| UniProt ID | RL8_MOUSE | |
|---|---|---|
| UniProt AC | P62918 | |
| Protein Name | 60S ribosomal protein L8 | |
| Gene Name | Rpl8 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 257 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | Component of the large ribosomal subunit.. | |
| Protein Sequence | MGRVIRGQRKGAGSVFRAHVKHRKGAARLRAVDFAERHGYIKGIVKDIIHDPGRGAPLAKVVFRDPYRFKKRTELFIAAEGIHTGQFVYCGKKAQLNIGNVLPVGTMPEGTIVCCLEEKPGDRGKLARASGNYATVISHNPETKKTRVKLPSGSKKVISSANRAVVGVVAGGGRIDKPILKAGRAYHKYKAKRNCWPRVRGVAMNPVEHPFGGGNHQHIGKPSTIRRDAPAGRKVGLIAARRTGRLRGTKTVQEKEN | |
| 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 |
|---|---|---|---|---|---|
| 14 | Phosphorylation | GQRKGAGSVFRAHVK CCCCCCCHHHHHHHC | 19.97 | 24453211 | |
| 46 | Ubiquitination | GYIKGIVKDIIHDPG CCCHHHHHHHHCCCC | 41.09 | - | |
| 46 | Acetylation | GYIKGIVKDIIHDPG CCCHHHHHHHHCCCC | 41.09 | 23806337 | |
| 60 | Succinylation | GRGAPLAKVVFRDPY CCCCCCHHEEECCCC | 46.76 | 23806337 | |
| 60 | Acetylation | GRGAPLAKVVFRDPY CCCCCCHHEEECCCC | 46.76 | 23806337 | |
| 67 | Phosphorylation | KVVFRDPYRFKKRTE HEEECCCCCCCCCEE | 32.73 | 29514104 | |
| 92 | Acetylation | GQFVYCGKKAQLNIG CCEEECCCCEEEECC | 41.18 | 2387935 | |
| 93 | Acetylation | QFVYCGKKAQLNIGN CEEECCCCEEEECCC | 27.01 | 7630765 | |
| 114 | S-palmitoylation | MPEGTIVCCLEEKPG CCCCEEEEECCCCCC | 1.61 | 28526873 | |
| 114 | Glutathionylation | MPEGTIVCCLEEKPG CCCCEEEEECCCCCC | 1.61 | 24333276 | |
| 115 | Glutathionylation | PEGTIVCCLEEKPGD CCCEEEEECCCCCCC | 3.57 | 24333276 | |
| 130 | Phosphorylation | RGKLARASGNYATVI CCHHHHHCCCEEEEE | 23.24 | 28066266 | |
| 133 | Phosphorylation | LARASGNYATVISHN HHHHCCCEEEEEECC | 13.74 | 29514104 | |
| 138 | Phosphorylation | GNYATVISHNPETKK CCEEEEEECCCCCCC | 16.93 | 25338131 | |
| 144 | Ubiquitination | ISHNPETKKTRVKLP EECCCCCCCEEEECC | 50.95 | - | |
| 144 | Malonylation | ISHNPETKKTRVKLP EECCCCCCCEEEECC | 50.95 | 26320211 | |
| 144 | Acetylation | ISHNPETKKTRVKLP EECCCCCCCEEEECC | 50.95 | 23201123 | |
| 145 | Ubiquitination | SHNPETKKTRVKLPS ECCCCCCCEEEECCC | 49.32 | - | |
| 145 | Acetylation | SHNPETKKTRVKLPS ECCCCCCCEEEECCC | 49.32 | 2381893 | |
| 149 | Malonylation | ETKKTRVKLPSGSKK CCCCEEEECCCCCCE | 51.92 | 26320211 | |
| 152 | Phosphorylation | KTRVKLPSGSKKVIS CEEEECCCCCCEEHH | 67.16 | 29176673 | |
| 154 | Phosphorylation | RVKLPSGSKKVISSA EEECCCCCCEEHHCC | 33.37 | 29176673 | |
| 155 | Acetylation | VKLPSGSKKVISSAN EECCCCCCEEHHCCC | 55.36 | 7630775 | |
| 177 | Acetylation | AGGGRIDKPILKAGR ECCCCCCHHHHHCHH | 31.42 | 23201123 | |
| 195 | Glutathionylation | KYKAKRNCWPRVRGV HHHCCCCCCCCCCCE | 6.50 | 24333276 | |
| 195 | S-nitrosylation | KYKAKRNCWPRVRGV HHHCCCCCCCCCCCE | 6.50 | 21278135 | |
| 195 | S-nitrosocysteine | KYKAKRNCWPRVRGV HHHCCCCCCCCCCCE | 6.50 | - | |
| 216 | Hydroxylation | HPFGGGNHQHIGKPS CCCCCCCCCCCCCCC | 24.70 | - | |
| 251 | Phosphorylation | GRLRGTKTVQEKEN- CCCCCCCCHHHCCC- | 27.53 | 29514104 |
| 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 RL8_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 216 | H | Hydroxylation |
| - |
* 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 RL8_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of RL8_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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