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Glutathione S-transferase Mu 1 (EC 2.5.1.18) (GST HB subunit 4) (GST class-mu 1) (GSTM1-1) (GSTM1a-1a) (GSTM1b-1b) (GTH4)

 GSTM1_HUMAN             Reviewed;         218 AA.
P09488; Q5GHG0; Q6FH88; Q8TC98; Q9UC96;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
27-SEP-2017, entry version 189.
RecName: Full=Glutathione S-transferase Mu 1;
EC=2.5.1.18;
AltName: Full=GST HB subunit 4;
AltName: Full=GST class-mu 1;
AltName: Full=GSTM1-1;
AltName: Full=GSTM1a-1a;
AltName: Full=GSTM1b-1b;
AltName: Full=GTH4;
Name=GSTM1; Synonyms=GST1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASN-173 (ALLELE
GSTM1B).
PubMed=3419925; DOI=10.1093/nar/16.17.8541;
Dejong J.L., Chang C.M., Whang Peng J., Knutsen T., Tu C.-P.D.;
"The human liver glutathione S-transferase gene superfamily:
expression and chromosome mapping of an Hb subunit cDNA.";
Nucleic Acids Res. 16:8541-8554(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3174634; DOI=10.1073/pnas.85.19.7293;
Seidegaard J., Vorachek W.R., Pero R.W., Pearson W.R.;
"Hereditary differences in the expression of the human glutathione
transferase active on trans-stilbene oxide are due to a gene
deletion.";
Proc. Natl. Acad. Sci. U.S.A. 85:7293-7297(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASN-173 (ALLELE
GSTM1B).
TISSUE=Liver;
Chen P., Wu Y., Zhang C., Han L., Wu Y., Xie D., Chen L.;
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Liver;
Chen P., Zhang C., Xie D., Wu Y., Han L., Chen L.;
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ASN-173 (ALLELE GSTM1B).
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-189 (ISOFORM 1), AND VARIANT
ASN-173 (ALLELE GSTM1B).
PubMed=8471052; DOI=10.1042/bj2910041;
Zhong S., Spurr N.K., Hayes J.D., Wolf C.R.;
"Deduced amino acid sequence, gene structure and chromosomal location
of a novel human class Mu glutathione S-transferase, GSTM4.";
Biochem. J. 291:41-50(1993).
[8]
PROTEIN SEQUENCE OF 2-31, AND TISSUE SPECIFICITY.
TISSUE=Fetal liver;
PubMed=7822249;
Mera N., Ohmori S., Itahashi K., Kiuchi M., Igarashi T., Rikihisa T.,
Kitada M.;
"Immunochemical evidence for the occurrence of Mu class glutathione S-
transferase in human fetal livers.";
J. Biochem. 116:315-320(1994).
[9]
PROTEIN SEQUENCE OF 2-25.
TISSUE=Aorta, and Heart;
PubMed=2110160;
Tsuchida S., Maki T., Sato K.;
"Purification and characterization of glutathione transferases with an
activity toward nitroglycerin from human aorta and heart. Multiplicity
of the human class Mu forms.";
J. Biol. Chem. 265:7150-7157(1990).
[10]
PROTEIN SEQUENCE OF 2-24.
PubMed=3979555; DOI=10.1016/0014-5793(85)80324-0;
Alin P., Mannervik B., Joernvall H.;
"Structural evidence for three different types of glutathione
transferase in human tissues.";
FEBS Lett. 182:319-322(1985).
[11]
PROTEIN SEQUENCE OF 2-24.
PubMed=3864155; DOI=10.1073/pnas.82.21.7202;
Mannervik B., Alin P., Guthenberg C., Jensson H., Tahir M.K.,
Warholm M., Joernvall H.;
"Identification of three classes of cytosolic glutathione transferase
common to several mammalian species: correlation between structural
data and enzymatic properties.";
Proc. Natl. Acad. Sci. U.S.A. 82:7202-7206(1985).
[12]
PROTEIN SEQUENCE OF 2-15.
PubMed=1846734; DOI=10.1016/0003-9861(91)90329-H;
Singhal S.S., Ahmad H., Sharma R., Gupta S., Haque A.K., Awasthi Y.C.;
"Purification and characterization of human muscle glutathione S-
transferases: evidence that glutathione S-transferase zeta corresponds
to a locus distinct from GST1, GST2, and GST3.";
Arch. Biochem. Biophys. 285:64-73(1991).
