| UniProt ID | RM50_HUMAN | |
|---|---|---|
| UniProt AC | Q8N5N7 | |
| Protein Name | 39S ribosomal protein L50, mitochondrial | |
| Gene Name | MRPL50 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 158 | |
| Subcellular Localization | Mitochondrion . | |
| Protein Description | ||
| Protein Sequence | MAARSVSGITRRVFMWTVSGTPCREFWSRFRKEKEPVVVETVEEKKEPILVCPPLRSRAYTPPEDLQSRLESYVKEVFGSSLPSNWQDISLEDSRLKFNLLAHLADDLGHVVPNSRLHQMCRVRDVLDFYNVPIQDRSKFDELSASNLPPNLKITWSY | |
| 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 |
|---|---|---|---|---|---|
| 7 | Phosphorylation | -MAARSVSGITRRVF -CCCCCCCCCCEEEE | 26.23 | 24719451 | |
| 19 | Phosphorylation | RVFMWTVSGTPCREF EEEEEEECCCCHHHH | 29.58 | 24719451 | |
| 21 | Phosphorylation | FMWTVSGTPCREFWS EEEEECCCCHHHHHH | 16.23 | 24719451 | |
| 32 | Ubiquitination | EFWSRFRKEKEPVVV HHHHHHHHCCCCEEE | 71.12 | 22817900 | |
| 34 | Ubiquitination | WSRFRKEKEPVVVET HHHHHHCCCCEEEEE | 71.06 | 22817900 | |
| 34 | Ubiquitination | WSRFRKEKEPVVVET HHHHHHCCCCEEEEE | 71.06 | 21890473 | |
| 46 | Ubiquitination | VETVEEKKEPILVCP EEECCCCCCCEEECC | 72.50 | 24816145 | |
| 60 | Phosphorylation | PPLRSRAYTPPEDLQ CCCCCCCCCCCHHHH | 20.76 | - | |
| 68 | Phosphorylation | TPPEDLQSRLESYVK CCCHHHHHHHHHHHH | 46.24 | - | |
| 139 | Ubiquitination | VPIQDRSKFDELSAS CCCCCHHHHHHHHHH | 58.70 | 22817900 | |
| 155 | Phosphorylation | LPPNLKITWSY---- CCCCCEEEECC---- | 13.53 | 17924679 | |
| 157 | Phosphorylation | PNLKITWSY------ CCCEEEECC------ | 16.59 | 17924679 | |
| 158 | Phosphorylation | NLKITWSY------- CCEEEECC------- | 17.71 | 17924679 |
| 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 RM50_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RM50_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 RM50_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 |
| "Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-155; SER-157 ANDTYR-158, AND MASS SPECTROMETRY. | |