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 | ||
* 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. |