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 1 activity is highly inducible by its substrate heme and by various non-heme substances such as heavy metals, bromobenzene, endotoxin, oxidizing agents and UVA. Expressed at higher levels in renal cancer tissue than in normal tissue. Belongs to the heme oxygenase family. Note: This description may include information from UniProtKB.
Protein type: EC 220.127.116.11; Oxidoreductase; Cofactor and Vitamin Metabolism - porphyrin and chlorophyll
Cellular Component: extracellular space; endoplasmic reticulum membrane; membrane; perinuclear region of cytoplasm; endoplasmic reticulum; nucleolus; caveola; nucleus; cytosol
Molecular Function: signal transducer activity; protein binding; protein homodimerization activity; enzyme binding; metal ion binding; phospholipase D activity; heme binding; heme oxygenase (decyclizing) activity
Biological Process: cell death; response to nicotine; negative regulation of smooth muscle cell proliferation; cellular iron ion homeostasis; negative regulation of mast cell degranulation; positive regulation of smooth muscle cell proliferation; excretion; positive regulation of vasodilation; erythrocyte homeostasis; regulation of transcription factor activity; heme catabolic process; regulation of blood pressure; small GTPase mediated signal transduction; porphyrin metabolic process; negative regulation of mast cell cytokine production; negative regulation of neuron apoptosis; angiogenesis; regulation of transcription from RNA polymerase II promoter in response to oxidative stress; transmembrane transport; healing during inflammatory response; protein homooligomerization; positive regulation of I-kappaB kinase/NF-kappaB cascade; negative regulation of transcription factor activity; heme oxidation; cellular response to nutrient; negative regulation of leukocyte migration; regulation of angiogenesis; negative regulation of DNA binding; iron ion homeostasis; positive regulation of angiogenesis; positive regulation of chemokine biosynthetic process; response to hydrogen peroxide; DNA damage response, signal transduction resulting in induction of apoptosis; response to estrogen stimulus; endothelial cell proliferation; response to oxidative stress; smooth muscle hyperplasia
LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.