Heme oxygenase 1

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityⁱ

• heme b

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  + 3 O₂

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  + 3 reduced [NADPH—hemoprotein reductase]

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.

  = biliverdin IXα

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  + CO

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  + Fe²⁺

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  + H⁺

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  + 3 H₂O

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  + 3 oxidized [NADPH—hemoprotein reductase]

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.

  By similarity

  <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toⁱ

  • UniProtKB:O48782 (HMOX1_ARATH)
  EC:1.14.14.18
  • Search proteins in UniProtKB for this EC number.
  • See the description of this EC number in ENZYME.
  By similarity

  Manual assertion inferred from sequence similarity toⁱ

  • UniProtKB:O48782 (HMOX1_ARATH)
  Source: Rhea

  • Search for this reaction in UniProtKB.
  • See the description of this reaction in Rhea.

  . Show »« Hide
  heme b

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  zoom

  +

  3

  O₂

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  

  +

  3

  reduced [NADPH—hemoprotein reductase]

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.

  

  FMNH₂

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  =

  biliverdin IXα

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  zoom

  +

  CO

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  

  +

  Fe²⁺

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  zoom

  +

  H⁺

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  

  +

  3

  H₂O

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  

  +

  3

  oxidized [NADPH—hemoprotein reductase]

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.

  

  FMN

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• enzyme binding Source: BHF-UCL <p>Inferred from Sequence or Structural Similarity <br />Used for any analysis based on sequence alignment, structure comparison, or evaluation of sequence features such as composition.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iss">GO evidence code guide</a></p> Inferred from sequence or structural similarityⁱ
  • "Involvement of NADPH in the interaction between heme oxygenase-1 and cytochrome P450 reductase."
    Higashimoto Y., Sakamoto H., Hayashi S., Sugishima M., Fukuyama K., Palmer G., Noguchi M.
    J. Biol. Chem. 280:729-737(2005) [PubMed] [Europe PMC] [Abstract]
• heme binding Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Expression and characterization of full-length human heme oxygenase-1: the presence of intact membrane-binding region leads to increased binding affinity for NADPH cytochrome P450 reductase."
    Huber W.J., Backes W.L.
    Biochemistry 46:12212-12219(2007) [PubMed] [Europe PMC] [Abstract]
• heme oxygenase (decyclizing) activity Source: BHF-UCLInferred from direct assayⁱ
  • "Expression and characterization of full-length human heme oxygenase-1: the presence of intact membrane-binding region leads to increased binding affinity for NADPH cytochrome P450 reductase."
    Huber W.J., Backes W.L.
    Biochemistry 46:12212-12219(2007) [PubMed] [Europe PMC] [Abstract]
• metal ion binding Source: UniProtKB-KW
• phospholipase D activity Source: Ensembl
• protein homodimerization activity Source: UniProtKBInferred from direct assayⁱ
  • "Oligomerization is crucial for the stability and function of heme oxygenase-1 in the endoplasmic reticulum."
    Hwang H.W., Lee J.R., Chou K.Y., Suen C.S., Hwang M.J., Chen C., Shieh R.C., Chau L.Y.
    J. Biol. Chem. 284:22672-22679(2009) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• angiogenesis Source: BHF-UCL <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementⁱ
  • "Significance of heme oxygenase in prolactin-mediated cell proliferation and angiogenesis in human endothelial cells."
    Malaguarnera L., Pilastro M.R., Quan S., Ghattas M.H., Yang L., Mezentsev A.V., Kushida T., Abraham N.G., Kappas A.
    Int. J. Mol. Med. 10:433-440(2002) [PubMed] [Europe PMC] [Abstract]
• cell death Source: BHF-UCL
• cellular iron ion homeostasis Source: CACAO <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Haem oxygenase-1 overexpression alters intracellular iron distribution."
    Lanceta L., Li C., Choi A.M., Eaton J.W.
    Biochem. J. 449:189-194(2013) [PubMed] [Europe PMC] [Abstract]
• cellular response to arsenic-containing substance Source: Ensembl
• cellular response to cadmium ion Source: Ensembl
• cellular response to cisplatin Source: Ensembl
• cellular response to heat Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Transformation of eEF1Bdelta into heat-shock response transcription factor by alternative splicing."
    Kaitsuka T., Tomizawa K., Matsushita M.
    EMBO Rep. 12:673-681(2011) [PubMed] [Europe PMC] [Abstract]
• cellular response to hypoxia Source: UniProtKB <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ
  • "Bach1 functions as a hypoxia-inducible repressor for the heme oxygenase-1 gene in human cells."
    Kitamuro T., Takahashi K., Ogawa K., Udono-Fujimori R., Takeda K., Furuyama K., Nakayama M., Sun J., Fujita H., Hida W., Hattori T., Shirato K., Igarashi K., Shibahara S.
    J. Biol. Chem. 278:9125-9133(2003) [PubMed] [Europe PMC] [Abstract]
• cellular response to nutrient Source: Ensembl
• cytokine-mediated signaling pathway Source: Reactome
• endothelial cell proliferation Source: BHF-UCLTraceable author statementⁱ
  • "Significance of heme oxygenase in prolactin-mediated cell proliferation and angiogenesis in human endothelial cells."
    Malaguarnera L., Pilastro M.R., Quan S., Ghattas M.H., Yang L., Mezentsev A.V., Kushida T., Abraham N.G., Kappas A.
    Int. J. Mol. Med. 10:433-440(2002) [PubMed] [Europe PMC] [Abstract]
• erythrocyte homeostasis Source: BHF-UCLInferred from mutant phenotypeⁱ
  • Ref.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.
• excretion Source: BHF-UCL <p>Inferred by Curator</p> <p>Used for cases where an annotation is not supported by any evidence but can be reasonably inferred by a curator from other GO annotations for which evidence <br />is available.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ic">GO evidence code guide</a></p> Inferred by curatorⁱ
  • "Expression and characterization of full-length human heme oxygenase-1: the presence of intact membrane-binding region leads to increased binding affinity for NADPH cytochrome P450 reductase."
    Huber W.J., Backes W.L.
    Biochemistry 46:12212-12219(2007) [PubMed] [Europe PMC] [Abstract]
• heme catabolic process Source: BHF-UCLInferred from direct assayⁱ
  • "Expression and characterization of full-length human heme oxygenase-1: the presence of intact membrane-binding region leads to increased binding affinity for NADPH cytochrome P450 reductase."
    Huber W.J., Backes W.L.
    Biochemistry 46:12212-12219(2007) [PubMed] [Europe PMC] [Abstract]
• heme oxidation Source: BHF-UCLInferred from direct assayⁱ
  • "Expression and characterization of full-length human heme oxygenase-1: the presence of intact membrane-binding region leads to increased binding affinity for NADPH cytochrome P450 reductase."
    Huber W.J., Backes W.L.
    Biochemistry 46:12212-12219(2007) [PubMed] [Europe PMC] [Abstract]
• intracellular signal transduction Source: BHF-UCLTraceable author statementⁱ
  • "Heme oxygenase-1 modulates the expression of the anti-angiogenic chemokine CXCL-10 in renal tubular epithelial cells."
    Datta D., Dormond O., Basu A., Briscoe D.M., Pal S.
    Am. J. Physiol. Renal Physiol. 293:F1222-30(2007) [PubMed] [Europe PMC] [Abstract]
• intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl
• iron ion homeostasis Source: BHF-UCLInferred from direct assayⁱ
  • "Expression and characterization of full-length human heme oxygenase-1: the presence of intact membrane-binding region leads to increased binding affinity for NADPH cytochrome P450 reductase."
    Huber W.J., Backes W.L.
    Biochemistry 46:12212-12219(2007) [PubMed] [Europe PMC] [Abstract]
• liver regeneration Source: Ensembl
• low-density lipoprotein particle clearance Source: BHF-UCLTraceable author statementⁱ
  • Ref.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.
• negative regulation of DNA binding Source: Ensembl
• negative regulation of DNA-binding transcription factor activity Source: Ensembl
• negative regulation of epithelial cell apoptotic process Source: Ensembl
• negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "HO-1 underlies resistance of AML cells to TNF-induced apoptosis."
    Rushworth S.A., MacEwan D.J.
    Blood 111:3793-3801(2008) [PubMed] [Europe PMC] [Abstract]
• negative regulation of leukocyte migration Source: BHF-UCLTraceable author statementⁱ
  • "Bifunctional role for VEGF-induced heme oxygenase-1 in vivo: induction of angiogenesis and inhibition of leukocytic infiltration."
    Bussolati B., Ahmed A., Pemberton H., Landis R.C., Di Carlo F., Haskard D.O., Mason J.C.
    Blood 103:761-766(2004) [PubMed] [Europe PMC] [Abstract]
• negative regulation of macroautophagy Source: Ensembl
• negative regulation of mast cell cytokine production Source: Ensembl
• negative regulation of mast cell degranulation Source: Ensembl
• negative regulation of muscle cell apoptotic process Source: Ensembl
• negative regulation of neuron apoptotic process Source: Ensembl
• negative regulation of smooth muscle cell proliferation Source: UniProtKBInferred from direct assayⁱ
  • "BMP4 induces HO-1 via a Smad-independent, p38MAPK-dependent pathway in pulmonary artery myocytes."
    Yang X., Lee P.J., Long L., Trembath R.C., Morrell N.W.
    Am. J. Respir. Cell Mol. Biol. 37:598-605(2007) [PubMed] [Europe PMC] [Abstract]
• negative regulation of vascular smooth muscle cell proliferation Source: Ensembl
• positive regulation of angiogenesis Source: BHF-UCLInferred from direct assayⁱ
  • "MicroRNA-24 regulates vascularity after myocardial infarction."
    Fiedler J., Jazbutyte V., Kirchmaier B.C., Gupta S.K., Lorenzen J., Hartmann D., Galuppo P., Kneitz S., Pena J.T., Sohn-Lee C., Loyer X., Soutschek J., Brand T., Tuschl T., Heineke J., Martin U., Schulte-Merker S., Ertl G.

    , Engelhardt S., Bauersachs J., Thum T.
    Circulation 124:720-730(2011) [PubMed] [Europe PMC] [Abstract]
• positive regulation of apoptotic process Source: Ensembl
• positive regulation of blood vessel diameter Source: BHF-UCLInferred by curatorⁱ
  • "Expression and characterization of full-length human heme oxygenase-1: the presence of intact membrane-binding region leads to increased binding affinity for NADPH cytochrome P450 reductase."
    Huber W.J., Backes W.L.
    Biochemistry 46:12212-12219(2007) [PubMed] [Europe PMC] [Abstract]
• positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis Source: BHF-UCL <p>Inferred from Genetic Interaction</p> <p>Used to describe “traditional” genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactionⁱ
  • "Hypoxia-responsive microRNA-101 promotes angiogenesis via heme oxygenase-1/vascular endothelial growth factor axis by targeting cullin 3."
    Kim J.H., Lee K.S., Lee D.K., Kim J., Kwak S.N., Ha K.S., Choe J., Won M.H., Cho B.R., Jeoung D., Lee H., Kwon Y.G., Kim Y.M.
    Antioxid. Redox Signal. 21:2469-2482(2014) [PubMed] [Europe PMC] [Abstract]
• positive regulation of cell migration involved in sprouting angiogenesis Source: BHF-UCLInferred from genetic interactionⁱ
  • "Hypoxia-responsive microRNA-101 promotes angiogenesis via heme oxygenase-1/vascular endothelial growth factor axis by targeting cullin 3."
    Kim J.H., Lee K.S., Lee D.K., Kim J., Kwak S.N., Ha K.S., Choe J., Won M.H., Cho B.R., Jeoung D., Lee H., Kwon Y.G., Kim Y.M.
    Antioxid. Redox Signal. 21:2469-2482(2014) [PubMed] [Europe PMC] [Abstract]
• positive regulation of chemokine biosynthetic process Source: BHF-UCLTraceable author statementⁱ
  • "Heme oxygenase-1 modulates the expression of the anti-angiogenic chemokine CXCL-10 in renal tubular epithelial cells."
    Datta D., Dormond O., Basu A., Briscoe D.M., Pal S.
    Am. J. Physiol. Renal Physiol. 293:F1222-30(2007) [PubMed] [Europe PMC] [Abstract]
• positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKBInferred from high throughput mutant phenotypeⁱ
  • "Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways."
    Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.
    Oncogene 22:3307-3318(2003) [PubMed] [Europe PMC] [Abstract]
• positive regulation of macroautophagy Source: Ensembl
• positive regulation of smooth muscle cell proliferation Source: UniProtKBInferred from direct assayⁱ
  • "BMP4 induces HO-1 via a Smad-independent, p38MAPK-dependent pathway in pulmonary artery myocytes."
    Yang X., Lee P.J., Long L., Trembath R.C., Morrell N.W.
    Am. J. Respir. Cell Mol. Biol. 37:598-605(2007) [PubMed] [Europe PMC] [Abstract]
• protein homooligomerization Source: UniProtKBInferred from direct assayⁱ
  • "Oligomerization is crucial for the stability and function of heme oxygenase-1 in the endoplasmic reticulum."
    Hwang H.W., Lee J.R., Chou K.Y., Suen C.S., Hwang M.J., Chen C., Shieh R.C., Chau L.Y.
    J. Biol. Chem. 284:22672-22679(2009) [PubMed] [Europe PMC] [Abstract]
• regulation of angiogenesis Source: BHF-UCLTraceable author statementⁱ
  • "Heme oxygenase-1 modulates the expression of the anti-angiogenic chemokine CXCL-10 in renal tubular epithelial cells."
    Datta D., Dormond O., Basu A., Briscoe D.M., Pal S.
    Am. J. Physiol. Renal Physiol. 293:F1222-30(2007) [PubMed] [Europe PMC] [Abstract]
• regulation of blood pressure Source: Ensembl
• regulation of DNA-binding transcription factor activity Source: BHF-UCL
• regulation of transcription from RNA polymerase II promoter in response to iron Source: Ensembl
• regulation of transcription from RNA polymerase II promoter in response to oxidative stress Source: BHF-UCL
• response to estrogen Source: Ensembl
• response to hydrogen peroxide Source: BHF-UCL
• response to nicotine Source: BHF-UCLInferred from direct assayⁱ
  • "Differential induction of heme oxygenase-1 against nicotine-induced cytotoxicity via the PI3K, MAPK, and NF-kappa B pathways in immortalized and malignant human oral keratinocytes."
    Lee H.J., Lee J., Min S.K., Guo H.Y., Lee S.K., Kim H.R., Pae H.O., Chung H.T., Hong S.H., Lee S.K., Kim E.C.
    J. Oral Pathol. Med. 37:278-286(2008) [PubMed] [Europe PMC] [Abstract]
• response to oxidative stress Source: BHF-UCLInferred from mutant phenotypeⁱ
  • Ref.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.
• small GTPase mediated signal transduction Source: Ensembl
• smooth muscle hyperplasia Source: BHF-UCLTraceable author statementⁱ
  • "The role of heme oxygenase-1 in T cell-mediated immunity: the all encompassing enzyme."
    Xia Z.W., Zhong W.W., Meyrowitz J.S., Zhang Z.L.
    Curr. Pharm. Des. 14:454-464(2008) [PubMed] [Europe PMC] [Abstract]
• wound healing involved in inflammatory response Source: BHF-UCLInferred from mutant phenotypeⁱ
  • Ref.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.

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseaseⁱ

Mutagenesis

Organism-specific databases

Miscellaneous databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductionⁱ

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• enzyme binding Source: BHF-UCLInferred from sequence or structural similarityⁱ
  • "Involvement of NADPH in the interaction between heme oxygenase-1 and cytochrome P450 reductase."
    Higashimoto Y., Sakamoto H., Hayashi S., Sugishima M., Fukuyama K., Palmer G., Noguchi M.
    J. Biol. Chem. 280:729-737(2005) [PubMed] [Europe PMC] [Abstract]
• protein homodimerization activity Source: UniProtKBInferred from direct assayⁱ
  • "Oligomerization is crucial for the stability and function of heme oxygenase-1 in the endoplasmic reticulum."
    Hwang H.W., Lee J.R., Chou K.Y., Suen C.S., Hwang M.J., Chen C., Shieh R.C., Chau L.Y.
    J. Biol. Chem. 284:22672-22679(2009) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

        10         20         30         40         50
MERPQPDSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV 
        60         70         80         90        100
MASLYHIYVA LEEEIERNKE SPVFAPVYFP EELHRKAALE QDLAFWYGPR 
       110        120        130        140        150
WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI 
       160        170        180        190        200
AQKALDLPSS GEGLAFFTFP NIASATKFKQ LYRSRMNSLE MTPAVRQRVI 
       210        220        230        240        250
EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKVQDSAPV 
       260        270        280 
ETPRGKPPLN TRSQAPLLRW VLTLSFLVAT VAVGLYAM              

Natural variant

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityⁱ

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
2. SIMILARITY comments
   Index of protein domains and families
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. Human chromosome 22
   Human chromosome 22: entries, gene names and cross-references to MIM
6. Human entries with polymorphisms or disease mutations
   List of human entries with polymorphisms or disease mutations