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
Gene location (Human)
Chr.	Chromosome 22 (human)
End	35,394,214 bp
Gene location (Mouse)
Chr.	Chromosome 8 (mouse)
End	75,100,589 bp
RNA expression pattern
	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; • GO:0001948 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; • GO:0007243 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
	3162
	15368
	ENSG00000100292
	ENSMUSG00000005413
	P09601
	P14901
	NM_002133
	NM_010442
	NP_002124
	NP_034572
	Wikidata
View/Edit Human	View/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]

References

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

External links

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

This article is issued from Offline. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000100292 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 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".

[1]

[2]

[3]

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[5]

[6]

Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14)
1.14.11: 2-oxoglutarate	Prolyl hydroxylase HIF prolyl-hydroxylase EGLN1 EGLN2 EGLN3 P4HTM Lysyl hydroxylase AlkB ALKBH1 FTO
1.14.13: NADH or NADPH	Flavin-containing monooxygenase FMO1 FMO2 FMO3 FMO4 FMO5 Nitric oxide synthase NOS1 NOS2 NOS3 Cholesterol 7 alpha-hydroxylase Methane monooxygenase 3A4 14α-demethylase 24-hydroxycholesterol 7α-hydroxylase
1.14.14: reduced flavin or flavoprotein	19A1 2D6 2E1
1.14.15: reduced iron-sulfur protein	11B1 11B2 11A1
1.14.16: reduced pteridine (BH4 dependent)	Phenylalanine hydroxylase Tyrosine hydroxylase Tryptophan hydroxylase
1.14.17: reduced ascorbate	Dopamine beta-hydroxylase
1.14.18-19: other	Tyrosinase Stearoyl-CoA desaturase-1
1.14.99 - miscellaneous	Cyclooxygenase Heme oxygenase (HMOX1) Squalene monooxygenase 17A1 21A2 Ecdysone 20-monooxygenase Deoxyhypusine monooxygenase

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

HMOX1

Related conditions

Heme oxygenase

See also

References

Further reading

External links