ID GSTM1_HUMAN Reviewed; 218 AA.
AC P09488; Q5GHG0; Q6FH88; Q8TC98; Q9UC96;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 227.
DE RecName: Full=Glutathione S-transferase Mu 1 {ECO:0000305};
DE EC=2.5.1.18 {ECO:0000269|PubMed:16548513};
DE AltName: Full=GST HB subunit 4;
DE AltName: Full=GST class-mu 1;
DE AltName: Full=GSTM1-1;
DE AltName: Full=GSTM1a-1a;
DE AltName: Full=GSTM1b-1b;
DE AltName: Full=GTH4;
GN Name=GSTM1 {ECO:0000312|HGNC:HGNC:4632}; Synonyms=GST1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASN-173.
RX PubMed=3419925; DOI=10.1093/nar/16.17.8541;
RA Dejong J.L., Chang C.M., Whang Peng J., Knutsen T., Tu C.-P.D.;
RT "The human liver glutathione S-transferase gene superfamily: expression and
RT chromosome mapping of an Hb subunit cDNA.";
RL Nucleic Acids Res. 16:8541-8554(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3174634; DOI=10.1073/pnas.85.19.7293;
RA Seidegaard J., Vorachek W.R., Pero R.W., Pearson W.R.;
RT "Hereditary differences in the expression of the human glutathione
RT transferase active on trans-stilbene oxide are due to a gene deletion.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:7293-7297(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASN-173.
RC TISSUE=Liver;
RA Chen P., Wu Y., Zhang C., Han L., Wu Y., Xie D., Chen L.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Liver;
RA Chen P., Zhang C., Xie D., Wu Y., Han L., Chen L.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASN-173.
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-189 (ISOFORM 1), AND VARIANT
RP ASN-173.
RX PubMed=8471052; DOI=10.1042/bj2910041;
RA Zhong S., Spurr N.K., Hayes J.D., Wolf C.R.;
RT "Deduced amino acid sequence, gene structure and chromosomal location of a
RT novel human class Mu glutathione S-transferase, GSTM4.";
RL Biochem. J. 291:41-50(1993).
RN [8]
RP PROTEIN SEQUENCE OF 2-31, AND TISSUE SPECIFICITY.
RC TISSUE=Fetal liver;
RX PubMed=7822249; DOI=10.1093/oxfordjournals.jbchem.a124525;
RA Mera N., Ohmori S., Itahashi K., Kiuchi M., Igarashi T., Rikihisa T.,
RA Kitada M.;
RT "Immunochemical evidence for the occurrence of Mu class glutathione S-
RT transferase in human fetal livers.";
RL J. Biochem. 116:315-320(1994).
RN [9]
RP PROTEIN SEQUENCE OF 2-25.
RC TISSUE=Aorta, and Heart;
RX PubMed=2110160; DOI=10.1016/s0021-9258(19)39092-1;
RA Tsuchida S., Maki T., Sato K.;
RT "Purification and characterization of glutathione transferases with an
RT activity toward nitroglycerin from human aorta and heart. Multiplicity of
RT the human class Mu forms.";
RL J. Biol. Chem. 265:7150-7157(1990).
RN [10]
RP PROTEIN SEQUENCE OF 2-24.
RX PubMed=3979555; DOI=10.1016/0014-5793(85)80324-0;
RA Alin P., Mannervik B., Joernvall H.;
RT "Structural evidence for three different types of glutathione transferase
RT in human tissues.";
RL FEBS Lett. 182:319-322(1985).
RN [11]
RP PROTEIN SEQUENCE OF 2-24.
RX PubMed=3864155; DOI=10.1073/pnas.82.21.7202;
RA Mannervik B., Alin P., Guthenberg C., Jensson H., Tahir M.K., Warholm M.,
RA Joernvall H.;
RT "Identification of three classes of cytosolic glutathione transferase
RT common to several mammalian species: correlation between structural data
RT and enzymatic properties.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:7202-7206(1985).
RN [12]
RP PROTEIN SEQUENCE OF 2-15.
RX PubMed=1846734; DOI=10.1016/0003-9861(91)90329-h;
RA Singhal S.S., Ahmad H., Sharma R., Gupta S., Haque A.K., Awasthi Y.C.;
RT "Purification and characterization of human muscle glutathione S-
RT transferases: evidence that glutathione S-transferase zeta corresponds to a
RT locus distinct from GST1, GST2, and GST3.";
RL Arch. Biochem. Biophys. 285:64-73(1991).
RN [13]
RP PROTEIN SEQUENCE OF 2-13.
RC TISSUE=Colon;
RX PubMed=1420361; DOI=10.1016/0167-4781(92)90135-m;
RA Singhal S.S., Saxena M., Awasthi S., Ahmad H., Sharma R., Awasthi Y.C.;
RT "Gender related differences in the expression and characteristics of
RT glutathione S-transferases of human colon.";
RL Biochim. Biophys. Acta 1171:19-26(1992).
RN [14]
RP PROTEIN SEQUENCE OF 53-60, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=11271497;
RX DOI=10.1002/1522-2683(200011)21:17<3785::aid-elps3785>3.0.co;2-2;
RA Hubbard M.J., McHugh N.J.;
RT "Human ERp29: isolation, primary structural characterisation and two-
RT dimensional gel mapping.";
RL Electrophoresis 21:3785-3796(2000).
RN [15]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 60-118.
RX PubMed=2362832; DOI=10.1093/nar/18.12.3670;
RA Comstock K.E., Sanderson B.J.S., Claflin G., Henner W.D.;
RT "GST1 gene deletion determined by polymerase chain reaction.";
RL Nucleic Acids Res. 18:3670-3670(1990).
RN [16]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 125-186.
RX PubMed=8317488;
RA Pearson W.R., Vorachek W.R., Xu S.J., Berger R., Hart I., Vannais D.,
RA Patterson D.;
RT "Identification of class-mu glutathione transferase genes GSTM1-GSTM5 on
RT human chromosome 1p13.";
RL Am. J. Hum. Genet. 53:220-233(1993).
RN [17]
RP CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9084911; DOI=10.1021/tx9601770;
RA Bogaards J.J., Venekamp J.C., van Bladeren P.J.;
RT "Stereoselective conjugation of prostaglandin A2 and prostaglandin J2 with
RT glutathione, catalyzed by the human glutathione S-transferases A1-1, A2-2,
RT M1a-1a, and P1-1.";
RL Chem. Res. Toxicol. 10:310-317(1997).
RN [18]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=21046276; DOI=10.1007/s11745-010-3485-1;
RA Brunnstroem A., Hamberg M., Griffiths W.J., Mannervik B., Claesson H.E.;
RT "Biosynthesis of 14,15-hepoxilins in human l1236 Hodgkin lymphoma cells and
RT eosinophils.";
RL Lipids 46:69-79(2011).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS), AND MUTAGENESIS OF HIS-108.
RX PubMed=9930979; DOI=10.1021/bi982164m;
RA Patskovsky Y.V., Patskovska L.N., Listowsky I.;
RT "Functions of His107 in the catalytic mechanism of human glutathione S-
RT transferase hGSTM1a-1a.";
RL Biochemistry 38:1193-1202(1999).
RN [20] {ECO:0007744|PDB:1YJ6}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.
RA Patskovsky Y.V., Patskovska L.N., Listowsky I., Almo S.C.;
RT "Human glutathione S-transferase M1A-1A catalyzes formation of Gsh-metal
RT complexes.";
RL Submitted (JAN-2005) to the PDB data bank.
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH GLUTAHIONE ANALOGS,
RP CATALYTIC ACTIVITY, FUNCTION, AND MUTAGENESIS OF TYR-7; HIS-108; MET-109
RP AND TYR-116.
RX PubMed=16548513; DOI=10.1021/bi051823+;
RA Patskovsky Y., Patskovska L., Almo S.C., Listowsky I.;
RT "Transition state model and mechanism of nucleophilic aromatic substitution
RT reactions catalyzed by human glutathione S-transferase M1a-1a.";
RL Biochemistry 45:3852-3862(2006).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles. Involved in the
CC formation of glutathione conjugates of both prostaglandin A2 (PGA2) and
CC prostaglandin J2 (PGJ2) (PubMed:9084911). Participates in the formation
CC of novel hepoxilin regioisomers (PubMed:21046276).
