UniProt ID | RL21_HUMAN | |
---|---|---|
UniProt AC | P46778 | |
Protein Name | 60S ribosomal protein L21 | |
Gene Name | RPL21 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 160 | |
Subcellular Localization | Cytoplasm, cytosol . Cytoplasm . 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 | MTNTKGKRRGTRYMFSRPFRKHGVVPLATYMRIYKKGDIVDIKGMGTVQKGMPHKCYHGKTGRVYNVTQHAVGIVVNKQVKGKILAKRINVRIEHIKHSKSRDSFLKRVKENDQKKKEAKEKGTWVQLKRQPAPPREAHFVRTNGKEPELLEPIPYEFMA | |
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 |
---|---|---|---|---|---|
13 | Phosphorylation | GKRRGTRYMFSRPFR CCCCCCCCCCCCCCH | 11.44 | 30576142 | |
14 | Sulfoxidation | KRRGTRYMFSRPFRK CCCCCCCCCCCCCHH | 1.90 | 28183972 | |
16 | Phosphorylation | RGTRYMFSRPFRKHG CCCCCCCCCCCHHCC | 23.63 | 30576142 | |
21 | Ubiquitination | MFSRPFRKHGVVPLA CCCCCCHHCCCEEHH | 45.12 | 21890473 | |
29 | Phosphorylation | HGVVPLATYMRIYKK CCCEEHHHEEEEEEC | 26.07 | 28152594 | |
30 | Phosphorylation | GVVPLATYMRIYKKG CCEEHHHEEEEEECC | 4.45 | 28152594 | |
31 | Sulfoxidation | VVPLATYMRIYKKGD CEEHHHEEEEEECCC | 1.50 | 28183972 | |
32 | Methylation | VPLATYMRIYKKGDI EEHHHEEEEEECCCE | 20.76 | 115491871 | |
35 | Ubiquitination | ATYMRIYKKGDIVDI HHEEEEEECCCEEEC | 48.16 | - | |
36 | Ubiquitination | TYMRIYKKGDIVDIK HEEEEEECCCEEECC | 44.86 | - | |
36 | Acetylation | TYMRIYKKGDIVDIK HEEEEEECCCEEECC | 44.86 | 26051181 | |
43 | Sumoylation | KGDIVDIKGMGTVQK CCCEEECCCCEEEEC | 38.08 | - | |
43 | Acetylation | KGDIVDIKGMGTVQK CCCEEECCCCEEEEC | 38.08 | 27452117 | |
43 | 2-Hydroxyisobutyrylation | KGDIVDIKGMGTVQK CCCEEECCCCEEEEC | 38.08 | - | |
43 | Ubiquitination | KGDIVDIKGMGTVQK CCCEEECCCCEEEEC | 38.08 | 21890473 | |
45 | Sulfoxidation | DIVDIKGMGTVQKGM CEEECCCCEEEECCC | 3.27 | 28183972 | |
47 | Phosphorylation | VDIKGMGTVQKGMPH EECCCCEEEECCCCC | 15.75 | 22817900 | |
50 | Acetylation | KGMGTVQKGMPHKCY CCCEEEECCCCCCEE | 53.49 | 25953088 | |
50 | 2-Hydroxyisobutyrylation | KGMGTVQKGMPHKCY CCCEEEECCCCCCEE | 53.49 | - | |
50 | Ubiquitination | KGMGTVQKGMPHKCY CCCEEEECCCCCCEE | 53.49 | - | |
55 | 2-Hydroxyisobutyrylation | VQKGMPHKCYHGKTG EECCCCCCEECCCCC | 30.53 | - | |
55 | Ubiquitination | VQKGMPHKCYHGKTG EECCCCCCEECCCCC | 30.53 | - | |
57 | Phosphorylation | KGMPHKCYHGKTGRV CCCCCCEECCCCCCE | 20.57 | 22817900 | |
60 | Acetylation | PHKCYHGKTGRVYNV CCCEECCCCCCEEEE | 34.20 | 26051181 | |
61 | Phosphorylation | HKCYHGKTGRVYNVT CCEECCCCCCEEEEC | 34.51 | 23882029 | |
65 | Phosphorylation | HGKTGRVYNVTQHAV CCCCCCEEEECCCEE | 11.53 | 28152594 | |
68 | Phosphorylation | TGRVYNVTQHAVGIV CCCEEEECCCEEEEE | 15.82 | 28152594 | |
