GSTK1_HUMAN
ID GSTK1_HUMAN Reviewed; 226 AA.
AC Q9Y2Q3; B4DIH1; B4DSY2; Q6P4H0; Q7Z520; Q9P1S4;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Glutathione S-transferase kappa 1;
DE EC=2.5.1.18 {ECO:0000269|PubMed:14709161, ECO:0000269|PubMed:14742434};
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND CATALYTIC ACTIVITY.
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 glutathione
RT transferase predict a novel third glutathione transferase family with
RT homology to prokaryotic 2-hydroxychromene-2-carboxylate (HCCA)
RT isomerases.";
RL Biochem. J. 379:541-552(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=14742434; DOI=10.1074/jbc.m313357200;
RA Morel F., Rauch C., Petit E., Piton A., Theret N., Coles B., Guillouzo A.;
RT "Gene and protein characterization of the human glutathione S-transferase
RT 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 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT 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., 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 [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., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., 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., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 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 project:
RT 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
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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., 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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, AND
RP 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: Glutathione S-transferase that catalyzes the conjugation of
CC glutathione to exogenous and endogenous compounds (PubMed:14709161,
CC PubMed:14742434). Significant glutathione conjugating activity is found
CC only with the model substrate, 1-chloro-2,4-dinitrobenzene (CDNB)
CC (PubMed:14709161). {ECO:0000269|PubMed:14709161,
CC ECO:0000269|PubMed:14742434}.
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:14709161, ECO:0000269|PubMed:14742434};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16081649}.
CC -!- INTERACTION:
CC Q9Y2Q3; O95273: CCNDBP1; NbExp=3; IntAct=EBI-1053767, EBI-748961;
CC Q9Y2Q3; Q8IZU0: FAM9B; NbExp=4; IntAct=EBI-1053767, EBI-10175124;
CC Q9Y2Q3; Q60994: Adipoq; Xeno; NbExp=2; IntAct=EBI-1053767, EBI-7264589;
CC Q9Y2Q3-2; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-12013556, EBI-3044087;
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:14742434}.
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. {ECO:0000269|PubMed:14742434}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Kappa family.
CC {ECO:0000305}.
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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 CCDS; CCDS47730.1; -. [Q9Y2Q3-2]
DR CCDS; CCDS47731.1; -. [Q9Y2Q3-3]
DR CCDS; CCDS47732.1; -. [Q9Y2Q3-4]
DR CCDS; CCDS5877.1; -. [Q9Y2Q3-1]
DR RefSeq; NP_001137151.1; NM_001143679.1. [Q9Y2Q3-2]
DR RefSeq; NP_001137152.1; NM_001143680.1. [Q9Y2Q3-3]
DR RefSeq; NP_001137153.1; NM_001143681.1. [Q9Y2Q3-4]
DR RefSeq; NP_057001.1; NM_015917.2. [Q9Y2Q3-1]
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 AlphaFoldDB; Q9Y2Q3; -.
DR SMR; Q9Y2Q3; -.
DR BioGRID; 131875; 127.
DR DIP; DIP-46924N; -.
DR IntAct; Q9Y2Q3; 22.
DR MINT; Q9Y2Q3; -.
DR BindingDB; Q9Y2Q3; -.
DR ChEMBL; CHEMBL4491; -.
DR DrugBank; DB00143; Glutathione.
DR DrugBank; DB04700; GLUTATHIONE SULFINATE.
DR DrugCentral; Q9Y2Q3; -.
DR iPTMnet; Q9Y2Q3; -.
DR MetOSite; Q9Y2Q3; -.
DR PhosphoSitePlus; Q9Y2Q3; -.
DR SwissPalm; Q9Y2Q3; -.
DR BioMuta; GSTK1; -.
DR DMDM; 12643338; -.
DR EPD; Q9Y2Q3; -.
DR jPOST; Q9Y2Q3; -.
DR MassIVE; Q9Y2Q3; -.
DR MaxQB; Q9Y2Q3; -.
DR PeptideAtlas; Q9Y2Q3; -.
DR PRIDE; Q9Y2Q3; -.
DR ProteomicsDB; 85865; -. [Q9Y2Q3-1]
DR ProteomicsDB; 85866; -. [Q9Y2Q3-2]
DR ProteomicsDB; 85867; -. [Q9Y2Q3-3]
DR ProteomicsDB; 85868; -. [Q9Y2Q3-4]
DR TopDownProteomics; Q9Y2Q3-1; -. [Q9Y2Q3-1]
DR TopDownProteomics; Q9Y2Q3-2; -. [Q9Y2Q3-2]
DR TopDownProteomics; Q9Y2Q3-4; -. [Q9Y2Q3-4]
DR Antibodypedia; 1607; 375 antibodies from 35 providers.
DR DNASU; 373156; -.
