Atlas of Genetics and Cytogenetics in Oncology and Haematology


Home   Genes   Leukemias   Solid Tumors   Cancer-Prone   Deep Insight   Case Reports   Journals  Portal   Teaching   

X Y 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 NA

GSTA1 (glutathione S-transferase alpha 1)

Written2014-01Ana Savic-Radojevic, Tanja Radic
Institute of Medical, Clinical Biochemistry, Faculty of Medicine, University of Belgrade, Serbia

(Note : for Links provided by Atlas : click)

Identity

Alias_namesglutathione S-transferase A1
Other aliasGST2
GSTA1-1
GTH1
HGNC (Hugo) GSTA1
LocusID (NCBI) 2938
Atlas_Id 40764
Location 6p12.2  [Link to chromosome band 6p12]
Location_base_pair Starts at 52791380 and ends at 52803967 bp from pter ( according to hg19-Feb_2009)  [Mapping GSTA1.png]
Local_order Between the LOC647169 (similar to glutathione transferase) and GSTA6P (glutathione S-transferase alpha 6 pseudogene) (according to PubMed).
Fusion genes
(updated 2016)
GSTA1 (6p12.2) / ZNF548 (19q13.43)
Note The GSTA1 gene is composed of 7 exons spanning a region of 12487 bases.

DNA/RNA

Note The human alpha class genes are located in a cluster on chromosome 6p12 and comprise five functional genes (GSTA1, GSTA2, GSTA3, GSTA4, GSTA5) and seven pseudogenes (Morel et al., 2002).
 
  GSTA1 gene. The GSTA1 gene spans a region of 12,5 kb composed of the seven exons (red) and six introns (green). Exons 1, 2, 3, 4, 5, 6 and 7 are 59 bp, 117 bp, 52 bp, 133 bp, 142 bp, 132 bp and 198 bp in length, respectively.
Description The GSTA1 gene is approximately 12 kb in length and is closely flanked by other alpha class gene sequences. The complete sequence of the 1,7-kb intergenic region between exon 7 of an upstream pseudogene and exon 1 of the GSTA1 gene has been determined (Suzuki et al., 1993).
Transcription The 1276-nucleotide transcript encodes a protein of 222 amino acid residues.
Pseudogene An additional gene that encodes an uncharacterized Alpha class GST has been identified. The protein derived from this gene would have 19 amino acid substitutions compared with the GSTA1 isoenzyme. Several pseudogenes with single-base and/or complete exon deletions have been identified, but no reverse-transcribed pseudogenes have been detected (Suzuki et al., 1993).
Polymorphisms: GSTA1 has a functional three apparently linked single nucleotide polymorphisms (SNPs) in an SP1-responsive element within the proximal promoter (G-52A, C-69T and T-567G), plus at least four SNPs further upstream and a silent SNP A-375G. Two variants, GSTA1*A (-567T, -69C,-52G) and GSTA1*B (-67G, -69T, -52A), have been named according to the linked functional SNPs. Specifically, these substitutions result in differential expression with lower transcriptional activation of variant GSTA1*B than common GSTA1*A allele. It has been suggested that this genetic variation can change an individual's susceptibility to carcinogens and toxins, as well as, affect the efficacy of some drugs (Coles and Kadlubar, 2003). In addition, the linkage disequilibrium between GSTA1*A/GSTA1*B and GSTA2G335C (Ser112Thr) has been shown in Caucasians: specifically, GSTA1*A/GSTA2C335 (Thr112) and GSTA1*B/GSTA2G335 (Ser112) (Ning et al., 2004). It seems that the higher hepatic expression of GSTA1 enzyme in homozygous GSTA1 individuals is associated with the lower hepatic expression of GSTA2 in GSTA2C335 (Thr112) individuals (Coles et al., 2001a; Ning et al., 2004). Other haplotypes within this nomenclature but including SNPs C-115T, T-631G, and C-1142G also have been proposed (Bredschneider et al., 2002; Guy et al., 2004). Polymorphisms upstream of G-52C seem to have little effect on GSTA1 expression (Morel et al., 2002).

Protein

Note Glutathione S-transferase A1 is N-terminally processed.
Amino acids: 222.
Calculated molecular mass: 25,63 kDa.
 
  Crystal structure of human glutathione transferase (GST) A1-1 in complex with glutathione. Adapted from PDB (Grahn et al., 2006).
Description The active GSTA1-1 enzyme is a homodimer, with each subunit containing a GSH-binding site (G-site) and a second adjacent hydrophobic binding site for the electrophilic substrate (H-site) (Wilce and Parker, 1994). The C-terminal region of GSTA1-1 contributes to the catalytic and noncatalytic ligand-binding functions of the enzyme, while the conserved G-site is located in the N-terminal domain (Balogh et al., 2009). Protein flexibility and dynamics in a molten globule-active site including the C-terminal α9 helix and the protruding ends of the α4-α5 helices result in achieving remarkable catalytic promiscuity of GSTA1-1 (Wu and Dong, 2012; Honaker et al., 2013). It has been proposed that the α9 helix may function as a mobile gate to the active-site cavity, controlling substrate access and product release.
 
  Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the MU and PI class enzymes. Adapted from PDB (Sinning et al., 1993).
Expression GSTA1-1 is highly expressed (as mRNA and protein) in liver, intestine, kidney, adrenal gland, pancreas and testis, while expression in a wide range of tissues is low (Hayes and Pulford, 1995; Coles et al., 2001a). Both positive and negative regulatory regions are present in the 5` noncoding region of GSTA1, including a polymorphic SP1-binding site within the proximal promoter. Binding of the transcription factor AP1 has been suggested as a common mechanism for up-regulation of GSTs (Hayes and Pulford, 1995). The results of recent study also implied the role of a Kelch-like ECH-associated protein 1 (Keap1)-dependent signaling pathway for the induction of the constitutive GSTA1 expression during epithelial cell differentiation (Kusano et al., 2008). Regarding GSH-dependent Δ54 isomerase activity of this class of enzyme, it has been shown that steroidogenic factor 1 (SF-1) is involved in regulation of expression of GSTA genes (Matsumura et al., 2013). Aberrant overexpression has been observed in various malignancies such as colorectal (Hengstler et al., 1998) and lung cancer (Carmichael et al., 1988), while decrease in alpha class GSTs has been observed in stomach and liver tumors (Howie et al., 1990). A detailed recent review on GSTA1 can be found in Wu and Dong, 2012.
Localisation Cytosolic.
Function Human GSTA1-1 enzyme catalyzes the GSH-dependent detoxification of electrophiles showing highly promiscuous substrate selectivity for many structurally unrelated chemicals, including environmental carcinogens (e.g. benzo(a)pyrene diol epoxides), several alkylating chemotherapeutic agents (such as busulfan, chlorambucil, melphalan, phosphoramide mustard, cyclophosphamide, thiotepa), as well as, steroids and products of lipid degradation. GSTA1-1 is the most highly expressed GST of the liver and could therefore, be critical for "systemic" detoxification of electrophilic xenobiotics including carcinogens and drugs (Coles and Kadlubar, 2005). In addition to enzymatic detoxification, GSTA1 acts as modulator of mitogen-activated protein kinase (MAPK) signal transduction pathway via a mechanism involving protein-protein interactions. Namely, GSTA1 forms complexes with c-Jun N-terminal kinase (JNK), modifying JNK activation during cellular stress (Adnan et al., 2012). Thus, it is possible that GSTA1 confer drug resistance by two distinct means: by direct inactivation (detoxification) of chemotherapeutic drugs and by acting as inhibitors of MAPK pathway.
Homology The alpha class GSTs is showing strong intra-class sequence similarity (Balogh et al., 2009).

