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ATP + a protein
ADP + a phosphoprotein
ATP + adaptor protein SH2 domain-containing leukocyte protein
ADP + phospho-[adaptor protein SH2 domain-containing leukocyte protein]
ATP + amphiphysin I
ADP + phosphorylated amphiphysin I
-
-
-
-
?
ATP + annexin 1
ADP + phospho-annexin 1
ATP + annexin 2
ADP + phospho-annexin 2
ATP + annexin 4
ADP + phospho-annexin 4
ATP + biotin-Ttds-TPGSRSRTPSLPT
ADP + phosphorylated biotin-Ttds-TPGSRSRTPSLPT
ATP + biotin-Ttds-VGLLKLASPELER
ADP + phosphorylated biotin-Ttds-VGLLKLASPELER
ATP + casein
ADP + phosphorylated casein
-
-
-
-
?
ATP + caspase-9
ADP + phosphorylated caspase-9
-
-
-
-
?
ATP + CREB
ADP + phosphorylated CREB
-
-
-
-
?
ATP + cyclin L2
ADP + phosphorylated cyclin L2
ATP + dynamin 1
ADP + phosphorylated dynamin 1
-
-
-
-
?
ATP + dynamin I
ADP + phosphorylated dynamin I
-
-
-
-
?
ATP + eIF2Bepsilon
ADP + phosphorylated eIF2Bepsilon
-
-
-
-
?
ATP + extracellular MAP kinase kinase
ADP + phospho-[MAP kinase kinase]
-
-
-
?
ATP + extracellular signal-regulated kinase
ADP + phospho-[extracellular signal-regulated kinase]
-
-
-
?
ATP + Gli1 protein
ADP + phosphorylated Gli1 protein
-
-
-
-
?
ATP + glycogen synthase
ADP + phosphorylated glycogen synthase
-
-
-
-
?
ATP + histone
ADP + phosphorylated histone
recombinant glutathione S-transferase-Dyrk/fusion protein catalyzes histone phosphorylation on tyrosine and Ser/Thr residues
-
-
?
ATP + histone H1
ADP + phosphorylated histone H1
-
-
-
-
?
ATP + immunglobulin-alpha
ADP + phospho-[immunglobulin-alpha]
ATP + insulin receptor kinase substrate 1
ADP + phosphorylated insulin receptor kinase substrate 1
ATP + microtubule associated protein 1B
ADP + phosphorylated microtubule associated protein 1B
-
DYRK1A phosphorylates the S1392 site on microtubule associated protein 1B
-
-
?
ATP + myelin basic protein
ADP + phospho-[myelin basic protein]
-
the substrate is phosphorylated on Ser, Thr, and Tyr residues by PrkG
-
-
?
ATP + myelin basic protein
ADP + phosphorylated myelin basic protein
ATP + neurodegeneration-related septin 4
ADP + phosphorylated neurodegeneration-related septin 4
SEPT4, also known as Pnutl2/CDCrel-2
-
-
?
ATP + NFAT
ADP + phosphorylated NFAT
-
-
-
-
?
ATP + Notch protein
ADP + phosphorylated Notch protein
-
-
-
-
?
ATP + Notch-IC
ADP + phosphorylated Notch-IC
-
-
-
?
ATP + p27
ADP + phospho-p27
-
p27 phosphorylation at Ser10 and Thr198
-
-
?
ATP + peptide DYRKtide
ADP + phosphorylated peptide DYRKtide
ATP + poly-(Tyr-Glu)
ADP + phospho-poly-(Tyr-Glu)
-
tyrosine kinase substrate
-
-
?
ATP + Pop2p
ADP + phosphorylated Pop2p
-
-
-
?
ATP + PRAS40
ADP + phospho-PRAS40
phosphorylation at Thr246
-
-
?
ATP + PRAS40
ADP + phosphorylated PRAS40
i.e. proline rich Akt substrate 40
-
-
?
ATP + protein
ADP + phosphoprotein
ATP + protein tyrosine
ADP + protein tyrosine phosphate
autophosphorylated on Ser and Thr residues
-
-
?
ATP + pyruvate kinase
ADP + phospho-[pyruvate kinase]
-
phosphorylated by PrkD on Ser and Thr residues
-
-
?
ATP + RNA binding family protein
ADP + phospho-RNA binding family protein
ATP + RRARKLTATPTPLGG
ADP + RRARKLTApTPTPLGG
ATP + RRRFRPASPLRGPPK
ADP + RRRFRPApSPLRGPPK
ATP + S6K1
ADP + phospho-S6K1
phosphorylation at Thr389
-
-
?
