| UniProt ID | RT16_HUMAN | |
|---|---|---|
| UniProt AC | Q9Y3D3 | |
| Protein Name | 28S ribosomal protein S16, mitochondrial | |
| Gene Name | MRPS16 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 137 | |
| Subcellular Localization | Mitochondrion . | |
| Protein Description | ||
| Protein Sequence | MVHLTTLLCKAYRGGHLTIRLALGGCTNRPFYRIVAAHNKCPRDGRFVEQLGSYDPLPNSHGEKLVALNLDRIRHWIGCGAHLSKPMEKLLGLAGFFPLHPMMITNAERLRRKRAREVLLASQKTDAEATDTEATET | |
| 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 |
|---|---|---|---|---|---|
| 13 | Methylation | TLLCKAYRGGHLTIR HHHHHHHCCCCEEEE | 49.86 | 115483803 | |
| 40 | Ubiquitination | RIVAAHNKCPRDGRF HHHHCCCCCCCCCCH | 35.43 | 24816145 | |
| 64 | Ubiquitination | LPNSHGEKLVALNLD CCCCCCCCEEEECHH | 53.50 | 22817900 | |
| 64 | Ubiquitination | LPNSHGEKLVALNLD CCCCCCCCEEEECHH | 53.50 | 21890473 | |
| 64 | Acetylation | LPNSHGEKLVALNLD CCCCCCCCEEEECHH | 53.50 | 26051181 | |
| 72 | Methylation | LVALNLDRIRHWIGC EEEECHHHHHHHHCC | 30.89 | 115483811 | |
| 85 | Malonylation | GCGAHLSKPMEKLLG CCCHHHCHHHHHHHH | 55.53 | 26320211 | |
| 85 | Acetylation | GCGAHLSKPMEKLLG CCCHHHCHHHHHHHH | 55.53 | 26051181 | |
| 122 | Phosphorylation | AREVLLASQKTDAEA HHHHHHHHCCCCCCC | 31.98 | 22210691 | |
| 125 | Phosphorylation | VLLASQKTDAEATDT HHHHHCCCCCCCCCC | 32.57 | 28176443 | |
| 130 | Phosphorylation | QKTDAEATDTEATET CCCCCCCCCCCCCCC | 34.65 | 30278072 | |
| 132 | Phosphorylation | TDAEATDTEATET-- CCCCCCCCCCCCC-- | 24.14 | 30278072 | |
| 135 | Phosphorylation | EATDTEATET----- CCCCCCCCCC----- | 33.65 | 28176443 | |
| 137 | Phosphorylation | TDTEATET------- CCCCCCCC------- | 39.29 | 24732914 |
| 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 RT16_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RT16_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 RT16_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| RT26_HUMAN | MRPS26 | physical | 22939629 | |
| RT25_HUMAN | MRPS25 | physical | 22939629 | |
| SSBP_HUMAN | SSBP1 | physical | 22939629 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 610498 | Combined oxidative phosphorylation deficiency 2 (COXPD2) | |||||
| 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 |
| "Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-130, AND MASSSPECTROMETRY. | |
| "A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-130, AND MASSSPECTROMETRY. | |
| "Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-130, AND MASSSPECTROMETRY. | |