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P24473

- GSTK1_RAT

UniProt

P24473 - GSTK1_RAT

Protein

Glutathione S-transferase kappa 1

Gene

Gstk1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Might confer protection against genotoxic and cytotoxic electrophiles in the mitochondrial compartment.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei53 – 531Glutathione1 Publication
    Binding sitei183 – 1831Glutathione; via amide nitrogen and carbonyl oxygen1 Publication

    GO - Molecular functioni

    1. glutathione peroxidase activity Source: Ensembl
    2. glutathione transferase activity Source: UniProtKB-EC
    3. protein disulfide oxidoreductase activity Source: InterPro

    GO - Biological processi

    1. glutathione metabolic process Source: Ensembl

    Keywords - Molecular functioni

    Transferase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase kappa 1 (EC:2.5.1.18)
    Alternative name(s):
    GST 13-13
    GST class-kappa
    GSTK1-1
    Short name:
    rGSTK1
    Glutathione S-transferase subunit 13
    Gene namesi
    Name:Gstk1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 4

    Organism-specific databases

    RGDi735188. Gstk1.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: Ensembl
    2. mitochondrial matrix Source: HGNC
    3. peroxisome Source: Ensembl

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi16 – 161S → A: Reduces catalytic activity about 30-fold. Reduces affinity for glutathione about 4-fold. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 226225Glutathione S-transferase kappa 1PRO_0000185893Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei36 – 361N6-succinyllysineBy similarity
    Modified residuei49 – 491N6-succinyllysineBy similarity
    Modified residuei68 – 681N6-acetyllysine; alternateBy similarity
    Modified residuei68 – 681N6-succinyllysine; alternateBy similarity
    Modified residuei74 – 741N6-acetyllysine; alternateBy similarity
    Modified residuei74 – 741N6-succinyllysine; alternateBy similarity
    Modified residuei85 – 851N6-acetyllysineBy similarity
    Modified residuei93 – 931N6-acetyllysine; alternateBy similarity
    Modified residuei93 – 931N6-succinyllysine; alternateBy similarity
    Modified residuei116 – 1161N6-acetyllysine; alternateBy similarity
    Modified residuei116 – 1161N6-succinyllysine; alternateBy similarity
    Modified residuei144 – 1441N6-succinyllysineBy similarity
    Modified residuei158 – 1581N6-acetyllysine; alternateBy similarity
    Modified residuei158 – 1581N6-succinyllysine; alternateBy similarity
    Modified residuei165 – 1651N6-acetyllysineBy similarity
    Modified residuei167 – 1671N6-acetyllysine; alternateBy similarity
    Modified residuei167 – 1671N6-succinyllysine; alternateBy similarity
    Modified residuei177 – 1771N6-acetyllysine; alternateBy similarity
    Modified residuei177 – 1771N6-succinyllysine; alternateBy similarity
    Modified residuei193 – 1931N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP24473.
    PRIDEiP24473.

    PTM databases

    PhosphoSiteiP24473.

    Expressioni

    Gene expression databases

    GenevestigatoriP24473.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    IntActiP24473. 1 interaction.
    MINTiMINT-4589693.
    STRINGi10116.ENSRNOP00000022275.

    Structurei

    Secondary structure

    1
    226
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 127
    Helixi17 – 2913
    Turni30 – 323
    Beta strandi33 – 419
    Helixi44 – 507
    Helixi60 – 7718
    Turni87 – 893
    Helixi90 – 945
    Helixi97 – 10913
    Helixi111 – 1133
    Helixi114 – 12613
    Helixi135 – 14410
    Helixi149 – 1568
    Turni157 – 1604
    Helixi162 – 17716
    Beta strandi185 – 1906
    Beta strandi193 – 1997
    Helixi203 – 2108

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1R4WX-ray2.50A/B/C/D1-226[»]
    ProteinModelPortaliP24473.
    SMRiP24473. Positions 2-222.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP24473.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni16 – 183Glutathione binding
    Regioni200 – 2012Glutathione binding

    Sequence similaritiesi

    Belongs to the GST superfamily. Kappa family.Curated

    Phylogenomic databases

    eggNOGiCOG3917.
    GeneTreeiENSGT00440000033697.
    HOGENOMiHOG000219769.
    HOVERGENiHBG051852.
    InParanoidiP24473.
    KOiK13299.
    OMAiELWRRIW.
    OrthoDBiEOG793B9B.
    PhylomeDBiP24473.
    TreeFamiTF105323.

