位置:首页 > 蛋白库 > GSTM1_HUMAN
GSTM1_HUMAN
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   03-AUG-2022, entry version 218.
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 (ALLELE
RP   GSTM1B).
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 (ALLELE
RP   GSTM1B).
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
RP   (ALLELE GSTM1B).
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 ASN-173
RP   (ALLELE GSTM1B).
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";
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 11.
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; DB00993; Azathioprine.
DR   DrugBank; DB01008; Busulfan.
DR   DrugBank; DB00958; Carboplatin.
DR   DrugBank; DB00608; Chloroquine.
DR   DrugBank; DB00515; Cisplatin.
DR   DrugBank; DB11672; Curcumin.
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; P09488; -.
DR   PeptideAtlas; P09488; -.
DR   PRIDE; P09488; -.
DR   ProteomicsDB; 52227; -. [P09488-1]
DR   ProteomicsDB; 52228; -. [P09488-2]
DR   Antibodypedia; 20073; 669 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   CTD; 2944; -.
DR   DisGeNET; 2944; -.
DR   GeneCards; GSTM1; -.
DR   HGNC; HGNC:4632; GSTM1.
DR   HPA; ENSG00000134184; Tissue enhanced (brain, 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; KWGNKKM; -.
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; 12 hits in 991 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 95 other 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   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   Pfam; PF14497; GST_C_3; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   PRINTS; PR01267; GSTRNSFRASEM.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024