HMOX1

Mammalian protein found in Homo sapiens
HMOX1
Available structures
PDBOrtholog 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
AliasesHMOX1, HMOX1D, HO-1, HSP32, bK286B10, heme oxygenase 1
External IDsOMIM: 141250; MGI: 96163; HomoloGene: 31075; GeneCards: HMOX1; OMA:HMOX1 - orthologs
Gene location (Human)
Chromosome 22 (human)
Chr.Chromosome 22 (human)[1]
Chromosome 22 (human)
Genomic location for HMOX1
Genomic location for HMOX1
Band22q12.3Start35,380,361 bp[1]
End35,394,214 bp[1]
Gene location (Mouse)
Chromosome 8 (mouse)
Chr.Chromosome 8 (mouse)[2]
Chromosome 8 (mouse)
Genomic location for HMOX1
Genomic location for HMOX1
Band8 35.59 cM|8 C1Start75,820,249 bp[2]
End75,827,217 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • spleen

  • monocyte

  • islet of Langerhans

  • gallbladder

  • upper lobe of left lung

  • trabecular bone

  • duodenum

  • right lobe of liver

  • left adrenal gland

  • skin of abdomen
Top expressed in
  • spleen

  • lens

  • lip

  • esophagus

  • placenta

  • calvaria

  • yolk sac

  • adrenal gland

  • entorhinal cortex

  • proximal tubule
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
SpeciesHumanMouse
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 MbChr 8: 75.82 – 75.83 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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.

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

Heme oxygenase, an essential enzyme in heme catabolism, cleaves heme to form biliverdin, carbon monoxide, and ferrous iron.[5] 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.[6]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000100292 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000005413 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Lehninger's Principles of Biochemistry, 5th Edition. New York: W.H. Freeman and Company. 2008. pp. 876. ISBN 978-0-7167-7108-1.
  6. ^ "Entrez Gene: HMOX1 heme oxygenase (decycling) 1".

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.


  • v
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  • 1n3u: Crystal structure of human heme oxygenase 1 (HO-1) in complex with its substrate heme, crystal form B
    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
    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
    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
    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
    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
    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
    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
    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
    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
    1s13: Human Heme Oxygenase Oxidatition of alpha- and gamma-meso-Phenylhemes
  • 1s8c: Crystal structure of human heme oxygenase in a complex with biliverdine
    1s8c: Crystal structure of human heme oxygenase in a complex with biliverdine
  • 1t5p: Human Heme Oxygenase Oxidation of alpha- and gamma-meso-phenylhemes
    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
    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
    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
    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
    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
    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
    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
    1xk3: NADPH- and Ascorbate-Supported Heme Oxygenase Reactions are Distinct. Regiospecificity of Heme Cleavage by the R183E Mutant
  • v
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1.14.11: 2-oxoglutarate
1.14.13: NADH or NADPH
1.14.14: reduced flavin or flavoprotein
1.14.15: reduced iron–sulfur protein
1.14.16: reduced pteridine (BH4 dependent)
1.14.17: reduced ascorbate
1.14.18-19: other
1.14.99 - miscellaneous
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