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P28161 (GSTM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase Mu 2

EC=2.5.1.18
Alternative name(s):
GST class-mu 2
GSTM2-2
Gene names
Name:GSTM2
Synonyms:GST4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length218 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Ref.10

Catalytic activity

RX + glutathione = HX + R-S-glutathione. Ref.10

Subunit structure

Homodimer. Ref.9

Subcellular location

Cytoplasm.

Tissue specificity

Muscle.

Sequence similarities

Belongs to the GST superfamily. Mu family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   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.1Ref.6. Source: BHF-UCL

cellular response to caffeine

Inferred from direct assay PubMed 22406107. Source: BHF-UCL

glutathione derivative biosynthetic process

Traceable author statement. Source: Reactome

glutathione metabolic process

Inferred from direct assay Ref.10. Source: UniProtKB

negative regulation of ryanodine-sensitive calcium-release channel activity

Inferred from direct assay PubMed 17023043PubMed 22406107. Source: BHF-UCL

nitrobenzene metabolic process

Inferred from direct assay Ref.1Ref.6. Source: BHF-UCL

positive regulation of ryanodine-sensitive calcium-release channel activity

Inferred from direct assay PubMed 17023043. Source: BHF-UCL

regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion

Inferred by curator PubMed 17023043PubMed 22406107. Source: BHF-UCL

regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum

Inferred from direct assay PubMed 17023043. Source: BHF-UCL

regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion

Inferred by curator PubMed 17023043. Source: BHF-UCL

relaxation of cardiac muscle

Traceable author statement PubMed 21323602. Source: BHF-UCL

small molecule metabolic process

Traceable author statement. Source: Reactome

xenobiotic catabolic process

Inferred from direct assay Ref.10. Source: UniProtKB

xenobiotic metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay Ref.1Ref.6. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

sarcoplasmic reticulum

Inferred from direct assay PubMed 22406107. Source: BHF-UCL

   Molecular_functionenzyme binding

Inferred from physical interaction Ref.6. Source: BHF-UCL

glutathione binding

Inferred from direct assay Ref.1Ref.6. Source: BHF-UCL

glutathione transferase activity

Inferred from direct assay Ref.10. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction Ref.6. Source: BHF-UCL

receptor binding

Inferred from physical interaction PubMed 22406107. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P28161-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P28161-2)

The sequence of this isoform differs from the canonical sequence as follows:
     190-218: GLEKISAYMKSSRFLPRPVFTKMAVWGNK → HS
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 218217Glutathione S-transferase Mu 2
PRO_0000185818

Regions

Domain2 – 8887GST N-terminal
Domain90 – 208119GST C-terminal
Region7 – 82Glutathione binding
Region46 – 505Glutathione binding
Region59 – 602Glutathione binding
Region72 – 732Glutathione binding

Sites

Binding site1161Substrate By similarity
Site2101Important for substrate specificity

Natural variations

Alternative sequence190 – 21829GLEKI…VWGNK → HS in isoform 2.
VSP_045614
Natural variant1731S → N.
Corresponds to variant rs2229050 [ dbSNP | Ensembl ].
VAR_049486

Experimental info

Mutagenesis2101T → C, F, H, I, K, L, R, Y or W: Reduced enzyme activity. Ref.10
Sequence conflict21P → S in AAV38750. Ref.3
Sequence conflict91N → D in AAV38750. Ref.3
Sequence conflict511F → L in BAG61446. Ref.2

Secondary structure

..................................... 218
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 15203709D4A63789

FASTA21825,745
        10         20         30         40         50         60 
MPMTLGYWNI RGLAHSIRLL LEYTDSSYEE KKYTMGDAPD YDRSQWLNEK FKLGLDFPNL 

        70         80         90        100        110        120 
PYLIDGTHKI TQSNAILRYI ARKHNLCGES EKEQIREDIL ENQFMDSRMQ LAKLCYDPDF 

       130        140        150        160        170        180 
EKLKPEYLQA LPEMLKLYSQ FLGKQPWFLG DKITFVDFIA YDVLERNQVF EPSCLDAFPN 

       190        200        210 
LKDFISRFEG LEKISAYMKS SRFLPRPVFT KMAVWGNK 

« Hide

Isoform 2 [UniParc].

