Hmox2 heme oxygenase (decycling) 2 [Mus musculus (house mouse)] - Gene

Summary

Go to the top of the page Help

Official Symbol: Hmox2provided by MGI
Official Full Name: heme oxygenase (decycling) 2provided by MGI
Primary source: MGI:109373
See related: Ensembl:ENSMUSG00000004070; Vega:OTTMUSG00000026637
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: HO2; HO-2

Genomic context

Go to the top of the page Help

Location :: 16 B1; 16 2.46 cM

Sequence :: Chromosome: 16; NC_000082.6 (4726361..4766249)

See Hmox2 in Epigenomics, MapViewer

Chromosome 16 - NC_000082.6 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Genomic Sequence

Go to nucleotideGraphics FASTA GenBank

Go to reference sequence details

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions What's a GeneRIF?

PFKFB4 and HO-2 are expressed in a coordinated manner to maintain glucose homeostasis.
Title: Coordinated expression of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4 and heme oxygenase 2: evidence for a regulatory link between glycolysis and heme catabolism.
ells other than neutrophils contribute to the exaggerated inflammation and impaired wound healing seen in the HO-2 null cornea
Title: The role of neutrophils in corneal wound healing in HO-2 null mice.
deficiency in HO-2 alters both the kinetics of secondary damage and fine motor recovery after traumatic brain injuries.
Title: Heme oxygenase-2 modulates early pathogenesis after traumatic injury to the immature brain.
The the expression of HO-2 protein was increased in the sub-endocardial myocardium of ventricles under hypoxia, while HO-1 protein level was increased in the full-thickness walls.
Title: Hypoxemia induces expression of heme oxygenase-1 and heme oxygenase-2 proteins in the mouse myocardium.
Blood pressure and renal blood flow responses to increased ANG II or inhibition of nitric oxide are not significantly enhanced in HO-2 KO mice.
Title: Blood pressure and renal blow flow responses in heme oxygenase-2 knockout mice.
is demonstrated that neither deletion of HO-2 nor BK channels affect acute, sustained, and chronic vascular responses to alveolar hypoxia in the lung.
Title: Heme oxygenase-2 and large-conductance Ca2+-activated K+ channels: lung vascular effects of hypoxia.
The results provide additional evidence that HO2 plays a critical protective role against ICH-induced early brain injury.
Title: Heme oxygenase 2 deficiency increases brain swelling and inflammation after intracerebral hemorrhage.
Report the role of heme oxygenase-2 in pial arteriolar response to acetylcholine in mice with and without transfusion of cell-free hemoglobin polymers.
Title: Role of heme oxygenase-2 in pial arteriolar response to acetylcholine in mice with and without transfusion of cell-free hemoglobin polymers.
Suggest membrane potential gradient in small intestine is dependent on carbon monoxide generated by HO-2 in interstital cells of Cajal.
Title: Membrane potential gradient is carbon monoxide-dependent in mouse and human small intestine.
The data suggest that redox disregulation resulting from HO-2 deficiency affects maxi-K(+) channel gene expression but it does not alter the intrinsic O(2) sensitivity of carotid body or adrenal medulla cells.
Title: Acute oxygen sensing in heme oxygenase-2 null mice.

Submit: New GeneRIF Correction See all (27)

Alleles

Go to the top of the page Help

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Targeted (knock-out) (1) 1 citation

Pathways from BioSystems

Go to the top of the page Help

Heme degradation, organism-specific biosystem (from REACTOME)
Heme degradation, organism-specific biosystemcomputationally inferred pathway (not manually curated)
Iron uptake and transport, organism-specific biosystem (from REACTOME)
Iron uptake and transport, organism-specific biosystemcomputationally inferred pathway (not manually curated)
Metabolism, organism-specific biosystem (from REACTOME)
Metabolism, organism-specific biosystemcomputationally inferred pathway (not manually curated)
Metabolism of porphyrins, organism-specific biosystem (from REACTOME)
Metabolism of porphyrins, organism-specific biosystemcomputationally inferred pathway (not manually curated)
Mineral absorption, organism-specific biosystem (from KEGG)
Mineral absorption, organism-specific biosystemMinerals are one of the five fundamental groups of nutrients needed to sustain life. Of the minerals, calcium plays innumerable roles in our bodies, serving as a main component of bone as well as an ...
Mineral absorption, conserved biosystem (from KEGG)
Mineral absorption, conserved biosystemMinerals are one of the five fundamental groups of nutrients needed to sustain life. Of the minerals, calcium plays innumerable roles in our bodies, serving as a main component of bone as well as an ...
Porphyrin and chlorophyll metabolism, organism-specific biosystem (from KEGG)
Porphyrin and chlorophyll metabolism, organism-specific biosystem
Porphyrin and chlorophyll metabolism
Porphyrin and chlorophyll metabolism, conserved biosystem (from KEGG)
Porphyrin and chlorophyll metabolism, conserved biosystem
Porphyrin and chlorophyll metabolism
Transmembrane transport of small molecules, organism-specific biosystem (from REACTOME)
Transmembrane transport of small molecules, organism-specific biosystemcomputationally inferred pathway (not manually curated)
heme degradation, organism-specific biosystem (from BIOCYC)
heme degradation, organism-specific biosystem
heme degradation

