Glutathione S-transferase Mu 1

Protein-coding gene in the species Homo sapiens
GSTM1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1GTU, 1XW6, 1XWK, 1YJ6, 2F3M

Identifiers
AliasesGSTM1, GST1, GSTM1-1, GSTM1a-1a, GSTM1b-1b, GTH4, GTM1, H-B, MU, MU-1, glutathione S-transferase mu 1
External IDsOMIM: 138350; MGI: 95861; HomoloGene: 121492; GeneCards: GSTM1; OMA:GSTM1 - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for GSTM1
Genomic location for GSTM1
Band1p13.3Start109,687,814 bp[1]
End109,709,039 bp[1]
Gene location (Mouse)
Chromosome 3 (mouse)
Chr.Chromosome 3 (mouse)[2]
Chromosome 3 (mouse)
Genomic location for GSTM1
Genomic location for GSTM1
Band3|3 F2.3Start107,889,018 bp[2]
End107,893,769 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • smooth muscle tissue

  • gastric mucosa

  • left uterine tube

  • duodenum

  • anterior pituitary

  • right lobe of liver

  • canal of the cervix

  • myometrium

  • skeletal muscle tissue

  • ascending aorta
Top expressed in
  • uterus

  • ovary

  • adrenal gland

  • white adipose tissue

  • esophagus

  • urinary bladder

  • lung

  • stomach

  • testicle

  • colon
More reference expression data
BioGPS




More reference expression data
Gene ontology
Molecular function
  • enzyme binding
  • glutathione binding
  • protein homodimerization activity
  • transferase activity
  • glutathione transferase activity
Cellular component
  • cytoplasm
  • cytosol
  • intercellular bridge
Biological process
  • xenobiotic catabolic process
  • nitrobenzene metabolic process
  • cellular detoxification of nitrogen compound
  • glutathione metabolic process
  • metabolism
  • glutathione derivative biosynthetic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

2944

14863

Ensembl

ENSG00000134184

ENSMUSG00000040562

UniProt

P09488

P15626

RefSeq (mRNA)

NM_000561
NM_146421

NM_008183

RefSeq (protein)

NP_000552
NP_666533

NP_032209

Location (UCSC)Chr 1: 109.69 – 109.71 MbChr 3: 107.89 – 107.89 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Glutathione S-transferase Mu 1 (gene name GSTM1) is a human glutathione S-transferase.

Function

Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. 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 cytoplasmic glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress, by conjugation with glutathione.

The genes encoding the mu class of enzymes are organized in a gene cluster on chromosome 1p13.3, and 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 certain drugs. Null mutations of this class mu gene have been linked with an increase in a number of cancers, likely due to an increased susceptibility to environmental toxins and carcinogens. Multiple protein isoforms are encoded by transcript variants of this gene.[5]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000134184 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000040562 – 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. ^ "Entrez Gene: GSTM1 glutathione S-transferase M1".

Further reading

  • Engel LS, Taioli E, Pfeiffer R, Garcia-Closas M, Marcus PM, Lan Q, et al. (July 2002). "Pooled analysis and meta-analysis of glutathione S-transferase M1 and bladder cancer: a HuGE review". American Journal of Epidemiology. 156 (2): 95–109. doi:10.1093/aje/kwf018. PMID 12117698.
  • Navarro SL, Chang JL, Peterson S, Chen C, King IB, Schwarz Y, Li SS, Li L, Potter JD, Lampe JW (November 2009). "Modulation of human serum glutathione S-transferase A1/2 concentration by cruciferous vegetables in a controlled feeding study is influenced by GSTM1 and GSTT1 genotypes". Cancer Epidemiology, Biomarkers & Prevention. 18 (11): 2974–8. doi:10.1158/1055-9965.EPI-09-0701. PMC 2777676. PMID 19900941.

External links

  • PDBe-KB provides an overview of all the structure information available in the PDB for Human Glutathione S-transferase Mu 1


  • v
  • t
  • e
  • 1gtu: LIGAND-FREE HUMAN GLUTATHIONE S-TRANSFERASE M1A-1A
    1gtu: LIGAND-FREE HUMAN GLUTATHIONE S-TRANSFERASE M1A-1A
  • 1xw6: 1.9 angstrom resolution structure of human glutathione S-transferase M1A-1A complexed with glutathione
    1xw6: 1.9 angstrom resolution structure of human glutathione S-transferase M1A-1A complexed with glutathione
  • 1xwk: 2.3 angstrom resolution crystal structure of human glutathione S-transferase M1A-1A complexed with glutathionyl-S-dinitrobenzene
    1xwk: 2.3 angstrom resolution crystal structure of human glutathione S-transferase M1A-1A complexed with glutathionyl-S-dinitrobenzene
  • 1yj6: crystal structure of human glutathione S-transferase M1A-1A complexed with glutathionyl-zinc-trihydroxide
    1yj6: crystal structure of human glutathione S-transferase M1A-1A complexed with glutathionyl-zinc-trihydroxide
  • 2f3m: Structure of human GLUTATHIONE S-TRANSFERASE M1A-1A complexed with 1-(S-(GLUTATHIONYL)-2,4,6-TRINITROCYCLOHEXADIENATE ANION
    2f3m: Structure of human GLUTATHIONE S-TRANSFERASE M1A-1A complexed with 1-(S-(GLUTATHIONYL)-2,4,6-TRINITROCYCLOHEXADIENATE ANION


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