ATP + Ser/Arg-rich splicing factors
ADP + phosphorylated Ser/Arg-rich splicing factor
-
-
-
?
ATP + serine/arginine-rich protein 55
ADP + phospho-serine/arginine-rich protein 55
ATP + SF3B1 protein-L-Thr434
ADP + [SF3B1 protein]-L-Thr434 phosphate
-
-
-
-
?
ATP + splicing factor 2
ADP + phosphorylated splicing factor 2
-
-
-
-
?
ATP + splicing factor 3
ADP + phosphorylated splicing factor 3
-
-
-
-
?
ATP + splicing factor 3B1
ADP + phosphorylated splicing factor 3B1
-
splicing factor 3B1 is poshorylated at Thr434
-
-
?
ATP + SR protein
ADP + hyperphosphorylated SR protein
i.e. serine-rich and arginine-rich proteins
-
?
ATP + STAT3
ADP + phosphorylated STAT3
-
-
-
-
?
ATP + synaptojanin I
ADP + phosphorylated synaptojanin I
-
-
-
-
?
ATP + tau protein-L-Thr434
ADP + [tau protein]-L-Thr434 phosphate
-
-
-
-
?
ATP + transcription factor FKHR
ADP + phosphorylated transcription factor FKHR
-
-
-
-
?
ATP + VSNGSPSLER
ADP + VSNGpSPSLER
-
a p27-derived peptide, residues 6-15
-
-
?
biliverdin + ?
bilirubin + ?
-
-
-
-
?
additional information
?
-
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
enzyme Syk phosphoryles serine and tyrosine residues
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + adaptor protein SH2 domain-containing leukocyte protein
ADP + phospho-[adaptor protein SH2 domain-containing leukocyte protein]
-
-
-
?
ATP + adaptor protein SH2 domain-containing leukocyte protein
ADP + phospho-[adaptor protein SH2 domain-containing leukocyte protein]
phosphorylation of SLP-65 on several tyrosines
-
-
?
ATP + annexin 1
ADP + phospho-annexin 1
phosphorylation at tyrosine and serine/threonine residues
-
-
?
ATP + annexin 1
ADP + phospho-annexin 1
phosphorylation at tyrosine and serine/threonine residues
-
-
?
ATP + annexin 2
ADP + phospho-annexin 2
phosphorylation at tyrosine and serine/threonine residues
-
-
?
ATP + annexin 2
ADP + phospho-annexin 2
phosphorylation at tyrosine and serine/threonine residues
-
-
?
ATP + annexin 4
ADP + phospho-annexin 4
phosphorylation at tyrosine residues
-
-
?
ATP + annexin 4
ADP + phospho-annexin 4
phosphorylation at tyrosine residues
-
-
?
ATP + biotin-Ttds-TPGSRSRTPSLPT
ADP + phosphorylated biotin-Ttds-TPGSRSRTPSLPT
i.e. peptide PEP3
-
-
?
ATP + biotin-Ttds-TPGSRSRTPSLPT
ADP + phosphorylated biotin-Ttds-TPGSRSRTPSLPT
i.e. peptide PEP3
-
-
?
ATP + biotin-Ttds-VGLLKLASPELER
ADP + phosphorylated biotin-Ttds-VGLLKLASPELER
i.e. peptide PEP285
-
-
?
ATP + biotin-Ttds-VGLLKLASPELER
ADP + phosphorylated biotin-Ttds-VGLLKLASPELER
i.e. peptide PEP285
-
-
?
ATP + cyclin L2
ADP + phosphorylated cyclin L2
-
-
-
?
ATP + cyclin L2
ADP + phosphorylated cyclin L2
-
-
-
-
?
ATP + immunglobulin-alpha
ADP + phospho-[immunglobulin-alpha]
the inhibitory residue of Ig-alpha S197 is phosphorylated in activated B cells by Syk
-
-
?
ATP + immunglobulin-alpha
ADP + phospho-[immunglobulin-alpha]
phosphorylation of tyrosines of Ig-alpha and Ig-beta and on Ser197, immunohistochemic determination of phosphorylation site Ser197
-
-
?
ATP + insulin receptor kinase substrate 1
ADP + phosphorylated insulin receptor kinase substrate 1
-
phosphorylation at serine residues, overview, the enzyme is involved in the insulin signaling pathway
-
-
?
