HMOX2: Difference between revisions

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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Heme oxygenase 2''' is an [[enzyme]] that in humans is encoded by the ''HMOX2'' [[gene]].<ref name="pmid1575508">{{cite journal | vauthors = McCoubrey WK, Ewing JF, Maines MD | title = 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 | journal = Arch Biochem Biophys | volume = 295 | issue = 1 | pages = 13–20 | date = Jun 1992 | pmid = 1575508 | pmc = | doi = 10.1016/0003-9861(92)90481-B }}</ref><ref name="entrez"/>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_HMOX2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2q32.
| PDB = {{PDB2|2q32}}
| Name = Heme oxygenase (decycling) 2
| HGNCid = 5014
| Symbol = HMOX2
| AltSymbols =; HO-2
| OMIM = 141251
| ECnumber = 
| Homologene = 1611
| MGIid = 109373
| GeneAtlas_image1 = PBB_GE_HMOX2_218120_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_HMOX2_218121_at_tn.png
| Function = {{GNF_GO|id=GO:0004392 |text = heme oxygenase (decyclizing) activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0009055 |text = electron carrier activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005792 |text = microsome}}
| Process = {{GNF_GO|id=GO:0006788 |text = heme oxidation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3163
    | Hs_Ensembl = ENSG00000103415
    | Hs_RefseqProtein = NP_002125
    | Hs_RefseqmRNA = NM_002134
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 16
    | Hs_GenLoc_start = 4466426
    | Hs_GenLoc_end = 4500348
    | Hs_Uniprot = P30519
    | Mm_EntrezGene = 15369
    | Mm_Ensembl = ENSMUSG00000004070
    | Mm_RefseqmRNA = NM_010443
    | Mm_RefseqProtein = NP_034573
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 16
    | Mm_GenLoc_start = 4641617
    | Mm_GenLoc_end = 4681474
    | Mm_Uniprot = Q3U6W4
  }}
}}
'''Heme oxygenase (decycling) 2''', also known as '''HMOX2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HMOX2 heme oxygenase (decycling) 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3163| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
[[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 [[isozyme]]s, an inducible heme oxygenase-1 and a constitutive heme oxygenase-2. [[HMOX1]] and HMOX2 (this enzyme) belong to the heme oxygenase family.<ref name="entrez">{{cite web | title = Entrez Gene: HMOX2 heme oxygenase (decycling) 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3163| accessdate = }}</ref>
{{PBB_Summary
| section_title =
| summary_text = 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 belong to the heme oxygenase family.<ref name="entrez">{{cite web | title = Entrez Gene: HMOX2 heme oxygenase (decycling) 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3163| accessdate = }}</ref>
}}


