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P0CG30

- GSTT2_HUMAN

UniProt

P0CG30 - GSTT2_HUMAN

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Protein
Glutathione S-transferase theta-2B
Gene
GSTT2B, GSTT2
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. 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

Organism-specific databases

HGNCiHGNC:33437. GSTT2B.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
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-2B
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiP0CG30.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8281GST N-terminal
Add
BLAST
Domaini88 – 224137GST C-terminal
Add
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.

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

Natural variant

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

Sequence conflict

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

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

« 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: September 3, 2014
This is version 36 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

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