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:0005575 | cellular_component | CC |
| GO:0005618 | cell wall | CC |
| GO:0005622 | intracellular anatomical structure | CC |
| GO:0005623 | obsolete cell | CC |
| GO:0005737 | cytoplasm | CC |
| GO:0005739 | mitochondrion | 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:0005911 | cell-cell junction | CC |
| GO:0006464 | protein modification process | BP |
| GO:0006486 | protein glycosylation | BP |
| GO:0006487 | protein N-linked glycosylation | BP |
| GO:0006807 | nitrogen compound metabolic process | BP |
| GO:0006950 | response to stress | BP |
| GO:0008150 | biological_process | BP |
| GO:0008152 | metabolic process | BP |
| GO:0008250 | oligosaccharyltransferase complex | CC |
| GO:0009058 | biosynthetic process | BP |
| GO:0009059 | macromolecule biosynthetic process | BP |
| GO:0009100 | glycoprotein metabolic process | BP |
| GO:0009101 | glycoprotein biosynthetic process | BP |
| GO:0009266 | response to temperature stimulus | BP |
| GO:0009409 | response to cold | BP |
| GO:0009505 | plant-type cell wall | CC |
| GO:0009506 | plasmodesma | CC |
| GO:0009628 | response to abiotic stimulus | BP |
| GO:0009987 | cellular process | BP |
| GO:0012505 | endomembrane system | CC |
| GO:0016020 | membrane | CC |
| GO:0018193 | peptidyl-amino acid modification | BP |
| GO:0018196 | obsolete peptidyl-asparagine modification | BP |
| GO:0018279 | protein N-linked glycosylation via asparagine | BP |
| GO:0019538 | protein metabolic process | BP |
| GO:0030054 | cell junction | CC |
| GO:0030312 | external encapsulating structure | CC |
| GO:0031090 | organelle membrane | CC |
| GO:0031984 | organelle subcompartment | CC |
| GO:0032991 | protein-containing complex | CC |
| GO:0034645 | cellular macromolecule biosynthetic process | BP |
| GO:0036211 | protein modification process | BP |
| GO:0042175 | nuclear outer membrane-endoplasmic reticulum membrane network | CC |
| GO:0043170 | macromolecule metabolic process | BP |
| GO:0043226 | organelle | CC |
| GO:0043227 | membrane-bounded organelle | CC |
| GO:0043229 | intracellular organelle | CC |
| GO:0043231 | intracellular membrane-bounded organelle | CC |
| GO:0043412 | macromolecule modification | BP |
| GO:0043413 | macromolecule glycosylation | BP |
| GO:0044237 | cellular metabolic process | BP |
| GO:0044238 | primary metabolic process | BP |
| GO:0044249 | cellular biosynthetic process | BP |
| GO:0044260 | cellular macromolecule metabolic process | BP |
| GO:0044267 | protein metabolic process | BP |
| 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: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:0050896 | response to stimulus | BP |
| GO:0055044 | symplast | CC |
| GO:0070085 | glycosylation | BP |
| GO:0071704 | organic substance metabolic process | BP |
| GO:0071944 | cell periphery | CC |
| GO:0098588 | bounding membrane of organelle | CC |
| GO:0098796 | membrane protein complex | CC |
| GO:0098805 | membrane | CC |
| GO:0098827 | endoplasmic reticulum subcompartment | CC |
| GO:1901135 | carbohydrate derivative metabolic process | BP |
| GO:1901137 | carbohydrate derivative biosynthetic process | BP |
| GO:1901564 | organonitrogen compound metabolic process | BP |
| GO:1901566 | organonitrogen compound biosynthetic process | BP |
| GO:1901576 | organic substance biosynthetic process | BP |
| GO:1902494 | catalytic complex | CC |
| GO:1990234 | transferase complex | CC |
| KEGG Term | Name | Description |
|---|---|---|
| map04144 | Endocytosis | Endocytosis is a mechanism for cells to remove ligands, nutrients, and plasma membrane (PM) proteins, and lipids from the cell surface, bringing them into the cell interior. Transmembrane proteins entering through clathrin-dependent endocytosis (CDE) have sequences in their cytoplasmic domains that bind to the APs (adaptor-related protein complexes) and enable their rapid removal from the PM. In addition to APs and clathrin, there are numerous accessory proteins including dynamin. Depending on the various proteins that enter the endosome membrane, these cargoes are sorted to distinct destinations. Some cargoes, such as nutrient receptors, are recycled back to the PM. Ubiquitylated membrane proteins, such as activated growth-factor receptors, are sorted into intraluminal vesicles and eventually end up in the lysosome lumen via multivesicular endosomes (MVEs). There are distinct mechanisms of clathrin-independent endocytosis (CIE) depending upon the cargo and the cell type. |
| 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. |
| map01100 | Metabolic pathways | - |
| map00513 | Various types of N-glycan biosynthesis | - |
| map00510 | N-Glycan biosynthesis | N-glycans or asparagine-linked glycans are major constituents of glycoproteins in eukaryotes. N-glycans are covalently attached to asparagine with the consensus sequence of Asn-X-Ser/Thr by an N-glycosidic bond, GlcNAc b1- Asn. Biosynthesis of N-glycans begins on the cytoplasmic face of the ER membrane with the transferase reaction of UDP-GlcNAc and the lipid-like precursor P-Dol (dolichol phosphate) to generate GlcNAc a1- PP-Dol. After sequential addition of monosaccharides by ALG glycosyltransferases [MD:M00055], the N-glycan precursor is attached by the OST (oligosaccharyltransferase) complex to the polypeptide chain that is being synthesized and translocated through the ER membrane. The protein-bound N-glycan precursor is subsequently trimmed, extended, and modified in the ER and Golgi by a complex series of reactions catalyzed by membrane-bound glycosidases and glycosyltransferases. N-glycans thus synthesized are classified into three types: high-mannose type, complex type, and hybrid type. Defects in N-glycan biosynthesis lead to a variety of human diseases known as congenital disorders of glycosylation [DS:H00118 H00119]. |