Glutathione S-transferase A2
Details
- Name
- Glutathione S-transferase A2
- Synonyms
- 2.5.1.18
- GST class-alpha member 2
- GST HA subunit 2
- GST-gamma
- GST2
- GSTA2-2
- GTH2
- Gene Name
- GSTA2
- Organism
- Humans
- Amino acid sequence
>lcl|BSEQ0011580|Glutathione S-transferase A2 MAEKPKLHYSNIRGRMESIRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLMFQQVPMVEI DGMKLVQTRAILNYIASKYNLYGKDIKEKALIDMYIEGIADLGEMILLLPFSQPEEQDAK LALIQEKTKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLVELLYYVEELDSSLISSFPL LKALKTRISNLPTVKKFLQPGSPRKPPMDEKSLEESRKIFRF
- Number of residues
- 222
- Molecular Weight
- 25663.675
- Theoretical pI
- 9.07
- GO Classification
- Functionsglutathione transferase activityProcessesepithelial cell differentiation / glutathione derivative biosynthetic process / glutathione metabolic process / small molecule metabolic process / xenobiotic metabolic processComponentscytosol / extracellular exosome
- General Function
- Glutathione transferase activity
- Specific Function
- Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0011581|Glutathione S-transferase A2 (GSTA2) ATGGCAGAGAAGCCCAAGCTCCACTACTCCAATATACGGGGCAGAATGGAGTCCATCCGG TGGCTCCTGGCTGCAGCTGGAGTAGAGTTTGAAGAGAAATTTATAAAATCTGCAGAAGAT TTGGACAAGTTAAGAAATGATGGATATTTGATGTTCCAGCAAGTGCCAATGGTTGAGATT GATGGGATGAAGCTGGTGCAGACCAGAGCCATTCTCAACTACATTGCCAGCAAATACAAC CTCTATGGGAAAGACATAAAGGAGAAAGCCCTGATTGATATGTATATAGAAGGTATAGCA GATTTGGGTGAAATGATCCTTCTTCTGCCCTTTAGTCAACCTGAGGAACAAGATGCCAAG CTTGCCTTGATCCAAGAGAAAACAAAAAATCGCTACTTCCCTGCCTTTGAAAAAGTCTTA AAGAGCCACGGACAAGACTACCTTGTTGGCAACAAGCTGAGCCGGGCTGACATTCACCTG GTGGAACTTCTCTACTACGTGGAAGAGCTTGACTCTAGCCTTATTTCCAGCTTCCCTCTG CTGAAGGCCCTGAAAACCAGAATCAGTAACCTGCCCACAGTGAAGAAGTTTCTACAGCCT GGCAGCCCAAGGAAGCCTCCCATGGATGAGAAATCTTTAGAAGAATCAAGGAAGATTTTC AGGTTTTAA
- Chromosome Location
- 6
- Locus
- 6p12.1
- External Identifiers
Resource Link UniProtKB ID P09210 UniProtKB Entry Name GSTA2_HUMAN GenBank Protein ID 306811 GenBank Gene ID M16594 GenAtlas ID GSTA2 HGNC ID HGNC:4627 - General References
- Rhoads DM, Zarlengo RP, Tu CP: The basic glutathione S-transferases from human livers are products of separate genes. Biochem Biophys Res Commun. 1987 May 29;145(1):474-81. [Article]
- Rohrdanz E, Nguyen T, Pickett CB: Isolation and characterization of the human glutathione S-transferase A2 subunit gene. Arch Biochem Biophys. 1992 Nov 1;298(2):747-52. [Article]
- Klone A, Hussnatter R, Sies H: Cloning, sequencing and characterization of the human alpha glutathione S-transferase gene corresponding to the cDNA clone pGTH2. Biochem J. 1992 Aug 1;285 ( Pt 3):925-8. [Article]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [Article]
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- Ahmad H, Singhal SS, Saxena M, Awasthi YC: Characterization of two novel subunits of the alpha-class glutathione S-transferases of human liver. Biochim Biophys Acta. 1993 Feb 13;1161(2-3):333-6. [Article]
- Hayes JD, Kerr LA, Cronshaw AD: Evidence that glutathione S-transferases B1B1 and B2B2 are the products of separate genes and that their expression in human liver is subject to inter-individual variation. Molecular relationships between the B1 and B2 subunits and other Alpha class glutathione S-transferases. Biochem J. 1989 Dec 1;264(2):437-45. [Article]
- Zeng K, Rose JP, Chen HC, Strickland CL, Tu CP, Wang BC: A surface mutant (G82R) of a human alpha-glutathione S-transferase shows decreased thermal stability and a new mode of molecular association in the crystal. Proteins. 1994 Nov;20(3):259-63. [Article]
- Tars K, Olin B, Mannervik B: Structural basis for featuring of steroid isomerase activity in alpha class glutathione transferases. J Mol Biol. 2010 Mar 19;397(1):332-40. doi: 10.1016/j.jmb.2010.01.023. Epub 2010 Jan 18. [Article]
- Tetlow N, Liu D, Board P: Polymorphism of human Alpha class glutathione transferases. Pharmacogenetics. 2001 Oct;11(7):609-17. [Article]
- Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB00608 Chloroquine approved, investigational, vet_approved unknown inhibitor Details DB00143 Glutathione approved, investigational, nutraceutical unknown Details DB00143 Glutathione approved, investigational, nutraceutical unknown substrate Details DB00163 Vitamin E approved, nutraceutical, vet_approved unknown inducer Details DB00636 Clofibrate approved, investigational unknown inhibitor Details DB00903 Etacrynic acid approved, investigational unknown inhibitor Details DB01008 Busulfan approved, investigational unknown substrate Details DB00993 Azathioprine approved unknown substrate Details DB14001 alpha-Tocopherol succinate approved, nutraceutical, vet_approved unknown inducer Details DB14002 D-alpha-Tocopherol acetate approved, nutraceutical, vet_approved unknown inducer Details DB03310 Glutathione disulfide approved, experimental, investigational unknown activator Details DB03619 Deoxycholic acid approved unknown inhibitor Details DB00321 Amitriptyline approved unknown inhibitor Details DB00291 Chlorambucil approved unknown substrate Details