| 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 |
| negative regulation of apoptotic process |
| regulation of blood pressure |
| negative regulation of leukocyte migration |
| response to hydrogen peroxide |
| response to nicotine |
| protein homooligomerization |
| cellular response to cadmium ion |
| angiogenesis |
| regulation of angiogenesis |
| negative regulation of smooth muscle cell proliferation |
| response to estrogen stimulus |
| cellular iron ion homeostasis |
| negative regulation of sequence-specific DNA binding transcription factor activity |
| positive regulation of I-kappaB kinase/NF-kappaB cascade |
| heme catabolic process |
| negative regulation of neuron apoptotic process |
| positive regulation of vasodilation |
| positive regulation of angiogenesis |
| low-density lipoprotein particle clearance |
| excretion |
| intracellular protein kinase cascade |
| negative regulation of DNA binding |
| wound healing involved in inflammatory response |
| smooth muscle hyperplasia |
| small GTPase mediated signal transduction |
| regulation of transcription from RNA polymerase II promoter in response to oxidative stress |
| regulation of sequence-specific DNA binding transcription factor activity |
| positive regulation of smooth muscle cell proliferation |
| positive regulation of chemokine biosynthetic process |
| negative regulation of mast cell degranulation |
| negative regulation of mast cell cytokine production |
| small molecule metabolic process |
| intrinsic apoptotic signaling pathway in response to DNA damage |
| heme oxidation |
| erythrocyte homeostasis |
| endothelial cell proliferation |
| cellular response to nutrient |
| cellular response to hypoxia |
| cell death |
| transmembrane transport |
| Cellular Component |
| caveola |
| nucleolus |
| endoplasmic reticulum membrane |
| extracellular space |
| cytosol |
| nucleus |
| Function |
| oxidoreductase activity |
| catalytic activity |
| heme oxygenase (decyclizing) activity |
| oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| Molecular Function |
| heme binding |
| metal ion binding |
| protein homodimerization activity |
| phospholipase D activity |
| heme oxygenase (decyclizing) activity |
| signal transducer activity |
| enzyme binding |
| Process |
| heme oxidation |
| heme metabolic process |
| oxidation reduction |
| porphyrin metabolic process |
| tetrapyrrole metabolic process |
| nitrogen compound metabolic process |
| metabolic process |
|
| 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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