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MGP001471

UniProt Annotations

Entry Information

Gene Name	heme oxygenase (decycling) 1
Protein Entry	HMOX1_HUMAN
UniProt ID	P09601
Species	Human

Comments

Comment type	Description
Catalytic Activity	Protoheme + 3 AH(2) + 3 O(2) = biliverdin + Fe(2+) + CO + 3 A + 3 H(2)O.
Disease	Heme oxygenase 1 deficiency (HMOX1D) [MIM:614034]: A disease characterized by impaired stress hematopoiesis, resulting in marked erythrocyte fragmentation and intravascular hemolysis, coagulation abnormalities, endothelial damage, and iron deposition in renal and hepatic tissues. Clinical features include persistent hemolytic anemia, asplenia, nephritis, generalized erythematous rash, growth retardation and hepatomegaly. {ECO:0000269\|PubMed:9884342}. Note=The disease is caused by mutations affecting the gene represented in this entry.
Function	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. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis.
Induction	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.
Similarity	Belongs to the heme oxygenase family. {ECO:0000305}.
Subcellular Location	Microsome {ECO:0000269\|PubMed:22419571}. Endoplasmic reticulum membrane {ECO:0000269\|PubMed:22419571}; Peripheral membrane protein {ECO:0000269\|PubMed:22419571}; Cytoplasmic side {ECO:0000269\|PubMed:22419571}.
Tissue Specificity	Expressed at higher levels in renal cancer tissue than in normal tissue (at protein level). {ECO:0000269\|PubMed:20855888}.
Web Resource	Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/hmox1/";