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    HMOX2 heme oxygenase (decycling) 2 [ Homo sapiens ]

    Gene ID: 3163, updated on 19-May-2012
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    Summary

    Official Symbol
    HMOX2provided by HGNC
    Official Full Name
    heme oxygenase (decycling) 2provided by HGNC
    Primary source
    HGNC:5014
    See related
    Ensembl:ENSG00000103415; HPRD:00783; MIM:141251; Vega:OTTHUMG00000129473
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Homo sapiens
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
    Also known as
    HO-2
    Summary
    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. Alternative splice variants encoding the same protein have been identified at this locus. [provided by RefSeq, Jul 2008]
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    Genomic context

    Location :
    16p13.3
    Sequence :
    Chromosome: 16; NC_000016.9 (4524719..4560348)
    See HMOX2 in Epigenomics, MapViewer

    Chromosome 16 - NC_000016.9Genomic Context describing neighboring genes Neighboring gene CORO7-PAM16 readthrough Neighboring gene coronin 7 Neighboring gene vasorin Neighboring gene DnaJ (Hsp40) homolog, subfamily A, member 3 Neighboring gene NmrA-like family domain containing 1 Neighboring gene chromosome 16 open reading frame 5 Neighboring gene chromosome 16 open reading frame 96

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    Genomic regions, transcripts, and products

    Go to nucleotideGraphics FASTA GenBank

    Go to reference sequence details
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    Bibliography

    Related articles in PubMed

    1. A directed protein interaction network for investigating intracellular signal transduction. Vinayagam A, et al. Sci Signal, 2011 Sep 6. PMID 21900206.
    2. A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles. Wagner SA, et al. Mol Cell Proteomics, 2011 Oct. PMID 21890473.
    3. Lack of association between the c.544G>A polymorphism of the heme oxygenase-2 gene and age-related macular degeneration. Wysokinski D, et al. Med Sci Monit, 2011 Aug. PMID 21804464.
    4. Heme-oxygenases during erythropoiesis in K562 and human bone marrow cells. Alves LR, et al. PLoS One, 2011. PMID 21765894.
    5. A polymorphism located at an ATG transcription start site of the heme oxygenase-2 gene is associated with classical Parkinson's disease. Ayuso P, et al. Pharmacogenet Genomics, 2011 Sep. PMID 21709601.

    See all (51) citations in PubMed

    GeneRIFs: Gene References Into Functions What's a GeneRIF?

    1. for the first time, copy number variations in the HMOX2 gene and an association of the SNP rs2270363 with Parkinson's disease risk.
      Title: A polymorphism located at an ATG transcription start site of the heme oxygenase-2 gene is associated with classical Parkinson's disease.
    2. Results suggest that the c.544G>A polymorphism of the heme oxygenase-2 gene is not associated with age-related macular degeneration in this population.
      Title: Lack of association between the c.544G>A polymorphism of the heme oxygenase-2 gene and age-related macular degeneration.
    3. Erythroid precursors were characterized by lack of significant expression of HO-1 and by progressive reduction of HO-2 during differentiation.
      Title: Heme-oxygenases during erythropoiesis in K562 and human bone marrow cells.
    4. HO-2, which is highly expressed in the corneal epithelium, appears to be critical for the wound healing process in the cornea.
      Title: Knockdown of heme oxygenase-2 impairs corneal epithelial cell wound healing.
    5. These findings are consistent with the presence of a hydrogen-bonding network at the heme's distal side within the active site of HO-2 with potentially significant differences from that observed in HO-1.
      Title: Spectroscopic insights into axial ligation and active-site H-bonding in substrate-bound human heme oxygenase-2.
    6. There was positive correlation between seminal plasma HO enzyme activity and sperm concentration, per cent of motile spermatozoa, number of motile spermatozoas ml(-1) and significant negative correlation with per cent of sperm abnormal forms.
      Title: Heme oxygenase enzyme activity in seminal plasma of oligoasthenoteratozoospermic males with varicocele.
    7. high expression in keratinocytes prevents basal and radiation-induced gene expression of heme oxygenase 1
      Title: A role for Bach1 and HO-2 in suppression of basal and UVA-induced HO-1 expression in human keratinocytes.
    8. HO-2 is important in maintaining endothelial viability and may preserve local regulation of vascular tone, thrombosis, and inflammatory responses during reductions in systemic oxygen delivery
      Title: Enhanced translation of heme oxygenase-2 preserves human endothelial cell viability during hypoxia.
    9. The thiol/disulfide switch in HO-2 responds to cellular oxidative stress and reductive conditions, representing a paradigm for how heme regulatory motifs can integrate heme homeostasis with carbon monoxide signaling and redox regulation.
      Title: Heme regulatory motifs in heme oxygenase-2 form a thiol/disulfide redox switch that responds to the cellular redox state.
    10. Enhanced oxidative stress and a decrease in the number of anti-oxidant enzymes may be associated with pre-eclampsia.
      Title: Cellular mRNA expressions of anti-oxidant factors in the blood of preeclamptic women.
    Submit: New GeneRIF Correction See all (24)
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    Phenotypes

