Q20585
Gene name |
rpn-7 (F49C12.8) |
Protein name |
26S proteasome non-ATPase regulatory subunit 6 |
Names |
26S proteasome regulatory subunit rpn-7 |
Species |
Caenorhabditis elegans |
KEGG Pathway |
cel:CELE_F49C12.8 |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q20585
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q20585-F1 | Predicted | AlphaFoldDB |
No variants for Q20585
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q20585 | |||||
No associated diseases with Q20585
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| proteasome regulatory particle | A multisubunit complex, which caps one or both ends of the proteasome core complex. This complex recognizes and unfolds ubiquitinated proteins, and translocates them to the proteasome core complex. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| enzyme regulator activity | Binds to and modulates the activity of an enzyme. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| proteasome-mediated ubiquitin-dependent protein catabolic process | The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9GS00 | csn-1 | COP9 signalosome complex subunit 1 | Caenorhabditis elegans | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTEAAKKSTK | KPVDDGNFDK | EIISRWPDLE | LSQTRFMLNH | PEVDSSVKEA | KLEKLQETIK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EFDMAPFYEL | VCADFKIVVD | ATQLAAMKAA | NQKKIDEITA | EVEDAEKNLG | ESEVRQGLLR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KFEYYCQIGD | KDNALKAYTA | TYEKTVGMGY | RIDVVFAMIR | VGLFFLDHHL | INKFITKAKE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LMEQGGDWER | KNRLRSYEAL | YRMSVRDFAG | AADLFLEAVP | TFGSYELMTY | ENLILYTVIT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TTFALDRPDL | RTKVIRCNEV | QEQLTGGGLN | GTLIPVREYL | ESYYDCHYDR | FFIQLAALES |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ERFKFDRYLS | PHFNYYSRGM | RHRAYEQFLT | PYKTVRIDMM | AKDFGVSRAF | IDRELHRLIA |
| 370 | 380 | 390 | 400 | ||
| TGQLQCRIDA | VNGVIEVNHR | DSKNHLYKAV | IKDGDILLNR | IQKLARVINA |