==References==
== References ==
{{reflist|2}}
{{reflist}}
==Further reading==
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
*{{cite journal | author=Bianchetti CM, Yi L, Ragsdale SW, Phillips GN Jr. |title=Comparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2. |journal=J Biol Chem. |volume=282 |issue= 52 |pages= 37624-31 |year= 2007 |pmid= 17965015 |doi= }}
* {{cite journal | vauthors = Bianchetti CM, Yi L, Ragsdale SW, Phillips GN | title = Comparison of Apo- and Heme-bound Crystal Structures of a Truncated Human Heme Oxygenase-2 | journal = J Biol Chem | volume = 282 | issue = 52 | pages = 37624–31 | year = 2007 | pmid = 17965015 | pmc = 2896506 | doi = 10.1074/jbc.M707396200 }}
{{PBB_Further_reading
* {{cite journal | vauthors = Wang J, Zhuang H, Doré S | title = Heme oxygenase 2 is neuroprotective against intracerebral hemorrhage. | journal = Neurobiol Dis. | volume = 22 | issue = 3 | pages = 473–6 | year = 2006 | pmid = 16459095 | doi = 10.1016/j.nbd.2005.12.009 }}
| citations =
* {{cite journal | vauthors = Wang J, Doré S | title = Heme oxygenase 2 deficiency increases brain swelling and inflammation after intracerebral hemorrhage | journal = Neuroscience | volume = 155 | issue = 4 | pages = 1133–41 | year = 2008 | pmid = 18674596 | pmc = 4696610 | doi = 10.1016/j.neuroscience.2008.07.004 }}
*{{cite journal | author=Barañano DE, Snyder SH |title=Neural roles for heme oxygenase: contrasts to nitric oxide synthase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 20 |pages= 10996-1002 |year= 2001 |pmid= 11572959 |doi= 10.1073/pnas.191351298 }}
* {{cite journal | vauthors = Barañano DE, Snyder SH | title = Neural roles for heme oxygenase: Contrasts to nitric oxide synthase | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 98 | issue = 20 | pages = 10996–1002 | year = 2001 | pmid = 11572959 | pmc = 58673 | doi = 10.1073/pnas.191351298 | bibcode = 2001PNAS...9810996B }}
*{{cite journal | author=Doré S |title=Decreased activity of the antioxidant heme oxygenase enzyme: implications in ischemia and in Alzheimer's disease. |journal=Free Radic. Biol. Med. |volume=32 |issue= 12 |pages= 1276-82 |year= 2002 |pmid= 12057765 |doi= }}
* {{cite journal | vauthors = Doré S | title = Decreased activity of the antioxidant heme oxygenase enzyme: implications in ischemia and in Alzheimer's disease | journal = Free Radic. Biol. Med. | volume = 32 | issue = 12 | pages = 1276–82 | year = 2002 | pmid = 12057765 | doi = 10.1016/S0891-5849(02)00805-5 }}
*{{cite journal | author=Kemp PJ |title=Hemeoxygenase-2 as an O2 sensor in K+ channel-dependent chemotransduction. |journal=Biochem. Biophys. Res. Commun. |volume=338 |issue= 1 |pages= 648-52 |year= 2005 |pmid= 16137652 |doi= 10.1016/j.bbrc.2005.08.110 }}
* {{cite journal | vauthors = Kemp PJ | title = Hemeoxygenase-2 as an O2 sensor in K+ channel-dependent chemotransduction | journal = Biochem. Biophys. Res. Commun. | volume = 338 | issue = 1 | pages = 648–52 | year = 2005 | pmid = 16137652 | doi = 10.1016/j.bbrc.2005.08.110 }}
*{{cite journal | author=McCoubrey WK, Ewing JF, Maines MD |title=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. |journal=Arch. Biochem. Biophys. |volume=295 |issue= 1 |pages= 13-20 |year= 1992 |pmid= 1575508 |doi= }}
* {{cite journal | vauthors = Ishikawa K, Takeuchi N, Takahashi S, Matera KM, Sato M, Shibahara S, Rousseau DL, Ikeda-Saito M, Yoshida T | title = Heme oxygenase-2. Properties of the heme complex of the purified tryptic fragment of recombinant human heme oxygenase-2 | journal = J. Biol. Chem. | volume = 270 | issue = 11 | pages = 6345–50 | year = 1995 | pmid = 7890772 | doi = 10.1074/jbc.270.11.6345 }}
*{{cite journal | author=Ishikawa K, Takeuchi N, Takahashi S, ''et al.'' |title=Heme oxygenase-2. Properties of the heme complex of the purified tryptic fragment of recombinant human heme oxygenase-2. |journal=J. Biol. Chem. |volume=270 |issue= 11 |pages= 6345-50 |year= 1995 |pmid= 7890772 |doi= }}
* {{cite journal | vauthors = Kutty RK, Kutty G, Rodriguez IR, Chader GJ, Wiggert B | title = 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 | journal = Genomics | volume = 20 | issue = 3 | pages = 513–6 | year = 1994 | pmid = 8034330 | doi = 10.1006/geno.1994.1213 }}
*{{cite journal | author=Kutty RK, Kutty G, Rodriguez IR, ''et al.'' |title=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. |journal=Genomics |volume=20 |issue= 3 |pages= 513-6 |year= 1994 |pmid= 8034330 |doi= 10.1006/geno.1994.1213 }}
* {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1–2 | pages = 171–4 | year = 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
* {{cite journal | vauthors = Takahashi K, Hara E, Suzuki H, Sasano H, Shibahara S | title = Expression of heme oxygenase isozyme mRNAs in the human brain and induction of heme oxygenase-1 by nitric oxide donors | journal = J. Neurochem. | volume = 67 | issue = 2 | pages = 482–9 | year = 1996 | pmid = 8764571 | doi = 10.1046/j.1471-4159.1996.67020482.x }}
*{{cite journal | author=Takahashi K, Hara E, Suzuki H, ''et al.'' |title=Expression of heme oxygenase isozyme mRNAs in the human brain and induction of heme oxygenase-1 by nitric oxide donors. |journal=J. Neurochem. |volume=67 |issue= 2 |pages= 482-9 |year= 1996 |pmid= 8764571 |doi= }}
* {{cite journal | vauthors = Saito-Ohara F, Ikeuchi T, Matsumoto M, Kurata S | title = 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 | journal = Cytogenet. Cell Genet. | volume = 77 | issue = 3–4 | pages = 180–1 | year = 1997 | pmid = 9284910 | doi = 10.1159/000134570 }}
*{{cite journal | author=Saito-Ohara F, Ikeuchi T, Matsumoto M, Kurata S |title=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. |journal=Cytogenet. Cell Genet. |volume=77 |issue= 3-4 |pages= 180-1 |year= 1997 |pmid= 9284910 |doi= }}
* {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1–2 | pages = 149–56 | year = 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
* {{cite journal | vauthors = Yoshiki N, Kubota T, Aso T | title = Expression and localization of heme oxygenase in human placental villi | journal = Biochem. Biophys. Res. Commun. | volume = 276 | issue = 3 | pages = 1136–42 | year = 2000 | pmid = 11027601 | doi = 10.1006/bbrc.2000.3551 }}
*{{cite journal | author=Yoshiki N, Kubota T, Aso T |title=Expression and localization of heme oxygenase in human placental villi. |journal=Biochem. Biophys. Res. Commun. |volume=276 |issue= 3 |pages= 1136-42 |year= 2000 |pmid= 11027601 |doi= 10.1006/bbrc.2000.3551 }}
* {{cite journal | vauthors = Hanselmann C, Mauch C, Werner S | title = Haem oxygenase-1: a novel player in cutaneous wound repair and psoriasis? | journal = Biochem. J. | volume = 353 | issue = Pt 3 | pages = 459–66 | year = 2001 | pmid = 11171041 | pmc = 1221590 | doi = 10.1042/0264-6021:3530459 }}
*{{cite journal | author=Hanselmann C, Mauch C, Werner S |title=Haem oxygenase-1: a novel player in cutaneous wound repair and psoriasis? |journal=Biochem. J. |volume=353 |issue= Pt 3 |pages= 459-66 |year= 2001 |pmid= 11171041 |doi= }}
