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P21266

- GSTM3_HUMAN

UniProt

P21266 - GSTM3_HUMAN

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Protein
Glutathione S-transferase Mu 3
Gene
GSTM3, GST5
Organism
Homo sapiens (Human)
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. 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 glutathione

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei120 – 1201Substrate By 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: UniProt
  4. nucleus Source: UniProt
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 3
PRO_0000185822Add
BLAST

Post-translational modificationi

The N-terminus is blocked.

Proteomic databases

MaxQBiP21266.
PaxDbiP21266.
PeptideAtlasiP21266.
PRIDEiP21266.

2D gel databases

OGPiP21266.
REPRODUCTION-2DPAGEIPI00246975.

PTM databases

PhosphoSiteiP21266.

Expressioni

Tissue specificityi

Testis and brain.

Gene expression databases

ArrayExpressiP21266.
BgeeiP21266.
CleanExiHS_GSTM3.
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. 9 interactions.
IntActiP21266. 3 interactions.
STRINGi9606.ENSP00000256594.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GTUX-ray2.80B/D2-225[»]
ProteinModelPortaliP21266.
SMRiP21266. Positions 2-225.

Miscellaneous databases

EvolutionaryTraceiP21266.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni11 – 122Glutathione binding By similarity
Regioni50 – 545Glutathione binding By similarity
Regioni63 – 642Glutathione binding By similarity
Regioni76 – 772Glutathione binding By similarity

Sequence similaritiesi

Belongs to the GST superfamily. Mu family.

Phylogenomic databases

eggNOGiNOG300089.
HOVERGENiHBG106842.
InParanoidiP21266.
KOiK00799.
OMAiCYNSDHE.
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

MSCESSMVLG YWDIRGLAHA IRLLLEFTDT SYEEKRYTCG EAPDYDRSQW    50
LDVKFKLDLD FPNLPYLLDG KNKITQSNAI LRYIARKHNM CGETEEEKIR 100
VDIIENQVMD FRTQLIRLCY SSDHEKLKPQ YLEELPGQLK QFSMFLGKFS 150
WFAGEKLTFV DFLTYDILDQ NRIFDPKCLD EFPNLKAFMC RFEALEKIAA 200
YLQSDQFCKM PINNKMAQWG NKPVC 225
Length:225
Mass (Da):26,560
Last modified:January 23, 2007 - v3
Checksum:i79093161ECEF5396
GO

Natural variant

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti147 – 1471G → W in AAA60964. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
ENST00000540225; ENSP00000444978; ENSG00000134202.
GeneIDi2947.
KEGGihsa:2947.
UCSCiuc001dyo.2. human.

Polymorphism databases

DMDMi21264423.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS812.1.
PIRi A35295.
RefSeqi NP_000840.2. NM_000849.4.
UniGenei Hs.2006.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3GTU X-ray 2.80 B/D 2-225 [» ]
ProteinModelPortali P21266.
SMRi P21266. Positions 2-225.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109202. 9 interactions.
IntActi P21266. 3 interactions.
STRINGi 9606.ENSP00000256594.

Chemistry

ChEMBLi CHEMBL2242.
DrugBanki DB00143. Glutathione.

PTM databases

PhosphoSitei P21266.

Polymorphism databases

DMDMi 21264423.

2D gel databases

OGPi P21266.
REPRODUCTION-2DPAGE IPI00246975.

Proteomic databases

MaxQBi P21266.
PaxDbi P21266.
PeptideAtlasi P21266.
PRIDEi P21266.

Protocols and materials databases

DNASUi 2947.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000256594 ; ENSP00000256594 ; ENSG00000134202 .
ENST00000361066 ; ENSP00000354357 ; ENSG00000134202 .
ENST00000540225 ; ENSP00000444978 ; ENSG00000134202 .
GeneIDi 2947.
KEGGi hsa:2947.
UCSCi uc001dyo.2. human.

Organism-specific databases

CTDi 2947.
GeneCardsi GC01M110276.
HGNCi HGNC:4635. GSTM3.
HPAi CAB017130.
CAB040583.
HPA035190.
MIMi 138390. gene.
neXtProti NX_P21266.
PharmGKBi PA29024.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG300089.
HOVERGENi HBG106842.
InParanoidi P21266.
KOi K00799.
OMAi CYNSDHE.
OrthoDBi EOG7KH9M3.
PhylomeDBi P21266.
TreeFami TF353040.

Enzyme and pathway databases

Reactomei REACT_6926. Glutathione conjugation.

Miscellaneous databases

EvolutionaryTracei P21266.
GeneWikii GSTM3.
GenomeRNAii 2947.
NextBioi 11678.
PROi P21266.
SOURCEi Search...

Gene expression databases

ArrayExpressi P21266.
Bgeei P21266.
CleanExi HS_GSTM3.
Genevestigatori P21266.

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

« 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: September 3, 2014
This is version 162 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

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