GSTO1

GSTO1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1EEM, 3LFL, 3VLN, 4IS0
Identifiers
Aliases	GSTO1, GSTO 1-1, GSTTLp28, HEL-S-21, P28, SPG-R, glutathione S-transferase omega 1
External IDs	OMIM: 605482 MGI: 1342273 HomoloGene: 37971 GeneCards: GSTO1
EC number	1.20.4.2
Gene location (Human)
Chr.	Chromosome 10 (human)[1]
End	104,267,459 bp[1]
Gene location (Mouse)
Chr.	Chromosome 19 (mouse)[2]
End	47,853,229 bp[2]
RNA expression pattern
	Top expressed in
	monocyte; ; right lobe of liver; ; right lung; ; middle temporal gyrus; ; kidney tubule; ; left ventricle; ; right ventricle; ; periodontal fiber; ; left adrenal gland; ; endothelial cell;
	Top expressed in
	conjunctival fornix; ; corneal stroma; ; ciliary body; ; gastric mucosa; ; mucous cell of stomach; ; epithelium of stomach; ; superior surface of tongue; ; pyloric antrum; ; duodenum; ; esophagus;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	transferase activity; glutathione dehydrogenase (ascorbate) activity; protein binding; methylarsonate reductase activity; oxidoreductase activity; glutathione transferase activity;
Cellular component	cytoplasm; cytosol; extracellular exosome;
Biological process	xenobiotic catabolic process; regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; negative regulation of ryanodine-sensitive calcium-release channel activity; positive regulation of ryanodine-sensitive calcium-release channel activity; methylation; cellular response to arsenic-containing substance; positive regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion; metabolism; regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; glutathione derivative biosynthetic process; L-ascorbic acid metabolic process; cellular oxidant detoxification; glutathione metabolic process; toxin catabolic process; interleukin-12-mediated signaling pathway;
	Sources:Amigo / QuickGO
Orthologs
	9446
	14873
	ENSG00000148834
	ENSMUSG00000025068
	P78417; Q5TA02
	O09131
	NM_004832; NM_001191002; NM_001191003
	NM_010362
	NP_001177931; NP_001177932; NP_004823
	NP_034492
	Wikidata
View/Edit Human	View/Edit Mouse

Glutathione S-transferase omega-1 is an enzyme that in humans is encoded by the GSTO1 gene.[5][6][7]

This gene encodes a member of the theta class glutathione S-transferase-like (GSTTL) protein family. In mouse, the encoded protein acts as a small stress response protein, likely involved in cellular redox homeostasis.[7] This protein has dehydroascorbate reductase activity and may function in the glutathione-ascorbate cycle as part of antioxidant metabolism.[8]

References

GRCh38: Ensembl release 89: ENSG00000148834 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000025068 - 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.
Board PG, Coggan M, Chelvanayagam G, Easteal S, Jermiin LS, Schulte GK, Danley DE, Hoth LR, Griffor MC, Kamath AV, Rosner MH, Chrunyk BA, Perregaux DE, Gabel CA, Geoghegan KF, Pandit J (Sep 2000). "Identification, characterization, and crystal structure of the Omega class glutathione transferases". J Biol Chem. 275 (32): 24798–806. doi:10.1074/jbc.M001706200. PMID 10783391.
Whitbread AK, Tetlow N, Eyre HJ, Sutherland GR, Board PG (Mar 2003). "Characterization of the human Omega class glutathione transferase genes and associated polymorphisms". Pharmacogenetics. 13 (3): 131–44. doi:10.1097/00008571-200303000-00003. PMID 12618591.
"Entrez Gene: GSTO1 glutathione S-transferase omega 1".
Whitbread AK, Masoumi A, Tetlow N, Schmuck E, Coggan M, Board PG (2005). "Characterization of the omega class of glutathione transferases". Meth. Enzymol. Methods in Enzymology. 401: 78–99. doi:10.1016/S0076-6879(05)01005-0. ISBN 978-0-12-182806-6. PMID 16399380.

