HMOX1

Heme oxygenase (decycling) 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
Identifiers
Symbols	HMOX1; HO-1; HSP32; bK286B10
External IDs	OMIM: 141250 MGI: 96163 HomoloGene: 31075 GeneCards: HMOX1 Gene
EC number	1.14.99.3
Gene Ontology Molecular function • heme oxygenase (decyclizing) activity • heme oxygenase (decyclizing) activity • phospholipase D activity • signal transducer activity • oxidoreductase activity • enzyme binding • heme binding • protein homodimerization activity • metal ion binding Cellular component • extracellular space • membrane fraction • nucleus • nucleolus • endoplasmic reticulum • endoplasmic reticulum • endoplasmic reticulum membrane • microsome • cytosol • caveola 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 • anti-apoptosis • response to oxidative stress • signal transduction • intracellular protein kinase cascade • small GTPase mediated signal transduction • excretion • regulation of blood pressure • cell death • DNA damage response, signal transduction resulting in induction of apoptosis • smooth muscle hyperplasia • cellular response to nutrient • negative regulation of mast cell cytokine production • erythrocyte homeostasis • low-density lipoprotein particle clearance • response to nicotine • heme catabolic process • heme catabolic process • response to hydrogen peroxide • positive regulation of I-kappaB kinase/NF-kappaB cascade • 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 apoptosis • regulation of transcription from RNA polymerase II promoter in response to oxidative stress • response to estrogen stimulus • small molecule metabolic process • positive regulation of chemokine biosynthetic process • regulation of angiogenesis • positive regulation of angiogenesis • positive regulation of anti-apoptosis • positive regulation of vasodilation • positive regulation of smooth muscle cell proliferation • negative regulation of smooth muscle cell proliferation • response to stimulus • regulation of sequence-specific DNA binding transcription factor activity • protein homooligomerization • iron ion homeostasis • iron ion homeostasis • transmembrane transport • cellular response to hypoxia 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_002133.2	NM_010442.2
RefSeq (protein)	NP_002124.1	NP_034572.1
Location (UCSC)	Chr 22: 35.78 – 35.79 Mb	Chr 8: 77.62 – 77.62 Mb
PubMed search	[1]	[2]

HMOX1 (heme oxygenase (decycling) 1) is a human gene that encodes for the enzyme heme oxygenase 1 (EC 1.14.99.3). Heme oxygenase is an essential enzyme in heme catabolism, it cleaves heme to form biliverdin.

Heme oxygenase, an essential enzyme in heme catabolism, cleaves heme to form biliverdin, which is subsequently converted to bilirubin by biliverdin reductase, and carbon monoxide, a putative neurotransmitter. 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.

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

See also

• HMOX2

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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=407858. 
• 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. 
• Morse D, Choi AM (2002). "Heme oxygenase-1: the "emerging molecule" has arrived". Am. J. Respir. Cell Mol. Biol. 27 (1): 8–16. 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. 
• 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. 
• 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.