Mutations

Germinal None described so far.
Somatic 36 mutations (COSMIC): 26 substitution-missense, 4 substitution-nonsense, 5 substitution-coding silent, 1 unknown type.

Implicated in

Note
  
Entity Colorectal cancer
Note Regarding the role of GSTA1 polymorphism in the risk of colorectal cancer, the results of epidemiological studies are still inconclusive. Several studies showed that GSTA1*B genotype (low hepatic expression) is associated with increased susceptibility to colorectal cancer, which imply the possible inefficient hepatic detoxification of food-derived carcinogen metabolite N-acetoxy-PhIP (Coles et al., 2001b; Sweeney et al., 2002). In contrast, meta-analysis of Economopoulos representing the pooled analysis of four studies (1648 cases, 2039 controls) does not confer this association.
  
  
Entity Breast cancer
Note The role of GSTA1 polymorphism in breast cancer risk was mainly based on investigation on response to chemotherapeutic drugs in these patients. In breast cancer patients on cyclophosphamide containing chemotherapy carriers of GSTA1*B/*B genotype showed significantly reduced five years risk of death in comparison to GSTA1*A homozygous carriers. This association was likely caused by decreased detoxification of the therapeutic metabolites of cyclophosphamide in GSTA1*B/*B patients (Sweeney et al., 2003).
  
  
Entity Bladder cancer
Note Recent investigation indicates that the GSTA1-low activity genotype in combination with the GSTM1-null genotype significantly increases the risk of bladder cancer in smokers (Matic et al., 2013). In addition, it seems that GSTA1 polymorphism may influence vulnerability to oxidative DNA damage, thereby contributing to the malignant potential of transitional cell carcinoma (Savic-Radojevic et al., 2013).
  
  
Entity Myeloid leukemia
Note Aberant overexpression of both GSTA1 and GSTA2 proteins was found in blast cells derived from acute myeloid leukemia patients, showing resistance to doxorubicin in vitro (Sargent et al., 1999). In addition, GSTA1 and CYP39A1 (member of cytochrome P450 family) polymorphisms were found to be associated with pharmacokinetics of busulfan, which is used in preparative regimens prior to stem cell transplantation in pediatric patients (ten Brink et al., 2013).
  
  
Entity Prostate cancer
Note Genetic variants of GSTA1 and GSTT1 may modify prostate cancer risk, especially among smokers (Komiya et al., 2005).
  
  
Entity Asthma
Note Genetic alterations in GST enzymes may influence the detoxification of environmental toxic substances in airway and increase the risk of asthma. Thus, it has been shown that subjects with at least one allele -69T in the GSTA1 genotype have an increased risk of asthma (Polimanti et al., 2010).
  

Bibliography

The effect of menadione on glutathione S-transferase A1 (GSTA1): c-Jun N-terminal kinase (JNK) complex dissociation in human colonic adenocarcinoma Caco-2 cells.
Adnan H, Antenos M, Kirby GM.
Toxicol Lett. 2012 Oct 2;214(1):53-62. doi: 10.1016/j.toxlet.2012.08.007. Epub 2012 Aug 13.
PMID 22906494
 
Structural analysis of a glutathione transferase A1-1 mutant tailored for high catalytic efficiency with toxic alkenals.
Balogh LM, Le Trong I, Kripps KA, Tars K, Stenkamp RE, Mannervik B, Atkins WM.
Biochemistry. 2009 Aug 18;48(32):7698-704. doi: 10.1021/bi900895b.
PMID 19618965
 
Genetic polymorphisms of glutathione S-transferase A1, the major glutathione S-transferase in human liver: consequences for enzyme expression and busulfan conjugation.
Bredschneider M, Klein K, Murdter TE, Marx C, Eichelbaum M, Nussler AK, Neuhaus P, Zanger UM, Schwab M.
Clin Pharmacol Ther. 2002 Jun;71(6):479-87.
PMID 12087351
 
Glutathione S-transferase isoenzymes and glutathione peroxidase activity in normal and tumour samples from human lung.
Carmichael J, Forrester LM, Lewis AD, Hayes JD, Hayes PC, Wolf CR.
Carcinogenesis. 1988 Sep;9(9):1617-21.
PMID 3409465
 
The role of human glutathione S-transferases (hGSTs) in the detoxification of the food-derived carcinogen metabolite N-acetoxy-PhIP, and the effect of a polymorphism in hGSTA1 on colorectal cancer risk.
Coles B, Nowell SA, MacLeod SL, Sweeney C, Lang NP, Kadlubar FF.
Mutat Res. 2001b Oct 1;482(1-2):3-10.
PMID 11535243
 
Human alpha class glutathione S-transferases: genetic polymorphism, expression, and susceptibility to disease.
Coles BF, Kadlubar FF.
Methods Enzymol. 2005;401:9-42. (REVIEW)
PMID 16399377
 
Effect of polymorphism in the human glutathione S-transferase A1 promoter on hepatic GSTA1 and GSTA2 expression.
Coles BF, Morel F, Rauch C, Huber WW, Yang M, Teitel CH, Green B, Lang NP, Kadlubar FF.
Pharmacogenetics. 2001a Nov;11(8):663-9.
PMID 11692074
 
GSTM1, GSTT1, GSTP1, GSTA1 and colorectal cancer risk: a comprehensive meta-analysis.
Economopoulos KP, Sergentanis TN.
Eur J Cancer. 2010 Jun;46(9):1617-31. doi: 10.1016/j.ejca.2010.02.009. Epub 2010 Mar 6. (REVIEW)
PMID 20207535
 
New crystal structures of human glutathione transferase A1-1 shed light on glutathione binding and the conformation of the C-terminal helix.
Grahn E, Novotny M, Jakobsson E, Gustafsson A, Grehn L, Olin B, Madsen D, Wahlberg M, Mannervik B, Kleywegt GJ.
Acta Crystallogr D Biol Crystallogr. 2006 Feb;62(Pt 2):197-207. Epub 2006 Jan 18.
PMID 16421451
 
Promoter polymorphisms in glutathione-S-transferase genes affect transcription.
Guy CA, Hoogendoorn B, Smith SK, Coleman S, O'Donovan MC, Buckland PR.
Pharmacogenetics. 2004 Jan;14(1):45-51.
PMID 15128050
 
The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance.
Hayes JD, Pulford DJ.
Crit Rev Biochem Mol Biol. 1995;30(6):445-600. (REVIEW)
PMID 8770536
 
Resistance factors in colon cancer tissue and the adjacent normal colon tissue: glutathione S-transferases alpha and pi, glutathione and aldehyde dehydrogenase.
Hengstler JG, Bottger T, Tanner B, Dietrich B, Henrich M, Knapstein PG, Junginger T, Oesch F.
Cancer Lett. 1998 Jun 5;128(1):105-12.
PMID 9652800
 
Enzymatic detoxication, conformational selection, and the role of molten globule active sites.
Honaker MT, Acchione M, Zhang W, Mannervik B, Atkins WM.
J Biol Chem. 2013 Jun 21;288(25):18599-611. doi: 10.1074/jbc.M112.445767. Epub 2013 May 6.
PMID 23649628
 
Glutathione S-transferase and glutathione peroxidase expression in normal and tumour human tissues.
Howie AF, Forrester LM, Glancey MJ, Schlager JJ, Powis G, Beckett GJ, Hayes JD, Wolf CR.
Carcinogenesis. 1990 Mar;11(3):451-8.
PMID 2311189
 
Human glutathione S-transferase A1, T1, M1, and P1 polymorphisms and susceptibility to prostate cancer in the Japanese population.
Komiya Y, Tsukino H, Nakao H, Kuroda Y, Imai H, Katoh T.
J Cancer Res Clin Oncol. 2005 Apr;131(4):238-42. Epub 2004 Dec 23.
PMID 15616829
 