ATP + insulin receptor kinase substrate 1
ADP + phosphorylated insulin receptor kinase substrate 1
-
phosphorylation at serine residues leading to blockage of insulin action, overview
-
-
?
ATP + myelin basic protein
ADP + phosphorylated myelin basic protein
-
-
-
-
?
ATP + myelin basic protein
ADP + phosphorylated myelin basic protein
phosphorylation on serine, threonine, and tyrosine residues
-
-
?
ATP + myelin basic protein
ADP + phosphorylated myelin basic protein
phosphorylation on a C-terminal Ser residue
-
-
?
ATP + peptide DYRKtide
ADP + phosphorylated peptide DYRKtide
-
synthetic peptide substrate
-
-
?
ATP + peptide DYRKtide
ADP + phosphorylated peptide DYRKtide
synthetic peptide substrate
-
-
?
ATP + protein
ADP + phosphoprotein
autophosphorylation
-
-
?
ATP + protein
ADP + phosphoprotein
autophosphorylates on Ser/Thr and Tyr residues
-
-
?
ATP + protein
ADP + phosphoprotein
autophosphorylation
-
-
?
ATP + protein
ADP + phosphoprotein
autophosphorylates on Ser/Thr and Tyr residues
-
-
?
ATP + protein
ADP + phosphoprotein
when expressed in E. coli the enzyme catalyzes autophosphorylation on Tyr residues
-
-
?
ATP + protein
ADP + phosphoprotein
can phosphorylate serine, threonine, and tyrosine hydroxyamino acids
-
-
?
ATP + protein
ADP + phosphoprotein
autophosphorylation
-
-
?
ATP + protein
ADP + phosphoprotein
autophosphorylation on serine, threonine, and tyrosine residues
-
-
?
ATP + protein
ADP + phosphoprotein
autophosphorylation
-
-
?
ATP + protein
ADP + phosphoprotein
recombinant glutathione S-transferase-Dyrk fusion protein catalyzed autophosphorylation on tyrosine and serine/threonine residues
-
-
?
ATP + protein
ADP + phosphoprotein
when expressed in E. coli the enzyme catalyzes autophosphorylation on Tyr residues
-
-
?
ATP + protein
ADP + phosphoprotein
autophosphorylation
-
-
?
ATP + protein
ADP + phosphoprotein
the enzyme phosphorylates proteins on serine, threonine, and tyrosine
-
-
?
ATP + protein
ADP + phosphoprotein
Rad53 autophosphorylation activity depends on trans phosphorylation mediated by Mec1 and does not require physical association with other proteins
-
-
?
ATP + protein
ADP + phosphoprotein
autophosphorylation on Tyr residues
-
-
?
ATP + protein
ADP + phosphoprotein
kinase can phosphorylate serine, threonine and tyrosine residues
-
-
?
ATP + RNA binding family protein
ADP + phospho-RNA binding family protein
phosphorylation at serine/threonine residues
-
-
?
ATP + RNA binding family protein
ADP + phospho-RNA binding family protein
phosphorylation at serine/threonine residues
-
-
?
ATP + RRARKLTATPTPLGG
ADP + RRARKLTApTPTPLGG
i.e. peptide SAPtide
-
-
?
ATP + RRARKLTATPTPLGG
ADP + RRARKLTApTPTPLGG
i.e. peptide SAPtide
-
-
?
ATP + RRRFRPASPLRGPPK
ADP + RRRFRPApSPLRGPPK
i.e. DYRKtide
-
-
?
ATP + RRRFRPASPLRGPPK
ADP + RRRFRPApSPLRGPPK
i.e. peptide DYRKtide, designed on the basis of the phosphorylation consensus sequence for DYRK1A
-
-
?
ATP + RRRFRPASPLRGPPK
ADP + RRRFRPApSPLRGPPK
i.e. peptide DYRKtide, designed on the basis of the phosphorylation consensus sequence for DYRK1A
-
-
?
ATP + serine/arginine-rich protein 55
ADP + phospho-serine/arginine-rich protein 55
i.e. splicing factor SRp55, DYRK1a mainly phosphorylates the proline-rich domain of SRp55
-
-
?
ATP + serine/arginine-rich protein 55
ADP + phospho-serine/arginine-rich protein 55
i.e. splicing factor SRp55, DYRK1a mainly phosphorylates the proline-rich domain of SRp55. Dyrk1A phosphorylation sites are Ser280, Ser303, and Ser316
-
-
?
ATP + SR protein
ADP + ?
the enzyme is required in distinct neuroblast proliferation centers during postembryonic neurogenesis
-
-
?
ATP + SR protein
ADP + ?
-
-
-
?
ATP + SR protein
ADP + ?
enzyme is involved in the regulation of nuclear functions
-
-
?
ATP + SR protein
ADP + ?
DYRK may be involved in the abnormal neurogenesis found in Down syndrome
-
-
?
ATP + SR protein
ADP + ?
MNB protein may play a significant role in a signaling pathway regulating nuclear functions of neuronal cell proliferation, contributing to certain features of Down syndrome
-
-
?
ATP + SR protein
ADP + ?
-
-
-
?
ATP + SR protein
ADP + ?
enzyme may be involved in cell cycle control
-
-
?
ATP + SR protein
ADP + ?
enzyme is a good candidate to mediate some of the pleiotropic effects of Down syndrome
-
-
?
ATP + SR protein
ADP + ?
enzyme may be constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing
-
-
?
ATP + SR protein
ADP + ?
the enzyme phosphorylates SR splicing factors and regulates their intranuclear distribution
-
-
?
ATP + SR protein
ADP + ?
might be a component of a signaling pathway regulating nuclear functions
-
-
?
ATP + SR protein
ADP + ?
enzyme regulates a predominately testicular function
-
-
?
ATP + SR protein
ADP + ?
functions as a negative regulator of the cell cycle in Saccharomyces cerevisiae, acting downstream of the cAMP-dependent protein kinase
-
-
?
ATP + SR protein
ADP + ?
Yak1 acts downstream from, or on a parallel pathway to, the kinase step in the Ras/cAMP pathway
-
-
?
ATP + SR protein
ADP + ?
Yak1p and Pop2p are part of a novel glucose-sensing system in yeast that is involved in growth control in response to glucose availability
-
-
?
additional information
?
-
the enzyme activates STE12-dependent processes in Saccharomyces cerevisiae
-
-
?
additional information
?
-
the enzyme activates STE12-dependent processes in Saccharomyces cerevisiae
-
-
?
additional information
?
-
the enzyme activates STE12-dependent processes in Saccharomyces cerevisiae
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of Mg-chelatase and chlorophyll biosynthesis
-
-
?
additional information
?
-
substrate specificity, overview. No activity with Rubisco activase and chlorophyll A/B binding protein 3
-
-
?
additional information
?
-
-
substrate specificity, overview. No activity with Rubisco activase and chlorophyll A/B binding protein 3
-
-
?
additional information
?
-
-
the enzyme autophosphorylates on both serine/threonine and tyrosine residues
-
-
?
additional information
?
-
substrate specificity, overview. No activity with Rubisco activase and chlorophyll A/B binding protein 3
-
-
?
additional information
?
-
-
the enzyme is developmentally regulated
-
-
?
additional information
?
-
-
the enzyme is developmentally regulated
-
-
?
additional information
?
-
-
PrkG is a unique dual specificity protein kinase that mediates autophosphorylation and substrate phosphorylation on Ser, Thr, and Tyr residues
-
-
?
additional information
?
-
-
no activity with pyruvate kinase as substrate, and with probable substrates Ef-Tu, Ef-G, SsbA, Bas4487, and Bas1176
-
-
?
additional information
?
-
-
the enzyme performs autophosphorylation on several Ser/Thr residues and three Tyr residues, e.g. Ser162 or Tyr182 and two probable phospho residues Thr180 and Thr181 that are present in the activation loop of the PrkD catalytic domain
-
-
?
additional information
?
-
-
the enzyme is associated with nitrate dissimilation involving the NirV domain
-
-
?
additional information
?
-
the kinase domain of TAR1 shows auto- and transphosphorylation activities
-
-
?
additional information
?
-
the kinase domain of TAR1 shows auto- and transphosphorylation activities
-
-
?
additional information
?
-
-
the enzyme probably interacts with chaperonic proteins via tetratrico peptide repeats TPR
-
-
?
additional information
?
-
a role for tyrosine phosphorylation in controlling Dictyostelium development
-
-
?
additional information
?
-
regulates the differentiation of spore cells
-
-
?
additional information
?
-
-
the enzyme probably interacts with chaperonic proteins via tetratrico peptide repeats TPR
-
-
?
additional information
?
-
-
the enzyme autophosphorylates on both serine/threonine and tyrosine residues
-
-
?
additional information
?
-
-
the enzyme is associated to ubiquinone biosynthesis
-
-
?
additional information
?
-
the enzyme is associated with cell proliferation
-
-
?
additional information
?
-
-
the enzyme performs autophosphorylation at Thr202, Tyr72 and Tyr83, the enzyme also shows biliverdin reductase activity
-
-
?
additional information
?
-
DYRK1A-mediated phosphorylation of the beta-amyloid (Ab) precursor protein APP
-
-
?
additional information
?
-
-
DYRK1A-mediated phosphorylation of the beta-amyloid (Ab) precursor protein APP
-
-
?
additional information
?
-
increased dosage of Dyrk1A in brains of individuals with Down syndrome (DS) correlates to increased level of 3R-tau protein, abnormal hyperphosphorylation and aggregation of tau proteins, leads to neurofibrillary degeneration in Down syndrome
-
-
?
additional information
?
-
-
increased dosage of Dyrk1A in brains of individuals with Down syndrome (DS) correlates to increased level of 3R-tau protein, abnormal hyperphosphorylation and aggregation of tau proteins, leads to neurofibrillary degeneration in Down syndrome
-
-
?
additional information
?
-
participation in regulating tau phosphorylation, provides a novel mechanism leading to neurofibrillary pathology in Down syndrome
-
-
?
additional information
?
-
phosphorylation of viral protein E7 of human papillomvirus HPV16, DYRK1A increases the transforming potential of HPV16-infected cells because of the greater stability of phosphorylated HPV16E7
-
-
?
additional information
?
-
autophosphorylation of the tyrosine 246 residue within the activation loop is necessary for full DYRK4 kinase activity, no differences in tyrosine phosphorylation are evident for the long and the short human DYRK4 isoforms
-
-
?
additional information
?
-
autophosphorylation of Syk at Tyr630
-
-
?
additional information
?
-
-
the enzyme probably interacts with chaperonic proteins via tetratrico peptide repeats TPR
-
-
?
additional information
?
-
-
the enzyme is associated to ubiquinone biosynthesis
-
-
?
additional information
?
-
-
the enzyme is associated to ubiquinone biosynthesis
-
-
?
additional information
?
-
Esk kinase may play some role in the control of cell proliferation or differentiation
-
-
?
additional information
?
-
-
Esk kinase may play some role in the control of cell proliferation or differentiation
-
-
?
additional information
?
-
DYRK3 attenuates red cell production selectively during anemia
-
-
?
additional information
?
-
-
DYRK3 attenuates red cell production selectively during anemia
-
-
?
additional information
?
-
role of Dyrk1A in cognitive phenotypes of monosomy 21
-
-
?
additional information
?
-
-
Dyrk1A undergoes self-activation through autophosphorylation at Tyr 321
-
-
?
additional information
?
-
autophosphorylation of a tyrosine residue within the activation loop is necessary for full DYRK4 kinase activity
-
-
?
additional information
?
-
-
the enzyme probably interacts with chaperonic proteins via tetratrico peptide repeats TPR
-
-
?
additional information
?
-
-
the enzyme probably interacts with chaperonic proteins via tetratrico peptide repeats TPR
-
-
?
additional information
?
-
-
the enzyme is associated to ubiquinone biosynthesis
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of Mg-chelatase and chlorophyll biosynthesis
-
-
?
additional information
?
-
-
the enzyme of strain PCC 7120 contains a pectinesterase domain catalyzing the hydrolysis of pectin, the enzyme probably interacts with chaperonic proteins via tetratrico peptide repeats TPR
-
-
?
additional information
?
-
the enzyme is involved in response to plant abiotic and biotic stresses
-
-
?
additional information
?
-
the enzyme is involved in response to plant abiotic and biotic stresses
-
-
?
additional information
?
-
the enzyme is involved in response to plant abiotic and biotic stresses
-
-
?
additional information
?
-
the enzyme is involved in response to plant abiotic and biotic stresses
-
-
?
additional information
?
-
-
the enzyme probably interacts with chaperonic proteins via tetratrico peptide repeats TPR
-
-
?
additional information
?
-
activity is dependent on tyrosine residues between subdomains VII and VIII
-
-
?
additional information
?
-
a glutathione S-transferase fusion protein of Clk3 catalyzes autophosphorylation of the kinase but not phosphorylation of the exogenous substrates histone or casein
-
-
?
additional information
?
-
-
neither clathrin heavy chain nor endophilin 1 is phosphorylated by the Dyrk1A
-
-
?
additional information
?
