Basic Information
Gene Structure
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Domain
| Database | EntryID | E-Value | Start | end | InterPro ID | Description |
|---|
Regulation&Interaction
Annotation
Orthologous Group
| Orthologous ID | Species Number | All hits in PereRegDB | Hits of this species | Orthologous Detail |
|---|
Pathway
| GO Term | Description | GO Category |
|---|---|---|
| GO:0000302 | response to reactive oxygen species | BP |
| GO:0003674 | molecular_function | MF |
| GO:0003824 | catalytic activity | MF |
| GO:0006725 | cellular aromatic compound metabolic process | BP |
| GO:0006950 | response to stress | BP |
| GO:0006979 | response to oxidative stress | BP |
| GO:0008150 | biological_process | BP |
| GO:0008152 | metabolic process | BP |
| GO:0008219 | cell death | BP |
| GO:0009058 | biosynthetic process | BP |
| GO:0009636 | response to toxic substance | BP |
| GO:0009698 | phenylpropanoid metabolic process | BP |
| GO:0009699 | phenylpropanoid biosynthetic process | BP |
| GO:0009804 | coumarin metabolic process | BP |
| GO:0009805 | coumarin biosynthetic process | BP |
| GO:0009987 | cellular process | BP |
| GO:0010035 | response to inorganic substance | BP |
| GO:0010421 | hydrogen peroxide-mediated programmed cell death | BP |
| GO:0012501 | programmed cell death | BP |
| GO:0016491 | oxidoreductase activity | MF |
| GO:0018130 | heterocycle biosynthetic process | BP |
| GO:0019438 | aromatic compound biosynthetic process | BP |
| GO:0019748 | secondary metabolic process | BP |
| GO:0033554 | cellular response to stress | BP |
| GO:0034599 | cellular response to oxidative stress | BP |
| GO:0034614 | cellular response to reactive oxygen species | BP |
| GO:0035690 | cellular response to xenobiotic stimulus | BP |
| GO:0036473 | cell death in response to oxidative stress | BP |
| GO:0036474 | cell death in response to hydrogen peroxide | BP |
| GO:0042221 | response to chemical | BP |
| GO:0042493 | response to xenobiotic stimulus | BP |
| GO:0042542 | response to hydrogen peroxide | BP |
| GO:0044237 | cellular metabolic process | BP |
| GO:0044249 | cellular biosynthetic process | BP |
| GO:0044550 | secondary metabolite biosynthetic process | BP |
| GO:0046483 | heterocycle metabolic process | BP |
| GO:0046677 | response to antibiotic | BP |
| GO:0050896 | response to stimulus | BP |
| GO:0051213 | dioxygenase activity | MF |
| GO:0051716 | cellular response to stimulus | BP |
| GO:0055114 | obsolete oxidation-reduction process | BP |
| GO:0070301 | cellular response to hydrogen peroxide | BP |
| GO:0070887 | cellular response to chemical stimulus | BP |
| GO:0071236 | cellular response to antibiotic | BP |
| GO:0071704 | organic substance metabolic process | BP |
| GO:0097237 | cellular response to toxic substance | BP |
| GO:0097468 | programmed cell death in response to reactive oxygen species | BP |
| GO:1901360 | organic cyclic compound metabolic process | BP |
| GO:1901362 | organic cyclic compound biosynthetic process | BP |
| GO:1901576 | organic substance biosynthetic process | BP |
| GO:1901700 | response to oxygen-containing compound | BP |
| GO:1901701 | cellular response to oxygen-containing compound | BP |
| KEGG Term | Name | Description |
|---|---|---|
| map04141 | Protein processing in endoplasmic reticulum | The endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylated. Correctly folded proteins are packaged into transport vesicles that shuttle them to the Golgi complex. Misfolded proteins are retained within the ER lumen in complex with molecular chaperones. Proteins that are terminally misfolded bind to BiP and are directed toward degradation through the proteasome in a process called ER-associated degradation (ERAD). Accumulation of misfolded proteins in the ER causes ER stress and activates a signaling pathway called the unfolded protein response (UPR). In certain severe situations, however, the protective mechanisms activated by the UPR are not sufficient to restore normal ER function and cells die by apoptosis. |
| map04120 | Ubiquitin mediated proteolysis | Protein ubiquitination plays an important role in eukaryotic cellular processes. It mainly functions as a signal for 26S proteasome dependent protein degradation. The addition of ubiquitin to proteins being degraded is performed by a reaction cascade consisting of three enzymes, named E1 (ubiquitin activating enzyme), E2 (ubiquitin conjugating enzyme), and E3 (ubiquitin ligase). Each E3 has specificity to its substrate, or proteins to be targeted by ubiquitination. Many E3s are discovered in eukaryotes and they are classified into four types: HECT type, U-box type, single RING-finger type, and multi-subunit RING-finger type. Multi-subunit RING-finger E3s are exemplified by cullin-Rbx E3s and APC/C. They consist of a RING-finger-containing subunit (RBX1 or RBX2) that functions to bind E2s, a scaffold-like cullin molecule, adaptor proteins, and a target recognizing subunit that binds substrates. |
| map01110 | Biosynthesis of secondary metabolites | - |