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Q5E9F2

- HMOX1_BOVIN

UniProt

Q5E9F2 - HMOX1_BOVIN

Protein

Heme oxygenase 1

Gene

HMOX1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (15 Mar 2005)
      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 By similarity.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei19 – 191HemeBy similarity
    Metal bindingi26 – 261Iron (heme axial ligand)By similarity
    Binding sitei135 – 1351HemeBy similarity
    Binding sitei184 – 1841HemeBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. cellular response to arsenic-containing substance Source: Ensembl
    3. cellular response to cadmium ion Source: Ensembl
    4. cellular response to hypoxia Source: Ensembl
    5. erythrocyte homeostasis Source: Ensembl
    6. heme oxidation Source: InterPro
    7. iron ion homeostasis Source: Ensembl
    8. negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
    9. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
    10. positive regulation of smooth muscle cell proliferation Source: Ensembl
    11. protein homooligomerization Source: Ensembl
    12. response to nicotine Source: Ensembl
    13. response to oxidative stress Source: Ensembl
    14. 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_204342. Iron uptake and transport.
    REACT_208785. Heme degradation.
    SABIO-RKQ5E9F2.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heme oxygenase 1 (EC:1.14.99.3)
    Short name:
    HO-1
    Gene namesi
    Name:HMOX1
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 5

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. nucleus Source: Ensembl

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 289289Heme oxygenase 1PRO_0000209686Add
    BLAST

    Proteomic databases

    PRIDEiQ5E9F2.

    Interactioni

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000020701.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5E9F2.
    SMRiQ5E9F2. Positions 1-224.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the heme oxygenase family.Curated

    Phylogenomic databases

    eggNOGiCOG5398.
    GeneTreeiENSGT00390000017673.
    HOGENOMiHOG000233221.
    HOVERGENiHBG005982.
    InParanoidiQ5E9F2.
    KOiK00510.
    OMAiYAPLYFP.
    OrthoDBiEOG7JQBNR.
    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.

    Q5E9F2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MERPQPDSSM PQDLSEALKE ATKEVHTQAE NAEFMKNFQK GELTQEGFKL    50
    VMASLYHIYV ALEEEIERNK ENPVYTPLYF PEELHRRASL EQDMAFWYGP 100
    RWQEAIPYTQ ATKRYVQRLQ EVGRTEPELL VAHAYTRYLG DLSGGQVLKK 150
    IAQKALNLPS SGEGLAFFTF PNIASATKFK QLYRSRMNTL EMTPEVRQRV 200
    LDEAKTAFLL NIQLFEELQG LLTQKAKDHD PLQAPELHRR AGSKVQDLAP 250
    TKASRGKPQP SVLSQAPLLR WVLTLSFLVA TVAVGLYAM 289
    Length:289
    Mass (Da):32,940
    Last modified:March 15, 2005 - v1
    Checksum:i8EAEA06BCCA4B96C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti28 – 281Q → E AA sequence (PubMed:1700666)Curated
    Sequence conflicti100 – 1001P → PH AA sequence (PubMed:1700666)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BT020968 mRNA. Translation: AAX08985.1.
    BC102105 mRNA. Translation: AAI02106.4.
    PIRiS13265.
    RefSeqiNP_001014912.1. NM_001014912.1.
    UniGeneiBt.4001.

    Genome annotation databases

    EnsembliENSBTAT00000020701; ENSBTAP00000020701; ENSBTAG00000015582.
    GeneIDi513221.
    KEGGibta:513221.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BT020968 mRNA. Translation: AAX08985.1 .
    BC102105 mRNA. Translation: AAI02106.4 .
    PIRi S13265.
    RefSeqi NP_001014912.1. NM_001014912.1.
    UniGenei Bt.4001.

    3D structure databases

    ProteinModelPortali Q5E9F2.
    SMRi Q5E9F2. Positions 1-224.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000020701.

    Chemistry

    ChEMBLi CHEMBL1255146.

    Proteomic databases

    PRIDEi Q5E9F2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000020701 ; ENSBTAP00000020701 ; ENSBTAG00000015582 .
    GeneIDi 513221.
    KEGGi bta:513221.

    Organism-specific databases

    CTDi 3162.

    Phylogenomic databases

    eggNOGi COG5398.
    GeneTreei ENSGT00390000017673.
    HOGENOMi HOG000233221.
    HOVERGENi HBG005982.
    InParanoidi Q5E9F2.
    KOi K00510.
    OMAi YAPLYFP.
    OrthoDBi EOG7JQBNR.
    TreeFami TF314786.

    Enzyme and pathway databases

    Reactomei REACT_204342. Iron uptake and transport.
    REACT_208785. Heme degradation.
    SABIO-RK Q5E9F2.

    Miscellaneous databases

    NextBioi 20870758.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    2. NIH - Mammalian Gene Collection (MGC) project
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Crossbred X Angus.
      Tissue: Ileum.
    3. "Structural studies on bovine spleen heme oxygenase. Immunological and structural diversity among mammalian heme oxygenase enzymes."
      Schacter B.A., Cripps V., Troxler R.F., Offner G.D.
      Arch. Biochem. Biophys. 282:404-412(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 24-33; 41-49; 88-113; 138-147; 155-158; 187-196 AND 200-205.
      Tissue: Spleen.

    Entry informationi

    Entry nameiHMOX1_BOVIN
    AccessioniPrimary (citable) accession number: Q5E9F2
    Secondary accession number(s): Q3ZCK7, Q7M338
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: March 15, 2005
    Last modified: October 1, 2014
    This is version 69 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, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3