Misplaced Pages

GSTA2

Article snapshot taken from Wikipedia with creative commons attribution-sharealike license. Give it a read and then ask your questions in the chat. We can research this topic together.
Protein-coding gene in the species Homo sapiens
GSTA2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1AGS, 2VCT, 2WJU, 4ACS

Identifiers
AliasesGSTA2, GST2, GSTA2-2, GTA2, GTH2, glutathione S-transferase alpha 2
External IDsOMIM: 138360; MGI: 95863; HomoloGene: 47952; GeneCards: GSTA2; OMA:GSTA2 - orthologs
Gene location (Human)
Chromosome 6 (human)
Chr.Chromosome 6 (human)
Chromosome 6 (human)Genomic location for GSTA2Genomic location for GSTA2
Band6p12.2Start52,750,087 bp
End52,763,475 bp
Gene location (Mouse)
Chromosome 9 (mouse)
Chr.Chromosome 9 (mouse)
Chromosome 9 (mouse)Genomic location for GSTA2Genomic location for GSTA2
Band9 E1|9 43.65 cMStart78,238,300 bp
End78,263,070 bp
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • body of pancreas

  • duodenum

  • olfactory zone of nasal mucosa

  • gallbladder

  • islet of Langerhans

  • liver

  • human kidney

  • right lobe of liver

  • right testis

  • left testis
Top expressed in
  • epithelium of stomach

  • right kidney

  • conjunctival fornix

  • human kidney

  • transitional epithelium of urinary bladder

  • left lobe of liver

  • mucous cell of stomach

  • esophagus

  • skin of external ear

  • retinal pigment epithelium
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

2939

14858

Ensembl

ENSG00000244067

ENSMUSG00000057933

UniProt

P09210

P10648

RefSeq (mRNA)

NM_000846

NM_008182

RefSeq (protein)

NP_000837

NP_032208

Location (UCSC)Chr 6: 52.75 – 52.76 MbChr 9: 78.24 – 78.26 Mb
PubMed search
Wikidata
View/Edit HumanView/Edit Mouse

Glutathione S-transferase A2 is an enzyme that in humans is encoded by the GSTA2 gene.

Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. These enzymes function in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding these enzymes are known to be highly polymorphic. These genetic variations can change an individual's susceptibility to carcinogens and toxins as well as affect the toxicity and efficacy of some drugs. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. This gene encodes a glutathione S-transferase belonging to the alpha class. The alpha class genes, located in a cluster mapped to chromosome 6, are the most abundantly expressed glutathione S-transferases in liver. In addition to metabolizing bilirubin and certain anti-cancer drugs in the liver, the alpha class of these enzymes exhibit glutathione peroxidase activity thereby protecting the cells from reactive oxygen species and the products of peroxidation.

References

  1. ^ GRCh38: Ensembl release 89: ENSG00000244067Ensembl, May 2017
  2. ^ GRCm38: Ensembl release 89: ENSMUSG00000057933Ensembl, 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. ^ "Entrez Gene: GSTA2 glutathione S-transferase A2".

Further reading

PDB gallery
  • 1ags: 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 1ags: 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
  • 1gsd: GLUTATHIONE TRANSFERASE A1-1 IN UNLIGANDED FORM 1gsd: GLUTATHIONE TRANSFERASE A1-1 IN UNLIGANDED FORM
  • 1gse: GLUTATHIONE TRANSFERASE A1-1 COMPLEXED WITH AN ETHACRYNIC ACID GLUTATHIONE CONJUGATE (MUTANT R15K) 1gse: GLUTATHIONE TRANSFERASE A1-1 COMPLEXED WITH AN ETHACRYNIC ACID GLUTATHIONE CONJUGATE (MUTANT R15K)
  • 1gsf: GLUTATHIONE TRANSFERASE A1-1 COMPLEXED WITH ETHACRYNIC ACID 1gsf: GLUTATHIONE TRANSFERASE A1-1 COMPLEXED WITH ETHACRYNIC ACID
  • 1guh: STRUCTURE DETERMINATION AND REFINEMENT OF HUMAN ALPHA CLASS GLUTATHIONE TRANSFERASE A1-1, AND A COMPARISON WITH THE MU AND PI CLASS ENZYMES 1guh: STRUCTURE DETERMINATION AND REFINEMENT OF HUMAN ALPHA CLASS GLUTATHIONE TRANSFERASE A1-1, AND A COMPARISON WITH THE MU AND PI CLASS ENZYMES
  • 1k3l: Crystal Structure Analysis of S-hexyl-glutathione Complex of Glutathione Transferase at 1.5 Angstroms Resolution 1k3l: Crystal Structure Analysis of S-hexyl-glutathione Complex of Glutathione Transferase at 1.5 Angstroms Resolution
  • 1k3o: Crystal Structure Analysis of apo Glutathione S-Transferase 1k3o: Crystal Structure Analysis of apo Glutathione S-Transferase
  • 1k3y: Crystal Structure Analysis of human Glutathione S-transferase with S-hexyl glutatione and glycerol at 1.3 Angstrom 1k3y: Crystal Structure Analysis of human Glutathione S-transferase with S-hexyl glutatione and glycerol at 1.3 Angstrom
  • 1pkw: Crystal structure of human glutathione transferase (GST) A1-1 in complex with glutathione 1pkw: Crystal structure of human glutathione transferase (GST) A1-1 in complex with glutathione
  • 1pkz: Crystal structure of human glutathione transferase (GST) A1-1 1pkz: Crystal structure of human glutathione transferase (GST) A1-1
  • 1pl1: Crystal structure of human glutathione transferase (GST) A1-1 in complex with a decarboxy-glutathione 1pl1: Crystal structure of human glutathione transferase (GST) A1-1 in complex with a decarboxy-glutathione
  • 1pl2: Crystal structure of human glutathione transferase (GST) A1-1 T68E mutant in complex with decarboxy-glutathione 1pl2: Crystal structure of human glutathione transferase (GST) A1-1 T68E mutant in complex with decarboxy-glutathione
  • 1usb: RATIONAL DESIGN OF A NOVEL ENZYME - EFFICIENT THIOESTER HYDROLYSIS ENABLED BY THE INCORPORATION OF A SINGLE HIS RESIDUE INTO HUMAN GLUTATHIONE TRANSFERASE A1-1 1usb: RATIONAL DESIGN OF A NOVEL ENZYME - EFFICIENT THIOESTER HYDROLYSIS ENABLED BY THE INCORPORATION OF A SINGLE HIS RESIDUE INTO HUMAN GLUTATHIONE TRANSFERASE A1-1
  • 1xwg: Human GST A1-1 T68E mutant 1xwg: Human GST A1-1 T68E mutant
  • 1ydk: Crystal structure of the I219A mutant of human glutathione transferase A1-1 with S-hexylglutathione 1ydk: Crystal structure of the I219A mutant of human glutathione transferase A1-1 with S-hexylglutathione
Stub icon

This article on a gene on human chromosome 6 is a stub. You can help Misplaced Pages by expanding it.

Categories: