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P30711 (GSTT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase theta-1

EC=2.5.1.18
Alternative name(s):
GST class-theta-1
Glutathione transferase T1-1
Gene names
Name:GSTT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length240 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10 Ref.12

Catalytic activity

RX + glutathione = HX + R-S-glutathione. Ref.10 Ref.12

Subunit structure

Homodimer. Ref.12

Subcellular location

Cytoplasm.

Tissue specificity

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. Ref.9

Polymorphism

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.

Sequence similarities

Belongs to the GST superfamily. Theta family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 240239Glutathione S-transferase theta-1
PRO_0000185938

Regions

Domain2 – 8281GST N-terminal
Domain88 – 220133GST C-terminal
Region53 – 542Glutathione binding
Region66 – 672Glutathione binding

Sites

Binding site401Glutathione

Natural variations

Natural variant211A → T.
Corresponds to variant rs2266635 [ dbSNP | Ensembl ].
VAR_014501
Natural variant1411D → N.
Corresponds to variant rs2266633 [ dbSNP | Ensembl ].
VAR_014502
Natural variant1691V → I. Ref.5
Corresponds to variant rs2266637 [ dbSNP | Ensembl ].
VAR_014503
Natural variant1731E → K.
Corresponds to variant rs2234953 [ dbSNP | Ensembl ].
VAR_014504

Experimental info

Mutagenesis1761H → Q: Increases activity towards alkylhalogenides, but not hydroperoxides. Ref.12
Mutagenesis2341W → R: Facilitates binding of substrates and increases catalytic activity. Ref.12
Sequence conflict43 – 442DA → SD AA sequence Ref.8
Sequence conflict451F → C in AAH07065. Ref.7
Sequence conflict1261E → G in CAA55935. Ref.1

Secondary structure

.......................................... 240
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P30711 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: BD19F2BFDEF9F619

FASTA24027,335
        10         20         30         40         50         60 
MGLELYLDLL SQPCRAVYIF AKKNDIPFEL RIVDLIKGQH LSDAFAQVNP LKKVPALKDG 

        70         80         90        100        110        120 
DFTLTESVAI LLYLTRKYKV PDYWYPQDLQ ARARVDEYLA WQHTTLRRSC LRALWHKVMF 

       130        140        150        160        170        180 
PVFLGEPVSP QTLAATLAEL DVTLQLLEDK FLQNKAFLTG PHISLADLVA ITELMHPVGA 

       190        200        210        220        230        240 
GCQVFEGRPK LATWRQRVEA AVGEDLFQEA HEVILKAKDF PPADPTIKQK LMPWVLAMIR 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS13822.1.
PIRS44358.
RefSeqNP_000844.2. NM_000853.2.
UniGeneHs.268573.
Hs.738514.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2C3NX-ray1.50A/B/C/D2-240[»]
2C3QX-ray1.85A/B/C/D2-240[»]
2C3TX-ray2.40A/B/C/D2-240[»]
ProteinModelPortalP30711.
SMRP30711. Positions 2-240.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109207. 1 interaction.
IntActP30711. 1 interaction.
STRING9606.ENSP00000248935.

Chemistry

ChEMBLCHEMBL2141.
DrugBankDB00143. Glutathione.

PTM databases

PhosphoSiteP30711.

Polymorphism databases

DMDM21264427.

Proteomic databases

MaxQBP30711.
PaxDbP30711.
PRIDEP30711.

Protocols and materials databases

DNASU2952.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000248935; ENSP00000248935; ENSG00000184674.
GeneID2952.
KEGGhsa:2952.
UCSCuc002zze.4. human.

Organism-specific databases

CTD2952.
GeneCardsGC22M024952.
H-InvDBHIX0019638.
HGNCHGNC:4641. GSTT1.
MIM600436. gene.
neXtProtNX_P30711.
PharmGKBPA183.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0625.
HOGENOMHOG000125747.
HOVERGENHBG051854.
InParanoidP30711.
KOK00799.
OMATVKQKLM.
PhylomeDBP30711.
TreeFamTF325759.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
SABIO-RKP30711.

Gene expression databases

ArrayExpressP30711.
BgeeP30711.
CleanExHS_GSTT1.
GenevestigatorP30711.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP30711.
GeneWikiGSTT1.
GenomeRNAi2952.
NextBio11698.
PROP30711.
SOURCESearch...

Entry information

Entry nameGSTT1_HUMAN
AccessionPrimary (citable) accession number: P30711
Secondary accession number(s): O00226 expand/collapse secondary AC list , Q5TZY2, Q969K8, Q96IY3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 157 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM