UniProt ID | RL9A_YEAST | |
---|---|---|
UniProt AC | P05738 | |
Protein Name | 60S ribosomal protein L9-A {ECO:0000303|PubMed:9559554} | |
Gene Name | RPL9A {ECO:0000303|PubMed:9559554} | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 191 | |
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 | MKYIQTEQQIEVPEGVTVSIKSRIVKVVGPRGTLTKNLKHIDVTFTKVNNQLIKVAVHNGGRKHVAALRTVKSLVDNMITGVTKGYKYKMRYVYAHFPINVNIVEKDGAKFIEVRNFLGDKKIRNVPVRDGVTIEFSTNVKDEIVLSGNSVEDVSQNAADLQQICRVRNKDIRKFLDGIYVSHKGFITEDL | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Ubiquitination | ------MKYIQTEQQ ------CCEECEEEE | 51.57 | 23749301 | |
3 | Phosphorylation | -----MKYIQTEQQI -----CCEECEEEEE | 9.28 | 30377154 | |
6 | Phosphorylation | --MKYIQTEQQIEVP --CCEECEEEEEECC | 26.63 | 30377154 | |
17 | Phosphorylation | IEVPEGVTVSIKSRI EECCCCCEEEEECCE | 21.28 | 29136822 | |
19 | Phosphorylation | VPEGVTVSIKSRIVK CCCCCEEEEECCEEE | 18.22 | 30377154 | |
21 | Ubiquitination | EGVTVSIKSRIVKVV CCCEEEEECCEEEEE | 26.61 | 23749301 | |
21 | Acetylation | EGVTVSIKSRIVKVV CCCEEEEECCEEEEE | 26.61 | 24489116 | |
21 | Succinylation | EGVTVSIKSRIVKVV CCCEEEEECCEEEEE | 26.61 | 23954790 | |
26 | Ubiquitination | SIKSRIVKVVGPRGT EEECCEEEEECCCCC | 28.91 | 23749301 | |
26 | 2-Hydroxyisobutyrylation | SIKSRIVKVVGPRGT EEECCEEEEECCCCC | 28.91 | - | |
26 | Acetylation | SIKSRIVKVVGPRGT EEECCEEEEECCCCC | 28.91 | 22865919 | |
36 | 2-Hydroxyisobutyrylation | GPRGTLTKNLKHIDV CCCCCCCCCCCEEEE | 64.49 | - | |
36 | Ubiquitination | GPRGTLTKNLKHIDV CCCCCCCCCCCEEEE | 64.49 | 22817900 | |
36 | Acetylation | GPRGTLTKNLKHIDV CCCCCCCCCCCEEEE | 64.49 | 24489116 | |
36 | Succinylation | GPRGTLTKNLKHIDV CCCCCCCCCCCEEEE | 64.49 | 23954790 | |
39 | Ubiquitination | GTLTKNLKHIDVTFT CCCCCCCCEEEEEEE | 48.16 | 23749301 | |
39 | Acetylation | GTLTKNLKHIDVTFT CCCCCCCCEEEEEEE | 48.16 | 24489116 | |
39 | 2-Hydroxyisobutyrylation | GTLTKNLKHIDVTFT CCCCCCCCEEEEEEE | 48.16 | - | |
47 | Ubiquitination | HIDVTFTKVNNQLIK EEEEEEEEECCEEEE | 38.48 | 23749301 | |
47 | Acetylation | HIDVTFTKVNNQLIK EEEEEEEEECCEEEE | 38.48 | 24489116 | |
54 | Acetylation | KVNNQLIKVAVHNGG EECCEEEEEEEECCC | 32.50 | 24489116 | |
63 | 2-Hydroxyisobutyrylation | AVHNGGRKHVAALRT EEECCCHHHHHHHHH | 45.78 | - | |
70 | Phosphorylation | KHVAALRTVKSLVDN HHHHHHHHHHHHHHH | 32.89 | 30377154 | |
72 | 2-Hydroxyisobutyrylation | VAALRTVKSLVDNMI HHHHHHHHHHHHHHH | 37.14 | - | |
72 | Ubiquitination | VAALRTVKSLVDNMI HHHHHHHHHHHHHHH | 37.14 | 17644757 | |
72 | Acetylation | VAALRTVKSLVDNMI HHHHHHHHHHHHHHH | 37.14 | 24489116 | |