[13]
PROTEIN SEQUENCE OF 2-13.
TISSUE=Colon;
PubMed=1420361; DOI=10.1016/0167-4781(92)90135-M;
Singhal S.S., Saxena M., Awasthi S., Ahmad H., Sharma R.,
Awasthi Y.C.;
"Gender related differences in the expression and characteristics of
glutathione S-transferases of human colon.";
Biochim. Biophys. Acta 1171:19-26(1992).
[14]
PROTEIN SEQUENCE OF 53-60, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Liver;
PubMed=11271497;
DOI=10.1002/1522-2683(200011)21:17<3785::AID-ELPS3785>3.0.CO;2-2;
Hubbard M.J., McHugh N.J.;
"Human ERp29: isolation, primary structural characterisation and two-
dimensional gel mapping.";
Electrophoresis 21:3785-3796(2000).
[15]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 60-118.
PubMed=2362832; DOI=10.1093/nar/18.12.3670;
Comstock K.E., Sanderson B.J.S., Claflin G., Henner W.D.;
"GST1 gene deletion determined by polymerase chain reaction.";
Nucleic Acids Res. 18:3670-3670(1990).
[16]
NUCLEOTIDE SEQUENCE [MRNA] OF 125-186.
PubMed=8317488;
Pearson W.R., Vorachek W.R., Xu S.J., Berger R., Hart I., Vannais D.,
Patterson D.;
"Identification of class-mu glutathione transferase genes GSTM1-GSTM5
on human chromosome 1p13.";
Am. J. Hum. Genet. 53:220-233(1993).
[17]
X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS), AND MUTAGENESIS OF HIS-108.
PubMed=9930979; DOI=10.1021/bi982164m;
Patskovsky Y.V., Patskovska L.N., Listowsky I.;
"Functions of His107 in the catalytic mechanism of human glutathione
S-transferase hGSTM1a-1a.";
Biochemistry 38:1193-1202(1999).
[18] {ECO:0000244|PDB:1YJ6}
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.
Patskovsky Y.V., Patskovska L.N., Listowsky I., Almo S.C.;
"Human glutathione S-transferase M1A-1A catalyzes formation of Gsh-
metal complexes.";
Submitted (JAN-2005) to the PDB data bank.
[19]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH GLUTAHIONE
ANALOGS, CATALYTIC ACTIVITY, FUNCTION, AND MUTAGENESIS OF TYR-7;
HIS-108; MET-109 AND TYR-116.
PubMed=16548513; DOI=10.1021/bi051823+;
Patskovsky Y., Patskovska L., Almo S.C., Listowsky I.;
"Transition state model and mechanism of nucleophilic aromatic
substitution reactions catalyzed by human glutathione S-transferase
M1a-1a.";
Biochemistry 45:3852-3862(2006).
-!- FUNCTION: Conjugation of reduced glutathione to a wide number of
exogenous and endogenous hydrophobic electrophiles.
{ECO:0000269|PubMed:16548513}.
-!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
{ECO:0000269|PubMed:16548513}.
-!- SUBUNIT: Homodimer.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P09488-1; Sequence=Displayed;
Name=2;
IsoId=P09488-2; Sequence=VSP_036618;
-!- TISSUE SPECIFICITY: Liver (at protein level).
{ECO:0000269|PubMed:7822249}.
-!- POLYMORPHISM: There are two alleles; GSTM1A and GSTM1B which
differ in position 173. The sequence shown is that of allele
GSTM1A. {ECO:0000269|PubMed:3174634, ECO:0000269|PubMed:8471052,
ECO:0000269|Ref.3, ECO:0000269|Ref.5}.
-!- SIMILARITY: Belongs to the GST superfamily. Mu family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=GSTM1";
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EMBL; X08020; CAA30821.1; -; mRNA.
EMBL; J03817; AAA59203.1; -; mRNA.
EMBL; AY510272; AAR85979.1; -; mRNA.
EMBL; AY532926; AAT06767.1; -; mRNA.
EMBL; AY532927; AAT06768.1; -; mRNA.
EMBL; CR541868; CAG46666.1; -; mRNA.
EMBL; BC024005; AAH24005.1; -; mRNA.
EMBL; X68676; CAA48636.1; -; Genomic_DNA.
EMBL; X51451; CAA35817.1; -; Genomic_DNA.
CCDS; CCDS809.1; -. [P09488-1]
CCDS; CCDS810.1; -. [P09488-2]
PIR; S01719; S01719.
