Heme oxygenase 1

Name	Heme oxygenase 1
Synonyms	1.14.14.18 HO HO-1 HO1
Gene Name	HMOX1
Organism	Human
Amino acid sequence	>lcl\|BSEQ0021270\|Heme oxygenase 1 MERPQPDSMPQDLSEALKEATKEVHTQAENAEFMRNFQKGQVTRDGFKLVMASLYHIYVA LEEEIERNKESPVFAPVYFPEELHRKAALEQDLAFWYGPRWQEVIPYTPAMQRYVKRLHE VGRTEPELLVAHAYTRYLGDLSGGQVLKKIAQKALDLPSSGEGLAFFTFPNIASATKFKQ LYRSRMNSLEMTPAVRQRVIEEAKTAFLLNIQLFEELQELLTHDTKDQSPSRAPGLRQRA SNKVQDSAPVETPRGKPPLNTRSQAPLLRWVLTLSFLVATVAVGLYAM
Number of residues	None
Molecular Weight	32818.345
Theoretical pI	8.68
GO Classification	Functions heme binding signal transducer activity metal ion binding enzyme binding protein homodimerization activity phospholipase D activity heme oxygenase (decyclizing) activity Processes transmembrane transport cellular response to arsenic-containing substance cellular response to cadmium ion positive regulation of angiogenesis negative regulation of smooth muscle cell proliferation heme oxidation response to hydrogen peroxide negative regulation of mast cell degranulation erythrocyte homeostasis excretion cellular iron ion homeostasis small GTPase mediated signal transduction negative regulation of extrinsic apoptotic signaling pathway via death domain receptors negative regulation of DNA binding regulation of blood pressure heme catabolic process intracellular signal transduction cellular response to nutrient negative regulation of neuron apoptotic process positive regulation of I-kappaB kinase/NF-kappaB signaling response to estrogen regulation of transcription from RNA polymerase II promoter in response to iron iron ion homeostasis protein homooligomerization small molecule metabolic process negative regulation of muscle cell apoptotic process wound healing involved in inflammatory response response to nicotine cellular response to heat angiogenesis negative regulation of mast cell cytokine production cell death negative regulation of leukocyte migration regulation of sequence-specific DNA binding transcription factor activity low-density lipoprotein particle clearance regulation of transcription from RNA polymerase II promoter in response to oxidative stress response to oxidative stress porphyrin-containing compound metabolic process positive regulation of chemokine biosynthetic process positive regulation of smooth muscle cell proliferation negative regulation of sequence-specific DNA binding transcription factor activity endothelial cell proliferation cellular response to hypoxia positive regulation of vasodilation intrinsic apoptotic signaling pathway in response to DNA damage regulation of angiogenesis smooth muscle hyperplasia Components membrane nucleus caveola endoplasmic reticulum cytosol nucleolus extracellular space perinuclear region of cytoplasm endoplasmic reticulum membrane
General Function	Signal transducer activity
Specific Function	Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis.