Keap1 regulates the constitutive expression of GST A1 during differentiation of Caco-2 cells.
Kusano Y, Horie S, Shibata T, Satsu H, Shimizu M, Hitomi E, Nishida M, Kurose H, Itoh K, Kobayashi A, Yamamoto M, Uchida K.
Biochemistry. 2008 Jun 10;47(23):6169-77. doi: 10.1021/bi800199z. Epub 2008 May 14.
PMID 18476723
 
GSTA1, GSTM1, GSTP1, and GSTT1 polymorphisms and susceptibility to smoking-related bladder cancer: a case-control study.
Matic M, Pekmezovic T, Djukic T, Mimic-Oka J, Dragicevic D, Krivic B, Suvakov S, Savic-Radojevic A, Pljesa-Ercegovac M, Tulic C, Coric V, Simic T.
Urol Oncol. 2013 Oct;31(7):1184-92. doi: 10.1016/j.urolonc.2011.08.005.
PMID 24075358
 
Human glutathione S-transferase A (GSTA) family genes are regulated by steroidogenic factor 1 (SF-1) and are involved in steroidogenesis.
Matsumura T, Imamichi Y, Mizutani T, Ju Y, Yazawa T, Kawabe S, Kanno M, Ayabe T, Katsumata N, Fukami M, Inatani M, Akagi Y, Umezawa A, Ogata T, Miyamoto K.
FASEB J. 2013 Aug;27(8):3198-208. doi: 10.1096/fj.12-222745. Epub 2013 May 6.
PMID 23650189
 
The human glutathione transferase alpha locus: genomic organization of the gene cluster and functional characterization of the genetic polymorphism in the hGSTA1 promoter.
Morel F, Rauch C, Coles B, Le Ferrec E, Guillouzo A.
Pharmacogenetics. 2002 Jun;12(4):277-86.
PMID 12042665
 
Human glutathione S-transferase A2 polymorphisms: variant expression, distribution in prostate cancer cases/controls and a novel form.
Ning B, Wang C, Morel F, Nowell S, Ratnasinghe DL, Carter W, Kadlubar FF, Coles B.
Pharmacogenetics. 2004 Jan;14(1):35-44.
PMID 15128049
 
GSTA1, GSTO1 and GSTO2 gene polymorphisms in Italian asthma patients.
Polimanti R, Piacentini S, Moscatelli B, Pellicciotti L, Manfellotto D, Fuciarelli M.
Clin Exp Pharmacol Physiol. 2010 Aug;37(8):870-2. doi: 10.1111/j.1440-1681.2010.05385.x. Epub 2010 Mar 30.
PMID 20374258
 
Evidence for the involvement of the glutathione pathway in drug resistance in AML.
Sargent JM, Williamson C, Hall AG, Elgie AW, Taylor CG.
Adv Exp Med Biol. 1999;457:205-9.
PMID 10500795
 
GSTM1-null and GSTA1-low activity genotypes are associated with enhanced oxidative damage in bladder cancer.
Savic-Radojevic A, Djukic T, Simic T, Pljesa-Ercegovac M, Dragicevic D, Pekmezovic T, Cekerevac M, Santric V, Matic M.
Redox Rep. 2013;18(1):1-7.
PMID 23394311
 
Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes.
Sinning I, Kleywegt GJ, Cowan SW, Reinemer P, Dirr HW, Huber R, Gilliland GL, Armstrong RN, Ji X, Board PG, et al.
J Mol Biol. 1993 Jul 5;232(1):192-212.
PMID 8331657
 
Structure and organization of the human alpha class glutathione S-transferase genes and related pseudogenes.
Suzuki T, Johnston PN, Board PG.
Genomics. 1993 Dec;18(3):680-6.
PMID 8307579
 
