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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei116 – 1161SubstrateBy similarity

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB-EC
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
ProteomesiUP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi108 – 1081R → E: Reduced affinity for glutathione. 1 Publication
Mutagenesisi108 – 1081R → L: Reduced catalytic activity. 1 Publication
Mutagenesisi210 – 2101W → F: Reduced affinity for glutathione. 1 Publication
Mutagenesisi210 – 2101W → H, I or P: Reduced catalytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 220219Glutathione S-transferase 2PRO_0000185838Add
BLAST

Proteomic databases

PRIDEiP20136.

Interactioni

Subunit structurei

Homodimer.2 Publications

Structurei

Secondary structure

1
220
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 119Combined sources
Helixi12 – 143Combined sources
Helixi15 – 239Combined sources
Beta strandi28 – 336Combined sources
Turni38 – 403Combined sources
Helixi44 – 474Combined sources
Helixi50 – 523Combined sources
Beta strandi60 – 656Combined sources
Beta strandi68 – 725Combined sources
Helixi73 – 8210Combined sources
Turni83 – 853Combined sources
Helixi91 – 11626Combined sources
Helixi120 – 14223Combined sources
Beta strandi146 – 1527Combined sources
Helixi155 – 17016Combined sources
Helixi175 – 1773Combined sources
Helixi180 – 18910Combined sources
Helixi192 – 1987Combined sources
Beta strandi200 – 2023Combined sources
Beta strandi214 – 2163Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C72X-ray2.80A/B/C/D2-220[»]
1GSUX-ray1.94A/B2-220[»]
ProteinModelPortaliP20136.
SMRiP20136. Positions 2-218.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20136.

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 binding
Regioni46 – 505Glutathione binding
Regioni59 – 602Glutathione binding
Regioni72 – 732Glutathione binding

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 22, 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
EntryMethodResolution (Å)ChainPositionsPDBsum
1C72X-ray2.80A/B/C/D2-220[»]
1GSUX-ray1.94A/B2-220[»]
ProteinModelPortaliP20136.
SMRiP20136. Positions 2-218.
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.
NextBioi20816041.

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

  1. "Nucleotide sequence of a class mu glutathione S-transferase from chicken liver."
    Liu L.-F., Tam M.F.
    Biochim. Biophys. Acta 1090:343-344(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: White leghorn.
    Tissue: Liver.
  2. "Characterization of glutathione S-transferases from day-old chick livers."
    Chang L.-H., Chuang L.-F., Tsai C.-P., Tu C.-P.D., Tam M.F.
    Biochemistry 29:744-750(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-35.
    Tissue: Liver.
  3. Liu L.-F.
    Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 130.
  4. "The three-dimensional structure of an avian class-mu glutathione S-transferase, cGSTM1-1 at 1.94-A resolution."
    Sun Y.-J., Kuan I.-C., Tam M.F., Hsiao C.-D.
    J. Mol. Biol. 278:239-252(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE ANALOG.
  5. "Tyr115, gln165 and trp209 contribute to the 1, 2-epoxy-3-(p-nitrophenoxy)propane-conjugating activity of glutathione S-transferase cGSTM1-1."
    Chern M.K., Wu T.C., Hsieh C.H., Chou C.C., Liu L.F., Kuan I.C., Yeh Y.H., Hsiao C.D., Tam M.F.
    J. Mol. Biol. 300:1257-1269(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE ANALOG, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-108 AND TRP-210.

Entry informationi

Entry nameiGSTM2_CHICK
AccessioniPrimary (citable) accession number: P20136
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 1991
Last sequence update: January 22, 2007
Last modified: February 3, 2015
This is version 109 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

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.