    Review eQTL and phenotype association data in this region using PheGenI

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    HIV-1 protein interactions

    Protein Gene Interaction Pubs
    Envelope surface glycoprotein gp120 env Genes, including GABRP, ADF, HINT, PRSS2, SDCBP, PTK9, PPP2R5B, ITGA3, PRKCBP1, HMOX2, HAT1, PPP1cB, and ICAM-1, are upregulated after treatment of human astrocytes with HIV-1 gp120 PubMed

    Go to the HIV-1, Human Protein Interaction Database

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    Interactions

    Products Interactant Other Gene Complex Source Pubs Description
    NP_002125.3 NP_002238.2 KCNMA1    BIND  PubMed KCNMA1 interacts with HO-2. 
    P30519 P05067 APP    HPRD  PubMed  
    P30519 Q7L5N1 COPS6    HPRD  PubMed  
    P30519 P68400 CSNK2A1    HPRD  PubMed  
    P30519 P26641 EEF1G    HPRD  PubMed  
    P30519 Q9Y2X7 GIT1    HPRD  PubMed  
    P30519 Q5JY77 GPRASP1    HPRD  PubMed  
    P30519 P54257 HAP1    HPRD  PubMed  
    P30519 Q12791 KCNMA1    HPRD  PubMed  
    P30519 Q9P2H0 KIAA1377    HPRD  PubMed  
    P30519 Q5T3J3 LRIF1    HPRD  PubMed  
    P30519 Q9Y3C7 MED31    HPRD  PubMed  
    P30519 Q15047 SETDB1    HPRD  PubMed  
    BioGRID:109406 BioGRID:106524 A2M    BioGRID  PubMed Two-hybrid 
    BioGRID:109406 BioGRID:106994 ATP5B    BioGRID  PubMed Two-hybrid 
    BioGRID:109406 BioGRID:129431 BLOC1S2    BioGRID  PubMed Two-hybrid 
    BioGRID:109406 BioGRID:115455 CEBPZ    BioGRID  PubMed Two-hybrid 
    BioGRID:109406 BioGRID:116176 COPS6    BioGRID  PubMed Two-hybrid 
    BioGRID:109406 BioGRID:108257 EEF1G    BioGRID  PubMed Two-hybrid 
    BioGRID:109406 BioGRID:114212 EIF3C    BioGRID  PubMed Two-hybrid 
    BioGRID:109406 BioGRID:118789 GIT1    BioGRID  PubMed Two-hybrid 
    BioGRID:109406 BioGRID:115086 GPRASP1    BioGRID  PubMed Two-hybrid 
    BioGRID:109406 BioGRID:114480 HAP1    BioGRID  PubMed Two-hybrid 
    BioGRID:109406 BioGRID:116185 IMMT    BioGRID  PubMed Two-hybrid 
    BioGRID:109406 BioGRID:119720 INPP5K    BioGRID  PubMed Two-hybrid 
    BioGRID:109406 BioGRID:123507 ITFG1    BioGRID  PubMed Two-hybrid 
    BioGRID:109406 BioGRID:121617 KIAA1377    BioGRID  PubMed Two-hybrid 
    BioGRID:109406 BioGRID:120905 LRIF1    BioGRID  PubMed Two-hybrid 
    BioGRID:109406 BioGRID:119211 MED31    BioGRID  PubMed Two-hybrid 
    BioGRID:109406 BioGRID:110800 NDUFS2    BioGRID  PubMed Two-hybrid 
    BioGRID:109406 BioGRID:121002 NKRF    BioGRID  PubMed Two-hybrid 
    BioGRID:109406 BioGRID:109165 NR3C1    BioGRID  PubMed Two-hybrid 
    BioGRID:109406 BioGRID:123029 PHF17    BioGRID  PubMed Two-hybrid 
    BioGRID:109406 BioGRID:117178 PLXNB2    BioGRID  PubMed Two-hybrid 
    BioGRID:109406 BioGRID:111863 RBBP4    BioGRID  PubMed Two-hybrid 
    BioGRID:109406 BioGRID:115202 SETDB1    BioGRID  PubMed Two-hybrid 
    BioGRID:109406 BioGRID:112361 SHC1    BioGRID  PubMed Two-hybrid 
    BioGRID:109406 BioGRID:118022 SNX5    BioGRID  PubMed Two-hybrid 
    BioGRID:109406 BioGRID:119508 SNX7    BioGRID  PubMed Two-hybrid 
    BioGRID:109406 BioGRID:113164 UBC    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:109406 BioGRID:116078 USP19    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:109406 BioGRID:126637 ZFP28    BioGRID  PubMed Two-hybrid 
    BioGRID:109406 BioGRID:127574 ZNF746    BioGRID  PubMed Two-hybrid 
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    General gene information

    Markers

    Genotypes

    Homology

    Pathways from BioSystems

    • Heme degradation, organism-specific biosystem (from REACTOME)
      Heme degradation, organism-specific biosystemMost of the heme degraded in humans comes from hemoglobin. Approximately 6-8 grams of hemoglobin is degraded daily which is equivalent to approximately 300 milligrams of heme per day. Heme is not rec...
    • Iron uptake and transport, organism-specific biosystem (from REACTOME)
      Iron uptake and transport, organism-specific biosystemThe transport of iron between cells is mediated by transferrin. However, iron can also enter and leave cells not only by itself, but also in the form of heme and siderophores. When entering the cell ...
    • Metabolism, organism-specific biosystem (from REACTOME)
      Metabolism, organism-specific biosystemMetabolic processes in human cells generate energy through the oxidation of molecules consumed in the diet and mediate the synthesis of diverse essential molecules not taken in the diet as well as th...
    • Metabolism of porphyrins, organism-specific biosystem (from REACTOME)
      Metabolism of porphyrins, organism-specific biosystemPorphyrins are heterocyclic macrocycles, consisting of four pyrrole subunits (tetrapyrrole) linked by four methine (=CH-) bridges. The extensive conjugated porphyrin macrocycle is chromatic and the n...
    • Mineral absorption, organism-specific biosystem (from KEGG)
      Mineral absorption, organism-specific biosystemMinerals are one of the five fundamental groups of nutrients needed to sustain life. Of the minerals, calcium plays innumerable roles in our bodies, serving as a main component of bone as well as an ...
    • Mineral absorption, conserved biosystem (from KEGG)
      Mineral absorption, conserved biosystemMinerals are one of the five fundamental groups of nutrients needed to sustain life. Of the minerals, calcium plays innumerable roles in our bodies, serving as a main component of bone as well as an ...
    • Porphyrin and chlorophyll metabolism, organism-specific biosystem (from KEGG)
      Porphyrin and chlorophyll metabolism, organism-specific biosystem
      Porphyrin and chlorophyll metabolism
    • Porphyrin and chlorophyll metabolism, conserved biosystem (from KEGG)
      Porphyrin and chlorophyll metabolism, conserved biosystem
      Porphyrin and chlorophyll metabolism
    • Transmembrane transport of small molecules, organism-specific biosystem (from REACTOME)
      Transmembrane transport of small molecules, organism-specific biosystem
      Transmembrane transport of small molecules
    • heme degradation, organism-specific biosystem (from BIOCYC)
      heme degradation, organism-specific biosystemThe heme degradation pathway in animals ensures the recycling of iron. The first enzyme in this pathway, : HS02027-MONOMER, catayzes the opening of the tetrapyrrole macrocycle of : PROTOHEME, forming...

    Gene Ontology Provided by GOA

    Function Evidence Code Pubs
    electron carrier activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    heme oxygenase (decyclizing) activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    oxidoreductase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    Process Evidence Code Pubs
    cellular iron ion homeostasis TAS
    Traceable Author Statement
    more info
    		  
    heme catabolic process TAS
    Traceable Author Statement
    more info
    		  
    heme oxidation IEA
    Inferred from Electronic Annotation
    more info
    		  
    porphyrin-containing compound metabolic process TAS
    Traceable Author Statement
    more info
    		  
    response to hypoxia IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    response to oxidative stress IEA
    Inferred from Electronic Annotation
    more info
    		  
    small molecule metabolic process TAS
    Traceable Author Statement
    more info
    		  
    transmembrane transport TAS
    Traceable Author Statement
    more info
    		  
    Component Evidence Code Pubs
    endoplasmic reticulum IEA
    Inferred from Electronic Annotation
    more info
    		  
    endoplasmic reticulum membrane TAS
    Traceable Author Statement
    more info
    		  
    microsome IEA
    Inferred from Electronic Annotation
    more info
    		  
    plasma membrane IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
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    General protein information

    Preferred Names
    heme oxygenase 2
    Names
    heme oxygenase 2
    NP_001120676.1
    NP_001120677.1
    NP_001120678.1
    NP_002125.3
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    NCBI Reference Sequences (RefSeq)

    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    mRNA and Protein(s)

    1. NM_001127204.1 → NP_001120676.1  heme oxygenase 2

      Status: REVIEWED

      Description
      Transcript Variant: This variant (1) represents the longest transcript. Variants 1, 2, 3 and 4 encode the same protein.
      Source sequence(s)
      BC002396, D21243, DA141643, DA694137
      Consensus CDS
      CCDS10517.1
      UniProtKB/Swiss-Prot
      P30519
      Related
      ENSP00000394103, ENST00000458134
      Conserved Domains (1) summary
      cd00232
      Location:32 – 238
      Blast Score: 551
      HemeO; Heme oxygenase catalyzes the rate limiting step in the degradation of heme to bilirubin, it is essential for recycling of iron from heme. Heme is used as a substrate and cofactor for its own degradation to biliverdin, iron, and carbon monoxide. This ...

