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Showing Protein Heme oxygenase 1 (HMDBP00198)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 12 metabolites
Identification
HMDB Protein ID HMDBP00198
Secondary Accession Numbers
  • 5430
  • HMDBP04880
Name Heme oxygenase 1
Synonyms
  1. 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
  1. Microsome
  2. 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
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
  1. 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 ]
  2. 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 ]
  3. 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 ]
  4. 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 ]
  5. 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 ]
  6. 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 ]
  7. 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 ]
  8. 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 ]
  9. 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 ]