Application | Comment | Organism |
---|---|---|
biotechnology | the Lec36 cell line will be useful for expressing therapeutic glycoproteins with hybrid-type glycans and as a sensitive host for detecting mutations in human MAN2A1 causing type II congenital dyserythropoietic anemia | Homo sapiens |
Cloned (Comment) | Organism |
---|---|
gene MAN2A1 from mutant strain Lec36 and wild-type gene, DNA and amino acid sequence determination and analysis. Wild-type and mutant enzyme expression analysis, overview | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
additional information | the mutant gene MAN2A1 from strain Lec36 harbors a point mutation in the active site in one allele and an in-frame deletion of 12 nucleotides in the other allele, compared to parent HEK293T cells, which alters the glycosylation pattern. Expression of the wild-type but not the mutant MAN2A1 alleles in Lec36 cells restores processing of the 19A reporter glycoprotein to complex-type glycosylation, overview | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
swainsonine | - |
Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
Golgi apparatus | - |
Homo sapiens | 5794 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
HEK-293T cell | mutant HEK293T cell line called Lec36, which displays sensitivity to ricin that lies between the parental HEK 293T cells, in which the secreted and membrane-expressed proteins are dominated by complex-type glycosylation, and 293S Lec1 cells, which produce only oligomannose-type N-linked glycans. Lec36 cells are dominated by hybrid-type glycosylation. Wild-type and mutant enzyme expression analysis, overview | Homo sapiens | - |
Synonyms | Comment | Organism |
---|---|---|
Golgi alpha-mannosidase II | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
physiological function | the enzyme is important for N-glycosylation of protein in the Golgi apparatus | Homo sapiens |