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:0003674 | molecular_function | MF |
| GO:0005215 | transporter activity | MF |
| GO:0005575 | cellular_component | CC |
| GO:0005622 | intracellular anatomical structure | CC |
| GO:0005623 | obsolete cell | CC |
| GO:0005737 | cytoplasm | CC |
| GO:0005783 | endoplasmic reticulum | CC |
| GO:0006605 | protein targeting | BP |
| GO:0006612 | protein targeting to membrane | BP |
| GO:0006620 | post-translational protein targeting to endoplasmic reticulum membrane | BP |
| GO:0006810 | transport | BP |
| GO:0006886 | intracellular protein transport | BP |
| GO:0008104 | protein localization | BP |
| GO:0008150 | biological_process | BP |
| GO:0008320 | protein transmembrane transporter activity | MF |
| GO:0008565 | obsolete protein transporter activity | MF |
| GO:0012505 | endomembrane system | CC |
| GO:0015031 | protein transport | BP |
| GO:0015399 | primary active transmembrane transporter activity | MF |
| GO:0015405 | ATPase-coupled transmembrane transporter activity | MF |
| GO:0015450 | protein-transporting ATPase activity | MF |
| GO:0015833 | peptide transport | BP |
| GO:0022804 | active transmembrane transporter activity | MF |
| GO:0022857 | transmembrane transporter activity | MF |
| GO:0022884 | macromolecule transmembrane transporter activity | MF |
| GO:0031204 | post-translational protein targeting to membrane, translocation | BP |
| GO:0033036 | macromolecule localization | BP |
| GO:0033365 | protein localization to organelle | BP |
| GO:0034613 | protein localization | BP |
| GO:0042886 | amide transport | BP |
| GO:0042887 | amide transmembrane transporter activity | MF |
| GO:0043226 | organelle | CC |
| GO:0043227 | membrane-bounded organelle | CC |
| GO:0043229 | intracellular organelle | CC |
| GO:0043231 | intracellular membrane-bounded organelle | CC |
| GO:0044424 | obsolete intracellular part | CC |
| GO:0044444 | obsolete cytoplasmic part | CC |
| GO:0044464 | obsolete cell part | CC |
| GO:0045047 | protein targeting to ER | BP |
| 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:0055085 | transmembrane transport | BP |
| GO:0065002 | intracellular protein transmembrane transport | BP |
| GO:0070727 | cellular macromolecule localization | BP |
| GO:0070972 | protein localization to endoplasmic reticulum | BP |
| GO:0071702 | organic substance transport | BP |
| GO:0071705 | nitrogen compound transport | BP |
| GO:0071806 | protein transmembrane transport | BP |
| GO:0072594 | establishment of protein localization to organelle | BP |
| GO:0072599 | establishment of protein localization to endoplasmic reticulum | BP |
| GO:0072657 | protein localization to membrane | BP |
| GO:0090150 | establishment of protein localization to membrane | BP |
| GO:1904680 | peptide transmembrane transporter activity | MF |
| KEGG Term | Name | Description |
|---|---|---|
| map04145 | Phagosome | Phagocytosis is the process of taking in relatively large particles by a cell, and is a central mechanism in the tissue remodeling, inflammation, and defense against infectious agents. A phagosome is formed when the specific receptors on the phagocyte surface recognize ligands on the particle surface. After formation, nascent phagosomes progressively acquire digestive characteristics. This maturation of phagosomes involves regulated interaction with the other membrane organelles, including recycling endosomes, late endosomes and lysosomes. The fusion of phagosomes and lysosomes releases toxic products that kill most bacteria and degrade them into fragments. However, some bacteria have strategies to escape the bactericidal mechanisms associated with phagocytosis and survive within host phagocytes. |
| 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. |
| map03060 | Protein export | The protein export is the active transport of proteins from the cytoplasm to the exterior of the cell, or to the periplasmic compartment in Gram-negative bacteria. The sec dependent pathway is the general protein export system that transports newly synthesized proteins into or across the cell membrane. The translocation channel is formed from a conserved trimeric membrane protein complex, called the Sec61/SecY complex. The twin-arginine translocation (Tat) pathway is another protein transport system that transports folded proteins in bacteria, archaea, and chloroplasts. Many Tat systems comprise three functionally different membrane proteins, TatA, TatB, and TatC, but TatA and TatE seem to have overlapping functions, with TatA having by far the more important role. |