HMOX1

Heme oxygenase 1
PDB rendering based on 1n3u.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1N3U​, 1N45​, 1NI6​, 1OYK​, 1OYL​, 1OZE​, 1OZL​, 1OZR​, 1OZW​, 1S13​, 1S8C​, 1T5P​, 1TWN​, 1TWR​, 1XJZ​, 1XK0​, 1XK1​, 1XK2​, 1XK3​, 3CZY​, 3HOK​, 3K4F​, 3TGM​
Identifiers
Symbols	HMOX1 ; HMOX1D; HO-1; HSP32; bK286B10
External IDs	OMIM: 141250 MGI: 96163 HomoloGene: 31075 ChEMBL: 2823 GeneCards: HMOX1 Gene
EC number	1.14.99.3
Gene ontology Molecular function • heme oxygenase (decyclizing) activity • phospholipase D activity • signal transducer activity • protein binding • enzyme binding • heme binding • protein homodimerization activity • metal ion binding Cellular component • extracellular space • nucleus • nucleolus • endoplasmic reticulum • endoplasmic reticulum membrane • cytosol • caveola • membrane • perinuclear region of cytoplasm Biological process • angiogenesis • endothelial cell proliferation • wound healing involved in inflammatory response • negative regulation of leukocyte migration • porphyrin-containing compound metabolic process • heme oxidation • cellular iron ion homeostasis • response to oxidative stress • small GTPase mediated signal transduction • excretion • regulation of blood pressure • cell death • intrinsic apoptotic signaling pathway in response to DNA damage • negative regulation of muscle cell apoptotic process • smooth muscle hyperplasia • cellular response to nutrient • negative regulation of mast cell cytokine production • erythrocyte homeostasis • low-density lipoprotein particle clearance • regulation of transcription from RNA polymerase II promoter in response to iron • cellular response to heat • response to nicotine • intracellular signal transduction • heme catabolic process • response to hydrogen peroxide • positive regulation of I-kappaB kinase/NF-kappaB signaling • negative regulation of mast cell degranulation • negative regulation of DNA binding • negative regulation of sequence-specific DNA binding transcription factor activity • negative regulation of neuron apoptotic process • regulation of transcription from RNA polymerase II promoter in response to oxidative stress • response to estrogen • small molecule metabolic process • positive regulation of chemokine biosynthetic process • regulation of angiogenesis • positive regulation of angiogenesis • positive regulation of vasodilation • positive regulation of smooth muscle cell proliferation • negative regulation of smooth muscle cell proliferation • regulation of sequence-specific DNA binding transcription factor activity • protein homooligomerization • iron ion homeostasis • transmembrane transport • cellular response to arsenic-containing substance • cellular response to cadmium ion • cellular response to hypoxia • negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	3162	15368
Ensembl	ENSG00000100292	ENSMUSG00000005413
UniProt	P09601	P14901
RefSeq (mRNA)	NM_002133	NM_010442
RefSeq (protein)	NP_002124	NP_034572
Location (UCSC)	Chr 22: 35.38 – 35.39 Mb	Chr 8: 75.09 – 75.1 Mb
PubMed search

HMOX1 (heme oxygenase (decycling) 1) is a human gene that encodes for the enzyme heme oxygenase 1 (EC 1.14.99.3). Heme oxygenase mediates the first step of heme catabolism, it cleaves heme to form biliverdin.

Heme oxygenase, an essential enzyme in heme catabolism, cleaves heme to form biliverdin, carbon monoxide, and ferrous iron.^[1] The biliverdin is subsequently converted to bilirubin by biliverdin reductase. Heme oxygenase activity is induced by its substrate heme and by various nonheme substances. Heme oxygenase occurs as 2 isozymes, an inducible heme oxygenase-1 and a constitutive heme oxygenase-2. HMOX1 and HMOX2 belong to the heme oxygenase family.^[2]

The HMOX gene is located on the long (q) arm of chromosome 22 at position 12.3, from base pair 34,101,636 to base pair 34,114,748.

Related conditions

Heme oxygenase-1 deficiency

Anti-inflammatory effect

The ability of oxygenase 1 to catabolize free heme and produce carbon monoxide (CO) gives its antiinflammatory properties by up-regulation of IL-10 and IL-1R antagonist expression.^[3]

See also

• HMOX2
• Focal segmental glomerulosclerosis

References

Further reading

PDB gallery 1n3u: Crystal structure of human heme oxygenase 1 (HO-1) in complex with its substrate heme, crystal form B  1n45: X-RAY CRYSTAL STRUCTURE OF HUMAN HEME OXYGENASE-1 (HO-1) IN COMPLEX WITH ITS SUBSTRATE HEME  1ni6: Comparisons of the Heme-Free and-Bound Crystal Structures of Human Heme Oxygenase-1  1oyk: Crystal Structures of the Ferric, Ferrous, and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications  1oyl: Crystal Structures of the Ferric, Ferrous, and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications  1oze: Crystal Structures of the Ferric, Ferrous, and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1:Catalytic Implications  1ozl: Crystal Structures of the Ferric, Ferrous, and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications  1ozr: Crystal Structures of the Ferric, Ferrous and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications  1ozw: Crystal Structures of the Ferric, Ferrous and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications  1s13: Human Heme Oxygenase Oxidatition of alpha- and gamma-meso-Phenylhemes  1s8c: Crystal structure of human heme oxygenase in a complex with biliverdine  1t5p: Human Heme Oxygenase Oxidation of alpha- and gamma-meso-phenylhemes  1twn: Crystal structures of ferrous and ferrous-NO forms of verdoheme in a complex with human heme oxygenase-1: catalytic implications for heme cleavage  1twr: Crystal structures of ferrous and ferrous-NO forms of verdoheme in a complex with human heme oxygenase-1: catalytic implications for heme cleavage  1xjz: Crystal Structures of the G139A, G139A-NO and G143H Mutants of Human Heme Oxygenase-1  1xk0: Crystal Structures of the G139A, G139A-NO and G143H Mutants of Human Heme Oxygenase-1  1xk1: Crystal Structures of the G139A, G139A-NO and G143H Mutants of Human Heme Oxygenase-1  1xk2: NADPH- and Ascorbate-Supported Heme Oxygenase Reactions are Distinct. Regiospecificity of Heme Cleavage by the R183E Mutant  1xk3: NADPH- and Ascorbate-Supported Heme Oxygenase Reactions are Distinct. Regiospecificity of Heme Cleavage by the R183E Mutant