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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)DescriptionActionsGraphical viewLength
    Binding sitei120SubstrateBy similarity1

    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
    • xenobiotic catabolic process Source: BHF-UCL
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    BioCyciZFISH:HS05833-MONOMER.
    BRENDAi2.5.1.18. 2681.
    ReactomeiR-HSA-156590. 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
    Proteomesi
    • UP000005640 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)DescriptionActionsGraphical viewLength
    Mutagenesisi120Y → A: No effect. 1 Publication1
    Mutagenesisi120Y → F: Strongly increased catalytic activity. 1 Publication1
    Mutagenesisi213N → F: Strongly increased catalytic activity. 1 Publication1
    Mutagenesisi213N → G: No effect. 1 Publication1

    Organism-specific databases

    DisGeNETi2947.
    OpenTargetsiENSG00000134202.
    PharmGKBiPA29024.

    Chemistry databases

    ChEMBLiCHEMBL2242.
    DrugBankiDB00143. Glutathione.
    DB00163. Vitamin E.

    Polymorphism and mutation databases

    BioMutaiGSTM3.
    DMDMi21264423.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001858221 – 225Glutathione S-transferase Mu 3Add BLAST225

    Post-translational modificationi

    The N-terminus is blocked.

    Proteomic databases

    EPDiP21266.
    PaxDbiP21266.
    PeptideAtlasiP21266.
    PRIDEiP21266.

    2D gel databases

    OGPiP21266.
    REPRODUCTION-2DPAGEIPI00246975.

    PTM databases

    iPTMnetiP21266.
    PhosphoSitePlusiP21266.

    Expressioni

    Tissue specificityi

    Testis and brain.

    Gene expression databases

    BgeeiENSG00000134202.
    CleanExiHS_GSTM3.
    ExpressionAtlasiP21266. baseline and differential.
    GenevisibleiP21266. HS.

    Organism-specific databases

    HPAiCAB017130.
    CAB040583.
    HPA035190.
    HPA055972.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself6EBI-350350,EBI-350350

    GO - Molecular functioni

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

    Protein-protein interaction databases

    BioGridi109202. 23 interactors.
    IntActiP21266. 4 interactors.
    STRINGi9606.ENSP00000256594.

    Structurei

    Secondary structure

    1225
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi7 – 15Combined sources9
    Helixi16 – 18Combined sources3
    Helixi19 – 27Combined sources9
    Beta strandi32 – 37Combined sources6
    Beta strandi42 – 44Combined sources3
    Helixi48 – 54Combined sources7
    Beta strandi64 – 69Combined sources6
    Beta strandi72 – 76Combined sources5
    Helixi77 – 87Combined sources11
    Helixi95 – 120Combined sources26
    Helixi124 – 146Combined sources23
    Beta strandi154 – 156Combined sources3
    Helixi159 – 174Combined sources16
    Helixi176 – 179Combined sources4
    Helixi183 – 193Combined sources11
    Helixi196 – 203Combined sources8
    Helixi205 – 208Combined sources4
    Beta strandi211 – 213Combined sources3
    Beta strandi217 – 220Combined sources4

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiP21266.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini5 – 92GST N-terminalAdd BLAST88
    Domaini94 – 212GST C-terminalAdd BLAST119

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni11 – 12Glutathione bindingBy similarity2
    Regioni50 – 54Glutathione bindingBy similarity5
    Regioni63 – 64Glutathione bindingBy similarity2
    Regioni76 – 77Glutathione bindingBy similarity2

    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.
    HOVERGENiHBG106842.
    InParanoidiP21266.
    KOiK00799.
    OMAiQVMDFRM.
    OrthoDBiEOG091G0K2E.
    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)DescriptionActionsGraphical viewLength
    Sequence conflicti147G → W in AAA60964 (PubMed:2345169).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_014498224V → I.1 PublicationCorresponds to variant rs7483dbSNPEnsembl.1

    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.

    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3GTUX-ray2.80B/D2-225[»]
    ProteinModelPortaliP21266.
    SMRiP21266.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi109202. 23 interactors.
    IntActiP21266. 4 interactors.
    STRINGi9606.ENSP00000256594.

    Chemistry databases

    ChEMBLiCHEMBL2242.
    DrugBankiDB00143. Glutathione.
    DB00163. Vitamin E.

    PTM databases

    iPTMnetiP21266.
    PhosphoSitePlusiP21266.

    Polymorphism and mutation databases

    BioMutaiGSTM3.
    DMDMi21264423.

    2D gel databases

    OGPiP21266.
    REPRODUCTION-2DPAGEIPI00246975.

    Proteomic databases

    EPDiP21266.
    PaxDbiP21266.
    PeptideAtlasiP21266.
    PRIDEiP21266.

    Protocols and materials databases

    DNASUi2947.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000256594; ENSP00000256594; ENSG00000134202.
    ENST00000361066; ENSP00000354357; ENSG00000134202.
    GeneIDi2947.
    KEGGihsa:2947.

    Organism-specific databases

    CTDi2947.
    DisGeNETi2947.
    GeneCardsiGSTM3.
    HGNCiHGNC:4635. GSTM3.
    HPAiCAB017130.
    CAB040583.
    HPA035190.
    HPA055972.
    MIMi138390. gene.
    neXtProtiNX_P21266.
    OpenTargetsiENSG00000134202.
    PharmGKBiPA29024.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiENOG410IN5J. Eukaryota.
    ENOG4110YU0. LUCA.
    GeneTreeiENSGT00550000074559.
    HOVERGENiHBG106842.
    InParanoidiP21266.
    KOiK00799.
    OMAiQVMDFRM.
    OrthoDBiEOG091G0K2E.
    PhylomeDBiP21266.
    TreeFamiTF353040.

    Enzyme and pathway databases

    BioCyciZFISH:HS05833-MONOMER.
    BRENDAi2.5.1.18. 2681.
    ReactomeiR-HSA-156590. Glutathione conjugation.

    Miscellaneous databases

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

    Gene expression databases

    BgeeiENSG00000134202.
    CleanExiHS_GSTM3.
    ExpressionAtlasiP21266. baseline and differential.
    GenevisibleiP21266. 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]
    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...

    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: November 30, 2016
    This is version 183 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.