UniProt ID | RT18C_HUMAN | |
---|---|---|
UniProt AC | Q9Y3D5 | |
Protein Name | 28S ribosomal protein S18c, mitochondrial | |
Gene Name | MRPS18C | |
Organism | Homo sapiens (Human). | |
Sequence Length | 142 | |
Subcellular Localization | Mitochondrion . | |
Protein Description | ||
Protein Sequence | MAAVVAVCGGLGRKKLTHLVTAAVSLTHPGTHTVLWRRGCSQQVSSNEDLPISMENPYKEPLKKCILCGKHVDYKNVQLLSQFVSPFTGCIYGRHITGLCGKKQKEITKAIKRAQIMGFMPVTYKDPAYLKDPKVCNIRYRE | |
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 |
---|---|---|---|---|---|
17 | Phosphorylation | GLGRKKLTHLVTAAV CCCHHHHHHHHHHHH | 23.26 | - | |
21 | Phosphorylation | KKLTHLVTAAVSLTH HHHHHHHHHHHHCCC | 18.43 | 22468782 | |
25 | Phosphorylation | HLVTAAVSLTHPGTH HHHHHHHHCCCCCCC | 23.87 | 22468782 | |
33 | Phosphorylation | LTHPGTHTVLWRRGC CCCCCCCEEEEECCC | 19.68 | 22468782 | |
53 | Phosphorylation | SNEDLPISMENPYKE CCCCCCCCCCCCCCC | 20.36 | 30576142 | |
64 | Malonylation | PYKEPLKKCILCGKH CCCCCHHHHHHCCCC | 33.90 | 26320211 | |
102 | 2-Hydroxyisobutyrylation | HITGLCGKKQKEITK HHHHCCCHHHHHHHH | 51.54 | - | |
105 | Acetylation | GLCGKKQKEITKAIK HCCCHHHHHHHHHHH | 61.02 | 20167786 | |
109 | Acetylation | KKQKEITKAIKRAQI HHHHHHHHHHHHHHH | 54.50 | 20167786 | |
125 | Acetylation | GFMPVTYKDPAYLKD CEEECEECCHHHHCC | 48.12 | 30590473 | |
125 | Ubiquitination | GFMPVTYKDPAYLKD CEEECEECCHHHHCC | 48.12 | 21890473 | |
131 | Acetylation | YKDPAYLKDPKVCNI ECCHHHHCCCCCCCC | 60.35 | 23236377 | |
131 | Malonylation | YKDPAYLKDPKVCNI ECCHHHHCCCCCCCC | 60.35 | 30639696 | |
131 | Succinylation | YKDPAYLKDPKVCNI ECCHHHHCCCCCCCC | 60.35 | 27452117 | |
134 | Malonylation | PAYLKDPKVCNIRYR HHHHCCCCCCCCEEC | 70.34 | 26320211 | |
134 | Acetylation | PAYLKDPKVCNIRYR HHHHCCCCCCCCEEC | 70.34 | 23236377 |
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 RT18C_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RT18C_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 RT18C_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of RT18C_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
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-131, AND MASS SPECTROMETRY. |