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    HMOX2 heme oxygenase 2 [ Homo sapiens (human) ]

    Gene ID: 3163, updated on 28-Jun-2015
    Official Symbol
    HMOX2provided by HGNC
    Official Full Name
    heme oxygenase 2provided by HGNC
    Primary source
    HGNC: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. Several alternatively spliced transcript variants encoding three different isoforms have been found for this gene. [provided by RefSeq, Oct 2013]
    Orthologs
    See HMOX2 in Epigenomics, MapViewer
    Location:
    16p13.3
    Exon count:
    12
    Annotation release Status Assembly Chr Location
    107 current GRCh38.p2 (GCF_000001405.28) 16 NC_000016.10 (4474703..4510347)
    105 previous assembly GRCh37.p13 (GCF_000001405.25) 16 NC_000016.9 (4524719..4560348)

    Chromosome 16 - NC_000016.10Genomic 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 cell death-inducing p53 target 1 Neighboring gene chromosome 16 open reading frame 96 Neighboring gene UBA-like domain containing 1

    GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

    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 Interaction Database

    • 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...
    Products Interactant Other Gene Complex Source Pubs Description

    Markers

    Homology

    Gene Ontology Provided by GOA

    Function Evidence Code Pubs
    heme oxygenase (decyclizing) activity IDA
    Inferred from Direct Assay
    more info
    PubMed 
    metal ion binding 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 
    small molecule metabolic process TAS
    Traceable Author Statement
    more info
     
    transmembrane transport TAS
    Traceable Author Statement
    more info
     
    Component Evidence Code Pubs
    endoplasmic reticulum membrane TAS
    Traceable Author Statement
    more info
     
    membrane IDA
    Inferred from Direct Assay
    more info
    PubMed 
    plasma membrane IDA
    Inferred from Direct Assay
    more info
    PubMed 
    Preferred Names
    heme oxygenase 2
    Names
    heme oxygenase 2
    heme oxygenase (decycling) 2
    NP_001120676.1
    NP_001120677.1
    NP_001120678.1
    NP_001273196.1
    NP_001273197.1
    NP_001273198.1
    NP_001273199.1
    NP_001273200.1
    NP_002125.3

    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_001127204.1NP_001120676.1  heme oxygenase 2 isoform b

      See identical proteins and their annotated locations for NP_001120676.1

      Status: REVIEWED

      Description
      Transcript Variant: This variant (1) differs in the 5' UTR and coding sequence compared to variant 5. The resulting isoform (b) is shorter at the N-terminus compared to isoform a. Variants 1, 2, 3, 4, 6, 7, and 8 all encode the same isoform (b).
      Source sequence(s)
      BC002396, D21243, DA141643, DA694137
      Consensus CDS
      CCDS10517.1
      UniProtKB/Swiss-Prot
      P30519
      Related
      ENSP00000394103, OTTHUMP00000257448, ENST00000458134, OTTHUMT00000438510
      Conserved Domains (1) summary
      cd00232
      Location:32238
      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_001127205.1NP_001120677.1  heme oxygenase 2 isoform b

      See identical proteins and their annotated locations for NP_001120677.1

      Status: REVIEWED

      Description
      Transcript Variant: This variant (2) differs in the 5' UTR and coding sequence compared to variant 5. The resulting isoform (b) is shorter at the N-terminus compared to isoform a. Variants 1, 2, 3, 4, 6, 7, and 8 all encode the same isoform (b).
      Source sequence(s)
      BC002396, BP368949, D21243
      Consensus CDS
      CCDS10517.1
      UniProtKB/Swiss-Prot
      P30519
      Related
      ENSP00000391637, ENST00000414777
      Conserved Domains (1) summary
      cd00232
      Location:32238
      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_001127206.2NP_001120678.1  heme oxygenase 2 isoform b

      See identical proteins and their annotated locations for NP_001120678.1

      Status: REVIEWED

      Description
      Transcript Variant: This variant (4) differs in the 5' UTR and coding sequence compared to variant 5. The resulting isoform (b) is shorter at the N-terminus compared to isoform a. Variants 1, 2, 3, 4, 6, 7, and 8 all encode the same isoform (b).
      Source sequence(s)
      BC002396, BE561721
      Consensus CDS
      CCDS10517.1
      UniProtKB/Swiss-Prot
      P30519
      Related
      ENSP00000385100, ENST00000406590
      Conserved Domains (1) summary
      cd00232
      Location:32238
      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_001286267.1NP_001273196.1  heme oxygenase 2 isoform a

      See identical proteins and their annotated locations for NP_001273196.1

      Status: REVIEWED

      Description
      Transcript Variant: This variant (5) encodes the longest isoform (a).
      Source sequence(s)
      BC002396, DA141643
      Consensus CDS
      CCDS73818.1
      UniProtKB/TrEMBL
      A0A087WT44
      UniProtKB/Swiss-Prot
      P30519
      Conserved Domains (1) summary
      cd00232
      Location:86292
      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 ...
    5. NM_001286268.1NP_001273197.1  heme oxygenase 2 isoform b

