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Q9Y2Q3

- GSTK1_HUMAN

UniProt

Q9Y2Q3 - GSTK1_HUMAN

Protein

Glutathione S-transferase kappa 1

Gene

GSTK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Significant glutathione conjugating activity is found only with the model substrate, 1-chloro-2,4-dinitrobenzene (CDNB).

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei53 – 531Glutathione1 Publication
    Binding sitei183 – 1831Glutathione; via amide nitrogen and carbonyl oxygen1 Publication

    GO - Molecular functioni

    1. glutathione peroxidase activity Source: UniProtKB
    2. glutathione transferase activity Source: UniProtKB
    3. protein disulfide oxidoreductase activity Source: InterPro
    4. receptor binding Source: UniProtKB

    GO - Biological processi

    1. epithelial cell differentiation Source: UniProt
    2. glutathione metabolic process Source: Ensembl
    3. oxidation-reduction process Source: GOC

    Keywords - Molecular functioni

    Transferase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase kappa 1 (EC:2.5.1.18)
    Alternative name(s):
    GST 13-13
    GST class-kappa
    GSTK1-1
    Short name:
    hGSTK1
    Glutathione S-transferase subunit 13
    Gene namesi
    Name:GSTK1
    ORF Names:HDCMD47P
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:16906. GSTK1.

    Subcellular locationi

    Peroxisome 1 Publication

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. intracellular Source: LIFEdb
    3. membrane Source: UniProtKB
    4. mitochondrial inner membrane Source: Ensembl
    5. mitochondrial matrix Source: Ensembl
    6. peroxisome Source: UniProtKB

    Keywords - Cellular componenti

    Peroxisome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134948237.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 226225Glutathione S-transferase kappa 1PRO_0000185891Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei49 – 491N6-succinyllysineBy similarity
    Modified residuei71 – 711N6-acetyllysine1 Publication
    Modified residuei85 – 851N6-acetyllysineBy similarity
    Modified residuei116 – 1161N6-acetyllysine; alternateBy similarity
    Modified residuei116 – 1161N6-succinyllysine; alternateBy similarity
    Modified residuei144 – 1441N6-succinyllysineBy similarity
    Modified residuei158 – 1581N6-acetyllysine; alternateBy similarity
    Modified residuei158 – 1581N6-succinyllysine; alternateBy similarity
    Modified residuei165 – 1651N6-acetyllysineBy similarity
    Modified residuei169 – 1691N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9Y2Q3.
    PaxDbiQ9Y2Q3.
    PRIDEiQ9Y2Q3.

    PTM databases

    PhosphoSiteiQ9Y2Q3.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    ArrayExpressiQ9Y2Q3.
    BgeeiQ9Y2Q3.
    CleanExiHS_GSTK1.
    GenevestigatoriQ9Y2Q3.

    Organism-specific databases

    HPAiHPA006311.
    HPA022904.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi131875. 36 interactions.
    DIPiDIP-46924N.
    IntActiQ9Y2Q3. 7 interactions.
    MINTiMINT-3084797.
    STRINGi9606.ENSP00000367415.

    Structurei

    Secondary structure

    1
    226
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 127
    Helixi17 – 2913
    Turni30 – 323
    Beta strandi33 – 419
    Helixi44 – 474
    Beta strandi57 – 593
    Helixi61 – 7717
    Helixi88 – 947
    Helixi97 – 10913
    Helixi111 – 1133
    Helixi114 – 12613
    Helixi135 – 14410
    Helixi149 – 1568
    Turni157 – 1604
    Helixi162 – 17716
    Beta strandi181 – 1833
    Beta strandi185 – 1906
    Beta strandi193 – 2019
    Helixi203 – 2108

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YZXX-ray1.93A/B1-226[»]
    3RPNX-ray1.90A/B/C/D/E/F1-226[»]
    3RPPX-ray1.80A/B/C1-226[»]
    ProteinModelPortaliQ9Y2Q3.
    SMRiQ9Y2Q3. Positions 2-221.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y2Q3.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni16 – 183Glutathione binding
    Regioni200 – 2012Glutathione binding

    Sequence similaritiesi

    Belongs to the GST superfamily. Kappa family.Curated

    Phylogenomic databases

    eggNOGiNOG70325.
    HOGENOMiHOG000219769.
    HOVERGENiHBG051852.
    KOiK13299.
    OMAiELWRRIW.
    PhylomeDBiQ9Y2Q3.
    TreeFamiTF105323.

