| UniProt ID | RL18_HUMAN | |
|---|---|---|
| UniProt AC | Q07020 | |
| Protein Name | 60S ribosomal protein L18 | |
| Gene Name | RPL18 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 188 | |
| Subcellular Localization | Cytoplasm, cytosol . Cytoplasm . Rough endoplasmic reticulum . Detected on cytosolic polysomes (PubMed:25957688). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). | |
| Protein Description | Component of the large ribosomal subunit.. | |
| Protein Sequence | MGVDIRHNKDRKVRRKEPKSQDIYLRLLVKLYRFLARRTNSTFNQVVLKRLFMSRTNRPPLSLSRMIRKMKLPGRENKTAVVVGTITDDVRVQEVPKLKVCALRVTSRARSRILRAGGKILTFDQLALDSPKGCGTVLLSGPRKGREVYRHFGKAPGTPHSHTKPYVRSKGRKFERARGRRASRGYKN | |
| 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 |
|---|---|---|---|---|---|
| 6 | Methylation | --MGVDIRHNKDRKV --CCCCCCCCCCCCC | 23.90 | 115491775 | |
| 19 | Acetylation | KVRRKEPKSQDIYLR CCCCCCCCCHHHHHH | 62.94 | 27452117 | |
| 19 | Ubiquitination | KVRRKEPKSQDIYLR CCCCCCCCCHHHHHH | 62.94 | - | |
| 20 | Ubiquitination | VRRKEPKSQDIYLRL CCCCCCCCHHHHHHH | 43.74 | - | |
| 26 | Methylation | KSQDIYLRLLVKLYR CCHHHHHHHHHHHHH | 14.70 | 115491785 | |
| 30 | Acetylation | IYLRLLVKLYRFLAR HHHHHHHHHHHHHHH | 39.51 | 25825284 | |
| 30 | 2-Hydroxyisobutyrylation | IYLRLLVKLYRFLAR HHHHHHHHHHHHHHH | 39.51 | - | |
| 30 | Ubiquitination | IYLRLLVKLYRFLAR HHHHHHHHHHHHHHH | 39.51 | 21906983 | |
| 39 | Phosphorylation | YRFLARRTNSTFNQV HHHHHHHCCCCHHHH | 28.15 | 28450419 | |
| 41 | Phosphorylation | FLARRTNSTFNQVVL HHHHHCCCCHHHHHH | 33.49 | 28450419 | |
| 42 | Phosphorylation | LARRTNSTFNQVVLK HHHHCCCCHHHHHHH | 28.77 | 28450419 | |
| 49 | Acetylation | TFNQVVLKRLFMSRT CHHHHHHHHHHHCCC | 35.13 | 26051181 | |
| 49 | Ubiquitination | TFNQVVLKRLFMSRT CHHHHHHHHHHHCCC | 35.13 | 21890473 | |
| 62 | Phosphorylation | RTNRPPLSLSRMIRK CCCCCCCCHHHHHHH | 30.03 | 28450419 | |
| 64 | Phosphorylation | NRPPLSLSRMIRKMK CCCCCCHHHHHHHCC | 19.20 | 28450419 | |
| 65 | Methylation | RPPLSLSRMIRKMKL CCCCCHHHHHHHCCC | 29.82 | 115491805 | |
| 78 | Ubiquitination | KLPGRENKTAVVVGT CCCCCCCCEEEEEEE | 32.86 | 21906983 | |
| 79 | Phosphorylation | LPGRENKTAVVVGTI CCCCCCCEEEEEEEE | 35.94 | 23911959 | |
| 85 | Phosphorylation | KTAVVVGTITDDVRV CEEEEEEEECCCCCH | 14.75 | - | |
| 87 | Phosphorylation | AVVVGTITDDVRVQE EEEEEEECCCCCHHC | 26.45 | 22210691 | |
| 91 | Methylation | GTITDDVRVQEVPKL EEECCCCCHHCCCCC | 31.25 | 115491795 | |
| 97 | Ubiquitination | VRVQEVPKLKVCALR CCHHCCCCCEEEEEH | 67.14 | 21906983 | |
| 97 | Acetylation | VRVQEVPKLKVCALR CCHHCCCCCEEEEEH | 67.14 | 25953088 | |
| 97 | 2-Hydroxyisobutyrylation | VRVQEVPKLKVCALR CCHHCCCCCEEEEEH | 67.14 | - | |
| 99 | Ubiquitination | VQEVPKLKVCALRVT HHCCCCCEEEEEHHH | 41.20 | 21906983 | |
| 99 | Acetylation | VQEVPKLKVCALRVT HHCCCCCEEEEEHHH | 41.20 | 27452117 | |
| 106 | Phosphorylation | KVCALRVTSRARSRI EEEEEHHHHHHHHHH | 13.18 | 20363803 | |
| 111 | Phosphorylation | RVTSRARSRILRAGG HHHHHHHHHHHHCCC | 23.76 | 20363803 | |
| 119 | 2-Hydroxyisobutyrylation | RILRAGGKILTFDQL HHHHCCCEEEEEEEE | 33.36 | - | |
| 119 | Sumoylation | RILRAGGKILTFDQL HHHHCCCEEEEEEEE | 33.36 | 28112733 | |
| 119 | Ubiquitination | RILRAGGKILTFDQL HHHHCCCEEEEEEEE | 33.36 | 21906983 | |
| 119 | Acetylation | RILRAGGKILTFDQL HHHHCCCEEEEEEEE | 33.36 | 23236377 | |
| 122 | Phosphorylation | RAGGKILTFDQLALD HCCCEEEEEEEECCC | 28.74 | 23403867 | |
| 125 | Acetylation | GKILTFDQLALDSPK CEEEEEEEECCCCCC | 25.17 | 19608861 | |
| 130 | Phosphorylation | FDQLALDSPKGCGTV EEEECCCCCCCCCEE | 29.39 | 19664994 | |
| 132 | Ubiquitination | QLALDSPKGCGTVLL EECCCCCCCCCEEEE | 71.44 | - | |
| 132 | Acetylation | QLALDSPKGCGTVLL EECCCCCCCCCEEEE | 71.44 | 26051181 | |
| 134 | S-palmitoylation | ALDSPKGCGTVLLSG CCCCCCCCCEEEECC | 5.29 | 29575903 | |
| 134 | Glutathionylation | ALDSPKGCGTVLLSG CCCCCCCCCEEEECC | 5.29 | 22555962 | |
| 136 | Phosphorylation | DSPKGCGTVLLSGPR CCCCCCCEEEECCCC | 16.44 | 24732914 | |
| 140 | Phosphorylation | GCGTVLLSGPRKGRE CCCEEEECCCCCCHH | 42.46 | 25159151 | |
| 150 | Methylation | RKGREVYRHFGKAPG CCCHHHHHHCCCCCC | 24.67 | 115491765 | |
| 154 | Acetylation | EVYRHFGKAPGTPHS HHHHHCCCCCCCCCC | 50.92 | 19608861 | |
| 154 | Ubiquitination | EVYRHFGKAPGTPHS HHHHHCCCCCCCCCC | 50.92 | 19608861 | |
| 158 | Phosphorylation | HFGKAPGTPHSHTKP HCCCCCCCCCCCCCH | 19.44 | 23927012 | |
| 161 | Phosphorylation | KAPGTPHSHTKPYVR CCCCCCCCCCCHHCC | 33.77 | 23927012 | |
| 163 | Phosphorylation | PGTPHSHTKPYVRSK CCCCCCCCCHHCCCC | 36.41 | 29496963 | |
| 164 | Sumoylation | GTPHSHTKPYVRSKG CCCCCCCCHHCCCCC | 29.00 | 28112733 | |
| 164 | Acetylation | GTPHSHTKPYVRSKG CCCCCCCCHHCCCCC | 29.00 | 25825284 | |
| 164 | Ubiquitination | GTPHSHTKPYVRSKG CCCCCCCCHHCCCCC | 29.00 | - | |
| 166 | Phosphorylation | PHSHTKPYVRSKGRK CCCCCCHHCCCCCHH | 15.28 | 28152594 | |
| 183 | Phosphorylation | RARGRRASRGYKN-- HHHHHHHCCCCCC-- | 25.15 | 23882029 |
| 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 RL18_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RL18_HUMAN !! | ||||||
* 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 RL18_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-154, AND MASS SPECTROMETRY. | |
| Phosphorylation | |
| Reference | PubMed |
| "Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND MASSSPECTROMETRY. | |
| "A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130 AND THR-158, ANDMASS SPECTROMETRY. | |
| "Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND MASSSPECTROMETRY. | |
| "A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND MASSSPECTROMETRY. | |