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: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:0004572 | mannosyl-oligosaccharide 1,3-1,6-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:0005794 | Golgi apparatus | CC |
| GO:0005975 | carbohydrate metabolic process | BP |
| GO:0005996 | monosaccharide metabolic process | BP |
| GO:0006013 | mannose metabolic process | BP |
| GO:0006464 | protein modification process | BP |
| GO:0006491 | N-glycan processing | BP |
| GO:0006517 | protein deglycosylation | 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:0019318 | hexose metabolic process | BP |
| GO:0019538 | protein metabolic process | BP |
| GO:0031090 | organelle membrane | CC |
| GO:0031984 | organelle subcompartment | CC |
| GO:0036211 | protein modification process | BP |
| 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: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:0044281 | small molecule 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: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 |
|---|---|---|
| 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]. |