DR Ensembl; ENST00000358406.10; ENSP00000351181.5; ENSG00000197448.14. [Q9Y2Q3-1]
DR Ensembl; ENST00000409500.7; ENSP00000386944.3; ENSG00000197448.14. [Q9Y2Q3-3]
DR Ensembl; ENST00000443571.6; ENSP00000415813.2; ENSG00000197448.14. [Q9Y2Q3-4]
DR Ensembl; ENST00000479303.1; ENSP00000431049.1; ENSG00000197448.14. [Q9Y2Q3-2]
DR GeneID; 373156; -.
DR KEGG; hsa:373156; -.
DR MANE-Select; ENST00000358406.10; ENSP00000351181.5; NM_015917.3; NP_057001.1.
DR UCSC; uc003wci.4; human. [Q9Y2Q3-1]
DR CTD; 373156; -.
DR DisGeNET; 373156; -.
DR GeneCards; GSTK1; -.
DR HGNC; HGNC:16906; GSTK1.
DR HPA; ENSG00000197448; Low tissue specificity.
DR MIM; 602321; gene.
DR neXtProt; NX_Q9Y2Q3; -.
DR OpenTargets; ENSG00000197448; -.
DR PharmGKB; PA134948237; -.
DR VEuPathDB; HostDB:ENSG00000197448; -.
DR GeneTree; ENSGT00440000033697; -.
DR HOGENOM; CLU_069253_1_1_1; -.
DR InParanoid; Q9Y2Q3; -.
DR OMA; AAFHHMW; -.
DR OrthoDB; 1320977at2759; -.
DR PhylomeDB; Q9Y2Q3; -.
DR TreeFam; TF105323; -.
DR PathwayCommons; Q9Y2Q3; -.
DR Reactome; R-HSA-156590; Glutathione conjugation.
DR Reactome; R-HSA-9033241; Peroxisomal protein import.
DR SignaLink; Q9Y2Q3; -.
DR BioGRID-ORCS; 373156; 10 hits in 1075 CRISPR screens.
DR ChiTaRS; GSTK1; human.
DR EvolutionaryTrace; Q9Y2Q3; -.
DR GeneWiki; GSTK1; -.
DR GenomeRNAi; 373156; -.
DR Pharos; Q9Y2Q3; Tchem.
DR PRO; PR:Q9Y2Q3; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9Y2Q3; protein.
DR Bgee; ENSG00000197448; Expressed in granulocyte and 201 other tissues.
DR ExpressionAtlas; Q9Y2Q3; baseline and differential.
DR Genevisible; Q9Y2Q3; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
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:0030855; P:epithelial cell differentiation; IEP:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR CDD; cd03021; DsbA_GSTK; 1.
DR InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR InterPro; IPR044088; GSTK.
DR InterPro; IPR014440; HCCAis_GSTk.
DR InterPro; IPR036249; Thioredoxin-like_sf.
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; Peroxisome;
KW Reference proteome; Transferase.
FT CHAIN 1..226
FT /note="Glutathione S-transferase kappa 1"
FT /id="PRO_0000185891"
FT BINDING 16..18
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:16081649"
FT BINDING 53
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:16081649"
FT BINDING 183
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:16081649"
FT BINDING 200..201
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:16081649"
FT MOD_RES 49
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM2"
FT MOD_RES 71
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 85
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM2"
FT MOD_RES 116
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM2"
FT MOD_RES 116
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM2"
FT MOD_RES 144
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM2"
FT MOD_RES 158
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM2"
FT MOD_RES 158
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM2"
FT MOD_RES 165
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCM2"
FT MOD_RES 169
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 52..94
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040978"
FT VAR_SEQ 128
FT /note="R -> RVSVGLWESSGRTLDDFLTFPRHVFRVMILPPPGGSTVLPVTPLSPH
FT RLPAVFSSSQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_040025"
FT VAR_SEQ 129..140
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040979"
FT CONFLICT 51
FT /note="S -> R (in Ref. 6; BAG61794)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="T -> A (in Ref. 6; BAG61794)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="G -> R (in Ref. 4; AAF65506)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="L -> V (in Ref. 5; AAP97160)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="P -> S (in Ref. 4; AAF65506)"
FT /evidence="ECO:0000305"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:3RPP"
FT HELIX 17..29
FT /evidence="ECO:0007829|PDB:3RPP"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:3RPP"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:3RPP"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:3RPP"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:3RPP"
FT HELIX 61..77
FT /evidence="ECO:0007829|PDB:3RPP"
FT HELIX 88..94
FT /evidence="ECO:0007829|PDB:3RPP"
FT HELIX 97..109
FT /evidence="ECO:0007829|PDB:3RPP"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:3RPP"
FT HELIX 114..126
FT /evidence="ECO:0007829|PDB:3RPP"
FT HELIX 135..144
FT /evidence="ECO:0007829|PDB:3RPP"
FT HELIX 149..156
FT /evidence="ECO:0007829|PDB:3RPP"
FT TURN 157..160
FT /evidence="ECO:0007829|PDB:3RPP"
FT HELIX 162..177
FT /evidence="ECO:0007829|PDB:3RPP"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:3RPP"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:3RPP"
FT STRAND 193..201
FT /evidence="ECO:0007829|PDB:3RPP"
FT HELIX 203..210
FT /evidence="ECO:0007829|PDB:3RPP"
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
