| UniProt ID | RS15A_HUMAN | |
|---|---|---|
| UniProt AC | P62244 | |
| Protein Name | 40S ribosomal protein S15a | |
| Gene Name | RPS15A | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 130 | |
| Subcellular Localization | ||
| Protein Description | ||
| Protein Sequence | MVRMNVLADALKSINNAEKRGKRQVLIRPCSKVIVRFLTVMMKHGYIGEFEIIDDHRAGKIVVNLTGRLNKCGVISPRFDVQLKDLEKWQNNLLPSRQFGFIVLTTSAGIMDHEEARRKHTGGKILGFFF | |
| 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 |
|---|---|---|---|---|---|
| 4 | Sulfoxidation | ----MVRMNVLADAL ----CCCHHHHHHHH | 2.50 | 21406390 | |
| 12 | Acetylation | NVLADALKSINNAEK HHHHHHHHHCCHHHH | 51.51 | 26051181 | |
| 12 | Ubiquitination | NVLADALKSINNAEK HHHHHHHHHCCHHHH | 51.51 | 21890473 | |
| 19 | Acetylation | KSINNAEKRGKRQVL HHCCHHHHHCCCCEE | 65.13 | 23749302 | |
| 19 | Ubiquitination | KSINNAEKRGKRQVL HHCCHHHHHCCCCEE | 65.13 | 21890473 | |
| 19 | Succinylation | KSINNAEKRGKRQVL HHCCHHHHHCCCCEE | 65.13 | 23954790 | |
| 19 | 2-Hydroxyisobutyrylation | KSINNAEKRGKRQVL HHCCHHHHHCCCCEE | 65.13 | - | |
| 32 | Ubiquitination | VLIRPCSKVIVRFLT EEEECCHHHHHHHHH | 42.57 | 21890473 | |
| 32 | Acetylation | VLIRPCSKVIVRFLT EEEECCHHHHHHHHH | 42.57 | 25953088 | |
| 46 | Phosphorylation | TVMMKHGYIGEFEII HHHHHCCCEEEEEEE | 12.89 | 28152594 | |
| 60 | Ubiquitination | IDDHRAGKIVVNLTG ECCCCCCEEEEECCC | 31.20 | 21890473 | |
| 60 | 2-Hydroxyisobutyrylation | IDDHRAGKIVVNLTG ECCCCCCEEEEECCC | 31.20 | - | |
| 66 | Phosphorylation | GKIVVNLTGRLNKCG CEEEEECCCCCCCCC | 18.30 | - | |
| 71 | Acetylation | NLTGRLNKCGVISPR ECCCCCCCCCCCCCC | 36.64 | 25953088 | |
| 71 | Ubiquitination | NLTGRLNKCGVISPR ECCCCCCCCCCCCCC | 36.64 | 21890473 | |
| 71 | 2-Hydroxyisobutyrylation | NLTGRLNKCGVISPR ECCCCCCCCCCCCCC | 36.64 | - | |
| 72 | S-palmitoylation | LTGRLNKCGVISPRF CCCCCCCCCCCCCCC | 5.25 | 29575903 | |
| 84 | 2-Hydroxyisobutyrylation | PRFDVQLKDLEKWQN CCCCEEHHHHHHHHH | 43.08 | - | |
| 84 | Ubiquitination | PRFDVQLKDLEKWQN CCCCEEHHHHHHHHH | 43.08 | 21890473 | |
| 84 | Acetylation | PRFDVQLKDLEKWQN CCCCEEHHHHHHHHH | 43.08 | 26822725 | |
| 88 | 2-Hydroxyisobutyrylation | VQLKDLEKWQNNLLP EEHHHHHHHHHCCCC | 62.47 | - | |
| 88 | Acetylation | VQLKDLEKWQNNLLP EEHHHHHHHHHCCCC | 62.47 | 25825284 | |
| 88 | Succinylation | VQLKDLEKWQNNLLP EEHHHHHHHHHCCCC | 62.47 | 21890473 | |
| 88 | Succinylation | VQLKDLEKWQNNLLP EEHHHHHHHHHCCCC | 62.47 | - | |
| 88 | Ubiquitination | VQLKDLEKWQNNLLP EEHHHHHHHHHCCCC | 62.47 | 21890473 | |
| 96 | Phosphorylation | WQNNLLPSRQFGFIV HHHCCCCHHHCCEEE | 38.39 | 25278378 | |
| 121 | Phosphorylation | EEARRKHTGGKILGF HHHHHHHCCCCEEEE | 51.14 | - | |
| 124 | 2-Hydroxyisobutyrylation | RRKHTGGKILGFFF- HHHHCCCCEEEEEC- | 35.78 | - | |
| 124 | Ubiquitination | RRKHTGGKILGFFF- HHHHCCCCEEEEEC- | 35.78 | 21890473 | |
| 124 | Acetylation | RRKHTGGKILGFFF- HHHHCCCCEEEEEC- | 35.78 | 19608861 |
| 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 RS15A_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RS15A_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 RS15A_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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| 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-124, AND MASS SPECTROMETRY. | |