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x * 79400, about, sequence calculation, x * 140000, about, recombinant NusA/His6-tagged isozyme DGK2, SDS-PAGE
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x * 34000, calculated and SDS-PAGE
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x * 13245, calculation from nucleotide sequence
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x * 14000 Da, SDS-PAGE
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x * 128000 DGKeta1, calculation from nucleotide sequence
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x * 104000, DGK-IVksi, calculation from amino acid sequence
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x * 135000, DGKeta2, calculation from nucleotide sequence
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x * 101400, DGK-Vtheta, calculation from amino acid sequence
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x * 130000, DGK-IIdelta, calculation from amino acid sequence
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x * 108000, enzyme from Hela cells, SDS-PAGE
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x * 152000, enzyme form DGK-I, SDS-PAGE
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x * 89000, DGK-Igamma, calculation from amino acid sequence
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x * 103900, calculation from nucleotide sequence
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x * 110000, enzyme from cell lines MDA-MB-453 and MCF-7, SDS-PAGE
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x * 82700, DGK-Ialpha, calculation from amino acid sequence
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x * 58000, enzyme form DGK-III, SDS-PAGE
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x *63900, DGK-IIIepsilon, calculation from amino acid sequence
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x * 124000, isoform DGKeta3, calculated from amino acid sequence
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x * 126000, isoform DGKeta3, SDS-PAGE
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x * 64000, His6-tagged enzyme lacking the first 40 residues, SDS-PAGE
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x * 80000, isoform DGKalpha, SDS-PAGE
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x * 85000, His6-tagged enzyme, SDS-PAGE
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x * 54630, calculated from amino acid sequence
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x * 126800, DGK-IIeta, calculation from amino acid sequence
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x * 130000, 3x-FLAG-tagged isoform variant DGKdelta2, SDS-PAGE
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x * 104000, DGK-IVksi, calculation from amino acid sequence
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x * 90300, DGK-Ibeta, calculation from amino acid sequence
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1 * 110000, enzyme from cell line PC12, SDS-PAGE
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x * 88500, DGK-Igamma, calculation from amino acid sequence
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x * 82200, DGK-Ialpha, calculation from amino acid sequence
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x * 88000-90000, isozymes DGKalpha, DGKbeta, and DGKgamma, SDS-PAGE
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x * 37333, calculated, x * 42000, SDS-PAGE
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x * 82600, DGK-Ialpha, calculation from amino acid sequence
homotrimer
solution nuclear magnetic resonance method
homotrimer
a homotrimeric enzyme with three transmembrane helices and an N-terminal amphiphilic helix per monomer. Bound lipid substrate and docked ATP identify the putative active site which is of the composite, shared site type. Each subunit within a trimer forms a bundle of 3 transmembrane helices. The three subunits are arranged around an approximate 3-fold symmetry axis that passes through the center of the trimer normal to the membrane plane, enzyme structure analysis, overview
monomer
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monomer
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1 * 51000, SDS-PAGE
monomer
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1 * 15000, SDS-PAGE
monomer
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1 * 86000, SDS-PAGE
monomer
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GKepsilon is monomeric on SDS-PAGE but exhibits partial dimerization with low concentrations of perfluorooctanoic acid
monomer
1 * 10000, isoform DGKalpha-EF domain, SDS-PAGE
monomer
1 * 10600, isoform DGKalpha-EF domain, calculated from amino acid sequence
monomer
1 * 106000, His6-tagged enzyme, calculated from amino acid sequence
monomer
1 * 125000, His6-tagged enzyme, SDS-PAGE
monomer
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1 * 78000, SDS-PAGE
trimer
optimized structures of the reactant, transition state and product with Mg2+ coordination, overview
trimer
the enzyme crafts three catalytic and substrate-binding sites centred about the membrane/cytosol interface
additional information
structural organization of isozymes containing a 1,2-diacylglycerol/phorbolester-binding domain 1, a zinc-finger dependent C1 domain, and a 1,2-diacylglycerol accessory domain, overview
additional information
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structural organization of isozymes containing a 1,2-diacylglycerol/phorbolester-binding domain 1, a zinc-finger dependent C1 domain, and a 1,2-diacylglycerol accessory domain, overview
additional information
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structure-function relationships of isozyme domain motifs, overview
additional information
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structure-function relationships of isozyme domain motifs, overview
additional information
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interaction with SH3 and SH2 domains of Src are mediated both via its proline-rich sequence and phosphorylation of Y335
additional information
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structure-function relationships of isozyme domain motifs, overview
additional information
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isozyme theta is the only one of 9 isozyme forms, that possesses three instead of two cysteine-rich domains at the N-terminal regulatory region
additional information
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structure-function relationships of isozyme domain motifs, e.g. the C1 domain, the EF hand, and the pleckstrin homology, structural motifs and their organization, mammalian isozymes require other domain in addition to the catalytic domain for activity, overview
additional information
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association of diacylglycerol kinase zeta with sorting nexin 27 via postsynaptic density protein-domain. The sorting nexin 27 postsynaptic density protein-domain contributes to its vesicle localization, interaction with diacylglycerol kinase zeta may regulate localization
additional information
association of diacylglycerol kinase zeta with sorting nexin 27 via postsynaptic density protein-domain. The sorting nexin 27 postsynaptic density protein-domain contributes to its vesicle localization, interaction with diacylglycerol kinase zeta may regulate localization
additional information
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diacylglycerol kinase delta2 interacts with the platform subdomain of adaptor protein AP2alpha through its DXF-type binding motif. Binding is involved in the transferrin internalization
additional information
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nuclear receptor steroidogenic factor 1 binds to diacylglycerol kinase zeta and diacylglycerol kinase theta in vitro and in vivo
additional information
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the N-terminal half of the catalytic region of diacylglycerol kinase gamma interacts with the Src homology 2 and C1 domains of beta-chimaerin. The Src homology 2 domain contributes to the interaction independently of phosphotyrosine
additional information
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wild-type protein has a weak tendency to oligomerize in presence of weak detergents
additional information
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structure-function relationships of isozyme domain motifs, e.g. the C1 domain, the EF hand, and the pleckstrin homology, structural motifs and their organization, mammalian isozymes require other domain in addition to the catalytic domain for activity, overview
additional information
diacylglycerol kinase zeta is associated with chromatin and dissociates from chromatin during mitotic phase
additional information
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sterile alpha-motif of diacylglycerol kinase delta1 forms helical polymers through a head-to-tail interaction. Disruption of polymerization by mutations constitutively localizes the enzyme to the plasma membrane