Checksum: 9267243C014F878F
Show »

FASTA19122,644

References

« Hide 'large scale' references
[1]"Cloning, expression, and characterization of a class-mu glutathione transferase from human muscle, the product of the GST4 locus."
Vorachek W.R., Pearson W.R., Rule G.S.
Proc. Natl. Acad. Sci. U.S.A. 88:4443-4447(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Muscle.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORM 1).
Tissue: Brain.
[6]"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.
[7]Lubec G., Vishwanath V.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 53-69 AND 153-182, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[8]"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].
[9]"Crystal structure of human class mu glutathione transferase GSTM2-2. Effects of lattice packing on conformational heterogeneity."
Raghunathan S., Chandross R.J., Kretsinger R.H., Allison T.J., Penington C.J., Rule G.S.
J. Mol. Biol. 238:815-832(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, SUBUNIT.
[10]"Alternative mutations of a positively selected residue elicit gain or loss of functionalities in enzyme evolution."
Norrgard M.A., Ivarsson Y., Tars K., Mannervik B.
Proc. Natl. Acad. Sci. U.S.A. 103:4876-4881(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, FUNCTION, MUTAGENESIS OF THR-210, CATALYTIC ACTIVITY.
[11]"Structural basis for the binding of the anticancer compound 6-(7-nitro-2,1,3-benzoxadiazol-4-ylthio)hexanol to human glutathione s-transferases."
Federici L., Lo Sterzo C., Pezzola S., Di Matteo A., Scaloni F., Federici G., Caccuri A.M.
Cancer Res. 69:8025-8034(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NBDHEX.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M63509 mRNA. Translation: AAA60963.1.
AK299482 mRNA. Translation: BAG61446.1.
BT019947 mRNA. Translation: AAV38750.1.
AC000031 Genomic DNA. No translation available.
AC000032 Genomic DNA. No translation available.
BC105038 mRNA. Translation: AAI05039.1.
BC105066 mRNA. Translation: AAI05067.1.
CCDSCCDS44192.1. [P28161-2]
CCDS808.1. [P28161-1]
PIRA39375.
RefSeqNP_000839.1. NM_000848.3. [P28161-1]
NP_001135840.1. NM_001142368.1. [P28161-2]
UniGeneHs.279837.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HNAX-ray1.85A2-218[»]
1HNBX-ray3.50A/B2-218[»]
1HNCX-ray3.00A/B/C/D2-218[»]
1XW5X-ray1.80A/B2-218[»]
1YKCX-ray2.10A/B2-218[»]
2AB6X-ray2.50A/B/C/D2-218[»]
2C4JX-ray1.35A/B/C/D2-218[»]
2GTUX-ray2.55A/B2-218[»]
3GTUX-ray2.80A/C2-218[»]
3GURX-ray2.50A/B/C/D2-218[»]
ProteinModelPortalP28161.
SMRP28161. Positions 2-218.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109201. 3 interactions.
DIPDIP-129N.
STRING9606.ENSP00000241337.

Chemistry

BindingDBP28161.
ChEMBLCHEMBL4589.
DrugBankDB00143. Glutathione.

PTM databases

PhosphoSiteP28161.

Polymorphism databases

DMDM232204.

2D gel databases

OGPP28161.
REPRODUCTION-2DPAGEP28161.

Proteomic databases

MaxQBP28161.
PaxDbP28161.
PRIDEP28161.

Protocols and materials databases

DNASU2946.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000241337; ENSP00000241337; ENSG00000213366. [P28161-1]
ENST00000442650; ENSP00000416883; ENSG00000213366. [P28161-2]
ENST00000460717; ENSP00000435910; ENSG00000213366. [P28161-2]
GeneID2946.
KEGGhsa:2946.
UCSCuc001dyi.3. human. [P28161-1]
uc010ovt.2. human.

Organism-specific databases

CTD2946.
GeneCardsGC01P110210.
HGNCHGNC:4634. GSTM2.
HPACAB040547.
MIM138380. gene.
neXtProtNX_P28161.
PharmGKBPA29023.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG300089.
HOGENOMHOG000115735.
HOVERGENHBG106842.
KOK00799.
OMAWASGMAF.
PhylomeDBP28161.
TreeFamTF353040.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
SABIO-RKP28161.

Gene expression databases

ArrayExpressP28161.
BgeeP28161.
CleanExHS_GSTM2.
GenevestigatorP28161.

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

ChiTaRSGSTM2. human.
EvolutionaryTraceP28161.
GeneWikiGSTM2.
GenomeRNAi2946.
NextBio11674.
PROP28161.
SOURCESearch...

Entry information

Entry nameGSTM2_HUMAN
AccessionPrimary (citable) accession number: P28161
Secondary accession number(s): B4DRY4 expand/collapse secondary AC list , E9PEM9, Q2M318, Q5TZY5, Q8WWE1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 150 of the entry and version 2 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