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Showing Protein Glutathione S-transferase kappa 1 (HMDBP00813)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 40 metabolites
Identification
HMDB Protein ID HMDBP00813
Secondary Accession Numbers
  • 6093
Name Glutathione S-transferase kappa 1
Synonyms
  1. GST 13-13
  2. GST class-kappa
  3. GSTK1-1
  4. Glutathione S-transferase subunit 13
  5. hGSTK1
Gene Name GSTK1
Protein Type Enzyme
Biological Properties
General Function Involved in protein disulfide oxidoreductase activity
Specific Function Significant glutathione conjugating activity is found only with the model substrate, 1-chloro-2,4-dinitrobenzene (CDNB).
Pathways
  • Chemical carcinogenesis - DNA adducts
  • Drug metabolism - cytochrome P450
  • Glutathione metabolism
  • Metabolism of xenobiotics by cytochrome P450
  • Peroxisome
Reactions
RX + Glutathione → HX + R-S-glutathione details
RX + Glutathione → Halide + R-S-Glutathione details
Naphthalene epoxide + Glutathione → (1R)-Hydroxy-(2R)-glutathionyl-1,2-dihydronaphthalene details
(1S,2R)-Naphthalene 1,2-oxide + Glutathione → (1R)-Glutathionyl-(2R)-hydroxy-1,2-dihydronaphthalene details
(1S,2R)-Naphthalene 1,2-oxide + Glutathione → (1S)-Hydroxy-(2S)-glutathionyl-1,2-dihydronaphthalene details
1-Nitronaphthalene-7,8-oxide + Glutathione → 1-Nitro-7-hydroxy-8-glutathionyl-7,8-dihydronaphthalene details
1-Nitronaphthalene-7,8-oxide + Glutathione → 1-Nitro-7-glutathionyl-8-hydroxy-7,8-dihydronaphthalene details
1-Nitronaphthalene-5,6-oxide + Glutathione → 1-Nitro-5-hydroxy-6-glutathionyl-5,6-dihydronaphthalene details
1-Nitronaphthalene-5,6-oxide + Glutathione → 1-Nitro-5-glutathionyl-6-hydroxy-5,6-dihydronaphthalene details
Bromobenzene-3,4-oxide + Glutathione → 3,4-Dihydro-3-hydroxy-4-S-glutathionyl bromobenzene details
Bromobenzene-2,3-oxide + Glutathione → 2,3-Dihydro-2-S-glutathionyl-3-hydroxy bromobenzene details
Benzo[a]pyrene-4,5-oxide + Glutathione → 4,5-Dihydro-4-hydroxy-5-S-glutathionyl-benzo[a]pyrene details
Benzo[a]pyrene-7,8-diol + Glutathione → 7,8-Dihydro-7-hydroxy-8-S-glutathionyl-benzo[a]pyrene + Water details
2,2-Dichloroacetaldehyde + Glutathione → S-(2,2-Dichloro-1-hydroxy)ethyl glutathione details
1,1-Dichloroethylene epoxide + Glutathione → 2-(S-Glutathionyl)acetyl chloride + Hydrochloric acid details
Chloroacetyl chloride + Glutathione → S-(2-Chloroacetyl)glutathione + Hydrochloric acid details
2-(S-Glutathionyl)acetyl chloride + Glutathione → 2-(S-Glutathionyl)acetyl glutathione + Hydrochloric acid details
Trichloroethylene + Glutathione → S-(1,2-Dichlorovinyl)glutathione + Hydrochloric acid details
1,2-Dibromoethane + Glutathione + Hydrogen Ion → Glutathione episulfonium ion + Bromide details
2-Bromoacetaldehyde + Glutathione → S-(Formylmethyl)glutathione + Bromide details
Aldophosphamide + Glutathione → 4-Glutathionyl cyclophosphamide + Water details
GO Classification
Biological Process
glutathione metabolic process
Cellular Component
peroxisome
mitochondrial inner membrane
Component
cell part
periplasmic space
outer membrane-bounded periplasmic space
Function
catalytic activity
oxidoreductase activity, acting on a sulfur group of donors
disulfide oxidoreductase activity
protein disulfide oxidoreductase activity
oxidoreductase activity
Molecular Function
glutathione peroxidase activity
glutathione transferase activity
protein disulfide oxidoreductase activity
Cellular Location
  1. Peroxisome
Gene Properties
Chromosome Location 7
Locus 7q34
SNPs GSTK1
Gene Sequence 
>681 bp
ATGGGGCCCCTGCCGCGCACCGTGGAGCTCTTCTATGACGTGCTGTCCCCCTACTCCTGG
CTGGGCTTCGAGATCCTGTGCCGGTATCAGAATATCTGGAACATCAACCTGCAGTTGCGG
CCCAGCCTCATAACAGGGATCATGAAAGACAGTGGAAACAAGCCTCCAGGTCTGCTTCCC
CGCAAAGGACTATACATGGCAAATGACTTAAAGCTCCTGAGACACCATCTCCAGATTCCC
ATCCACTTCCCCAAGGATTTCTTGTCTGTGATGCTTGAAAAAGGAAGTTTGTCTGCCATG
CGTTTCCTCACCGCCGTGAACTTGGAGCATCCAGAGATGCTGGAGAAAGCGTCCCGGGAG
CTGTGGATGCGCGTCTGGTCAAGGAATGAAGACATCACCGAGCCGCAGAGCATCCTGGCG
GCTGCAGAGAAGGCTGGTATGTCTGCAGAACAAGCCCAGGGACTTCTGGAAAAGATCGCA
ACGCCAAAGGTGAAGAACCAGCTCAAGGAGACCACTGAGGCAGCCTGCAGATACGGAGCC
TTTGGGCTGCCCATCACCGTGGCCCATGTGGATGGCCAAACCCACATGTTATTTGGCTCT
GACCGGATGGAGCTGCTGGCGCACCTGCTGGGAGAGAAGTGGATGGGCCCTATACCTCCA
GCCGTGAATGCCAGACTTTAA
Protein Properties
Number of Residues 226
Molecular Weight 31565.605
Theoretical pI 8.737
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Glutathione S-transferase kappa 1
MGPLPRTVELFYDVLSPYSWLGFEILCRYQNIWNINLQLRPSLITGIMKDSGNKPPGLLP
RKGLYMANDLKLLRHHLQIPIHFPKDFLSVMLEKGSLSAMRFLTAVNLEHPEMLEKASRE
LWMRVWSRNEDITEPQSILAAAEKAGMSAEQAQGLLEKIATPKVKNQLKETTEAACRYGA
FGLPITVAHVDGQTHMLFGSDRMELLAHLLGEKWMGPIPPAVNARL
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q9Y2Q3
UniProtKB/Swiss-Prot Entry Name GSTK1_HUMAN
PDB IDs
GenBank Gene ID AY520571
GeneCard ID GSTK1
GenAtlas ID GSTK1
HGNC ID HGNC:16906
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed:11230166 ]
  4. Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed:11042152 ]
  5. Robinson A, Huttley GA, Booth HS, Board PG: Modelling and bioinformatics studies of the human Kappa-class glutathione transferase predict a novel third glutathione transferase family with similarity to prokaryotic 2-hydroxychromene-2-carboxylate isomerases. Biochem J. 2004 May 1;379(Pt 3):541-52. [PubMed:14709161 ]
  6. 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. 2004 Apr 16;279(16):16246-53. Epub 2004 Jan 23. [PubMed:14742434 ]