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Protein

Glutathione S-transferase 2

Gene

GSTM2

Organism
Gallus gallus (Chicken)
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.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei50GlutathioneBy similarity1
Binding sitei116SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase 2 (EC:2.5.1.18)
Alternative name(s):
GST class-mu
GST-CL2
GSTM1-1
Gene namesi
Name:GSTM2
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi108R → E: Reduced affinity for glutathione. 1 Publication1
Mutagenesisi108R → L: Reduced catalytic activity. 1 Publication1
Mutagenesisi210W → F: Reduced affinity for glutathione. 1 Publication1
Mutagenesisi210W → H, I or P: Reduced catalytic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001858382 – 220Glutathione S-transferase 2Add BLAST219

Proteomic databases

PRIDEiP20136.

Interactioni

Subunit structurei

Homodimer.2 Publications

Structurei

Secondary structure

1220
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 11Combined sources9
Helixi12 – 14Combined sources3
Helixi15 – 23Combined sources9
Beta strandi28 – 33Combined sources6
Turni38 – 40Combined sources3
Helixi44 – 47Combined sources4
Helixi50 – 52Combined sources3
Beta strandi60 – 65Combined sources6
Beta strandi68 – 72Combined sources5
Helixi73 – 82Combined sources10
Turni83 – 85Combined sources3
Helixi91 – 116Combined sources26
Helixi120 – 142Combined sources23
Beta strandi146 – 152Combined sources7
Helixi155 – 170Combined sources16
Helixi175 – 177Combined sources3
Helixi180 – 189Combined sources10
Helixi192 – 198Combined sources7
Beta strandi200 – 202Combined sources3
Beta strandi214 – 216Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C72X-ray2.80A/B/C/D2-220[»]
1GSUX-ray1.94A/B2-220[»]
ProteinModelPortaliP20136.
SMRiP20136.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20136.

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 binding2 Publications2
Regioni43 – 46Glutathione binding2 Publications4
Regioni59 – 60Glutathione binding2 Publications2
Regioni72 – 73Glutathione binding2 Publications2

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

HOVERGENiHBG106842.
InParanoidiP20136.
KOiK00799.
PhylomeDBiP20136.

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.

P20136-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVVTLGYWDI RGLAHAIRLL LEYTETPYQE RRYKAGPAPD FDPSDWTNEK
60 70 80 90 100
EKLGLDFPNL PYLIDGDVKL TQSNAILRYI ARKHNMCGET EVEKQRVDVL
110 120 130 140 150
ENHLMDLRMA FARLCYSPDF EKLKPAYLEQ LPGKLRQLSR FLGSRSWFVG
160 170 180 190 200
DKLTFVDFLA YDVLDQQRMF VPDCPELQGN LSQFLQRFEA LEKISAYMRS
210 220
GRFMKAPIFW YTALWNNKKE
Length:220
Mass (Da):25,893
Last modified:January 23, 2007 - v4
Checksum:iA7A7D843CE54E6F9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58248 mRNA. Translation: CAA41202.1.
PIRiS18464.
RefSeqiNP_990421.1. NM_205090.1.
UniGeneiGga.4223.

Genome annotation databases

GeneIDi395976.
KEGGigga:395976.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58248 mRNA. Translation: CAA41202.1.
PIRiS18464.
RefSeqiNP_990421.1. NM_205090.1.
UniGeneiGga.4223.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C72X-ray2.80A/B/C/D2-220[»]
1GSUX-ray1.94A/B2-220[»]
ProteinModelPortaliP20136.
SMRiP20136.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP20136.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi395976.
KEGGigga:395976.

Organism-specific databases

CTDi2946.

Phylogenomic databases

HOVERGENiHBG106842.
InParanoidiP20136.
KOiK00799.
PhylomeDBiP20136.

Miscellaneous databases

EvolutionaryTraceiP20136.
PROiP20136.

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_CHICK
AccessioniPrimary (citable) accession number: P20136
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 117 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.