UniProt ID | PSME1_HUMAN | |
---|---|---|
UniProt AC | Q06323 | |
Protein Name | Proteasome activator complex subunit 1 | |
Gene Name | PSME1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 249 | |
Subcellular Localization | ||
Protein Description | Implicated in immunoproteasome assembly and required for efficient antigen processing. The PA28 activator complex enhances the generation of class I binding peptides by altering the cleavage pattern of the proteasome.. | |
Protein Sequence | MAMLRVQPEAQAKVDVFREDLCTKTENLLGSYFPKKISELDAFLKEPALNEANLSNLKAPLDIPVPDPVKEKEKEERKKQQEKEDKDEKKKGEDEDKGPPCGPVNCNEKIVVLLQRLKPEIKDVIEQLNLVTTWLQLQIPRIEDGNNFGVAVQEKVFELMTSLHTKLEGFHTQISKYFSERGDAVTKAAKQPHVGDYRQLVHELDEAEYRDIRLMVMEIRNAYAVLYDIILKNFEKLKKPRGETKGMIY | |
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 |
---|---|---|---|---|---|
13 | Acetylation | VQPEAQAKVDVFRED CCHHHHHHHHHHHHH | 27.21 | - | |
13 | Ubiquitination | VQPEAQAKVDVFRED CCHHHHHHHHHHHHH | 27.21 | - | |
13 | Acetylation | VQPEAQAKVDVFRED CCHHHHHHHHHHHHH | 27.21 | 23749302 | |
13 | Ubiquitination | VQPEAQAKVDVFRED CCHHHHHHHHHHHHH | 27.21 | - | |
23 | Phosphorylation | VFREDLCTKTENLLG HHHHHHHHHHHHHHH | 48.58 | 29255136 | |
24 | Ubiquitination | FREDLCTKTENLLGS HHHHHHHHHHHHHHH | 53.50 | - | |
24 | Ubiquitination | FREDLCTKTENLLGS HHHHHHHHHHHHHHH | 53.50 | - | |
24 | Acetylation | FREDLCTKTENLLGS HHHHHHHHHHHHHHH | 53.50 | 26051181 | |
25 | Phosphorylation | REDLCTKTENLLGSY HHHHHHHHHHHHHHH | 16.38 | 29255136 | |
31 | Phosphorylation | KTENLLGSYFPKKIS HHHHHHHHHCCCCHH | 24.46 | 29255136 | |
32 | Phosphorylation | TENLLGSYFPKKISE HHHHHHHHCCCCHHH | 23.31 | 25849741 | |
35 | Ubiquitination | LLGSYFPKKISELDA HHHHHCCCCHHHHHH | 53.49 | 21890473 | |
35 | Acetylation | LLGSYFPKKISELDA HHHHHCCCCHHHHHH | 53.49 | 23954790 | |
35 | Ubiquitination | LLGSYFPKKISELDA HHHHHCCCCHHHHHH | 53.49 | 21890473 | |
35 | Succinylation | LLGSYFPKKISELDA HHHHHCCCCHHHHHH | 53.49 | 23954790 | |
35 | Ubiquitination | LLGSYFPKKISELDA HHHHHCCCCHHHHHH | 53.49 | 21890473 | |
35 | Ubiquitination | LLGSYFPKKISELDA HHHHHCCCCHHHHHH | 53.49 | - | |
35 | Acetylation | LLGSYFPKKISELDA HHHHHCCCCHHHHHH | 53.49 | - | |
36 | Ubiquitination | LGSYFPKKISELDAF HHHHCCCCHHHHHHH | 52.26 | - | |
36 | Ubiquitination | LGSYFPKKISELDAF HHHHCCCCHHHHHHH | 52.26 | - | |
38 | Phosphorylation | SYFPKKISELDAFLK HHCCCCHHHHHHHHC | 40.77 | 28258704 | |
45 | Ubiquitination | SELDAFLKEPALNEA HHHHHHHCCHHCCCC | 56.02 | - | |
55 | Phosphorylation | ALNEANLSNLKAPLD HCCCCCHHCCCCCCC | 39.67 | 25159151 | |
58 | Sumoylation | EANLSNLKAPLDIPV CCCHHCCCCCCCCCC | 52.81 | - | |
