UniProt ID | RL17A_YEAST | |
---|---|---|
UniProt AC | P05740 | |
Protein Name | 60S ribosomal protein L17-A {ECO:0000303|PubMed:9559554} | |
Gene Name | RPL17A {ECO:0000303|PubMed:9559554} | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 184 | |
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 | MARYGATSTNPAKSASARGSYLRVSFKNTRETAQAINGWELTKAQKYLEQVLDHQRAIPFRRFNSSIGRTAQGKEFGVTKARWPAKSVKFVQGLLQNAAANAEAKGLDATKLYVSHIQVNQAPKQRRRTYRAHGRINKYESSPSHIELVVTEKEEAVAKAAEKKVVRLTSRQRGRIAAQKRIAA | |
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 | Phosphorylation | -MARYGATSTNPAKS -CCCCCCCCCCCCCC | 31.55 | 22369663 | |
8 | Phosphorylation | MARYGATSTNPAKSA CCCCCCCCCCCCCCC | 26.17 | 22369663 | |
9 | Phosphorylation | ARYGATSTNPAKSAS CCCCCCCCCCCCCCC | 40.65 | 22369663 | |
13 | 2-Hydroxyisobutyrylation | ATSTNPAKSASARGS CCCCCCCCCCCCCCC | 48.05 | - | |
13 | Ubiquitination | ATSTNPAKSASARGS CCCCCCCCCCCCCCC | 48.05 | 23749301 | |
14 | Phosphorylation | TSTNPAKSASARGSY CCCCCCCCCCCCCCE | 29.57 | 17287358 | |
16 | Phosphorylation | TNPAKSASARGSYLR CCCCCCCCCCCCEEE | 26.11 | 28889911 | |
20 | Phosphorylation | KSASARGSYLRVSFK CCCCCCCCEEEEEEE | 18.55 | 22369663 | |
21 | Phosphorylation | SASARGSYLRVSFKN CCCCCCCEEEEEEEC | 11.01 | 22369663 | |
25 | Phosphorylation | RGSYLRVSFKNTRET CCCEEEEEEECHHHH | 24.86 | 22369663 | |
27 | Acetylation | SYLRVSFKNTRETAQ CEEEEEEECHHHHHH | 50.32 | 24489116 | |
27 | Succinylation | SYLRVSFKNTRETAQ CEEEEEEECHHHHHH | 50.32 | 23954790 | |
27 | 2-Hydroxyisobutyrylation | SYLRVSFKNTRETAQ CEEEEEEECHHHHHH | 50.32 | - | |
32 | Phosphorylation | SFKNTRETAQAINGW EEECHHHHHHHHCHH | 22.30 | 21440633 | |
43 | Acetylation | INGWELTKAQKYLEQ HCHHHHHHHHHHHHH | 62.54 | 24489116 | |
43 | Ubiquitination | INGWELTKAQKYLEQ HCHHHHHHHHHHHHH | 62.54 | 23749301 | |
46 | Ubiquitination | WELTKAQKYLEQVLD HHHHHHHHHHHHHHH | 57.57 | 23749301 | |
46 | Acetylation | WELTKAQKYLEQVLD HHHHHHHHHHHHHHH | 57.57 | 24489116 | |
65 | Phosphorylation | IPFRRFNSSIGRTAQ CCHHHCCCCCCCCCC | 22.18 | 25533186 | |
66 | Phosphorylation | PFRRFNSSIGRTAQG CHHHCCCCCCCCCCC | 30.11 | 25533186 | |
70 | Phosphorylation | FNSSIGRTAQGKEFG CCCCCCCCCCCCCCC | 20.37 | 17287358 | |
74 | Ubiquitination | IGRTAQGKEFGVTKA CCCCCCCCCCCCCCC | 37.48 | 23749301 | |
74 | Succinylation | IGRTAQGKEFGVTKA CCCCCCCCCCCCCCC | 37.48 | 23954790 | |
74 | Acetylation | IGRTAQGKEFGVTKA CCCCCCCCCCCCCCC | 37.48 | 24489116 | |
74 | 2-Hydroxyisobutyrylation | IGRTAQGKEFGVTKA CCCCCCCCCCCCCCC | 37.48 | - | |
80 | Acetylation | GKEFGVTKARWPAKS CCCCCCCCCCCCHHH | 33.28 | 22865919 | |
80 | Ubiquitination | GKEFGVTKARWPAKS CCCCCCCCCCCCHHH | 33.28 | 23749301 | |
