Microsomal glutathione S-transferase 1: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Microsomal glutathione S-transferase 1''' is an [[enzyme]] that in humans is encoded by the ''MGST1'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MGST1 microsomal glutathione S-transferase 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4257| accessdate = }}</ref>
| 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 =
| image_source =
| PDB =
| Name = Microsomal glutathione S-transferase 1
| HGNCid = 7061
| Symbol = MGST1
| AltSymbols =; GST12; MGC14525; MGST; MGST-I
| OMIM = 138330
| ECnumber = 
| Homologene = 10544
| MGIid = 1913850
| Function = {{GNF_GO|id=GO:0004364 |text = glutathione transferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005743 |text = mitochondrial inner membrane}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006749 |text = glutathione metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4257
    | Hs_Ensembl = ENSG00000008394
    | Hs_RefseqProtein = NP_064696
    | Hs_RefseqmRNA = NM_020300
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 12
    | Hs_GenLoc_start = 16391343
    | Hs_GenLoc_end = 16408610
    | Hs_Uniprot = P10620
    | Mm_EntrezGene = 56615
    | Mm_Ensembl = ENSMUSG00000008540
    | Mm_RefseqmRNA = NM_019946
    | Mm_RefseqProtein = NP_064330
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 6
    | Mm_GenLoc_start = 138104733
    | Mm_GenLoc_end = 138120948
    | Mm_Uniprot = Q53ZD4
  }}
}}
'''Microsomal glutathione S-transferase 1''', also known as '''MGST1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MGST1 microsomal glutathione S-transferase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4257| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The [[MAPEG family]] (Membrane-Associated Proteins in Eicosanoid and Glutathione metabolism) consists of six human proteins, two of which are involved in the production of [[leukotriene]]s and [[prostaglandin E]], important mediators of [[inflammation]]. Other family members, demonstrating [[glutathione S-transferase]] and [[peroxidase]] activities, are involved in cellular defense against toxic, carcinogenic, and pharmacologically active electrophilic compounds. This gene encodes a protein that catalyzes the conjugation of [[glutathione]] to electrophiles and the reduction of lipid hydroperoxides. This protein is localized to the [[endoplasmic reticulum]] and outer [[mitochondrial membrane]] where it is thought to protect these membranes from [[oxidative stress]]. Four [[transcript variants]] of this gene encode one protein [[protein isoform|isoform]].<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = The MAPEG (Membrane Associated Proteins in Eicosanoid and Glutathione metabolism) family consists of six human proteins, two of which are involved in the production of leukotrienes and prostaglandin E, important mediators of inflammation. Other family members, demonstrating glutathione S-transferase and peroxidase activities, are involved in cellular defense against toxic, carcinogenic, and pharmacologically active electrophilic compounds. This gene encodes a protein that catalyzes the conjugation of glutathione to electrophiles and the reduction of lipid hydroperoxides. This protein is localized to the endoplasmic reticulum and outer mitochondrial membrane where it is thought to protect these membranes from oxidative stress. Four transcript variants of this gene encode one protein isoform.<ref name="entrez">{{cite web | title = Entrez Gene: MGST1 microsomal glutathione S-transferase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4257| accessdate = }}</ref>
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal   |vauthors=Jakobsson PJ, Morgenstern R, Mancini J |title=Membrane-associated proteins in eicosanoid and glutathione metabolism (MAPEG). A widespread protein superfamily. |journal=Am. J. Respir. Crit. Care Med. |volume=161 |issue= 2 Pt 2 |pages= S20–4 |year= 2000 |pmid= 10673221 |doi=  10.1164/ajrccm.161.supplement_1.ltta-5}}
| citations =
*{{cite journal   |vauthors=Cholon A, Giaccia AJ, Lewis AD |title=What role do glutathione S-transferases play in the cellular response to ionizing radiation? |journal=Int. J. Radiat. Oncol. Biol. Phys. |volume=22 |issue= 4 |pages= 759–63 |year= 1992 |pmid= 1544849 |doi=  }}
*{{cite journal | author=Jakobsson PJ, Morgenstern R, Mancini J, ''et al.'' |title=Membrane-associated proteins in eicosanoid and glutathione metabolism (MAPEG). A widespread protein superfamily. |journal=Am. J. Respir. Crit. Care Med. |volume=161 |issue= 2 Pt 2 |pages= S20-4 |year= 2000 |pmid= 10673221 |doi=  }}
*{{cite journal  | vauthors=DeJong JL, Mohandas T, Tu CP |title=The gene for the microsomal glutathione S-transferase is on human chromosome 12. |journal=Genomics |volume=6 |issue= 2 |pages= 379–82 |year= 1990 |pmid= 2307478 |doi=10.1016/0888-7543(90)90580-N }}
*{{cite journal | author=Cholon A, Giaccia AJ, Lewis AD, ''et al.'' |title=What role do glutathione S-transferases play in the cellular response to ionizing radiation? |journal=Int. J. Radiat. Oncol. Biol. Phys. |volume=22 |issue= 4 |pages= 759-63 |year= 1992 |pmid= 1544849 |doi=  }}
*{{cite journal   |vauthors=DeJong JL, Morgenstern R, Jörnvall H |title=Gene expression of rat and human microsomal glutathione S-transferases. |journal=J. Biol. Chem. |volume=263 |issue= 17 |pages= 8430–6 |year= 1988 |pmid= 3372534 |doi=  }}
*{{cite journal  | author=DeJong JL, Mohandas T, Tu CP |title=The gene for the microsomal glutathione S-transferase is on human chromosome 12. |journal=Genomics |volume=6 |issue= 2 |pages= 379-82 |year= 1990 |pmid= 2307478 |doi=  }}
*{{cite journal   |vauthors=Adams MD, Kerlavage AR, Fleischmann RD |title=Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence. |journal=Nature |volume=377 |issue= 6547 Suppl |pages= 3–174 |year= 1995 |pmid= 7566098 |doi=<!-- none available --> |url=http://www.columbia.edu/itc/biology/pollack/w4065/client_edit/readings/nature377_3.pdf | format=PDF  }}  
*{{cite journal | author=DeJong JL, Morgenstern R, Jörnvall H, ''et al.'' |title=Gene expression of rat and human microsomal glutathione S-transferases. |journal=J. Biol. Chem. |volume=263 |issue= 17 |pages= 8430-6 |year= 1988 |pmid= 3372534 |doi=  }}
*{{cite journal  | vauthors=Söderström M, Morgenstern R, Hammarström S |title=Protein-protein interaction affinity chromatography of leukotriene C4 synthase. |journal=Protein Expr. Purif. |volume=6 |issue= 3 |pages= 352–6 |year= 1995 |pmid= 7663172 |doi= 10.1006/prep.1995.1046 }}
*{{cite journal | author=Adams MD, Kerlavage AR, Fleischmann RD, ''et al.'' |title=Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence. |journal=Nature |volume=377 |issue= 6547 Suppl |pages= 3-174 |year= 1995 |pmid= 7566098 |doi= }}
*{{cite journal  | vauthors=Kelner MJ, Stokely MN, Stovall NE, Montoya MA |title=Structural organization of the human microsomal glutathione S-transferase gene (GST12). |journal=Genomics |volume=36 |issue= 1 |pages= 100–3 |year= 1997 |pmid= 8812420 |doi= 10.1006/geno.1996.0429 }}
