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: 16p13.3
Cellular Component:  endoplasmic reticulum membrane; plasma membrane; specific granule membrane
Molecular Function:  heme oxygenase (decyclizing) activity; metal ion binding; protein binding
Biological Process:  cellular iron ion homeostasis; heme catabolic process; neutrophil degranulation; response to hypoxia
Reference #:  P30519 (UniProtKB)
Alt. Names/Synonyms: heme oxygenase (decycling) 2; Heme oxygenase 2; HMOX2; HO-2; HO2
Gene Symbols: HMOX2
Molecular weight: 36,033 Da
Basal Isoelectric point: 5.31  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:  AlphaFold  |  STRING  |  cBioPortal  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  InnateDB  |  Ensembl Protein