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Protein

Glutathione S-transferase Mu 2

Gene

Gstm2

Organism
Rattus norvegicus (Rat)
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. The olfactory GST may be crucial for the acuity of the olfactory process.

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei50Glutathione1 Publication1
Binding sitei116SubstrateBy similarity1

GO - Molecular functioni

  • glutathione transferase activity Source: RGD
  • protein homodimerization activity Source: RGD

GO - Biological processi

  • aging Source: RGD
  • response to catechin Source: RGD
  • response to genistein Source: RGD
  • response to metal ion Source: RGD
  • response to organic cyclic compound Source: RGD
  • sensory perception of smell Source: UniProtKB-KW
  • xenobiotic metabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Olfaction, Sensory transduction

Enzyme and pathway databases

ReactomeiR-RNO-156590. Glutathione conjugation.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase Mu 2 (EC:2.5.1.18)
Alternative name(s):
GST 4-4
GSTM2-2
Glutathione S-transferase Yb-2
Short name:
GST Yb2
Gene namesi
Name:Gstm2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi2756. Gstm2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: RGD
  • plasma membrane Source: RGD
  • protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2504.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved4 Publications
ChainiPRO_00001858322 – 218Glutathione S-transferase Mu 2Add BLAST217

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei27PhosphoserineCombined sources1
Modified residuei44PhosphoserineCombined sources1
Modified residuei117PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP08010.
PRIDEiP08010.

PTM databases

iPTMnetiP08010.
PhosphoSitePlusiP08010.

Expressioni

Gene expression databases

BgeeiENSRNOG00000019094.
ExpressionAtlasiP08010. baseline and differential.
GenevisibleiP08010. RN.

Interactioni

Subunit structurei

Homodimer or heterodimer.1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

IntActiP08010. 1 interactor.
STRINGi10116.ENSRNOP00000025939.

Structurei

Secondary structure

1218
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 10Combined sources8
Turni12 – 14Combined sources3
Helixi15 – 23Combined sources9
Beta strandi28 – 33Combined sources6
Turni38 – 40Combined sources3
Helixi44 – 50Combined sources7
Beta strandi60 – 65Combined sources6
Beta strandi68 – 72Combined sources5
Helixi73 – 83Combined sources11
Helixi91 – 116Combined sources26
Helixi120 – 142Combined sources23
Beta strandi150 – 152Combined sources3
Helixi155 – 170Combined sources16
Turni172 – 177Combined sources6
Helixi179 – 189Combined sources11
Helixi192 – 198Combined sources7
Beta strandi214 – 216Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B4PX-ray1.70A2-218[»]
ProteinModelPortaliP08010.
SMRiP08010.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08010.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 88GST N-terminalAdd BLAST87
Domaini90 – 214GST C-terminalAdd BLAST125

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni7 – 8Glutathione binding1 Publication2
Regioni43 – 46Glutathione binding1 Publication4
Regioni59 – 60Glutathione binding1 Publication2
Regioni72 – 73Glutathione binding1 Publication2

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

eggNOGiENOG410IN5J. Eukaryota.
ENOG4110YU0. LUCA.
GeneTreeiENSGT00550000074559.
HOGENOMiHOG000115735.
HOVERGENiHBG106842.
InParanoidiP08010.
KOiK00799.
OMAiRPWFAGN.
OrthoDBiEOG091G0K2E.
PhylomeDBiP08010.
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.

P08010-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPMTLGYWDI RGLAHAIRLF LEYTDTSYED KKYSMGDAPD YDRSQWLSEK
60 70 80 90 100
FKLGLDFPNL PYLIDGSHKI TQSNAILRYL GRKHNLCGET EEERIRVDVL
110 120 130 140 150
ENQAMDTRLQ LAMVCYSPDF ERKKPEYLEG LPEKMKLYSE FLGKQPWFAG
160 170 180 190 200
NKITYVDFLV YDVLDQHRIF EPKCLDAFPN LKDFVARFEG LKKISDYMKS
210
GRFLSKPIFA KMAFWNPK
Length:218
Mass (Da):25,703
Last modified:January 23, 2007 - v2
Checksum:iC23B30C171DB852F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti147W → S AA sequence (PubMed:3699019).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02592 mRNA. Translation: AAA41285.1.
M13590 mRNA. Translation: AAA42351.1.
J03914 Genomic DNA. Translation: AAA41296.1.
PIRiA29231. XURTG4.
RefSeqiNP_803175.1. NM_177426.1.
UniGeneiRn.625.

Genome annotation databases

EnsembliENSRNOT00000025939; ENSRNOP00000025939; ENSRNOG00000018937.
GeneIDi24424.
KEGGirno:24424.
UCSCiRGD:2756. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02592 mRNA. Translation: AAA41285.1.
M13590 mRNA. Translation: AAA42351.1.
J03914 Genomic DNA. Translation: AAA41296.1.
PIRiA29231. XURTG4.
RefSeqiNP_803175.1. NM_177426.1.
UniGeneiRn.625.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B4PX-ray1.70A2-218[»]
ProteinModelPortaliP08010.
SMRiP08010.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP08010. 1 interactor.
STRINGi10116.ENSRNOP00000025939.

Chemistry databases

ChEMBLiCHEMBL2504.

PTM databases

iPTMnetiP08010.
PhosphoSitePlusiP08010.

Proteomic databases

PaxDbiP08010.
PRIDEiP08010.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000025939; ENSRNOP00000025939; ENSRNOG00000018937.
GeneIDi24424.
KEGGirno:24424.
UCSCiRGD:2756. rat.

Organism-specific databases

CTDi2946.
RGDi2756. Gstm2.

Phylogenomic databases

eggNOGiENOG410IN5J. Eukaryota.
ENOG4110YU0. LUCA.
GeneTreeiENSGT00550000074559.
HOGENOMiHOG000115735.
HOVERGENiHBG106842.
InParanoidiP08010.
KOiK00799.
OMAiRPWFAGN.
OrthoDBiEOG091G0K2E.
PhylomeDBiP08010.
TreeFamiTF353040.

Enzyme and pathway databases

ReactomeiR-RNO-156590. Glutathione conjugation.

Miscellaneous databases

EvolutionaryTraceiP08010.
PROiP08010.

Gene expression databases

BgeeiENSRNOG00000019094.
ExpressionAtlasiP08010. baseline and differential.
GenevisibleiP08010. RN.

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...

Entry informationi

Entry nameiGSTM2_RAT
AccessioniPrimary (citable) accession number: P08010
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Yb subclass selectively binds steroid hormones.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.