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P14901 (HMOX1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heme oxygenase 1

Short name=HO-1
EC=1.14.99.3
Alternative name(s):
P32 protein
Gene names
Name:Hmox1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length289 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Subcellular location

Microsome. Endoplasmic reticulum membrane By similarity; Peripheral membrane protein; Cytoplasmic side.

Induction

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 (Ref.5), or dependent on NO (Ref.4). Ref.4 Ref.5

Sequence similarities

Belongs to the heme oxygenase family.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentEndoplasmic reticulum
Membrane
Microsome
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from electronic annotation. Source: Ensembl

cellular response to arsenic-containing substance

Inferred from direct assay PubMed 12220541. Source: MGI

cellular response to cadmium ion

Inferred from direct assay PubMed 16183037. Source: MGI

cellular response to hypoxia

Inferred from electronic annotation. Source: Ensembl

cellular response to nutrient

Inferred from electronic annotation. Source: Ensembl

erythrocyte homeostasis

Inferred from electronic annotation. Source: Ensembl

heme catabolic process

Inferred from electronic annotation. Source: Ensembl

heme metabolic process

Inferred from direct assay PubMed 16183037. Source: MGI

heme oxidation

Inferred from electronic annotation. Source: InterPro

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from electronic annotation. Source: Ensembl

iron ion homeostasis

Inferred from electronic annotation. Source: Ensembl

negative regulation of DNA binding

Inferred from electronic annotation. Source: Ensembl

negative regulation of extrinsic apoptotic signaling pathway via death domain receptors

Inferred from electronic annotation. Source: Ensembl

negative regulation of mast cell cytokine production

Inferred from electronic annotation. Source: Ensembl

negative regulation of mast cell degranulation

Inferred from electronic annotation. Source: Ensembl

negative regulation of muscle cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of angiogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

protein homooligomerization

Inferred from electronic annotation. Source: Ensembl

regulation of blood pressure

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter in response to iron

Inferred from direct assay PubMed 23395172. Source: MGI

regulation of transcription from RNA polymerase II promoter in response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

response to estrogen

Inferred from electronic annotation. Source: Ensembl

response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

response to nicotine

Inferred from electronic annotation. Source: Ensembl

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: Ensembl

wound healing involved in inflammatory response

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcaveola

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 17430897. Source: BHF-UCL

   Molecular_functionheme binding

Inferred from electronic annotation. Source: Ensembl

heme oxygenase (decyclizing) activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phospholipase D activity

Inferred from electronic annotation. Source: Ensembl

signal transducer activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 289289Heme oxygenase 1
PRO_0000209688

Sites

Metal binding251Iron (heme axial ligand) By similarity
Binding site181Heme By similarity
Binding site1341Heme By similarity
Binding site1831Heme By similarity

Amino acid modifications

Modified residue2291Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
P14901 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 19DB0DCCD574044B

FASTA28932,929
        10         20         30         40         50         60 
MERPQPDSMP QDLSEALKEA TKEVHIQAEN AEFMKNFQKG QVSREGFKLV MASLYHIYTA 

        70         80         90        100        110        120 
LEEEIERNKQ NPVYAPLYFP EELHRRAALE QDMAFWYGPH WQEIIPCTPA TQHYVKRLHE 

       130        140        150        160        170        180 
VGRTHPELLV AHAYTRYLGD LSGGQVLKKI AQKAMALPSS GEGLAFFTFP NIDSPTKFKQ 

       190        200        210        220        230        240 
LYRARMNTLE MTPEVKHRVT EEAKTAFLLN IELFEELQVM LTEEHKDQSP SQMASLRQRP 

       250        260        270        280 
ASLVQDTAPA ETPRGKPQIS TSSSQTPLLQ WVLTLSFLLA TVAVGIYAM 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M33203 mRNA. Translation: AAA39872.1.
X13356 mRNA. Translation: CAA31732.1.
X56824 expand/collapse EMBL AC list , X56825, X56826, X56827 Genomic DNA. Translation: CAA40159.1.
BC010757 mRNA. Translation: AAH10757.1.
CCDSCCDS22423.1.
PIRI48409.
RefSeqNP_034572.1. NM_010442.2.
UniGeneMm.276389.

3D structure databases

ProteinModelPortalP14901.
SMRP14901. Positions 30-225.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP14901. 3 interactions.
MINTMINT-4097595.

Chemistry

ChEMBLCHEMBL4434.

PTM databases

PhosphoSiteP14901.

Proteomic databases

MaxQBP14901.
PaxDbP14901.
PRIDEP14901.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000005548; ENSMUSP00000005548; ENSMUSG00000005413.
GeneID15368.
KEGGmmu:15368.
UCSCuc009mhc.2. mouse.

Organism-specific databases

CTD3162.
MGIMGI:96163. Hmox1.

Phylogenomic databases

eggNOGCOG5398.
HOGENOMHOG000233221.
HOVERGENHBG005982.
InParanoidP14901.
KOK00510.
OMAYAPLYFP.
OrthoDBEOG7JQBNR.
PhylomeDBP14901.
TreeFamTF314786.

Gene expression databases

ArrayExpressP14901.
BgeeP14901.
CleanExMM_HMOX1.
GenevestigatorP14901.

Family and domain databases

Gene3D1.20.910.10. 1 hit.
InterProIPR002051. Haem_Oase.
IPR016053. Haem_Oase-like.
IPR016084. Haem_Oase-like_multi-hlx.
IPR018207. Haem_oxygenase_CS.
[Graphical view]
PANTHERPTHR10720. PTHR10720. 1 hit.
PfamPF01126. Heme_oxygenase. 1 hit.
[Graphical view]
PIRSFPIRSF000343. Haem_Oase. 1 hit.
PRINTSPR00088. HAEMOXYGNASE.
SUPFAMSSF48613. SSF48613. 1 hit.
PROSITEPS00593. HEME_OXYGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio287998.
PROP14901.
SOURCESearch...

Entry information

Entry nameHMOX1_MOUSE
AccessionPrimary (citable) accession number: P14901
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: July 9, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot