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HMOX2
Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter. Belongs to the heme oxygenase family. Note: This description may include information from UniProtKB.
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| Protein type: EC 1.14.99.3; Cofactor and Vitamin Metabolism - porphyrin and chlorophyll; Oxidoreductase |
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Cellular Component: endoplasmic reticulum membrane; plasma membrane
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Molecular Function: protein binding; metal ion binding; heme oxygenase (decyclizing) activity
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Biological Process: heme catabolic process; cellular iron ion homeostasis; porphyrin metabolic process; response to hypoxia; heme oxidation; response to oxidative stress; transmembrane transport
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Reference #:
P30519 (UniProtKB)
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| Alt. Names/Synonyms: heme oxygenase (decycling) 2; Heme oxygenase 2; HMOX2; HO-2; HO2 |
| Gene Symbols: HMOX2 |
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Molecular weight: 36,033 Da
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Basal Isoelectric point: 5.31
Predict pI for various phosphorylation states
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Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®
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