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Protein

Heme oxygenase 1

Gene

Hmox1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.14.99.3. 3474.
ReactomeiREACT_292451. Iron uptake and transport.
REACT_341594. 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 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:96163. Hmox1.

Subcellular locationi

GO - Cellular componenti

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.
GenevisibleiP14901. MM.

Interactioni

Protein-protein interaction databases

IntActiP14901. 3 interactions.
MINTiMINT-4097595.
STRINGi10090.ENSMUSP00000005548.

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.
CCDSiCCDS22423.1.
PIRiI48409.
RefSeqiNP_034572.1. NM_010442.2.
UniGeneiMm.276389.

3D structure databases

ProteinModelPortaliP14901.
SMRiP14901. Positions 30-225.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP14901. 3 interactions.
MINTiMINT-4097595.
STRINGi10090.ENSMUSP00000005548.

Chemistry

ChEMBLiCHEMBL4434.

PTM databases

PhosphoSiteiP14901.

Proteomic databases

MaxQBiP14901.
PaxDbiP14901.
PRIDEiP14901.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000005548; ENSMUSP00000005548; ENSMUSG00000005413.
GeneIDi15368.
KEGGimmu:15368.
UCSCiuc009mhc.2. mouse.

Organism-specific databases

CTDi3162.
MGIiMGI:96163. Hmox1.

Phylogenomic databases

eggNOGiCOG5398.
HOGENOMiHOG000233221.
HOVERGENiHBG005982.
InParanoidiP14901.
KOiK00510.
OMAiYAPLYFP.
OrthoDBiEOG7JQBNR.
PhylomeDBiP14901.
TreeFamiTF314786.

Enzyme and pathway databases

BRENDAi1.14.99.3. 3474.
ReactomeiREACT_292451. Iron uptake and transport.
REACT_341594. Heme degradation.

Miscellaneous databases

NextBioi287998.
PROiP14901.
SOURCEiSearch...

Gene expression databases

BgeeiP14901.
CleanExiMM_HMOX1.
ExpressionAtlasiP14901. baseline and differential.
GenevisibleiP14901. MM.

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]
ProtoNetiSearch...

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: June 24, 2015
This is version 132 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.