80 | Succinylation | GKEFGVTKARWPAKS CCCCCCCCCCCCHHH | 33.28 | 23954790 | |
80 | 2-Hydroxyisobutyrylation | GKEFGVTKARWPAKS CCCCCCCCCCCCHHH | 33.28 | - | |
86 | 2-Hydroxyisobutyrylation | TKARWPAKSVKFVQG CCCCCCHHHHHHHHH | 52.26 | - | |
86 | Ubiquitination | TKARWPAKSVKFVQG CCCCCCHHHHHHHHH | 52.26 | 22817900 | |
87 | Phosphorylation | KARWPAKSVKFVQGL CCCCCHHHHHHHHHH | 32.42 | 21440633 | |
89 | Ubiquitination | RWPAKSVKFVQGLLQ CCCHHHHHHHHHHHH | 47.08 | 23749301 | |
89 | Acetylation | RWPAKSVKFVQGLLQ CCCHHHHHHHHHHHH | 47.08 | 24489116 | |
105 | Ubiquitination | AAANAEAKGLDATKL HHHHHHHCCCCCCEE | 52.06 | 23749301 | |
105 | Succinylation | AAANAEAKGLDATKL HHHHHHHCCCCCCEE | 52.06 | 23954790 | |
105 | Acetylation | AAANAEAKGLDATKL HHHHHHHCCCCCCEE | 52.06 | 24489116 | |
111 | Ubiquitination | AKGLDATKLYVSHIQ HCCCCCCEEEEEEEE | 39.27 | 23749301 | |
111 | 2-Hydroxyisobutyrylation | AKGLDATKLYVSHIQ HCCCCCCEEEEEEEE | 39.27 | - | |
111 | Acetylation | AKGLDATKLYVSHIQ HCCCCCCEEEEEEEE | 39.27 | 24489116 | |
113 | Phosphorylation | GLDATKLYVSHIQVN CCCCCEEEEEEEECC | 11.06 | 21440633 | |
115 | Phosphorylation | DATKLYVSHIQVNQA CCCEEEEEEEECCCC | 11.00 | 28152593 | |
124 | Acetylation | IQVNQAPKQRRRTYR EECCCCHHHHHHHHH | 60.49 | 24489116 | |
124 | Ubiquitination | IQVNQAPKQRRRTYR EECCCCHHHHHHHHH | 60.49 | 23749301 | |
138 | Ubiquitination | RAHGRINKYESSPSH HHHCCCCCCCCCCCE | 48.28 | 22817900 | |
138 | Acetylation | RAHGRINKYESSPSH HHHCCCCCCCCCCCE | 48.28 | 24489116 | |
139 | Phosphorylation | AHGRINKYESSPSHI HHCCCCCCCCCCCEE | 19.29 | 29734811 | |
141 | Phosphorylation | GRINKYESSPSHIEL CCCCCCCCCCCEEEE | 44.45 | 22369663 | |
142 | Phosphorylation | RINKYESSPSHIELV CCCCCCCCCCEEEEE | 20.62 | 22369663 | |
144 | Phosphorylation | NKYESSPSHIELVVT CCCCCCCCEEEEEEE | 38.76 | 22369663 | |
153 | Acetylation | IELVVTEKEEAVAKA EEEEEECHHHHHHHH | 52.03 | 24489116 | |
153 | Ubiquitination | IELVVTEKEEAVAKA EEEEEECHHHHHHHH | 52.03 | 24961812 | |
159 | Ubiquitination | EKEEAVAKAAEKKVV CHHHHHHHHHHHHHH | 41.34 | 17644757 | |
159 | Acetylation | EKEEAVAKAAEKKVV CHHHHHHHHHHHHHH | 41.34 | 22865919 | |
159 | 2-Hydroxyisobutyrylation | EKEEAVAKAAEKKVV CHHHHHHHHHHHHHH | 41.34 | - | |
170 | Phosphorylation | KKVVRLTSRQRGRIA HHHHHHHHHHHCCHH | 30.89 | 17287358 | |
180 | 2-Hydroxyisobutyrylation | RGRIAAQKRIAA--- HCCHHHHHHHCC--- | 40.83 | - |
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 RL17A_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RL17A_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 RL17A_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 SER-14; SER-65 AND SER-66,AND MASS SPECTROMETRY. | |
"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 SER-65, AND MASSSPECTROMETRY. |