UniProt ID | RS26_HUMAN | |
---|---|---|
UniProt AC | P62854 | |
Protein Name | 40S ribosomal protein S26 | |
Gene Name | RPS26 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 115 | |
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 | MTKKRRNNGRAKKGRGHVQPIRCTNCARCVPKDKAIKKFVIRNIVEAAAVRDISEASVFDAYVLPKLYVKLHYCVSCAIHSKVVRNRSREARKDRTPPPRFRPAGAAPRPPPKPM | |
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 |
---|---|---|---|---|---|
15 | Methylation | NGRAKKGRGHVQPIR CCCCCCCCCCCCCCC | 40.71 | 115492613 | |
54 | Phosphorylation | AAAVRDISEASVFDA HHHCCCCHHHHCCCC | 31.25 | 20873877 | |
57 | Phosphorylation | VRDISEASVFDAYVL CCCCHHHHCCCCHHH | 21.18 | 21712546 | |
62 | Phosphorylation | EASVFDAYVLPKLYV HHHCCCCHHHHHHHH | 12.36 | 28152594 | |
66 | Acetylation | FDAYVLPKLYVKLHY CCCHHHHHHHHHHHH | 48.57 | 23236377 | |
66 | Ubiquitination | FDAYVLPKLYVKLHY CCCHHHHHHHHHHHH | 48.57 | 21890473 | |
66 | Malonylation | FDAYVLPKLYVKLHY CCCHHHHHHHHHHHH | 48.57 | 26320211 | |
66 | 2-Hydroxyisobutyrylation | FDAYVLPKLYVKLHY CCCHHHHHHHHHHHH | 48.57 | - | |
66 | Sumoylation | FDAYVLPKLYVKLHY CCCHHHHHHHHHHHH | 48.57 | - | |
70 | Ubiquitination | VLPKLYVKLHYCVSC HHHHHHHHHHHHHHH | 18.91 | - | |
73 | Phosphorylation | KLYVKLHYCVSCAIH HHHHHHHHHHHHHHH | 12.65 | 27080861 | |
74 | Glutathionylation | LYVKLHYCVSCAIHS HHHHHHHHHHHHHHH | 0.95 | 22555962 | |
76 | Phosphorylation | VKLHYCVSCAIHSKV HHHHHHHHHHHHHHH | 8.35 | 27080861 | |
81 | Phosphorylation | CVSCAIHSKVVRNRS HHHHHHHHHHHHCCC | 22.49 | 27080861 | |
82 | Ubiquitination | VSCAIHSKVVRNRSR HHHHHHHHHHHCCCH | 30.50 | - | |
82 | Acetylation | VSCAIHSKVVRNRSR HHHHHHHHHHHCCCH | 30.50 | 25953088 | |
96 | Phosphorylation | REARKDRTPPPRFRP HHHHCCCCCCCCCCC | 50.73 | 30266825 | |
113 | Acetylation | AAPRPPPKPM----- CCCCCCCCCC----- | 60.53 | 22649439 | |
113 | Methylation | AAPRPPPKPM----- CCCCCCCCCC----- | 60.53 | 22649439 | |
115 | Sulfoxidation | PRPPPKPM------- CCCCCCCC------- | 12.23 | 28183972 |
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 RS26_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RS26_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 RS26_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
613309 | Diamond-Blackfan anemia 10 (DBA10) | |||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
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-66 AND LYS-113, AND MASSSPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-96, AND MASSSPECTROMETRY. |