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P14901

- HMOX1_MOUSE

UniProt

P14901 - HMOX1_MOUSE

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Protein

Heme oxygenase 1

Gene

Hmox1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_205755. Iron uptake and transport.
REACT_233393. Heme degradation.

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 Source: UniProtKB-KW
  4. nucleolus Source: Ensembl
  5. nucleus Source: BHF-UCL
Complete GO annotation...

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

BgeeiP14901.
CleanExiMM_HMOX1.
ExpressionAtlasiP14901. baseline and differential.
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

        10         20         30         40         50
MERPQPDSMP QDLSEALKEA TKEVHIQAEN AEFMKNFQKG QVSREGFKLV
60 70 80 90 100
MASLYHIYTA LEEEIERNKQ NPVYAPLYFP EELHRRAALE QDMAFWYGPH
110 120 130 140 150
WQEIIPCTPA TQHYVKRLHE VGRTHPELLV AHAYTRYLGD LSGGQVLKKI
160 170 180 190 200
AQKAMALPSS GEGLAFFTFP NIDSPTKFKQ LYRARMNTLE MTPEVKHRVT
210 220 230 240 250
EEAKTAFLLN IELFEELQVM LTEEHKDQSP SQMASLRQRP ASLVQDTAPA
260 270 280
ETPRGKPQIS TSSSQTPLLQ WVLTLSFLLA TVAVGIYAM
Length:289
Mass (Da):32,929
Last modified:April 1, 1990 - v1
Checksum:i19DB0DCCD574044B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
REACT_233393. Heme degradation.

Miscellaneous databases

NextBioi 287998.
PROi P14901.
SOURCEi Search...

Gene expression databases

Bgeei P14901.
CleanExi MM_HMOX1.
ExpressionAtlasi P14901. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 125 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