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P0CG29

- GST2_HUMAN

UniProt

P0CG29 - GST2_HUMAN

Protein

Glutathione S-transferase theta-2

Gene

GSTT2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 35 (01 Oct 2014)
      Sequence version 1 (13 Jul 2010)
      Previous versions | rss
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    Functioni

    Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Has a sulfatase activity.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei40 – 401GlutathioneBy similarity

    GO - Molecular functioni

    1. glutathione transferase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    ReactomeiREACT_6926. Glutathione conjugation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase theta-2 (EC:2.5.1.18)
    Alternative name(s):
    GST class-theta-2
    Gene namesi
    Name:GSTT2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:4642. GSTT2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 244243Glutathione S-transferase theta-2PRO_0000185939Add
    BLAST

    Proteomic databases

    MaxQBiP0CG29.
    PRIDEiP0CG29.

    Expressioni

    Tissue specificityi

    Expressed at low levels in liver. In lung, expressed at low levels in ciliated bronchiolar cells, alveolar macrophages and alveolar type II cells.1 Publication

    Gene expression databases

    BgeeiP0CG29.
    GenevestigatoriP30712.

    Organism-specific databases

    HPAiHPA000750.

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    Secondary structure

    1
    244
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 75
    Helixi12 – 2312
    Beta strandi28 – 325
    Turni35 – 384
    Helixi39 – 413
    Helixi43 – 464
    Beta strandi56 – 594
    Beta strandi62 – 654
    Helixi67 – 7711
    Helixi82 – 843
    Helixi89 – 10517
    Turni106 – 1116
    Helixi112 – 1176
    Helixi119 – 1224
    Helixi129 – 14820
    Turni149 – 1535
    Beta strandi154 – 1563
    Beta strandi159 – 1613
    Helixi164 – 17714
    Turni178 – 1803
    Turni183 – 1864
    Helixi188 – 20114
    Helixi203 – 21412
    Helixi216 – 2216
    Helixi230 – 24112

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4MPFX-ray2.10A/B1-244[»]
    ProteinModelPortaliP0CG29.
    SMRiP0CG29. Positions 1-244.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 8281GST N-terminalAdd
    BLAST
    Domaini88 – 224137GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni53 – 542Glutathione bindingBy similarity
    Regioni66 – 672Glutathione bindingBy similarity

    Sequence similaritiesi

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

    Phylogenomic databases

    HOGENOMiHOG000125747.
    OMAiGVPLWVQ.
    OrthoDBiEOG7V1FRJ.
    PhylomeDBiP0CG29.
    TreeFamiTF325759.

    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.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view]
    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.

    P0CG29-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGLELFLDLV SQPSRAVYIF AKKNGIPLEL RTVDLVKGQH KSKEFLQINS    50
    LGKLPTLKDG DFILTESSAI LIYLSCKYQT PDHWYPSDLQ ARARVHEYLG 100
    WHADCIRGTF GIPLWVQVLG PLIGVQVPKE KVERNRTAMD QALQWLEDKF 150
    LGDRPFLAGQ QVTLADLMAL EELMQPVALG YELFEGRPRL AAWRGRVEAF 200
    LGAELCQEAH SIILSILEQA AKKTLPTPSP EAYQAMLLRI ARIP 244
    Length:244
    Mass (Da):27,506
    Last modified:July 13, 2010 - v1
    Checksum:iDBA15D045262FFC3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21G → V AA sequence (PubMed:1417752)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF240786 Genomic DNA. Translation: AAG02373.1.
    AP000351 Genomic DNA. No translation available.
    PIRiA56847.
    UniGeneiHs.654462.

    Genome annotation databases

    EnsembliENST00000215780; ENSP00000215780; ENSG00000099984.

    Polymorphism databases

    DMDMi300680960.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF240786 Genomic DNA. Translation: AAG02373.1 .
    AP000351 Genomic DNA. No translation available.
    PIRi A56847.
    UniGenei Hs.654462.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4MPF X-ray 2.10 A/B 1-244 [» ]
    ProteinModelPortali P0CG29.
    SMRi P0CG29. Positions 1-244.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    ChEMBLi CHEMBL2142.
    DrugBanki DB00143. Glutathione.

    Polymorphism databases

    DMDMi 300680960.

    Proteomic databases

    MaxQBi P0CG29.
    PRIDEi P0CG29.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000215780 ; ENSP00000215780 ; ENSG00000099984 .

    Organism-specific databases

    GeneCardsi GC22P024322.
    HGNCi HGNC:4642. GSTT2.
    HPAi HPA000750.
    MIMi 600437. gene.
    neXtProti NX_P0CG29.
    GenAtlasi Search...

    Phylogenomic databases

    HOGENOMi HOG000125747.
    OMAi GVPLWVQ.
    OrthoDBi EOG7V1FRJ.
    PhylomeDBi P0CG29.
    TreeFami TF325759.

    Enzyme and pathway databases

    Reactomei REACT_6926. Glutathione conjugation.

    Miscellaneous databases

    NextBioi 11702.
    PROi P0CG29.
    SOURCEi Search...

    Gene expression databases

    Bgeei P0CG29.
    Genevestigatori P30712.

    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.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view ]
    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. "Characterization of the glutathione S-transferase GSTT1 deletion: discrimination of all genotypes by polymerase chain reaction indicates a trimodular genotype-phenotype correlation."
      Sprenger R., Schlagenhaufer R., Kerb R., Bruhn C., Brockmoeller J., Roots I., Brinkmann U.
      Pharmacogenetics 10:557-565(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Characterization of a human class-theta glutathione S-transferase with activity towards 1-menaphthyl sulphate."
      Hussey A.J., Hayes J.D.
      Biochem. J. 286:929-935(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-21.
      Tissue: Liver.
    4. "The distribution of theta-class glutathione S-transferases in the liver and lung of mouse, rat and human."
      Mainwaring G.W., Williams S.M., Foster J.R., Tugwood J., Green T.
      Biochem. J. 318:297-303(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
      Tissue: Liver and Lung.

    Entry informationi

    Entry nameiGST2_HUMAN
    AccessioniPrimary (citable) accession number: P0CG29
    Secondary accession number(s): O60665
    , P30712, Q6IPV7, Q9HD76
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 13, 2010
    Last sequence update: July 13, 2010
    Last modified: October 1, 2014
    This is version 35 of the entry and version 1 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 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3