CP — Ceruloplasmin
CP belongs to a gene co-expression module in 2 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.
CP's module in each cell type
| Cell type | Module | Shares the module with | |
|---|---|---|---|
| Endothelial | Vascular Homeostasis Endothelial cell development | ATP2A3, ATP6V1C2, C19orf33, EMP3, ICAM2, MERTK, PLLP, PPP1R14A +5 more | View in SCUBA |
| Fibroblasts | Subepithelial Fibroblast Identity Developmental | ANGPTL1, APBB1IP, ARHGAP15, CNTN1, ECM2, EFEMP1, FAM107A, FGF13 +12 more | View in SCUBA |
About the gene
| Synonyms | AB073614 |
|---|---|
| Chromosome | 3: 149162410-149221829 |
| Predicted location | Intracellular, Secreted |
| Essential gene | No |
| Protein class | Cancer-related genes, Candidate cardiovascular disease genes, Disease related genes, Enzymes, Human disease related genes, Metabolic proteins, Plasma proteins, Potential drug targets, Predicted intracellular proteins, Predicted secreted proteins, Transporters |
| Molecular function | Oxidoreductase |
Function
Multifunctional blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Copper ions provide a large number of enzymatic activites. Oxidizes highly toxic ferrous ions to the ferric state for further incorporation onto apo- transferrins, catalyzes Cu(+) oxidation and promotes the oxidation of biogenic amines such as norepinephrin and serotonin. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1 (By similarity). Has glutathione peroxidase-like activity, can remove both hydrogen peroxide and lipid hydroperoxide in the presence of thiols. Also shows NO-oxidase and NO2 synthase activities that determine endocrine NO homeostasis.
Human Protein Atlas · Open Targets · UniProt
Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.