HMOX2

Available structures

Ortholog search: PDBe RCSB

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

Identifiers

Aliases

HMOX2, HO-2, heme oxygenase 2

External IDs

MGI: 109373 HomoloGene: 1611 GeneCards: HMOX2

Gene location (Human)

Chr.	Chromosome 16 (human)^[1]

Band	No data available	Start	4,474,690 bp^[1]
Band	No data available	End	4,510,347 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 16 (mouse)^[2]

Band	No data available	Start	4,726,361 bp^[2]
Band	No data available	End	4,766,742 bp^[2]

RNA expression pattern

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 • oxidation-reduction process • 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

RefSeq (protein)

NP_001120676 NP_001120677 NP_001120678 NP_001273196 NP_001273197
NP_001273198 NP_001273199 NP_001273200 NP_002125


NP_001129538 NP_034573

Location (UCSC)

Chr 16: 4.47 – 4.51 Mb

Chr 16: 4.73 – 4.77 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

1 2 3 ENSG00000103415 GRCh38: Ensembl release 89: ENSG00000277424, ENSG00000103415 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000004070 - Ensembl, May 2017
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ 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. PMID 1575508. doi:10.1016/0003-9861(92)90481-B.
1 2 "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. PMC 2896506 . PMID 17965015. doi:10.1074/jbc.M707396200.
Wang J, Zhuang H, Doré S (2006). "Heme oxygenase 2 is neuroprotective against intracerebral hemorrhage.". Neurobiol Dis. 22 (3): 473–6. PMID 16459095. doi:10.1016/j.nbd.2005.12.009.
Wang J, Doré S (2008). "Heme oxygenase 2 deficiency increases brain swelling and inflammation after intracerebral hemorrhage". Neuroscience. 155 (4): 1133–41. PMC 4696610 . PMID 18674596. doi:10.1016/j.neuroscience.2008.07.004.
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. PMC 58673 . PMID 11572959. doi:10.1073/pnas.191351298.
Doré S (2002). "Decreased activity of the antioxidant heme oxygenase enzyme: implications in ischemia and in Alzheimer's disease". Free Radic. Biol. Med. 32 (12): 1276–82. PMID 12057765. doi:10.1016/S0891-5849(02)00805-5.
Kemp PJ (2005). "Hemeoxygenase-2 as an O2 sensor in K+ channel-dependent chemotransduction". Biochem. Biophys. Res. Commun. 338 (1): 648–52. PMID 16137652. doi:10.1016/j.bbrc.2005.08.110.
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. PMID 7890772. doi:10.1074/jbc.270.11.6345.
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. PMID 8034330. doi:10.1006/geno.1994.1213.
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. PMID 8125298. doi:10.1016/0378-1119(94)90802-8.
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. PMID 8764571. doi:10.1046/j.1471-4159.1996.67020482.x.
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. PMID 9284910. doi:10.1159/000134570.
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. PMID 9373149. doi:10.1016/S0378-1119(97)00411-3.
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. PMID 11027601. doi:10.1006/bbrc.2000.3551.
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. PMC 1221590 . PMID 11171041. doi:10.1042/0264-6021:3530459.
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. PMID 12578814. doi:10.1152/ajpheart.00655.2002.
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. PMID 12775419. doi:10.1080/13550280390201119.
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. PMID 14506930. doi:10.1034/j.1600-0897.2003.00047.x.
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. PMID 14527438. doi:10.1016/S0896-6273(03)00596-8.
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. PMID 14615405. doi:10.1152/ajpregu.00234.2003.

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HMOX2

Function

References

Further reading