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Literature summary for 1.14.11.2 extracted from
- Subcellular localization of procollagen I and prolyl 4-hydroxylase in corneal endothelial cells (2001), Exp. Cell Res., 264, 363-371.
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| endoplasmic reticulum | co-localization with procollagen I: perinuclear site | Oryctolagus cuniculus | 5783 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Oryctolagus cuniculus | molecular mechanism of intracellular degradation of type I collagen in normal corneal endothelial cells, role of the enzyme and protein-disulfide isomerase, which is the beta subunit of the enzyme, during procollagen I biosynthesis | ? | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Oryctolagus cuniculus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| corneal endothelium | - |
Oryctolagus cuniculus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | molecular mechanism of intracellular degradation of type I collagen in normal corneal endothelial cells, role of the enzyme and protein-disulfide isomerase, which is the beta subunit of the enzyme, during procollagen I biosynthesis | Oryctolagus cuniculus | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| tetramer | alpha2 beta2, alpha: 65000, beta: 60000, SDS-PAGE | Oryctolagus cuniculus |
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