Full text data of GSTK1
GSTK1
[Confidence: low (only semi-automatic identification from reviews)]
Glutathione S-transferase kappa 1; 2.5.1.18 (GST 13-13; GST class-kappa; GSTK1-1; hGSTK1; Glutathione S-transferase subunit 13)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Glutathione S-transferase kappa 1; 2.5.1.18 (GST 13-13; GST class-kappa; GSTK1-1; hGSTK1; Glutathione S-transferase subunit 13)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9Y2Q3
ID GSTK1_HUMAN Reviewed; 226 AA.
AC Q9Y2Q3; B4DIH1; B4DSY2; Q6P4H0; Q7Z520; Q9P1S4;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 123.
DE RecName: Full=Glutathione S-transferase kappa 1;
DE EC=2.5.1.18;
DE AltName: Full=GST 13-13;
DE AltName: Full=GST class-kappa;
DE AltName: Full=GSTK1-1;
DE Short=hGSTK1;
DE AltName: Full=Glutathione S-transferase subunit 13;
GN Name=GSTK1; ORFNames=HDCMD47P;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION.
RC TISSUE=Mammary gland;
RX PubMed=14709161; DOI=10.1042/BJ20031656;
RA Robinson A., Huttley G.A., Booth H.S., Board P.G.;
RT "Modelling and bioinformatics studies of the human kappa class
RT glutathione transferase predict a novel third glutathione transferase
RT family with homology to prokaryotic 2-hydroxychromene-2-carboxylate
RT (HCCA) isomerases.";
RL Biochem. J. 379:541-552(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=14742434; DOI=10.1074/jbc.M313357200;
RA Morel F., Rauch C., Petit E., Piton A., Theret N., Coles B.,
RA Guillouzo A.;
RT "Gene and protein characterization of the human glutathione S-
RT transferase kappa and evidence for a peroxisomal localization.";
RL J. Biol. Chem. 279:16246-16253(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Dendritic cell;
RA Zhao Z., Huang X., Li N., Zhu X., Cao X.;
RT "A novel gene from human dendritic cell.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Zhang M., Yu L., Zhou Y., Hu P.R., Xin Y.R., Zhao S.Y.;
RT "Cloning of a novel human cDNA homologous to rats rGSTK1-1 mRNA.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC TISSUE=Cerebellum, and Hippocampus;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Blood, Cervix, and Pancreas;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-71 AND LYS-169, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
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.,
RA Buerckstuemmer T., 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 [13]
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE,
RP AND SUBUNIT.
RX PubMed=16081649; DOI=10.1110/ps.051463905;
RA Li J., Xia Z., Ding J.;
RT "Thioredoxin-like domain of human kappa class glutathione transferase
RT reveals sequence homology and structure similarity to the theta class
RT enzyme.";
RL Protein Sci. 14:2361-2369(2005).
CC -!- FUNCTION: Significant glutathione conjugating activity is found
CC only with the model substrate, 1-chloro-2,4-dinitrobenzene (CDNB).
CC -!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Peroxisome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9Y2Q3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y2Q3-2; Sequence=VSP_040025;
CC Name=3;
CC IsoId=Q9Y2Q3-3; Sequence=VSP_040979;
CC Name=4;
CC IsoId=Q9Y2Q3-4; Sequence=VSP_040978;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the GST superfamily. Kappa family.
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DR EMBL; AY520571; AAS00610.1; -; mRNA.
DR EMBL; AY486465; AAS01180.1; -; Genomic_DNA.
DR EMBL; AF070657; AAD20963.1; -; mRNA.
DR EMBL; AF068287; AAF65506.1; -; mRNA.
DR EMBL; AF087849; AAP97160.1; -; mRNA.
DR EMBL; AL136938; CAB66872.1; -; mRNA.
DR EMBL; AK289570; BAF82259.1; -; mRNA.
DR EMBL; AK295592; BAG58483.1; -; mRNA.
DR EMBL; AK299968; BAG61794.1; -; mRNA.
DR EMBL; AC073342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471198; EAW51877.1; -; Genomic_DNA.
DR EMBL; BC001231; AAH01231.1; -; mRNA.
DR EMBL; BC050715; AAH50715.1; -; mRNA.
DR EMBL; BC063425; AAH63425.1; -; mRNA.
DR RefSeq; NP_001137151.1; NM_001143679.1.
DR RefSeq; NP_001137152.1; NM_001143680.1.
DR RefSeq; NP_001137153.1; NM_001143681.1.
