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P09601

- HMOX1_HUMAN

UniProt

P09601 - HMOX1_HUMAN

Protein

Heme oxygenase 1

Gene

HMOX1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      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 – 181Heme
    Metal bindingi25 – 251Iron (heme axial ligand)
    Binding sitei134 – 1341Heme
    Binding sitei183 – 1831Heme

    GO - Molecular functioni

    1. enzyme binding Source: BHF-UCL
    2. heme binding Source: BHF-UCL
    3. heme oxygenase (decyclizing) activity Source: UniProtKB
    4. metal ion binding Source: UniProtKB-KW
    5. phospholipase D activity Source: Ensembl
    6. protein homodimerization activity Source: UniProtKB
    7. signal transducer activity Source: UniProtKB

    GO - Biological processi

    1. angiogenesis Source: BHF-UCL
    2. cell death Source: BHF-UCL
    3. cellular iron ion homeostasis Source: Reactome
    4. cellular response to arsenic-containing substance Source: Ensembl
    5. cellular response to cadmium ion Source: Ensembl
    6. cellular response to hypoxia Source: UniProtKB
    7. cellular response to nutrient Source: Ensembl
    8. endothelial cell proliferation Source: BHF-UCL
    9. erythrocyte homeostasis Source: BHF-UCL
    10. excretion Source: BHF-UCL
    11. heme catabolic process Source: BHF-UCL
    12. heme oxidation Source: BHF-UCL
    13. intracellular signal transduction Source: BHF-UCL
    14. intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl
    15. iron ion homeostasis Source: BHF-UCL
    16. low-density lipoprotein particle clearance Source: BHF-UCL
    17. negative regulation of DNA binding Source: Ensembl
    18. negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
    19. negative regulation of leukocyte migration Source: BHF-UCL
    20. negative regulation of mast cell cytokine production Source: Ensembl
    21. negative regulation of mast cell degranulation Source: Ensembl
    22. negative regulation of muscle cell apoptotic process Source: Ensembl
    23. negative regulation of neuron apoptotic process Source: Ensembl
    24. negative regulation of sequence-specific DNA binding transcription factor activity Source: Ensembl
    25. negative regulation of smooth muscle cell proliferation Source: UniProtKB
    26. porphyrin-containing compound metabolic process Source: Reactome
    27. positive regulation of angiogenesis Source: Ensembl
    28. positive regulation of chemokine biosynthetic process Source: BHF-UCL
    29. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    30. positive regulation of smooth muscle cell proliferation Source: UniProtKB
    31. positive regulation of vasodilation Source: BHF-UCL
    32. protein homooligomerization Source: UniProtKB
    33. regulation of angiogenesis Source: BHF-UCL
    34. regulation of blood pressure Source: Ensembl
    35. regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    36. regulation of transcription from RNA polymerase II promoter in response to oxidative stress Source: BHF-UCL
    37. response to estrogen Source: Ensembl
    38. response to hydrogen peroxide Source: BHF-UCL
    39. response to nicotine Source: BHF-UCL
    40. response to oxidative stress Source: BHF-UCL
    41. small GTPase mediated signal transduction Source: Ensembl
    42. small molecule metabolic process Source: Reactome
    43. smooth muscle hyperplasia Source: BHF-UCL
    44. transmembrane transport Source: Reactome
    45. wound healing involved in inflammatory response Source: BHF-UCL

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Apoptosis

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS02027-MONOMER.
    ReactomeiREACT_22297. Heme degradation.
    REACT_25060. Iron uptake and transport.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heme oxygenase 1 (EC:1.14.99.3)
    Short name:
    HO-1
    Gene namesi
    Name:HMOX1
    Synonyms:HO, HO1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:5013. HMOX1.

