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:0000139 | Golgi membrane | CC |
| GO:0003674 | molecular_function | MF |
| GO:0003824 | catalytic activity | MF |
| GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds | MF |
| GO:0004559 | alpha-mannosidase activity | MF |
| GO:0004571 | mannosyl-oligosaccharide 1,2-alpha-mannosidase activity | MF |
| GO:0005575 | cellular_component | CC |
| GO:0005622 | intracellular anatomical structure | CC |
| GO:0005623 | obsolete cell | CC |
| GO:0005737 | cytoplasm | CC |
| GO:0005768 | endosome | CC |
| GO:0005783 | endoplasmic reticulum | CC |
| GO:0005794 | Golgi apparatus | CC |
| GO:0005802 | trans-Golgi network | CC |
| GO:0006491 | N-glycan processing | BP |
| GO:0006807 | nitrogen compound metabolic process | BP |
| GO:0008150 | biological_process | BP |
| GO:0008152 | metabolic process | BP |
| GO:0009100 | glycoprotein metabolic process | BP |
| GO:0009987 | cellular process | BP |
| GO:0012505 | endomembrane system | CC |
| GO:0015923 | mannosidase activity | MF |
| GO:0015924 | mannosyl-oligosaccharide mannosidase activity | MF |
| GO:0016020 | membrane | CC |
| GO:0016787 | hydrolase activity | MF |
| GO:0016798 | hydrolase activity, acting on glycosyl bonds | MF |
| GO:0019538 | protein metabolic process | BP |
| GO:0031090 | organelle membrane | CC |
| GO:0031410 | cytoplasmic vesicle | CC |
| GO:0031982 | vesicle | CC |
| GO:0031984 | organelle subcompartment | 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:0044237 | cellular metabolic process | BP |
| GO:0044238 | primary metabolic process | BP |
| GO:0044260 | cellular macromolecule metabolic process | BP |
| GO:0044422 | obsolete organelle part | CC |
| GO:0044424 | obsolete intracellular part | CC |
| GO:0044431 | obsolete Golgi apparatus part | CC |
| GO:0044444 | obsolete cytoplasmic part | CC |
| GO:0044446 | obsolete intracellular organelle part | CC |
| GO:0044464 | obsolete cell part | CC |
| GO:0071704 | organic substance metabolic process | BP |
| GO:0097708 | intracellular vesicle | CC |
| GO:0098588 | bounding membrane of organelle | CC |
| GO:0098791 | Golgi apparatus subcompartment | CC |
| GO:1901135 | carbohydrate derivative metabolic process | BP |
| 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. |
| 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]. |