UniProt ID | RS21_HUMAN | |
---|---|---|
UniProt AC | P63220 | |
Protein Name | 40S ribosomal protein S21 | |
Gene Name | RPS21 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 83 | |
Subcellular Localization | Cytoplasm, cytosol . Cytoplasm . Rough endoplasmic reticulum . Detected on cytosolic polysomes (PubMed:25957688). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). | |
Protein Description | ||
Protein Sequence | MQNDAGEFVDLYVPRKCSASNRIIGAKDHASIQMNVAEVDKVTGRFNGQFKTYAICGAIRRMGESDDSILRLAKADGIVSKNF | |
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 |
---|---|---|---|---|---|
1 | Sulfoxidation | -------MQNDAGEF -------CCCCCCCE | 8.29 | 28183972 | |
1 | Acetylation | -------MQNDAGEF -------CCCCCCCE | 8.29 | 19413330 | |
12 | Phosphorylation | AGEFVDLYVPRKCSA CCCEEEEEECCCCCC | 12.16 | 26657352 | |
12 | Nitration | AGEFVDLYVPRKCSA CCCEEEEEECCCCCC | 12.16 | - | |
27 | Acetylation | SNRIIGAKDHASIQM CCCCCCCCCCEEEEE | 44.85 | 23954790 | |
27 | Ubiquitination | SNRIIGAKDHASIQM CCCCCCCCCCEEEEE | 44.85 | 21890473 | |
34 | Sulfoxidation | KDHASIQMNVAEVDK CCCEEEEEEEEEHHE | 4.09 | 30846556 | |
41 | Sumoylation | MNVAEVDKVTGRFNG EEEEEHHEEEEEECC | 47.04 | 25114211 | |
41 | Malonylation | MNVAEVDKVTGRFNG EEEEEHHEEEEEECC | 47.04 | 26320211 | |
41 | Ubiquitination | MNVAEVDKVTGRFNG EEEEEHHEEEEEECC | 47.04 | - | |
41 | Acetylation | MNVAEVDKVTGRFNG EEEEEHHEEEEEECC | 47.04 | 23954790 | |
51 | Ubiquitination | GRFNGQFKTYAICGA EEECCCEEHHHHHHH | 32.51 | 21890473 | |
51 | Acetylation | GRFNGQFKTYAICGA EEECCCEEHHHHHHH | 32.51 | 25953088 | |
51 | Methylation | GRFNGQFKTYAICGA EEECCCEEHHHHHHH | 32.51 | 30592059 | |
52 | Phosphorylation | RFNGQFKTYAICGAI EECCCEEHHHHHHHH | 21.34 | 23403867 | |
53 | Phosphorylation | FNGQFKTYAICGAIR ECCCEEHHHHHHHHH | 8.44 | 25394399 | |
56 | Glutathionylation | QFKTYAICGAIRRMG CEEHHHHHHHHHHHC | 1.99 | 22555962 | |
56 | S-palmitoylation | QFKTYAICGAIRRMG CEEHHHHHHHHHHHC | 1.99 | 29575903 | |
62 | Sulfoxidation | ICGAIRRMGESDDSI HHHHHHHHCCCCHHH | 5.12 | 21406390 | |
65 | Phosphorylation | AIRRMGESDDSILRL HHHHHCCCCHHHHHH | 40.77 | 22617229 | |
68 | Phosphorylation | RMGESDDSILRLAKA HHCCCCHHHHHHHHH | 28.63 | 20068231 | |
71 | Methylation | ESDDSILRLAKADGI CCCHHHHHHHHHCCC | 30.81 | 115492605 | |
74 | 2-Hydroxyisobutyrylation | DSILRLAKADGIVSK HHHHHHHHHCCCCCC | 52.15 | - | |
74 | Ubiquitination | DSILRLAKADGIVSK HHHHHHHHHCCCCCC | 52.15 | 2190698 | |
74 | Acetylation | DSILRLAKADGIVSK HHHHHHHHHCCCCCC | 52.15 | 26051181 | |
80 | Phosphorylation | AKADGIVSKNF---- HHHCCCCCCCC---- | 21.69 | 27251275 | |
81 | Ubiquitination | KADGIVSKNF----- HHCCCCCCCC----- | 52.02 | 21890473 | |
81 | Acetylation | KADGIVSKNF----- HHCCCCCCCC----- | 52.02 | 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 RS21_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RS21_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 RS21_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 |
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY. | |
"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-81, AND MASS SPECTROMETRY. |