| UniProt ID | RT23_HUMAN | |
|---|---|---|
| UniProt AC | Q9Y3D9 | |
| Protein Name | 28S ribosomal protein S23, mitochondrial | |
| Gene Name | MRPS23 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 190 | |
| Subcellular Localization | Mitochondrion . | |
| Protein Description | ||
| Protein Sequence | MAGSRLETVGSIFSRTRDLVRAGVLKEKPLWFDVYDAFPPLREPVFQRPRVRYGKAKAPIQDIWYHEDRIRAKFYSVYGSGQRAFDLFNPNFKSTCQRFVEKYTELQKLGETDEEKLFVETGKALLAEGVILRRVGEARTQHGGSHVSRKSEHLSVRPQTALEENETQKEVPQDQHLEAPADQSKGLLPP | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MAGSRLETV ------CCCCCCCCH | 25.35 | 25944712 | |
| 8 | Phosphorylation | MAGSRLETVGSIFSR CCCCCCCCHHHHHHH | 34.46 | 23403867 | |
| 11 | Phosphorylation | SRLETVGSIFSRTRD CCCCCHHHHHHHHHH | 19.00 | 24043423 | |
| 14 | Phosphorylation | ETVGSIFSRTRDLVR CCHHHHHHHHHHHHH | 30.95 | 23403867 | |
| 16 | Phosphorylation | VGSIFSRTRDLVRAG HHHHHHHHHHHHHCC | 27.60 | 24043423 | |
| 21 | Methylation | SRTRDLVRAGVLKEK HHHHHHHHCCCCCCC | 32.68 | 16187653 | |
| 55 | Ubiquitination | RPRVRYGKAKAPIQD CCCCHHCCCCCCHHH | 37.47 | 22817900 | |
| 57 | Ubiquitination | RVRYGKAKAPIQDIW CCHHCCCCCCHHHCE | 59.17 | 21890473 | |
| 57 | Malonylation | RVRYGKAKAPIQDIW CCHHCCCCCCHHHCE | 59.17 | 33225896 | |
| 65 | Phosphorylation | APIQDIWYHEDRIRA CCHHHCEECHHHHHH | 8.82 | - | |
| 73 | Ubiquitination | HEDRIRAKFYSVYGS CHHHHHHEEEEECCC | 34.68 | - | |
| 73 | Acetylation | HEDRIRAKFYSVYGS CHHHHHHEEEEECCC | 34.68 | 23954790 | |
| 73 | Malonylation | HEDRIRAKFYSVYGS CHHHHHHEEEEECCC | 34.68 | 26320211 | |
| 78 | Phosphorylation | RAKFYSVYGSGQRAF HHEEEEECCCCCHHH | 10.30 | 28152594 | |
| 80 | Phosphorylation | KFYSVYGSGQRAFDL EEEEECCCCCHHHHC | 17.67 | 28152594 | |
| 93 | Succinylation | DLFNPNFKSTCQRFV HCCCCCHHHHHHHHH | 52.04 | 23954790 | |
| 93 | Ubiquitination | DLFNPNFKSTCQRFV HCCCCCHHHHHHHHH | 52.04 | - | |
| 93 | Acetylation | DLFNPNFKSTCQRFV HCCCCCHHHHHHHHH | 52.04 | 25953088 | |
| 102 | Acetylation | TCQRFVEKYTELQKL HHHHHHHHHHHHHHC | 52.77 | 19608861 | |
| 102 | 2-Hydroxyisobutyrylation | TCQRFVEKYTELQKL HHHHHHHHHHHHHHC | 52.77 | - | |
| 108 | Acetylation | EKYTELQKLGETDEE HHHHHHHHCCCCCHH | 71.70 | 23236377 | |
| 108 | Ubiquitination | EKYTELQKLGETDEE HHHHHHHHCCCCCHH | 71.70 | 22817900 | |
| 112 | Phosphorylation | ELQKLGETDEEKLFV HHHHCCCCCHHHHHH | 47.08 | 29396449 | |
| 116 | Acetylation | LGETDEEKLFVETGK CCCCCHHHHHHHHHH | 45.22 | 25953088 | |
| 145 | Phosphorylation | ARTQHGGSHVSRKSE HHHCCCCCCCCCCCC | 25.88 | 20860994 |
| 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 RT23_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RT23_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 RT23_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| RT27_HUMAN | MRPS27 | physical | 22939629 | |
| SYQ_HUMAN | QARS | physical | 22939629 | |
| USBP1_HUMAN | USHBP1 | physical | 25416956 |
| 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. | ||||||
loading...
| 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-102, AND MASS SPECTROMETRY. | |