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P09488 (GSTM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase Mu 1

EC=2.5.1.18
Alternative name(s):
GST HB subunit 4
GST class-mu 1
GSTM1-1
GSTM1a-1a
GSTM1b-1b
GTH4
Gene names
Name:GSTM1
Synonyms:GST1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length218 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Ref.18

Catalytic activity

RX + glutathione = HX + R-S-glutathione. Ref.18

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Tissue specificity

Liver (at protein level). Ref.8

Polymorphism

There are two alleles; GSTM1A and GSTM1B which differ in position 173.

Sequence similarities

Belongs to the GST superfamily. Mu family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P09488-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P09488-2)

The sequence of this isoform differs from the canonical sequence as follows:
     153-189: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
Chain2 – 218217Glutathione S-transferase Mu 1
PRO_0000185816

Regions

Domain2 – 8887GST N-terminal
Domain90 – 208119GST C-terminal
Region7 – 82Glutathione binding
Region46 – 505Glutathione binding
Region59 – 602Glutathione binding
Region72 – 732Glutathione binding

Sites

Binding site1161Substrate

Natural variations

Alternative sequence153 – 18937Missing in isoform 2.
VSP_036618
Natural variant1731K → N in allele GSTM1B. Ref.3 Ref.5
Corresponds to variant rs1065411 [ dbSNP | Ensembl ].
VAR_003617
Natural variant2101S → T.
Corresponds to variant rs449856 [ dbSNP | Ensembl ].
VAR_014497

Experimental info

Mutagenesis71Y → F: Reduces catalytic activity 100-fold. Ref.18
Mutagenesis1081H → Q: Reduces catalytic activity by half. Ref.17 Ref.18
Mutagenesis1081H → S: Changes the properties of the enzyme toward some substrates. Ref.17 Ref.18
Mutagenesis1091M → I: Reduces catalytic activity by half. Ref.18
Mutagenesis1161Y → A: Reduces catalytic activity 10-fold. Ref.18
Mutagenesis1161Y → F: Slight increase of catalytic activity. Ref.18
Sequence conflict441S → T in CAA48636. Ref.7
Sequence conflict2071P → T in AAT06767. Ref.4

Secondary structure

.................................. 218
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 98FB03E87B83A31B

FASTA21825,712
        10         20         30         40         50         60 
MPMILGYWDI RGLAHAIRLL LEYTDSSYEE KKYTMGDAPD YDRSQWLNEK FKLGLDFPNL 

        70         80         90        100        110        120 
PYLIDGAHKI TQSNAILCYI ARKHNLCGET EEEKIRVDIL ENQTMDNHMQ LGMICYNPEF 

       130        140        150        160        170        180 
EKLKPKYLEE LPEKLKLYSE FLGKRPWFAG NKITFVDFLV YDVLDLHRIF EPKCLDAFPN 

       190        200        210 
LKDFISRFEG LEKISAYMKS SRFLPRPVFS KMAVWGNK 

« Hide

Isoform 2 [UniParc].

Checksum: 1FB16A0418115A26
Show »

FASTA18121,253

References

« Hide 'large scale' references
[1]"The human liver glutathione S-transferase gene superfamily: expression and chromosome mapping of an Hb subunit cDNA."
Dejong J.L., Chang C.M., Whang Peng J., Knutsen T., Tu C.-P.D.
Nucleic Acids Res. 16:8541-8554(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Hereditary differences in the expression of the human glutathione transferase active on trans-stilbene oxide are due to a gene deletion."
Seidegaard J., Vorachek W.R., Pero R.W., Pearson W.R.
Proc. Natl. Acad. Sci. U.S.A. 85:7293-7297(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]Chen P., Wu Y., Zhang C., Han L., Wu Y., Xie D., Chen L.
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASN-173.
Tissue: Liver.
[4]Chen P., Zhang C., Xie D., Wu Y., Han L., Chen L.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Liver.
[5]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
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.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ASN-173.
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Testis.
[7]"Deduced amino acid sequence, gene structure and chromosomal location of a novel human class Mu glutathione S-transferase, GSTM4."
Zhong S., Spurr N.K., Hayes J.D., Wolf C.R.
Biochem. J. 291:41-50(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-189 (ISOFORM 1).
[8]"Immunochemical evidence for the occurrence of Mu class glutathione S-transferase in human fetal livers."
Mera N., Ohmori S., Itahashi K., Kiuchi M., Igarashi T., Rikihisa T., Kitada M.
J. Biochem. 116:315-320(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-31, TISSUE SPECIFICITY.
Tissue: Fetal liver.
[9]"Purification and characterization of glutathione transferases with an activity toward nitroglycerin from human aorta and heart. Multiplicity of the human class Mu forms."
Tsuchida S., Maki T., Sato K.
J. Biol. Chem. 265:7150-7157(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-25.
Tissue: Aorta and Heart.
[10]"Structural evidence for three different types of glutathione transferase in human tissues."
Alin P., Mannervik B., Joernvall H.
FEBS Lett. 182:319-322(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-24.
[11]"Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties."
Mannervik B., Alin P., Guthenberg C., Jensson H., Tahir M.K., Warholm M., Joernvall H.
Proc. Natl. Acad. Sci. U.S.A. 82:7202-7206(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-24.
[12]"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."
Singhal S.S., Ahmad H., Sharma R., Gupta S., Haque A.K., Awasthi Y.C.
Arch. Biochem. Biophys. 285:64-73(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-15.
[13]"Gender related differences in the expression and characteristics of glutathione S-transferases of human colon."
Singhal S.S., Saxena M., Awasthi S., Ahmad H., Sharma R., Awasthi Y.C.
Biochim. Biophys. Acta 1171:19-26(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-13.
Tissue: Colon.
[14]"Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping."
Hubbard M.J., McHugh N.J.
Electrophoresis 21:3785-3796(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 53-60, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Liver.
[15]"GST1 gene deletion determined by polymerase chain reaction."
Comstock K.E., Sanderson B.J.S., Claflin G., Henner W.D.
Nucleic Acids Res. 18:3670-3670(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 60-118.
[16]"Identification of class-mu glutathione transferase genes GSTM1-GSTM5 on human chromosome 1p13."
Pearson W.R., Vorachek W.R., Xu S.J., Berger R., Hart I., Vannais D., Patterson D.
Am. J. Hum. Genet. 53:220-233(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 125-186.
[17]"Functions of His107 in the catalytic mechanism of human glutathione S-transferase hGSTM1a-1a."
Patskovsky Y.V., Patskovska L.N., Listowsky I.
Biochemistry 38:1193-1202(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS), MUTAGENESIS OF HIS-108.
[18]"Transition state model and mechanism of nucleophilic aromatic substitution reactions catalyzed by human glutathione S-transferase M1a-1a."
Patskovsky Y., Patskovska L., Almo S.C., Listowsky I.
Biochemistry 45:3852-3862(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH GLUTAHIONE ANALOGS, CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF TYR-7; HIS-108; MET-109 AND TYR-116.
+Additional computationally mapped references.

Web resources

SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X08020 mRNA. Translation: CAA30821.1.
J03817 mRNA. Translation: AAA59203.1.
AY510272 mRNA. Translation: AAR85979.1.
AY532926 mRNA. Translation: AAT06767.1.
AY532927 mRNA. Translation: AAT06768.1.
CR541868 mRNA. Translation: CAG46666.1.
BC024005 mRNA. Translation: AAH24005.1.
X68676 Genomic DNA. Translation: CAA48636.1.
X51451 Genomic DNA. Translation: CAA35817.1.
CCDSCCDS809.1. [P09488-1]
CCDS810.1. [P09488-2]
PIRS01719.
RefSeqNP_000552.2. NM_000561.3. [P09488-1]
NP_666533.1. NM_146421.2. [P09488-2]
UniGeneHs.301961.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GTUX-ray2.68A/B/C/D2-218[»]
1XW6X-ray1.90A/B/C/D1-218[»]
1XWKX-ray2.30A/B/C1-218[»]
1YJ6X-ray2.50A/B/C1-218[»]
2F3MX-ray2.70A/B/C/D/E/F1-218[»]
ProteinModelPortalP09488.
SMRP09488. Positions 2-218.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109199. 4 interactions.
IntActP09488. 6 interactions.
STRING9606.ENSP00000311469.

Chemistry

BindingDBP09488.
ChEMBLCHEMBL2081.
DrugBankDB00143. Glutathione.

PTM databases

PhosphoSiteP09488.

Polymorphism databases

DMDM121735.

Proteomic databases

MaxQBP09488.
PaxDbP09488.
PRIDEP09488.

Protocols and materials databases

DNASU2944.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309851; ENSP00000311469; ENSG00000134184. [P09488-1]
ENST00000349334; ENSP00000234981; ENSG00000134184. [P09488-2]
GeneID2944.
KEGGhsa:2944.
UCSCuc001dyk.3. human. [P09488-1]
uc001dyl.3. human. [P09488-2]

Organism-specific databases

CTD2944.
GeneCardsGC01P110232.
HGNCHGNC:4632. GSTM1.
HPACAB022669.
CAB047357.
MIM138350. gene.
neXtProtNX_P09488.
PharmGKBPA182.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG300089.
HOGENOMHOG000115735.
HOVERGENHBG106842.
KOK00799.
PhylomeDBP09488.
TreeFamTF353040.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
SABIO-RKP09488.

Gene expression databases

ArrayExpressP09488.
BgeeP09488.
CleanExHS_GSTM1.
GenevestigatorP09488.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR003081. GST_mu.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSPR01267. GSTRNSFRASEM.
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGSTM1. human.
EvolutionaryTraceP09488.
GeneWikiGlutathione_S-transferase_Mu_1.
GenomeRNAi2944.
NextBio11663.
PROP09488.
SOURCESearch...

Entry information

Entry nameGSTM1_HUMAN
AccessionPrimary (citable) accession number: P09488
Secondary accession number(s): Q5GHG0 expand/collapse secondary AC list , Q6FH88, Q8TC98, Q9UC96
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 162 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM