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P08263

- GSTA1_HUMAN

UniProt

P08263 - GSTA1_HUMAN

Protein

Glutathione S-transferase A1

Gene

GSTA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 3 (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.1 Publication

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei9 – 91Glutathione2 Publications
    Binding sitei45 – 451Glutathione2 Publications

    GO - Molecular functioni

    1. glutathione transferase activity Source: UniProtKB

    GO - Biological processi

    1. epithelial cell differentiation Source: UniProt
    2. glutathione derivative biosynthetic process Source: Reactome
    3. glutathione metabolic process Source: UniProtKB
    4. metabolic process Source: UniProtKB
    5. small molecule metabolic process Source: Reactome
    6. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    BioCyciMetaCyc:G66-32542-MONOMER.
    ReactomeiREACT_6926. Glutathione conjugation.
    SABIO-RKP08263.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase A1 (EC:2.5.1.18)
    Alternative name(s):
    GST HA subunit 1
    GST class-alpha member 1
    GST-epsilon
    GSTA1-1
    GTH1
    Cleaved into the following chain:
    Gene namesi
    Name:GSTA1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:4626. GSTA1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi71 – 711I → A or V: No significant effect on enzyme activity. Reduces protein stability. 1 Publication
    Mutagenesisi216 – 2161A → H: Confers ability to hydrolyze S-glutathionyl benzoate to glutathione and benzoic acid. 1 Publication

    Organism-specific databases

    PharmGKBiPA29016.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 222222Glutathione S-transferase A1PRO_0000423203Add
    BLAST
    Initiator methioninei1 – 11Removed; alternate1 Publication
    Chaini2 – 222221Glutathione S-transferase A1, N-terminally processedPRO_0000185783Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP08263.
    PaxDbiP08263.
    PRIDEiP08263.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00657682.

    PTM databases

    PhosphoSiteiP08263.

    Expressioni

    Tissue specificityi

    Liver.

    Gene expression databases

    BgeeiP08263.
    CleanExiHS_GSTA1.
    GenevestigatoriP08263.

    Organism-specific databases

    HPAiHPA004342.
    HPA053817.

    Interactioni

    Subunit structurei

    Homodimer or heterodimer of GSTA1 and GSTA2.8 Publications

    Protein-protein interaction databases

    BioGridi109193. 8 interactions.
    IntActiP08263. 6 interactions.
    MINTiMINT-5000131.
    STRINGi9606.ENSP00000335620.

    Structurei

    Secondary structure

    1
    222
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 138
    Turni14 – 163
    Helixi17 – 2610
    Beta strandi31 – 355
    Helixi38 – 469
    Beta strandi57 – 604
    Beta strandi63 – 675
    Helixi68 – 7811
    Helixi86 – 10823
    Helixi109 – 1113
    Helixi114 – 13017
    Helixi132 – 14312
    Beta strandi146 – 1494
    Helixi155 – 17016
    Turni172 – 1776
    Helixi179 – 19012
    Helixi192 – 1987
    Helixi210 – 22011

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GSDX-ray2.50A/B/C/D2-222[»]
    1GSEX-ray2.00A/B2-222[»]
    1GSFX-ray2.70A/B/C/D2-222[»]
    1GUHX-ray2.60A/B/C/D2-222[»]
    1K3LX-ray1.50A/B2-222[»]
    1K3OX-ray1.80A/B2-222[»]
    1K3YX-ray1.30A/B2-222[»]
    1LBKX-ray1.86A/B208-213[»]
    1PKWX-ray2.00A/B1-222[»]
    1PKZX-ray2.10A/B1-222[»]
    1PL1X-ray1.75A/B1-222[»]
    1PL2X-ray1.80A/B1-222[»]
    1USBX-ray2.07A/B2-222[»]
    1XWGX-ray1.85A/B2-222[»]
    1YDKX-ray1.95A/B1-222[»]
    2R3XX-ray1.80A/B1-222[»]
    2R6KX-ray2.51A/B1-222[»]
    3I69X-ray2.38A/B/C/D/E/F/G/H1-222[»]
    3I6AX-ray1.98A/B/C/D/E/F/G/H1-222[»]
    3IK9X-ray2.20A/B/C/D/E/F/G/H1-222[»]
    3KTLX-ray1.75A/B2-222[»]
    3L0HX-ray2.13A/B1-222[»]
    3Q74X-ray1.79A/B2-222[»]
    3U6VX-ray2.20A/B1-222[»]
    3ZFBX-ray1.86A/B1-222[»]
    3ZFLX-ray1.88A/B1-222[»]
    4HJ2X-ray2.10A/B4-220[»]
    ProteinModelPortaliP08263.
    SMRiP08263. Positions 2-222.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08263.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 8381GST N-terminalAdd
    BLAST
    Domaini85 – 207123GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni54 – 552Glutathione binding
    Regioni67 – 682Glutathione binding

    Domaini

    The C-terminal domain may form a component of the hydrophobic substrate-binding site, but in contrast appears not to be directly involved in GSH binding and is not absolutely essential for catalytic activity.

    Sequence similaritiesi

    Belongs to the GST superfamily. Alpha family.Curated
    Contains 1 GST C-terminal domain.Curated
    Contains 1 GST N-terminal domain.Curated

    Phylogenomic databases

    eggNOGiNOG266414.
    HOGENOMiHOG000115734.
    HOVERGENiHBG053749.
    InParanoidiP08263.
    KOiK00799.
    OMAiDTNILAN.
    OrthoDBiEOG79CZ0K.
    PhylomeDBiP08263.
    TreeFamiTF105321.

    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.
    IPR003080. GST_alpha.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view]
    PRINTSiPR01266. GSTRNSFRASEA.
    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.

    P08263-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEKPKLHYF NARGRMESTR WLLAAAGVEF EEKFIKSAED LDKLRNDGYL    50
    MFQQVPMVEI DGMKLVQTRA ILNYIASKYN LYGKDIKERA LIDMYIEGIA 100
    DLGEMILLLP VCPPEEKDAK LALIKEKIKN RYFPAFEKVL KSHGQDYLVG 150
    NKLSRADIHL VELLYYVEEL DSSLISSFPL LKALKTRISN LPTVKKFLQP 200
    GSPRKPPMDE KSLEEARKIF RF 222
    Length:222
    Mass (Da):25,631
    Last modified:January 23, 2007 - v3
    Checksum:iC8B6786DCD761350
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti18 – 181S → C in AAA36174. (PubMed:3678589)Curated
    Sequence conflicti51 – 511M → T in AAT06769. 1 PublicationCurated
    Sequence conflicti56 – 583PMV → AML in AAA36174. (PubMed:3678589)Curated
    Sequence conflicti212 – 2121S → L AA sequence (PubMed:2604726)Curated
    Sequence conflicti216 – 2161A → S AA sequence (PubMed:8431482)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti19 – 191T → I.
    Corresponds to variant rs1051578 [ dbSNP | Ensembl ].
    VAR_033978
    Natural varianti113 – 1131P → Q.
    Corresponds to variant rs1051745 [ dbSNP | Ensembl ].
    VAR_049482
    Natural varianti117 – 1171K → Q.
    Corresponds to variant rs1051757 [ dbSNP | Ensembl ].
    VAR_049483

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15872 mRNA. Translation: AAA70226.1.
    M21758 mRNA. Translation: AAA52615.1.
    M25627 mRNA. Translation: AAA36174.1.
    M14777 mRNA. Translation: AAA52618.1.
    S76235
    , S76221, S76223, S76225, S76228, S76232 Genomic DNA. Translation: AAB20973.1.
    S49975 mRNA. Translation: AAB24012.1.
    AY532928 mRNA. Translation: AAT06769.1.
    CR407656 mRNA. Translation: CAG28584.1.
    AL590363 Genomic DNA. Translation: CAI13812.1.
    CH471081 Genomic DNA. Translation: EAX04385.1.
    BC053578 mRNA. Translation: AAH53578.1.
    BC110891 mRNA. Translation: AAI10892.1.
    CCDSiCCDS4945.1.
    PIRiA25909. A56666.
    S29657.
    RefSeqiNP_665683.1. NM_145740.3.
    UniGeneiHs.446309.

    Genome annotation databases

    EnsembliENST00000334575; ENSP00000335620; ENSG00000243955.
    GeneIDi2938.
    KEGGihsa:2938.
    UCSCiuc003paz.3. human.

    Polymorphism databases

    DMDMi121730.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15872 mRNA. Translation: AAA70226.1 .
    M21758 mRNA. Translation: AAA52615.1 .
    M25627 mRNA. Translation: AAA36174.1 .
    M14777 mRNA. Translation: AAA52618.1 .
    S76235
    , S76221 , S76223 , S76225 , S76228 , S76232 Genomic DNA. Translation: AAB20973.1 .
    S49975 mRNA. Translation: AAB24012.1 .
    AY532928 mRNA. Translation: AAT06769.1 .
    CR407656 mRNA. Translation: CAG28584.1 .
    AL590363 Genomic DNA. Translation: CAI13812.1 .
    CH471081 Genomic DNA. Translation: EAX04385.1 .
    BC053578 mRNA. Translation: AAH53578.1 .
    BC110891 mRNA. Translation: AAI10892.1 .
    CCDSi CCDS4945.1.
    PIRi A25909. A56666.
    S29657.
    RefSeqi NP_665683.1. NM_145740.3.
    UniGenei Hs.446309.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GSD X-ray 2.50 A/B/C/D 2-222 [» ]
    1GSE X-ray 2.00 A/B 2-222 [» ]
    1GSF X-ray 2.70 A/B/C/D 2-222 [» ]
    1GUH X-ray 2.60 A/B/C/D 2-222 [» ]
    1K3L X-ray 1.50 A/B 2-222 [» ]
    1K3O X-ray 1.80 A/B 2-222 [» ]
    1K3Y X-ray 1.30 A/B 2-222 [» ]
    1LBK X-ray 1.86 A/B 208-213 [» ]
    1PKW X-ray 2.00 A/B 1-222 [» ]
    1PKZ X-ray 2.10 A/B 1-222 [» ]
    1PL1 X-ray 1.75 A/B 1-222 [» ]
    1PL2 X-ray 1.80 A/B 1-222 [» ]
    1USB X-ray 2.07 A/B 2-222 [» ]
    1XWG X-ray 1.85 A/B 2-222 [» ]
    1YDK X-ray 1.95 A/B 1-222 [» ]
    2R3X X-ray 1.80 A/B 1-222 [» ]
    2R6K X-ray 2.51 A/B 1-222 [» ]
    3I69 X-ray 2.38 A/B/C/D/E/F/G/H 1-222 [» ]
    3I6A X-ray 1.98 A/B/C/D/E/F/G/H 1-222 [» ]
    3IK9 X-ray 2.20 A/B/C/D/E/F/G/H 1-222 [» ]
    3KTL X-ray 1.75 A/B 2-222 [» ]
    3L0H X-ray 2.13 A/B 1-222 [» ]
    3Q74 X-ray 1.79 A/B 2-222 [» ]
    3U6V X-ray 2.20 A/B 1-222 [» ]
    3ZFB X-ray 1.86 A/B 1-222 [» ]
    3ZFL X-ray 1.88 A/B 1-222 [» ]
    4HJ2 X-ray 2.10 A/B 4-220 [» ]
    ProteinModelPortali P08263.
    SMRi P08263. Positions 2-222.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109193. 8 interactions.
    IntActi P08263. 6 interactions.
    MINTi MINT-5000131.
    STRINGi 9606.ENSP00000335620.

    Chemistry

    BindingDBi P08263.
    ChEMBLi CHEMBL3409.
    DrugBanki DB00276. Amsacrine.
    DB01008. Busulfan.
    DB00143. Glutathione.

    PTM databases

    PhosphoSitei P08263.

    Polymorphism databases

    DMDMi 121730.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00657682.

    Proteomic databases

    MaxQBi P08263.
    PaxDbi P08263.
    PRIDEi P08263.

    Protocols and materials databases

    DNASUi 2938.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000334575 ; ENSP00000335620 ; ENSG00000243955 .
    GeneIDi 2938.
    KEGGi hsa:2938.
    UCSCi uc003paz.3. human.

    Organism-specific databases

    CTDi 2938.
    GeneCardsi GC06M052656.
    HGNCi HGNC:4626. GSTA1.
    HPAi HPA004342.
    HPA053817.
    MIMi 138359. gene.
    neXtProti NX_P08263.
    PharmGKBi PA29016.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG266414.
    HOGENOMi HOG000115734.
    HOVERGENi HBG053749.
    InParanoidi P08263.
    KOi K00799.
    OMAi DTNILAN.
    OrthoDBi EOG79CZ0K.
    PhylomeDBi P08263.
    TreeFami TF105321.

    Enzyme and pathway databases

    BioCyci MetaCyc:G66-32542-MONOMER.
    Reactomei REACT_6926. Glutathione conjugation.
    SABIO-RK P08263.

    Miscellaneous databases

    EvolutionaryTracei P08263.
    GeneWikii Glutathione_S-transferase_A1.
    GenomeRNAii 2938.
    NextBioi 11643.
    PROi P08263.
    SOURCEi Search...

    Gene expression databases

    Bgeei P08263.
    CleanExi HS_GSTA1.
    Genevestigatori P08263.

    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.
    IPR003080. GST_alpha.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view ]
    PRINTSi PR01266. GSTRNSFRASEA.
    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. "Human liver glutathione S-transferases: complete primary sequence of an Ha subunit cDNA."
      Tu C.-P.D., Qian B.
      Biochem. Biophys. Res. Commun. 141:229-237(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The basic glutathione S-transferases from human livers are products of separate genes."
      Rhoads D.M., Zarlengo R.P., Tu C.-P.D.
      Biochem. Biophys. Res. Commun. 145:474-481(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Nucleotide sequence of the human liver glutathione S-transferase subunit 1 cDNA."
      Tu C.-P.D., Qian B.
      Biochem. Soc. Trans. 15:734-736(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    4. "Isolation of a cDNA clone and localization of human glutathione S-transferase 2 genes to chromosome band 6p12."
      Board P.G., Webb G.C.
      Proc. Natl. Acad. Sci. U.S.A. 84:2377-2381(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "Isolation and characterization of a human glutathione S-transferase Ha1 subunit gene."
      Rozen F., Nguyen T., Pickett C.B.
      Arch. Biochem. Biophys. 292:589-593(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "Heterologous expression of recombinant human glutathione transferase A1-1 from a hepatoma cell line."
      Stenberg G., Bjornestedt R., Mannervik B.
      Protein Expr. Purif. 3:80-84(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    7. Chen P., Zhang C., Xie D., Wu Y., Han L., Chen L.
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    8. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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].
      Tissue: Brain.
    11. "Human glutathione S-transferases. The Ha multigene family encodes products of different but overlapping substrate specificities."
      Chow N.W., Whang-Peng J., Kao-Shan C.S., Tam M.F., Lai H.-C.J., Tu C.-P.D.
      J. Biol. Chem. 263:12797-12800(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 1-9.
    12. "Characterization of two novel subunits of the alpha-class glutathione S-transferases of human liver."
      Ahmad H., Singhal S.S., Saxena M., Awasthi Y.C.
      Biochim. Biophys. Acta 1161:333-336(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-170; 188-195 AND 209-222.
    13. "Evidence that glutathione S-transferases B1B1 and B2B2 are the products of separate genes and that their expression in human liver is subject to inter-individual variation. Molecular relationships between the B1 and B2 subunits and other alpha class glutathione S-transferases."
      Hayes J.D., Kerr L.A., Cronshaw A.D.
      Biochem. J. 264:437-445(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 16-36; 63-155 AND 208-212.
    14. "The contribution of the C-terminal sequence to the catalytic activity of GST2, a human alpha-class glutathione transferase."
      Board P.G., Mannervik B.
      Biochem. J. 275:171-174(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 200-222.
    15. "Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes."
      Sinning I., Kleywegt G.J., Cowan S.W., Reinemer P., Dirr H.W., Huber R., Gilliland G.L., Armstrong R.N., Ji X., Board P.G., Olin B., Mannervik B., Jones T.A.
      J. Mol. Biol. 232:192-212(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH S-BENZYL-GLUTATHIONE, SUBUNIT.
    16. "Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complexes with ethacrynic acid and its glutathione conjugate."
      Cameron A.D., Sinning I., L'Hermite G., Olin B., Board P.G., Mannervik B., Jones T.A.
      Structure 3:717-727(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEXES WITH ETHACRYNIC ACID AND GLUTATHIONE, SUBUNIT.
    17. "1.3-A resolution structure of human glutathione S-transferase with S-hexyl glutathione bound reveals possible extended ligandin binding site."
      Le Trong I., Stenkamp R.E., Ibarra C., Atkins W.M., Adman E.T.
      Proteins 48:618-627(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEXES WITH S-HEXYL GLUTATHIONE, SUBUNIT.
    18. "Incorporation of a single His residue by rational design enables thiol-ester hydrolysis by human glutathione transferase A1-1."
      Hederos S., Broo K.S., Jakobsson E., Kleywegt G.J., Mannervik B., Baltzer L.
      Proc. Natl. Acad. Sci. U.S.A. 101:13163-13167(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) IN COMPLEX WITH S-BENZYLGLUTATHIONE, MUTAGENESIS OF ALA-216.
    19. "Tertiary interactions stabilise the C-terminal region of human glutathione transferase A1-1: a crystallographic and calorimetric study."
      Kuhnert D.C., Sayed Y., Mosebi S., Sayed M., Sewell T., Dirr H.W.
      J. Mol. Biol. 349:825-838(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF MUTANT ALA-219 IN COMPLEX WITH S-HEXYLGLUTATHIONE.
    20. "New crystal structures of human glutathione transferase A1-1 shed light on glutathione binding and the conformation of the C-terminal helix."
      Grahn E., Novotny M., Jakobsson E., Gustafsson A., Grehn L., Olin B., Madsen D., Wahlberg M., Mannervik B., Kleywegt G.J.
      Acta Crystallogr. D 62:197-207(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, SUBUNIT.
    21. "Structural analysis of a glutathione transferase A1-1 mutant tailored for high catalytic efficiency with toxic alkenals."
      Balogh L.M., Le Trong I., Kripps K.A., Tars K., Stenkamp R.E., Mannervik B., Atkins W.M.
      Biochemistry 48:7698-7704(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 1-210 IN COMPLEX WITH GLUTATHIONE.
    22. "The role of a topologically conserved isoleucine in glutathione transferase structure, stability and function."
      Achilonu I., Gildenhuys S., Fisher L., Burke J., Fanucchi S., Sewell B.T., Fernandes M., Dirr H.W.
      Acta Crystallogr. F 66:776-780(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF MUTANTS ALA-71 AND VAL-71 IN COMPLEX WITH S-HEXYLGLUTATHIONE, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ILE-71.

    Entry informationi

    Entry nameiGSTA1_HUMAN
    AccessioniPrimary (citable) accession number: P08263
    Secondary accession number(s): Q14750, Q5GHF8, Q5SZC1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 167 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 6
      Human chromosome 6: 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