    Family and domain databases

    Gene3Di3.40.30.10. 1 hit.
    InterProiIPR001853. DSBA-like_thioredoxin_dom.
    IPR014440. HCCAis_GSTk.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF01323. DSBA. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006386. HCCAis_GSTk. 1 hit.
    SUPFAMiSSF52833. SSF52833. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P24473-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGPAPRVLEL FYDVLSPYSW LGFEVLCRYQ HLWNIKLKLR PALLAGIMKD    50
    SGNQPPAMVP HKGQYILKEI PLLKQLFQVP MSVPKDFFGE HVKKGTVNAM 100
    RFLTAVSMEQ PEMLEKVSRE LWMRIWSRDE DITESQNILS AAEKAGMATA 150
    QAQHLLNKIS TELVKSKLRE TTGAACKYGA FGLPTTVAHV DGKTYMLFGS 200
    DRMELLAYLL GEKWMGPVPP TLNARL 226
    Length:226
    Mass (Da):25,493
    Last modified:January 23, 2007 - v3
    Checksum:iD1E5514C5A65B3CC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21G → C AA sequence (PubMed:1883325)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S83436 mRNA. Translation: AAB50831.1.
    PIRiS17164.
    RefSeqiNP_852036.1. NM_181371.2.
    UniGeneiRn.109452.

    Genome annotation databases

    EnsembliENSRNOT00000022275; ENSRNOP00000022275; ENSRNOG00000016484.
    GeneIDi297029.
    KEGGirno:297029.
    UCSCiRGD:735188. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S83436 mRNA. Translation: AAB50831.1 .
    PIRi S17164.
    RefSeqi NP_852036.1. NM_181371.2.
    UniGenei Rn.109452.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1R4W X-ray 2.50 A/B/C/D 1-226 [» ]
    ProteinModelPortali P24473.
    SMRi P24473. Positions 2-222.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P24473. 1 interaction.
    MINTi MINT-4589693.
    STRINGi 10116.ENSRNOP00000022275.

    Chemistry

    DrugBanki DB00143. Glutathione.

    PTM databases

    PhosphoSitei P24473.

    Proteomic databases

    PaxDbi P24473.
    PRIDEi P24473.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000022275 ; ENSRNOP00000022275 ; ENSRNOG00000016484 .
    GeneIDi 297029.
    KEGGi rno:297029.
    UCSCi RGD:735188. rat.

    Organism-specific databases

    CTDi 373156.
    RGDi 735188. Gstk1.

    Phylogenomic databases

    eggNOGi COG3917.
    GeneTreei ENSGT00440000033697.
    HOGENOMi HOG000219769.
    HOVERGENi HBG051852.
    InParanoidi P24473.
    KOi K13299.
    OMAi ELWRRIW.
    OrthoDBi EOG793B9B.
    PhylomeDBi P24473.
    TreeFami TF105323.

    Miscellaneous databases

    EvolutionaryTracei P24473.
    NextBioi 642014.
    PROi P24473.

    Gene expression databases

    Genevestigatori P24473.

    Family and domain databases

    Gene3Di 3.40.30.10. 1 hit.
    InterProi IPR001853. DSBA-like_thioredoxin_dom.
    IPR014440. HCCAis_GSTk.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF01323. DSBA. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF006386. HCCAis_GSTk. 1 hit.
    SUPFAMi SSF52833. SSF52833. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Glutathione S-transferase class Kappa: characterization by the cloning of rat mitochondrial GST and identification of a human homologue."
      Pemble S.E., Wardle A.F., Taylor J.B.
      Biochem. J. 319:749-754(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "A novel glutathione transferase (13-13) isolated from the matrix of rat liver mitochondria having structural similarity to class theta enzymes."
      Harris M.J., Meyer D.J., Coles B., Ketterer B.
      Biochem. J. 278:137-141(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-34.
    3. "Parallel evolutionary pathways for glutathione transferases: structure and mechanism of the mitochondrial class kappa enzyme rGSTK1-1."
      Ladner J.E., Parsons J.F., Rife C.L., Gilliland G.L., Armstrong R.N.
      Biochemistry 43:352-361(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, SUBUNIT, MUTAGENESIS OF SER-16.

    Entry informationi

    Entry nameiGSTK1_RAT
    AccessioniPrimary (citable) accession number: P24473
    Secondary accession number(s): O09034
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 111 of the entry and version 3 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