| Identification |
|---|
| HMDB Protein ID
| HMDBP00198 |
| Secondary Accession Numbers
| |
| Name
| Heme oxygenase 1 |
| Synonyms
|
- HO-1
|
| Gene Name
| HMOX1 |
| Protein Type
| Unknown |
| Biological Properties |
|---|
| General Function
| Involved in heme oxygenase (decyclizing) 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.
|
| Pathways
|
- Acute Intermittent Porphyria
- Congenital Erythropoietic Porphyria (CEP) or Gunther Disease
- Hereditary Coproporphyria (HCP)
- HIF-1 signaling pathway
- Mineral absorption
- Porphyria Variegata (PV)
- Porphyrin and chlorophyll metabolism
- Porphyrin Metabolism
|
| Reactions
|
| Heme + AH(2) + Oxygen → Biliverdin + Fe2+ + CO + A + Water |
details
|
| Hemoglobin + FADH + Oxygen → Globin + Biliverdin + Carbon monoxide + Iron + FAD + Water |
details
|
|
| GO Classification
|
| Biological Process |
| small molecule metabolic process |
| negative regulation of sequence-specific DNA binding transcription factor activity |
| regulation of angiogenesis |
| negative regulation of neuron apoptotic process |
| negative regulation of apoptotic process |
| positive regulation of vasodilation |
| response to nicotine |
| heme catabolic process |
| cellular iron ion homeostasis |
| intracellular protein kinase cascade |
| angiogenesis |
| positive regulation of angiogenesis |
| protein homooligomerization |
| cellular response to cadmium ion |
| low-density lipoprotein particle clearance |
| positive regulation of I-kappaB kinase/NF-kappaB cascade |
| negative regulation of smooth muscle cell proliferation |
| regulation of blood pressure |
| negative regulation of leukocyte migration |
| cellular response to hypoxia |
| cellular response to nutrient |
| excretion |
| endothelial cell proliferation |
| erythrocyte homeostasis |
| heme oxidation |
| intrinsic apoptotic signaling pathway in response to DNA damage |
| negative regulation of DNA binding |
| negative regulation of mast cell cytokine production |
| negative regulation of mast cell degranulation |
| positive regulation of chemokine biosynthetic process |
| response to hydrogen peroxide |
| positive regulation of smooth muscle cell proliferation |
| regulation of sequence-specific DNA binding transcription factor activity |
| regulation of transcription from RNA polymerase II promoter in response to oxidative stress |
| small GTPase mediated signal transduction |
| smooth muscle hyperplasia |
| wound healing involved in inflammatory response |
| cell death |
| transmembrane transport |
| response to estrogen stimulus |
| Cellular Component |
| endoplasmic reticulum membrane |
| cytosol |
| nucleolus |
| nucleus |
| caveola |
| extracellular space |
| Function |
| catalytic activity |
| heme oxygenase (decyclizing) activity |
| oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| oxidoreductase activity |
| Molecular Function |
| metal ion binding |
| signal transducer activity |
| heme binding |
| protein homodimerization activity |
| enzyme binding |
| heme oxygenase (decyclizing) activity |
| phospholipase D activity |
| Process |
| metabolic process |
| nitrogen compound metabolic process |
| heme metabolic process |
| heme oxidation |
| tetrapyrrole metabolic process |
| porphyrin metabolic process |
| oxidation reduction |
|
| Cellular Location
|
- Microsome
- Endoplasmic reticulum
|
| Gene Properties |
|---|
| Chromosome Location
| 22 |
| Locus
| 22q13.1 |
| SNPs
| HMOX1 |
| Gene Sequence
|
>867 bp
ATGGAGCGTCCGCAACCCGACAGCATGCCCCAGGATTTGTCAGAGGCCCTGAAGGAGGCC
ACCAAGGAGGTGCACACCCAGGCAGAGAATGCTGAGTTCATGAGGAACTTTCAGAAGGGC
CAGGTGACCCGAGACGGCTTCAAGCTGGTGATGGCCTCCCTGTACCACATCTATGTGGCC
CTGGAGGAGGAGATTGAGCGCAACAAGGAGAGCCCAGTCTTCGCCCCTGTCTACTTCCCA
GAAGAGCTGCACCGCAAGGCTGCCCTGGAGCAGGACCTGGCCTTCTGGTACGGGCCCCGC
TGGCAGGAGGTCATCCCCTACACACCAGCCATGCAGCGCTATGTGAAGCGGCTCCACGAG
GTGGGGCGCACAGAGCCCGAGCTGCTGGTGGCCCACGCCTACACCCGCTACCTGGGTGAC
CTGTCTGGGGGCCAGGTGCTCAAAAAGATTGCCCAGAAAGCCCTGGACCTGCCCAGCTCT
GGCGAGGGCCTGGCCTTCTTCACCTTCCCCAACATTGCCAGTGCCACCAAGTTCAAGCAG
CTCTACCGCTCCCGCATGAACTCCCTGGAGATGACTCCCGCAGTCAGGCAGAGGGTGATA
GAAGAGGCCAAGACTGCGTTCCTGCTCAACATCCAGCTCTTTGAGGAGTTGCAGGAGCTG
CTGACCCATGACACCAAGGACCAGAGCCCCTCACGGGCACCAGGGCTTCGCCAGCGGGCC
AGCAACAAAGTGCAAGATTCTGCCCCCGTGGAGACTCCCAGAGGGAAGCCCCCACTCAAC
ACCCGCTCCCAGGCTCCGCTTCTCCGATGGGTCCTTACACTCAGCTTTCTGGTGGCGACA
GTTGCTGTAGGGCTTTATGCCATGTGA
|
| Protein Properties |
|---|
| Number of Residues
| 288 |
| Molecular Weight
| 32818.345 |
| Theoretical pI
| 8.257 |
| Pfam Domain Function
|
|
| Signals
|
Not Available
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
>Heme oxygenase 1
MERPQPDSMPQDLSEALKEATKEVHTQAENAEFMRNFQKGQVTRDGFKLVMASLYHIYVA
LEEEIERNKESPVFAPVYFPEELHRKAALEQDLAFWYGPRWQEVIPYTPAMQRYVKRLHE
VGRTEPELLVAHAYTRYLGDLSGGQVLKKIAQKALDLPSSGEGLAFFTFPNIASATKFKQ
LYRSRMNSLEMTPAVRQRVIEEAKTAFLLNIQLFEELQELLTHDTKDQSPSRAPGLRQRA
SNKVQDSAPVETPRGKPPLNTRSQAPLLRWVLTLSFLVATVAVGLYAM
|
| External Links |
|---|
| GenBank ID Protein
| 35173 |
| UniProtKB/Swiss-Prot ID
| P09601 |
| UniProtKB/Swiss-Prot Entry Name
| HMOX1_HUMAN |
| PDB IDs
|
|
| GenBank Gene ID
| X06985 |
| GeneCard ID
| HMOX1 |
| GenAtlas ID
| HMOX1 |
| HGNC ID
| HGNC:5013 |
| References |
|---|
| General References
| - Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
- 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. [PubMed:17081983 ]
- 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. [PubMed:10591208 ]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
- 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. [PubMed:15461802 ]
- 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. [PubMed:3345742 ]
- 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. [PubMed: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. [PubMed:2537723 ]
- 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. [PubMed:10467099 ]
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