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P09488

- GSTM1_HUMAN

UniProt

P09488 - GSTM1_HUMAN

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Protein

Glutathione S-transferase Mu 1

Gene

GSTM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.1 Publication

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei116 – 1161Substrate

GO - Molecular functioni

  1. enzyme binding Source: BHF-UCL
  2. glutathione binding Source: BHF-UCL
  3. glutathione transferase activity Source: BHF-UCL
  4. protein homodimerization activity Source: BHF-UCL

GO - Biological processi

  1. cellular detoxification of nitrogen compound Source: BHF-UCL
  2. glutathione derivative biosynthetic process Source: Reactome
  3. glutathione metabolic process Source: BHF-UCL
  4. nitrobenzene metabolic process Source: BHF-UCL
  5. small molecule metabolic process Source: Reactome
  6. xenobiotic catabolic process Source: BHF-UCL
  7. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

ReactomeiREACT_6926. Glutathione conjugation.
SABIO-RKP09488.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:GSTM1
Synonyms:GST1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:4632. GSTM1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi7 – 71Y → F: Reduces catalytic activity 100-fold. 1 Publication
Mutagenesisi108 – 1081H → Q: Reduces catalytic activity by half. 2 Publications
Mutagenesisi108 – 1081H → S: Changes the properties of the enzyme toward some substrates. 2 Publications
Mutagenesisi109 – 1091M → I: Reduces catalytic activity by half. 1 Publication
Mutagenesisi116 – 1161Y → A: Reduces catalytic activity 10-fold. 1 Publication
Mutagenesisi116 – 1161Y → F: Slight increase of catalytic activity. 1 Publication

Organism-specific databases

PharmGKBiPA182.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed6 Publications
Chaini2 – 218217Glutathione S-transferase Mu 1PRO_0000185816Add
BLAST

Proteomic databases

MaxQBiP09488.
PaxDbiP09488.
PRIDEiP09488.

PTM databases

PhosphoSiteiP09488.

Expressioni

Tissue specificityi

Liver (at protein level).1 Publication

Gene expression databases

BgeeiP09488.
CleanExiHS_GSTM1.
ExpressionAtlasiP09488. baseline.
GenevestigatoriP09488.

Organism-specific databases

HPAiCAB022669.
CAB047357.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi109199. 8 interactions.
IntActiP09488. 6 interactions.
STRINGi9606.ENSP00000311469.

Structurei

Secondary structure

1
218
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 119
Helixi12 – 143
Helixi15 – 239
Beta strandi28 – 336
Turni38 – 414
Helixi44 – 507
Beta strandi60 – 656
Beta strandi68 – 725
Helixi73 – 8311
Helixi91 – 11525
Helixi120 – 14223
Beta strandi146 – 1527
Helixi156 – 17015
Turni172 – 1776
Helixi179 – 18911
Helixi192 – 1987
Beta strandi200 – 2023
Beta strandi214 – 2163

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP09488.
SMRiP09488. Positions 2-218.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09488.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8887GST N-terminalAdd
BLAST
Domaini90 – 208119GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni7 – 82Glutathione binding
Regioni46 – 505Glutathione binding
Regioni59 – 602Glutathione binding
Regioni72 – 732Glutathione binding

Sequence similaritiesi

Belongs to the GST superfamily. Mu family.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Phylogenomic databases

eggNOGiNOG300089.
HOGENOMiHOG000115735.
HOVERGENiHBG106842.
InParanoidiP09488.
KOiK00799.
PhylomeDBiP09488.
TreeFamiTF353040.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR003081. GST_mu.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01267. GSTRNSFRASEM.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P09488-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MPMILGYWDI RGLAHAIRLL LEYTDSSYEE KKYTMGDAPD YDRSQWLNEK
60 70 80 90 100
FKLGLDFPNL PYLIDGAHKI TQSNAILCYI ARKHNLCGET EEEKIRVDIL
110 120 130 140 150
ENQTMDNHMQ LGMICYNPEF EKLKPKYLEE LPEKLKLYSE FLGKRPWFAG
160 170 180 190 200
NKITFVDFLV YDVLDLHRIF EPKCLDAFPN LKDFISRFEG LEKISAYMKS
210
SRFLPRPVFS KMAVWGNK
Length:218
Mass (Da):25,712
Last modified:January 23, 2007 - v3
Checksum:i98FB03E87B83A31B
GO
Isoform 2 (identifier: P09488-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:181
Mass (Da):21,253
Checksum:i1FB16A0418115A26
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti44 – 441S → T in CAA48636. (PubMed:8471052)Curated
Sequence conflicti207 – 2071P → T in AAT06767. 1 PublicationCurated

