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Protein

Glutathione S-transferase Mu 1

Gene

Gstm1

Organism
Mus musculus (Mouse)
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.

Catalytic activityi

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

Sites

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

GO - Molecular functioni

  • glutathione transferase activity Source: MGI
  • protein heterodimerization activity Source: MGI
  • protein homodimerization activity Source: MGI

GO - Biological processi

  • cellular response to drug Source: MGI
  • glutathione metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

ReactomeiREACT_317599. Glutathione conjugation.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase Mu 1 (EC:2.5.1.18)
Alternative name(s):
GST 1-1
GST class-mu 1
Glutathione S-transferase GT8.7
pmGT10
Gene namesi
Name:Gstm1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:95860. Gstm1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • myelin sheath Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 218217Glutathione S-transferase Mu 1PRO_0000185826Add
BLAST

Proteomic databases

MaxQBiP10649.
PaxDbiP10649.
PRIDEiP10649.

2D gel databases

REPRODUCTION-2DPAGEP10649.
SWISS-2DPAGEP10649.

PTM databases

PhosphoSiteiP10649.

Expressioni

Gene expression databases

BgeeiP10649.
CleanExiMM_GSTM1.
ExpressionAtlasiP10649. baseline and differential.
GenevisibleiP10649. MM.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi200094. 2 interactions.
IntActiP10649. 5 interactions.
MINTiMINT-1869211.
STRINGi10090.ENSMUSP00000004140.

Structurei

3D structure databases

ProteinModelPortaliP10649.
SMRiP10649. Positions 2-218.
ModBaseiSearch...
MobiDBiSearch...

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 bindingBy similarity
Regioni46 – 505Glutathione bindingBy similarity
Regioni59 – 602Glutathione bindingBy similarity
Regioni72 – 732Glutathione bindingBy similarity

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.
GeneTreeiENSGT00550000074559.
HOGENOMiHOG000115735.
HOVERGENiHBG106842.
InParanoidiP10649.
KOiK00799.
OMAiQLAVICY.
OrthoDBiEOG7KH9M3.
PhylomeDBiP10649.
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]

Sequencei

Sequence statusi: Complete.

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

P10649-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPMILGYWNV RGLTHPIRML LEYTDSSYDE KRYTMGDAPD FDRSQWLNEK
60 70 80 90 100
FKLGLDFPNL PYLIDGSHKI TQSNAILRYL ARKHHLDGET EEERIRADIV
110 120 130 140 150
ENQVMDTRMQ LIMLCYNPDF EKQKPEFLKT IPEKMKLYSE FLGKRPWFAG
160 170 180 190 200
DKVTYVDFLA YDILDQYRMF EPKCLDAFPN LRDFLARFEG LKKISAYMKS
210
SRYIATPIFS KMAHWSNK
Length:218
Mass (Da):25,970
Last modified:January 23, 2007 - v2
Checksum:i91AE34A1B5B44599
GO

Mass spectrometryi

Molecular mass is 25838.4±2 Da from positions 2 - 218. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03952 mRNA. Translation: AAA37747.1.
J04632 mRNA. Translation: AAA37705.1.
L13448 Genomic DNA. No translation available.
AL671877, AC079042 Genomic DNA. Translation: CAM17697.1.
BC003822 mRNA. Translation: AAH03822.1.
BC046758 mRNA. Translation: AAH46758.1.
BC091763 mRNA. Translation: AAH91763.1.
CCDSiCCDS17747.1.
PIRiH24735.
S30373.
S33860.
RefSeqiNP_034488.1. NM_010358.5.
UniGeneiMm.37199.

Genome annotation databases

EnsembliENSMUST00000004140; ENSMUSP00000004140; ENSMUSG00000058135.
GeneIDi14862.
KEGGimmu:14862.
UCSCiuc008qxx.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03952 mRNA. Translation: AAA37747.1.
J04632 mRNA. Translation: AAA37705.1.
L13448 Genomic DNA. No translation available.
AL671877, AC079042 Genomic DNA. Translation: CAM17697.1.
BC003822 mRNA. Translation: AAH03822.1.
BC046758 mRNA. Translation: AAH46758.1.
BC091763 mRNA. Translation: AAH91763.1.
CCDSiCCDS17747.1.
PIRiH24735.
S30373.
S33860.
RefSeqiNP_034488.1. NM_010358.5.
UniGeneiMm.37199.

3D structure databases

ProteinModelPortaliP10649.
SMRiP10649. Positions 2-218.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200094. 2 interactions.
IntActiP10649. 5 interactions.
MINTiMINT-1869211.
STRINGi10090.ENSMUSP00000004140.

Chemistry

ChEMBLiCHEMBL3722.

PTM databases

PhosphoSiteiP10649.

2D gel databases

REPRODUCTION-2DPAGEP10649.
SWISS-2DPAGEP10649.

Proteomic databases

MaxQBiP10649.
PaxDbiP10649.
PRIDEiP10649.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000004140; ENSMUSP00000004140; ENSMUSG00000058135.
GeneIDi14862.
KEGGimmu:14862.
UCSCiuc008qxx.2. mouse.

Organism-specific databases

CTDi2944.
MGIiMGI:95860. Gstm1.

Phylogenomic databases

eggNOGiNOG300089.
GeneTreeiENSGT00550000074559.
HOGENOMiHOG000115735.
HOVERGENiHBG106842.
InParanoidiP10649.
KOiK00799.
OMAiQLAVICY.
OrthoDBiEOG7KH9M3.
PhylomeDBiP10649.
TreeFamiTF353040.

Enzyme and pathway databases

ReactomeiREACT_317599. Glutathione conjugation.

Miscellaneous databases

ChiTaRSiGstm1. mouse.
NextBioi287105.
PROiP10649.
SOURCEiSearch...

Gene expression databases

BgeeiP10649.
CleanExiMM_GSTM1.
ExpressionAtlasiP10649. baseline and differential.
GenevisibleiP10649. MM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Tissue-specific induction of murine glutathione transferase mRNAs by butylated hydroxyanisole."
    Pearson W.R., Reinhart J., Sisk S.C., Anderson K.S., Adler P.N.
    J. Biol. Chem. 263:13324-13332(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Isolation, characterization, and expression in Escherichia coli of two murine Mu class glutathione S-transferase cDNAs homologous to the rat subunits 3 (Yb1) and 4 (Yb2)."
    Townsend A.J., Goldsmith M.E., Pickett C.B., Cowan K.H.
    J. Biol. Chem. 264:21582-21590(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The structure of two murine class-mu glutathione transferase genes coordinately induced by butylated hydroxyanisole."
    Reinhart J., Pearson W.R.
    Arch. Biochem. Biophys. 303:383-393(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "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].
    Strain: C57BL/6 and FVB/N.
    Tissue: Brain and Liver.
  6. "Increased synthesis of glutathione S-transferases in response to anticarcinogenic antioxidants. Cloning and measurement of messenger RNA."
    Pearson W.R., Windle J.J., Morrow J.F., Benson A.M., Talalay P.
    J. Biol. Chem. 258:2052-2062(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-41.
  7. "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: PRELIMINARY PROTEIN SEQUENCE OF 2-25.
  8. Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-11; 19-31; 33-43; 53-78; 97-108; 137-144; 153-168; 174-192 AND 203-211, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6 and OF1.
    Tissue: Brain and Hippocampus.
  9. "Purification, mass spectrometric characterization, and covalent modification of murine glutathione S-transferases."
    Mitchell A.E., Morin D., Lame M.W., Jones A.D.
    Chem. Res. Toxicol. 8:1054-1062(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, MASS SPECTROMETRY.
    Strain: CD-1.
    Tissue: Liver.

Entry informationi

Entry nameiGSTM1_MOUSE
AccessioniPrimary (citable) accession number: P10649
Secondary accession number(s): A2AE90, Q58ET5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.