*{{cite journal  | author=Söderström M, Morgenstern R, Hammarström S |title=Protein-protein interaction affinity chromatography of leukotriene C4 synthase. |journal=Protein Expr. Purif. |volume=6 |issue= 3 |pages= 352-6 |year= 1995 |pmid= 7663172 |doi= 10.1006/prep.1995.1046 }}
*{{cite journal   |vauthors=Estonius M, Forsberg L, Danielsson O |title=Distribution of microsomal glutathione transferase 1 in mammalian tissues. A predominant alternate first exon in human tissues. |journal=Eur. J. Biochem. |volume=260 |issue= 2 |pages= 409–13 |year= 1999 |pmid= 10095775 |doi=10.1046/j.1432-1327.1999.00165.x }}
*{{cite journal  | author=Kelner MJ, Stokely MN, Stovall NE, Montoya MA |title=Structural organization of the human microsomal glutathione S-transferase gene (GST12). |journal=Genomics |volume=36 |issue= 1 |pages= 100-3 |year= 1997 |pmid= 8812420 |doi= 10.1006/geno.1996.0429 }}
*{{cite journal  | vauthors=Lee SH, DeJong J |title=Microsomal GST-I: genomic organization, expression, and alternative splicing of the human gene. |journal=Biochim. Biophys. Acta |volume=1446 |issue= 3 |pages= 389–96 |year= 1999 |pmid= 10524215 |doi=  10.1016/S0167-4781(99)00112-8}}
*{{cite journal | author=Estonius M, Forsberg L, Danielsson O, ''et al.'' |title=Distribution of microsomal glutathione transferase 1 in mammalian tissues. A predominant alternate first exon in human tissues. |journal=Eur. J. Biochem. |volume=260 |issue= 2 |pages= 409-13 |year= 1999 |pmid= 10095775 |doi=  }}
*{{cite journal   |vauthors=Kelner MJ, Bagnell RD, Montoya MA |title=Structural organization of the microsomal glutathione S-transferase gene (MGST1) on chromosome 12p13.1-13.2. Identification of the correct promoter region and demonstration of transcriptional regulation in response to oxidative stress. |journal=J. Biol. Chem. |volume=275 |issue= 17 |pages= 13000–6 |year= 2000 |pmid= 10777602 |doi=10.1074/jbc.275.17.13000 }}
*{{cite journal  | author=Lee SH, DeJong J |title=Microsomal GST-I: genomic organization, expression, and alternative splicing of the human gene. |journal=Biochim. Biophys. Acta |volume=1446 |issue= 3 |pages= 389-96 |year= 1999 |pmid= 10524215 |doi=  }}
*{{cite journal   |vauthors=Surapureddi S, Svartz J, Magnusson KE |title=Colocalization of leukotriene C synthase and microsomal glutathione S-transferase elucidated by indirect immunofluorescence analysis. |journal=FEBS Lett. |volume=480 |issue= 2–3 |pages= 239–43 |year= 2000 |pmid= 11034337 |doi=10.1016/S0014-5793(00)01885-8 }}
*{{cite journal | author=Kelner MJ, Bagnell RD, Montoya MA, ''et al.'' |title=Structural organization of the microsomal glutathione S-transferase gene (MGST1) on chromosome 12p13.1-13.2. Identification of the correct promoter region and demonstration of transcriptional regulation in response to oxidative stress. |journal=J. Biol. Chem. |volume=275 |issue= 17 |pages= 13000-6 |year= 2000 |pmid= 10777602 |doi=  }}
*{{cite journal   |vauthors=Iida A, Saito S, Sekine A |title=Catalog of 46 single-nucleotide polymorphisms (SNPs) in the microsomal glutathione S-transferase 1 (MGST1) gene |journal=J. Hum. Genet. |volume=46 |issue= 10 |pages= 590–4 |year= 2001 |pmid= 11587073 |doi=10.1007/s100380170026 }}
*{{cite journal | author=Surapureddi S, Svartz J, Magnusson KE, ''et al.'' |title=Colocalization of leukotriene C synthase and microsomal glutathione S-transferase elucidated by indirect immunofluorescence analysis. |journal=FEBS Lett. |volume=480 |issue= 2-3 |pages= 239-43 |year= 2000 |pmid= 11034337 |doi=  }}
*{{cite journal   |vauthors=To-Figueras J, Gené M, Gómez-Catalán J |title=Microsomal epoxide hydrolase and glutathione S-transferase polymorphisms in relation to laryngeal carcinoma risk |journal=Cancer Lett. |volume=187 |issue= 1–2 |pages= 95–101 |year= 2003 |pmid= 12359356 |doi=10.1016/S0304-3835(02)00406-8 }}
*{{cite journal | author=Iida A, Saito S, Sekine A, ''et al.'' |title=Catalog of 46 single-nucleotide polymorphisms (SNPs) in the microsomal glutathione S-transferase 1 (MGST1) gene. |journal=J. Hum. Genet. |volume=46 |issue= 10 |pages= 590-4 |year= 2001 |pmid= 11587073 |doi=  }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH |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 | pmc=139241 }}
*{{cite journal | author=To-Figueras J, Gené M, Gómez-Catalán J, ''et al.'' |title=Microsomal epoxide hydrolase and glutathione S-transferase polymorphisms in relation to laryngeal carcinoma risk. |journal=Cancer Lett. |volume=187 |issue= 1-2 |pages= 95-101 |year= 2003 |pmid= 12359356 |doi=  }}
*{{cite journal   |vauthors=Ekström L, Lyrenäs L, Jakobsson PJ |title=Basal expression of the human MAPEG members microsomal glutathione transferase 1 and prostaglandin E synthase genes is mediated by Sp1 and Sp3 |journal=Biochim. Biophys. Acta |volume=1627 |issue= 2–3 |pages= 79–84 |year= 2003 |pmid= 12818425 |doi=  10.1016/S0167-4781(03)00077-0}}
*{{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=Lengqvist J, Svensson R, Evergren E|title=Observation of an intact noncovalent homotrimer of detergent-solubilized rat microsomal glutathione transferase-1 by electrospray mass spectrometry |journal=J. Biol. Chem. |volume=279 |issue= 14 |pages= 13311–6 |year= 2004 |pmid= 14726533 |doi= 10.1074/jbc.M310958200 }}
*{{cite journal | author=Ekström L, Lyrenäs L, Jakobsson PJ, ''et al.'' |title=Basal expression of the human MAPEG members microsomal glutathione transferase 1 and prostaglandin E synthase genes is mediated by Sp1 and Sp3. |journal=Biochim. Biophys. Acta |volume=1627 |issue= 2-3 |pages= 79-84 |year= 2003 |pmid= 12818425 |doi=  }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
*{{cite journal | author=Lengqvist J, Svensson R, Evergren E, ''et al.'' |title=Observation of an intact noncovalent homotrimer of detergent-solubilized rat microsomal glutathione transferase-1 by electrospray mass spectrometry. |journal=J. Biol. Chem. |volume=279 |issue= 14 |pages= 13311-6 |year= 2004 |pmid= 14726533 |doi= 10.1074/jbc.M310958200 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
}}
{{refend}}
{{refend}}


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[[Category:Human proteins]]
[[Category:EC 2.5.1]]

Latest revision as of 23:23, 30 May 2018

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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

Microsomal glutathione S-transferase 1 is an enzyme that in humans is encoded by the MGST1 gene.[1]

Function

The MAPEG family (Membrane-Associated Proteins in Eicosanoid and Glutathione metabolism) consists of six human proteins, two of which are involved in the production of leukotrienes and prostaglandin E, important mediators of inflammation. Other family members, demonstrating glutathione S-transferase and peroxidase activities, are involved in cellular defense against toxic, carcinogenic, and pharmacologically active electrophilic compounds. This gene encodes a protein that catalyzes the conjugation of glutathione to electrophiles and the reduction of lipid hydroperoxides. This protein is localized to the endoplasmic reticulum and outer mitochondrial membrane where it is thought to protect these membranes from oxidative stress. Four transcript variants of this gene encode one protein isoform.[1]

References

  1. 1.0 1.1 "Entrez Gene: MGST1 microsomal glutathione S-transferase 1".

Further reading