      See identical proteins and their annotated locations for NP_001273197.1

      Status: REVIEWED

      Description
      Transcript Variant: This variant (6) differs in the 5' UTR and coding sequence compared to variant 5. The resulting isoform (b) is shorter at the N-terminus compared to isoform a. Variants 1, 2, 3, 4, 6, 7, and 8 all encode the same isoform (b).
      Source sequence(s)
      BC002396, DA141643, DB184091
      Consensus CDS
      CCDS10517.1
      UniProtKB/Swiss-Prot
      P30519
      Related
      ENSP00000484467, ENST00000619913
      Conserved Domains (1) summary
      cd00232
      Location:32238
      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 ...
    6. NM_001286269.1NP_001273198.1  heme oxygenase 2 isoform b

      See identical proteins and their annotated locations for NP_001273198.1

      Status: REVIEWED

      Description
      Transcript Variant: This variant (7) differs in the 5' UTR and coding sequence compared to variant 5. The resulting isoform (b) is shorter at the N-terminus compared to isoform a. Variants 1, 2, 3, 4, 6, 7, and 8 all encode the same isoform (b).
      Source sequence(s)
      BC002396, BP329113, DA141643
      Consensus CDS
      CCDS10517.1
      UniProtKB/Swiss-Prot
      P30519
      Related
      ENSP00000484423, ENST00000619528
      Conserved Domains (1) summary
      cd00232
      Location:32238
      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 ...
    7. NM_001286270.1NP_001273199.1  heme oxygenase 2 isoform b

      See identical proteins and their annotated locations for NP_001273199.1

      Status: REVIEWED

      Description
      Transcript Variant: This variant (8) differs in the 5' UTR and coding sequence compared to variant 5. The resulting isoform (b) is shorter at the N-terminus compared to isoform a. Variants 1, 2, 3, 4, 6, 7, and 8 all encode the same isoform (b).
      Source sequence(s)
      AK093388, BC002396, BP369861
      Consensus CDS
      CCDS10517.1
      UniProtKB/TrEMBL
      B3KSE0
      UniProtKB/Swiss-Prot
      P30519
      Conserved Domains (1) summary
      cd00232
      Location:32238
      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 ...
    8. NM_001286271.1NP_001273200.1  heme oxygenase 2 isoform c

      Status: REVIEWED

      Description
      Transcript Variant: This variant (9) differs in the 5' UTR and coding sequence compared to variant 5. The resulting isoform (c) is shorter at the N-terminus compared to isoform a.
      Source sequence(s)
      BC002396, BM905872, DA141643
      Consensus CDS
      CCDS66931.1
      UniProtKB/Swiss-Prot
      P30519
      Conserved Domains (1) summary
      cd00232
      Location:3209
      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 ...
    9. NM_002134.3NP_002125.3  heme oxygenase 2 isoform b

      See identical proteins and their annotated locations for NP_002125.3

      Status: REVIEWED

      Description
      Transcript Variant: This variant (3) differs in the 5' UTR and coding sequence compared to variant 5. The resulting isoform (b) is shorter at the N-terminus compared to isoform a. Variants 1, 2, 3, 4, 6, 7, and 8 all encode the same isoform (b).
      Source sequence(s)
      BC002396, DA141643
      Consensus CDS
      CCDS10517.1
      UniProtKB/Swiss-Prot
      P30519
      Related
      ENSP00000459214, OTTHUMP00000159847, ENST00000570646, OTTHUMT00000251636
      Conserved Domains (1) summary
      cd00232
      Location:32238
      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: Homo sapiens Annotation Release 107

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

    Reference GRCh38.p2 Primary Assembly

    Genomic

    1. NC_000016.10 Reference GRCh38.p2 Primary Assembly

      Range
      4474703..4510347
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_011522473.1XP_011520775.1  

      See identical proteins and their annotated locations for XP_011520775.1

      Related
      ENSP00000477572, ENST00000613539
      Conserved Domains (1) summary
      cd00232
      Location:86292
      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 ...

    Reference GRCh38.p2 ALT_REF_LOCI_1

    Genomic

    1. NT_187608.1 Reference GRCh38.p2 ALT_REF_LOCI_1

      Range
      177026..212670
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_011546746.1XP_011545048.1  

      See identical proteins and their annotated locations for XP_011545048.1

      Conserved Domains (1) summary
      cd00232
      Location:86292
      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 ...

    Alternate CHM1_1.1

    Genomic

    1. NC_018927.2 Alternate CHM1_1.1

      Range
      4524642..4560277
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)