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P14901

- HMOX1_MOUSE

UniProt

P14901 - HMOX1_MOUSE

Protein

Heme oxygenase 1

Gene

Hmox1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    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. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis.

    Catalytic activityi

    Protoheme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei18 – 181HemeBy similarity
    Metal bindingi25 – 251Iron (heme axial ligand)By similarity
    Binding sitei134 – 1341HemeBy similarity
    Binding sitei183 – 1831HemeBy similarity

    GO - Molecular functioni

    1. heme binding Source: Ensembl
    2. heme oxygenase (decyclizing) activity Source: UniProtKB-EC
    3. metal ion binding Source: UniProtKB-KW
    4. phospholipase D activity Source: Ensembl
    5. signal transducer activity Source: Ensembl

    GO - Biological processi

    1. angiogenesis Source: Ensembl
    2. cellular response to arsenic-containing substance Source: MGI
    3. cellular response to cadmium ion Source: MGI
    4. cellular response to hypoxia Source: Ensembl
    5. cellular response to nutrient Source: Ensembl
    6. erythrocyte homeostasis Source: Ensembl
    7. heme catabolic process Source: Ensembl
    8. heme metabolic process Source: MGI
    9. heme oxidation Source: InterPro
    10. intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl
    11. iron ion homeostasis Source: Ensembl
    12. negative regulation of DNA binding Source: Ensembl
    13. negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
    14. negative regulation of mast cell cytokine production Source: Ensembl
    15. negative regulation of mast cell degranulation Source: Ensembl
    16. negative regulation of muscle cell apoptotic process Source: Ensembl
    17. negative regulation of neuron apoptotic process Source: Ensembl
    18. negative regulation of sequence-specific DNA binding transcription factor activity Source: Ensembl
    19. negative regulation of smooth muscle cell proliferation Source: Ensembl
    20. positive regulation of angiogenesis Source: Ensembl
    21. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
    22. positive regulation of smooth muscle cell proliferation Source: Ensembl
    23. protein homooligomerization Source: Ensembl
    24. regulation of blood pressure Source: Ensembl
    25. regulation of transcription from RNA polymerase II promoter in response to iron Source: MGI
    26. regulation of transcription from RNA polymerase II promoter in response to oxidative stress Source: Ensembl
    27. response to estrogen Source: Ensembl
    28. response to hydrogen peroxide Source: Ensembl
    29. response to nicotine Source: Ensembl
    30. small GTPase mediated signal transduction Source: Ensembl
    31. wound healing involved in inflammatory response Source: Ensembl

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Apoptosis

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_205755. Iron uptake and transport.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heme oxygenase 1 (EC:1.14.99.3)
    Short name:
    HO-1
    Alternative name(s):
    P32 protein
    Gene namesi
    Name:Hmox1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:96163. Hmox1.

    Subcellular locationi

    GO - Cellular componenti

    1. caveola Source: Ensembl
    2. cytosol Source: Ensembl
    3. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    4. nucleolus Source: Ensembl
    5. nucleus Source: BHF-UCL

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 289289Heme oxygenase 1PRO_0000209688Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei229 – 2291PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP14901.
    PaxDbiP14901.
    PRIDEiP14901.

    PTM databases

    PhosphoSiteiP14901.

    Expressioni

    Inductioni

    Heme oxygenase 1 activity is highly inducible by its substrate heme and by various non-heme substances such as heavy metals, bromobenzene, and endotoxin. It is also induced in macrophages, liver and the lungs upon infection with M.tuberculosis (at protein level). Data is conflicting as to whether macrophage induction is independent of the nitric oxide (NO) signaling pathway (PubMed:18400743), or dependent on NO (PubMed:18474359).2 Publications

    Gene expression databases

    ArrayExpressiP14901.
    BgeeiP14901.
    CleanExiMM_HMOX1.
    GenevestigatoriP14901.

    Interactioni

    Protein-protein interaction databases

    IntActiP14901. 3 interactions.
    MINTiMINT-4097595.

    Structurei

    3D structure databases

    ProteinModelPortaliP14901.
    SMRiP14901. Positions 30-225.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the heme oxygenase family.Curated

    Phylogenomic databases

    eggNOGiCOG5398.
    HOGENOMiHOG000233221.
    HOVERGENiHBG005982.
    InParanoidiP14901.
    KOiK00510.
    OMAiYAPLYFP.
    OrthoDBiEOG7JQBNR.
    PhylomeDBiP14901.
    TreeFamiTF314786.

    Family and domain databases

    Gene3Di1.20.910.10. 1 hit.
    InterProiIPR002051. Haem_Oase.
    IPR016053. Haem_Oase-like.
    IPR016084. Haem_Oase-like_multi-hlx.
    IPR018207. Haem_oxygenase_CS.
    [Graphical view]
    PANTHERiPTHR10720. PTHR10720. 1 hit.
    PfamiPF01126. Heme_oxygenase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000343. Haem_Oase. 1 hit.
    PRINTSiPR00088. HAEMOXYGNASE.
    SUPFAMiSSF48613. SSF48613. 1 hit.
    PROSITEiPS00593. HEME_OXYGENASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P14901-1 [UniParc]FASTAAdd to Basket