CC {ECO:0000269|PubMed:16548513, ECO:0000269|PubMed:21046276,
CC ECO:0000269|PubMed:9084911}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC Evidence={ECO:0000269|PubMed:16548513};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + prostaglandin A2 = prostaglandin A2-S-(R)-
CC glutathione; Xref=Rhea:RHEA:50796, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:133370, ChEBI:CHEBI:133768;
CC Evidence={ECO:0000269|PubMed:9084911};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50797;
CC Evidence={ECO:0000305|PubMed:9084911};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + prostaglandin J2 = prostaglandin J2-S-(R)-
CC glutathione; Xref=Rhea:RHEA:50804, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:133396, ChEBI:CHEBI:133771;
CC Evidence={ECO:0000269|PubMed:9084911};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50805;
CC Evidence={ECO:0000305|PubMed:9084911};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + prostaglandin J2 = prostaglandin J2-S-(S)-
CC glutathione; Xref=Rhea:RHEA:50808, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:133396, ChEBI:CHEBI:133772;
CC Evidence={ECO:0000269|PubMed:9084911};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50809;
CC Evidence={ECO:0000305|PubMed:9084911};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + prostaglandin A2 = prostaglandin A2-S-(S)-
CC glutathione; Xref=Rhea:RHEA:50800, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:133370, ChEBI:CHEBI:133769;
CC Evidence={ECO:0000269|PubMed:9084911};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50801;
CC Evidence={ECO:0000305|PubMed:9084911};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11(S)-hydroxy-14(S),15(S)-epoxy-(5Z,8Z,12E)-eicosatrienoate +
CC glutathione = (11S,15S)-dihydroxy-14(R)-S-glutathionyl-(5Z,8Z,12E)-
CC eicosatrienoate; Xref=Rhea:RHEA:50260, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:132200, ChEBI:CHEBI:132201;
CC Evidence={ECO:0000269|PubMed:21046276};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50261;
CC Evidence={ECO:0000305|PubMed:21046276};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=26 uM for prostaglandin A2 (at pH 7.0 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:9084911};
CC KM=95 uM for prostaglandin J2 (at pH 7.0 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:9084911};
CC Vmax=27 nmol/min/mg enzyme for the formation of the glutathione-S-
CC conjugate of prostaglandin A2 (at pH 7.0 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:9084911};
CC Vmax=72 nmol/min/mg enzyme for the formation of the glutathione-S-
CC conjugate of prostaglandin J2 (at pH 7.0 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:9084911};
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P09488-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P09488-2; Sequence=VSP_036618;
CC -!- TISSUE SPECIFICITY: Liver (at protein level).
CC {ECO:0000269|PubMed:7822249}.
CC -!- POLYMORPHISM: There are two alleles; GSTM1A and GSTM1B which differ in
CC position 173. The sequence shown is that of allele GSTM1A.
CC {ECO:0000269|PubMed:3174634, ECO:0000269|PubMed:8471052,
CC ECO:0000269|Ref.3, ECO:0000269|Ref.5}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
CC polymorphism database;
CC URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=C&genename=GSTM1";
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DR EMBL; X08020; CAA30821.1; -; mRNA.
DR EMBL; J03817; AAA59203.1; -; mRNA.
DR EMBL; AY510272; AAR85979.1; -; mRNA.
DR EMBL; AY532926; AAT06767.1; -; mRNA.
DR EMBL; AY532927; AAT06768.1; -; mRNA.
DR EMBL; CR541868; CAG46666.1; -; mRNA.
DR EMBL; BC024005; AAH24005.1; -; mRNA.
DR EMBL; X68676; CAA48636.1; -; Genomic_DNA.
DR EMBL; X51451; CAA35817.1; -; Genomic_DNA.
DR CCDS; CCDS809.1; -. [P09488-1]
DR CCDS; CCDS810.1; -. [P09488-2]
DR PIR; S01719; S01719.
DR RefSeq; NP_000552.2; NM_000561.3. [P09488-1]
DR RefSeq; NP_666533.1; NM_146421.2. [P09488-2]
DR PDB; 1GTU; X-ray; 2.68 A; A/B/C/D=2-218.
DR PDB; 1XW6; X-ray; 1.90 A; A/B/C/D=1-218.
DR PDB; 1XWK; X-ray; 2.30 A; A/B/C=1-218.
DR PDB; 1YJ6; X-ray; 2.50 A; A/B/C=1-218.
DR PDB; 2F3M; X-ray; 2.70 A; A/B/C/D/E/F=1-218.
DR PDB; 7BEU; X-ray; 1.59 A; A/B/C/D=1-218.
DR PDBsum; 1GTU; -.
DR PDBsum; 1XW6; -.
DR PDBsum; 1XWK; -.
DR PDBsum; 1YJ6; -.
DR PDBsum; 2F3M; -.
DR PDBsum; 7BEU; -.
DR AlphaFoldDB; P09488; -.
DR SMR; P09488; -.
DR BioGRID; 109199; 14.
DR IntAct; P09488; 12.
DR STRING; 9606.ENSP00000311469; -.
DR BindingDB; P09488; -.
DR ChEMBL; CHEMBL2081; -.
DR DrugBank; DB01834; (9R,10R)-9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene.
DR DrugBank; DB04187; (9S,10S)-9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene.
DR DrugBank; DB03314; 5-fluorotryptophan.
DR DrugBank; DB00316; Acetaminophen.
DR DrugBank; DB00321; Amitriptyline.
DR DrugBank; DB00993; Azathioprine.
DR DrugBank; DB01008; Busulfan.
DR DrugBank; DB00958; Carboplatin.
DR DrugBank; DB00291; Chlorambucil.
DR DrugBank; DB00608; Chloroquine.
DR DrugBank; DB00515; Cisplatin.
DR DrugBank; DB11672; Curcumin.
DR DrugBank; DB03619; Deoxycholic acid.
DR DrugBank; DB00143; Glutathione.
DR DrugBank; DB03310; Glutathione disulfide.
DR DrugBank; DB01020; Isosorbide mononitrate.
DR DrugBank; DB00526; Oxaliplatin.
DR DrugBank; DB02458; S-(2,4-dinitrophenyl)glutathione.
DR DrugBank; DB02165; Zinc trihydroxide.
DR SwissLipids; SLP:000001613; -.
DR iPTMnet; P09488; -.
DR MetOSite; P09488; -.
DR PhosphoSitePlus; P09488; -.
DR BioMuta; GSTM1; -.
DR DMDM; 121735; -.
DR EPD; P09488; -.
DR jPOST; P09488; -.
DR MassIVE; P09488; -.
DR PaxDb; 9606-ENSP00000311469; -.
DR PeptideAtlas; P09488; -.
DR ProteomicsDB; 52227; -. [P09488-1]
DR ProteomicsDB; 52228; -. [P09488-2]
DR Pumba; P09488; -.
DR Antibodypedia; 20073; 713 antibodies from 43 providers.
DR CPTC; P09488; 7 antibodies.
DR DNASU; 2944; -.
DR Ensembl; ENST00000309851.10; ENSP00000311469.5; ENSG00000134184.13. [P09488-1]
DR Ensembl; ENST00000349334.7; ENSP00000234981.4; ENSG00000134184.13. [P09488-2]
DR GeneID; 2944; -.
DR KEGG; hsa:2944; -.
DR MANE-Select; ENST00000309851.10; ENSP00000311469.5; NM_000561.4; NP_000552.2.
DR AGR; HGNC:4632; -.
DR CTD; 2944; -.
DR DisGeNET; 2944; -.
DR GeneCards; GSTM1; -.
DR HGNC; HGNC:4632; GSTM1.
DR HPA; ENSG00000134184; Tissue enhanced (liver).
DR MIM; 138350; gene.
DR neXtProt; NX_P09488; -.
DR OpenTargets; ENSG00000134184; -.
DR PharmGKB; PA182; -.
DR VEuPathDB; HostDB:ENSG00000134184; -.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00940000160258; -.
DR InParanoid; P09488; -.
DR OMA; FAKMALW; -.
DR PhylomeDB; P09488; -.
DR TreeFam; TF353040; -.
DR BRENDA; 2.5.1.18; 2681.
DR PathwayCommons; P09488; -.
DR Reactome; R-HSA-156590; Glutathione conjugation.
DR Reactome; R-HSA-9748787; Azathioprine ADME.
DR Reactome; R-HSA-9753281; Paracetamol ADME.
DR SABIO-RK; P09488; -.
DR SignaLink; P09488; -.
DR SIGNOR; P09488; -.
DR BioGRID-ORCS; 2944; 15 hits in 1058 CRISPR screens.
DR ChiTaRS; GSTM1; human.
DR EvolutionaryTrace; P09488; -.
DR GeneWiki; Glutathione_S-transferase_Mu_1; -.
DR GenomeRNAi; 2944; -.
DR Pharos; P09488; Tbio.
DR PRO; PR:P09488; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P09488; Protein.
DR Bgee; ENSG00000134184; Expressed in smooth muscle tissue and 97 other cell types or tissues.
DR ExpressionAtlas; P09488; baseline and differential.
DR Genevisible; P09488; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0043295; F:glutathione binding; IDA:BHF-UCL.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
DR GO; GO:0070458; P:cellular detoxification of nitrogen compound; IDA:BHF-UCL.
DR GO; GO:1901687; P:glutathione derivative biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; IDA:BHF-UCL.
DR GO; GO:0051122; P:hepoxilin biosynthetic process; IDA:UniProtKB.
DR GO; GO:0018916; P:nitrobenzene metabolic process; IDA:BHF-UCL.
DR GO; GO:0006693; P:prostaglandin metabolic process; IDA:UniProtKB.
DR GO; GO:0042178; P:xenobiotic catabolic process; IDA:BHF-UCL.
DR CDD; cd03209; GST_C_Mu; 1.
DR CDD; cd03075; GST_N_Mu; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR003081; GST_mu.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR PANTHER; PTHR11571:SF247; GLUTATHIONE S-TRANSFERASE MU 1; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01267; GSTRNSFRASEM.
DR SFLD; SFLDG01205; AMPS.1; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Lipid metabolism; Phosphoprotein; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1420361,
FT ECO:0000269|PubMed:1846734, ECO:0000269|PubMed:2110160,
FT ECO:0000269|PubMed:3864155, ECO:0000269|PubMed:3979555,
FT ECO:0000269|PubMed:7822249"
FT CHAIN 2..218
FT /note="Glutathione S-transferase Mu 1"
FT /id="PRO_0000185816"
FT DOMAIN 2..88
FT /note="GST N-terminal"
FT DOMAIN 90..208
FT /note="GST C-terminal"
FT BINDING 7..8
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|Ref.20, ECO:0000305|PubMed:16548513"
FT BINDING 43..46
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|Ref.20, ECO:0000305|PubMed:16548513"
FT BINDING 50
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|Ref.20, ECO:0000305|PubMed:16548513"
FT BINDING 59..60
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|Ref.20, ECO:0000305|PubMed:16548513"
FT BINDING 72..73
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|Ref.20, ECO:0000305|PubMed:16548513"
FT BINDING 116
FT /ligand="substrate"
FT MOD_RES 34
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10649"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04905"
FT VAR_SEQ 153..189
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_036618"
FT VARIANT 173
FT /note="K -> N (in allele GSTM1B; dbSNP:rs1065411)"
FT /evidence="ECO:0000269|PubMed:3174634,
FT ECO:0000269|PubMed:8471052, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.5"
FT /id="VAR_003617"
FT VARIANT 210
FT /note="S -> T (in dbSNP:rs449856)"
FT /id="VAR_014497"
FT MUTAGEN 7
FT /note="Y->F: Reduces catalytic activity 100-fold."
FT /evidence="ECO:0000269|PubMed:16548513"
FT MUTAGEN 108
FT /note="H->Q: Reduces catalytic activity by half."
FT /evidence="ECO:0000269|PubMed:16548513,
FT ECO:0000269|PubMed:9930979"
FT MUTAGEN 108
FT /note="H->S: Changes the properties of the enzyme toward
FT some substrates."
FT /evidence="ECO:0000269|PubMed:16548513,
FT ECO:0000269|PubMed:9930979"
FT MUTAGEN 109
FT /note="M->I: Reduces catalytic activity by half."
FT /evidence="ECO:0000269|PubMed:16548513"
FT MUTAGEN 116
FT /note="Y->A: Reduces catalytic activity 10-fold."
FT /evidence="ECO:0000269|PubMed:16548513"
FT MUTAGEN 116
FT /note="Y->F: Slight increase of catalytic activity."
FT /evidence="ECO:0000269|PubMed:16548513"
FT CONFLICT 44
FT /note="S -> T (in Ref. 7; CAA48636)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="P -> T (in Ref. 4; AAT06767)"
FT /evidence="ECO:0000305"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:7BEU"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:7BEU"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:7BEU"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:7BEU"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:7BEU"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:7BEU"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:7BEU"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:7BEU"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:7BEU"
FT HELIX 73..83
FT /evidence="ECO:0007829|PDB:7BEU"
FT HELIX 91..115
FT /evidence="ECO:0007829|PDB:7BEU"
FT HELIX 120..142
FT /evidence="ECO:0007829|PDB:7BEU"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:7BEU"
FT HELIX 155..170
FT /evidence="ECO:0007829|PDB:7BEU"
FT TURN 172..177
FT /evidence="ECO:0007829|PDB:7BEU"
FT HELIX 179..189
FT /evidence="ECO:0007829|PDB:7BEU"
FT HELIX 192..199
FT /evidence="ECO:0007829|PDB:7BEU"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:1XW6"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:7BEU"
SQ SEQUENCE 218 AA; 25712 MW; 98FB03E87B83A31B CRC64;
MPMILGYWDI RGLAHAIRLL LEYTDSSYEE KKYTMGDAPD YDRSQWLNEK FKLGLDFPNL
PYLIDGAHKI TQSNAILCYI ARKHNLCGET EEEKIRVDIL ENQTMDNHMQ LGMICYNPEF
EKLKPKYLEE LPEKLKLYSE FLGKRPWFAG NKITFVDFLV YDVLDLHRIF EPKCLDAFPN
LKDFISRFEG LEKISAYMKS SRFLPRPVFS KMAVWGNK
//
