HMOX1

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

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; OMA:HMOX1 - orthologs
Gene location (Human) Chr. Chromosome 22 (human) Band 22q12.3 Start 35,380,361 bp End 35,394,214 bp
Gene location (Mouse) Chr. Chromosome 8 (mouse) Band 8 35.59 cM|8 C1 Start 75,820,249 bp End 75,827,217 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in cartilage tissue spleen monocyte granulocyte islet of Langerhans left ovary mucosa of transverse colon skin of leg gallbladder right ovary Top expressed in stroma of bone marrow spleen tibiofemoral joint lens granulocyte lip esophagus placenta calvaria yolk sac More reference expression data BioGPS More reference expression data
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 nucleolus endoplasmic reticulum caveola perinuclear region of cytoplasm nucleus extracellular space 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 small GTPase mediated signal transduction 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 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 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 negative regulation of leukocyte migration cellular response to hypoxia response to hydrogen peroxide negative regulation of cell population 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 associated smooth muscle cell proliferation negative regulation of epithelial cell apoptotic process liver regeneration negative regulation of macroautophagy Sources:Amigo / QuickGO
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: 75.82 – 75.83 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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

Heme oxygenase

Main article: Heme oxygenase

Heme oxygenase, an essential enzyme in heme catabolism, cleaves heme to form biliverdin, carbon monoxide, and ferrous iron. 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.

See also

• HMOX2
• Focal segmental glomerulosclerosis

Further reading

• Yachie A, Niida Y, Wada T, Igarashi N, Kaneda H, Toma T, Ohta K, Kasahara Y, Koizumi S (1999). "Oxidative stress causes enhanced endothelial cell injury in human heme oxygenase-1 deficiency". J Clin Invest. 103 (1): 129–35. doi:10.1172/JCI4165. PMC 407858. PMID 9884342.
• Zhang Z, Song Y, Zhang Z, Li D, Zhu H, Liang R, Gu Y, Pang Y, Qi J, Wu H, Wang J (2016). "Distinct role of heme oxygenase-1 in early- and late-stage intracerebral hemorrhage in 12-month-old mice". J Cereb Blood Flow Metab. 37 (1): 25–38. doi:10.1177/0271678X16655814. PMC 5363754. PMID 27317654.
• Wang J, Doré S (2007). "Heme oxygenase-1 exacerbates early brain injury after intracerebral haemorrhage". Brain. 130 (6): 1643–52. doi:10.1093/brain/awm095. PMC 2291147. PMID 17525142.
• Soares MP, Brouard S, Smith RN, Bach FH (2002). "Heme oxygenase-1, a protective gene that prevents the rejection of transplanted organs". Immunol. Rev. 184: 275–85. doi:10.1034/j.1600-065x.2001.1840124.x. PMID 12086318. S2CID 5876166.
• Morse D, Choi AM (2002). "Heme oxygenase-1: the "emerging molecule" has arrived". Am. J. Respir. Cell Mol. Biol. 27 (1): 8–16. doi:10.1165/ajrcmb.27.1.4862. PMID 12091240.
• Buelow R, Tullius SG, Volk HD (2002). "Protection of grafts by hemoxygenase-1 and its toxic product carbon monoxide". Am. J. Transplant. 1 (4): 313–5. doi:10.1034/j.1600-6143.2001.10404.x. PMID 12099373. S2CID 41282418.
• Ishikawa K (2003). "Heme oxygenase-1 against vascular insufficiency: roles of atherosclerotic disorders". Curr. Pharm. Des. 9 (30): 2489–97. doi:10.2174/1381612033453767. PMID 14529548.
• Exner M, Minar E, Wagner O, Schillinger M (2005). "The role of heme oxygenase-1 promoter polymorphisms in human disease". Free Radic. Biol. Med. 37 (8): 1097–104. doi:10.1016/j.freeradbiomed.2004.07.008. PMID 15451051.
• Ozono R (2006). "New biotechnological methods to reduce oxidative stress in the cardiovascular system: focusing on the Bach1/heme oxygenase-1 pathway". Current Pharmaceutical Biotechnology. 7 (2): 87–93. doi:10.2174/138920106776597630. PMID 16724942.
• Tracz MJ, Alam J, Nath KA (2007). "Physiology and pathophysiology of heme: implications for kidney disease". J. Am. Soc. Nephrol. 18 (2): 414–20. doi:10.1681/ASN.2006080894. PMID 17229906.
• Chang CF, Cho S, Wang J (2014). "(-)-Epicatechin protects hemorrhagic brain via synergistic Nrf2 pathways". Annals of Clinical and Translational Neurology. 1 (4): 258–271. doi:10.1002/acn3.54. PMC 3984761. PMID 24741667.
• Hill-Kapturczak N, Agarwal A (2007). "Haem oxygenase-1--a culprit in vascular and renal damage?". Nephrol. Dial. Transplant. 22 (6): 1495–9. doi:10.1093/ndt/gfm093. PMID 17389623.

External links

• Overview of all the structural information available in the PDB for UniProt: P09601 (Heme oxygenase 1) at the PDBe-KB.