Application | Comment | Organism |
---|---|---|
medicine | insulin/IGF-1 stimulation of asparaginyl-beta-hydroxylase and Notch are enhanced by inhibiting kinases that could phosphorylate asparaginyl-beta-hydroxylase protein. Targeted manipulation of the phosphorylation state of asparaginyl-beta-hydroxylase may have therapeutic value for reducing asparaginyl-beta-hydroxylase-Notch activation and attendant infiltrative growth of hepatocellular carcinomas | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytoplasm | the pattern of diffuse cytoplasmic staining iss reticular or particulate, consistent with the known microsomal and mitochondrial distributions of the enzyme | Homo sapiens | 5737 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q12797 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
Huh-7 cell | - |
Homo sapiens | - |
Synonyms | Comment | Organism |
---|---|---|
aspartyl-(asparaginyl)-beta-hydroxylase | - |
Homo sapiens |
Organism | Comment | Expression |
---|---|---|
Homo sapiens | IGF-1 stimulation increases asparaginyl-beta-hydroxylase protein expression and shifts localization of asparaginyl-beta-hydroxylase from the perinuclear zone to the cell periphery, including podocytes. Subsequently, Notch-1 intracellular domain is translocated to the nucleus, which is critical for Notch-modulated gene expression. Besides glycogen synthase kinase-3beta, inhibition of protein kinase C, protein kinase A, and casein kinase 2, which can potentially phosphorylate asparaginyl-beta-hydroxylase, increases IGF-1 stimulated asparaginyl-beta-hydroxylase protein. Insulin and LiCl independently and additively increase long-term asparaginyl-beta-hydroxylase protein expression | up |