DR RefSeq; NP_057001.1; NM_015917.2.
DR UniGene; Hs.390667; -.
DR PDB; 1YZX; X-ray; 1.93 A; A/B=1-226.
DR PDB; 3RPN; X-ray; 1.90 A; A/B/C/D/E/F=1-226.
DR PDB; 3RPP; X-ray; 1.80 A; A/B/C=1-226.
DR PDBsum; 1YZX; -.
DR PDBsum; 3RPN; -.
DR PDBsum; 3RPP; -.
DR ProteinModelPortal; Q9Y2Q3; -.
DR SMR; Q9Y2Q3; 2-221.
DR DIP; DIP-46924N; -.
DR IntAct; Q9Y2Q3; 7.
DR MINT; MINT-3084797; -.
DR STRING; 9606.ENSP00000367415; -.
DR BindingDB; Q9Y2Q3; -.
DR ChEMBL; CHEMBL4491; -.
DR DrugBank; DB00143; Glutathione.
DR PhosphoSite; Q9Y2Q3; -.
DR DMDM; 12643338; -.
DR PaxDb; Q9Y2Q3; -.
DR PRIDE; Q9Y2Q3; -.
DR DNASU; 373156; -.
DR Ensembl; ENST00000358406; ENSP00000351181; ENSG00000197448.
DR Ensembl; ENST00000409500; ENSP00000386944; ENSG00000197448.
DR Ensembl; ENST00000443571; ENSP00000415813; ENSG00000197448.
DR Ensembl; ENST00000479303; ENSP00000431049; ENSG00000197448.
DR GeneID; 373156; -.
DR KEGG; hsa:373156; -.
DR UCSC; uc003wci.3; human.
DR CTD; 373156; -.
DR GeneCards; GC07P142942; -.
DR HGNC; HGNC:16906; GSTK1.
DR HPA; HPA006311; -.
DR HPA; HPA022904; -.
DR MIM; 602321; gene.
DR neXtProt; NX_Q9Y2Q3; -.
DR PharmGKB; PA134948237; -.
DR eggNOG; NOG70325; -.
DR HOGENOM; HOG000219769; -.
DR HOVERGEN; HBG051852; -.
DR KO; K13299; -.
DR OMA; ELWRRIW; -.
DR PhylomeDB; Q9Y2Q3; -.
DR ChiTaRS; GSTK1; human.
DR EvolutionaryTrace; Q9Y2Q3; -.
DR GeneWiki; GSTK1; -.
DR GenomeRNAi; 373156; -.
DR NextBio; 100114; -.
DR PRO; PR:Q9Y2Q3; -.
DR ArrayExpress; Q9Y2Q3; -.
DR Bgee; Q9Y2Q3; -.
DR CleanEx; HS_GSTK1; -.
DR Genevestigator; Q9Y2Q3; -.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0004602; F:glutathione peroxidase activity; IDA:UniProtKB.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:Ensembl.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR InterPro; IPR014440; HCCAis_GSTk.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR Pfam; PF01323; DSBA; 1.
DR PIRSF; PIRSF006386; HCCAis_GSTk; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Peroxisome; Reference proteome; Transferase.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 226 Glutathione S-transferase kappa 1.
FT /FTId=PRO_0000185891.
FT REGION 16 18 Glutathione binding.
FT REGION 200 201 Glutathione binding.
FT BINDING 53 53 Glutathione.
FT BINDING 183 183 Glutathione; via amide nitrogen and
FT carbonyl oxygen.
FT MOD_RES 71 71 N6-acetyllysine.
FT MOD_RES 85 85 N6-acetyllysine (By similarity).
FT MOD_RES 116 116 N6-acetyllysine (By similarity).
FT MOD_RES 158 158 N6-acetyllysine (By similarity).
FT MOD_RES 165 165 N6-acetyllysine (By similarity).
FT MOD_RES 169 169 N6-acetyllysine.
FT VAR_SEQ 52 94 Missing (in isoform 4).
FT /FTId=VSP_040978.
FT VAR_SEQ 128 128 R -> RVSVGLWESSGRTLDDFLTFPRHVFRVMILPPPGGS
FT TVLPVTPLSPHRLPAVFSSSQ (in isoform 2).
FT /FTId=VSP_040025.
FT VAR_SEQ 129 140 Missing (in isoform 3).
FT /FTId=VSP_040979.
FT CONFLICT 51 51 S -> R (in Ref. 6; BAG61794).
FT CONFLICT 171 171 T -> A (in Ref. 6; BAG61794).
