Basic Information
Gene Structure
upstream:
Get Sequence
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:0005575 | cellular_component | CC |
| GO:0005622 | intracellular anatomical structure | CC |
| GO:0005623 | obsolete cell | CC |
| GO:0005737 | cytoplasm | CC |
| GO:0005773 | vacuole | CC |
| GO:0005774 | vacuolar membrane | CC |
| GO:0005783 | endoplasmic reticulum | CC |
| GO:0005789 | endoplasmic reticulum membrane | CC |
| GO:0005794 | Golgi apparatus | CC |
| GO:0005886 | plasma membrane | CC |
| GO:0006605 | protein targeting | BP |
| GO:0006612 | protein targeting to membrane | BP |
| GO:0006613 | cotranslational protein targeting to membrane | BP |
| GO:0006810 | transport | BP |
| GO:0006886 | intracellular protein transport | BP |
| GO:0008104 | protein localization | BP |
| GO:0008150 | biological_process | BP |
| GO:0009507 | chloroplast | CC |
| GO:0009534 | chloroplast thylakoid | CC |
| GO:0009535 | chloroplast thylakoid membrane | CC |
| GO:0009536 | plastid | CC |
| GO:0009579 | thylakoid | CC |
| GO:0012505 | endomembrane system | CC |
| GO:0015031 | protein transport | BP |
| GO:0015833 | peptide transport | BP |
| GO:0016020 | membrane | CC |
| GO:0031090 | organelle membrane | CC |
| GO:0031976 | plastid thylakoid | CC |
| GO:0031984 | organelle subcompartment | CC |
| GO:0033036 | macromolecule localization | BP |
| GO:0034357 | photosynthetic membrane | CC |
| GO:0034613 | protein localization | BP |
| GO:0042175 | nuclear outer membrane-endoplasmic reticulum membrane network | CC |
| GO:0042651 | thylakoid membrane | CC |
| GO:0042886 | amide transport | BP |
| GO:0043226 | organelle | CC |
| GO:0043227 | membrane-bounded organelle | CC |
| GO:0043229 | intracellular organelle | CC |
| GO:0043231 | intracellular membrane-bounded organelle | CC |
| GO:0044422 | obsolete organelle part | CC |
| GO:0044424 | obsolete intracellular part | CC |
| GO:0044425 | obsolete membrane part | CC |
| GO:0044432 | obsolete endoplasmic reticulum part | CC |
| GO:0044434 | obsolete chloroplast part | CC |
| GO:0044435 | obsolete plastid part | CC |
| GO:0044436 | obsolete thylakoid part | CC |
| GO:0044437 | obsolete vacuolar part | CC |
| GO:0044444 | obsolete cytoplasmic part | CC |
| GO:0044446 | obsolete intracellular organelle part | CC |
| GO:0044464 | obsolete cell part | CC |
| GO:0045184 | establishment of protein localization | BP |
| GO:0046907 | intracellular transport | BP |
| GO:0051179 | localization | BP |
| GO:0051234 | establishment of localization | BP |
| GO:0051641 | cellular localization | BP |
| GO:0051649 | establishment of localization in cell | BP |
| GO:0055035 | plastid thylakoid membrane | CC |
| GO:0070727 | cellular macromolecule localization | BP |
| GO:0071702 | organic substance transport | BP |
| GO:0071705 | nitrogen compound transport | BP |
| GO:0071944 | cell periphery | CC |
| GO:0072657 | protein localization to membrane | BP |
| GO:0090150 | establishment of protein localization to membrane | BP |
| GO:0098588 | bounding membrane of organelle | CC |
| GO:0098805 | membrane | CC |
| GO:0098827 | endoplasmic reticulum subcompartment | CC |
| 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. |

