HMOX1

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Heme oxygenase (decycling) 1
Protein HMOX1 PDB 1n3u.png
PDB rendering based on 1n3u.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols HMOX1 ; HMOX1D; HO-1; HSP32; bK286B10
External IDs OMIM141250 MGI96163 HomoloGene31075 ChEMBL: 2823 GeneCards: HMOX1 Gene
EC number 1.14.99.3
RNA expression pattern
PBB GE HMOX1 203665 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 3162 15368
Ensembl ENSG00000100292 ENSMUSG00000005413
UniProt P09601 P14901
RefSeq (mRNA) NM_002133 NM_010442
RefSeq (protein) NP_002124 NP_034572
Location (UCSC) Chr 22:
35.78 – 35.79 Mb
Chr 8:
75.09 – 75.1 Mb
PubMed search [1] [2]

HMOX1 (heme oxygenase (decycling) 1) is a human gene that encodes for the enzyme heme oxygenase 1 (EC 1.14.99.3). Heme oxygenase is an essential enzyme in heme catabolism, it cleaves heme to form biliverdin.

Heme oxygenase, an essential enzyme in heme catabolism, cleaves heme to form biliverdin, which is subsequently converted to bilirubin by biliverdin reductase, and carbon monoxide, a putative neurotransmitter. Heme oxygenase activity is induced by its substrate heme and by various nonheme substances. Heme oxygenase occurs as 2 isozymes, an inducible heme oxygenase-1 and a constitutive heme oxygenase-2. HMOX1 and HMOX2 belong to the heme oxygenase family.[1]

The HMOX gene is located on the long (q) arm of chromosome 22 at position 12.3, from base pair 34,101,636 to base pair 34,114,748.

Related conditions[edit]

Heme oxygenase-1 deficiency

Anti-inflammatory effect[edit]

The ability of oxygenase 1 to catabolize free heme and produce carbon monoxide (CO) gives its antiinflammatory properties by up-regulation of IL-10 and IL-1R antagonist expression.[2]

See also[edit]

References[edit]

  1. ^ "Entrez Gene: HMOX1 heme oxygenase (decycling) 1". 
  2. ^ Piantadosi CA, Withers CM, Bartz RR, MacGarvey NC, Fu P, Sweeney TE, Welty-Wolf KE, Suliman HB (May 2011). "Heme oxygenase-1 couples activation of mitochondrial biogenesis to anti-inflammatory cytokine expression". J. Biol. Chem. 286 (18): 16374–85. doi:10.1074/jbc.M110.207738. PMC 3091243. PMID 21454555. 

Further reading[edit]