Polymorphismi

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti173 – 1731K → N in allele GSTM1B. 2 Publications
Corresponds to variant rs1065411 [ dbSNP | Ensembl ].
VAR_003617
Natural varianti210 – 2101S → T.
Corresponds to variant rs449856 [ dbSNP | Ensembl ].
VAR_014497

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei153 – 18937Missing in isoform 2. 2 PublicationsVSP_036618Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS809.1. [P09488-1]
CCDS810.1. [P09488-2]
PIRiS01719.
RefSeqiNP_000552.2. NM_000561.3. [P09488-1]
NP_666533.1. NM_146421.2. [P09488-2]
UniGeneiHs.301961.

Genome annotation databases

EnsembliENST00000309851; ENSP00000311469; ENSG00000134184. [P09488-1]
ENST00000349334; ENSP00000234981; ENSG00000134184. [P09488-2]
GeneIDi2944.
KEGGihsa:2944.
UCSCiuc001dyk.3. human. [P09488-1]
uc001dyl.3. human. [P09488-2]

Polymorphism databases

DMDMi121735.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SHMPD

The Singapore human mutation and polymorphism database

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS809.1. [P09488-1 ]
CCDS810.1. [P09488-2 ]
PIRi S01719.
RefSeqi NP_000552.2. NM_000561.3. [P09488-1 ]
NP_666533.1. NM_146421.2. [P09488-2 ]
UniGenei Hs.301961.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GTU X-ray 2.68 A/B/C/D 2-218 [» ]
1XW6 X-ray 1.90 A/B/C/D 1-218 [» ]
1XWK X-ray 2.30 A/B/C 1-218 [» ]
1YJ6 X-ray 2.50 A/B/C 1-218 [» ]
2F3M X-ray 2.70 A/B/C/D/E/F 1-218 [» ]
ProteinModelPortali P09488.
SMRi P09488. Positions 2-218.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109199. 8 interactions.
IntActi P09488. 6 interactions.
STRINGi 9606.ENSP00000311469.

Chemistry

BindingDBi P09488.
ChEMBLi CHEMBL2081.
DrugBanki DB00993. Azathioprine.
DB01008. Busulfan.
DB00958. Carboplatin.
DB00515. Cisplatin.
DB00143. Glutathione.
DB00526. Oxaliplatin.

PTM databases

PhosphoSitei P09488.

Polymorphism databases

DMDMi 121735.

Proteomic databases

MaxQBi P09488.
PaxDbi P09488.
PRIDEi P09488.

Protocols and materials databases

DNASUi 2944.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000309851 ; ENSP00000311469 ; ENSG00000134184 . [P09488-1 ]
ENST00000349334 ; ENSP00000234981 ; ENSG00000134184 . [P09488-2 ]
GeneIDi 2944.
KEGGi hsa:2944.
UCSCi uc001dyk.3. human. [P09488-1 ]
uc001dyl.3. human. [P09488-2 ]

Organism-specific databases

CTDi 2944.
GeneCardsi GC01P110232.
HGNCi HGNC:4632. GSTM1.
HPAi CAB022669.
CAB047357.
MIMi 138350. gene.
neXtProti NX_P09488.
PharmGKBi PA182.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG300089.
HOGENOMi HOG000115735.
HOVERGENi HBG106842.
InParanoidi P09488.
KOi K00799.
PhylomeDBi P09488.
TreeFami TF353040.

Enzyme and pathway databases

Reactomei REACT_6926. Glutathione conjugation.
SABIO-RK P09488.

Miscellaneous databases

ChiTaRSi GSTM1. human.
EvolutionaryTracei P09488.
GeneWikii Glutathione_S-transferase_Mu_1.
GenomeRNAii 2944.
NextBioi 11663.
PROi P09488.
SOURCEi Search...

Gene expression databases

Bgeei P09488.
CleanExi HS_GSTM1.
ExpressionAtlasi P09488. baseline.
Genevestigatori P09488.

Family and domain databases

Gene3Di 1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProi IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR003081. GST_mu.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view ]
PRINTSi PR01267. GSTRNSFRASEM.
SUPFAMi SSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEi PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiGSTM1_HUMAN
AccessioniPrimary (citable) accession number: P09488
Secondary accession number(s): Q5GHG0
, Q6FH88, Q8TC98, Q9UC96
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 165 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3