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P09210

- GSTA2_HUMAN

UniProt

P09210 - GSTA2_HUMAN

Protein

Glutathione S-transferase A2

Gene

GSTA2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 163 (01 Oct 2014)
      Sequence version 4 (20 Feb 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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei9 – 91Glutathione1 Publication
    Binding sitei45 – 451Glutathione1 Publication

    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. small molecule metabolic process Source: Reactome
    5. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01846-MONOMER.
    ReactomeiREACT_6926. Glutathione conjugation.
    SABIO-RKP09210.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase A2 (EC:2.5.1.18)
    Alternative name(s):
    GST HA subunit 2
    GST class-alpha member 2
    GST-gamma
    GSTA2-2
    GTH2
    Gene namesi
    Name:GSTA2
    Synonyms:GST2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:4627. GSTA2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29017.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 222221Glutathione S-transferase A2PRO_0000185784Add
    BLAST

    Proteomic databases

    MaxQBiP09210.
    PaxDbiP09210.
    PRIDEiP09210.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00745233.

    PTM databases

    PhosphoSiteiP09210.

    Expressioni

    Tissue specificityi

    Liver.

    Gene expression databases

    BgeeiP09210.
    CleanExiHS_GSTA2.
    GenevestigatoriP09210.

    Organism-specific databases

    HPAiHPA004342.

    Interactioni

    Subunit structurei

    Homodimer or heterodimer of GSTA1 and GSTA2.2 Publications

    Protein-protein interaction databases

    STRINGi9606.ENSP00000420168.

    Structurei

    Secondary structure

    1
    222
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 94
    Beta strandi11 – 133
    Turni14 – 163
    Helixi17 – 259
    Beta strandi31 – 344
    Helixi38 – 469
    Beta strandi57 – 604
    Beta strandi63 – 675
    Helixi68 – 7811
    Helixi86 – 10823
    Helixi109 – 1113
    Turni114 – 1163
    Helixi117 – 13014
    Helixi132 – 14312
    Beta strandi146 – 1494
    Helixi155 – 17016
    Turni172 – 1776
    Helixi179 – 19012
    Helixi192 – 1976
    Helixi210 – 22011

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AGSX-ray2.50A/B2-222[»]
    2VCTX-ray2.10A/B/C/D/E/F/G/H1-222[»]
    2WJUX-ray2.30A/B/C/D/E/F/G/H1-222[»]
    4ACSX-ray2.10A/B/C/D1-221[»]
    ProteinModelPortaliP09210.
    SMRiP09210. Positions 2-222.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09210.

    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

    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.
    InParanoidiP09210.
    KOiK00799.
    OMAiNIRGRME.
    OrthoDBiEOG79CZ0K.
    PhylomeDBiP09210.
    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.

    P09210-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEKPKLHYS NIRGRMESIR WLLAAAGVEF EEKFIKSAED LDKLRNDGYL    50
    MFQQVPMVEI DGMKLVQTRA ILNYIASKYN LYGKDIKEKA LIDMYIEGIA 100
    DLGEMILLLP FSQPEEQDAK LALIQEKTKN RYFPAFEKVL KSHGQDYLVG 150
    NKLSRADIHL VELLYYVEEL DSSLISSFPL LKALKTRISN LPTVKKFLQP 200
    GSPRKPPMDE KSLEESRKIF RF 222
    Length:222
    Mass (Da):25,664
    Last modified:February 20, 2007 - v4
    Checksum:i2823565A693A30AC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti10 – 123SNI → FNA AA sequence (PubMed:8431482)Curated
    Sequence conflicti12 – 121I → T in CAA46642. (PubMed:1497629)Curated
    Sequence conflicti19 – 191I → T AA sequence (PubMed:8431482)Curated
    Sequence conflicti89 – 891K → R AA sequence (PubMed:8431482)Curated
    Sequence conflicti128 – 1281T → I AA sequence (PubMed:8431482)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti110 – 1101P → S.
    Corresponds to variant rs2234951 [ dbSNP | Ensembl ].
    VAR_014495
    Natural varianti112 – 1121S → T.3 Publications
    Corresponds to variant rs2180314 [ dbSNP | Ensembl ].
    VAR_012205
    Natural varianti149 – 1491V → A.
    Corresponds to variant rs2266631 [ dbSNP | Ensembl ].
    VAR_014496
    Natural varianti210 – 2101E → A.3 Publications
    Corresponds to variant rs6577 [ dbSNP | Ensembl ].
    VAR_012206

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16594 mRNA. Translation: AAA52616.1.
    S45640
    , S45627, S45629, S45636, S45637, S45639 Genomic DNA. Translation: AAB23672.1.
    X65727
    , X65728, X65729, X65730, X65731, X65732 Genomic DNA. Translation: CAA46642.1.
    AL109918 Genomic DNA. Translation: CAB92770.1.
    BC002895 mRNA. Translation: AAH02895.1.
    CCDSiCCDS4944.1.
    PIRiS24330.
    S29658.
    RefSeqiNP_000837.3. NM_000846.4.
    UniGeneiHs.94107.