Transmembrane Regions
GenBank Protein ID
UniProtKB ID	P09601
UniProtKB Entry Name
Cellular Location	Microsome
Gene sequence	>lcl\|BSEQ0021271\|Heme oxygenase 1 (HMOX1) ATGGAGCGTCCGCAACCCGACAGCATGCCCCAGGATTTGTCAGAGGCCCTGAAGGAGGCC ACCAAGGAGGTGCACACCCAGGCAGAGAATGCTGAGTTCATGAGGAACTTTCAGAAGGGC CAGGTGACCCGAGACGGCTTCAAGCTGGTGATGGCCTCCCTGTACCACATCTATGTGGCC CTGGAGGAGGAGATTGAGCGCAACAAGGAGAGCCCAGTCTTCGCCCCTGTCTACTTCCCA GAAGAGCTGCACCGCAAGGCTGCCCTGGAGCAGGACCTGGCCTTCTGGTACGGGCCCCGC TGGCAGGAGGTCATCCCCTACACACCAGCCATGCAGCGCTATGTGAAGCGGCTCCACGAG GTGGGGCGCACAGAGCCCGAGCTGCTGGTGGCCCACGCCTACACCCGCTACCTGGGTGAC CTGTCTGGGGGCCAGGTGCTCAAAAAGATTGCCCAGAAAGCCCTGGACCTGCCCAGCTCT GGCGAGGGCCTGGCCTTCTTCACCTTCCCCAACATTGCCAGTGCCACCAAGTTCAAGCAG CTCTACCGCTCCCGCATGAACTCCCTGGAGATGACTCCCGCAGTCAGGCAGAGGGTGATA GAAGAGGCCAAGACTGCGTTCCTGCTCAACATCCAGCTCTTTGAGGAGTTGCAGGAGCTG CTGACCCATGACACCAAGGACCAGAGCCCCTCACGGGCACCAGGGCTTCGCCAGCGGGCC AGCAACAAAGTGCAAGATTCTGCCCCCGTGGAGACTCCCAGAGGGAAGCCCCCACTCAAC ACCCGCTCCCAGGCTCCGCTTCTCCGATGGGTCCTTACACTCAGCTTTCTGGTGGCGACA GTTGCTGTAGGGCTTTATGCCATGTGA
GenBank Gene ID
GeneCard ID	None
GenAtlas ID
HGNC ID
Chromosome Location	22
Locus	22q12\|22q13.1
References	Yoshida T, Biro P, Cohen T, Muller RM, Shibahara S: Human heme oxygenase cDNA and induction of its mRNA by hemin. Eur J Biochem. 1988 Feb 1;171(3):457-61. [3345742 ] Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [15461802 ] Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [10591208 ] Keyse SM, Tyrrell RM: Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite. Proc Natl Acad Sci U S A. 1989 Jan;86(1):99-103. [2911585 ] Shibahara S, Sato M, Muller RM, Yoshida T: Structural organization of the human heme oxygenase gene and the function of its promoter. Eur J Biochem. 1989 Feb 15;179(3):557-63. [2537723 ] Yachie A, Niida Y, Wada T, Igarashi N, Kaneda H, Toma T, Ohta K, Kasahara Y, Koizumi S: Oxidative stress causes enhanced endothelial cell injury in human heme oxygenase-1 deficiency. J Clin Invest. 1999 Jan;103(1):129-35. [9884342 ] Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [17081983 ] Gozzelino R, Jeney V, Soares MP: Mechanisms of cell protection by heme oxygenase-1. Annu Rev Pharmacol Toxicol. 2010;50:323-54. doi: 10.1146/annurev.pharmtox.010909.105600. [20055707 ] Datta D, Banerjee P, Gasser M, Waaga-Gasser AM, Pal S: CXCR3-B can mediate growth-inhibitory signals in human renal cancer cells by down-regulating the expression of heme oxygenase-1. J Biol Chem. 2010 Nov 19;285(47):36842-8. doi: 10.1074/jbc.M110.170324. Epub 2010 Sep 20. [20855888 ] Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal. 2010 Jan 12;3(104):ra3. doi: 10.1126/scisignal.2000475. [20068231 ] Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [21269460 ] Gottlieb Y, Truman M, Cohen LA, Leichtmann-Bardoogo Y, Meyron-Holtz EG: Endoplasmic reticulum anchored heme-oxygenase 1 faces the cytosol. Haematologica. 2012 Oct;97(10):1489-93. doi: 10.3324/haematol.2012.063651. Epub 2012 Mar 14. [22419571 ] Schuller DJ, Wilks A, Ortiz de Montellano PR, Poulos TL: Crystal structure of human heme oxygenase-1. Nat Struct Biol. 1999 Sep;6(9):860-7. [10467099 ] Lad L, Wang J, Li H, Friedman J, Bhaskar B, Ortiz de Montellano PR, Poulos TL: Crystal structures of the ferric, ferrous, and ferrous-NO forms of the Asp140Ala mutant of human heme oxygenase-1: catalytic implications. J Mol Biol. 2003 Jul 11;330(3):527-38. [12842469 ]

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