HMOX2

Protein-coding gene in the species Homo sapiens

HMOX2

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
2Q32, 2QPP, 2RGZ, 4WMH

Identifiers

Aliases

HMOX2, HO-2, heme oxygenase 2

External IDs

OMIM: 141251; MGI: 109373; HomoloGene: 1611; GeneCards: HMOX2; OMA:HMOX2 - orthologs

Gene location (Human)

Chr.	Chromosome 16 (human)^[1]

Band	16p13.3	Start	4,474,690 bp^[1]
Band	16p13.3	End	4,510,347 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 16 (mouse)^[2]

Band	16 A1\|16 2.46 cM	Start	4,544,225 bp^[2]
Band	16 A1\|16 2.46 cM	End	4,584,606 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

right testis

left testis

prefrontal cortex

left ventricle

apex of heart

superior frontal gyrus

Brodmann area 9

right auricle

nucleus accumbens

body of stomach

Top expressed in

spermatid

seminiferous tubule

facial motor nucleus

anterior horn of spinal cord

dentate gyrus of hippocampal formation granule cell

supraoptic nucleus

stroma of bone marrow

endothelial cell of lymphatic vessel

external carotid artery

internal carotid artery

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	oxidoreductase activity protein binding metal ion binding heme oxygenase (decyclizing) activity heme binding
Cellular component	intracellular membrane-bounded organelle endoplasmic reticulum membrane membrane endoplasmic reticulum plasma membrane specific granule membrane
Biological process	response to hypoxia cellular iron ion homeostasis heme oxidation response to oxidative stress heme catabolic process neutrophil degranulation iron ion homeostasis
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


3163


15369

Ensembl


ENSG00000277424 ENSG00000103415


ENSMUSG00000004070

UniProt


P30519


O70252

RefSeq (mRNA)

NM_001127204 NM_001127205 NM_001127206 NM_001286267 NM_001286268
NM_001286269 NM_001286270 NM_001286271 NM_002134


NM_001136066 NM_010443 NM_001357050 NM_001378999

RefSeq (protein)

NP_001120676 NP_001120677 NP_001120678 NP_001273196 NP_001273197
NP_001273198 NP_001273199 NP_001273200 NP_002125


NP_001129538 NP_034573 NP_001343979 NP_001365928

Location (UCSC)

Chr 16: 4.47 – 4.51 Mb

Chr 16: 4.54 – 4.58 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Heme oxygenase 2 is an enzyme that in humans is encoded by the HMOX2 gene.^[5]^[6]

Function

Heme oxygenase, an essential enzyme in heme catabolism, cleaves heme to form biliverdin, which is subsequently converted to bilirubin by biliverdin reductase, and carbon monoxide, a putative neurotransmitter. Heme oxygenase activity is induced by its substrate heme and by various nonheme substances. Heme oxygenase occurs as 2 isozymes, an inducible heme oxygenase-1 and a constitutive heme oxygenase-2. HMOX1 and HMOX2 (this enzyme) belong to the heme oxygenase family.^[6]

References

^ ^a ^b ^c ENSG00000103415 GRCh38: Ensembl release 89: ENSG00000277424, ENSG00000103415 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000004070 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ McCoubrey WK, Ewing JF, Maines MD (Jun 1992). "Human heme oxygenase-2: characterization and expression of a full-length cDNA and evidence suggesting that the two HO-2 transcripts may differ by choice of polyadenylation signal". Arch Biochem Biophys. 295 (1): 13–20. doi:10.1016/0003-9861(92)90481-B. PMID 1575508.
^ ^a ^b "Entrez Gene: HMOX2 heme oxygenase (decycling) 2".

