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. 2 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: Cofactor and Vitamin Metabolism - porphyrin and chlorophyll; EC 1.14.99.3; Endoplasmic reticulum; Oxidoreductase
Chromosomal Location of Human Ortholog: 16 A1|16 2.46 cM
Cellular Component:  endoplasmic reticulum; intracellular membrane-bounded organelle; membrane; plasma membrane
Molecular Function:  heme binding; heme oxygenase (decyclizing) activity; metal ion binding; oxidoreductase activity
Biological Process:  heme catabolic process; heme oxidation; iron ion homeostasis; response to hypoxia; response to oxidative stress
Reference #:  O70252 (UniProtKB)
Alt. Names/Synonyms: heme oxygenase (decycling) 2; Heme oxygenase 2; Hmox2; HO-2; HO2
Gene Symbols: Hmox2
Molecular weight: 35,739 Da
Basal Isoelectric point: 5.61  Predict pI for various phosphorylation states
Protein-Specific Antibodies, siRNAs or Recombinant Proteins from Cell Signaling Technology® Total Proteins
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HMOX2

Protein Structure Not Found.


Cross-references to other databases:  STRING  |  Reactome  |  BioGPS  |  Pfam  |  ENZYME  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene