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Protein

Glutathione S-transferase theta-2

Gene

Gstt2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.

Catalytic activityi

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

Sites

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

ReactomeiREACT_317599. 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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:106188. Gstt2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: MGI
  • extracellular exosome Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 244243Glutathione S-transferase theta-2PRO_0000185941Add
BLAST

Proteomic databases

PaxDbiQ61133.
PRIDEiQ61133.

PTM databases

PhosphoSiteiQ61133.

Expressioni

Tissue specificityi

In liver, highest expression found in central vein limiting plate hepatocytes. Also expressed in interlobular bile duct epithelial cells. In lung, expressed in Clara cells and ciliated cells of the bronchiolar epithelium and in type II alveolar cells of the lung parenchyma.

Gene expression databases

CleanExiMM_GSTT2.
GenevestigatoriQ61133.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

IntActiQ61133. 2 interactions.
MINTiMINT-4120895.

Structurei

3D structure databases

ProteinModelPortaliQ61133.
SMRiQ61133. Positions 1-244.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8281GST N-terminalAdd
BLAST
Domaini88 – 230143GST 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

eggNOGiCOG0625.
GeneTreeiENSGT00540000069741.
HOGENOMiHOG000125747.
HOVERGENiHBG051854.
InParanoidiQ61133.
KOiK00799.
OMAiGVPLWVQ.
OrthoDBiEOG7V1FRJ.
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.
PF13417. GST_N_3. 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.

Q61133-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLELYLDLL SQPSRAVYIF AKKNGIPFQT RTVDILKGQH MSEQFSQVNC
60 70 80 90 100
LNKVPVLKDG SFVLTESTAI LIYLSSKYQV ADHWYPADLQ ARAQVHEYLG
110 120 130 140 150
WHADNIRGTF GVLLWTKVLG PLIGVQVPQE KVERNRDRMV LVLQQLEDKF
160 170 180 190 200
LRDRAFLVGQ QVTLADLMSL EELMQPVALG YNLFEGRPQL TAWRERVEAF
210 220 230 240
LGAELCQEAH STILSILGQA AKKMLPVPPP EVHASMQLRI ARIP
Length:244
Mass (Da):27,634
Last modified:October 3, 2012 - v4
Checksum:i3F45D6E12DA3DF29
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 381Missing in AAB03533 (PubMed:8617493).Curated
Sequence conflicti67 – 671S → R in AAB03533 (PubMed:8617493).Curated
Sequence conflicti178 – 1781A → G in AAB03534 (PubMed:8617493).Curated
Sequence conflicti206 – 2061C → Y in AAB03534 (PubMed:8617493).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U48419 Genomic DNA. Translation: AAB03533.1.
U48420 mRNA. Translation: AAB03534.1.
X98056 mRNA. Translation: CAA66666.1.
AK002392 mRNA. Translation: BAB22065.1.
AK158939 mRNA. Translation: BAE34734.1.
AC142499 Genomic DNA. No translation available.
CH466553 Genomic DNA. Translation: EDL31881.1.
BC012707 mRNA. Translation: AAH12707.1.
CCDSiCCDS48601.1.
PIRiS71879.
RefSeqiNP_034491.2. NM_010361.2.
XP_006513303.1. XM_006513240.1.
UniGeneiMm.24118.

Genome annotation databases

EnsembliENSMUST00000038257; ENSMUSP00000046324; ENSMUSG00000033318.
GeneIDi14872.
KEGGimmu:14872.
UCSCiuc011xgs.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U48419 Genomic DNA. Translation: AAB03533.1.
U48420 mRNA. Translation: AAB03534.1.
X98056 mRNA. Translation: CAA66666.1.
AK002392 mRNA. Translation: BAB22065.1.
AK158939 mRNA. Translation: BAE34734.1.
AC142499 Genomic DNA. No translation available.
CH466553 Genomic DNA. Translation: EDL31881.1.
BC012707 mRNA. Translation: AAH12707.1.
CCDSiCCDS48601.1.
PIRiS71879.
RefSeqiNP_034491.2. NM_010361.2.
XP_006513303.1. XM_006513240.1.
UniGeneiMm.24118.

3D structure databases

ProteinModelPortaliQ61133.
SMRiQ61133. Positions 1-244.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ61133. 2 interactions.
MINTiMINT-4120895.

PTM databases

PhosphoSiteiQ61133.

Proteomic databases

PaxDbiQ61133.
PRIDEiQ61133.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000038257; ENSMUSP00000046324; ENSMUSG00000033318.
GeneIDi14872.
KEGGimmu:14872.
UCSCiuc011xgs.1. mouse.

Organism-specific databases

CTDi2953.
MGIiMGI:106188. Gstt2.

Phylogenomic databases

eggNOGiCOG0625.
GeneTreeiENSGT00540000069741.
HOGENOMiHOG000125747.
HOVERGENiHBG051854.
InParanoidiQ61133.
KOiK00799.
OMAiGVPLWVQ.
OrthoDBiEOG7V1FRJ.
TreeFamiTF325759.

Enzyme and pathway databases

ReactomeiREACT_317599. Glutathione conjugation.

Miscellaneous databases

NextBioi287141.
PROiQ61133.
SOURCEiSearch...

Gene expression databases

CleanExiMM_GSTT2.
GenevestigatoriQ61133.

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.
PF13417. GST_N_3. 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 a cDNA and gene encoding the mouse theta class glutathione transferase mGSTT2 and its localization to chromosome 10B5-C1."
    Whittington A.T., Webb G.C., Baker R.T., Board P.G.
    Genomics 33:105-111(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: 129/Sv and C57BL/6 X CBA.
    Tissue: Liver.
  2. "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: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6 X C3H.
    Tissue: Liver and Lung.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Kidney and Visual cortex.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Strain: Czech II.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiGSTT2_MOUSE
AccessioniPrimary (citable) accession number: Q61133
Secondary accession number(s): Q61134, Q64472, Q91VB0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 3, 2012
Last modified: May 27, 2015
This is version 122 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.