Bianchetti CM, Yi L, Ragsdale SW, Phillips GN (2007). "Comparison of Apo- and Heme-bound Crystal Structures of a Truncated Human Heme Oxygenase-2". J Biol Chem. 282 (52): 37624–31. doi:10.1074/jbc.M707396200. PMC 2896506. PMID 17965015.
Wang J, Zhuang H, Doré S (2006). "Heme oxygenase 2 is neuroprotective against intracerebral hemorrhage". Neurobiol. Dis. 22 (3): 473–6. doi:10.1016/j.nbd.2005.12.009. PMID 16459095. S2CID 43195015.
Wang J, Doré S (2008). "Heme oxygenase 2 deficiency increases brain swelling and inflammation after intracerebral hemorrhage". Neuroscience. 155 (4): 1133–41. doi:10.1016/j.neuroscience.2008.07.004. PMC 4696610. PMID 18674596.
Barañano DE, Snyder SH (2001). "Neural roles for heme oxygenase: Contrasts to nitric oxide synthase". Proc. Natl. Acad. Sci. U.S.A. 98 (20): 10996–1002. Bibcode:2001PNAS...9810996B. doi:10.1073/pnas.191351298. PMC 58673. PMID 11572959.
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Kemp PJ (2005). "Hemeoxygenase-2 as an O2 sensor in K+ channel-dependent chemotransduction". Biochem. Biophys. Res. Commun. 338 (1): 648–52. doi:10.1016/j.bbrc.2005.08.110. PMID 16137652.
Ishikawa K, Takeuchi N, Takahashi S, Matera KM, Sato M, Shibahara S, Rousseau DL, Ikeda-Saito M, Yoshida T (1995). "Heme oxygenase-2. Properties of the heme complex of the purified tryptic fragment of recombinant human heme oxygenase-2". J. Biol. Chem. 270 (11): 6345–50. doi:10.1074/jbc.270.11.6345. PMID 7890772.
Kutty RK, Kutty G, Rodriguez IR, Chader GJ, Wiggert B (1994). "Chromosomal localization of the human heme oxygenase genes: heme oxygenase-1 (HMOX1) maps to chromosome 22q12 and heme oxygenase-2 (HMOX2) maps to chromosome 16p13.3". Genomics. 20 (3): 513–6. doi:10.1006/geno.1994.1213. PMID 8034330.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Takahashi K, Hara E, Suzuki H, Sasano H, Shibahara S (1996). "Expression of heme oxygenase isozyme mRNAs in the human brain and induction of heme oxygenase-1 by nitric oxide donors". J. Neurochem. 67 (2): 482–9. doi:10.1046/j.1471-4159.1996.67020482.x. PMID 8764571. S2CID 12552519.
Saito-Ohara F, Ikeuchi T, Matsumoto M, Kurata S (1997). "Assignment of the mouse heme oxygenase genes: heme oxygenase-1 (Hmox1) to chromosome 10 band C1 and heme oxygenase-2 (Hmox2) to chromosome 16 band B1". Cytogenet. Cell Genet. 77 (3–4): 180–1. doi:10.1159/000134570. PMID 9284910.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Yoshiki N, Kubota T, Aso T (2000). "Expression and localization of heme oxygenase in human placental villi". Biochem. Biophys. Res. Commun. 276 (3): 1136–42. doi:10.1006/bbrc.2000.3551. PMID 11027601.
Hanselmann C, Mauch C, Werner S (2001). "Haem oxygenase-1: a novel player in cutaneous wound repair and psoriasis?". Biochem. J. 353 (Pt 3): 459–66. doi:10.1042/0264-6021:3530459. PMC 1221590. PMID 11171041.
Appleton SD, Marks GS, Nakatsu K, Brien JF, Smith GN, Graham CH, Lash GE (2003). "Effects of hypoxia on heme oxygenase expression in human chorionic villi explants and immortalized trophoblast cells". Am. J. Physiol. Heart Circ. Physiol. 284 (3): H853–8. doi:10.1152/ajpheart.00655.2002. PMID 12578814.
Galey D, Becker K, Haughey N, Kalehua A, Taub D, Woodward J, Mattson MP, Nath A (2003). "Differential transcriptional regulation by human immunodeficiency virus type 1 and gp120 in human astrocytes". J. Neurovirol. 9 (3): 358–71. doi:10.1080/13550280390201119. PMID 12775419. S2CID 22016092.
Zenclussen AC, Lim E, Knoeller S, Knackstedt M, Hertwig K, Hagen E, Klapp BF, Arck PC (2004). "Heme oxygenases in pregnancy II: HO-2 is downregulated in human pathologic pregnancies". Am. J. Reprod. Immunol. 50 (1): 66–76. doi:10.1034/j.1600-0897.2003.00047.x. PMID 14506930. S2CID 35763984.
Boehning D, Moon C, Sharma S, Hurt KJ, Hester LD, Ronnett GV, Shugar D, Snyder SH (2003). "Carbon monoxide neurotransmission activated by CK2 phosphorylation of heme oxygenase-2". Neuron. 40 (1): 129–37. doi:10.1016/S0896-6273(03)00596-8. PMID 14527438. S2CID 11562548.
Appleton SD, Lash GE, Marks GS, Nakatsu K, Brien JF, Smith GN, Graham CH (2004). "Effect of glucose and oxygen deprivation on heme oxygenase expression in human chorionic villi explants and immortalized trophoblast cells". Am. J. Physiol. Regul. Integr. Comp. Physiol. 285 (6): R1453–60. doi:10.1152/ajpregu.00234.2003. PMID 14615405.