    Genome annotation databases

    EnsembliENST00000493422; ENSP00000420168; ENSG00000244067.
    GeneIDi2939.
    KEGGihsa:2939.
    UCSCiuc003pay.3. human.

    Polymorphism databases

    DMDMi126302551.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16594 mRNA. Translation: AAA52616.1 .
    S45640
    , S45627 , S45629 , S45636 , S45637 , S45639 Genomic DNA. Translation: AAB23672.1 .
    X65727
    , X65728 , X65729 , X65730 , X65731 , X65732 Genomic DNA. Translation: CAA46642.1 .
    AL109918 Genomic DNA. Translation: CAB92770.1 .
    BC002895 mRNA. Translation: AAH02895.1 .
    CCDSi CCDS4944.1.
    PIRi S24330.
    S29658.
    RefSeqi NP_000837.3. NM_000846.4.
    UniGenei Hs.94107.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AGS X-ray 2.50 A/B 2-222 [» ]
    2VCT X-ray 2.10 A/B/C/D/E/F/G/H 1-222 [» ]
    2WJU X-ray 2.30 A/B/C/D/E/F/G/H 1-222 [» ]
    4ACS X-ray 2.10 A/B/C/D 1-221 [» ]
    ProteinModelPortali P09210.
    SMRi P09210. Positions 2-222.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000420168.

    Chemistry

    BindingDBi P09210.
    ChEMBLi CHEMBL2241.
    DrugBanki DB01424. Aminophenazone.
    DB00276. Amsacrine.
    DB01008. Busulfan.
    DB00291. Chlorambucil.
    DB00608. Chloroquine.
    DB00568. Cinnarizine.
    DB00636. Clofibrate.
    DB00903. Ethacrynic acid.
    DB00143. Glutathione.
    DB00888. Mechlorethamine.
    DB01058. Praziquantel.
    DB00163. Vitamin E.

    PTM databases

    PhosphoSitei P09210.

    Polymorphism databases

    DMDMi 126302551.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00745233.

    Proteomic databases

    MaxQBi P09210.
    PaxDbi P09210.
    PRIDEi P09210.

    Protocols and materials databases

    DNASUi 2939.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000493422 ; ENSP00000420168 ; ENSG00000244067 .
    GeneIDi 2939.
    KEGGi hsa:2939.
    UCSCi uc003pay.3. human.

    Organism-specific databases

    CTDi 2939.
    GeneCardsi GC06M052614.
    H-InvDB HIX0200871.
    HGNCi HGNC:4627. GSTA2.
    HPAi HPA004342.
    MIMi 138360. gene.
    neXtProti NX_P09210.
    PharmGKBi PA29017.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG266414.
    HOGENOMi HOG000115734.
    HOVERGENi HBG053749.
    InParanoidi P09210.
    KOi K00799.
    OMAi NIRGRME.
    OrthoDBi EOG79CZ0K.
    PhylomeDBi P09210.
    TreeFami TF105321.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS01846-MONOMER.
    Reactomei REACT_6926. Glutathione conjugation.
    SABIO-RK P09210.

    Miscellaneous databases

    EvolutionaryTracei P09210.
    GeneWikii GSTA2.
    GenomeRNAii 2939.
    NextBioi 11647.
    PROi P09210.
    SOURCEi Search...

    Gene expression databases

    Bgeei P09210.
    CleanExi HS_GSTA2.
    Genevestigatori P09210.

    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. "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], VARIANT THR-112.
    2. "Isolation and characterization of the human glutathione S-transferase A2 subunit gene."
      Rohrdanz E., Nguyen T., Pickett C.B.
      Arch. Biochem. Biophys. 298:747-752(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-210.
      Tissue: Liver.
    3. "Cloning, sequencing and characterization of the human alpha glutathione S-transferase gene corresponding to the cDNA clone pGTH2."
      Klone A., Hussnatter R., Sies H.
      Biochem. J. 285:925-928(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-210.
      Tissue: Blood.
    4. "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].
    5. "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 THR-112.
      Tissue: Lung.
    6. "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.
    7. "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 63-155 AND 208-222.
    8. "A surface mutant (G82R) of a human alpha-glutathione S-transferase shows decreased thermal stability and a new mode of molecular association in the crystal."
      Zeng K., Rose J.P., Chen H.C., Strickland C.L., Tu C.P., Wang B.C.
      Proteins 20:259-263(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SUBUNIT.
    9. "Structural basis for featuring of steroid isomerase activity in alpha class glutathione transferases."
      Tars K., Olin B., Mannervik B.
      J. Mol. Biol. 397:332-340(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE AND DELTA5-ANDROSTENE-3-17-DIONE, SUBUNIT.
    10. "Polymorphism of human alpha class glutathione transferases."
      Tetlow N., Liu D., Board P.
      Pharmacogenetics 11:609-617(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS THR-112 AND ALA-210.

    Entry informationi

    Entry nameiGSTA2_HUMAN
    AccessioniPrimary (citable) accession number: P09210
    Secondary accession number(s): Q12759, Q16491, Q9NTY6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: February 20, 2007
    Last modified: October 1, 2014
    This is version 163 of the entry and version 4 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