Matoba R, Okubo K, Hori N, et al. (1994). "The addition of 5'-coding information to a 3'-directed cDNA library improves analysis of gene expression". Gene. 146 (2): 199–207. doi:10.1016/0378-1119(94)90293-3. PMID 8076819.
Ishikawa T, Casini AF, Nishikimi M (1998). "Molecular cloning and functional expression of rat liver glutathione-dependent dehydroascorbate reductase". J. Biol. Chem. 273 (44): 28708–12. doi:10.1074/jbc.273.44.28708. PMID 9786866.
Kodym R, Calkins P, Story M (1999). "The cloning and characterization of a new stress response protein. A mammalian member of a family of theta class glutathione s-transferase-like proteins". J. Biol. Chem. 274 (8): 5131–7. doi:10.1074/jbc.274.8.5131. PMID 9988762.
Hubbard MJ, McHugh NJ (2001). "Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping". Electrophoresis. 21 (17): 3785–96. doi:10.1002/1522-2683(200011)21:17<3785::AID-ELPS3785>3.0.CO;2-2. PMID 11271497. S2CID 42538820.
Yin ZL, Dahlstrom JE, Le Couteur DG, Board PG (2001). "Immunohistochemistry of omega class glutathione S-transferase in human tissues". J. Histochem. Cytochem. 49 (8): 983–7. doi:10.1177/002215540104900806. PMID 11457926.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Tanaka-Kagawa T, Jinno H, Hasegawa T, et al. (2003). "Functional characterization of two variant human GSTO 1-1s (Ala140Asp and Thr217Asn)". Biochem. Biophys. Res. Commun. 301 (2): 516–20. doi:10.1016/S0006-291X(02)03066-8. PMID 12565892.
Yu L, Kalla K, Guthrie E, et al. (2004). "Genetic variation in genes associated with arsenic metabolism: glutathione S-transferase omega 1-1 and purine nucleoside phosphorylase polymorphisms in European and indigenous Americans". Environ. Health Perspect. 111 (11): 1421–7. doi:10.1289/ehp.6420. PMC 1241635. PMID 12928150.
Li YJ, Oliveira SA, Xu P, et al. (2004). "Glutathione S-transferase omega-1 modifies age-at-onset of Alzheimer disease and Parkinson disease". Hum. Mol. Genet. 12 (24): 3259–67. doi:10.1093/hmg/ddg357. PMID 14570706.
Whitbread AK, Mellick GD, Silburn PA, et al. (2004). "Glutathione transferase Omega class polymorphisms in Parkinson disease". Neurology. 62 (10): 1910–1. doi:10.1212/01.wnl.0000125282.09308.b1. PMID 15159516. S2CID 46505059.
Deloukas P, Earthrowl ME, Grafham DV, et al. (2004). "The DNA sequence and comparative analysis of human chromosome 10". Nature. 429 (6990): 375–81. Bibcode:2004Natur.429..375D. doi:10.1038/nature02462. PMID 15164054.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Kölsch H, Linnebank M, Lütjohann D, et al. (2005). "Polymorphisms in glutathione S-transferase omega-1 and AD, vascular dementia, and stroke". Neurology. 63 (12): 2255–60. doi:10.1212/01.wnl.0000147294.29309.47. PMID 15623683. S2CID 21431373.
Ozturk A, Desai PP, Minster RL, et al. (2005). "Three SNPs in the GSTO1, GSTO2 and PRSS11 genes on chromosome 10 are not associated with age-at-onset of Alzheimer's disease". Neurobiol. Aging. 26 (8): 1161–5. doi:10.1016/j.neurobiolaging.2004.11.001. PMID 15917099. S2CID 10878355.
Stelzl U, Worm U, Lalowski M, et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.
Fujihara J, Kunito T, Takeshita H (2007). "Frequency of two human glutathione-S-transferase omega-1 polymorphisms (E155 deletion and E208K) in Ovambo and Japanese populations using the PCR-based genotyping method". Clin. Chem. Lab. Med. 45 (5): 621–4. doi:10.1515/CCLM.2007.128. PMID 17484623. S2CID 1553700.
Harju TH, Peltoniemi MJ, Rytilä PH, et al. (2007). "Glutathione S-transferase omega in the lung and sputum supernatants of COPD patients". Respir. Res. 8 (1): 48. doi:10.1186/1465-9921-8-48. PMC 1939846. PMID 17617905.
Kölsch H, Larionov S, Dedeck O, et al. (2007). "Association of the glutathione S-transferase omega-1 Ala140Asp polymorphism with cerebrovascular atherosclerosis and plaque-associated interleukin-1 alpha expression". Stroke. 38 (10): 2847–50. doi:10.1161/STROKEAHA.107.484162. PMID 17717316.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000148834 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000025068 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid10783391-5] Board PG, Coggan M, Chelvanayagam G, Easteal S, Jermiin LS, Schulte GK, Danley DE, Hoth LR, Griffor MC, Kamath AV, Rosner MH, Chrunyk BA, Perregaux DE, Gabel CA, Geoghegan KF, Pandit J (Sep 2000). "Identification, characterization, and crystal structure of the Omega class glutathione transferases". J Biol Chem. 275 (32): 24798–806. doi:10.1074/jbc.M001706200. PMID 10783391.

[pmid12618591-6] Whitbread AK, Tetlow N, Eyre HJ, Sutherland GR, Board PG (Mar 2003). "Characterization of the human Omega class glutathione transferase genes and associated polymorphisms". Pharmacogenetics. 13 (3): 131–44. doi:10.1097/00008571-200303000-00003. PMID 12618591.

[entrez-7] "Entrez Gene: GSTO1 glutathione S-transferase omega 1".

[8] Whitbread AK, Masoumi A, Tetlow N, Schmuck E, Coggan M, Board PG (2005). "Characterization of the omega class of glutathione transferases". Meth. Enzymol. Methods in Enzymology. 401: 78–99. doi:10.1016/S0076-6879(05)01005-0. ISBN 978-0-12-182806-6. PMID 16399380.

GSTO1

References

Further reading