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P15626 (GSTM2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase Mu 2

EC=2.5.1.18
Alternative name(s):
GST 5-5
GST class-mu 2
Glutathione S-transferase pmGT2
Gene names
Name:Gstm2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length218 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the GST superfamily. Mu family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 218217Glutathione S-transferase Mu 2
PRO_0000185827

Regions

Domain2 – 8887GST N-terminal
Domain90 – 208119GST C-terminal
Region7 – 82Glutathione binding By similarity
Region46 – 505Glutathione binding By similarity
Region59 – 602Glutathione binding By similarity
Region72 – 732Glutathione binding By similarity

Sites

Binding site1161Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P15626 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 93D790DD75CBF51E

FASTA21825,717
        10         20         30         40         50         60 
MPMTLGYWDI RGLAHAIRLL LEYTDTSYED KKYTMGDAPD YDRSQWLSEK FKLGLDFPNL 

        70         80         90        100        110        120 
PYLIDGSHKI TQSNAILRYL ARKHNLCGET EEERIRVDIL ENQAMDTRIQ LAMVCYSPDF 

       130        140        150        160        170        180 
EKKKPEYLEG LPEKMKLYSE FLGKQPWFAG NKVTYVDFLV YDVLDQHRIF EPKCLDAFPN 

       190        200        210 
LKDFMGRFEG LKKISDYMKS SRFLSKPIFA KMAFWNPK 

« Hide

References

« Hide 'large scale' references
[1]"Isolation, characterization, and expression in Escherichia coli of two murine Mu class glutathione S-transferase cDNAs homologous to the rat subunits 3 (Yb1) and 4 (Yb2)."
Townsend A.J., Goldsmith M.E., Pickett C.B., Cowan K.H.
J. Biol. Chem. 264:21582-21590(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Genomic organization and characterization of the promoter region of murine GSTM2 gene."
Kumar A., Reddy E.P.
Gene 270:221-229(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/SvJ.
[3]"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: FVB/N.
Tissue: Colon.
[4]"Purification and characterization of glutathione S-transferase of murine ovary and testis."
Awasthi S., Singhal S.S., Srivastava S.K., Awasthi Y.C.
Arch. Biochem. Biophys. 301:143-150(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-25.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04696 mRNA. Translation: AAA37706.1.
AF319526 Genomic DNA. Translation: AAK28508.1.
BC037068 mRNA. Translation: AAH37068.1.
PIRB34159.
RefSeqNP_032209.1. NM_008183.3.
UniGeneMm.440086.

3D structure databases

ProteinModelPortalP15626.
SMRP15626. Positions 2-218.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP15626. 3 interactions.
MINTMINT-1869197.
STRING10090.ENSMUSP00000012348.

PTM databases

PhosphoSiteP15626.

2D gel databases

REPRODUCTION-2DPAGEIPI00228820.
P15626.
SWISS-2DPAGEP15626.

Proteomic databases

PaxDbP15626.
PRIDEP15626.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000012348; ENSMUSP00000012348; ENSMUSG00000040562.
GeneID14863.
KEGGmmu:14863.
UCSCuc008qxw.1. mouse.

Organism-specific databases

CTD2946.
MGIMGI:95861. Gstm2.

Phylogenomic databases

eggNOGNOG300089.
GeneTreeENSGT00550000074559.
HOGENOMHOG000115735.
HOVERGENHBG106842.
InParanoidP15626.
KOK00799.
OMAYSPDFER.
OrthoDBEOG7KH9M3.
PhylomeDBP15626.
TreeFamTF353040.

Gene expression databases

ArrayExpressP15626.
BgeeP15626.
CleanExMM_GSTM2.
GenevestigatorP15626.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR003081. GST_mu.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSPR01267. GSTRNSFRASEM.
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio287109.
PROP15626.
SOURCESearch...

Entry information

Entry nameGSTM2_MOUSE
AccessionPrimary (citable) accession number: P15626
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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