Heme oxygenase 1
Details
- Name
- Heme oxygenase 1
- Synonyms
- 1.14.14.18
- HO
- HO-1
- HO1
- Gene Name
- HMOX1
- Organism
- Humans
- Amino acid sequence
>lcl|BSEQ0021270|Heme oxygenase 1 MERPQPDSMPQDLSEALKEATKEVHTQAENAEFMRNFQKGQVTRDGFKLVMASLYHIYVA LEEEIERNKESPVFAPVYFPEELHRKAALEQDLAFWYGPRWQEVIPYTPAMQRYVKRLHE VGRTEPELLVAHAYTRYLGDLSGGQVLKKIAQKALDLPSSGEGLAFFTFPNIASATKFKQ LYRSRMNSLEMTPAVRQRVIEEAKTAFLLNIQLFEELQELLTHDTKDQSPSRAPGLRQRA SNKVQDSAPVETPRGKPPLNTRSQAPLLRWVLTLSFLVATVAVGLYAM
- Number of residues
- 288
- Molecular Weight
- 32818.345
- Theoretical pI
- 8.68
- GO Classification
- Functionsenzyme binding / heme binding / heme oxygenase (decyclizing) activity / metal ion binding / phospholipase D activity / protein homodimerization activity / signal transducer activityProcessesangiogenesis / cell death / cellular iron ion homeostasis / cellular response to arsenic-containing substance / cellular response to cadmium ion / cellular response to heat / cellular response to hypoxia / cellular response to nutrient / endothelial cell proliferation / erythrocyte homeostasis / excretion / heme catabolic process / heme oxidation / intracellular signal transduction / intrinsic apoptotic signaling pathway in response to DNA damage / iron ion homeostasis / low-density lipoprotein particle clearance / negative regulation of DNA binding / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / negative regulation of leukocyte migration / negative regulation of mast cell cytokine production / negative regulation of mast cell degranulation / negative regulation of muscle cell apoptotic process / negative regulation of neuron apoptotic process / negative regulation of sequence-specific DNA binding transcription factor activity / negative regulation of smooth muscle cell proliferation / porphyrin-containing compound metabolic process / positive regulation of angiogenesis / positive regulation of chemokine biosynthetic process / positive regulation of I-kappaB kinase/NF-kappaB signaling / positive regulation of smooth muscle cell proliferation / positive regulation of vasodilation / protein homooligomerization / regulation of angiogenesis / regulation of blood pressure / regulation of sequence-specific DNA binding transcription factor activity / regulation of transcription from RNA polymerase II promoter in response to iron / regulation of transcription from RNA polymerase II promoter in response to oxidative stress / response to estrogen / response to hydrogen peroxide / response to nicotine / response to oxidative stress / small GTPase mediated signal transduction / small molecule metabolic process / smooth muscle hyperplasia / transmembrane transport / wound healing involved in inflammatory responseComponentscaveola / cytosol / endoplasmic reticulum / endoplasmic reticulum membrane / extracellular space / membrane / nucleolus / nucleus / perinuclear region of cytoplasm
- 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.
- Pfam Domain Function
- Heme_oxygenase (PF01126)
- Transmembrane Regions
- Not Available
- 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
- Chromosome Location
- 22
- Locus
- 22q12|22q13.1
- External Identifiers
Resource Link UniProtKB ID P09601 UniProtKB Entry Name HMOX1_HUMAN GenBank Protein ID 35173 GenBank Gene ID X06985 GenAtlas ID HMOX1 HGNC ID HGNC:5013 - General 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB00157 NADH approved, nutraceutical unknown Details DB01942 Formic acid experimental, investigational unknown Details DB02073 Biliverdine IX Alpha experimental unknown Details DB02468 12-Phenylheme experimental unknown Details DB03906 2-Phenylheme experimental unknown Details DB04912 Stannsoporfin investigational unknown Details DB04803 Verdoheme experimental unknown Details DB06914 1-({2-[2-(4-CHLOROPHENYL)ETHYL]-1,3-DIOXOLAN-2-YL}METHYL)-1H-IMIDAZOLE experimental unknown Details DB07342 1-(adamantan-1-yl)-2-(1H-imidazol-1-yl)ethanone experimental unknown Details DB00163 Vitamin E approved, nutraceutical, vet_approved unknown inducer Details DB09221 Polaprezinc experimental unknown inducer Details DB14001 alpha-Tocopherol succinate approved, nutraceutical, vet_approved unknown inducer Details DB14002 D-alpha-Tocopherol acetate approved, nutraceutical, vet_approved unknown inducer Details