    Family and domain databases

    Gene3Di3.40.30.10. 1 hit.
    InterProiIPR001853. DSBA-like_thioredoxin_dom.
    IPR014440. HCCAis_GSTk.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF01323. DSBA. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006386. HCCAis_GSTk. 1 hit.
    SUPFAMiSSF52833. SSF52833. 1 hit.

    Sequences (4)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y2Q3-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MGPLPRTVEL FYDVLSPYSW LGFEILCRYQ NIWNINLQLR PSLITGIMKD    50
    SGNKPPGLLP RKGLYMANDL KLLRHHLQIP IHFPKDFLSV MLEKGSLSAM 100
    RFLTAVNLEH PEMLEKASRE LWMRVWSRNE DITEPQSILA AAEKAGMSAE 150
    QAQGLLEKIA TPKVKNQLKE TTEAACRYGA FGLPITVAHV DGQTHMLFGS 200
    DRMELLAHLL GEKWMGPIPP AVNARL 226
    Length:226
    Mass (Da):25,497
    Last modified:January 23, 2007 - v3
    Checksum:iD3FDAFD1533B58A4
    GO
    Isoform 2 (identifier: Q9Y2Q3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         128-128: R → RVSVGLWESSGRTLDDFLTFPRHVFRVMILPPPGGSTVLPVTPLSPHRLPAVFSSSQ

    Show »
    Length:282
    Mass (Da):31,566
    Checksum:i6F88B28A6081324D
    GO
    Isoform 3 (identifier: Q9Y2Q3-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         129-140: Missing.

    Show »
    Length:214
    Mass (Da):24,185
    Checksum:iFA98AC407CF8FB7B
    GO
    Isoform 4 (identifier: Q9Y2Q3-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         52-94: Missing.

    Show »
    Length:183
    Mass (Da):20,538
    Checksum:i2AA664FBDBB510C9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti51 – 511S → R in BAG61794. (PubMed:14702039)Curated
    Sequence conflicti171 – 1711T → A in BAG61794. (PubMed:14702039)Curated
    Sequence conflicti179 – 1791G → R in AAF65506. 1 PublicationCurated
    Sequence conflicti206 – 2061L → V in AAP97160. 1 PublicationCurated
    Sequence conflicti220 – 2201P → S in AAF65506. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei52 – 9443Missing in isoform 4. 1 PublicationVSP_040978Add
    BLAST
    Alternative sequencei128 – 1281R → RVSVGLWESSGRTLDDFLTF PRHVFRVMILPPPGGSTVLP VTPLSPHRLPAVFSSSQ in isoform 2. 2 PublicationsVSP_040025
    Alternative sequencei129 – 14012Missing in isoform 3. 1 PublicationVSP_040979Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY520571 mRNA. Translation: AAS00610.1.
    AY486465 Genomic DNA. Translation: AAS01180.1.
    AF070657 mRNA. Translation: AAD20963.1.
    AF068287 mRNA. Translation: AAF65506.1.
    AF087849 mRNA. Translation: AAP97160.1.
    AL136938 mRNA. Translation: CAB66872.1.
    AK289570 mRNA. Translation: BAF82259.1.
    AK295592 mRNA. Translation: BAG58483.1.
    AK299968 mRNA. Translation: BAG61794.1.
    AC073342 Genomic DNA. No translation available.
    CH471198 Genomic DNA. Translation: EAW51877.1.
    BC001231 mRNA. Translation: AAH01231.1.
    BC050715 mRNA. Translation: AAH50715.1.
    BC063425 mRNA. Translation: AAH63425.1.
    CCDSiCCDS47730.1. [Q9Y2Q3-2]
    CCDS47731.1. [Q9Y2Q3-3]
    CCDS47732.1. [Q9Y2Q3-4]
    CCDS5877.1. [Q9Y2Q3-1]
    RefSeqiNP_001137151.1. NM_001143679.1. [Q9Y2Q3-2]
    NP_001137152.1. NM_001143680.1. [Q9Y2Q3-3]
    NP_001137153.1. NM_001143681.1. [Q9Y2Q3-4]
    NP_057001.1. NM_015917.2. [Q9Y2Q3-1]
    UniGeneiHs.390667.

    Genome annotation databases

    EnsembliENST00000358406; ENSP00000351181; ENSG00000197448. [Q9Y2Q3-1]
    ENST00000409500; ENSP00000386944; ENSG00000197448. [Q9Y2Q3-3]
    ENST00000443571; ENSP00000415813; ENSG00000197448. [Q9Y2Q3-4]
    ENST00000479303; ENSP00000431049; ENSG00000197448. [Q9Y2Q3-2]
    GeneIDi373156.
    KEGGihsa:373156.
    UCSCiuc003wci.3. human. [Q9Y2Q3-1]
    uc003wcj.3. human. [Q9Y2Q3-2]
    uc011ksy.2. human. [Q9Y2Q3-4]
    uc011ksz.2. human. [Q9Y2Q3-3]

    Polymorphism databases

    DMDMi12643338.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY520571 mRNA. Translation: AAS00610.1 .
    AY486465 Genomic DNA. Translation: AAS01180.1 .
    AF070657 mRNA. Translation: AAD20963.1 .
    AF068287 mRNA. Translation: AAF65506.1 .
    AF087849 mRNA. Translation: AAP97160.1 .
    AL136938 mRNA. Translation: CAB66872.1 .
    AK289570 mRNA. Translation: BAF82259.1 .
    AK295592 mRNA. Translation: BAG58483.1 .
    AK299968 mRNA. Translation: BAG61794.1 .
    AC073342 Genomic DNA. No translation available.
    CH471198 Genomic DNA. Translation: EAW51877.1 .
    BC001231 mRNA. Translation: AAH01231.1 .
    BC050715 mRNA. Translation: AAH50715.1 .
    BC063425 mRNA. Translation: AAH63425.1 .
    CCDSi CCDS47730.1. [Q9Y2Q3-2 ]
    CCDS47731.1. [Q9Y2Q3-3 ]
    CCDS47732.1. [Q9Y2Q3-4 ]
    CCDS5877.1. [Q9Y2Q3-1 ]
    RefSeqi NP_001137151.1. NM_001143679.1. [Q9Y2Q3-2 ]
    NP_001137152.1. NM_001143680.1. [Q9Y2Q3-3 ]
    NP_001137153.1. NM_001143681.1. [Q9Y2Q3-4 ]
    NP_057001.1. NM_015917.2. [Q9Y2Q3-1 ]
    UniGenei Hs.390667.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YZX X-ray 1.93 A/B 1-226 [» ]
    3RPN X-ray 1.90 A/B/C/D/E/F 1-226 [» ]
    3RPP X-ray 1.80 A/B/C 1-226 [» ]
    ProteinModelPortali Q9Y2Q3.
    SMRi Q9Y2Q3. Positions 2-221.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 131875. 36 interactions.
    DIPi DIP-46924N.
    IntActi Q9Y2Q3. 7 interactions.
    MINTi MINT-3084797.
    STRINGi 9606.ENSP00000367415.

    Chemistry

    BindingDBi Q9Y2Q3.
    ChEMBLi CHEMBL4491.
    DrugBanki DB00143. Glutathione.

    PTM databases

    PhosphoSitei Q9Y2Q3.

    Polymorphism databases

    DMDMi 12643338.

    Proteomic databases

    MaxQBi Q9Y2Q3.
    PaxDbi Q9Y2Q3.
    PRIDEi Q9Y2Q3.

