UniProt ID | RL8_HUMAN | |
---|---|---|
UniProt AC | P62917 | |
Protein Name | 60S ribosomal protein L8 | |
Gene Name | RPL8 | |
Organism | Homo sapiens (Human). | |
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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
10 | Sumoylation | RVIRGQRKGAGSVFR CEECCCCCCCCHHHH | 45.27 | - | |
10 | Ubiquitination | RVIRGQRKGAGSVFR CEECCCCCCCCHHHH | 45.27 | 24816145 | |
10 | Sumoylation | RVIRGQRKGAGSVFR CEECCCCCCCCHHHH | 45.27 | - | |
14 | Phosphorylation | GQRKGAGSVFRAHVK CCCCCCCHHHHHHHC | 19.97 | 23911959 | |
37 | Methylation | RAVDFAERHGYIKGI HHHHHHHHHCCCHHH | 25.71 | 115492307 | |
40 | Phosphorylation | DFAERHGYIKGIVKD HHHHHHCCCHHHHHH | 8.04 | 28152594 | |
42 | 2-Hydroxyisobutyrylation | AERHGYIKGIVKDII HHHHCCCHHHHHHHH | 33.82 | - | |
42 | Succinylation | AERHGYIKGIVKDII HHHHCCCHHHHHHHH | 33.82 | 23954790 | |
42 | Ubiquitination | AERHGYIKGIVKDII HHHHCCCHHHHHHHH | 33.82 | 23000965 | |
42 | Sumoylation | AERHGYIKGIVKDII HHHHCCCHHHHHHHH | 33.82 | 28112733 | |
42 | Acetylation | AERHGYIKGIVKDII HHHHCCCHHHHHHHH | 33.82 | 26051181 | |
46 | Ubiquitination | GYIKGIVKDIIHDPG CCCHHHHHHHHCCCC | 41.09 | 23000965 | |
46 | Succinylation | GYIKGIVKDIIHDPG CCCHHHHHHHHCCCC | 41.09 | 23954790 | |
46 | 2-Hydroxyisobutyrylation | GYIKGIVKDIIHDPG CCCHHHHHHHHCCCC | 41.09 | - | |
46 | Acetylation | GYIKGIVKDIIHDPG CCCHHHHHHHHCCCC | 41.09 | 23749302 | |
54 | Methylation | DIIHDPGRGAPLAKV HHHCCCCCCCCCHHE | 43.41 | 115492315 | |
60 | 2-Hydroxyisobutyrylation | GRGAPLAKVVFRDPY CCCCCCHHEEECCCC | 46.76 | - | |
60 | Ubiquitination | GRGAPLAKVVFRDPY CCCCCCHHEEECCCC | 46.76 | 23000965 | |
60 | Neddylation | GRGAPLAKVVFRDPY CCCCCCHHEEECCCC | 46.76 | 32015554 | |
67 | Phosphorylation | KVVFRDPYRFKKRTE HEEECCCCCCCCCEE | 32.73 | 28152594 | |
73 | Phosphorylation | PYRFKKRTELFIAAE CCCCCCCEEEEEEEE | 46.01 | 20068231 | |
84 | Phosphorylation | IAAEGIHTGQFVYCG EEEECCCCCCEEECC | 30.66 | 28152594 | |
89 | Phosphorylation | IHTGQFVYCGKKAQL CCCCCEEECCCCEEE | 9.21 | 28152594 | |
92 | Acetylation | GQFVYCGKKAQLNIG CCEEECCCCEEEECC | 41.18 | 25953088 | |
92 | 2-Hydroxyisobutyrylation | GQFVYCGKKAQLNIG CCEEECCCCEEEECC | 41.18 | - | |
92 | Ubiquitination | GQFVYCGKKAQLNIG CCEEECCCCEEEECC | 41.18 | 21963094 | |
93 | 2-Hydroxyisobutyrylation | QFVYCGKKAQLNIGN CEEECCCCEEEECCC | 27.01 | - | |
93 | Ubiquitination | QFVYCGKKAQLNIGN CEEECCCCEEEECCC | 27.01 | 22817900 | |
106 | Phosphorylation | GNVLPVGTMPEGTIV CCEECCEECCCCEEE | 29.77 | - | |
107 | Sulfoxidation | NVLPVGTMPEGTIVC CEECCEECCCCEEEE | 2.04 | 30846556 | |
111 | Phosphorylation | VGTMPEGTIVCCLEE CEECCCCEEEEECCC | 14.47 | - | |
114 | S-palmitoylation | MPEGTIVCCLEEKPG CCCCEEEEECCCCCC | 1.61 | 19801377 | |
119 | Acetylation | IVCCLEEKPGDRGKL EEEECCCCCCCCCHH | 44.95 | 25953088 | |
119 | Ubiquitination | IVCCLEEKPGDRGKL EEEECCCCCCCCCHH | 44.95 | 21906983 | |
125 | Ubiquitination | EKPGDRGKLARASGN CCCCCCCHHHHHCCC | 39.61 | 23503661 | |
130 | Phosphorylation | RGKLARASGNYATVI CCHHHHHCCCEEEEE | 23.24 | 28152594 | |
133 | Phosphorylation | LARASGNYATVISHN HHHHCCCEEEEEECC | 13.74 | 25159151 | |
133 | Nitration | LARASGNYATVISHN HHHHCCCEEEEEECC | 13.74 | - | |
135 | Phosphorylation | RASGNYATVISHNPE HHCCCEEEEEECCCC | 14.17 | 28442448 | |
138 | Phosphorylation | GNYATVISHNPETKK CCEEEEEECCCCCCC | 16.93 | 28442448 | |
143 | Phosphorylation | VISHNPETKKTRVKL EEECCCCCCCEEEEC | 38.81 | 24117733 | |
144 | Ubiquitination | ISHNPETKKTRVKLP EECCCCCCCEEEECC | 50.95 | 21906983 | |
144 | Sumoylation | ISHNPETKKTRVKLP EECCCCCCCEEEECC | 50.95 | - | |
144 | 2-Hydroxyisobutyrylation | ISHNPETKKTRVKLP EECCCCCCCEEEECC | 50.95 | - | |
144 | Acetylation | ISHNPETKKTRVKLP EECCCCCCCEEEECC | 50.95 | 23236377 | |
145 | Ubiquitination | SHNPETKKTRVKLPS ECCCCCCCEEEECCC | 49.32 | 21963094 | |
149 | Sumoylation | ETKKTRVKLPSGSKK CCCCEEEECCCCCCE | 51.92 | 28112733 | |
149 | 2-Hydroxyisobutyrylation | ETKKTRVKLPSGSKK CCCCEEEECCCCCCE | 51.92 | - | |
149 | Acetylation | ETKKTRVKLPSGSKK CCCCEEEECCCCCCE | 51.92 | 26051181 | |
149 | Ubiquitination | ETKKTRVKLPSGSKK CCCCEEEECCCCCCE | 51.92 | 27667366 | |
152 | Phosphorylation | KTRVKLPSGSKKVIS CEEEECCCCCCEEHH | 67.16 | 20860994 | |
154 | O-linked_Glycosylation | RVKLPSGSKKVISSA EEECCCCCCEEHHCC | 33.37 | 31492838 | |
154 | Phosphorylation | RVKLPSGSKKVISSA EEECCCCCCEEHHCC | 33.37 | 23312004 | |
155 | Acetylation | VKLPSGSKKVISSAN EECCCCCCEEHHCCC | 55.36 | 25953088 | |
155 | Ubiquitination | VKLPSGSKKVISSAN EECCCCCCEEHHCCC | 55.36 | 24816145 | |
156 | Ubiquitination | KLPSGSKKVISSANR ECCCCCCEEHHCCCC | 46.64 | 27667366 | |
156 | 2-Hydroxyisobutyrylation | KLPSGSKKVISSANR ECCCCCCEEHHCCCC | 46.64 | - | |
159 | Phosphorylation | SGSKKVISSANRAVV CCCCEEHHCCCCEEE | 26.78 | 21406692 | |
160 | Phosphorylation | GSKKVISSANRAVVG CCCEEHHCCCCEEEE | 20.59 | 21406692 | |
177 | Ubiquitination | AGGGRIDKPILKAGR ECCCCCCHHHHHCHH | 31.42 | 23000965 | |
177 | Sumoylation | AGGGRIDKPILKAGR ECCCCCCHHHHHCHH | 31.42 | - | |
177 | Sumoylation | AGGGRIDKPILKAGR ECCCCCCHHHHHCHH | 31.42 | - | |
177 | Acetylation | AGGGRIDKPILKAGR ECCCCCCHHHHHCHH | 31.42 | 26822725 | |
181 | Ubiquitination | RIDKPILKAGRAYHK CCCHHHHHCHHHHHH | 49.90 | 23000965 | |
181 | Acetylation | RIDKPILKAGRAYHK CCCHHHHHCHHHHHH | 49.90 | 26051181 | |
188 | Ubiquitination | KAGRAYHKYKAKRNC HCHHHHHHHHCCCCC | 35.45 | 21906983 | |
190 | Ubiquitination | GRAYHKYKAKRNCWP HHHHHHHHCCCCCCC | 52.84 | 22817900 | |
192 | Ubiquitination | AYHKYKAKRNCWPRV HHHHHHCCCCCCCCC | 39.74 | 22817900 | |
192 | Methylation | AYHKYKAKRNCWPRV HHHHHHCCCCCCCCC | 39.74 | 116252491 | |
216 | Hydroxylation | HPFGGGNHQHIGKPS CCCCCCCCCCCCCCC | 24.70 | 23103944 | |
234 | 2-Hydroxyisobutyrylation | RDAPAGRKVGLIAAR CCCCCCCCEEEEEEH | 39.47 | - | |
234 | Sumoylation | RDAPAGRKVGLIAAR CCCCCCCCEEEEEEH | 39.47 | 28112733 | |
234 | Ubiquitination | RDAPAGRKVGLIAAR CCCCCCCCEEEEEEH | 39.47 | 27667366 | |
234 | Sumoylation | RDAPAGRKVGLIAAR CCCCCCCCEEEEEEH | 39.47 | - | |
242 | Methylation | VGLIAARRTGRLRGT EEEEEEHHCCCCCCC | 36.48 | 24376817 | |
242 | Dimethylation | VGLIAARRTGRLRGT EEEEEEHHCCCCCCC | 36.48 | - | |
250 | Ubiquitination | TGRLRGTKTVQEKEN CCCCCCCCCHHHCCC | 49.91 | 24816145 | |
250 | Sumoylation | TGRLRGTKTVQEKEN CCCCCCCCCHHHCCC | 49.91 | 28112733 | |
255 | Ubiquitination | GTKTVQEKEN----- CCCCHHHCCC----- | 45.53 | 33845483 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
130 | S | Phosphorylation | Kinase | AURKB | Q96GD4 | GPS |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
216 | H | Hydroxylation |
| 23103944 |
* 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_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-46, AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-133, AND MASSSPECTROMETRY. |