HMOX1

HMOX1
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, 4WD4, 5BTQ
Identifiers
Aliases	HMOX1, HMOX1D, HO-1, HSP32, bK286B10, heme oxygenase 1
External IDs	OMIM: 141250 MGI: 96163 HomoloGene: 31075 GeneCards: HMOX1
Genetically Related Diseases
obesity[1]
Gene ontology Molecular function • phospholipase D activity • protein homodimerization activity • heme oxygenase (decyclizing) activity • metal ion binding • signal transducer activity • heme binding • protein binding • enzyme binding • oxidoreductase activity Cellular component • cytosol • endoplasmic reticulum membrane • membrane • intracellular membrane-bounded organelle • extracellular fluid • nucleolus • endoplasmic reticulum • caveola • perinuclear region of cytoplasm • nucleus Biological process • negative regulation of neuron apoptotic process • apoptotic process • cellular iron ion homeostasis • negative regulation of smooth muscle cell proliferation • cellular response to heat • intracellular signal transduction • negative regulation of mast cell cytokine production • response to hypoxia • excretion • low-density lipoprotein particle clearance • regulation of transcription from RNA polymerase II promoter in response to oxidative stress • positive regulation of chemokine biosynthetic process • small GTPase mediated signal transduction • positive regulation of vasodilation • negative regulation of DNA binding • response to nicotine • iron ion homeostasis • cell death • heme oxidation • negative regulation of mast cell degranulation • cellular response to cadmium ion • regulation of angiogenesis • negative regulation of muscle cell apoptotic process • response to oxidative stress • negative regulation of sequence-specific DNA binding transcription factor activity • cellular response to nutrient • positive regulation of angiogenesis • response to estrogen • wound healing involved in inflammatory response • regulation of blood pressure • heme catabolic process • erythrocyte homeostasis • regulation of sequence-specific DNA binding transcription factor activity • cellular response to arsenic-containing substance • negative regulation of extrinsic apoptotic signaling pathway via death domain receptors • angiogenesis • intrinsic apoptotic signaling pathway in response to DNA damage • endothelial cell proliferation • positive regulation of I-kappaB kinase/NF-kappaB signaling • smooth muscle hyperplasia • protein homooligomerization • oxidation-reduction process • negative regulation of leukocyte migration • cellular response to hypoxia • response to hydrogen peroxide • negative regulation of cell proliferation • heme metabolic process • positive regulation of smooth muscle cell proliferation • regulation of transcription from RNA polymerase II promoter in response to iron • positive regulation of apoptotic process • cellular response to cisplatin • positive regulation of macroautophagy • negative regulation of vascular smooth muscle cell proliferation • negative regulation of epithelial cell apoptotic process • liver regeneration 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_002124.1	NP_034572.1
Location (UCSC)	Chr 22: 35.38 – 35.39 Mb	Chr 8: 75.09 – 75.1 Mb
PubMed search	[2]	[3]
Wikidata

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.^[4] 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.^[5]

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 interleukin 10 (IL-10) and interleukin 1 receptor antagonist (IL-1RA) expression.^[6]

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