Go Annotations as Summary Text (Tabular View) (GO Graph)

GO curators for mouse genes have assigned the following annotations to the gene product of Gstm1. (This text reflects annotations as of Wednesday, January 23, 2013.)

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Summary from NCBI RefSeq

[Summary is not available for the mouse gene. This summary is for the human ortholog.] 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 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. [provided by RefSeq, Jul 2008]

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Summary text based on GO annotations supported by experimental evidence in mouse

• Researchers have inferred from direct assay, that the gene product of Gstm1
  • participates in the following biological processes:
    • cellular response to drug ^[1]
  • performs the following molecular functions:
    • protein heterodimerization activity ^[3]
    • protein homodimerization activity ^[3]
• The gene product of Gstm1 has been shown to bind to the gene products of Iqub. ^[2]

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Summary text based on GO annotations supported by experimental evidence in other organisms

• From comparative sequence analysis (see table for details), MGI curators have determined that the gene product of Gstm1:
  • participates in the following biological processes:
    • cellular detoxification of nitrogen compound
    • glutathione metabolic process
    • nitrobenzene metabolic process
    • xenobiotic catabolic process
  • performs the following molecular functions:
    • enzyme binding
    • glutathione binding
    • glutathione transferase activity
    • protein homodimerization activity
    • steroid binding
  • is located in the following cellular components:
    • cytoplasm
    • extracellular region

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Summary text based on GO annotations supported by structural data

• Gstm1 encodes a protein or proteins that contain the following InterPro domains: Glutathione S-transferase, C-terminal, Glutathione S-transferase, C-terminal-like, Glutathione S-transferase, Mu class, Glutathione S-transferase, N-terminal, Glutathione S-transferase/chloride channel, C-terminal, Thioredoxin-like fold, indicating that the gene product:
  • participates in the following biological processes:
    • metabolic process

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Summary text for additional MGI annotations

• Automated translation to GO terms of SwissProt keywords that describe Gstm1 indicates that it:
  • performs the following molecular functions:
    • transferase activity

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References

1. Reinhart J et al. (1993) The structure of two murine class-mu glutathione transferase genes coordinately induced by butylated hydroxyanisole. Arch Biochem Biophys, 303:383-93. (PubMed:8512323)
2. Shi YQ et al. (2009) Male germ cell-specific protein Trs4 binds to multiple proteins. Biochem Biophys Res Commun, 388:583-8. (PubMed:19706271)
3. Townsend AJ et al. (1989) Isolation, characterization, and expression in Escherichia coli of two murine Mu class glutathione S-transferase cDNAs homologous to the rat subunits 3 (Yb1) and 4 (Yb2). J Biol Chem, 264:21582-90. (PubMed:2689439)

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Gene Ontology Evidence Code Abbreviations:

EXP Inferred from experiment

IC Inferred by curator

IDA Inferred from direct assay

IEA Inferred from electronic annotation

IGI Inferred from genetic interaction

IMP Inferred from mutant phenotype

IPI Inferred from physical interaction

ISS Inferred from sequence or structural similarity

ISO Inferred from sequence orthology

ISA Inferred from sequence alignment

ISM Inferred from sequence model

NAS Non-traceable author statement

ND No biological data available

RCA Reviewed computational analysis

TAS Traceable author statement

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