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P20136

- GSTM2_CHICK

UniProt

P20136 - GSTM2_CHICK

Protein

Glutathione S-transferase 2

Gene

GSTM2

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 4 (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.1 Publication

    Sites

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

    GO - Molecular functioni

    1. glutathione transferase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Transferase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase 2 (EC:2.5.1.18)
    Alternative name(s):
    GST class-mu
    GST-CL2
    GSTM1-1
    Gene namesi
    Name:GSTM2
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi108 – 1081R → E: Reduced affinity for glutathione. 1 Publication
    Mutagenesisi108 – 1081R → L: Reduced catalytic activity. 1 Publication
    Mutagenesisi210 – 2101W → F: Reduced affinity for glutathione. 1 Publication
    Mutagenesisi210 – 2101W → H, I or P: Reduced catalytic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 220219Glutathione S-transferase 2PRO_0000185838Add
    BLAST

    Proteomic databases

    PRIDEiP20136.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Structurei

    Secondary structure

    1
    220
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 119
    Helixi12 – 143
    Helixi15 – 239
    Beta strandi28 – 336
    Turni38 – 403
    Helixi44 – 474
    Helixi50 – 523
    Beta strandi60 – 656
    Beta strandi68 – 725
    Helixi73 – 8210
    Turni83 – 853
    Helixi91 – 11626
    Helixi120 – 14223
    Beta strandi146 – 1527
    Helixi155 – 17016
    Helixi175 – 1773
    Helixi180 – 18910
    Helixi192 – 1987
    Beta strandi200 – 2023
    Beta strandi214 – 2163

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1C72X-ray2.80A/B/C/D2-220[»]
    1GSUX-ray1.94A/B2-220[»]
    ProteinModelPortaliP20136.
    SMRiP20136. Positions 2-218.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP20136.

    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 binding
    Regioni46 – 505Glutathione binding
    Regioni59 – 602Glutathione binding
    Regioni72 – 732Glutathione binding

    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

    HOVERGENiHBG106842.
    KOiK00799.
    PhylomeDBiP20136.

    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.

    P20136-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVVTLGYWDI RGLAHAIRLL LEYTETPYQE RRYKAGPAPD FDPSDWTNEK    50
    EKLGLDFPNL PYLIDGDVKL TQSNAILRYI ARKHNMCGET EVEKQRVDVL 100
    ENHLMDLRMA FARLCYSPDF EKLKPAYLEQ LPGKLRQLSR FLGSRSWFVG 150
    DKLTFVDFLA YDVLDQQRMF VPDCPELQGN LSQFLQRFEA LEKISAYMRS 200
    GRFMKAPIFW YTALWNNKKE 220
    Length:220
    Mass (Da):25,893
    Last modified:January 23, 2007 - v4
    Checksum:iA7A7D843CE54E6F9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58248 mRNA. Translation: CAA41202.1.
    PIRiS18464.
    RefSeqiNP_990421.1. NM_205090.1.
    UniGeneiGga.4223.

    Genome annotation databases

    GeneIDi395976.
    KEGGigga:395976.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58248 mRNA. Translation: CAA41202.1 .
    PIRi S18464.
    RefSeqi NP_990421.1. NM_205090.1.
    UniGenei Gga.4223.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1C72 X-ray 2.80 A/B/C/D 2-220 [» ]
    1GSU X-ray 1.94 A/B 2-220 [» ]
    ProteinModelPortali P20136.
    SMRi P20136. Positions 2-218.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P20136.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 395976.
    KEGGi gga:395976.

    Organism-specific databases

    CTDi 2946.

    Phylogenomic databases

    HOVERGENi HBG106842.
    KOi K00799.
    PhylomeDBi P20136.

    Miscellaneous databases

    EvolutionaryTracei P20136.
    NextBioi 20816041.

    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. "Nucleotide sequence of a class mu glutathione S-transferase from chicken liver."
      Liu L.-F., Tam M.F.
      Biochim. Biophys. Acta 1090:343-344(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: White leghorn.
      Tissue: Liver.
    2. "Characterization of glutathione S-transferases from day-old chick livers."
      Chang L.-H., Chuang L.-F., Tsai C.-P., Tu C.-P.D., Tam M.F.
      Biochemistry 29:744-750(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-35.
      Tissue: Liver.
    3. Liu L.-F.
      Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 130.
    4. "The three-dimensional structure of an avian class-mu glutathione S-transferase, cGSTM1-1 at 1.94-A resolution."
      Sun Y.-J., Kuan I.-C., Tam M.F., Hsiao C.-D.
      J. Mol. Biol. 278:239-252(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE ANALOG.
    5. "Tyr115, gln165 and trp209 contribute to the 1, 2-epoxy-3-(p-nitrophenoxy)propane-conjugating activity of glutathione S-transferase cGSTM1-1."
      Chern M.K., Wu T.C., Hsieh C.H., Chou C.C., Liu L.F., Kuan I.C., Yeh Y.H., Hsiao C.D., Tam M.F.
      J. Mol. Biol. 300:1257-1269(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE ANALOG, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-108 AND TRP-210.

    Entry informationi

    Entry nameiGSTM2_CHICK
    AccessioniPrimary (citable) accession number: P20136
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 105 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3