Association between a glutathione S-transferase A1 promoter polymorphism and survival after breast cancer treatment.
Sweeney C, Ambrosone CB, Joseph L, Stone A, Hutchins LF, Kadlubar FF, Coles BF.
Int J Cancer. 2003 Mar 1;103(6):810-4.
PMID 12516103
 
Novel markers of susceptibility to carcinogens in diet: associations with colorectal cancer.
Sweeney C, Coles BF, Nowell S, Lang NP, Kadlubar FF.
Toxicology. 2002 Dec 27;181-182:83-7.
PMID 12505289
 
Structure and function of glutathione S-transferases.
Wilce MC, Parker MW.
Biochim Biophys Acta. 1994 Mar 16;1205(1):1-18. (REVIEW)
PMID 8142473
 
Human cytosolic glutathione transferases: structure, function, and drug discovery.
Wu B, Dong D.
Trends Pharmacol Sci. 2012 Dec;33(12):656-68. doi: 10.1016/j.tips.2012.09.007. Epub 2012 Oct 31. (REVIEW)
PMID 23121834
 
Effect of genetic variants GSTA1 and CYP39A1 and age on busulfan clearance in pediatric patients undergoing hematopoietic stem cell transplantation.
ten Brink MH1, van Bavel T, Swen JJ, van der Straaten T, Bredius RG, Lankester AC, Zwaveling J, Guchelaar HJ.
Pharmacogenomics. 2013 Nov;14(14):1683-90. doi: 10.2217/pgs.13.159.
PMID 24192117
 

Citation

This paper should be referenced as such :
A Savic-Radojevic, T Radic
GSTA1 (glutathione S-transferase alpha 1)
Atlas Genet Cytogenet Oncol Haematol. 2014;18(9):645-649.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/GSTA1ID40764ch6p12.html


External links

Nomenclature
HGNC (Hugo)GSTA1   4626
Cards
AtlasGSTA1ID40764ch6p12
Entrez_Gene (NCBI)GSTA1  2938  glutathione S-transferase alpha 1
AliasesGST-epsilon; GST2; GSTA1-1; GTH1
GeneCards (Weizmann)GSTA1
Ensembl hg19 (Hinxton)ENSG00000243955 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000243955 [Gene_View]  chr6:52791380-52803967 [Contig_View]  GSTA1 [Vega]
ICGC DataPortalENSG00000243955
TCGA cBioPortalGSTA1
AceView (NCBI)GSTA1
Genatlas (Paris)GSTA1
WikiGenes2938
SOURCE (Princeton)GSTA1
Genetics Home Reference (NIH)GSTA1
Genomic and cartography
GoldenPath hg38 (UCSC)GSTA1  -     chr6:52791380-52803967 -  6p12.2   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)GSTA1  -     6p12.2   [Description]    (hg19-Feb_2009)
EnsemblGSTA1 - 6p12.2 [CytoView hg19]  GSTA1 - 6p12.2 [CytoView hg38]
Mapping of homologs : NCBIGSTA1 [Mapview hg19]  GSTA1 [Mapview hg38]
OMIM138359   
Gene and transcription
Genbank (Entrez)AK293371 AK310324 AL096729 AY532928 BC053578
RefSeq transcript (Entrez)NM_001319059 NM_145740
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)GSTA1
Cluster EST : UnigeneHs.446309 [ NCBI ]
CGAP (NCI)Hs.446309
Alternative Splicing GalleryENSG00000243955
Gene ExpressionGSTA1 [ NCBI-GEO ]   GSTA1 [ EBI - ARRAY_EXPRESS ]   GSTA1 [ SEEK ]   GSTA1 [ MEM ]
Gene Expression Viewer (FireBrowse)GSTA1 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)2938
GTEX Portal (Tissue expression)GSTA1
Protein : pattern, domain, 3D structure
UniProt/SwissProtP08263   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP08263  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP08263
Splice isoforms : SwissVarP08263
Catalytic activity : Enzyme2.5.1.18 [ Enzyme-Expasy ]   2.5.1.182.5.1.18 [ IntEnz-EBI ]   2.5.1.18 [ BRENDA ]   2.5.1.18 [ KEGG ]   
PhosPhoSitePlusP08263
Domaine pattern : Prosite (Expaxy)GST_CTER (PS50405)    GST_NTER (PS50404)   
Domains : Interpro (EBI)Glutathione-S-Trfase_C-like    Glutathione_S-Trfase_N    GST_alpha    GST_C    Thioredoxin-like_fold   
Domain families : Pfam (Sanger)GST_C (PF00043)    GST_N (PF02798)   
Domain families : Pfam (NCBI)pfam00043    pfam02798   
Conserved Domain (NCBI)GSTA1
DMDM Disease mutations2938
Blocks (Seattle)GSTA1
PDB (SRS)1GSD    1GSE    1GSF    1GUH    1K3L    1K3O    1K3Y    1LBK    1PKW    1PKZ    1PL1    1PL2    1USB    1XWG    1YDK    2R3X    2R6K    3I69    3I6A    3IK9    3KTL    3L0H    3Q74    3U6V    3ZFB    3ZFL    4HJ2    5JCU    5LCZ    5LD0   
PDB (PDBSum)1GSD    1GSE    1GSF    1GUH    1K3L    1K3O    1K3Y    1LBK    1PKW    1PKZ    1PL1    1PL2    1USB    1XWG    1YDK    2R3X    2R6K    3I69    3I6A    3IK9    3KTL    3L0H    3Q74    3U6V    3ZFB    3ZFL    4HJ2    5JCU    5LCZ    5LD0   
PDB (IMB)1GSD    1GSE    1GSF    1GUH    1K3L    1K3O    1K3Y    1LBK    1PKW    1PKZ    1PL1    1PL2    1USB    1XWG    1YDK    2R3X    2R6K    3I69    3I6A    3IK9    3KTL    3L0H    3Q74    3U6V    3ZFB    3ZFL    4HJ2    5JCU    5LCZ    5LD0   
PDB (RSDB)1GSD    1GSE    1GSF    1GUH    1K3L    1K3O    1K3Y    1LBK    1PKW    1PKZ    1PL1    1PL2    1USB    1XWG    1YDK    2R3X    2R6K    3I69    3I6A    3IK9    3KTL    3L0H    3Q74    3U6V    3ZFB    3ZFL    4HJ2    5JCU    5LCZ    5LD0   
Structural Biology KnowledgeBase1GSD    1GSE    1GSF    1GUH    1K3L    1K3O    1K3Y    1LBK    1PKW    1PKZ    1PL1    1PL2    1USB    1XWG    1YDK    2R3X    2R6K    3I69    3I6A    3IK9    3KTL    3L0H    3Q74    3U6V    3ZFB    3ZFL    4HJ2    5JCU    5LCZ    5LD0   
SCOP (Structural Classification of Proteins)1GSD    1GSE    1GSF    1GUH    1K3L    1K3O    1K3Y    1LBK    1PKW    1PKZ    1PL1    1PL2    1USB    1XWG    1YDK    2R3X    2R6K    3I69    3I6A    3IK9    3KTL    3L0H    3Q74    3U6V    3ZFB    3ZFL    4HJ2    5JCU    5LCZ    5LD0   