73 | Phosphorylation | AALRTVKSLVDNMIT HHHHHHHHHHHHHHH | 29.32 | 28152593 | |
80 | Phosphorylation | SLVDNMITGVTKGYK HHHHHHHHCCCCCCE | 18.16 | 28152593 | |
83 | Phosphorylation | DNMITGVTKGYKYKM HHHHHCCCCCCEEEE | 21.79 | 30377154 | |
84 | Succinylation | NMITGVTKGYKYKMR HHHHCCCCCCEEEEE | 58.81 | 23954790 | |
84 | Acetylation | NMITGVTKGYKYKMR HHHHCCCCCCEEEEE | 58.81 | 24489116 | |
84 | Ubiquitination | NMITGVTKGYKYKMR HHHHCCCCCCEEEEE | 58.81 | 23749301 | |
87 | Ubiquitination | TGVTKGYKYKMRYVY HCCCCCCEEEEEEEE | 47.25 | 22817900 | |
89 | Ubiquitination | VTKGYKYKMRYVYAH CCCCCEEEEEEEEEE | 16.85 | 22817900 | |
106 | Succinylation | INVNIVEKDGAKFIE EEEEEEECCCCEEEE | 51.04 | 23954790 | |
106 | Ubiquitination | INVNIVEKDGAKFIE EEEEEEECCCCEEEE | 51.04 | 23749301 | |
106 | Acetylation | INVNIVEKDGAKFIE EEEEEEECCCCEEEE | 51.04 | 24489116 | |
106 | 2-Hydroxyisobutyrylation | INVNIVEKDGAKFIE EEEEEEECCCCEEEE | 51.04 | - | |
110 | Ubiquitination | IVEKDGAKFIEVRNF EEECCCCEEEEEEEC | 53.02 | 23749301 | |
110 | Acetylation | IVEKDGAKFIEVRNF EEECCCCEEEEEEEC | 53.02 | 24489116 | |
110 | 2-Hydroxyisobutyrylation | IVEKDGAKFIEVRNF EEECCCCEEEEEEEC | 53.02 | - | |
121 | Acetylation | VRNFLGDKKIRNVPV EEECCCCCCCCCCEE | 48.58 | 25381059 | |
121 | Ubiquitination | VRNFLGDKKIRNVPV EEECCCCCCCCCCEE | 48.58 | 23749301 | |
122 | Ubiquitination | RNFLGDKKIRNVPVR EECCCCCCCCCCEEC | 52.19 | 22817900 | |
133 | Phosphorylation | VPVRDGVTIEFSTNV CEECCCEEEEEECCC | 21.96 | 27017623 | |
137 | Phosphorylation | DGVTIEFSTNVKDEI CCEEEEEECCCCCEE | 13.29 | 27017623 | |
138 | Phosphorylation | GVTIEFSTNVKDEIV CEEEEEECCCCCEEE | 49.72 | 27017623 | |
147 | Phosphorylation | VKDEIVLSGNSVEDV CCCEEEECCCCHHHH | 25.65 | 30377154 | |
150 | Phosphorylation | EIVLSGNSVEDVSQN EEEECCCCHHHHHHC | 30.34 | 30377154 | |
174 | Acetylation | VRNKDIRKFLDGIYV HCCHHHHHHHCEEEE | 51.08 | 24489116 | |
174 | 2-Hydroxyisobutyrylation | VRNKDIRKFLDGIYV HCCHHHHHHHCEEEE | 51.08 | - | |
174 | Ubiquitination | VRNKDIRKFLDGIYV HCCHHHHHHHCEEEE | 51.08 | 17644757 | |
180 | Phosphorylation | RKFLDGIYVSHKGFI HHHHCEEEEEECCCC | 11.05 | 28889911 | |
182 | Phosphorylation | FLDGIYVSHKGFITE HHCEEEEEECCCCCC | 11.51 | 21440633 | |
184 | Ubiquitination | DGIYVSHKGFITEDL CEEEEEECCCCCCCC | 48.27 | 23749301 |
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 RL9A_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RL9A_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 RL9A_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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