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HMOX1

From Wikipedia, the free encyclopedia
Mammalian protein found in Homo sapiens
HMOX1
Available structures
PDBOrtholog search:PDBeRCSB
List of PDB id codes

1N3U,1N45,1NI6,1OYK,1OYL,1OZE,1OZL,1OZR,1OZW,1S13,1S8C,1T5P,1TWN,1TWR,1XJZ,1XK0,1XK1,1XK2,1XK3,3CZY,3HOK,3K4F,3TGM,4WD4,5BTQ

Identifiers
AliasesHMOX1, HMOX1D, HO-1, HSP32, bK286B10, heme oxygenase 1
External IDsOMIM:141250;MGI:96163;HomoloGene:31075;GeneCards:HMOX1;OMA:HMOX1 - orthologs
Gene location (Human)
Chromosome 22 (human)
Chr.Chromosome 22 (human)[1]
Chromosome 22 (human)
Genomic location for HMOX1
Genomic location for HMOX1
Band22q12.3Start35,380,361bp[1]
End35,394,214bp[1]
Gene location (Mouse)
Chromosome 8 (mouse)
Chr.Chromosome 8 (mouse)[2]
Chromosome 8 (mouse)
Genomic location for HMOX1
Genomic location for HMOX1
Band8 35.59 cM|8 C1Start75,820,249bp[2]
End75,827,217bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • cartilage tissue

  • spleen

  • monocyte

  • granulocyte

  • islet of Langerhans

  • left ovary

  • mucosa of transverse colon

  • skin of leg

  • gallbladder

  • right ovary
Top expressed in
  • stroma of bone marrow

  • spleen

  • tibiofemoral joint

  • lens

  • granulocyte

  • lip

  • esophagus

  • placenta

  • calvaria

  • yolk sac
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo /QuickGO
Orthologs
SpeciesHumanMouse
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: 35.38 – 35.39 MbChr 8: 75.82 – 75.83 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

HMOX1 (heme oxygenase 1 gene) is ahumangene that encodes for the enzymeheme oxygenase 1 (EC1.14.99.3). Heme oxygenase (abbreviated HMOX or HO) mediates the first step ofheme catabolism, it cleavesheme to formbiliverdin.

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

Related conditions

[edit]

Heme oxygenase

[edit]
Main article:Heme oxygenase

Heme oxygenase, an essential enzyme in heme catabolism, cleaves heme to form biliverdin,carbon monoxide, andferrousiron.[5] The biliverdin is subsequently converted to bilirubin by biliverdin reductase. 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.[6]

See also

[edit]

References

[edit]
  1. ^abcGRCh38: Ensembl release 89: ENSG00000100292Ensembl, May 2017
  2. ^abcGRCm38: Ensembl release 89: ENSMUSG00000005413Ensembl, May 2017
  3. ^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^Lehninger's Principles of Biochemistry, 5th Edition. New York: W.H. Freeman and Company. 2008. pp. 876.ISBN 978-0-7167-7108-1.
  6. ^"Entrez Gene: HMOX1 heme oxygenase (decycling) 1".

Further reading

[edit]

External links

[edit]


