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P30711

- GSTT1_HUMAN

UniProt

P30711 - GSTT1_HUMAN

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Protein

Glutathione S-transferase theta-1

Gene
GSTT1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Acts on 1,2-epoxy-3-(4-nitrophenoxy)propane, phenethylisothiocyanate 4-nitrobenzyl chloride and 4-nitrophenethyl bromide. Displays glutathione peroxidase activity with cumene hydroperoxide.2 Publications

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.2 Publications

Sites

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

GO - Molecular functioni

  1. glutathione peroxidase activity Source: UniProtKB
  2. glutathione transferase activity Source: UniProtKB

GO - Biological processi

  1. glutathione derivative biosynthetic process Source: Reactome
  2. glutathione metabolic process Source: UniProtKB
  3. oxidation-reduction process Source: GOC
  4. response to drug Source: Ensembl
  5. response to organic cyclic compound Source: Ensembl
  6. small molecule metabolic process Source: Reactome
  7. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

ReactomeiREACT_6926. Glutathione conjugation.
SABIO-RKP30711.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase theta-1 (EC:2.5.1.18)
Alternative name(s):
GST class-theta-1
Glutathione transferase T1-1
Gene namesi
Name:GSTT1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:4641. GSTT1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi176 – 1761H → Q: Increases activity towards alkylhalogenides, but not hydroperoxides. 1 Publication
Mutagenesisi234 – 2341W → R: Facilitates binding of substrates and increases catalytic activity. 1 Publication

Organism-specific databases

PharmGKBiPA183.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 240239Glutathione S-transferase theta-1PRO_0000185938Add
BLAST

Proteomic databases

MaxQBiP30711.
PaxDbiP30711.
PRIDEiP30711.

PTM databases

PhosphoSiteiP30711.

Expressioni

Tissue specificityi

Found in erythrocyte. Expressed at low levels in liver. In lung, expressed at low levels in Clara cells and ciliated cells at the alveolar/bronchiolar junction. Absent from epithelial cells of larger bronchioles.1 Publication

Gene expression databases

ArrayExpressiP30711.
BgeeiP30711.
CleanExiHS_GSTT1.
GenevestigatoriP30711.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi109207. 1 interaction.
IntActiP30711. 1 interaction.
STRINGi9606.ENSP00000248935.

Structurei

Secondary structure

1
240
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75
Helixi12 – 2312
Beta strandi29 – 324
Helixi35 – 373
Helixi39 – 413
Helixi43 – 486
Beta strandi56 – 594
Beta strandi62 – 654
Helixi67 – 7711
Helixi82 – 843
Helixi89 – 10113
Helixi102 – 1043
Helixi106 – 11712
Helixi118 – 1236
Helixi130 – 15021
Turni151 – 1544
Beta strandi155 – 1628
Helixi165 – 17915
Helixi189 – 20214
Helixi204 – 2107
Helixi212 – 2154
Helixi216 – 2194
Helixi225 – 23915

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C3NX-ray1.50A/B/C/D2-240[»]
2C3QX-ray1.85A/B/C/D2-240[»]
2C3TX-ray2.40A/B/C/D2-240[»]
ProteinModelPortaliP30711.
SMRiP30711. Positions 2-240.

Miscellaneous databases

EvolutionaryTraceiP30711.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8281GST N-terminalAdd
BLAST
Domaini88 – 220133GST C-terminalAdd
BLAST

Region

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

Sequence similaritiesi

Belongs to the GST superfamily. Theta family.

Phylogenomic databases

eggNOGiCOG0625.
HOGENOMiHOG000125747.
HOVERGENiHBG051854.
InParanoidiP30711.
KOiK00799.
OMAiTVKQKLM.
PhylomeDBiP30711.
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.

P30711-1 [UniParc]FASTAAdd to Basket

« Hide

MGLELYLDLL SQPCRAVYIF AKKNDIPFEL RIVDLIKGQH LSDAFAQVNP    50
LKKVPALKDG DFTLTESVAI LLYLTRKYKV PDYWYPQDLQ ARARVDEYLA 100
WQHTTLRRSC LRALWHKVMF PVFLGEPVSP QTLAATLAEL DVTLQLLEDK 150
FLQNKAFLTG PHISLADLVA ITELMHPVGA GCQVFEGRPK LATWRQRVEA 200
AVGEDLFQEA HEVILKAKDF PPADPTIKQK LMPWVLAMIR 240
Length:240
Mass (Da):27,335
Last modified:January 23, 2007 - v4
Checksum:iBD19F2BFDEF9F619
GO

Polymorphismi

The GSTT1 gene is absent from 38% of the population. The presence or absence of the GSTT1 gene is coincident with the conjugator (GSST1+) and non-conjugator (GSTT1-) phenotypes respectively. The GSTT1+ phenotype can catalyze the glutathione conjugation of dichloromethane.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti21 – 211A → T.
Corresponds to variant rs2266635 [ dbSNP | Ensembl ].
VAR_014501
Natural varianti141 – 1411D → N.
Corresponds to variant rs2266633 [ dbSNP | Ensembl ].
VAR_014502
Natural varianti169 – 1691V → I.1 Publication
Corresponds to variant rs2266637 [ dbSNP | Ensembl ].
VAR_014503
Natural varianti173 – 1731E → K.
Corresponds to variant rs2234953 [ dbSNP | Ensembl ].
VAR_014504

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 442DA → SD AA sequence 1 Publication
Sequence conflicti45 – 451F → C in AAH07065. 1 Publication
Sequence conflicti126 – 1261E → G in CAA55935. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X79389 mRNA. Translation: CAA55935.1.
AF435971 mRNA. Translation: AAL31549.1.
AF240786 Genomic DNA. Translation: AAG02374.1.
AB057594 Genomic DNA. Translation: BAB39498.1.
BT019951 mRNA. Translation: AAV38754.1.
Z84718 Genomic DNA. No translation available.
BC007065 mRNA. Translation: AAH07065.1.
CCDSiCCDS13822.1.
PIRiS44358.
RefSeqiNP_000844.2. NM_000853.2.
UniGeneiHs.268573.
Hs.738514.

Genome annotation databases

EnsembliENST00000248935; ENSP00000248935; ENSG00000184674.
GeneIDi2952.
KEGGihsa:2952.
UCSCiuc002zze.4. human.

Polymorphism databases

DMDMi21264427.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SHMPD

The Singapore human mutation and polymorphism database

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X79389 mRNA. Translation: CAA55935.1 .
AF435971 mRNA. Translation: AAL31549.1 .
AF240786 Genomic DNA. Translation: AAG02374.1 .
AB057594 Genomic DNA. Translation: BAB39498.1 .
BT019951 mRNA. Translation: AAV38754.1 .
Z84718 Genomic DNA. No translation available.
BC007065 mRNA. Translation: AAH07065.1 .
CCDSi CCDS13822.1.
PIRi S44358.
RefSeqi NP_000844.2. NM_000853.2.
UniGenei Hs.268573.
Hs.738514.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2C3N X-ray 1.50 A/B/C/D 2-240 [» ]
2C3Q X-ray 1.85 A/B/C/D 2-240 [» ]
2C3T X-ray 2.40 A/B/C/D 2-240 [» ]
ProteinModelPortali P30711.
SMRi P30711. Positions 2-240.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109207. 1 interaction.
IntActi P30711. 1 interaction.
STRINGi 9606.ENSP00000248935.

Chemistry

ChEMBLi CHEMBL2141.
DrugBanki DB00143. Glutathione.

PTM databases

PhosphoSitei P30711.

Polymorphism databases

DMDMi 21264427.

Proteomic databases

MaxQBi P30711.
PaxDbi P30711.
PRIDEi P30711.

Protocols and materials databases

DNASUi 2952.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000248935 ; ENSP00000248935 ; ENSG00000184674 .
GeneIDi 2952.
KEGGi hsa:2952.
UCSCi uc002zze.4. human.

Organism-specific databases

CTDi 2952.
GeneCardsi GC22M024952.
H-InvDB HIX0019638.
HGNCi HGNC:4641. GSTT1.
MIMi 600436. gene.
neXtProti NX_P30711.
PharmGKBi PA183.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0625.
HOGENOMi HOG000125747.
HOVERGENi HBG051854.
InParanoidi P30711.
KOi K00799.
OMAi TVKQKLM.
PhylomeDBi P30711.
TreeFami TF325759.

Enzyme and pathway databases

Reactomei REACT_6926. Glutathione conjugation.
SABIO-RK P30711.

Miscellaneous databases

EvolutionaryTracei P30711.
GeneWikii GSTT1.
GenomeRNAii 2952.
NextBioi 11698.
PROi P30711.
SOURCEi Search...

Gene expression databases

ArrayExpressi P30711.
Bgeei P30711.
CleanExi HS_GSTT1.
Genevestigatori P30711.

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

« Hide 'large scale' publications
  1. "Human glutathione S-transferase theta (GSTT1): cDNA cloning and the characterization of a genetic polymorphism."
    Pemble S., Schroeder K.R., Spencer S.R., Meyer D.J., Hallier E., Bolt H.M., Ketterer B., Taylor J.B.
    Biochem. J. 300:271-276(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Kinetic characterization of recombinant human glutathione transferase T1-1, a polymorphic detoxication enzyme."
    Jemth P., Mannervik B.
    Arch. Biochem. Biophys. 348:247-254(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
  3. "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].
  4. "Complete genomic structure of human glutathione S-transferase TT1."
    Iida A., Kondo K., Kitamura Y., Mishima C., Osawa S., Kitamoto T., Harigae C., Nakamura Y.
    Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Thymus.
  5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-169.
  6. "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].
  7. "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: Urinary bladder.
  8. "Theta, a new class of glutathione transferases purified from rat and man."
    Meyer D.J., Coles B., Pemble S.E., Gilmore K.S., Fraser G.M., Ketterer B.
    Biochem. J. 274:409-414(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-47.
    Tissue: Liver.
  9. "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.
  10. "Residue 234 is a master switch of the alternative-substrate activity profile of human and rodent theta class glutathione transferase T1-1."
    Shokeer A., Mannervik B.
    Biochim. Biophys. Acta 1800:466-473(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Structural basis of the suppressed catalytic activity of wild-type human glutathione transferase T1-1 compared to its W234R mutant."
    Tars K., Larsson A.K., Shokeer A., Olin B., Mannervik B., Kleywegt G.J.
    J. Mol. Biol. 355:96-105(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF WILD-TYPE AND MUTANT ARG-234 IN COMPLEX WITH HEXYLGLUTATHIONE, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, MUTAGENESIS OF HIS-176 AND TRP-234.

Entry informationi

Entry nameiGSTT1_HUMAN
AccessioniPrimary (citable) accession number: P30711
Secondary accession number(s): O00226
, Q5TZY2, Q969K8, Q96IY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 158 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 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. 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

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