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Protein

Glutathione S-transferase Mu 1

Gene

GSTM1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei50Glutathione1 Publication1 Publication1
Binding sitei116Substrate1

GO - Molecular functioni

  • enzyme binding Source: BHF-UCL
  • glutathione binding Source: BHF-UCL
  • glutathione transferase activity Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL

GO - Biological processi

  • cellular detoxification of nitrogen compound Source: BHF-UCL
  • glutathione derivative biosynthetic process Source: Reactome
  • glutathione metabolic process Source: BHF-UCL
  • nitrobenzene metabolic process Source: BHF-UCL
  • xenobiotic catabolic process Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciZFISH:HS05827-MONOMER.
BRENDAi2.5.1.18. 2681.
ReactomeiR-HSA-156590. Glutathione conjugation.
SABIO-RKP09488.

Chemistry databases

SwissLipidsiSLP:000001613.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:4632. GSTM1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi7Y → F: Reduces catalytic activity 100-fold. 1 Publication1
Mutagenesisi108H → Q: Reduces catalytic activity by half. 2 Publications1
Mutagenesisi108H → S: Changes the properties of the enzyme toward some substrates. 2 Publications1
Mutagenesisi109M → I: Reduces catalytic activity by half. 1 Publication1
Mutagenesisi116Y → A: Reduces catalytic activity 10-fold. 1 Publication1
Mutagenesisi116Y → F: Slight increase of catalytic activity. 1 Publication1

Organism-specific databases

DisGeNETi2944.
MalaCardsiGSTM1.
OpenTargetsiENSG00000134184.
PharmGKBiPA182.

Chemistry databases

ChEMBLiCHEMBL2081.
DrugBankiDB00993. Azathioprine.
DB01008. Busulfan.
DB00958. Carboplatin.
DB00515. Cisplatin.
DB00143. Glutathione.
DB00526. Oxaliplatin.

Polymorphism and mutation databases

BioMutaiGSTM1.
DMDMi121735.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved6 Publications
ChainiPRO_00001858162 – 218Glutathione S-transferase Mu 1Add BLAST217

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei34PhosphothreonineBy similarity1
Modified residuei210PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP09488.
PaxDbiP09488.
PeptideAtlasiP09488.
PRIDEiP09488.

PTM databases

iPTMnetiP09488.
PhosphoSitePlusiP09488.

Expressioni

Tissue specificityi

Liver (at protein level).1 Publication

Gene expression databases

BgeeiENSG00000134184.
CleanExiHS_GSTM1.
ExpressionAtlasiP09488. baseline and differential.
GenevisibleiP09488. HS.

Organism-specific databases

HPAiCAB022669.
CAB047357.
HPA055972.
HPA055973.

Interactioni

Subunit structurei

Homodimer.

GO - Molecular functioni

  • enzyme binding Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL

Protein-protein interaction databases

BioGridi109199. 8 interactors.
IntActiP09488. 6 interactors.
STRINGi9606.ENSP00000311469.

Chemistry databases

BindingDBiP09488.

Structurei

Secondary structure

1218
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 11Combined sources9
Helixi12 – 14Combined sources3
Helixi15 – 23Combined sources9
Beta strandi28 – 33Combined sources6
Turni38 – 41Combined sources4
Helixi44 – 50Combined sources7
Beta strandi60 – 65Combined sources6
Beta strandi68 – 72Combined sources5
Helixi73 – 83Combined sources11
Helixi91 – 115Combined sources25
Helixi120 – 142Combined sources23
Beta strandi146 – 152Combined sources7
Helixi156 – 170Combined sources15
Turni172 – 177Combined sources6
Helixi179 – 189Combined sources11
Helixi192 – 198Combined sources7
Beta strandi200 – 202Combined sources3
Beta strandi214 – 216Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09488.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 88GST N-terminalAdd BLAST87
Domaini90 – 208GST C-terminalAdd BLAST119

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni7 – 8Glutathione binding1 Publication1 Publication2
Regioni43 – 46Glutathione binding1 Publication1 Publication4
Regioni59 – 60Glutathione binding1 Publication1 Publication2
Regioni72 – 73Glutathione binding1 Publication1 Publication2

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

eggNOGiENOG410IN5J. Eukaryota.
ENOG4110YU0. LUCA.
GeneTreeiENSGT00550000074559.
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]
PfamiPF14497. GST_C_3. 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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Sequence conflicti44S → T in CAA48636 (PubMed:8471052).Curated1
Sequence conflicti207P → T in AAT06767 (Ref. 4) Curated1

Polymorphismi

There are two alleles; GSTM1A and GSTM1B which differ in position 173. The sequence shown is that of allele GSTM1A.4 Publications

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_003617173K → N in allele GSTM1B. 4 PublicationsCorresponds to variant rs1065411dbSNPEnsembl.1
Natural variantiVAR_014497210S → T.Corresponds to variant rs449856dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_036618153 – 189Missing in isoform 2. 2 PublicationsAdd BLAST37

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109199. 8 interactors.
IntActiP09488. 6 interactors.
STRINGi9606.ENSP00000311469.

Chemistry databases

BindingDBiP09488.
ChEMBLiCHEMBL2081.
DrugBankiDB00993. Azathioprine.
DB01008. Busulfan.
DB00958. Carboplatin.
DB00515. Cisplatin.
DB00143. Glutathione.
DB00526. Oxaliplatin.
SwissLipidsiSLP:000001613.

PTM databases

iPTMnetiP09488.
PhosphoSitePlusiP09488.

Polymorphism and mutation databases

BioMutaiGSTM1.
DMDMi121735.

Proteomic databases

EPDiP09488.
PaxDbiP09488.
PeptideAtlasiP09488.
PRIDEiP09488.

Protocols and materials databases

DNASUi2944.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2944.
DisGeNETi2944.
GeneCardsiGSTM1.
HGNCiHGNC:4632. GSTM1.
HPAiCAB022669.
CAB047357.
HPA055972.
HPA055973.
MalaCardsiGSTM1.
MIMi138350. gene.
neXtProtiNX_P09488.
OpenTargetsiENSG00000134184.
PharmGKBiPA182.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IN5J. Eukaryota.
ENOG4110YU0. LUCA.
GeneTreeiENSGT00550000074559.
HOGENOMiHOG000115735.
HOVERGENiHBG106842.
InParanoidiP09488.
KOiK00799.
PhylomeDBiP09488.
TreeFamiTF353040.

Enzyme and pathway databases

BioCyciZFISH:HS05827-MONOMER.
BRENDAi2.5.1.18. 2681.
ReactomeiR-HSA-156590. Glutathione conjugation.
SABIO-RKP09488.

Miscellaneous databases

ChiTaRSiGSTM1. human.
EvolutionaryTraceiP09488.
GeneWikiiGlutathione_S-transferase_Mu_1.
GenomeRNAii2944.
PROiP09488.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000134184.
CleanExiHS_GSTM1.
ExpressionAtlasiP09488. baseline and differential.
GenevisibleiP09488. HS.

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]
PfamiPF14497. GST_C_3. 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]
ProtoNetiSearch...

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: November 2, 2016
This is version 185 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.