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Protein

Glutathione S-transferase Mu 1

Gene

Gstm1

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.2 Publications

Sites

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

GO - Molecular functioni

  • glutathione transferase activity Source: RGD
  • nickel cation binding Source: RGD
  • protein homodimerization activity Source: RGD
  • protein kinase binding Source: RGD
  • steroid binding Source: RGD

GO - Biological processi

  • glutathione metabolic process Source: UniProtKB
  • response to amino acid Source: RGD
  • response to antibiotic Source: RGD
  • response to axon injury Source: RGD
  • response to drug Source: RGD
  • response to ethanol Source: RGD
  • response to lead ion Source: RGD
  • response to lithium ion Source: RGD
  • response to metal ion Source: RGD
  • sensory perception of smell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Olfaction, Sensory transduction

Enzyme and pathway databases

BRENDAi2.5.1.18. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase Mu 1 (EC:2.5.1.18)
Alternative name(s):
GST 3-3
GSTM1-1
Glutathione S-transferase Yb-1
Short name:
GST Yb1
Gene namesi
Name:Gstm1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2755. Gstm1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • extracellular region Source: RGD
  • protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi7Y → F or L: Reduces catalytic activity about 100-fold. 1 Publication1
Mutagenesisi87C → S: No change in activity. 1 Publication1
Mutagenesisi116Y → F: Reduces enzyme activity about 100-fold. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL2209.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved6 Publications
ChainiPRO_00001858312 – 218Glutathione S-transferase Mu 1Add BLAST217

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei67PhosphoserineCombined sources1
Modified residuei205PhosphoserineCombined sources1
Modified residuei210PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP04905.
PRIDEiP04905.

PTM databases

iPTMnetiP04905.
PhosphoSitePlusiP04905.

Interactioni

Subunit structurei

Homodimer or heterodimer.3 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: RGD
  • protein kinase binding Source: RGD

Protein-protein interaction databases

BioGridi246588. 1 interactor.
MINTiMINT-4564586.
STRINGi10116.ENSRNOP00000039050.

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 – 41Combined sources4
Helixi44 – 47Combined sources4
Turni48 – 51Combined sources4
Beta strandi60 – 65Combined sources6
Beta strandi68 – 72Combined sources5
Helixi73 – 83Combined sources11
Helixi91 – 115Combined sources25
Helixi120 – 142Combined sources23
Beta strandi146 – 152Combined sources7
Helixi155 – 170Combined sources16
Turni172 – 175Combined sources4
Helixi179 – 189Combined sources11
Helixi192 – 198Combined sources7
Beta strandi200 – 202Combined sources3
Beta strandi213 – 216Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GSBX-ray2.50A/B/C/D2-218[»]
1GSCX-ray2.50A/B/C/D2-218[»]
1MTCX-ray2.20A/B2-218[»]
2GSTX-ray1.80A/B2-218[»]
3FYGX-ray2.20A/B2-218[»]
3GSTX-ray1.90A/B2-218[»]
4GSTX-ray1.90A/B2-218[»]
5FWGX-ray2.00A/B2-218[»]
5GSTX-ray2.00A/B2-218[»]
6GSTX-ray2.20A/B2-218[»]
6GSUX-ray1.85A/B2-218[»]
6GSVX-ray1.75A/B2-218[»]
6GSWX-ray1.85A/B2-218[»]
6GSXX-ray1.91A/B2-218[»]
6GSYX-ray2.20A/B2-218[»]
ProteinModelPortaliP04905.
SMRiP04905.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04905.

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 binding1 Publication1 Publication2
Regioni43 – 46Glutathione binding1 Publication1 Publication4
Regioni59 – 60Glutathione binding1 Publication1 Publication2
Regioni72 – 73Glutathione binding1 Publication1 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.
HOGENOMiHOG000115735.
HOVERGENiHBG106842.
InParanoidiP04905.
KOiK00799.
PhylomeDBiP04905.

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.

P04905-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPMILGYWNV RGLTHPIRLL LEYTDSSYEE KRYAMGDAPD YDRSQWLNEK
60 70 80 90 100
FKLGLDFPNL PYLIDGSRKI TQSNAIMRYL ARKHHLCGET EEERIRADIV
110 120 130 140 150
ENQVMDNRMQ LIMLCYNPDF EKQKPEFLKT IPEKMKLYSE FLGKRPWFAG
160 170 180 190 200
DKVTYVDFLA YDILDQYHIF EPKCLDAFPN LKDFLARFEG LKKISAYMKS
210
SRYLSTPIFS KLAQWSNK
Length:218
Mass (Da):25,914
Last modified:January 23, 2007 - v2
Checksum:i1A8E80D09A5CACA8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti199 – 200KS → NC in AAA41287 (PubMed:3840477).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04229 mRNA. Translation: CAA27811.1.
M11719 mRNA. Translation: AAA41287.1.
J02810 mRNA. Translation: AAA41293.1.
BC063172 mRNA. Translation: AAH63172.1.
PIRiA29794.
RefSeqiNP_058710.1. NM_017014.1.
UniGeneiRn.202944.

Genome annotation databases

GeneIDi24423.
KEGGirno:24423.
UCSCiRGD:2755. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04229 mRNA. Translation: CAA27811.1.
M11719 mRNA. Translation: AAA41287.1.
J02810 mRNA. Translation: AAA41293.1.
BC063172 mRNA. Translation: AAH63172.1.
PIRiA29794.
RefSeqiNP_058710.1. NM_017014.1.
UniGeneiRn.202944.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GSBX-ray2.50A/B/C/D2-218[»]
1GSCX-ray2.50A/B/C/D2-218[»]
1MTCX-ray2.20A/B2-218[»]
2GSTX-ray1.80A/B2-218[»]
3FYGX-ray2.20A/B2-218[»]
3GSTX-ray1.90A/B2-218[»]
4GSTX-ray1.90A/B2-218[»]
5FWGX-ray2.00A/B2-218[»]
5GSTX-ray2.00A/B2-218[»]
6GSTX-ray2.20A/B2-218[»]
6GSUX-ray1.85A/B2-218[»]
6GSVX-ray1.75A/B2-218[»]
6GSWX-ray1.85A/B2-218[»]
6GSXX-ray1.91A/B2-218[»]
6GSYX-ray2.20A/B2-218[»]
ProteinModelPortaliP04905.
SMRiP04905.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246588. 1 interactor.
MINTiMINT-4564586.
STRINGi10116.ENSRNOP00000039050.

Chemistry databases

ChEMBLiCHEMBL2209.

PTM databases

iPTMnetiP04905.
PhosphoSitePlusiP04905.

Proteomic databases

PaxDbiP04905.
PRIDEiP04905.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24423.
KEGGirno:24423.
UCSCiRGD:2755. rat.

Organism-specific databases

CTDi2944.
RGDi2755. Gstm1.

Phylogenomic databases

eggNOGiENOG410IN5J. Eukaryota.
ENOG4110YU0. LUCA.
HOGENOMiHOG000115735.
HOVERGENiHBG106842.
InParanoidiP04905.
KOiK00799.
PhylomeDBiP04905.

Enzyme and pathway databases

BRENDAi2.5.1.18. 5301.

Miscellaneous databases

EvolutionaryTraceiP04905.
PROiP04905.

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 nameiGSTM1_RAT
AccessioniPrimary (citable) accession number: P04905
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 162 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.