    « Hide

    MERPQPDSMP QDLSEALKEA TKEVHIQAEN AEFMKNFQKG QVSREGFKLV    50
    MASLYHIYTA LEEEIERNKQ NPVYAPLYFP EELHRRAALE QDMAFWYGPH 100
    WQEIIPCTPA TQHYVKRLHE VGRTHPELLV AHAYTRYLGD LSGGQVLKKI 150
    AQKAMALPSS GEGLAFFTFP NIDSPTKFKQ LYRARMNTLE MTPEVKHRVT 200
    EEAKTAFLLN IELFEELQVM LTEEHKDQSP SQMASLRQRP ASLVQDTAPA 250
    ETPRGKPQIS TSSSQTPLLQ WVLTLSFLLA TVAVGIYAM 289
    Length:289
    Mass (Da):32,929
    Last modified:April 1, 1990 - v1
    Checksum:i19DB0DCCD574044B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M33203 mRNA. Translation: AAA39872.1.
    X13356 mRNA. Translation: CAA31732.1.
    X56824
    , X56825, X56826, X56827 Genomic DNA. Translation: CAA40159.1.
    BC010757 mRNA. Translation: AAH10757.1.
    CCDSiCCDS22423.1.
    PIRiI48409.
    RefSeqiNP_034572.1. NM_010442.2.
    UniGeneiMm.276389.

    Genome annotation databases

    EnsembliENSMUST00000005548; ENSMUSP00000005548; ENSMUSG00000005413.
    GeneIDi15368.
    KEGGimmu:15368.
    UCSCiuc009mhc.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M33203 mRNA. Translation: AAA39872.1 .
    X13356 mRNA. Translation: CAA31732.1 .
    X56824
    , X56825 , X56826 , X56827 Genomic DNA. Translation: CAA40159.1 .
    BC010757 mRNA. Translation: AAH10757.1 .
    CCDSi CCDS22423.1.
    PIRi I48409.
    RefSeqi NP_034572.1. NM_010442.2.
    UniGenei Mm.276389.

    3D structure databases

    ProteinModelPortali P14901.
    SMRi P14901. Positions 30-225.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P14901. 3 interactions.
    MINTi MINT-4097595.

    Chemistry

    ChEMBLi CHEMBL4434.

    PTM databases

    PhosphoSitei P14901.

    Proteomic databases

    MaxQBi P14901.
    PaxDbi P14901.
    PRIDEi P14901.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000005548 ; ENSMUSP00000005548 ; ENSMUSG00000005413 .
    GeneIDi 15368.
    KEGGi mmu:15368.
    UCSCi uc009mhc.2. mouse.

    Organism-specific databases

    CTDi 3162.
    MGIi MGI:96163. Hmox1.

    Phylogenomic databases

    eggNOGi COG5398.
    HOGENOMi HOG000233221.
    HOVERGENi HBG005982.
    InParanoidi P14901.
    KOi K00510.
    OMAi YAPLYFP.
    OrthoDBi EOG7JQBNR.
    PhylomeDBi P14901.
    TreeFami TF314786.

    Enzyme and pathway databases

    Reactomei REACT_205755. Iron uptake and transport.

    Miscellaneous databases

    NextBioi 287998.
    PROi P14901.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P14901.
    Bgeei P14901.
    CleanExi MM_HMOX1.
    Genevestigatori P14901.

    Family and domain databases

    Gene3Di 1.20.910.10. 1 hit.
    InterProi IPR002051. Haem_Oase.
    IPR016053. Haem_Oase-like.
    IPR016084. Haem_Oase-like_multi-hlx.
    IPR018207. Haem_oxygenase_CS.
    [Graphical view ]
    PANTHERi PTHR10720. PTHR10720. 1 hit.
    Pfami PF01126. Heme_oxygenase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000343. Haem_Oase. 1 hit.
    PRINTSi PR00088. HAEMOXYGNASE.
    SUPFAMi SSF48613. SSF48613. 1 hit.
    PROSITEi PS00593. HEME_OXYGENASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of a complementary DNA clone for a Mr 32,000 protein which is induced with tumor promoters in BALB/c 3T3 cells."
      Kageyama H., Hiwasa T., Tokunaga K., Sakiyama S.
      Cancer Res. 48:4795-4798(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Fibroblast.
    2. "Isolation and characterization of the mouse heme oxygenase-1 gene. Distal 5' sequences are required for induction by heme or heavy metals."
      Alam J., Cai J., Smith A.
      J. Biol. Chem. 269:1001-1009(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Kidney.
    4. "Mycobacterium tuberculosis senses host-derived carbon monoxide during macrophage infection."
      Shiloh M.U., Manzanillo P., Cox J.S.
      Cell Host Microbe 3:323-330(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY M.TUBERCULOSIS.
    5. "Heme oxygenase-1-derived carbon monoxide induces the Mycobacterium tuberculosis dormancy regulon."
      Kumar A., Deshane J.S., Crossman D.K., Bolisetty S., Yan B.S., Kramnik I., Agarwal A., Steyn A.J.
      J. Biol. Chem. 283:18032-18039(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION IN MACROPHAGES AND LUNGS BY M.TUBERCULOSIS.
      Strain: C3Heb/FeJ and C57BL/6 X FVB.
      Tissue: Lung and Macrophage.

    Entry informationi

    Entry nameiHMOX1_MOUSE
    AccessioniPrimary (citable) accession number: P14901
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 123 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3