    2. NM_001127205.1 → NP_001120677.1  heme oxygenase 2

      Status: REVIEWED

      Description
      Transcript Variant: This variant (2) differs in the 5' UTR compared to variant 1. Variants 1, 2, 3 and 4 encode the same protein.
      Source sequence(s)
      BC002396, BP368949, D21243
      Consensus CDS
      CCDS10517.1
      UniProtKB/Swiss-Prot
      P30519
      Related
      ENSP00000391637, ENST00000414777
      Conserved Domains (1) summary
      cd00232
      Location:32 – 238
      Blast Score: 551
      HemeO; Heme oxygenase catalyzes the rate limiting step in the degradation of heme to bilirubin, it is essential for recycling of iron from heme. Heme is used as a substrate and cofactor for its own degradation to biliverdin, iron, and carbon monoxide. This ...

    3. NM_001127206.1 → NP_001120678.1  heme oxygenase 2

      Status: REVIEWED

      Description
      Transcript Variant: This variant (4) differs in the 5' UTR compared to variant 1. Variants 1, 2, 3 and 4 encode the same protein.
      Source sequence(s)
      BC002396, BI225653, D21243
      Consensus CDS
      CCDS10517.1
      UniProtKB/Swiss-Prot
      P30519
      Related
      ENSP00000385100, ENST00000406590
      Conserved Domains (1) summary
      cd00232
      Location:32 – 238
      Blast Score: 551
      HemeO; Heme oxygenase catalyzes the rate limiting step in the degradation of heme to bilirubin, it is essential for recycling of iron from heme. Heme is used as a substrate and cofactor for its own degradation to biliverdin, iron, and carbon monoxide. This ...

    4. NM_002134.3 → NP_002125.3  heme oxygenase 2

      Status: REVIEWED

      Description
      Transcript Variant: This variant (3) differs in the 5' UTR compared to variant 1. Variants 1, 2, 3 and 4 encode the same protein.
      Source sequence(s)
      BC002396, DA141643
      Consensus CDS
      CCDS10517.1
      UniProtKB/Swiss-Prot
      P30519
      Related
      ENSP00000459214, ENST00000570646
      Conserved Domains (1) summary
      cd00232
      Location:32 – 238
      Blast Score: 551
      HemeO; Heme oxygenase catalyzes the rate limiting step in the degradation of heme to bilirubin, it is essential for recycling of iron from heme. Heme is used as a substrate and cofactor for its own degradation to biliverdin, iron, and carbon monoxide. This ...

    RefSeqs of Annotated Genomes: Build 37.3

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference GRCh37.p5 Primary Assembly

    Genomic

    1. NC_000016.9 Reference GRCh37.p5 Primary Assembly

      Range
      4524719..4560348
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    Alternate HuRef

    Genomic

    1. AC_000148.1 Alternate HuRef

      Range
      4492031..4527516
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)
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    Related Sequences

    Nucleotide Protein
    Heading Accession and Version
    genomic AC007606.8 (25008..58910) None
    genomic AY771350.1 AAV28730.1
    genomic CH471112.2 EAW85299.1
      EAW85300.1
    mRNA AF051306.1 AAC05297.1
    mRNA AK093388.1 BAG52702.1
    mRNA AK222629.1 BAD96349.1
    mRNA AK313660.1 None
    mRNA BC002396.2 AAH02396.1
    mRNA BI225653.1 None
    mRNA BP368949.1 None
    mRNA BT019788.1 AAV38591.1
    mRNA CR456760.1 CAG33041.1
    mRNA CR541839.1 CAG46638.1
    mRNA D21243.1 BAA04789.1
    mRNA DA141643.1 None
    mRNA DA694137.1 None
    mRNA S34389.1 AAB22110.2
    other-genetic EU831457.1 ACE87144.1
    other-genetic EU831544.1 ACE86463.1
    Protein Accession Links
    GenPept Link UniProtKB Link
    P30519.2 GenPept UniProtKB/Swiss-Prot:P30519
    Q53HF1 GenPept UniProtKB/TrEMBL:Q53HF1
    Q6FHB5 GenPept UniProtKB/TrEMBL:Q6FHB5
    Q6IBP2 GenPept UniProtKB/TrEMBL:Q6IBP2
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    Additional Links

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

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