Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P10649 (GSTM1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·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 1-1
GST class-mu 1
Glutathione S-transferase GT8.7
pmGT10
Gene names
Name:Gstm1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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.

Catalytic activity

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

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the GST superfamily. Mu family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Mass spectrometry

Molecular mass is 25838.4±2 Da from positions 2 - 218. Determined by ESI. Ref.9

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6 Ref.7 Ref.8
Chain2 – 218217Glutathione S-transferase Mu 1
PRO_0000185826

Regions

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

Sites

Binding site1161Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P10649 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 91AE34A1B5B44599

FASTA21825,970
        10         20         30         40         50         60 
MPMILGYWNV RGLTHPIRML LEYTDSSYDE KRYTMGDAPD FDRSQWLNEK FKLGLDFPNL 

        70         80         90        100        110        120 
PYLIDGSHKI TQSNAILRYL ARKHHLDGET EEERIRADIV ENQVMDTRMQ LIMLCYNPDF 

       130        140        150        160        170        180 
EKQKPEFLKT IPEKMKLYSE FLGKRPWFAG DKVTYVDFLA YDILDQYRMF EPKCLDAFPN 

       190        200        210 
LRDFLARFEG LKKISAYMKS SRYIATPIFS KMAHWSNK 

« Hide

References

« Hide 'large scale' references
[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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS17747.1.
PIRH24735.
S30373.
S33860.
RefSeqNP_034488.1. NM_010358.5.
UniGeneMm.37199.

3D structure databases

ProteinModelPortalP10649.
SMRP10649. Positions 2-218.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200094. 1 interaction.
IntActP10649. 5 interactions.
MINTMINT-1869211.

Chemistry

ChEMBLCHEMBL3722.

PTM databases

PhosphoSiteP10649.

2D gel databases

REPRODUCTION-2DPAGEP10649.
SWISS-2DPAGEP10649.

Proteomic databases

MaxQBP10649.
PaxDbP10649.
PRIDEP10649.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000004140; ENSMUSP00000004140; ENSMUSG00000058135.
GeneID14862.
KEGGmmu:14862.
UCSCuc008qxx.2. mouse.

Organism-specific databases

CTD2944.
MGIMGI:95860. Gstm1.

Phylogenomic databases

eggNOGNOG300089.
GeneTreeENSGT00550000074559.
HOGENOMHOG000115735.
HOVERGENHBG106842.
KOK00799.
OMAFIMLCYN.
OrthoDBEOG7KH9M3.
PhylomeDBP10649.
TreeFamTF353040.

Gene expression databases

ArrayExpressP10649.
BgeeP10649.
CleanExMM_GSTM1.
GenevestigatorP10649.

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. mouse.
NextBio287105.
PROP10649.
SOURCESearch...

Entry information

Entry nameGSTM1_MOUSE
AccessionPrimary (citable) accession number: P10649
Secondary accession number(s): A2AE90, Q58ET5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot