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Protein

Glutathione S-transferase Mu 2

Gene

GSTM2

Organism
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Has activity toward aflatoxin B(1)-8,9-epoxide (AFBO).

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei50GlutathioneBy similarity1
Binding sitei116SubstrateBy similarity1
Sitei210Important for substrate specificityBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase Mu 2 (EC:2.5.1.18)
Alternative name(s):
GST class-mu 2
GSTM2-2
Gene namesi
Name:GSTM2
OrganismiMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Taxonomic identifieri9541 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001858192 – 218Glutathione S-transferase Mu 2Add BLAST217

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei27PhosphoserineBy similarity1
Modified residuei44PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ9TSM4.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9TSM4.
ModBaseiSearch...
MobiDBiSearch...

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 bindingBy similarity2
Regioni43 – 46Glutathione bindingBy similarity4
Regioni59 – 60Glutathione bindingBy similarity2
Regioni72 – 73Glutathione bindingBy similarity2

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.
KOiK00799.

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.

Q9TSM4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPMTLGYWNI RGLAHSIRLL LEYTGSSYEE KKYTMGDAPD YDRSQWLNEK
60 70 80 90 100
FKLGLDFPNL PYLIDGTHKI TQSNAILRYI ARKHNLCGET EKEKIREDIL
110 120 130 140 150
ENQLMDNRMQ LARLCYDPDF EKLKPEYLEG LPEMLKLYSQ FLGKQPWFLG
160 170 180 190 200
DKITFVDFIA YDVLERNQVF EPSCLDAFPN LKDFISRFEG LEKISAYMKS
210
SRFLPRPVFT KMAVWGNK
Length:218
Mass (Da):25,709
Last modified:January 23, 2007 - v3
Checksum:iF2E509C3949F9051
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF200710 mRNA. Translation: AAF08540.1.
RefSeqiNP_001274584.1. NM_001287655.1.
UniGeneiMfa.5908.

Genome annotation databases

GeneIDi102146720.
KEGGimcf:102146720.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF200710 mRNA. Translation: AAF08540.1.
RefSeqiNP_001274584.1. NM_001287655.1.
UniGeneiMfa.5908.

3D structure databases

ProteinModelPortaliQ9TSM4.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ9TSM4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi102146720.
KEGGimcf:102146720.

Organism-specific databases

CTDi2946.

Phylogenomic databases

HOVERGENiHBG106842.
KOiK00799.

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_MACFA
AccessioniPrimary (citable) accession number: Q9TSM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 23, 2007
Last modified: October 5, 2016
This is version 72 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. 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.