58 | Ubiquitination | EANLSNLKAPLDIPV CCCHHCCCCCCCCCC | 52.81 | - | |
70 | Acetylation | IPVPDPVKEKEKEER CCCCCCCCHHHHHHH | 69.34 | 25953088 | |
90 | Acetylation | KEDKDEKKKGEDEDK HHHHHHHHCCCCCCC | 65.05 | 8270215 | |
91 | Acetylation | EDKDEKKKGEDEDKG HHHHHHHCCCCCCCC | 77.82 | 25953088 | |
97 | Acetylation | KKGEDEDKGPPCGPV HCCCCCCCCCCCCCC | 71.86 | 26051181 | |
109 | Ubiquitination | GPVNCNEKIVVLLQR CCCCCCHHHHHHHHH | 27.15 | - | |
155 | Ubiquitination | FGVAVQEKVFELMTS CCHHHHHHHHHHHHH | 34.82 | - | |
172 | Phosphorylation | TKLEGFHTQISKYFS HHHHHHHHHHHHHHH | 25.90 | 28348404 | |
175 | Phosphorylation | EGFHTQISKYFSERG HHHHHHHHHHHHHHC | 16.10 | 28348404 | |
176 | Ubiquitination | GFHTQISKYFSERGD HHHHHHHHHHHHHCH | 52.52 | 21890473 | |
176 | Ubiquitination | GFHTQISKYFSERGD HHHHHHHHHHHHHCH | 52.52 | 21890473 | |
176 | Ubiquitination | GFHTQISKYFSERGD HHHHHHHHHHHHHCH | 52.52 | 21890473 | |
176 | Acetylation | GFHTQISKYFSERGD HHHHHHHHHHHHHCH | 52.52 | 27452117 | |
177 | Phosphorylation | FHTQISKYFSERGDA HHHHHHHHHHHHCHH | 12.92 | 28270605 | |
179 | Phosphorylation | TQISKYFSERGDAVT HHHHHHHHHHCHHHH | 24.24 | 28270605 | |
186 | Phosphorylation | SERGDAVTKAAKQPH HHHCHHHHHHHHCCC | 19.38 | 23532336 | |
187 | Acetylation | ERGDAVTKAAKQPHV HHCHHHHHHHHCCCC | 39.48 | 25953088 | |
187 | Ubiquitination | ERGDAVTKAAKQPHV HHCHHHHHHHHCCCC | 39.48 | - | |
190 | Ubiquitination | DAVTKAAKQPHVGDY HHHHHHHHCCCCCCH | 70.04 | - | |
190 | Acetylation | DAVTKAAKQPHVGDY HHHHHHHHCCCCCCH | 70.04 | 25953088 | |
209 | Phosphorylation | HELDEAEYRDIRLMV HHCCHHHHHHHHHHH | 22.19 | - | |
213 | Methylation | EAEYRDIRLMVMEIR HHHHHHHHHHHHHHH | 22.48 | 115372757 | |
213 | Dimethylation | EAEYRDIRLMVMEIR HHHHHHHHHHHHHHH | 22.48 | - | |
215 | Sulfoxidation | EYRDIRLMVMEIRNA HHHHHHHHHHHHHHH | 1.61 | 21406390 | |
220 | Dimethylation | RLMVMEIRNAYAVLY HHHHHHHHHHHHHHH | 14.39 | - | |
220 | Methylation | RLMVMEIRNAYAVLY HHHHHHHHHHHHHHH | 14.39 | 115372763 | |
227 | Phosphorylation | RNAYAVLYDIILKNF HHHHHHHHHHHHHCH | 9.86 | 20068231 | |
232 | Acetylation | VLYDIILKNFEKLKK HHHHHHHHCHHHHCC | 49.54 | 156757 | |
238 | Phosphorylation | LKNFEKLKKPRGETK HHCHHHHCCCCCCCC | 72.33 | - | |
238 (in isoform 2) | Phosphorylation | - | 72.33 | - | |
245 | Ubiquitination | KKPRGETKGMIY--- CCCCCCCCCCCC--- | 42.03 | - | |
249 | Phosphorylation | GETKGMIY------- CCCCCCCC------- | 12.01 | - |
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 PSME1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PSME1_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 PSME1_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. |
loading...