FT CONFLICT 179 179 G -> R (in Ref. 4; AAF65506).
FT CONFLICT 206 206 L -> V (in Ref. 5; AAP97160).
FT CONFLICT 220 220 P -> S (in Ref. 4; AAF65506).
FT STRAND 6 12
FT HELIX 17 29
FT TURN 30 32
FT STRAND 33 41
FT HELIX 44 47
FT STRAND 57 59
FT HELIX 61 77
FT HELIX 88 94
FT HELIX 97 109
FT HELIX 111 113
FT HELIX 114 126
FT HELIX 135 144
FT HELIX 149 156
FT TURN 157 160
FT HELIX 162 177
FT STRAND 181 183
FT STRAND 185 190
FT STRAND 193 201
FT HELIX 203 210
SQ SEQUENCE 226 AA; 25497 MW; D3FDAFD1533B58A4 CRC64;
MGPLPRTVEL FYDVLSPYSW LGFEILCRYQ NIWNINLQLR PSLITGIMKD SGNKPPGLLP
RKGLYMANDL KLLRHHLQIP IHFPKDFLSV MLEKGSLSAM RFLTAVNLEH PEMLEKASRE
LWMRVWSRNE DITEPQSILA AAEKAGMSAE QAQGLLEKIA TPKVKNQLKE TTEAACRYGA
FGLPITVAHV DGQTHMLFGS DRMELLAHLL GEKWMGPIPP AVNARL
//
ID GSTK1_HUMAN Reviewed; 226 AA.
AC Q9Y2Q3; B4DIH1; B4DSY2; Q6P4H0; Q7Z520; Q9P1S4;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 123.
DE RecName: Full=Glutathione S-transferase kappa 1;
DE EC=2.5.1.18;
DE AltName: Full=GST 13-13;
DE AltName: Full=GST class-kappa;
DE AltName: Full=GSTK1-1;
DE Short=hGSTK1;
DE AltName: Full=Glutathione S-transferase subunit 13;
GN Name=GSTK1; ORFNames=HDCMD47P;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION.
RC TISSUE=Mammary gland;
RX PubMed=14709161; DOI=10.1042/BJ20031656;
RA Robinson A., Huttley G.A., Booth H.S., Board P.G.;
RT "Modelling and bioinformatics studies of the human kappa class
RT glutathione transferase predict a novel third glutathione transferase
RT family with homology to prokaryotic 2-hydroxychromene-2-carboxylate
RT (HCCA) isomerases.";
RL Biochem. J. 379:541-552(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=14742434; DOI=10.1074/jbc.M313357200;
RA Morel F., Rauch C., Petit E., Piton A., Theret N., Coles B.,
RA Guillouzo A.;
RT "Gene and protein characterization of the human glutathione S-
RT transferase kappa and evidence for a peroxisomal localization.";
RL J. Biol. Chem. 279:16246-16253(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Dendritic cell;
RA Zhao Z., Huang X., Li N., Zhu X., Cao X.;
RT "A novel gene from human dendritic cell.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Zhang M., Yu L., Zhou Y., Hu P.R., Xin Y.R., Zhao S.Y.;
RT "Cloning of a novel human cDNA homologous to rats rGSTK1-1 mRNA.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC TISSUE=Cerebellum, and Hippocampus;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Blood, Cervix, and Pancreas;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-71 AND LYS-169, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
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.,
RA Buerckstuemmer T., 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 [13]
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE,
RP AND SUBUNIT.
RX PubMed=16081649; DOI=10.1110/ps.051463905;
RA Li J., Xia Z., Ding J.;
RT "Thioredoxin-like domain of human kappa class glutathione transferase
RT reveals sequence homology and structure similarity to the theta class
RT enzyme.";
RL Protein Sci. 14:2361-2369(2005).
CC -!- FUNCTION: Significant glutathione conjugating activity is found
CC only with the model substrate, 1-chloro-2,4-dinitrobenzene (CDNB).
CC -!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Peroxisome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9Y2Q3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y2Q3-2; Sequence=VSP_040025;
CC Name=3;
CC IsoId=Q9Y2Q3-3; Sequence=VSP_040979;
CC Name=4;
CC IsoId=Q9Y2Q3-4; Sequence=VSP_040978;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the GST superfamily. Kappa family.
CC -----------------------------------------------------------------------
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DR EMBL; AY520571; AAS00610.1; -; mRNA.
DR EMBL; AY486465; AAS01180.1; -; Genomic_DNA.
DR EMBL; AF070657; AAD20963.1; -; mRNA.
