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] Band 10q25.1 Start 104,235,356 bp [1] End 104,267,459 bp [1]
Gene location (Mouse) Chr. Chromosome 19 (mouse) [2] Band 19|19 D1 Start 47,843,409 bp [2] End 47,853,229 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) 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 BioGPS 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 Species Human Mouse Entrez 9446 14873 Ensembl ENSG00000148834 ENSMUSG00000025068 UniProt P78417 Q5TA02 O09131 RefSeq (mRNA) NM_004832 NM_001191002 NM_001191003 NM_010362 RefSeq (protein) NP_001177931 NP_001177932 NP_004823 NP_034492 Location (UCSC) Chr 10: 104.24 – 104.27 Mb Chr 19: 47.84 – 47.85 Mb PubMed search [3] [4]
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

1. GRCh38: Ensembl release 89: ENSG00000148834 - Ensembl, May 2017
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.
5. Board PG, Coggan M, Chelvanayagam G, Easteal S, Jermiin LS, Schulte GK, et al. (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.
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.
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". Gluthione Transferases and Gamma-Glutamyl Transpeptidases. Methods in Enzymology. Vol. 401. pp.  78–99. doi:10.1016/S0076-6879(05)01005-0. ISBN   978-0-12-182806-6. PMID   16399380.

Further reading

• Matoba R, Okubo K, Hori N, Atsushi F, Kenichi M (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, Derge JG, Klausner RD, Collins FS, 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, Makino Y, Seko Y, Hanioka N, 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, Vidrine A, Klimecki WT (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, Martin ER, Stenger JE, Scherzer CR, 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, Le Couteur DG, Board PG (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, Rubenfield M, French L, Steward CA, 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, Shenmen CM, Grouse LH, Schuler G, 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, Jessen F, Wüllner U, Harbrecht U, 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, Dekosky ST, Kamboh MI (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, Haenig C, Brembeck FH, Goehler H, 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, Soini Y, Salmenkivi KM, Board PG, 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, Orantes M, Birkenmeier G, Griffin WS, 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.