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Protein

Glutathione S-transferase Mu 1

Gene

GSTM1

Organism
Bos taurus (Bovine)
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. Protects against the thiol-mediated metal-catalysed oxidative inactivation of enzymes.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei116 – 1161SubstrateBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

ReactomeiREACT_322474. Glutathione conjugation.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase Mu 1 (EC:2.5.1.18)
Alternative name(s):
GST class-mu 1
GSTM1-1
Gene namesi
Name:GSTM1
Synonyms:GSTM
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Chromosome 3

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 218217Glutathione S-transferase Mu 1PRO_0000240625Add
BLAST

Proteomic databases

PaxDbiQ9N0V4.
PRIDEiQ9N0V4.

Expressioni

Gene expression databases

ExpressionAtlasiQ9N0V4. baseline.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000023627.

Structurei

3D structure databases

ProteinModelPortaliQ9N0V4.
SMRiQ9N0V4. Positions 1-218.
ModBaseiSearch...
MobiDBiSearch...

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 bindingBy similarity
Regioni46 – 505Glutathione bindingBy similarity
Regioni59 – 602Glutathione bindingBy similarity
Regioni72 – 732Glutathione bindingBy similarity

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

eggNOGiNOG300089.
GeneTreeiENSGT00550000074559.
HOGENOMiHOG000115735.
HOVERGENiHBG106842.
InParanoidiQ9N0V4.
KOiK00799.
OMAiRITESWA.
OrthoDBiEOG7KH9M3.
TreeFamiTF353040.

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.

Q9N0V4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPMILGYWDI RGLAHAIRLL LEYTDTNYEE RQYSVGDAPD YDRSQWLNEK
60 70 80 90 100
FKLGLDFPNL PYLIDGTHKL TQSNAILRYI ARKHNLCGET EEEMIRVDIL
110 120 130 140 150
ENQVMDVRLA MARICYSPDF EKLKPGFLKE IPEKIKLFSE FLGKRPWFAG
160 170 180 190 200
DKLTYVDFLV YDVLDMHRIF EPKCLDAFPN LKDFISRFEG LKKISAYMKS
210
SRFLPGPLFM KLAVWGNK
Length:218
Mass (Da):25,635
Last modified:January 23, 2007 - v3
Checksum:i3D02EA0F43C07B0A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC102050 mRNA. Translation: AAI02051.1.
AF249588 mRNA. Translation: AAF64308.1.
RefSeqiNP_787019.1. NM_175825.3.
UniGeneiBt.49673.

Genome annotation databases

EnsembliENSBTAT00000023627; ENSBTAP00000023627; ENSBTAG00000017765.
GeneIDi327709.
KEGGibta:327709.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC102050 mRNA. Translation: AAI02051.1.
AF249588 mRNA. Translation: AAF64308.1.
RefSeqiNP_787019.1. NM_175825.3.
UniGeneiBt.49673.

3D structure databases

ProteinModelPortaliQ9N0V4.
SMRiQ9N0V4. Positions 1-218.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000023627.

Proteomic databases

PaxDbiQ9N0V4.
PRIDEiQ9N0V4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000023627; ENSBTAP00000023627; ENSBTAG00000017765.
GeneIDi327709.
KEGGibta:327709.

Organism-specific databases

CTDi2944.

Phylogenomic databases

eggNOGiNOG300089.
GeneTreeiENSGT00550000074559.
HOGENOMiHOG000115735.
HOVERGENiHBG106842.
InParanoidiQ9N0V4.
KOiK00799.
OMAiRITESWA.
OrthoDBiEOG7KH9M3.
TreeFamiTF353040.

Enzyme and pathway databases

ReactomeiREACT_322474. Glutathione conjugation.

Miscellaneous databases

NextBioi20810173.

Gene expression databases

ExpressionAtlasiQ9N0V4. baseline.

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

« Hide 'large scale' publications
  1. "A lens glutathione S-transferase, class mu, with thiol-specific antioxidant activity."
    Jimenez-Asensio J., Garland D.
    Exp. Eye Res. 71:255-265(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT.
    Tissue: Lens.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Ileum.

Entry informationi

Entry nameiGSTM1_BOVIN
AccessioniPrimary (citable) accession number: Q9N0V4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 98 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.