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Protein

Glutathione S-transferase theta-2B

Gene

GSTT2B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. 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
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-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, UP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:33437. GSTT2B.

Subcellular locationi

GO - Cellular componenti

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

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.
ExpressionAtlasiP0CG30. baseline and differential.

Organism-specific databases

HPAiHPA000750.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi109208. 1 interaction.

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

GeneTreeiENSGT00540000069741.
InParanoidiP0CG30.
KOiK00799.
OMAiGVPLWVQ.
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

        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 PLIGVQVPEE 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):27,507
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:
EMBLi
GenBanki
DDBJi
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_001074312.1. NM_001080843.3.
UniGeneiHs.654462.
Hs.656498.

Genome annotation databases

EnsembliENST00000290765; ENSP00000290765; ENSG00000133433.
ENST00000616938; ENSP00000478389; ENSG00000278695.
GeneIDi653689.
KEGGihsa:2953.
hsa:653689.
UCSCiuc002zyw.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001074312.1. NM_001080843.3.
UniGeneiHs.654462.
Hs.656498.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi109208. 1 interaction.

PTM databases

PhosphoSiteiP0CG30.

Proteomic databases

MaxQBiP0CG30.
PRIDEiP0CG30.

Protocols and materials databases

DNASUi2953.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000290765; ENSP00000290765; ENSG00000133433.
ENST00000616938; ENSP00000478389; ENSG00000278695.
GeneIDi653689.
KEGGihsa:2953.
hsa:653689.
UCSCiuc002zyw.4. human.

Organism-specific databases

CTDi2953.
653689.
GeneCardsiGC22M024299.
HGNCiHGNC:33437. GSTT2B.
HPAiHPA000750.
neXtProtiNX_P0CG30.
PharmGKBiPA162390358.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00540000069741.
InParanoidiP0CG30.
KOiK00799.
OMAiGVPLWVQ.
OrthoDBiEOG7V1FRJ.
PhylomeDBiP0CG30.
TreeFamiTF325759.

Enzyme and pathway databases

ReactomeiREACT_6926. Glutathione conjugation.

Miscellaneous databases

EvolutionaryTraceiP0CG30.
GeneWikiiGSTT2.
NextBioi11702.
PROiP0CG30.

Gene expression databases

BgeeiP0CG30.
ExpressionAtlasiP0CG30. baseline and differential.

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. "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: February 4, 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. 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

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.