Q17361
Gene name |
usp-14 (tgt-1, C13B4.2) |
Protein name |
Ubiquitin carboxyl-terminal hydrolase 14 |
Names |
Deubiquitinating enzyme 14, Ubiquitin thioesterase 14, Ubiquitin-specific-processing protease 14 |
Species |
Caenorhabditis elegans |
KEGG Pathway |
cel:CELE_C13B4.2 |
EC number |
3.4.19.12: Omega peptidases |
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 Q17361
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q17361-F1 | Predicted | AlphaFoldDB |
No variants for Q17361
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q17361 | |||||
No associated diseases with Q17361
5 regional properties for Q17361
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Ubiquitin-like domain | 2 - 71 | IPR000626 |
| domain | Peptidase C19, ubiquitin carboxyl-terminal hydrolase | 102 - 455 | IPR001394 |
| conserved_site | Ubiquitin specific protease, conserved site | 103 - 118 | IPR018200-1 |
| conserved_site | Ubiquitin specific protease, conserved site | 392 - 410 | IPR018200-2 |
| domain | Ubiquitin specific protease domain | 102 - 458 | IPR028889 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.4.19.12 | Omega peptidases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| proteasome complex | A large multisubunit complex which catalyzes protein degradation, found in eukaryotes, archaea and some bacteria. In eukaryotes, this complex consists of the barrel shaped proteasome core complex and one or two associated proteins or complexes that act in regulating entry into or exit from the core. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| cysteine-type deubiquitinase activity | An thiol-dependent isopeptidase activity that cleaves ubiquitin from a target protein to which it is conjugated. |
| proteasome binding | Binding to a proteasome, a large multisubunit protein complex that catalyzes protein degradation. |
3 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. |
| protein deubiquitination | The removal of one or more ubiquitin groups from a protein. |
| regulation of proteasomal protein catabolic process | Any process that modulates the rate, frequency, or extent of the chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds that is mediated by the proteasome. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| O14562 | UBFD1 | Ubiquitin domain-containing protein UBFD1 | Homo sapiens (Human) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MPIVNVKWQK | EKYVVEVDTS | APPMVFKAQL | FALTQVVPER | QKVVIMGRTL | GDDDWEGITI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KENMTIMMMG | SVGEIPKPPT | VLEKKQANRD | KQAEEISALY | PCGLANLGNT | CYFNSCVQML |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KEVNELVLKP | AEEMRIREHN | DRLCHNLATL | FNSLRDKDRA | LRSKGEPIKP | FAAILTLSDS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FPQFEKFKQQ | DANECLVSIM | SNVTRIYGLS | GWNIESLFRI | QTETTMKCLE | SDEVSEKKVE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RNNQLTCYVN | QDVRFLQTGI | KAGFEEEMTR | NSEELNRDAK | WQKNTQISRL | PKYLTVNINR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| FFYKESTKTN | AKILKSVQFP | MQLDTYDLCS | QELKDKLVAR | RADIKLEEDA | KLERELRKKV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LDKEQGDKIF | DDGVALPTAF | EDDAGSNNSG | FYDLKGIITH | KGRSSQDGHY | VAWMRSSEDG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| KWRLFDDEHV | TVVDEEAILK | TSGGGDWHSA | YVLLYEARVI | KQFPELPPAP | VPTEVAADTA |
| EPMEVSEKQ |