GSTM2_HUMAN
ID GSTM2_HUMAN Reviewed; 218 AA.
AC P28161; B4DRY4; E9PEM9; Q2M318; Q5TZY5; Q8WWE1;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Glutathione S-transferase Mu 2 {ECO:0000305};
DE EC=2.5.1.18 {ECO:0000269|PubMed:16549767};
DE AltName: Full=GST class-mu 2;
DE AltName: Full=GSTM2-2;
GN Name=GSTM2 {ECO:0000312|HGNC:HGNC:4634}; Synonyms=GST4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
RX PubMed=2034681; DOI=10.1073/pnas.88.10.4443;
RA Vorachek W.R., Pearson W.R., Rule G.S.;
RT "Cloning, expression, and characterization of a class-mu glutathione
RT transferase from human muscle, the product of the GST4 locus.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:4443-4447(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF N-TERMINUS.
RC TISSUE=Testis;
RX PubMed=8373352; DOI=10.1042/bj2940373;
RA Ross V.L., Board P.G.;
RT "Molecular cloning and heterologous expression of an alternatively spliced
RT human Mu class glutathione S-transferase transcript.";
RL Biochem. J. 294:373-380(1993).
RN [7]
RP PROTEIN SEQUENCE OF 53-69 AND 153-182, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21046276; DOI=10.1007/s11745-010-3485-1;
RA Brunnstroem A., Hamberg M., Griffiths W.J., Mannervik B., Claesson H.E.;
RT "Biosynthesis of 14,15-hepoxilins in human l1236 Hodgkin lymphoma cells and
RT eosinophils.";
RL Lipids 46:69-79(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, AND
RP SUBUNIT.
RX PubMed=8182750; DOI=10.1006/jmbi.1994.1336;
RA Raghunathan S., Chandross R.J., Kretsinger R.H., Allison T.J.,
RA Penington C.J., Rule G.S.;
RT "Crystal structure of human class mu glutathione transferase GSTM2-2.
RT Effects of lattice packing on conformational heterogeneity.";
RL J. Mol. Biol. 238:815-832(1994).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE ANALOG,
RP FUNCTION, MUTAGENESIS OF THR-210, AND CATALYTIC ACTIVITY.
RX PubMed=16549767; DOI=10.1073/pnas.0600849103;
RA Norrgard M.A., Ivarsson Y., Tars K., Mannervik B.;
RT "Alternative mutations of a positively selected residue elicit gain or loss
RT of functionalities in enzyme evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:4876-4881(2006).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE AND
RP NBDHEX.
RX PubMed=19808963; DOI=10.1158/0008-5472.can-09-1314;
RA Federici L., Lo Sterzo C., Pezzola S., Di Matteo A., Scaloni F.,
RA Federici G., Caccuri A.M.;
RT "Structural basis for the binding of the anticancer compound 6-(7-nitro-
RT 2,1,3-benzoxadiazol-4-ylthio)hexanol to human glutathione s-transferases.";
RL Cancer Res. 69:8025-8034(2009).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles. Participates in the
CC formation of novel hepoxilin regioisomers (PubMed:21046276).
CC {ECO:0000269|PubMed:16549767, ECO:0000269|PubMed:21046276}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC Evidence={ECO:0000269|PubMed:16549767};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438;
CC Evidence={ECO:0000305|PubMed:16549767};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11(S)-hydroxy-14(S),15(S)-epoxy-(5Z,8Z,12E)-eicosatrienoate +
CC glutathione = (11S,15S)-dihydroxy-14(R)-S-glutathionyl-(5Z,8Z,12E)-
CC eicosatrienoate; Xref=Rhea:RHEA:50260, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:132200, ChEBI:CHEBI:132201;
CC Evidence={ECO:0000269|PubMed:21046276};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50261;
CC Evidence={ECO:0000305|PubMed:21046276};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16549767,
CC ECO:0000269|PubMed:19808963, ECO:0000269|PubMed:8182750}.
CC -!- INTERACTION:
CC P28161; P46439: GSTM5; NbExp=6; IntAct=EBI-9023362, EBI-4312072;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P28161-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P28161-2; Sequence=VSP_045614;
CC -!- TISSUE SPECIFICITY: Muscle.
CC -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M63509; AAA60963.1; -; mRNA.
DR EMBL; AK299482; BAG61446.1; -; mRNA.
DR EMBL; BT019947; AAV38750.1; -; mRNA.
DR EMBL; AC000031; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC000032; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC105038; AAI05039.1; -; mRNA.
DR EMBL; BC105066; AAI05067.1; -; mRNA.
DR CCDS; CCDS44192.1; -. [P28161-2]
DR CCDS; CCDS808.1; -. [P28161-1]
DR PIR; A39375; A39375.
DR RefSeq; NP_000839.1; NM_000848.3. [P28161-1]
DR RefSeq; NP_001135840.1; NM_001142368.1. [P28161-2]
DR PDB; 1HNA; X-ray; 1.85 A; A=2-218.
DR PDB; 1HNB; X-ray; 3.50 A; A/B=2-218.
DR PDB; 1HNC; X-ray; 3.00 A; A/B/C/D=2-218.
DR PDB; 1XW5; X-ray; 1.80 A; A/B=2-218.
DR PDB; 1YKC; X-ray; 2.10 A; A/B=2-218.
DR PDB; 2AB6; X-ray; 2.50 A; A/B/C/D=2-218.
DR PDB; 2C4J; X-ray; 1.35 A; A/B/C/D=2-218.
DR PDB; 2GTU; X-ray; 2.55 A; A/B=2-218.
DR PDB; 3GTU; X-ray; 2.80 A; A/C=2-218.
DR PDB; 3GUR; X-ray; 2.50 A; A/B/C/D=2-218.
DR PDB; 5HWL; X-ray; 1.60 A; A/B=2-218.
DR PDBsum; 1HNA; -.
DR PDBsum; 1HNB; -.
DR PDBsum; 1HNC; -.
DR PDBsum; 1XW5; -.
DR PDBsum; 1YKC; -.
DR PDBsum; 2AB6; -.
DR PDBsum; 2C4J; -.
DR PDBsum; 2GTU; -.
DR PDBsum; 3GTU; -.
DR PDBsum; 3GUR; -.
DR PDBsum; 5HWL; -.
DR AlphaFoldDB; P28161; -.
DR BMRB; P28161; -.
DR SMR; P28161; -.
DR BioGRID; 109201; 12.
DR IntAct; P28161; 4.
DR STRING; 9606.ENSP00000241337; -.
DR BindingDB; P28161; -.
DR ChEMBL; CHEMBL4589; -.
DR DrugBank; DB00143; Glutathione.
DR DrugBank; DB03310; Glutathione disulfide.
DR DrugBank; DB02458; S-(2,4-dinitrophenyl)glutathione.
DR DrugBank; DB04701; S-Methyl glutathione.
DR SwissLipids; SLP:000001614; -.
DR GlyGen; P28161; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P28161; -.
DR PhosphoSitePlus; P28161; -.
DR BioMuta; GSTM2; -.
DR DMDM; 232204; -.
DR OGP; P28161; -.
DR REPRODUCTION-2DPAGE; P28161; -.
DR EPD; P28161; -.
DR jPOST; P28161; -.
DR MassIVE; P28161; -.
DR MaxQB; P28161; -.
DR PaxDb; P28161; -.
DR PeptideAtlas; P28161; -.
DR PRIDE; P28161; -.
DR ProteomicsDB; 19925; -.
DR ProteomicsDB; 54450; -. [P28161-1]
DR Antibodypedia; 20072; 247 antibodies from 31 providers.
DR CPTC; P28161; 3 antibodies.
DR DNASU; 2946; -.
DR Ensembl; ENST00000241337.9; ENSP00000241337.4; ENSG00000213366.13. [P28161-1]
DR Ensembl; ENST00000442650.5; ENSP00000416883.1; ENSG00000213366.13. [P28161-2]
DR Ensembl; ENST00000460717.7; ENSP00000435910.2; ENSG00000213366.13. [P28161-2]
DR GeneID; 2946; -.
DR KEGG; hsa:2946; -.
DR MANE-Select; ENST00000241337.9; ENSP00000241337.4; NM_000848.4; NP_000839.1.
DR UCSC; uc001dyj.4; human. [P28161-1]
DR CTD; 2946; -.
DR DisGeNET; 2946; -.
DR GeneCards; GSTM2; -.
DR HGNC; HGNC:4634; GSTM2.
DR HPA; ENSG00000213366; Low tissue specificity.
DR MIM; 138380; gene.
DR neXtProt; NX_P28161; -.
DR OpenTargets; ENSG00000213366; -.
DR PharmGKB; PA29023; -.
DR VEuPathDB; HostDB:ENSG00000213366; -.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00940000155416; -.
DR InParanoid; P28161; -.
DR OMA; NRLPEMM; -.
DR PhylomeDB; P28161; -.
DR TreeFam; TF353040; -.
DR BRENDA; 2.5.1.18; 2681.
DR PathwayCommons; P28161; -.
DR Reactome; R-HSA-156590; Glutathione conjugation.
DR SABIO-RK; P28161; -.
DR SignaLink; P28161; -.
DR BioGRID-ORCS; 2946; 12 hits in 1078 CRISPR screens.
DR ChiTaRS; GSTM2; human.
DR EvolutionaryTrace; P28161; -.
DR GeneWiki; GSTM2; -.