    Subcellular locationi

    Microsome 1 Publication. Endoplasmic reticulum membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication

    GO - Cellular componenti

    1. caveola Source: Ensembl
    2. cytosol Source: Ensembl
    3. endoplasmic reticulum Source: UniProtKB
    4. endoplasmic reticulum membrane Source: Reactome
    5. extracellular space Source: BHF-UCL
    6. membrane Source: ProtInc
    7. nucleolus Source: Ensembl
    8. nucleus Source: BHF-UCL

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome

    Pathology & Biotechi

    Involvement in diseasei

    Heme oxygenase 1 deficiency (HMOX1D) [MIM:614034]: A disease characterized by impaired stress hematopoiesis, resulting in marked erythrocyte fragmentation and intravascular hemolysis, coagulation abnormalities, endothelial damage, and iron deposition in renal and hepatic tissues. Clinical features include persistent hemolytic anemia, asplenia, nephritis, generalized erythematous rash, growth retardation and hepatomegaly.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi140 – 1401D → A: Inactive as a heme oxygenase but active as a peroxidase. 1 Publication

    Organism-specific databases

    MIMi614034. phenotype.
    PharmGKBiPA29341.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 288288Heme oxygenase 1PRO_0000209687Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei229 – 2291Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP09601.
    PaxDbiP09601.
    PRIDEiP09601.

    PTM databases

    PhosphoSiteiP09601.

    Expressioni

    Tissue specificityi

    Expressed at higher levels in renal cancer tissue than in normal tissue (at protein level).1 Publication

    Inductioni

    Heme oxygenase 1 activity is highly inducible by its substrate heme and by various non-heme substances such as heavy metals, bromobenzene, endotoxin, oxidizing agents and UVA.

    Gene expression databases

    ArrayExpressiP09601.
    BgeeiP09601.
    CleanExiHS_HMOX1.
    GenevestigatoriP09601.

    Organism-specific databases

    HPAiCAB017444.
    HPA000635.

    Interactioni

    Protein-protein interaction databases

    BioGridi109405. 11 interactions.
    IntActiP09601. 8 interactions.
    STRINGi9606.ENSP00000216117.

    Structurei

    Secondary structure

    1
    288
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi13 – 208
    Helixi22 – 309
    Helixi32 – 387
    Helixi44 – 6825
    Turni72 – 743
    Helixi75 – 773
    Helixi80 – 834
    Helixi86 – 9712
    Helixi101 – 1033
    Helixi109 – 12416
    Helixi126 – 1283
    Helixi129 – 15527
    Beta strandi159 – 1613
    Helixi165 – 1673
    Helixi175 – 18814
    Helixi193 – 22028

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1N3UX-ray2.58A/B1-233[»]
    1N45X-ray1.50A/B1-233[»]
    1NI6X-ray2.10A/B/C/D1-224[»]
    1OYKX-ray2.59A/B1-233[»]
    1OYLX-ray1.59A/B1-233[»]
    1OZEX-ray2.19A/B1-233[»]
    1OZLX-ray1.58A/B1-233[»]
    1OZRX-ray1.74A/B1-233[»]
    1OZWX-ray1.55A/B1-233[»]
    1S13X-ray2.29A/B1-233[»]
    1S8CX-ray2.19A/B/C/D1-233[»]
    1T5PX-ray2.11A/B1-233[»]
    1TWNX-ray2.20A/B1-233[»]
    1TWRX-ray2.10A/B1-233[»]
    1XJZX-ray1.88A/B1-233[»]
    1XK0X-ray2.18A/B1-233[»]
    1XK1X-ray2.08A/B1-233[»]
    1XK2X-ray2.20A/B1-233[»]
    1XK3X-ray2.08A/B1-233[»]
    3CZYX-ray1.54A/B1-233[»]
    3HOKX-ray2.19A/B1-233[»]
    3K4FX-ray2.17A/B1-233[»]
    3TGMX-ray2.85A/B1-233[»]
    ProteinModelPortaliP09601.
    SMRiP09601. Positions 10-223.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09601.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the heme oxygenase family.Curated

    Phylogenomic databases

    eggNOGiCOG5398.
    HOGENOMiHOG000233221.
    HOVERGENiHBG005982.
    InParanoidiP09601.
    KOiK00510.
    OMAiYAPLYFP.
    PhylomeDBiP09601.
    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.