DR EMBL; AF068287; AAF65506.1; -; mRNA.
DR EMBL; AF087849; AAP97160.1; -; mRNA.
DR EMBL; AL136938; CAB66872.1; -; mRNA.
DR EMBL; AK289570; BAF82259.1; -; mRNA.
DR EMBL; AK295592; BAG58483.1; -; mRNA.
DR EMBL; AK299968; BAG61794.1; -; mRNA.
DR EMBL; AC073342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471198; EAW51877.1; -; Genomic_DNA.
DR EMBL; BC001231; AAH01231.1; -; mRNA.
DR EMBL; BC050715; AAH50715.1; -; mRNA.
DR EMBL; BC063425; AAH63425.1; -; mRNA.
DR RefSeq; NP_001137151.1; NM_001143679.1.
DR RefSeq; NP_001137152.1; NM_001143680.1.
DR RefSeq; NP_001137153.1; NM_001143681.1.
DR RefSeq; NP_057001.1; NM_015917.2.
DR UniGene; Hs.390667; -.
DR PDB; 1YZX; X-ray; 1.93 A; A/B=1-226.
DR PDB; 3RPN; X-ray; 1.90 A; A/B/C/D/E/F=1-226.
DR PDB; 3RPP; X-ray; 1.80 A; A/B/C=1-226.
DR PDBsum; 1YZX; -.
DR PDBsum; 3RPN; -.
DR PDBsum; 3RPP; -.
DR ProteinModelPortal; Q9Y2Q3; -.
DR SMR; Q9Y2Q3; 2-221.
DR DIP; DIP-46924N; -.
DR IntAct; Q9Y2Q3; 7.
DR MINT; MINT-3084797; -.
DR STRING; 9606.ENSP00000367415; -.
DR BindingDB; Q9Y2Q3; -.
DR ChEMBL; CHEMBL4491; -.
DR DrugBank; DB00143; Glutathione.
DR PhosphoSite; Q9Y2Q3; -.
DR DMDM; 12643338; -.
DR PaxDb; Q9Y2Q3; -.
DR PRIDE; Q9Y2Q3; -.
DR DNASU; 373156; -.
DR Ensembl; ENST00000358406; ENSP00000351181; ENSG00000197448.
DR Ensembl; ENST00000409500; ENSP00000386944; ENSG00000197448.
DR Ensembl; ENST00000443571; ENSP00000415813; ENSG00000197448.
DR Ensembl; ENST00000479303; ENSP00000431049; ENSG00000197448.
DR GeneID; 373156; -.
DR KEGG; hsa:373156; -.
DR UCSC; uc003wci.3; human.
DR CTD; 373156; -.
DR GeneCards; GC07P142942; -.
DR HGNC; HGNC:16906; GSTK1.
DR HPA; HPA006311; -.
DR HPA; HPA022904; -.
DR MIM; 602321; gene.
DR neXtProt; NX_Q9Y2Q3; -.
DR PharmGKB; PA134948237; -.
DR eggNOG; NOG70325; -.
DR HOGENOM; HOG000219769; -.
DR HOVERGEN; HBG051852; -.
DR KO; K13299; -.
DR OMA; ELWRRIW; -.
DR PhylomeDB; Q9Y2Q3; -.
DR ChiTaRS; GSTK1; human.
DR EvolutionaryTrace; Q9Y2Q3; -.
DR GeneWiki; GSTK1; -.
DR GenomeRNAi; 373156; -.
DR NextBio; 100114; -.
DR PRO; PR:Q9Y2Q3; -.
DR ArrayExpress; Q9Y2Q3; -.
DR Bgee; Q9Y2Q3; -.
DR CleanEx; HS_GSTK1; -.
DR Genevestigator; Q9Y2Q3; -.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0004602; F:glutathione peroxidase activity; IDA:UniProtKB.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:Ensembl.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR InterPro; IPR014440; HCCAis_GSTk.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR Pfam; PF01323; DSBA; 1.
DR PIRSF; PIRSF006386; HCCAis_GSTk; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Peroxisome; Reference proteome; Transferase.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 226 Glutathione S-transferase kappa 1.
FT /FTId=PRO_0000185891.
FT REGION 16 18 Glutathione binding.
FT REGION 200 201 Glutathione binding.
FT BINDING 53 53 Glutathione.
FT BINDING 183 183 Glutathione; via amide nitrogen and
FT carbonyl oxygen.
FT MOD_RES 71 71 N6-acetyllysine.
FT MOD_RES 85 85 N6-acetyllysine (By similarity).
FT MOD_RES 116 116 N6-acetyllysine (By similarity).
FT MOD_RES 158 158 N6-acetyllysine (By similarity).
FT MOD_RES 165 165 N6-acetyllysine (By similarity).
FT MOD_RES 169 169 N6-acetyllysine.
FT VAR_SEQ 52 94 Missing (in isoform 4).
FT /FTId=VSP_040978.
FT VAR_SEQ 128 128 R -> RVSVGLWESSGRTLDDFLTFPRHVFRVMILPPPGGS
FT TVLPVTPLSPHRLPAVFSSSQ (in isoform 2).
FT /FTId=VSP_040025.
FT VAR_SEQ 129 140 Missing (in isoform 3).
FT /FTId=VSP_040979.
FT CONFLICT 51 51 S -> R (in Ref. 6; BAG61794).
FT CONFLICT 171 171 T -> A (in Ref. 6; BAG61794).
FT CONFLICT 179 179 G -> R (in Ref. 4; AAF65506).
FT CONFLICT 206 206 L -> V (in Ref. 5; AAP97160).
FT CONFLICT 220 220 P -> S (in Ref. 4; AAF65506).
FT STRAND 6 12
FT HELIX 17 29
FT TURN 30 32
FT STRAND 33 41
FT HELIX 44 47
FT STRAND 57 59
FT HELIX 61 77
FT HELIX 88 94
FT HELIX 97 109
FT HELIX 111 113
FT HELIX 114 126
FT HELIX 135 144
FT HELIX 149 156
FT TURN 157 160
FT HELIX 162 177
FT STRAND 181 183
FT STRAND 185 190
FT STRAND 193 201
FT HELIX 203 210
SQ SEQUENCE 226 AA; 25497 MW; D3FDAFD1533B58A4 CRC64;
MGPLPRTVEL FYDVLSPYSW LGFEILCRYQ NIWNINLQLR PSLITGIMKD SGNKPPGLLP
RKGLYMANDL KLLRHHLQIP IHFPKDFLSV MLEKGSLSAM RFLTAVNLEH PEMLEKASRE
LWMRVWSRNE DITEPQSILA AAEKAGMSAE QAQGLLEKIA TPKVKNQLKE TTEAACRYGA
FGLPITVAHV DGQTHMLFGS DRMELLAHLL GEKWMGPIPP AVNARL
//
MIM
602321
*RECORD*
*FIELD* NO
602321
*FIELD* TI
*602321 GLUTATHIONE S-TRANSFERASE, KAPPA-1; GSTK1
;;GLUTATHIONE S-TRANSFERASE K1;;
read moreGST13-13, RAT, HOMOLOG OF
*FIELD* TX
DESCRIPTION
Glutathione S-transferases (GSTs), such as GSTK1, catalyze the
conjugation of glutathione to a wide range of potential toxins as the
first step in detoxification (Pemble et al., 1996). For further
background information on GSTs, see 138350.
CLONING
Pemble et al. (1996) stated that rat GST 13-13 was originally purified
from mitochondria. Based on this localization and on its unique
sequence, they proposed that rat GST 13-13 constitutes a novel family of
GSTs that they termed kappa. Pemble et al. (1996) cloned the cDNA
encoding rat GST 13-13, which they renamed GSTK1. They assembled a human
cDNA sequence from sequences in EST databases. The deduced 225-amino
acid human GSTK1 polypeptide is 70% identical to rat GSTK1. Pemble et
al. (1996) noted that the GSTK1 sequence contains a putative peroxisomal
targeting sequence.
By database analysis and 5-prime RACE, Morel et al. (2004) cloned GSTK1.
The deduced 226-amino acid protein has a putative N-terminal
mitochondrial presequence and a C-terminal peroxisomal targeting
tripeptide (ARL). Real-time PCR detected GSTK1 expression in all tissues
examined, with highest levels in kidney, liver, and adrenal gland.
SDS-PAGE detected native GSTK1 at an apparent molecular mass of 29.5 kD.
Western blot analysis of subcellular fractions of HepG2 cells showed
GSTK1 in the peroxisomal and mitochondrial fractions, but not in
cytosol. Fluorescence-labeled GSTK1 localized to peroxisomes, but GSTK1
lacking the ARL tripeptide did not.
GENE STRUCTURE
Morel et al. (2004) determined that the GSTK1 gene contains 8 exons and
spans 5.68 kb. Exon 8 encompasses the 3-prime UTR. The promoter region
contains no CCAAT or TATA boxes, but it has binding sites for STAT (see
600555) and SP1 (189906) transcription factors and a GC-rich region.
MAPPING
By genomic sequence analysis, Morel et al. (2004) mapped the GSTK1 gene
to chromosome 7q34.
*FIELD* RF
1. Morel, F.; Rauch, C.; Petit, E.; Piton, A.; Theret, N.; Coles,
B.; Guillouzo, A.: Gene and protein characterization of the human
glutathione S-transferase kappa and evidence for a peroxisomal localization. J.
Biol. Chem. 279: 16246-16253, 2004.
2. Pemble, S. E.; Wardle, A. F.; Taylor, J. B.: Glutathione S-transferase
class kappa: characterization by the cloning of rat mitochondrial
GST and identification of a human homologue. Biochem. J. 319: 749-754,
1996.
*FIELD* CN
Patricia A. Hartz - updated: 12/11/2008
*FIELD* CD
Jennifer P. Macke: 2/6/1998
*FIELD* ED
mgross: 12/15/2008
terry: 12/11/2008
carol: 9/23/2008
psherman: 6/17/1998
alopez: 2/17/1998
alopez: 2/6/1998
*RECORD*
*FIELD* NO
602321
*FIELD* TI
*602321 GLUTATHIONE S-TRANSFERASE, KAPPA-1; GSTK1
;;GLUTATHIONE S-TRANSFERASE K1;;
read moreGST13-13, RAT, HOMOLOG OF
*FIELD* TX
DESCRIPTION
Glutathione S-transferases (GSTs), such as GSTK1, catalyze the
conjugation of glutathione to a wide range of potential toxins as the
first step in detoxification (Pemble et al., 1996). For further
background information on GSTs, see 138350.
CLONING
Pemble et al. (1996) stated that rat GST 13-13 was originally purified
from mitochondria. Based on this localization and on its unique
sequence, they proposed that rat GST 13-13 constitutes a novel family of
GSTs that they termed kappa. Pemble et al. (1996) cloned the cDNA
encoding rat GST 13-13, which they renamed GSTK1. They assembled a human
cDNA sequence from sequences in EST databases. The deduced 225-amino
acid human GSTK1 polypeptide is 70% identical to rat GSTK1. Pemble et
al. (1996) noted that the GSTK1 sequence contains a putative peroxisomal
targeting sequence.
By database analysis and 5-prime RACE, Morel et al. (2004) cloned GSTK1.
The deduced 226-amino acid protein has a putative N-terminal
mitochondrial presequence and a C-terminal peroxisomal targeting
tripeptide (ARL). Real-time PCR detected GSTK1 expression in all tissues
examined, with highest levels in kidney, liver, and adrenal gland.
SDS-PAGE detected native GSTK1 at an apparent molecular mass of 29.5 kD.
Western blot analysis of subcellular fractions of HepG2 cells showed
GSTK1 in the peroxisomal and mitochondrial fractions, but not in
cytosol. Fluorescence-labeled GSTK1 localized to peroxisomes, but GSTK1
lacking the ARL tripeptide did not.
GENE STRUCTURE
Morel et al. (2004) determined that the GSTK1 gene contains 8 exons and
spans 5.68 kb. Exon 8 encompasses the 3-prime UTR. The promoter region
contains no CCAAT or TATA boxes, but it has binding sites for STAT (see
600555) and SP1 (189906) transcription factors and a GC-rich region.
MAPPING
By genomic sequence analysis, Morel et al. (2004) mapped the GSTK1 gene
to chromosome 7q34.
*FIELD* RF
1. Morel, F.; Rauch, C.; Petit, E.; Piton, A.; Theret, N.; Coles,
B.; Guillouzo, A.: Gene and protein characterization of the human
glutathione S-transferase kappa and evidence for a peroxisomal localization. J.
Biol. Chem. 279: 16246-16253, 2004.
2. Pemble, S. E.; Wardle, A. F.; Taylor, J. B.: Glutathione S-transferase
class kappa: characterization by the cloning of rat mitochondrial
GST and identification of a human homologue. Biochem. J. 319: 749-754,
1996.
*FIELD* CN
Patricia A. Hartz - updated: 12/11/2008
*FIELD* CD
Jennifer P. Macke: 2/6/1998
*FIELD* ED
mgross: 12/15/2008
terry: 12/11/2008
carol: 9/23/2008
psherman: 6/17/1998
alopez: 2/17/1998
alopez: 2/6/1998