General gene information

Go to the top of the page Help

Homology

Homologs of the Hmox2 gene: The Hmox2 gene is conserved in human, chimpanzee, Rhesus monkey, dog, cow, rat, chicken, and zebrafish.
Map Viewer (Human, Rat)

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
heme oxygenase (decyclizing) activity	ISO Inferred from Sequence Orthology more info
metal ion binding	IEA Inferred from Electronic Annotation more info
oxidoreductase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
heme oxidation	IEA Inferred from Electronic Annotation more info
oxidation-reduction process	ISO Inferred from Sequence Orthology more info
response to hypoxia	ISO Inferred from Sequence Orthology more info
response to oxidative stress	ISO Inferred from Sequence Orthology more info

Component	Evidence Code	Pubs
endoplasmic reticulum	IEA Inferred from Electronic Annotation more info
intracellular membrane-bounded organelle	IEA Inferred from Electronic Annotation more info
plasma membrane	ISO Inferred from Sequence Orthology more info

General protein information

Go to the top of the page Help

Preferred Names: heme oxygenase 2

Names: heme oxygenase 2

NP_001129538.1

EC 1.14.99.3

NP_034573.2

EC 1.14.99.3

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001136066.2 → NP_001129538.1 heme oxygenase 2

Status: VALIDATED

Description

Transcript Variant: This variant (1) represents the predominant transcript. Both variants 1 and 2 encode the same protein.

Source sequence(s)

AK134536, BP769523, BY071995

Consensus CDS

CCDS27924.1

UniProtKB/Swiss-Prot

O70252

UniProtKB/TrEMBL

Q544R7

Conserved Domains (1) summary

cd00232
Location:31 – 237
Blast Score: 544

HemeO; Heme oxygenase catalyzes the rate limiting step in the degradation of heme to bilirubin, it is essential for recycling of iron from heme. Heme is used as a substrate and cofactor for its own degradation to biliverdin, iron, and carbon monoxide. This ...
NM_010443.2 → NP_034573.2 heme oxygenase 2

Status: VALIDATED

Description

Transcript Variant: This variant (2) differs in the 5' UTR compared to transcript variant 1. Both variants 1 and 2 encode the same protein.

Source sequence(s)

AK134536, BP769523, CA465845

Consensus CDS

CCDS27924.1

UniProtKB/Swiss-Prot

O70252

UniProtKB/TrEMBL

Q544R7

Related

ENSMUSP00000112397, OTTMUSP00000032916, ENSMUST00000120232, OTTMUST00000065915

Conserved Domains (1) summary

cd00232
Location:31 – 237
Blast Score: 544

HemeO; Heme oxygenase catalyzes the rate limiting step in the degradation of heme to bilirubin, it is essential for recycling of iron from heme. Heme is used as a substrate and cofactor for its own degradation to biliverdin, iron, and carbon monoxide. This ...

RefSeqs of Annotated Genomes: Mus musculus Annotation Release 103

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCm38.p1 C57BL/6J

Genomic

NC_000082.6 Reference GRCm38.p1 C57BL/6J

Range

4726361..4766249

Download

GenBank, FASTA, Sequence Viewer (Graphics)

Alternate Mm_Celera

Genomic

AC_000038.1 Alternate Mm_Celera

Range

5357042..5398127

Download

GenBank, FASTA, Sequence Viewer (Graphics)

Nucleotide		Protein	Strain
Heading	Accession and Version	Protein	Strain
genomic	AAHY01125349.1	None
genomic	AAHY01125350.1	None
genomic	AAHY01125351.1	None
genomic	AAHY01125352.1	None
genomic	AAHY01125353.1	None
genomic	AAHY01125354.1	None
genomic	AAHY01125355.1	None
genomic	AC166903.2 (32412..57047)	None
genomic	CH466521.1	EDK97247.1	mixed
mRNA	AF029874.1	AAC17981.1	CD-1
mRNA	AF054669.1	AAC82363.1
mRNA	AF054670.1	AAC82364.1
mRNA	AK032175.1	BAC27744.1	C57BL/6J
mRNA	AK134536.1	BAE22174.1	C57BL/6J
mRNA	AK141426.1	BAE24682.1	C57BL/6J
mRNA	AK152936.1	BAE31610.1	C57BL/6J
mRNA	AK179622.1	None
mRNA	AK179824.1	None
mRNA	BC002011.1	AAH02011.1
mRNA	BC055742.1	None	C57BL/6
mRNA	BP769523.1	None	C57BL/6
mRNA	BY071995.1	None
mRNA	CA465845.1	None