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P21266 (GSTM3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase Mu 3

EC=2.5.1.18
Alternative name(s):
GST class-mu 3
GSTM3-3
Short name=hGSTM3-3
Gene names
Name:GSTM3
Synonyms:GST5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length225 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. May govern uptake and detoxification of both endogenous compounds and xenobiotics at the testis and brain blood barriers. Ref.8

Catalytic activity

RX + glutathione = HX + R-S-glutathione. Ref.8

Subunit structure

Homodimer. Ref.8

Subcellular location

Cytoplasm.

Tissue specificity

Testis and brain.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the GST superfamily. Mu family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Biophysicochemical properties

Kinetic parameters:

KM=1.1 mM for 1-chloro-2,4-dinitrobenzene Ref.8

KM=0.084 mM for glutathione

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   Molecular functionTransferase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular detoxification of nitrogen compound

Inferred from direct assay Ref.5. Source: BHF-UCL

establishment of blood-nerve barrier

Traceable author statement Ref.1. Source: ProtInc

glutathione derivative biosynthetic process

Traceable author statement. Source: Reactome

glutathione metabolic process

Inferred from direct assay Ref.8. Source: UniProtKB

nitrobenzene metabolic process

Inferred from direct assay Ref.5. Source: BHF-UCL

response to estrogen

Inferred from expression pattern PubMed 10037815. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

xenobiotic catabolic process

Inferred from direct assay Ref.5. Source: BHF-UCL

xenobiotic metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay Ref.5. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

   Molecular_functionenzyme binding

Inferred from physical interaction Ref.5. Source: BHF-UCL

glutathione binding

Inferred from direct assay Ref.5. Source: BHF-UCL

glutathione transferase activity

Inferred from direct assay Ref.8. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 16189514PubMed 19060904PubMed 21516116. Source: IntAct

protein homodimerization activity

Inferred from physical interaction Ref.5. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself4EBI-350350,EBI-350350

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 225225Glutathione S-transferase Mu 3
PRO_0000185822

Regions

Domain5 – 9288GST N-terminal
Domain94 – 212119GST C-terminal
Region11 – 122Glutathione binding By similarity
Region50 – 545Glutathione binding By similarity
Region63 – 642Glutathione binding By similarity
Region76 – 772Glutathione binding By similarity

Sites

Binding site1201Substrate By similarity

Natural variations

Natural variant2241V → I. Ref.4
Corresponds to variant rs7483 [ dbSNP | Ensembl ].
VAR_014498

Experimental info

Mutagenesis1201Y → A: No effect. Ref.8
Mutagenesis1201Y → F: Strongly increased catalytic activity. Ref.8
Mutagenesis2131N → F: Strongly increased catalytic activity. Ref.8
Mutagenesis2131N → G: No effect. Ref.8
Sequence conflict1471G → W in AAA60964. Ref.1

Secondary structure

.................................... 225
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P21266 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 79093161ECEF5396

FASTA22526,560
        10         20         30         40         50         60 
MSCESSMVLG YWDIRGLAHA IRLLLEFTDT SYEEKRYTCG EAPDYDRSQW LDVKFKLDLD 

        70         80         90        100        110        120 
FPNLPYLLDG KNKITQSNAI LRYIARKHNM CGETEEEKIR VDIIENQVMD FRTQLIRLCY 

       130        140        150        160        170        180 
SSDHEKLKPQ YLEELPGQLK QFSMFLGKFS WFAGEKLTFV DFLTYDILDQ NRIFDPKCLD 

       190        200        210        220 
EFPNLKAFMC RFEALEKIAA YLQSDQFCKM PINNKMAQWG NKPVC 

« Hide

References

« Hide 'large scale' references
[1]"A distinct human testis and brain mu-class glutathione S-transferase. Molecular cloning and characterization of a form present even in individuals lacking hepatic type mu isoenzymes."
Campbell E., Takahashi Y., Abramovitz M., Peretz M., Listowsky I.
J. Biol. Chem. 265:9188-9193(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Brain and Testis.
[2]"Distinctive structure of the human GSTM3 gene-inverted orientation relative to the mu class glutathione transferase gene cluster."
Patskovsky Y.V., Huang M.Q., Takayama T., Listowsky I., Pearson W.R.
Arch. Biochem. Biophys. 361:85-93(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-224.
Tissue: Brain and Uterus.
[5]"Molecular cloning and heterologous expression of an alternatively spliced human Mu class glutathione S-transferase transcript."
Ross V.L., Board P.G.
Biochem. J. 294:373-380(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF N-TERMINUS.
Tissue: Testis.
[6]"Human Mu-class glutathione S-transferases present in liver, skeletal muscle and testicular tissue."
Hussey A.J., Hayes J.D.
Biochim. Biophys. Acta 1203:131-141(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 190-209.
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"An asparagine-phenylalanine substitution accounts for catalytic differences between hGSTM3-3 and other human class mu glutathione S-transferases."
Patskovsky Y.V., Patskovska L.N., Listowsky I.
Biochemistry 38:16187-16194(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF TYR-120 AND ASN-213.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05459 mRNA. Translation: AAA60964.1.
AF043105 Genomic DNA. Translation: AAC17866.1.
BT019945 mRNA. Translation: AAV38748.1.
BC000088 mRNA. Translation: AAH00088.1.
BC008790 mRNA. Translation: AAH08790.1.
PIRA35295.
RefSeqNP_000840.2. NM_000849.4.
UniGeneHs.2006.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3GTUX-ray2.80B/D2-225[»]
ProteinModelPortalP21266.
SMRP21266. Positions 2-225.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109202. 9 interactions.
IntActP21266. 3 interactions.
STRING9606.ENSP00000256594.

Chemistry

ChEMBLCHEMBL2242.
DrugBankDB00143. Glutathione.

PTM databases

PhosphoSiteP21266.

Polymorphism databases

DMDM21264423.

2D gel databases

OGPP21266.
REPRODUCTION-2DPAGEIPI00246975.

Proteomic databases

PaxDbP21266.
PeptideAtlasP21266.
PRIDEP21266.

Protocols and materials databases

DNASU2947.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000256594; ENSP00000256594; ENSG00000134202.
ENST00000361066; ENSP00000354357; ENSG00000134202.
ENST00000540225; ENSP00000444978; ENSG00000134202.
GeneID2947.
KEGGhsa:2947.
UCSCuc001dyo.2. human.

Organism-specific databases

CTD2947.
GeneCardsGC01M110276.
HGNCHGNC:4635. GSTM3.
HPACAB017130.
CAB040583.
HPA035190.
MIM138390. gene.
neXtProtNX_P21266.
PharmGKBPA29024.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG300089.
HOVERGENHBG106842.
InParanoidP21266.
KOK00799.
OMAMSCESSM.
OrthoDBEOG7KH9M3.
PhylomeDBP21266.
TreeFamTF353040.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP21266.
BgeeP21266.
CleanExHS_GSTM3.
GenevestigatorP21266.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR003081. GST_mu.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSPR01267. GSTRNSFRASEM.
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP21266.
GeneWikiGSTM3.
GenomeRNAi2947.
NextBio11678.
PROP21266.
SOURCESearch...

Entry information

Entry nameGSTM3_HUMAN
AccessionPrimary (citable) accession number: P21266
Secondary accession number(s): O60550, Q96HA3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 158 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM