| UniProt ID | RM54_HUMAN | |
|---|---|---|
| UniProt AC | Q6P161 | |
| Protein Name | 39S ribosomal protein L54, mitochondrial | |
| Gene Name | MRPL54 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 138 | |
| Subcellular Localization | Mitochondrion . | |
| Protein Description | ||
| Protein Sequence | MATKRLFGATRTWAGWGAWELLNPATSGRLLARDYAKKPVMKGAKSGKGAVTSEALKDPDVCTDPVQLTTYAMGVNIYKEGQDVPLKPDAEYPEWLFEMNLGPPKTLEELDPESREYWRRLRKQNIWRHNRLSKNKRL | |
| 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 |
|---|---|---|---|---|---|
| 3 | Phosphorylation | -----MATKRLFGAT -----CCCCCCCCCC | 18.52 | 24719451 | |
| 62 | Glutathionylation | ALKDPDVCTDPVQLT HHCCCCCCCCCHHHE | 4.69 | 22555962 | |
| 106 | Phosphorylation | MNLGPPKTLEELDPE CCCCCCCCHHHHCHH | 45.21 | 27966365 | |
| 115 | Methylation | EELDPESREYWRRLR HHHCHHHHHHHHHHH | 39.09 | 115483797 |
| 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 RM54_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RM54_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 RM54_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| RT07_HUMAN | MRPS7 | physical | 22939629 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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