PDB gallery
  • 1n3u: Crystal structure of human heme oxygenase 1 (HO-1) in complex with its substrate heme, crystal form B
    1n3u: Crystal structure of human heme oxygenase 1 (HO-1) in complex with its substrate heme, crystal form B
  • 1n45: X-RAY CRYSTAL STRUCTURE OF HUMAN HEME OXYGENASE-1 (HO-1) IN COMPLEX WITH ITS SUBSTRATE HEME
    1n45: X-RAY CRYSTAL STRUCTURE OF HUMAN HEME OXYGENASE-1 (HO-1) IN COMPLEX WITH ITS SUBSTRATE HEME
  • 1ni6: Comparisons of the Heme-Free and-Bound Crystal Structures of Human Heme Oxygenase-1
    1ni6: Comparisons of the Heme-Free and-Bound Crystal Structures of Human Heme Oxygenase-1
  • 1oyk: Crystal Structures of the Ferric, Ferrous, and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications
    1oyk: Crystal Structures of the Ferric, Ferrous, and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications
  • 1oyl: Crystal Structures of the Ferric, Ferrous, and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications
    1oyl: Crystal Structures of the Ferric, Ferrous, and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications
  • 1oze: Crystal Structures of the Ferric, Ferrous, and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1:Catalytic Implications
    1oze: Crystal Structures of the Ferric, Ferrous, and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1:Catalytic Implications
  • 1ozl: Crystal Structures of the Ferric, Ferrous, and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications
    1ozl: Crystal Structures of the Ferric, Ferrous, and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications
  • 1ozr: Crystal Structures of the Ferric, Ferrous and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications
    1ozr: Crystal Structures of the Ferric, Ferrous and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications
  • 1ozw: Crystal Structures of the Ferric, Ferrous and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications
    1ozw: Crystal Structures of the Ferric, Ferrous and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications
  • 1s13: Human Heme Oxygenase Oxidatition of alpha- and gamma-meso-Phenylhemes
    1s13: Human Heme Oxygenase Oxidatition of alpha- and gamma-meso-Phenylhemes
  • 1s8c: Crystal structure of human heme oxygenase in a complex with biliverdine
    1s8c: Crystal structure of human heme oxygenase in a complex with biliverdine
  • 1t5p: Human Heme Oxygenase Oxidation of alpha- and gamma-meso-phenylhemes
    1t5p: Human Heme Oxygenase Oxidation of alpha- and gamma-meso-phenylhemes
  • 1twn: Crystal structures of ferrous and ferrous-NO forms of verdoheme in a complex with human heme oxygenase-1: catalytic implications for heme cleavage
    1twn: Crystal structures of ferrous and ferrous-NO forms of verdoheme in a complex with human heme oxygenase-1: catalytic implications for heme cleavage
  • 1twr: Crystal structures of ferrous and ferrous-NO forms of verdoheme in a complex with human heme oxygenase-1: catalytic implications for heme cleavage
    1twr: Crystal structures of ferrous and ferrous-NO forms of verdoheme in a complex with human heme oxygenase-1: catalytic implications for heme cleavage
  • 1xjz: Crystal Structures of the G139A, G139A-NO and G143H Mutants of Human Heme Oxygenase-1
    1xjz: Crystal Structures of the G139A, G139A-NO and G143H Mutants of Human Heme Oxygenase-1
  • 1xk0: Crystal Structures of the G139A, G139A-NO and G143H Mutants of Human Heme Oxygenase-1
    1xk0: Crystal Structures of the G139A, G139A-NO and G143H Mutants of Human Heme Oxygenase-1
  • 1xk1: Crystal Structures of the G139A, G139A-NO and G143H Mutants of Human Heme Oxygenase-1
    1xk1: Crystal Structures of the G139A, G139A-NO and G143H Mutants of Human Heme Oxygenase-1
  • 1xk2: NADPH- and Ascorbate-Supported Heme Oxygenase Reactions are Distinct. Regiospecificity of Heme Cleavage by the R183E Mutant
    1xk2: NADPH- and Ascorbate-Supported Heme Oxygenase Reactions are Distinct. Regiospecificity of Heme Cleavage by the R183E Mutant
  • 1xk3: NADPH- and Ascorbate-Supported Heme Oxygenase Reactions are Distinct. Regiospecificity of Heme Cleavage by the R183E Mutant
    1xk3: NADPH- and Ascorbate-Supported Heme Oxygenase Reactions are Distinct. Regiospecificity of Heme Cleavage by the R183E Mutant
1.14.11:2-oxoglutarate
1.14.13:NADH orNADPH
1.14.14: reducedflavin orflavoprotein
1.14.15: reducediron–sulfur protein
1.14.16: reducedpteridine (BH4 dependent)
1.14.17: reducedascorbate
1.14.18-19: other
1.14.99 - miscellaneous
Activity
Regulation
Classification
Kinetics
Types
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