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P10648

- GSTA2_MOUSE

UniProt

P10648 - GSTA2_MOUSE

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Protein
Glutathione S-transferase A2
Gene
Gsta2
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei9 – 91Glutathione By similarity
Binding sitei45 – 451Glutathione
Binding sitei55 – 551Glutathione; via amide nitrogen and carbonyl oxygen

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. glutathione metabolic process Source: UniProtKB
  2. response to stilbenoid Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

ReactomeiREACT_215316. Glutathione conjugation.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase A2 (EC:2.5.1.18)
Alternative name(s):
GST class-alpha member 2
Glutathione S-transferase GT41A
Gene namesi
Name:Gsta2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:95863. Gsta2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 222221Glutathione S-transferase A2
PRO_0000185789Add
BLAST

Proteomic databases

PaxDbiP10648.

PTM databases

PhosphoSiteiP10648.

Expressioni

Gene expression databases

CleanExiMM_GSTA2.
GenevestigatoriP10648.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

IntActiP10648. 2 interactions.
MINTiMINT-4080211.
STRINGi10090.ENSMUSP00000034902.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 127
Helixi14 – 163
Helixi17 – 2610
Beta strandi31 – 355
Helixi38 – 469
Beta strandi57 – 604
Beta strandi63 – 675
Helixi68 – 7811
Helixi86 – 10823
Helixi109 – 1113
Turni114 – 1163
Helixi117 – 13014
Helixi132 – 14312
Beta strandi146 – 1494
Helixi155 – 17117
Helixi172 – 1754
Helixi179 – 19012
Helixi192 – 1987
Helixi210 – 21910

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML6X-ray1.90A/B2-222[»]
ProteinModelPortaliP10648.
SMRiP10648. Positions 3-222.

Miscellaneous databases

EvolutionaryTraceiP10648.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 8381GST N-terminal
Add
BLAST
Domaini85 – 208124GST C-terminal
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni67 – 682Glutathione binding

Sequence similaritiesi

Belongs to the GST superfamily. Alpha family.

Phylogenomic databases

eggNOGiNOG266414.
GeneTreeiENSGT00670000097856.
HOGENOMiHOG000115734.
HOVERGENiHBG053749.
InParanoidiP10648.
KOiK00799.
OMAiICQPEER.
OrthoDBiEOG79CZ0K.
TreeFamiTF105321.

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.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01266. GSTRNSFRASEA.
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.

P10648-1 [UniParc]FASTAAdd to Basket

« Hide

MAGKPVLHYF NARGRMECIR WLLAAAGVEF EEKFIQSPED LEKLKKDGNL    50
MFDQVPMVEI DGMKLVQTRA ILNYIATKYD LYGKDMKERA LIDMYTEGIL 100
DLTEMIGQLV LCPPDQREAK TALAKDRTKN RYLPAFEKVL KSHGQDYLVG 150
NRLTRVDVHL LELLLYVEEL DASLLTPFPL LKAFKSRISS LPNVKKFLHP 200
GSQRKPPLDA KQIEEARKVF KF 222
Length:222
Mass (Da):25,542
Last modified:October 3, 2012 - v3
Checksum:i837FFFC49C56F70F
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti199 – 1991H → Q in AAA37749. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03958 mRNA. Translation: AAA37749.1.
AC138587 Genomic DNA. No translation available.
CH466522 Genomic DNA. Translation: EDL26384.1.
CH466522 Genomic DNA. Translation: EDL26385.1.
CH466522 Genomic DNA. Translation: EDL26386.1.
CH466522 Genomic DNA. Translation: EDL26387.1.
BC061133 mRNA. Translation: AAH61133.1.
CCDSiCCDS23359.1.
RefSeqiNP_032208.2. NM_008182.3.
XP_006510877.1. XM_006510814.1.
UniGeneiMm.422778.

Genome annotation databases

EnsembliENSMUST00000034902; ENSMUSP00000034902; ENSMUSG00000057933.
GeneIDi14858.
KEGGimmu:14858.
UCSCiuc009quf.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03958 mRNA. Translation: AAA37749.1 .
AC138587 Genomic DNA. No translation available.
CH466522 Genomic DNA. Translation: EDL26384.1 .
CH466522 Genomic DNA. Translation: EDL26385.1 .
CH466522 Genomic DNA. Translation: EDL26386.1 .
CH466522 Genomic DNA. Translation: EDL26387.1 .
BC061133 mRNA. Translation: AAH61133.1 .
CCDSi CCDS23359.1.
RefSeqi NP_032208.2. NM_008182.3.
XP_006510877.1. XM_006510814.1.
UniGenei Mm.422778.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ML6 X-ray 1.90 A/B 2-222 [» ]
ProteinModelPortali P10648.
SMRi P10648. Positions 3-222.
ModBasei Search...

Protein-protein interaction databases

IntActi P10648. 2 interactions.
MINTi MINT-4080211.
STRINGi 10090.ENSMUSP00000034902.

PTM databases

PhosphoSitei P10648.

Proteomic databases

PaxDbi P10648.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000034902 ; ENSMUSP00000034902 ; ENSMUSG00000057933 .
GeneIDi 14858.
KEGGi mmu:14858.
UCSCi uc009quf.1. mouse.

Organism-specific databases

CTDi 2939.
MGIi MGI:95863. Gsta2.

Phylogenomic databases

eggNOGi NOG266414.
GeneTreei ENSGT00670000097856.
HOGENOMi HOG000115734.
HOVERGENi HBG053749.
InParanoidi P10648.
KOi K00799.
OMAi ICQPEER.
OrthoDBi EOG79CZ0K.
TreeFami TF105321.

Enzyme and pathway databases

Reactomei REACT_215316. Glutathione conjugation.

Miscellaneous databases

EvolutionaryTracei P10648.
NextBioi 287091.
PROi P10648.
SOURCEi Search...

Gene expression databases

CleanExi MM_GSTA2.
Genevestigatori P10648.

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.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view ]
PRINTSi PR01266. GSTRNSFRASEA.
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. "Tissue-specific induction of murine glutathione transferase mRNAs by butylated hydroxyanisole."
    Pearson W.R., Reinhart J., Sisk S.C., Anderson K.S., Adler P.N.
    J. Biol. Chem. 263:13324-13332(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. 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].
  4. "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: Kidney.
  5. "Residues 207, 216, and 221 and the catalytic activity of mGSTA1-1 and mGSTA2-2 toward benzo[a]pyrene-(7R,8S)-diol-(9S,10R)-epoxide."
    Gu Y., Xiao B., Wargo H.L., Bucher M.H., Singh S.V., Ji X.
    Biochemistry 42:917-921(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE AND SUBSTRATE ANALOG, SUBUNIT.

Entry informationi

Entry nameiGSTA2_MOUSE
AccessioniPrimary (citable) accession number: P10648
Secondary accession number(s): Q6P8Q1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 3, 2012
Last modified: September 3, 2014
This is version 118 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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