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Protein

Glutathione S-transferase Mu 3

Gene

GSTM3

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. May govern uptake and detoxification of both endogenous compounds and xenobiotics at the testis and brain blood barriers.1 Publication

Catalytic activityi

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

Kineticsi

  1. KM=1.1 mM for 1-chloro-2,4-dinitrobenzene1 Publication
  2. KM=0.084 mM for glutathione1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei120 – 1201SubstrateBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    • cellular detoxification of nitrogen compound Source: BHF-UCL
    • establishment of blood-nerve barrier Source: ProtInc
    • glutathione derivative biosynthetic process Source: Reactome
    • glutathione metabolic process Source: UniProtKB
    • nitrobenzene metabolic process Source: BHF-UCL
    • response to estrogen Source: UniProtKB
    • small molecule metabolic process Source: Reactome
    • xenobiotic catabolic process Source: BHF-UCL
    • xenobiotic metabolic process Source: Reactome
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    BRENDAi2.5.1.18. 2681.
    ReactomeiREACT_6926. Glutathione conjugation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase Mu 3 (EC:2.5.1.18)
    Alternative name(s):
    GST class-mu 3
    GSTM3-3
    Short name:
    hGSTM3-3
    Gene namesi
    Name:GSTM3
    Synonyms:GST5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:4635. GSTM3.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: BHF-UCL
    • cytosol Source: Reactome
    • extracellular exosome Source: UniProtKB
    • nucleus Source: UniProtKB
    • sperm fibrous sheath Source: Ensembl
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi120 – 1201Y → A: No effect. 1 Publication
    Mutagenesisi120 – 1201Y → F: Strongly increased catalytic activity. 1 Publication
    Mutagenesisi213 – 2131N → F: Strongly increased catalytic activity. 1 Publication
    Mutagenesisi213 – 2131N → G: No effect. 1 Publication

    Organism-specific databases

    PharmGKBiPA29024.

    Chemistry

    DrugBankiDB00143. Glutathione.
    DB00163. Vitamin E.

    Polymorphism and mutation databases

    BioMutaiGSTM3.
    DMDMi21264423.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 225225Glutathione S-transferase Mu 3PRO_0000185822Add
    BLAST

    Post-translational modificationi

    The N-terminus is blocked.

    Proteomic databases

    PaxDbiP21266.
    PeptideAtlasiP21266.
    PRIDEiP21266.

    2D gel databases

    OGPiP21266.
    REPRODUCTION-2DPAGEIPI00246975.

    PTM databases

    PhosphoSiteiP21266.

    Expressioni

    Tissue specificityi

    Testis and brain.

    Gene expression databases

    BgeeiP21266.
    CleanExiHS_GSTM3.
    ExpressionAtlasiP21266. baseline and differential.
    GenevestigatoriP21266.

    Organism-specific databases

    HPAiCAB017130.
    CAB040583.
    HPA035190.
    HPA055972.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-350350,EBI-350350

    Protein-protein interaction databases

    BioGridi109202. 25 interactions.
    IntActiP21266. 3 interactions.
    STRINGi9606.ENSP00000256594.

    Structurei

    Secondary structure

    1
    225
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 159Combined sources
    Helixi16 – 183Combined sources
    Helixi19 – 279Combined sources
    Beta strandi32 – 376Combined sources
    Beta strandi42 – 443Combined sources
    Helixi48 – 547Combined sources
    Beta strandi64 – 696Combined sources
    Beta strandi72 – 765Combined sources
    Helixi77 – 8711Combined sources
    Helixi95 – 12026Combined sources
    Helixi124 – 14623Combined sources
    Beta strandi154 – 1563Combined sources
    Helixi159 – 17416Combined sources
    Helixi176 – 1794Combined sources
    Helixi183 – 19311Combined sources
    Helixi196 – 2038Combined sources
    Helixi205 – 2084Combined sources
    Beta strandi211 – 2133Combined sources
    Beta strandi217 – 2204Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3GTUX-ray2.80B/D2-225[»]
    ProteinModelPortaliP21266.
    SMRiP21266. Positions 2-225.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP21266.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 9288GST N-terminalAdd
    BLAST
    Domaini94 – 212119GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni11 – 122Glutathione bindingBy similarity
    Regioni50 – 545Glutathione bindingBy similarity
    Regioni63 – 642Glutathione bindingBy similarity
    Regioni76 – 772Glutathione 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.
    HOVERGENiHBG106842.
    InParanoidiP21266.
    KOiK00799.
    OMAiMSCESSM.
    OrthoDBiEOG7KH9M3.
    PhylomeDBiP21266.
    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.

    P21266-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSCESSMVLG YWDIRGLAHA IRLLLEFTDT SYEEKRYTCG EAPDYDRSQW
    60 70 80 90 100
    LDVKFKLDLD FPNLPYLLDG KNKITQSNAI LRYIARKHNM CGETEEEKIR
    110 120 130 140 150
    VDIIENQVMD FRTQLIRLCY SSDHEKLKPQ YLEELPGQLK QFSMFLGKFS
    160 170 180 190 200
    WFAGEKLTFV DFLTYDILDQ NRIFDPKCLD EFPNLKAFMC RFEALEKIAA
    210 220
    YLQSDQFCKM PINNKMAQWG NKPVC
    Length:225
    Mass (Da):26,560
    Last modified:January 23, 2007 - v3
    Checksum:i79093161ECEF5396
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti147 – 1471G → W in AAA60964 (PubMed:2345169).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti224 – 2241V → I.1 Publication
    Corresponds to variant rs7483 [ dbSNP | Ensembl ].
    VAR_014498

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J05459 mRNA. Translation: AAA60964.1.
    AF043105 Genomic DNA. Translation: AAC17866.1.
    BT019945 mRNA. Translation: AAV38748.1.
    BC000088 mRNA. Translation: AAH00088.1.
    BC008790 mRNA. Translation: AAH08790.1.
    CCDSiCCDS812.1.
    PIRiA35295.
    RefSeqiNP_000840.2. NM_000849.4.
    UniGeneiHs.2006.

    Genome annotation databases

    EnsembliENST00000256594; ENSP00000256594; ENSG00000134202.
    ENST00000361066; ENSP00000354357; ENSG00000134202.
    GeneIDi2947.
    KEGGihsa:2947.
    UCSCiuc001dyo.2. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J05459 mRNA. Translation: AAA60964.1.
    AF043105 Genomic DNA. Translation: AAC17866.1.
    BT019945 mRNA. Translation: AAV38748.1.
    BC000088 mRNA. Translation: AAH00088.1.
    BC008790 mRNA. Translation: AAH08790.1.
    CCDSiCCDS812.1.
    PIRiA35295.
    RefSeqiNP_000840.2. NM_000849.4.
    UniGeneiHs.2006.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3GTUX-ray2.80B/D2-225[»]
    ProteinModelPortaliP21266.
    SMRiP21266. Positions 2-225.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi109202. 25 interactions.
    IntActiP21266. 3 interactions.
    STRINGi9606.ENSP00000256594.

    Chemistry

    ChEMBLiCHEMBL2242.
    DrugBankiDB00143. Glutathione.
    DB00163. Vitamin E.

    PTM databases

    PhosphoSiteiP21266.

    Polymorphism and mutation databases

    BioMutaiGSTM3.
    DMDMi21264423.

    2D gel databases

    OGPiP21266.
    REPRODUCTION-2DPAGEIPI00246975.

    Proteomic databases

    PaxDbiP21266.
    PeptideAtlasiP21266.
    PRIDEiP21266.

    Protocols and materials databases

    DNASUi2947.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000256594; ENSP00000256594; ENSG00000134202.
    ENST00000361066; ENSP00000354357; ENSG00000134202.
    GeneIDi2947.
    KEGGihsa:2947.
    UCSCiuc001dyo.2. human.

    Organism-specific databases

    CTDi2947.
    GeneCardsiGC01M110276.
    HGNCiHGNC:4635. GSTM3.
    HPAiCAB017130.
    CAB040583.
    HPA035190.
    HPA055972.
    MIMi138390. gene.
    neXtProtiNX_P21266.
    PharmGKBiPA29024.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiNOG300089.
    HOVERGENiHBG106842.
    InParanoidiP21266.
    KOiK00799.
    OMAiMSCESSM.
    OrthoDBiEOG7KH9M3.
    PhylomeDBiP21266.
    TreeFamiTF353040.

    Enzyme and pathway databases

    BRENDAi2.5.1.18. 2681.
    ReactomeiREACT_6926. Glutathione conjugation.

    Miscellaneous databases

    EvolutionaryTraceiP21266.
    GeneWikiiGSTM3.
    GenomeRNAii2947.
    NextBioi11678.
    PROiP21266.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP21266.
    CleanExiHS_GSTM3.
    ExpressionAtlasiP21266. baseline and differential.
    GenevestigatoriP21266.

    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. "A distinct human testis and brain mu-class glutathione S-transferase. Molecular cloning and characterization of a form present even in individuals lacking hepatic type mu isoenzymes."
      Campbell E., Takahashi Y., Abramovitz M., Peretz M., Listowsky I.
      J. Biol. Chem. 265:9188-9193(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Tissue: Brain and Testis.
    2. "Distinctive structure of the human GSTM3 gene-inverted orientation relative to the mu class glutathione transferase gene cluster."
      Patskovsky Y.V., Huang M.Q., Takayama T., Listowsky I., Pearson W.R.
      Arch. Biochem. Biophys. 361:85-93(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "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], VARIANT ILE-224.
      Tissue: Brain and Uterus.
    5. "Molecular cloning and heterologous expression of an alternatively spliced human Mu class glutathione S-transferase transcript."
      Ross V.L., Board P.G.
      Biochem. J. 294:373-380(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF N-TERMINUS.
      Tissue: Testis.
    6. "Human Mu-class glutathione S-transferases present in liver, skeletal muscle and testicular tissue."
      Hussey A.J., Hayes J.D.
      Biochim. Biophys. Acta 1203:131-141(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 190-209.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "An asparagine-phenylalanine substitution accounts for catalytic differences between hGSTM3-3 and other human class mu glutathione S-transferases."
      Patskovsky Y.V., Patskovska L.N., Listowsky I.
      Biochemistry 38:16187-16194(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF TYR-120 AND ASN-213.

    Entry informationi

    Entry nameiGSTM3_HUMAN
    AccessioniPrimary (citable) accession number: P21266
    Secondary accession number(s): O60550, Q96HA3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: January 23, 2007
    Last modified: May 27, 2015
    This is version 170 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

    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.