| UniProt ID | RL23_HUMAN | |
|---|---|---|
| UniProt AC | P62829 | |
| Protein Name | 60S ribosomal protein L23 | |
| Gene Name | RPL23 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 140 | |
| Subcellular Localization | ||
| Protein Description | ||
| Protein Sequence | MSKRGRGGSSGAKFRISLGLPVGAVINCADNTGAKNLYIISVKGIKGRLNRLPAAGVGDMVMATVKKGKPELRKKVHPAVVIRQRKSYRRKDGVFLYFEDNAGVIVNNKGEMKGSAITGPVAKECADLWPRIASNAGSIA | |
| 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 |
|---|---|---|---|---|---|
| 4 | Methylation | ----MSKRGRGGSSG ----CCCCCCCCCCC | 32.50 | 83436611 | |
| 6 | Methylation | --MSKRGRGGSSGAK --CCCCCCCCCCCCE | 50.78 | 26494289 | |
| 13 | Acetylation | RGGSSGAKFRISLGL CCCCCCCEEEEECCC | 38.41 | 25825284 | |
| 13 | Ubiquitination | RGGSSGAKFRISLGL CCCCCCCEEEEECCC | 38.41 | 21906983 | |
| 13 | 2-Hydroxyisobutyrylation | RGGSSGAKFRISLGL CCCCCCCEEEEECCC | 38.41 | - | |
| 17 | Phosphorylation | SGAKFRISLGLPVGA CCCEEEEECCCCCEE | 16.48 | 25159151 | |
| 28 | S-nitrosocysteine | PVGAVINCADNTGAK CCEEEEECCCCCCCC | 3.28 | - | |
| 28 | S-nitrosylation | PVGAVINCADNTGAK CCEEEEECCCCCCCC | 3.28 | 19483679 | |
| 28 | Glutathionylation | PVGAVINCADNTGAK CCEEEEECCCCCCCC | 3.28 | 22555962 | |
| 28 | S-palmitoylation | PVGAVINCADNTGAK CCEEEEECCCCCCCC | 3.28 | 29575903 | |
| 32 | Phosphorylation | VINCADNTGAKNLYI EEECCCCCCCCCEEE | 38.78 | 21712546 | |
| 35 | Acetylation | CADNTGAKNLYIISV CCCCCCCCCEEEEEE | 49.16 | 26051181 | |
| 35 | Ubiquitination | CADNTGAKNLYIISV CCCCCCCCCEEEEEE | 49.16 | 21906983 | |
| 38 | Phosphorylation | NTGAKNLYIISVKGI CCCCCCEEEEEEECC | 12.95 | 25159151 | |
| 41 | Phosphorylation | AKNLYIISVKGIKGR CCCEEEEEEECCCHH | 14.28 | 28355574 | |
| 43 | 2-Hydroxyisobutyrylation | NLYIISVKGIKGRLN CEEEEEEECCCHHHH | 48.40 | - | |
| 43 | Ubiquitination | NLYIISVKGIKGRLN CEEEEEEECCCHHHH | 48.40 | 21890473 | |
| 43 | Acetylation | NLYIISVKGIKGRLN CEEEEEEECCCHHHH | 48.40 | 21466224 | |
| 46 | Ubiquitination | IISVKGIKGRLNRLP EEEEECCCHHHHCCC | 46.80 | - | |
| 46 | Acetylation | IISVKGIKGRLNRLP EEEEECCCHHHHCCC | 46.80 | 21466224 | |
| 60 | Sulfoxidation | PAAGVGDMVMATVKK CCCCCCHHHHEEHHC | 1.50 | 28465586 | |
| 62 | Sulfoxidation | AGVGDMVMATVKKGK CCCCHHHHEEHHCCC | 1.76 | 28465586 | |
| 64 | Phosphorylation | VGDMVMATVKKGKPE CCHHHHEEHHCCCHH | 18.11 | 21406692 | |
| 66 | Ubiquitination | DMVMATVKKGKPELR HHHHEEHHCCCHHHH | 51.99 | 21906983 | |
| 66 | 2-Hydroxyisobutyrylation | DMVMATVKKGKPELR HHHHEEHHCCCHHHH | 51.99 | - | |
| 66 | Acetylation | DMVMATVKKGKPELR HHHHEEHHCCCHHHH | 51.99 | 25953088 | |
| 67 | Ubiquitination | MVMATVKKGKPELRK HHHEEHHCCCHHHHH | 68.76 | - | |
| 69 | Ubiquitination | MATVKKGKPELRKKV HEEHHCCCHHHHHHC | 44.17 | - | |
| 69 | Acetylation | MATVKKGKPELRKKV HEEHHCCCHHHHHHC | 44.17 | 30592035 | |
| 74 | Ubiquitination | KGKPELRKKVHPAVV CCCHHHHHHCCCEEE | 72.30 | - | |
| 75 | Ubiquitination | GKPELRKKVHPAVVI CCHHHHHHCCCEEEE | 39.06 | 21906983 | |
| 87 | Phosphorylation | VVIRQRKSYRRKDGV EEEEECCCCCCCCCE | 26.51 | - | |
| 113 | Ubiquitination | VNNKGEMKGSAITGP ECCCCCCCCCCCCHH | 45.47 | 21890473 | |
| 113 | Acetylation | VNNKGEMKGSAITGP ECCCCCCCCCCCCHH | 45.47 | 26051181 | |
| 113 | 2-Hydroxyisobutyrylation | VNNKGEMKGSAITGP ECCCCCCCCCCCCHH | 45.47 | - | |
| 113 | Malonylation | VNNKGEMKGSAITGP ECCCCCCCCCCCCHH | 45.47 | 26320211 | |
| 115 | Phosphorylation | NKGEMKGSAITGPVA CCCCCCCCCCCHHHH | 15.81 | 20068231 | |
| 118 | Phosphorylation | EMKGSAITGPVAKEC CCCCCCCCHHHHHHH | 34.84 | 20068231 | |
| 123 | Ubiquitination | AITGPVAKECADLWP CCCHHHHHHHHHHHH | 54.26 | 21906983 | |
| 123 | Acetylation | AITGPVAKECADLWP CCCHHHHHHHHHHHH | 54.26 | 26051181 | |
| 125 | Glutathionylation | TGPVAKECADLWPRI CHHHHHHHHHHHHHH | 3.35 | 22555962 | |
| 125 | S-palmitoylation | TGPVAKECADLWPRI CHHHHHHHHHHHHHH | 3.35 | 29575903 | |
| 138 | Phosphorylation | RIASNAGSIA----- HHHHCCCCCC----- | 16.97 | 29514088 |
| 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 RL23_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RL23_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 RL23_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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| Phosphorylation | |
| Reference | PubMed |
| "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-17, AND MASSSPECTROMETRY. | |
| "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-38, AND MASSSPECTROMETRY. | |
