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Protein

Glutathione S-transferase theta-2

Gene

GSTT2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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
Complete GO annotation...

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 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:4642. GSTT2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

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 – 75Combined sources
Helixi12 – 2312Combined sources
Beta strandi28 – 325Combined sources
Turni35 – 384Combined sources
Helixi39 – 413Combined sources
Helixi43 – 464Combined sources
Beta strandi56 – 594Combined sources
Beta strandi62 – 654Combined sources
Helixi67 – 7711Combined sources
Helixi82 – 843Combined sources
Helixi89 – 10517Combined sources
Turni106 – 1116Combined sources
Helixi112 – 1176Combined sources
Helixi119 – 1224Combined sources
Helixi129 – 14820Combined sources
Turni149 – 1535Combined sources
Beta strandi154 – 1563Combined sources
Beta strandi159 – 1613Combined sources
Helixi164 – 17714Combined sources
Turni178 – 1803Combined sources
Turni183 – 1864Combined sources
Helixi188 – 20114Combined sources
Helixi203 – 21412Combined sources
Helixi216 – 2216Combined sources
Helixi230 – 24112Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP0CG29.
KOiK00799.
OMAiIAYGPCA.
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

        10         20         30         40         50
MGLELFLDLV SQPSRAVYIF AKKNGIPLEL RTVDLVKGQH KSKEFLQINS
60 70 80 90 100
LGKLPTLKDG DFILTESSAI LIYLSCKYQT PDHWYPSDLQ ARARVHEYLG
110 120 130 140 150
WHADCIRGTF GIPLWVQVLG PLIGVQVPKE KVERNRTAMD QALQWLEDKF
160 170 180 190 200
LGDRPFLAGQ QVTLADLMAL EELMQPVALG YELFEGRPRL AAWRGRVEAF
210 220 230 240
LGAELCQEAH SIILSILEQA AKKTLPTPSP EAYQAMLLRI ARIP
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:
EMBLi
GenBanki
DDBJi
Links Updated
AF240786 Genomic DNA. Translation: AAG02373.1.
AP000351 Genomic DNA. No translation available.
PIRiA56847.
RefSeqiNP_000845.2. NM_000854.4.
UniGeneiHs.654462.
Hs.656498.

Genome annotation databases

EnsembliENST00000215780; ENSP00000215780; ENSG00000099984.
ENST00000618279; ENSP00000477540; ENSG00000277897.
GeneIDi2953.
KEGGihsa:2953.

Polymorphism databases

DMDMi300680960.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF240786 Genomic DNA. Translation: AAG02373.1.
AP000351 Genomic DNA. No translation available.
PIRiA56847.
RefSeqiNP_000845.2. NM_000854.4.
UniGeneiHs.654462.
Hs.656498.

3D structure databases

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

Chemistry

ChEMBLiCHEMBL2142.

Polymorphism databases

DMDMi300680960.

Proteomic databases

MaxQBiP0CG29.
PRIDEiP0CG29.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000215780; ENSP00000215780; ENSG00000099984.
ENST00000618279; ENSP00000477540; ENSG00000277897.
GeneIDi2953.
KEGGihsa:2953.

Organism-specific databases

GeneCardsiGC22P024322.
HGNCiHGNC:4642. GSTT2.
HPAiHPA000750.
MIMi600437. gene.
neXtProtiNX_P0CG29.
GenAtlasiSearch...

Phylogenomic databases

HOGENOMiHOG000125747.
InParanoidiP0CG29.
KOiK00799.
OMAiIAYGPCA.
OrthoDBiEOG7V1FRJ.
PhylomeDBiP0CG29.
TreeFamiTF325759.

Enzyme and pathway databases

ReactomeiREACT_6926. Glutathione conjugation.

Miscellaneous databases

NextBioi11702.
PROiP0CG29.
SOURCEiSearch...

Gene expression databases

BgeeiP0CG29.
GenevestigatoriP30712.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1999) [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(1998) [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(1991) [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(1995) [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: April 1, 2015
This is version 41 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.