RefSeq; NP_000552.2; NM_000561.3. [P09488-1]
RefSeq; NP_666533.1; NM_146421.2. [P09488-2]
UniGene; Hs.301961; -.
PDB; 1GTU; X-ray; 2.68 A; A/B/C/D=2-218.
PDB; 1XW6; X-ray; 1.90 A; A/B/C/D=1-218.
PDB; 1XWK; X-ray; 2.30 A; A/B/C=1-218.
PDB; 1YJ6; X-ray; 2.50 A; A/B/C=1-218.
PDB; 2F3M; X-ray; 2.70 A; A/B/C/D/E/F=1-218.
PDBsum; 1GTU; -.
PDBsum; 1XW6; -.
PDBsum; 1XWK; -.
PDBsum; 1YJ6; -.
PDBsum; 2F3M; -.
ProteinModelPortal; P09488; -.
SMR; P09488; -.
BioGrid; 109199; 8.
IntAct; P09488; 6.
STRING; 9606.ENSP00000311469; -.
BindingDB; P09488; -.
ChEMBL; CHEMBL2081; -.
DrugBank; DB00993; Azathioprine.
DrugBank; DB01008; Busulfan.
DrugBank; DB00958; Carboplatin.
DrugBank; DB00515; Cisplatin.
DrugBank; DB03314; Fluorotryptophane.
DrugBank; DB00143; Glutathione.
DrugBank; DB00526; Oxaliplatin.
DrugBank; DB02165; Zinc Trihydroxide.
SwissLipids; SLP:000001613; -.
iPTMnet; P09488; -.
PhosphoSitePlus; P09488; -.
BioMuta; GSTM1; -.
DMDM; 121735; -.
EPD; P09488; -.
PaxDb; P09488; -.
PeptideAtlas; P09488; -.
PRIDE; P09488; -.
DNASU; 2944; -.
Ensembl; ENST00000309851; ENSP00000311469; ENSG00000134184. [P09488-1]
Ensembl; ENST00000349334; ENSP00000234981; ENSG00000134184. [P09488-2]
GeneID; 2944; -.
KEGG; hsa:2944; -.
CTD; 2944; -.
DisGeNET; 2944; -.
EuPathDB; HostDB:ENSG00000134184.12; -.
GeneCards; GSTM1; -.
HGNC; HGNC:4632; GSTM1.
HPA; CAB022669; -.
HPA; CAB047357; -.
HPA; HPA055972; -.
HPA; HPA055973; -.
MalaCards; GSTM1; -.
MIM; 138350; gene.
neXtProt; NX_P09488; -.
OpenTargets; ENSG00000134184; -.
PharmGKB; PA182; -.
eggNOG; ENOG410IN5J; Eukaryota.
eggNOG; ENOG4110YU0; LUCA.
GeneTree; ENSGT00550000074559; -.
HOGENOM; HOG000115735; -.
HOVERGEN; HBG106842; -.
InParanoid; P09488; -.
KO; K00799; -.
PhylomeDB; P09488; -.
TreeFam; TF353040; -.
BRENDA; 2.5.1.18; 2681.
Reactome; R-HSA-156590; Glutathione conjugation.
SABIO-RK; P09488; -.
ChiTaRS; GSTM1; human.
EvolutionaryTrace; P09488; -.
GeneWiki; Glutathione_S-transferase_Mu_1; -.
GenomeRNAi; 2944; -.
PRO; PR:P09488; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000134184; -.
CleanEx; HS_GSTM1; -.
ExpressionAtlas; P09488; baseline and differential.
Genevisible; P09488; HS.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0043295; F:glutathione binding; IDA:BHF-UCL.
GO; GO:0004364; F:glutathione transferase activity; IDA:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
GO; GO:0070458; P:cellular detoxification of nitrogen compound; IDA:BHF-UCL.
GO; GO:1901687; P:glutathione derivative biosynthetic process; TAS:Reactome.
GO; GO:0006749; P:glutathione metabolic process; IDA:BHF-UCL.
GO; GO:0018916; P:nitrobenzene metabolic process; IDA:BHF-UCL.
GO; GO:0042178; P:xenobiotic catabolic process; IDA:BHF-UCL.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR004046; GST_C.
InterPro; IPR003081; GST_mu.
InterPro; IPR012336; Thioredoxin-like_fold.
Pfam; PF14497; GST_C_3; 1.
Pfam; PF02798; GST_N; 1.
PRINTS; PR01267; GSTRNSFRASEM.