DR GenomeRNAi; 2946; -.
DR Pharos; P28161; Tchem.
DR PRO; PR:P28161; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P28161; protein.
DR Bgee; ENSG00000213366; Expressed in left ovary and 94 other tissues.
DR ExpressionAtlas; P28161; baseline and differential.
DR Genevisible; P28161; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:BHF-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0005504; F:fatty acid binding; IPI:BHF-UCL.
DR GO; GO:0043295; F:glutathione binding; IDA:BHF-UCL.
DR GO; GO:0004602; F:glutathione peroxidase activity; IDA:BHF-UCL.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
DR GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL.
DR GO; GO:0070458; P:cellular detoxification of nitrogen compound; IDA:BHF-UCL.
DR GO; GO:0071313; P:cellular response to caffeine; IDA:BHF-UCL.
DR GO; GO:0006749; P:glutathione metabolic process; IDA:UniProtKB.
DR GO; GO:0051122; P:hepoxilin biosynthetic process; IDA:UniProtKB.
DR GO; GO:0043651; P:linoleic acid metabolic process; IDA:BHF-UCL.
DR GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL.
DR GO; GO:0018916; P:nitrobenzene metabolic process; IDA:BHF-UCL.
DR GO; GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL.
DR GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; IC:BHF-UCL.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IDA:BHF-UCL.
DR GO; GO:0014809; P:regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion; IC:BHF-UCL.
DR GO; GO:0055119; P:relaxation of cardiac muscle; TAS:BHF-UCL.
DR GO; GO:0042178; P:xenobiotic catabolic process; IDA:UniProtKB.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR003081; GST_mu.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01267; GSTRNSFRASEM.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Lipid metabolism; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..218
FT /note="Glutathione S-transferase Mu 2"
FT /id="PRO_0000185818"
FT DOMAIN 2..88
FT /note="GST N-terminal"
FT DOMAIN 90..208
FT /note="GST C-terminal"
FT BINDING 7..8
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:16549767,
FT ECO:0000269|PubMed:19808963"
FT BINDING 43..46
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:16549767,
FT ECO:0000269|PubMed:19808963"
FT BINDING 50
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08010"
FT BINDING 59..60
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:16549767,
FT ECO:0000269|PubMed:19808963"
FT BINDING 72..73
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:16549767,
FT ECO:0000269|PubMed:19808963"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 210
FT /note="Important for substrate specificity"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08010"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08010"
FT VAR_SEQ 190..218
FT /note="GLEKISAYMKSSRFLPRPVFTKMAVWGNK -> HS (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_045614"
FT VARIANT 173
FT /note="S -> N (in dbSNP:rs2229050)"
FT /id="VAR_049486"
FT MUTAGEN 210
FT /note="T->C,F,H,I,K,L,R,Y,W: Reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:16549767"
FT CONFLICT 2
FT /note="P -> S (in Ref. 3; AAV38750)"
FT /evidence="ECO:0000305"
FT CONFLICT 9
FT /note="N -> D (in Ref. 3; AAV38750)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="F -> L (in Ref. 2; BAG61446)"
FT /evidence="ECO:0000305"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:2C4J"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:2C4J"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:2C4J"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:2C4J"
FT TURN 38..41
FT /evidence="ECO:0007829|PDB:2C4J"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:2C4J"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:2C4J"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:2C4J"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:2C4J"
FT HELIX 73..83
FT /evidence="ECO:0007829|PDB:2C4J"
FT HELIX 91..116
FT /evidence="ECO:0007829|PDB:2C4J"
FT HELIX 120..142
FT /evidence="ECO:0007829|PDB:2C4J"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:2C4J"
FT HELIX 155..170
FT /evidence="ECO:0007829|PDB:2C4J"
FT TURN 172..177
FT /evidence="ECO:0007829|PDB:2C4J"
FT HELIX 179..190
FT /evidence="ECO:0007829|PDB:2C4J"
FT HELIX 192..199
FT /evidence="ECO:0007829|PDB:2C4J"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:1XW5"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:1HNC"
FT TURN 208..212
FT /evidence="ECO:0007829|PDB:1HNA"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:2C4J"
SQ SEQUENCE 218 AA; 25745 MW; 15203709D4A63789 CRC64;
MPMTLGYWNI RGLAHSIRLL LEYTDSSYEE KKYTMGDAPD YDRSQWLNEK FKLGLDFPNL
PYLIDGTHKI TQSNAILRYI ARKHNLCGES EKEQIREDIL ENQFMDSRMQ LAKLCYDPDF
EKLKPEYLQA LPEMLKLYSQ FLGKQPWFLG DKITFVDFIA YDVLERNQVF EPSCLDAFPN
LKDFISRFEG LEKISAYMKS SRFLPRPVFT KMAVWGNK