CATH (Classification of proteins structures)1GSD    1GSE    1GSF    1GUH    1K3L    1K3O    1K3Y    1LBK    1PKW    1PKZ    1PL1    1PL2    1USB    1XWG    1YDK    2R3X    2R6K    3I69    3I6A    3IK9    3KTL    3L0H    3Q74    3U6V    3ZFB    3ZFL    4HJ2    5JCU    5LCZ    5LD0   
SuperfamilyP08263
Human Protein AtlasENSG00000243955
Peptide AtlasP08263
HPRD00708
IPIIPI00657682   
Protein Interaction databases
DIP (DOE-UCLA)P08263
IntAct (EBI)P08263
FunCoupENSG00000243955
BioGRIDGSTA1
STRING (EMBL)GSTA1
ZODIACGSTA1
Ontologies - Pathways
QuickGOP08263
Ontology : AmiGOglutathione transferase activity  glutathione transferase activity  glutathione transferase activity  glutathione peroxidase activity  cytosol  cytosol  glutathione metabolic process  metabolic process  epithelial cell differentiation  linoleic acid metabolic process  extracellular exosome  cellular oxidant detoxification  glutathione derivative biosynthetic process  
Ontology : EGO-EBIglutathione transferase activity  glutathione transferase activity  glutathione transferase activity  glutathione peroxidase activity  cytosol  cytosol  glutathione metabolic process  metabolic process  epithelial cell differentiation  linoleic acid metabolic process  extracellular exosome  cellular oxidant detoxification  glutathione derivative biosynthetic process  
Pathways : KEGGGlutathione metabolism    Metabolism of xenobiotics by cytochrome P450    Drug metabolism - cytochrome P450    Chemical carcinogenesis   
REACTOMEP08263 [protein]
REACTOME PathwaysR-HSA-156590 [pathway]   
NDEx NetworkGSTA1
Atlas of Cancer Signalling NetworkGSTA1
Wikipedia pathwaysGSTA1
Orthology - Evolution
OrthoDB2938
GeneTree (enSembl)ENSG00000243955
Phylogenetic Trees/Animal Genes : TreeFamGSTA1
HOVERGENP08263
HOGENOMP08263
Homologs : HomoloGeneGSTA1
Homology/Alignments : Family Browser (UCSC)GSTA1
Gene fusions - Rearrangements
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerGSTA1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)GSTA1
dbVarGSTA1
ClinVarGSTA1
1000_GenomesGSTA1 
Exome Variant ServerGSTA1
ExAC (Exome Aggregation Consortium)GSTA1 (select the gene name)
Genetic variants : HAPMAP2938
Genomic Variants (DGV)GSTA1 [DGVbeta]
DECIPHERGSTA1 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisGSTA1 
Mutations
ICGC Data PortalGSTA1 
TCGA Data PortalGSTA1 
Broad Tumor PortalGSTA1
OASIS PortalGSTA1 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICGSTA1  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDGSTA1
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch GSTA1
DgiDB (Drug Gene Interaction Database)GSTA1
DoCM (Curated mutations)GSTA1 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)GSTA1 (select a term)
intoGenGSTA1
NCG5 (London)GSTA1
Cancer3DGSTA1(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM138359   
Orphanet
MedgenGSTA1
Genetic Testing Registry GSTA1
NextProtP08263 [Medical]
TSGene2938
GENETestsGSTA1
Target ValidationGSTA1
Huge Navigator GSTA1 [HugePedia]
snp3D : Map Gene to Disease2938
BioCentury BCIQGSTA1
ClinGenGSTA1
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD2938
Chemical/Pharm GKB GenePA29016
Clinical trialGSTA1
Miscellaneous
canSAR (ICR)GSTA1 (select the gene name)
Probes
Litterature
PubMed199 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineGSTA1
EVEXGSTA1
GoPubMedGSTA1
iHOPGSTA1
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

Search in all EBI   NCBI

© Atlas of Genetics and Cytogenetics in Oncology and Haematology
indexed on : Fri Jun 30 11:08:11 CEST 2017

Home   Genes   Leukemias   Solid Tumors   Cancer-Prone   Deep Insight   Case Reports   Journals  Portal   Teaching   

For comments and suggestions or contributions, please contact us

jlhuret@AtlasGeneticsOncology.org.