    Protocols and materials databases

    DNASUi 373156.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000358406 ; ENSP00000351181 ; ENSG00000197448 . [Q9Y2Q3-1 ]
    ENST00000409500 ; ENSP00000386944 ; ENSG00000197448 . [Q9Y2Q3-3 ]
    ENST00000443571 ; ENSP00000415813 ; ENSG00000197448 . [Q9Y2Q3-4 ]
    ENST00000479303 ; ENSP00000431049 ; ENSG00000197448 . [Q9Y2Q3-2 ]
    GeneIDi 373156.
    KEGGi hsa:373156.
    UCSCi uc003wci.3. human. [Q9Y2Q3-1 ]
    uc003wcj.3. human. [Q9Y2Q3-2 ]
    uc011ksy.2. human. [Q9Y2Q3-4 ]
    uc011ksz.2. human. [Q9Y2Q3-3 ]

    Organism-specific databases

    CTDi 373156.
    GeneCardsi GC07P142942.
    HGNCi HGNC:16906. GSTK1.
    HPAi HPA006311.
    HPA022904.
    MIMi 602321. gene.
    neXtProti NX_Q9Y2Q3.
    PharmGKBi PA134948237.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG70325.
    HOGENOMi HOG000219769.
    HOVERGENi HBG051852.
    KOi K13299.
    OMAi ELWRRIW.
    PhylomeDBi Q9Y2Q3.
    TreeFami TF105323.

    Miscellaneous databases

    ChiTaRSi GSTK1. human.
    EvolutionaryTracei Q9Y2Q3.
    GeneWikii GSTK1.
    GenomeRNAii 373156.
    NextBioi 100114.
    PROi Q9Y2Q3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y2Q3.
    Bgeei Q9Y2Q3.
    CleanExi HS_GSTK1.
    Genevestigatori Q9Y2Q3.

    Family and domain databases

    Gene3Di 3.40.30.10. 1 hit.
    InterProi IPR001853. DSBA-like_thioredoxin_dom.
    IPR014440. HCCAis_GSTk.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF01323. DSBA. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF006386. HCCAis_GSTk. 1 hit.
    SUPFAMi SSF52833. SSF52833. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Modelling and bioinformatics studies of the human kappa class glutathione transferase predict a novel third glutathione transferase family with homology to prokaryotic 2-hydroxychromene-2-carboxylate (HCCA) isomerases."
      Robinson A., Huttley G.A., Booth H.S., Board P.G.
      Biochem. J. 379:541-552(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
      Tissue: Mammary gland.
    2. "Gene and protein characterization of the human glutathione S-transferase kappa and evidence for a peroxisomal localization."
      Morel F., Rauch C., Petit E., Piton A., Theret N., Coles B., Guillouzo A.
      J. Biol. Chem. 279:16246-16253(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    3. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Umbilical cord blood.
    4. "A novel gene from human dendritic cell."
      Zhao Z., Huang X., Li N., Zhu X., Cao X.
      Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Dendritic cell.
    5. "Cloning of a novel human cDNA homologous to rats rGSTK1-1 mRNA."
      Zhang M., Yu L., Zhou Y., Hu P.R., Xin Y.R., Zhao S.Y.
      Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    6. "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.
      , 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] (ISOFORMS 2; 3 AND 4).
      Tissue: Cerebellum and Hippocampus.
    7. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Uterus.
    10. "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] (ISOFORMS 1 AND 2).
      Tissue: Blood, Cervix and Pancreas.
    11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-71 AND LYS-169, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Thioredoxin-like domain of human kappa class glutathione transferase reveals sequence homology and structure similarity to the theta class enzyme."
      Li J., Xia Z., Ding J.
      Protein Sci. 14:2361-2369(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, SUBUNIT.

    Entry informationi

    Entry nameiGSTK1_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y2Q3
    Secondary accession number(s): B4DIH1
    , B4DSY2, Q6P4H0, Q7Z520, Q9P1S4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 130 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3