH | 9.83 | 21440633 | |
| 121 | Acetylation | GMRGAWGKPHGLAAR HCCCCCCCCCCEEEE | 24.12 | 24489116 | |
| 121 | Ubiquitination | GMRGAWGKPHGLAAR HCCCCCCCCCCEEEE | 24.12 | 23749301 | |
| 137 | Phosphorylation | DIGQIIFSVRTKDSN EECEEEEEEECCCCC | 10.57 | 21440633 | |
| 140 | Phosphorylation | QIIFSVRTKDSNKDV EEEEEEECCCCCCCE | 36.73 | 21082442 | |
| 141 | Ubiquitination | IIFSVRTKDSNKDVV EEEEEECCCCCCCEE | 48.90 | 22817900 | |
| 143 | Phosphorylation | FSVRTKDSNKDVVVE EEEECCCCCCCEEEE | 47.54 | 17330950 | |
| 145 | Acetylation | VRTKDSNKDVVVEGL EECCCCCCCEEEEEE | 56.71 | 24489116 | |
| 145 | 2-Hydroxyisobutyrylation | VRTKDSNKDVVVEGL EECCCCCCCEEEEEE | 56.71 | - | |
| 145 | Ubiquitination | VRTKDSNKDVVVEGL EECCCCCCCEEEEEE | 56.71 | 23749301 | |
| 145 | Succinylation | VRTKDSNKDVVVEGL EECCCCCCCEEEEEE | 56.71 | 23954790 | |
| 158 | Acetylation | GLRRARYKFPGQQKI EECEEECCCCCCCEE | 39.26 | 24489116 | |
| 164 | 2-Hydroxyisobutyrylation | YKFPGQQKIILSKKW CCCCCCCEEEEECCC | 24.67 | - | |
| 164 | Acetylation | YKFPGQQKIILSKKW CCCCCCCEEEEECCC | 24.67 | 24489116 | |
| 169 | Ubiquitination | QQKIILSKKWGFTNL CCEEEEECCCCCCCC | 49.45 | 17644757 | |
| 169 | 2-Hydroxyisobutyrylation | QQKIILSKKWGFTNL CCEEEEECCCCCCCC | 49.45 | - | |
| 170 | Ubiquitination | QKIILSKKWGFTNLD CEEEEECCCCCCCCC | 49.53 | 24961812 | |
| 170 | 2-Hydroxyisobutyrylation | QKIILSKKWGFTNLD CEEEEECCCCCCCCC | 49.53 | - | |
| 170 | Acetylation | QKIILSKKWGFTNLD CEEEEECCCCCCCCC | 49.53 | 24489116 | |
| 174 | Phosphorylation | LSKKWGFTNLDRPEY EECCCCCCCCCCHHH | 30.82 | 21440633 | |
| 183 | Acetylation | LDRPEYLKKREAGEV CCCHHHHHHHCCCCC | 49.21 | 24489116 | |
| 183 | Ubiquitination | LDRPEYLKKREAGEV CCCHHHHHHHCCCCC | 49.21 | 23749301 | |
| 184 | Ubiquitination | DRPEYLKKREAGEVK CCHHHHHHHCCCCCC | 53.53 | 22817900 | |
| 191 | Acetylation | KREAGEVKDDGAFVK HHCCCCCCCCCHHHH | 45.88 | 24489116 | |
| 191 | Succinylation | KREAGEVKDDGAFVK HHCCCCCCCCCHHHH | 45.88 | 23954790 | |
| 191 | Ubiquitination | KREAGEVKDDGAFVK HHCCCCCCCCCHHHH | 45.88 | 23749301 | |
| 191 | 2-Hydroxyisobutyrylation | KREAGEVKDDGAFVK HHCCCCCCCCCHHHH | 45.88 | - | |
| 198 | Succinylation | KDDGAFVKFLSKKGS CCCCHHHHHHHHCCC | 33.85 | 23954790 | |
| 198 | Acetylation | KDDGAFVKFLSKKGS CCCCHHHHHHHHCCC | 33.85 | 24489116 | |
| 198 | Ubiquitination | KDDGAFVKFLSKKGS CCCCHHHHHHHHCCC | 33.85 | 22817900 | |
| 202 | Ubiquitination | AFVKFLSKKGSLENN HHHHHHHHCCCHHCC | 64.40 | 22817900 | |
| 203 | Ubiquitination | FVKFLSKKGSLENNI HHHHHHHCCCHHCCH | 50.81 | 23749301 | |
| 205 | Phosphorylation | KFLSKKGSLENNIRE HHHHHCCCHHCCHHH | 41.19 | 22369663 | |
| 216 | Phosphorylation | NIREFPEYFAAQA-- CHHHCHHHHHHCC-- | 9.96 | 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 RL10_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RL10_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 RL10_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-104, AND MASSSPECTROMETRY. | |
| "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-143 AND SER-205, ANDMASS SPECTROMETRY. | |
