Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glutathione S-transferase Mu 2

Gene

Gstm2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Binding sitei50GlutathioneBy similarity1
Binding sitei116SubstrateBy similarity1

GO - Molecular functioni

  • enzyme binding Source: MGI
  • glutathione binding Source: MGI
  • glutathione transferase activity Source: MGI
  • protein heterodimerization activity Source: MGI
  • protein homodimerization activity Source: MGI

GO - Biological processi

Keywordsi

Molecular functionTransferase

Enzyme and pathway databases

ReactomeiR-MMU-156590 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:95861 Gstm2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001858272 – 218Glutathione S-transferase Mu 2Add BLAST217

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei27PhosphoserineBy similarity1
Modified residuei44PhosphoserineBy similarity1
Modified residuei117PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP15626
PaxDbiP15626
PeptideAtlasiP15626
PRIDEiP15626

2D gel databases

REPRODUCTION-2DPAGEIPI00228820
P15626
SWISS-2DPAGEP15626

PTM databases

iPTMnetiP15626
PhosphoSitePlusiP15626

Expressioni

Gene expression databases

BgeeiENSMUSG00000040562
CleanExiMM_GSTM2
ExpressionAtlasiP15626 baseline and differential
GenevisibleiP15626 MM

Interactioni

Subunit structurei

Homodimer.

GO - Molecular functioni

  • enzyme binding Source: MGI
  • protein heterodimerization activity Source: MGI
  • protein homodimerization activity Source: MGI

Protein-protein interaction databases

BioGridi200095, 1 interactor
IntActiP15626, 4 interactors
MINTiP15626
STRINGi10090.ENSMUSP00000012348

Structurei

3D structure databases

ProteinModelPortaliP15626
SMRiP15626
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 88GST N-terminalAdd BLAST87
Domaini90 – 208GST C-terminalAdd BLAST119

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni7 – 8Glutathione bindingBy similarity2
Regioni43 – 46Glutathione bindingBy similarity4
Regioni59 – 60Glutathione bindingBy similarity2
Regioni72 – 73Glutathione bindingBy similarity2

Sequence similaritiesi

Belongs to the GST superfamily. Mu family.Curated

Phylogenomic databases

eggNOGiENOG410IN5J Eukaryota
ENOG4110YU0 LUCA
GeneTreeiENSGT00550000074559
HOGENOMiHOG000115735
HOVERGENiHBG106842
InParanoidiP15626
KOiK00799
OMAiYWDIRGR
OrthoDBiEOG091G0K2E
PhylomeDBiP15626
TreeFamiTF353040

Family and domain databases

InterProiView protein in InterPro
IPR010987 Glutathione-S-Trfase_C-like
IPR036282 Glutathione-S-Trfase_C_sf
IPR004045 Glutathione_S-Trfase_N
IPR004046 GST_C
IPR003081 GST_mu
IPR036249 Thioredoxin-like_sf
PfamiView protein in Pfam
PF00043 GST_C, 1 hit
PF02798 GST_N, 1 hit
PRINTSiPR01267 GSTRNSFRASEM
SUPFAMiSSF47616 SSF47616, 1 hit
SSF52833 SSF52833, 1 hit
PROSITEiView protein in PROSITE
PS50405 GST_CTER, 1 hit
PS50404 GST_NTER, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiGSTM2_MOUSE
AccessioniPrimary (citable) accession number: P15626
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 156 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health