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Protein

Glutathione S-transferase Mu 3

Gene

GSTM3

Organism
Homo sapiens (Human)
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. May govern uptake and detoxification of both endogenous compounds and xenobiotics at the testis and brain blood barriers.1 Publication

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.1 Publication

Kineticsi

  1. KM=1.1 mM for 1-chloro-2,4-dinitrobenzene1 Publication
  2. KM=0.084 mM for glutathione1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei120 – 1201SubstrateBy similarity

GO - Molecular functioni

  1. enzyme binding Source: BHF-UCL
  2. glutathione binding Source: BHF-UCL
  3. glutathione transferase activity Source: UniProtKB
  4. identical protein binding Source: IntAct
  5. protein homodimerization activity Source: BHF-UCL

GO - Biological processi

  1. cellular detoxification of nitrogen compound Source: BHF-UCL
  2. establishment of blood-nerve barrier Source: ProtInc
  3. glutathione derivative biosynthetic process Source: Reactome
  4. glutathione metabolic process Source: UniProtKB
  5. nitrobenzene metabolic process Source: BHF-UCL
  6. response to estrogen Source: UniProtKB
  7. small molecule metabolic process Source: Reactome
  8. xenobiotic catabolic process Source: BHF-UCL
  9. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

ReactomeiREACT_6926. Glutathione conjugation.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:GSTM3
Synonyms:GST5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:4635. GSTM3.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProtKB
  4. nucleus Source: UniProtKB
  5. sperm fibrous sheath Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi120 – 1201Y → A: No effect. 1 Publication
Mutagenesisi120 – 1201Y → F: Strongly increased catalytic activity. 1 Publication
Mutagenesisi213 – 2131N → F: Strongly increased catalytic activity. 1 Publication
Mutagenesisi213 – 2131N → G: No effect. 1 Publication

Organism-specific databases

PharmGKBiPA29024.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 225225Glutathione S-transferase Mu 3PRO_0000185822Add
BLAST

Post-translational modificationi

The N-terminus is blocked.

Proteomic databases

PaxDbiP21266.
PeptideAtlasiP21266.
PRIDEiP21266.

2D gel databases

OGPiP21266.
REPRODUCTION-2DPAGEIPI00246975.

PTM databases

PhosphoSiteiP21266.

Expressioni

Tissue specificityi

Testis and brain.

Gene expression databases

BgeeiP21266.
CleanExiHS_GSTM3.
ExpressionAtlasiP21266. baseline and differential.
GenevestigatoriP21266.

Organism-specific databases

HPAiCAB017130.
CAB040583.
HPA035190.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-350350,EBI-350350

Protein-protein interaction databases

BioGridi109202. 22 interactions.
IntActiP21266. 3 interactions.
STRINGi9606.ENSP00000256594.

Structurei

Secondary structure

1
225
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 159Combined sources
Helixi16 – 183Combined sources
Helixi19 – 279Combined sources
Beta strandi32 – 376Combined sources
Beta strandi42 – 443Combined sources
Helixi48 – 547Combined sources
Beta strandi64 – 696Combined sources
Beta strandi72 – 765Combined sources
Helixi77 – 8711Combined sources
Helixi95 – 12026Combined sources
Helixi124 – 14623Combined sources
Beta strandi154 – 1563Combined sources
Helixi159 – 17416Combined sources
Helixi176 – 1794Combined sources
Helixi183 – 19311Combined sources
Helixi196 – 2038Combined sources
Helixi205 – 2084Combined sources
Beta strandi211 – 2133Combined sources
Beta strandi217 – 2204Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GTUX-ray2.80B/D2-225[»]
ProteinModelPortaliP21266.
SMRiP21266. Positions 2-225.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21266.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 9288GST N-terminalAdd
BLAST
Domaini94 – 212119GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni11 – 122Glutathione bindingBy similarity
Regioni50 – 545Glutathione bindingBy similarity
Regioni63 – 642Glutathione bindingBy similarity
Regioni76 – 772Glutathione 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.
HOVERGENiHBG106842.
InParanoidiP21266.
KOiK00799.
OMAiMSCESSM.
OrthoDBiEOG7KH9M3.
PhylomeDBiP21266.
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.

P21266-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSCESSMVLG YWDIRGLAHA IRLLLEFTDT SYEEKRYTCG EAPDYDRSQW
60 70 80 90 100
LDVKFKLDLD FPNLPYLLDG KNKITQSNAI LRYIARKHNM CGETEEEKIR
110 120 130 140 150
VDIIENQVMD FRTQLIRLCY SSDHEKLKPQ YLEELPGQLK QFSMFLGKFS
160 170 180 190 200
WFAGEKLTFV DFLTYDILDQ NRIFDPKCLD EFPNLKAFMC RFEALEKIAA
210 220
YLQSDQFCKM PINNKMAQWG NKPVC
Length:225
Mass (Da):26,560
Last modified:January 23, 2007 - v3
Checksum:i79093161ECEF5396
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti147 – 1471G → W in AAA60964. (PubMed:2345169)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti224 – 2241V → I.1 Publication
Corresponds to variant rs7483 [ dbSNP | Ensembl ].
VAR_014498

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS812.1.
PIRiA35295.
RefSeqiNP_000840.2. NM_000849.4.
UniGeneiHs.2006.

Genome annotation databases

EnsembliENST00000256594; ENSP00000256594; ENSG00000134202.
ENST00000361066; ENSP00000354357; ENSG00000134202.
GeneIDi2947.
KEGGihsa:2947.
UCSCiuc001dyo.2. human.

Polymorphism databases

DMDMi21264423.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS812.1.
PIRiA35295.
RefSeqiNP_000840.2. NM_000849.4.
UniGeneiHs.2006.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GTUX-ray2.80B/D2-225[»]
ProteinModelPortaliP21266.
SMRiP21266. Positions 2-225.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109202. 22 interactions.
IntActiP21266. 3 interactions.
STRINGi9606.ENSP00000256594.

Chemistry

ChEMBLiCHEMBL2242.
DrugBankiDB00143. Glutathione.
DB00163. Vitamin E.

PTM databases

PhosphoSiteiP21266.

Polymorphism databases

DMDMi21264423.

2D gel databases

OGPiP21266.
REPRODUCTION-2DPAGEIPI00246975.

Proteomic databases

PaxDbiP21266.
PeptideAtlasiP21266.
PRIDEiP21266.

Protocols and materials databases

DNASUi2947.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000256594; ENSP00000256594; ENSG00000134202.
ENST00000361066; ENSP00000354357; ENSG00000134202.
GeneIDi2947.
KEGGihsa:2947.
UCSCiuc001dyo.2. human.

Organism-specific databases

CTDi2947.
GeneCardsiGC01M110276.
HGNCiHGNC:4635. GSTM3.
HPAiCAB017130.
CAB040583.
HPA035190.
MIMi138390. gene.
neXtProtiNX_P21266.
PharmGKBiPA29024.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG300089.
HOVERGENiHBG106842.
InParanoidiP21266.
KOiK00799.
OMAiMSCESSM.
OrthoDBiEOG7KH9M3.
PhylomeDBiP21266.
TreeFamiTF353040.

Enzyme and pathway databases

ReactomeiREACT_6926. Glutathione conjugation.

Miscellaneous databases

EvolutionaryTraceiP21266.
GeneWikiiGSTM3.
GenomeRNAii2947.
NextBioi11678.
PROiP21266.
SOURCEiSearch...

Gene expression databases

BgeeiP21266.
CleanExiHS_GSTM3.
ExpressionAtlasiP21266. baseline and differential.
GenevestigatoriP21266.

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 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. 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.

Entry informationi

Entry nameiGSTM3_HUMAN
AccessioniPrimary (citable) accession number: P21266
Secondary accession number(s): O60550, Q96HA3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 166 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.