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P0CG30

- GSTT2_HUMAN

UniProt

P0CG30 - GSTT2_HUMAN

Protein

Glutathione S-transferase theta-2B

Gene

GSTT2B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 37 (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.

    GO - Molecular functioni

    1. glutathione transferase activity Source: UniProtKB

    GO - Biological processi

    1. glutathione derivative biosynthetic process Source: Reactome
    2. small molecule metabolic process Source: Reactome
    3. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    ReactomeiREACT_6926. Glutathione conjugation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase theta-2B (EC:2.5.1.18)
    Alternative name(s):
    GST class-theta-2
    Glutathione S-transferase theta-2
    Gene namesi
    Name:GSTT2B
    Synonyms:GSTT2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:33437. GSTT2B.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162390358.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 244243Glutathione S-transferase theta-2BPRO_0000395344Add
    BLAST

    Proteomic databases

    MaxQBiP0CG30.
    PRIDEiP0CG30.

    PTM databases

    PhosphoSiteiP0CG30.

    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

    BgeeiP0CG30.

    Organism-specific databases

    HPAiHPA000750.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    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 – 17815
    Turni183 – 1864
    Helixi188 – 20114
    Helixi203 – 22220
    Helixi230 – 24112

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1LJRX-ray3.20A/B1-244[»]
    2LJRX-ray3.20A/B1-244[»]
    3LJRX-ray3.30A/B1-244[»]
    4MPGX-ray1.95A/B1-244[»]
    ProteinModelPortaliP0CG30.
    SMRiP0CG30. Positions 1-244.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0CG30.

    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
    Regioni40 – 412Glutathione binding
    Regioni53 – 542Glutathione binding
    Regioni66 – 672Glutathione binding

    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

    KOiK00799.
    OMAiEDIWLNG.
    OrthoDBiEOG7V1FRJ.
    PhylomeDBiP0CG30.
    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.

    P0CG30-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGLELFLDLV SQPSRAVYIF AKKNGIPLEL RTVDLVKGQH KSKEFLQINS    50
    LGKLPTLKDG DFILTESSAI LIYLSCKYQT PDHWYPSDLQ ARARVHEYLG 100
    WHADCIRGTF GIPLWVQVLG PLIGVQVPEE KVERNRTAMD QALQWLEDKF 150
    LGDRPFLAGQ QVTLADLMAL EELMQPVALG YELFEGRPRL AAWRGRVEAF 200
    LGAELCQEAH SIILSILEQA AKKTLPTPSP EAYQAMLLRI ARIP 244
    Length:244
    Mass (Da):27,507
    Last modified:July 13, 2010 - v1
    Checksum:iDBAF5D00F8C2FFC3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21G → V AA sequence (PubMed:1417752)Curated
    Sequence conflicti156 – 1583FLA → P in AAC13317. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti139 – 1391M → I.1 Publication
    Corresponds to variant rs1622002 [ dbSNP | Ensembl ].
    VAR_033982

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L38503 mRNA. Translation: AAB63956.1.
    AF057176
    , AF057173, AF057174, AF057175 Genomic DNA. Translation: AAC13317.1.
    CR456500 mRNA. Translation: CAG30386.1.
    AP000350 Genomic DNA. No translation available.
    BC002415 mRNA. Translation: AAH02415.1.
    CCDSiCCDS33617.1.
    PIRiA56847.
    RefSeqiNP_000845.1. NM_000854.3.
    NP_001074312.1. NM_001080843.3.
    UniGeneiHs.654462.
    Hs.656498.

    Genome annotation databases

    EnsembliENST00000290765; ENSP00000290765; ENSG00000133433.
    GeneIDi2953.
    653689.
    KEGGihsa:2953.
    hsa:653689.
    UCSCiuc002zyw.4. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L38503 mRNA. Translation: AAB63956.1 .
    AF057176
    , AF057173 , AF057174 , AF057175 Genomic DNA. Translation: AAC13317.1 .
    CR456500 mRNA. Translation: CAG30386.1 .
    AP000350 Genomic DNA. No translation available.
    BC002415 mRNA. Translation: AAH02415.1 .
    CCDSi CCDS33617.1.
    PIRi A56847.
    RefSeqi NP_000845.1. NM_000854.3.
    NP_001074312.1. NM_001080843.3.
    UniGenei Hs.654462.
    Hs.656498.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1LJR X-ray 3.20 A/B 1-244 [» ]
    2LJR X-ray 3.20 A/B 1-244 [» ]
    3LJR X-ray 3.30 A/B 1-244 [» ]
    4MPG X-ray 1.95 A/B 1-244 [» ]
    ProteinModelPortali P0CG30.
    SMRi P0CG30. Positions 1-244.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei P0CG30.

    Proteomic databases

    MaxQBi P0CG30.
    PRIDEi P0CG30.

    Protocols and materials databases

    DNASUi 2953.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000290765 ; ENSP00000290765 ; ENSG00000133433 .
    GeneIDi 2953.
    653689.
    KEGGi hsa:2953.
    hsa:653689.
    UCSCi uc002zyw.4. human.

    Organism-specific databases

    CTDi 2953.
    653689.
    GeneCardsi GC22M024299.
    HGNCi HGNC:33437. GSTT2B.
    HPAi HPA000750.
    neXtProti NX_P0CG30.
    PharmGKBi PA162390358.
    GenAtlasi Search...

    Phylogenomic databases

    KOi K00799.
    OMAi EDIWLNG.
    OrthoDBi EOG7V1FRJ.
    PhylomeDBi P0CG30.
    TreeFami TF325759.

    Enzyme and pathway databases

    Reactomei REACT_6926. Glutathione conjugation.

    Miscellaneous databases

    EvolutionaryTracei P0CG30.
    GeneWikii GSTT2.
    NextBioi 11702.
    PROi P0CG30.

    Gene expression databases

    Bgeei P0CG30.

    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. "Molecular cloning of a cDNA and chromosomal localization of a human theta-class glutathione S-transferase gene (GSTT2) to chromosome 22."
      Tan K.L., Webb G.C., Baker R.T., Board P.G.
      Genomics 25:381-387(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. Coggan M.A., Board P.G.
      Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-139.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "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].
    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].
      Tissue: Brain.
    6. "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.
    7. "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.
    8. "Human theta class glutathione transferase: the crystal structure reveals a sulfate-binding pocket within a buried active site."
      Rossjohn J., McKinstry W.J., Oakley A.J., Verger D., Flanagan J., Chelvanayagam G., Tan K.-L., Board P.G., Parker M.W.
      Structure 6:309-322(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, SUBUNIT.

    Entry informationi

    Entry nameiGSTT2_HUMAN
    AccessioniPrimary (citable) accession number: P0CG30
    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 37 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. 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3