(Q21146254)

Glutathione S-transferase, Mu class

1 reference

Glutathione S-transferase, C-terminal domain superfamily

1 reference

Glutathione S-transferase, C-terminal domain, protein family

1 reference

based on heuristic

inferred from protein domain or family

Glutathione S-transferase, C-terminal-like, protein family

1 reference

based on heuristic

inferred from protein domain or family

Glutathione S-transferase, N-terminal domain, protein family

1 reference

based on heuristic

inferred from protein domain or family

1 reference

13 November 2019

1 reference

13 November 2019

1 reference

9 May 2019

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

protein homodimerization activity

IEA

1 reference

9 May 2019

Molecular cloning and heterologous expression of an alternatively spliced human Mu class glutathione S-transferase transcript

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

1 reference

9 May 2019

Host factors that interact with the pestivirus N-terminal protease, Npro, are components of the ribonucleoprotein complex

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

1 reference

9 May 2019

Molecular cloning and heterologous expression of an alternatively spliced human Mu class glutathione S-transferase transcript

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

signaling receptor binding

IPI

1 reference

9 May 2019

The inhibitory glutathione transferase M2-2 binding site is located in divergent region 3 of the cardiac ryanodine receptor

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

glutathione peroxidase activity

IPI

1 reference

9 May 2019

Metabolism of oxidized linoleic acid by glutathione transferases: peroxidase activity toward 13-hydroperoxyoctadecadienoic acid

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

glutathione transferase activity

6 references

1 January 2018

http://www.ebi.ac.uk/QuickGO/annotations?protein=P28161&geneProductId=UniProtKB:P28161

1 January 2018

http://www.ebi.ac.uk/QuickGO/annotations?protein=P28161&geneProductId=UniProtKB:P28161

1 January 2018

http://www.ebi.ac.uk/QuickGO/annotations?protein=P28161&geneProductId=UniProtKB:P28161

1 January 2018

Alternative mutations of a positively selected residue elicit gain or loss of functionalities in enzyme evolution

http://www.ebi.ac.uk/QuickGO/annotations?protein=P28161&geneProductId=UniProtKB:P28161

1 January 2018

Molecular cloning and heterologous expression of an alternatively spliced human Mu class glutathione S-transferase transcript

http://www.ebi.ac.uk/QuickGO/annotations?protein=P28161&geneProductId=UniProtKB:P28161

1 January 2018

Cloning, expression, and characterization of a class-mu glutathione transferase from human muscle, the product of the GST4 locus

http://www.ebi.ac.uk/QuickGO/annotations?protein=P28161&geneProductId=UniProtKB:P28161

glutathione transferase activity

5 references

8 April 2019

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

8 April 2019

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

8 April 2019

Alternative mutations of a positively selected residue elicit gain or loss of functionalities in enzyme evolution

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

8 April 2019

Cloning, expression, and characterization of a class-mu glutathione transferase from human muscle, the product of the GST4 locus

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

8 April 2019

Molecular cloning and heterologous expression of an alternatively spliced human Mu class glutathione S-transferase transcript

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

glutathione transferase activity

6 references

9 May 2019

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

9 May 2019

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

9 May 2019

Alternative mutations of a positively selected residue elicit gain or loss of functionalities in enzyme evolution

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

9 May 2019

Cloning, expression, and characterization of a class-mu glutathione transferase from human muscle, the product of the GST4 locus

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

9 May 2019

Molecular cloning and heterologous expression of an alternatively spliced human Mu class glutathione S-transferase transcript

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

9 May 2019

Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

3 references

9 May 2019

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

9 May 2019

Cloning, expression, and characterization of a class-mu glutathione transferase from human muscle, the product of the GST4 locus

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

9 May 2019

Molecular cloning and heterologous expression of an alternatively spliced human Mu class glutathione S-transferase transcript

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

1 reference

26 September 2017

http://www.ebi.ac.uk/QuickGO/annotations?protein=P28161&geneProductId=UniProtKB:P28161

The inhibitory glutathione transferase M2-2 binding site is located in divergent region 3 of the cardiac ryanodine receptor

TAS

sarcoplasmic reticulum

1 reference

9 May 2019

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

Proteomic analysis of podocyte exosome-enriched fraction from normal human urine

extracellular exosome

3 references

26 September 2017

http://www.ebi.ac.uk/QuickGO/annotations?protein=P28161&geneProductId=UniProtKB:P28161

26 September 2017

Large-scale proteomics and phosphoproteomics of urinary exosomes

http://www.ebi.ac.uk/QuickGO/annotations?protein=P28161&geneProductId=UniProtKB:P28161

26 September 2017

In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine

http://www.ebi.ac.uk/QuickGO/annotations?protein=P28161&geneProductId=UniProtKB:P28161

2 references

8 April 2019

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

8 April 2019

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

1 reference

9 May 2019

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

xenobiotic catabolic process

3 references

8 April 2019

Alternative mutations of a positively selected residue elicit gain or loss of functionalities in enzyme evolution

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

8 April 2019

Cloning, expression, and characterization of a class-mu glutathione transferase from human muscle, the product of the GST4 locus

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

8 April 2019

Molecular cloning and heterologous expression of an alternatively spliced human Mu class glutathione S-transferase transcript

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

glutathione metabolic process

3 references

8 April 2019

Alternative mutations of a positively selected residue elicit gain or loss of functionalities in enzyme evolution

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

8 April 2019

Cloning, expression, and characterization of a class-mu glutathione transferase from human muscle, the product of the GST4 locus

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

8 April 2019

Molecular cloning and heterologous expression of an alternatively spliced human Mu class glutathione S-transferase transcript

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion

negative regulation of ryanodine-sensitive calcium-release channel activity

IC

positive regulation of ryanodine-sensitive calcium-release channel activity

1 reference

9 May 2019

The Mu class glutathione transferase is abundant in striated muscle and is an isoform-specific regulator of ryanodine receptor calcium channels

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

cellular detoxification of nitrogen compound

nitrobenzene metabolic process

cellular response to caffeine

1 reference

9 May 2019

The inhibitory glutathione transferase M2-2 binding site is located in divergent region 3 of the cardiac ryanodine receptor

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

1 reference

26 September 2017

http://www.ebi.ac.uk/QuickGO/annotations?protein=P28161&geneProductId=UniProtKB:P28161

regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum

IEA

1 reference

9 May 2019

The Mu class glutathione transferase is abundant in striated muscle and is an isoform-specific regulator of ryanodine receptor calcium channels

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

relaxation of cardiac muscle

1 reference

9 May 2019

Regulation of the cardiac muscle ryanodine receptor by glutathione transferases

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

glutathione derivative biosynthetic process

TAS

1 reference

9 May 2019

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion

TAS

1 reference

9 May 2019

The Mu class glutathione transferase is abundant in striated muscle and is an isoform-specific regulator of ryanodine receptor calcium channels

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

cellular oxidant detoxification

IC

1 reference

9 May 2019

Gene Ontology Consortium

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

linoleic acid metabolic process

IEA

1 reference

9 May 2019

Metabolism of oxidized linoleic acid by glutathione transferases: peroxidase activity toward 13-hydroperoxyoctadecadienoic acid

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

glutathione metabolic process

4 references

9 May 2019

Alternative mutations of a positively selected residue elicit gain or loss of functionalities in enzyme evolution

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

9 May 2019

Cloning, expression, and characterization of a class-mu glutathione transferase from human muscle, the product of the GST4 locus

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

9 May 2019

Molecular cloning and heterologous expression of an alternatively spliced human Mu class glutathione S-transferase transcript

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

9 May 2019

Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

xenobiotic catabolic process

IBA

4 references

9 May 2019

Alternative mutations of a positively selected residue elicit gain or loss of functionalities in enzyme evolution

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

9 May 2019

Cloning, expression, and characterization of a class-mu glutathione transferase from human muscle, the product of the GST4 locus

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

9 May 2019

Molecular cloning and heterologous expression of an alternatively spliced human Mu class glutathione S-transferase transcript

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

9 May 2019

Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P28161

Glutathione S-transferase, C-terminal

IBA

has part(s)

1 reference

glutathione S-transferase, C-terminal-like

1 reference

Glutathione S-transferase, N-terminal

1 reference

Identifiers

1 reference

30 May 2020

1 reference

30 May 2020

1 reference

13 November 2019

1 reference

1 reference

1 reference

1 reference

1 reference

1 reference

1 reference

1 reference

1 reference

4 August 2016

1 reference

4 August 2016

1 reference

4 August 2016

1 reference

4 August 2016

1 reference

4 August 2016

1 reference

4 August 2016

1 reference

4 August 2016

1 reference

4 August 2016

1 reference

4 August 2016

1 reference

4 August 2016