SUPFAM; SSF47616; SSF47616; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS50405; GST_CTER; 1.
PROSITE; PS50404; GST_NTER; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Phosphoprotein; Polymorphism;
Reference proteome; Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1420361,
ECO:0000269|PubMed:1846734,
ECO:0000269|PubMed:2110160,
ECO:0000269|PubMed:3864155,
ECO:0000269|PubMed:3979555,
ECO:0000269|PubMed:7822249}.
CHAIN 2 218 Glutathione S-transferase Mu 1.
/FTId=PRO_0000185816.
DOMAIN 2 88 GST N-terminal.
DOMAIN 90 208 GST C-terminal.
REGION 7 8 Glutathione binding. {ECO:0000269|Ref.18,
ECO:0000305|PubMed:16548513}.
REGION 43 46 Glutathione binding. {ECO:0000269|Ref.18,
ECO:0000305|PubMed:16548513}.
REGION 59 60 Glutathione binding. {ECO:0000269|Ref.18,
ECO:0000305|PubMed:16548513}.
REGION 72 73 Glutathione binding. {ECO:0000269|Ref.18,
ECO:0000305|PubMed:16548513}.
BINDING 50 50 Glutathione. {ECO:0000269|Ref.18,
ECO:0000305|PubMed:16548513}.
BINDING 116 116 Substrate.
MOD_RES 34 34 Phosphothreonine.
{ECO:0000250|UniProtKB:P10649}.
MOD_RES 210 210 Phosphoserine.
{ECO:0000250|UniProtKB:P04905}.
VAR_SEQ 153 189 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.4}.
/FTId=VSP_036618.
VARIANT 173 173 K -> N (in allele GSTM1B;
dbSNP:rs1065411).
{ECO:0000269|PubMed:3174634,
ECO:0000269|PubMed:8471052,
ECO:0000269|Ref.3, ECO:0000269|Ref.5}.
/FTId=VAR_003617.
VARIANT 210 210 S -> T (in dbSNP:rs449856).
/FTId=VAR_014497.
MUTAGEN 7 7 Y->F: Reduces catalytic activity 100-
fold. {ECO:0000269|PubMed:16548513}.
MUTAGEN 108 108 H->Q: Reduces catalytic activity by half.
{ECO:0000269|PubMed:16548513,
ECO:0000269|PubMed:9930979}.
MUTAGEN 108 108 H->S: Changes the properties of the
enzyme toward some substrates.
{ECO:0000269|PubMed:16548513,
ECO:0000269|PubMed:9930979}.
MUTAGEN 109 109 M->I: Reduces catalytic activity by half.
{ECO:0000269|PubMed:16548513}.
MUTAGEN 116 116 Y->A: Reduces catalytic activity 10-fold.
{ECO:0000269|PubMed:16548513}.
MUTAGEN 116 116 Y->F: Slight increase of catalytic
activity. {ECO:0000269|PubMed:16548513}.
CONFLICT 44 44 S -> T (in Ref. 7; CAA48636).
{ECO:0000305}.
CONFLICT 207 207 P -> T (in Ref. 4; AAT06767).
{ECO:0000305}.
STRAND 3 11 {ECO:0000244|PDB:1XW6}.
HELIX 12 14 {ECO:0000244|PDB:1XW6}.
HELIX 15 23 {ECO:0000244|PDB:1XW6}.
STRAND 28 33 {ECO:0000244|PDB:1XW6}.
TURN 38 41 {ECO:0000244|PDB:1XW6}.
HELIX 44 50 {ECO:0000244|PDB:1XW6}.
STRAND 60 65 {ECO:0000244|PDB:1XW6}.
STRAND 68 72 {ECO:0000244|PDB:1XW6}.
HELIX 73 83 {ECO:0000244|PDB:1XW6}.
HELIX 91 115 {ECO:0000244|PDB:1XW6}.
HELIX 120 142 {ECO:0000244|PDB:1XW6}.
STRAND 146 152 {ECO:0000244|PDB:1XW6}.
HELIX 156 170 {ECO:0000244|PDB:1XW6}.
TURN 172 177 {ECO:0000244|PDB:1XW6}.
HELIX 179 189 {ECO:0000244|PDB:1XW6}.
HELIX 192 198 {ECO:0000244|PDB:1XW6}.
STRAND 200 202 {ECO:0000244|PDB:1XW6}.
STRAND 214 216 {ECO:0000244|PDB:1XW6}.
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


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