| UniProt ID | RL38_HUMAN | |
|---|---|---|
| UniProt AC | P63173 | |
| Protein Name | 60S ribosomal protein L38 | |
| Gene Name | RPL38 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 70 | |
| Subcellular Localization | ||
| Protein Description | ||
| Protein Sequence | MPRKIEEIKDFLLTARRKDAKSVKIKKNKDNVKFKVRCSRYLYTLVITDKEKAEKLKQSLPPGLAVKELK | |
| 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 | Ubiquitination | ----MPRKIEEIKDF ----CCCCHHHHHHH | 48.91 | 21906983 | |
| 4 | Sumoylation | ----MPRKIEEIKDF ----CCCCHHHHHHH | 48.91 | 28112733 | |
| 4 | 2-Hydroxyisobutyrylation | ----MPRKIEEIKDF ----CCCCHHHHHHH | 48.91 | - | |
| 9 | Acetylation | PRKIEEIKDFLLTAR CCCHHHHHHHHHHHH | 45.79 | 19608861 | |
| 9 | Ubiquitination | PRKIEEIKDFLLTAR CCCHHHHHHHHHHHH | 45.79 | 21890473 | |
| 9 | 2-Hydroxyisobutyrylation | PRKIEEIKDFLLTAR CCCHHHHHHHHHHHH | 45.79 | - | |
| 9 | Sumoylation | PRKIEEIKDFLLTAR CCCHHHHHHHHHHHH | 45.79 | 28112733 | |
| 9 | Sumoylation | PRKIEEIKDFLLTAR CCCHHHHHHHHHHHH | 45.79 | - | |
| 9 | Ubiquitination | PRKIEEIKDFLLTAR CCCHHHHHHHHHHHH | 45.79 | 21906983 | |
| 14 | Phosphorylation | EIKDFLLTARRKDAK HHHHHHHHHHCCCCC | 21.92 | - | |
| 16 | Methylation | KDFLLTARRKDAKSV HHHHHHHHCCCCCCC | 40.73 | 115492169 | |
| 33 | Ubiquitination | KKNKDNVKFKVRCSR ECCCCCCEEEEEEEE | 45.80 | 21906983 | |
| 39 | Phosphorylation | VKFKVRCSRYLYTLV CEEEEEEEEEEEEEE | 17.25 | 27422710 | |
| 41 | Phosphorylation | FKVRCSRYLYTLVIT EEEEEEEEEEEEEEC | 6.43 | 28152594 | |
| 43 | Phosphorylation | VRCSRYLYTLVITDK EEEEEEEEEEEECCH | 6.79 | 28152594 | |
| 44 | Phosphorylation | RCSRYLYTLVITDKE EEEEEEEEEEECCHH | 16.38 | 28152594 | |
| 48 | Phosphorylation | YLYTLVITDKEKAEK EEEEEEECCHHHHHH | 33.27 | 29978859 | |
| 50 | 2-Hydroxyisobutyrylation | YTLVITDKEKAEKLK EEEEECCHHHHHHHH | 53.09 | - | |
| 50 | Ubiquitination | YTLVITDKEKAEKLK EEEEECCHHHHHHHH | 53.09 | 21890473 | |
| 50 | Acetylation | YTLVITDKEKAEKLK EEEEECCHHHHHHHH | 53.09 | 25953088 | |
| 50 | Ubiquitination | YTLVITDKEKAEKLK EEEEECCHHHHHHHH | 53.09 | 21906983 | |
| 52 | Acetylation | LVITDKEKAEKLKQS EEECCHHHHHHHHHH | 68.53 | 23749302 | |
| 52 | Ubiquitination | LVITDKEKAEKLKQS EEECCHHHHHHHHHH | 68.53 | - | |
| 55 | Ubiquitination | TDKEKAEKLKQSLPP CCHHHHHHHHHHCCC | 66.88 | 21890473 | |
| 55 | Ubiquitination | TDKEKAEKLKQSLPP CCHHHHHHHHHHCCC | 66.88 | 21906983 | |
| 57 | Ubiquitination | KEKAEKLKQSLPPGL HHHHHHHHHHCCCCC | 49.24 | 21906983 | |
| 57 | Ubiquitination | KEKAEKLKQSLPPGL HHHHHHHHHHCCCCC | 49.24 | 21890473 | |
| 59 | Phosphorylation | KAEKLKQSLPPGLAV HHHHHHHHCCCCCCC | 41.05 | 21712546 | |
| 67 | Sumoylation | LPPGLAVKELK---- CCCCCCCCCCC---- | 52.28 | 19608861 | |
| 67 | Ubiquitination | LPPGLAVKELK---- CCCCCCCCCCC---- | 52.28 | 21906983 | |
| 67 | Acetylation | LPPGLAVKELK---- CCCCCCCCCCC---- | 52.28 | 19608861 | |
| 67 | Ubiquitination | LPPGLAVKELK---- CCCCCCCCCCC---- | 52.28 | 21890473 |
| 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 RL38_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RL38_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 RL38_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-9 AND LYS-67, AND MASSSPECTROMETRY. | |