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P20136

- GSTM2_CHICK

UniProt

P20136 - GSTM2_CHICK

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Protein
Glutathione S-transferase 2
Gene
GSTM2
Organism
Gallus gallus (Chicken)
Status
Reviewed - 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 – 1161Substrate By 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: 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 2
PRO_0000185838Add
BLAST

Proteomic databases

PRIDEiP20136.

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP20136.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8887GST N-terminal
Add
BLAST
Domaini90 – 208119GST C-terminal
Add
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.

Phylogenomic databases

HOVERGENiHBG106842.
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

MVVTLGYWDI RGLAHAIRLL LEYTETPYQE RRYKAGPAPD FDPSDWTNEK    50
EKLGLDFPNL PYLIDGDVKL TQSNAILRYI ARKHNMCGET EVEKQRVDVL 100
ENHLMDLRMA FARLCYSPDF EKLKPAYLEQ LPGKLRQLSR FLGSRSWFVG 150
DKLTFVDFLA YDVLDQQRMF VPDCPELQGN LSQFLQRFEA LEKISAYMRS 200
GRFMKAPIFW YTALWNNKKE 220
Length:220
Mass (Da):25,893
Last modified:January 23, 2007 - v4
Checksum:iA7A7D843CE54E6F9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
X58248 mRNA. Translation: CAA41202.1 .
PIRi S18464.
RefSeqi NP_990421.1. NM_205090.1.
UniGenei Gga.4223.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1C72 X-ray 2.80 A/B/C/D 2-220 [» ]
1GSU X-ray 1.94 A/B 2-220 [» ]
ProteinModelPortali P20136.
SMRi P20136. Positions 2-218.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P20136.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 395976.
KEGGi gga:395976.

Organism-specific databases

CTDi 2946.

Phylogenomic databases

HOVERGENi HBG106842.
KOi K00799.
PhylomeDBi P20136.

Miscellaneous databases

EvolutionaryTracei P20136.
NextBioi 20816041.

Family and domain databases

Gene3Di 1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProi IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR003081. GST_mu.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view ]
PRINTSi PR01267. GSTRNSFRASEM.
SUPFAMi SSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEi PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1991) [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(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-35.
    Tissue: Liver.
  3. Liu L.-F.
    Submitted (MAR-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(1998) [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(2000) [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: February 1, 1991
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 104 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

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