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 |
|---|
Expression Profile
| DataSet | Number of Samples expressed(TPM>1) | Mean | Min | Max | Standard deviation(SD) | Coeffcient variation(CV) |
|---|
Pathway
| GO Term | Description | GO Category |
|---|---|---|
| GO:0000209 | protein polyubiquitination | BP |
| GO:0003674 | molecular_function | MF |
| GO:0003824 | catalytic activity | MF |
| GO:0004842 | ubiquitin-protein transferase activity | MF |
| GO:0005488 | binding | MF |
| GO:0005515 | protein binding | MF |
| GO:0005575 | cellular_component | CC |
| GO:0005622 | intracellular anatomical structure | CC |
| GO:0005623 | obsolete cell | CC |
| GO:0005737 | cytoplasm | CC |
| GO:0006464 | protein modification process | BP |
| GO:0006807 | nitrogen compound metabolic process | BP |
| GO:0008150 | biological_process | BP |
| GO:0008152 | metabolic process | BP |
| GO:0009987 | cellular process | BP |
| GO:0016567 | protein ubiquitination | BP |
| GO:0016740 | transferase activity | MF |
| GO:0019538 | protein metabolic process | BP |
| GO:0019787 | ubiquitin-like protein transferase activity | MF |
| GO:0019899 | enzyme binding | MF |
| GO:0031625 | ubiquitin protein ligase binding | MF |
| GO:0032446 | protein modification by small protein conjugation | BP |
| GO:0036211 | protein modification process | BP |
| GO:0043170 | macromolecule metabolic process | BP |
| GO:0043412 | macromolecule modification | BP |
| GO:0044237 | cellular metabolic process | BP |
| GO:0044238 | primary metabolic process | BP |
| GO:0044260 | cellular macromolecule metabolic process | BP |
| GO:0044267 | protein metabolic process | BP |
| GO:0044389 | ubiquitin-like protein ligase binding | MF |
| GO:0044424 | obsolete intracellular part | CC |
| GO:0044464 | obsolete cell part | CC |
| GO:0061630 | ubiquitin protein ligase activity | MF |
| GO:0061659 | ubiquitin-like protein ligase activity | MF |
| GO:0070647 | protein modification by small protein conjugation or removal | BP |
| GO:0071704 | organic substance metabolic process | BP |
| GO:0140096 | catalytic activity, acting on a protein | MF |
| GO:1901564 | organonitrogen compound metabolic process | 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. |