    P09601-1 [UniParc]FASTAAdd to Basket

    « Hide

    MERPQPDSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV    50
    MASLYHIYVA LEEEIERNKE SPVFAPVYFP EELHRKAALE QDLAFWYGPR 100
    WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI 150
    AQKALDLPSS GEGLAFFTFP NIASATKFKQ LYRSRMNSLE MTPAVRQRVI 200
    EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKVQDSAPV 250
    ETPRGKPPLN TRSQAPLLRW VLTLSFLVAT VAVGLYAM 288
    Length:288
    Mass (Da):32,819
    Last modified:July 1, 1989 - v1
    Checksum:iAB47827778694064
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti7 – 71D → H.1 Publication
    Corresponds to variant rs2071747 [ dbSNP | Ensembl ].
    VAR_019165
    Natural varianti106 – 1061P → L.
    Corresponds to variant rs9282702 [ dbSNP | Ensembl ].
    VAR_022156

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06985 mRNA. Translation: CAA30045.1.
    CR456505 mRNA. Translation: CAG30391.1.
    AY460337 Genomic DNA. Translation: AAR23262.1.
    Z82244 Genomic DNA. Translation: CAB05109.1.
    M23041 mRNA. Translation: AAA50403.1.
    X14782 Genomic DNA. Translation: CAA32886.1.
    CCDSiCCDS13914.1.
    PIRiS00325.
    RefSeqiNP_002124.1. NM_002133.2.
    UniGeneiHs.517581.

    Genome annotation databases

    EnsembliENST00000216117; ENSP00000216117; ENSG00000100292.
    GeneIDi3162.
    KEGGihsa:3162.
    UCSCiuc003ant.2. human.

    Polymorphism databases

    DMDMi123446.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06985 mRNA. Translation: CAA30045.1 .
    CR456505 mRNA. Translation: CAG30391.1 .
    AY460337 Genomic DNA. Translation: AAR23262.1 .
    Z82244 Genomic DNA. Translation: CAB05109.1 .
    M23041 mRNA. Translation: AAA50403.1 .
    X14782 Genomic DNA. Translation: CAA32886.1 .
    CCDSi CCDS13914.1.
    PIRi S00325.
    RefSeqi NP_002124.1. NM_002133.2.
    UniGenei Hs.517581.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1N3U X-ray 2.58 A/B 1-233 [» ]
    1N45 X-ray 1.50 A/B 1-233 [» ]
    1NI6 X-ray 2.10 A/B/C/D 1-224 [» ]
    1OYK X-ray 2.59 A/B 1-233 [» ]
    1OYL X-ray 1.59 A/B 1-233 [» ]
    1OZE X-ray 2.19 A/B 1-233 [» ]
    1OZL X-ray 1.58 A/B 1-233 [» ]
    1OZR X-ray 1.74 A/B 1-233 [» ]
    1OZW X-ray 1.55 A/B 1-233 [» ]
    1S13 X-ray 2.29 A/B 1-233 [» ]
    1S8C X-ray 2.19 A/B/C/D 1-233 [» ]
    1T5P X-ray 2.11 A/B 1-233 [» ]
    1TWN X-ray 2.20 A/B 1-233 [» ]
    1TWR X-ray 2.10 A/B 1-233 [» ]
    1XJZ X-ray 1.88 A/B 1-233 [» ]
    1XK0 X-ray 2.18 A/B 1-233 [» ]
    1XK1 X-ray 2.08 A/B 1-233 [» ]
    1XK2 X-ray 2.20 A/B 1-233 [» ]
    1XK3 X-ray 2.08 A/B 1-233 [» ]
    3CZY X-ray 1.54 A/B 1-233 [» ]
    3HOK X-ray 2.19 A/B 1-233 [» ]
    3K4F X-ray 2.17 A/B 1-233 [» ]
    3TGM X-ray 2.85 A/B 1-233 [» ]
    ProteinModelPortali P09601.
    SMRi P09601. Positions 10-223.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109405. 11 interactions.
    IntActi P09601. 8 interactions.
    STRINGi 9606.ENSP00000216117.