* {{cite journal | vauthors = Appleton SD, Marks GS, Nakatsu K, Brien JF, Smith GN, Graham CH, Lash GE | title = Effects of hypoxia on heme oxygenase expression in human chorionic villi explants and immortalized trophoblast cells | journal = Am. J. Physiol. Heart Circ. Physiol. | volume = 284 | issue = 3 | pages = H853–8 | year = 2003 | pmid = 12578814 | doi = 10.1152/ajpheart.00655.2002 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{cite journal | vauthors = Galey D, Becker K, Haughey N, Kalehua A, Taub D, Woodward J, Mattson MP, Nath A | title = Differential transcriptional regulation by human immunodeficiency virus type 1 and gp120 in human astrocytes | journal = J. Neurovirol. | volume = 9 | issue = 3 | pages = 358–71 | year = 2003 | pmid = 12775419 | doi = 10.1080/13550280390201119 }}
*{{cite journal | author=Appleton SD, Marks GS, Nakatsu K, ''et al.'' |title=Effects of hypoxia on heme oxygenase expression in human chorionic villi explants and immortalized trophoblast cells. |journal=Am. J. Physiol. Heart Circ. Physiol. |volume=284 |issue= 3 |pages= H853-8 |year= 2003 |pmid= 12578814 |doi= 10.1152/ajpheart.00655.2002 }}
* {{cite journal | vauthors = Zenclussen AC, Lim E, Knoeller S, Knackstedt M, Hertwig K, Hagen E, Klapp BF, Arck PC | title = Heme oxygenases in pregnancy II: HO-2 is downregulated in human pathologic pregnancies | journal = Am. J. Reprod. Immunol. | volume = 50 | issue = 1 | pages = 66–76 | year = 2004 | pmid = 14506930 | doi = 10.1034/j.1600-0897.2003.00047.x }}
*{{cite journal | author=Galey D, Becker K, Haughey N, ''et al.'' |title=Differential transcriptional regulation by human immunodeficiency virus type 1 and gp120 in human astrocytes. |journal=J. Neurovirol. |volume=9 |issue= 3 |pages= 358-71 |year= 2003 |pmid= 12775419 |doi= }}
* {{cite journal | vauthors = Boehning D, Moon C, Sharma S, Hurt KJ, Hester LD, Ronnett GV, Shugar D, Snyder SH | title = Carbon monoxide neurotransmission activated by CK2 phosphorylation of heme oxygenase-2 | journal = Neuron | volume = 40 | issue = 1 | pages = 129–37 | year = 2003 | pmid = 14527438 | doi = 10.1016/S0896-6273(03)00596-8 }}
*{{cite journal | author=Zenclussen AC, Lim E, Knoeller S, ''et al.'' |title=Heme oxygenases in pregnancy II: HO-2 is downregulated in human pathologic pregnancies. |journal=Am. J. Reprod. Immunol. |volume=50 |issue= 1 |pages= 66-76 |year= 2004 |pmid= 14506930 |doi= }}
* {{cite journal | vauthors = Appleton SD, Lash GE, Marks GS, Nakatsu K, Brien JF, Smith GN, Graham CH | title = Effect of glucose and oxygen deprivation on heme oxygenase expression in human chorionic villi explants and immortalized trophoblast cells | journal = Am. J. Physiol. Regul. Integr. Comp. Physiol. | volume = 285 | issue = 6 | pages = R1453–60 | year = 2004 | pmid = 14615405 | doi = 10.1152/ajpregu.00234.2003 }}
*{{cite journal | author=Boehning D, Moon C, Sharma S, ''et al.'' |title=Carbon monoxide neurotransmission activated by CK2 phosphorylation of heme oxygenase-2. |journal=Neuron |volume=40 |issue= 1 |pages= 129-37 |year= 2003 |pmid= 14527438 |doi= }}
*{{cite journal  | author=Appleton SD, Lash GE, Marks GS, ''et al.'' |title=Effect of glucose and oxygen deprivation on heme oxygenase expression in human chorionic villi explants and immortalized trophoblast cells. |journal=Am. J. Physiol. Regul. Integr. Comp. Physiol. |volume=285 |issue= 6 |pages= R1453-60 |year= 2004 |pmid= 14615405 |doi= 10.1152/ajpregu.00234.2003 }}
}}
{{refend}}
{{refend}}


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Revision as of 21:43, 10 September 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Heme oxygenase 2 is an enzyme that in humans is encoded by the HMOX2 gene.[1][2]

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.[2]

References

  1. 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.
  2. 2.0 2.1 "Entrez Gene: HMOX2 heme oxygenase (decycling) 2".

Further reading