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P10649

- GSTM1_MOUSE

UniProt

P10649 - GSTM1_MOUSE

Protein

Glutathione S-transferase Mu 1

Gene

Gstm1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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

    1. glutathione transferase activity Source: UniProtKB-EC
    2. protein binding Source: MGI
    3. protein heterodimerization activity Source: MGI
    4. protein homodimerization activity Source: MGI

    GO - Biological processi

    1. cellular response to drug Source: MGI

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    ReactomeiREACT_215316. 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: Chromosome 3

    Organism-specific databases

    MGIiMGI:95860. Gstm1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    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

    ArrayExpressiP10649.
    BgeeiP10649.
    CleanExiMM_GSTM1.
    GenevestigatoriP10649.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi200094. 1 interaction.
    IntActiP10649. 5 interactions.
    MINTiMINT-1869211.

    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.
    KOiK00799.
    OMAiFIMLCYN.
    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

    MPMILGYWNV RGLTHPIRML LEYTDSSYDE KRYTMGDAPD FDRSQWLNEK    50
    FKLGLDFPNL PYLIDGSHKI TQSNAILRYL ARKHHLDGET EEERIRADIV 100
    ENQVMDTRMQ LIMLCYNPDF EKQKPEFLKT IPEKMKLYSE FLGKRPWFAG 150
    DKVTYVDFLA YDILDQYRMF EPKCLDAFPN LRDFLARFEG LKKISAYMKS 200
    SRYIATPIFS KMAHWSNK 218
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS17747.1.
    PIRi H24735.
    S30373.
    S33860.
    RefSeqi NP_034488.1. NM_010358.5.
    UniGenei Mm.37199.

    3D structure databases

    ProteinModelPortali P10649.
    SMRi P10649. Positions 2-218.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200094. 1 interaction.
    IntActi P10649. 5 interactions.
    MINTi MINT-1869211.

    Chemistry

    ChEMBLi CHEMBL3722.

    PTM databases

    PhosphoSitei P10649.

    2D gel databases

    REPRODUCTION-2DPAGE P10649.
    SWISS-2DPAGE P10649.

    Proteomic databases

    MaxQBi P10649.
    PaxDbi P10649.
    PRIDEi P10649.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000004140 ; ENSMUSP00000004140 ; ENSMUSG00000058135 .
    GeneIDi 14862.
    KEGGi mmu:14862.
    UCSCi uc008qxx.2. mouse.

    Organism-specific databases

    CTDi 2944.
    MGIi MGI:95860. Gstm1.

    Phylogenomic databases

    eggNOGi NOG300089.
    GeneTreei ENSGT00550000074559.
    HOGENOMi HOG000115735.
    HOVERGENi HBG106842.
    KOi K00799.
    OMAi FIMLCYN.
    OrthoDBi EOG7KH9M3.
    PhylomeDBi P10649.
    TreeFami TF353040.

    Enzyme and pathway databases

    Reactomei REACT_215316. Glutathione conjugation.

    Miscellaneous databases

    ChiTaRSi GSTM1. mouse.
    NextBioi 287105.
    PROi P10649.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P10649.
    Bgeei P10649.
    CleanExi MM_GSTM1.
    Genevestigatori P10649.

    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

    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: October 1, 2014
    This is version 147 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