    Chemistry

    BindingDBi P09601.
    ChEMBLi CHEMBL2823.
    DrugBanki DB00157. NADH.

    PTM databases

    PhosphoSitei P09601.

    Polymorphism databases

    DMDMi 123446.

    Proteomic databases

    MaxQBi P09601.
    PaxDbi P09601.
    PRIDEi P09601.

    Protocols and materials databases

    DNASUi 3162.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216117 ; ENSP00000216117 ; ENSG00000100292 .
    GeneIDi 3162.
    KEGGi hsa:3162.
    UCSCi uc003ant.2. human.

    Organism-specific databases

    CTDi 3162.
    GeneCardsi GC22P035776.
    HGNCi HGNC:5013. HMOX1.
    HPAi CAB017444.
    HPA000635.
    MIMi 141250. gene.
    614034. phenotype.
    neXtProti NX_P09601.
    PharmGKBi PA29341.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5398.
    HOGENOMi HOG000233221.
    HOVERGENi HBG005982.
    InParanoidi P09601.
    KOi K00510.
    OMAi YAPLYFP.
    PhylomeDBi P09601.
    TreeFami TF314786.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS02027-MONOMER.
    Reactomei REACT_22297. Heme degradation.
    REACT_25060. Iron uptake and transport.

    Miscellaneous databases

    EvolutionaryTracei P09601.
    GeneWikii HMOX1.
    GenomeRNAii 3162.
    NextBioi 12538.
    PROi P09601.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P09601.
    Bgeei P09601.
    CleanExi HS_HMOX1.
    Genevestigatori P09601.

    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. "Human heme oxygenase cDNA and induction of its mRNA by hemin."
      Yoshida T., Biro P., Cohen T., Mueller R.M., Shibahara S.
      Eur. J. Biochem. 171:457-461(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. SeattleSNPs variation discovery resource
      Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HIS-7.
    4. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite."
      Keyse S.M., Tyrrell R.M.
      Proc. Natl. Acad. Sci. U.S.A. 86:99-103(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-103.
      Tissue: Foreskin.
    6. "Structural organization of the human heme oxygenase gene and the function of its promoter."
      Shibahara S., Sato M., Muller R.M., Yoshida T.
      Eur. J. Biochem. 179:557-563(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
    7. "Oxidative stress causes enhanced endothelial cell injury in human heme oxygenase-1 deficiency."
      Yachie A., Niida Y., Wada T., Igarashi N., Kaneda H., Toma T., Ohta K., Kasahara Y., Koizumi S.
      J. Clin. Invest. 103:129-135(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN HMOX1D.
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: REVIEW ON ANTIAPOPTOTIC FUNCTION.
    10. "CXCR3-B can mediate growth-inhibitory signals in human renal cancer cells by down-regulating the expression of heme oxygenase-1."
      Datta D., Banerjee P., Gasser M., Waaga-Gasser A.M., Pal S.
      J. Biol. Chem. 285:36842-36848(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Endoplasmic reticulum anchored heme-oxygenase 1 faces the cytosol."
      Gottlieb Y., Truman M., Cohen L.A., Leichtmann-Bardoogo Y., Meyron-Holtz E.G.
      Haematologica 97:1489-1493(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    14. Cited for: X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS).
    15. "Crystal structures of the ferric, ferrous, and ferrous-NO forms of the Asp140Ala mutant of human heme oxygenase-1: catalytic implications."
      Lad L., Wang J., Li H., Friedman J., Bhaskar B., Ortiz de Montellano P.R., Poulos T.L.
      J. Mol. Biol. 330:527-538(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 1-233 OF MUTANT ALA-140, HEME-BINDING SITES, MUTAGENESIS OF ASP-140.

    Entry informationi

    Entry nameiHMOX1_HUMAN
    AccessioniPrimary (citable) accession number: P09601
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 158 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3