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Protein

Glutathione S-transferase Mu 2

Gene

Gstm2

Organism
Mus musculus (Mouse)
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.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei116 – 1161SubstrateBy similarity

GO - Molecular functioni

  1. enzyme binding Source: MGI
  2. glutathione binding Source: MGI
  3. glutathione transferase activity Source: MGI
  4. protein heterodimerization activity Source: MGI
  5. protein homodimerization activity Source: MGI

GO - Biological processi

  1. cellular detoxification of nitrogen compound Source: MGI
  2. glutathione metabolic process Source: MGI
  3. nitrobenzene metabolic process Source: MGI
  4. xenobiotic catabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

ReactomeiREACT_215316. Glutathione conjugation.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Gstm2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:95861. Gstm2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 218217Glutathione S-transferase Mu 2PRO_0000185827Add
BLAST

Proteomic databases

MaxQBiP15626.
PaxDbiP15626.
PRIDEiP15626.

2D gel databases

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

PTM databases

PhosphoSiteiP15626.

Expressioni

Gene expression databases

BgeeiP15626.
CleanExiMM_GSTM2.
ExpressionAtlasiP15626. baseline and differential.
GenevestigatoriP15626.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

IntActiP15626. 3 interactions.
MINTiMINT-1869197.
STRINGi10090.ENSMUSP00000012348.

Structurei

3D structure databases

ProteinModelPortaliP15626.
SMRiP15626. Positions 2-218.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8887GST N-terminalAdd
BLAST
Domaini90 – 208119GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni7 – 82Glutathione bindingBy similarity
Regioni46 – 505Glutathione bindingBy similarity
Regioni59 – 602Glutathione bindingBy similarity
Regioni72 – 732Glutathione bindingBy similarity

Sequence similaritiesi

Belongs to the GST superfamily. Mu family.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Phylogenomic databases

eggNOGiNOG300089.
GeneTreeiENSGT00550000074559.
HOGENOMiHOG000115735.
HOVERGENiHBG106842.
InParanoidiP15626.
KOiK00799.
OMAiRVCYNPD.
OrthoDBiEOG7KH9M3.
PhylomeDBiP15626.
TreeFamiTF353040.

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.
IPR003081. GST_mu.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01267. GSTRNSFRASEM.
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.

P15626-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPMTLGYWDI RGLAHAIRLL LEYTDTSYED KKYTMGDAPD YDRSQWLSEK
60 70 80 90 100
FKLGLDFPNL PYLIDGSHKI TQSNAILRYL ARKHNLCGET EEERIRVDIL
110 120 130 140 150
ENQAMDTRIQ LAMVCYSPDF EKKKPEYLEG LPEKMKLYSE FLGKQPWFAG
160 170 180 190 200
NKVTYVDFLV YDVLDQHRIF EPKCLDAFPN LKDFMGRFEG LKKISDYMKS
210
SRFLSKPIFA KMAFWNPK
Length:218
Mass (Da):25,717
Last modified:January 23, 2007 - v2
Checksum:i93D790DD75CBF51E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04696 mRNA. Translation: AAA37706.1.
AF319526 Genomic DNA. Translation: AAK28508.1.
BC037068 mRNA. Translation: AAH37068.1.
CCDSiCCDS17746.1.
PIRiB34159.
RefSeqiNP_032209.1. NM_008183.3.
UniGeneiMm.440086.

Genome annotation databases

EnsembliENSMUST00000012348; ENSMUSP00000012348; ENSMUSG00000040562.
GeneIDi14863.
KEGGimmu:14863.
UCSCiuc008qxw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04696 mRNA. Translation: AAA37706.1.
AF319526 Genomic DNA. Translation: AAK28508.1.
BC037068 mRNA. Translation: AAH37068.1.
CCDSiCCDS17746.1.
PIRiB34159.
RefSeqiNP_032209.1. NM_008183.3.
UniGeneiMm.440086.

3D structure databases

ProteinModelPortaliP15626.
SMRiP15626. Positions 2-218.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP15626. 3 interactions.
MINTiMINT-1869197.
STRINGi10090.ENSMUSP00000012348.

PTM databases

PhosphoSiteiP15626.

2D gel databases

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

Proteomic databases

MaxQBiP15626.
PaxDbiP15626.
PRIDEiP15626.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000012348; ENSMUSP00000012348; ENSMUSG00000040562.
GeneIDi14863.
KEGGimmu:14863.
UCSCiuc008qxw.1. mouse.

Organism-specific databases

CTDi2946.
MGIiMGI:95861. Gstm2.

Phylogenomic databases

eggNOGiNOG300089.
GeneTreeiENSGT00550000074559.
HOGENOMiHOG000115735.
HOVERGENiHBG106842.
InParanoidiP15626.
KOiK00799.
OMAiRVCYNPD.
OrthoDBiEOG7KH9M3.
PhylomeDBiP15626.
TreeFamiTF353040.

Enzyme and pathway databases

ReactomeiREACT_215316. Glutathione conjugation.

Miscellaneous databases

NextBioi287109.
PROiP15626.
SOURCEiSearch...

Gene expression databases

BgeeiP15626.
CleanExiMM_GSTM2.
ExpressionAtlasiP15626. baseline and differential.
GenevestigatoriP15626.

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.
IPR003081. GST_mu.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01267. GSTRNSFRASEM.
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. "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.

Entry informationi

Entry nameiGSTM2_MOUSE
AccessioniPrimary (citable) accession number: P15626
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.