78 | Acetylation | AVGIVVNKQVKGKIL EEEEEECCHHCCCEE | 44.87 | 23749302 | |
78 | Malonylation | AVGIVVNKQVKGKIL EEEEEECCHHCCCEE | 44.87 | 26320211 | |
78 | Ubiquitination | AVGIVVNKQVKGKIL EEEEEECCHHCCCEE | 44.87 | 21890473 | |
81 | Ubiquitination | IVVNKQVKGKILAKR EEECCHHCCCEEEEE | 52.58 | - | |
97 | 2-Hydroxyisobutyrylation | NVRIEHIKHSKSRDS CEEEEEECCCCCHHH | 43.67 | - | |
97 | Acetylation | NVRIEHIKHSKSRDS CEEEEEECCCCCHHH | 43.67 | 25825284 | |
101 | Phosphorylation | EHIKHSKSRDSFLKR EEECCCCCHHHHHHH | 44.31 | 30266825 | |
104 | Phosphorylation | KHSKSRDSFLKRVKE CCCCCHHHHHHHHHH | 31.22 | 23401153 | |
107 | Ubiquitination | KSRDSFLKRVKENDQ CCHHHHHHHHHHHHH | 53.81 | - | |
107 | Acetylation | KSRDSFLKRVKENDQ CCHHHHHHHHHHHHH | 53.81 | 26051181 | |
107 | Methylation | KSRDSFLKRVKENDQ CCHHHHHHHHHHHHH | 53.81 | 2380247 | |
122 | Ubiquitination | KKKEAKEKGTWVQLK HHHHHHHHCCEEEEE | 62.02 | - | |
122 | Acetylation | KKKEAKEKGTWVQLK HHHHHHHHCCEEEEE | 62.02 | 25953088 | |
122 | 2-Hydroxyisobutyrylation | KKKEAKEKGTWVQLK HHHHHHHHCCEEEEE | 62.02 | - | |
122 | Malonylation | KKKEAKEKGTWVQLK HHHHHHHHCCEEEEE | 62.02 | 26320211 | |
124 | Phosphorylation | KEAKEKGTWVQLKRQ HHHHHHCCEEEEECC | 33.27 | 23403867 | |
129 | Sumoylation | KGTWVQLKRQPAPPR HCCEEEEECCCCCCC | 31.71 | - | |
129 | Succinylation | KGTWVQLKRQPAPPR HCCEEEEECCCCCCC | 31.71 | 23954790 | |
129 | Acetylation | KGTWVQLKRQPAPPR HCCEEEEECCCCCCC | 31.71 | 26051181 | |
129 | Sumoylation | KGTWVQLKRQPAPPR HCCEEEEECCCCCCC | 31.71 | - | |
129 | Ubiquitination | KGTWVQLKRQPAPPR HCCEEEEECCCCCCC | 31.71 | 21890473 | |
129 | 2-Hydroxyisobutyrylation | KGTWVQLKRQPAPPR HCCEEEEECCCCCCC | 31.71 | - | |
136 | Methylation | KRQPAPPREAHFVRT ECCCCCCCCEEEEEC | 53.31 | 115491879 | |
143 | Phosphorylation | REAHFVRTNGKEPEL CCEEEEECCCCCCHH | 42.92 | 21712546 | |
146 | Ubiquitination | HFVRTNGKEPELLEP EEEECCCCCCHHCCC | 72.64 | 2190698 | |
146 | Acetylation | HFVRTNGKEPELLEP EEEECCCCCCHHCCC | 72.64 | 26051181 | |
156 | Phosphorylation | ELLEPIPYEFMA--- HHCCCCCCCCCC--- | 23.63 | 27642862 | |
159 | Sulfoxidation | EPIPYEFMA------ CCCCCCCCC------ | 2.64 | 21406390 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
104 | S | Phosphorylation | Kinase | AURKB | Q96GD4 | GPS |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RL21_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 RL21_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
615885 | Hypotrichosis 12 (HYPT12) | |||||
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 |
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-47, AND MASSSPECTROMETRY. |