UniProt ID | RL6A_YEAST | |
---|---|---|
UniProt AC | Q02326 | |
Protein Name | 60S ribosomal protein L6-A {ECO:0000303|PubMed:9559554} | |
Gene Name | RPL6A {ECO:0000303|PubMed:9559554} | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 176 | |
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 | MSAQKAPKWYPSEDVAALKKTRKAARPQKLRASLVPGTVLILLAGRFRGKRVVYLKHLEDNTLLISGPFKVNGVPLRRVNARYVIATSTKVSVEGVNVEKFNVEYFAKEKLTKKEKKEANLFPEQQNKEIKAERVEDQKVVDKALIAEIKKTPLLKQYLSASFSLKNGDKPHMLKF | |
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 | Acetylation | ------MSAQKAPKW ------CCCCCCCCC | 39.13 | 10601260 | |
5 | Ubiquitination | ---MSAQKAPKWYPS ---CCCCCCCCCCCH | 67.39 | 22817900 | |
8 | Ubiquitination | MSAQKAPKWYPSEDV CCCCCCCCCCCHHHH | 65.31 | 23749301 | |
8 | Acetylation | MSAQKAPKWYPSEDV CCCCCCCCCCCHHHH | 65.31 | 24489116 | |
10 | Phosphorylation | AQKAPKWYPSEDVAA CCCCCCCCCHHHHHH | 11.73 | 25521595 | |
12 | Phosphorylation | KAPKWYPSEDVAALK CCCCCCCHHHHHHHH | 30.63 | 22369663 | |
19 | Ubiquitination | SEDVAALKKTRKAAR HHHHHHHHHHHHHHC | 47.58 | 23749301 | |
19 | Acetylation | SEDVAALKKTRKAAR HHHHHHHHHHHHHHC | 47.58 | 24489116 | |
20 | Ubiquitination | EDVAALKKTRKAARP HHHHHHHHHHHHHCC | 55.18 | 15699485 | |
29 | Ubiquitination | RKAARPQKLRASLVP HHHHCCHHHHHHCCC | 42.49 | 23749301 | |
29 | Acetylation | RKAARPQKLRASLVP HHHHCCHHHHHHCCC | 42.49 | 24489116 | |
33 | Phosphorylation | RPQKLRASLVPGTVL CCHHHHHHCCCCCHH | 24.38 | 22369663 | |
38 | Phosphorylation | RASLVPGTVLILLAG HHHCCCCCHHEEEEE | 13.18 | 22369663 | |
56 | Ubiquitination | GKRVVYLKHLEDNTL CCEEEEEEECCCCEE | 28.58 | 17644757 | |
66 | Phosphorylation | EDNTLLISGPFKVNG CCCEEEEECCEEECC | 40.14 | 28889911 | |
70 | Ubiquitination | LLISGPFKVNGVPLR EEEECCEEECCEECC | 37.61 | 17644757 | |
70 | Acetylation | LLISGPFKVNGVPLR EEEECCEEECCEECC | 37.61 | 24489116 | |
90 | Ubiquitination | YVIATSTKVSVEGVN EEEEECEEEEEECCC | 32.07 | 23749301 | |
92 | Phosphorylation | IATSTKVSVEGVNVE EEECEEEEEECCCHH | 18.92 | 30377154 | |
100 | Ubiquitination | VEGVNVEKFNVEYFA EECCCHHHEEHHHHH | 37.65 | 23749301 | |
108 | Ubiquitination | FNVEYFAKEKLTKKE EEHHHHHHHHCCHHH | 45.54 | 23749301 | |
110 | Ubiquitination | VEYFAKEKLTKKEKK HHHHHHHHCCHHHHH | 61.83 | 22817900 | |
113 | Ubiquitination | FAKEKLTKKEKKEAN HHHHHCCHHHHHHHC | 70.17 | 22817900 | |
114 | Ubiquitination | AKEKLTKKEKKEANL HHHHCCHHHHHHHCC | 70.32 | 22817900 | |
116 | Ubiquitination | EKLTKKEKKEANLFP HHCCHHHHHHHCCCH | 65.87 | 22817900 | |
117 | Ubiquitination | KLTKKEKKEANLFPE HCCHHHHHHHCCCHH | 64.25 | 23749301 | |
128 | Acetylation | LFPEQQNKEIKAERV CCHHHHHHHHHHHHH | 57.38 | 24489116 | |
128 | Ubiquitination | LFPEQQNKEIKAERV CCHHHHHHHHHHHHH | 57.38 | 23749301 | |
131 | Ubiquitination | EQQNKEIKAERVEDQ HHHHHHHHHHHHCCH | 45.33 | 22817900 | |
131 | Acetylation | EQQNKEIKAERVEDQ HHHHHHHHHHHHCCH | 45.33 | 24489116 | |
139 | Ubiquitination | AERVEDQKVVDKALI HHHHCCHHHHCHHHH | 57.45 | 23749301 | |
143 | Ubiquitination | EDQKVVDKALIAEIK CCHHHHCHHHHHHHH | 33.22 | 22817900 | |
150 | Ubiquitination | KALIAEIKKTPLLKQ HHHHHHHHCCHHHHH | 41.94 | 15699485 | |
151 | Ubiquitination | ALIAEIKKTPLLKQY HHHHHHHCCHHHHHH | 62.12 | 22817900 | |
156 | Ubiquitination | IKKTPLLKQYLSASF HHCCHHHHHHHHHHE | 44.58 | 23749301 | |
160 | Phosphorylation | PLLKQYLSASFSLKN HHHHHHHHHHEECCC | 19.55 | 22369663 | |
162 | Phosphorylation | LKQYLSASFSLKNGD HHHHHHHHEECCCCC | 16.40 | 22369663 | |
164 | Phosphorylation | QYLSASFSLKNGDKP HHHHHHEECCCCCCC | 35.62 | 22369663 | |
166 | Ubiquitination | LSASFSLKNGDKPHM HHHHEECCCCCCCCC | 58.65 | 22817900 | |
170 | Ubiquitination | FSLKNGDKPHMLKF- EECCCCCCCCCCCC- | 37.92 | 23749301 | |
175 | Ubiquitination | GDKPHMLKF------ CCCCCCCCC------ | 41.26 | 23749301 | |
175 | Acetylation | GDKPHMLKF------ CCCCCCCCC------ | 41.26 | 24489116 |
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 RL6A_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RL6A_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 RL6A_YEAST !! |
Kegg Drug | ||||||
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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 |
"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-12, AND MASSSPECTROMETRY. | |
"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-12, 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 SER-12 AND SER-162, AND MASSSPECTROMETRY. |