-
-
the enzyme is associated to ubiquinone biosynthesis
-
-
?
additional information
?
-
-
the enzyme probably interacts with chaperonic proteins via tetratrico peptide repeats TPR
-
-
?
additional information
?
-
autophosphorylation
-
-
?
additional information
?
-
required for the execution of checkpoint arrest at multiple stages of the cell cycle. Rad53 modulates the lagging strand replication apparatus by controlling phosphorylation of the DNA polymerase alpha-primase complex in response to intra-S DNA damage
-
-
?
additional information
?
-
-
required for the execution of checkpoint arrest at multiple stages of the cell cycle. Rad53 modulates the lagging strand replication apparatus by controlling phosphorylation of the DNA polymerase alpha-primase complex in response to intra-S DNA damage
-
-
?
additional information
?
-
Rad53 exerts its role in checkpoint control through regulation of the Polo kinase Cdc5
-
-
?
additional information
?
-
the SAD1/RAD53 protein kinase controls multiple checkpoints and DNA damage-induced transcription in yeast
-
-
?
additional information
?
-
the enzyme is not essential for cell growth and a variety of other cellular processes in yeast
-
-
?
additional information
?
-
negative regulation of filamentous growth and flocculation
-
-
?
additional information
?
-
-
negative regulation of filamentous growth and flocculation
-
-
?
additional information
?
-
may function in a checkpoint control which couples DNA replication to mitosis. The level of the RPK1 transcript is extremely low and constant throughout the mitotic cycle. However it is regulated during cellular differentiation, being decreased in alpha-factor-treated cells and increased late in meiosis in alpha diploids. Rpk1 is involved in a pathway that coordinates cell proliferation and differentiation
-
-
?
additional information
?
-
-
may function in a checkpoint control which couples DNA replication to mitosis. The level of the RPK1 transcript is extremely low and constant throughout the mitotic cycle. However it is regulated during cellular differentiation, being decreased in alpha-factor-treated cells and increased late in meiosis in alpha diploids. Rpk1 is involved in a pathway that coordinates cell proliferation and differentiation
-
-
?
additional information
?
-
-
the enzyme probably interacts with chaperonic proteins via tetratrico peptide repeats TPR
-
-
?
additional information
?
-
-
the enzyme is associated to ubiquinone biosynthesis
-
-
?
additional information
?
-
-
the enzyme probably interacts with chaperonic proteins via tetratrico peptide repeats TPR
-
-
?
additional information
?
-
-
the enzyme is associated to ubiquinone biosynthesis
-
-
?
additional information
?
-
-
the enzyme is associated to ubiquinone biosynthesis
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + a protein
ADP + a phosphoprotein
ATP + adaptor protein SH2 domain-containing leukocyte protein
ADP + phospho-[adaptor protein SH2 domain-containing leukocyte protein]
phosphorylation of SLP-65 on several tyrosines
-
-
?
ATP + amphiphysin I
ADP + phosphorylated amphiphysin I
-
-
-
-
?
ATP + annexin 1
ADP + phospho-annexin 1
ATP + annexin 2
ADP + phospho-annexin 2
ATP + annexin 4
ADP + phospho-annexin 4
ATP + caspase-9
ADP + phosphorylated caspase-9
-
-
-
-
?
ATP + CREB
ADP + phosphorylated CREB
-
-
-
-
?
ATP + cyclin L2
ADP + phosphorylated cyclin L2
-
-
-
-
?
ATP + dynamin 1
ADP + phosphorylated dynamin 1
-
-
-
-
?
ATP + dynamin I
ADP + phosphorylated dynamin I
-
-
-
-
?
ATP + eIF2Bepsilon
ADP + phosphorylated eIF2Bepsilon
-
-
-
-
?
ATP + extracellular MAP kinase kinase
ADP + phospho-[MAP kinase kinase]
-
-
-
?
ATP + extracellular signal-regulated kinase
ADP + phospho-[extracellular signal-regulated kinase]
-
-
-
?
ATP + Gli1 protein
ADP + phosphorylated Gli1 protein
-
-
-
-
?
ATP + glycogen synthase
ADP + phosphorylated glycogen synthase
-
-
-
-
?
ATP + immunglobulin-alpha
ADP + phospho-[immunglobulin-alpha]
the inhibitory residue of Ig-alpha S197 is phosphorylated in activated B cells by Syk
-
-
?
ATP + insulin receptor kinase substrate 1
ADP + phosphorylated insulin receptor kinase substrate 1
-
phosphorylation at serine residues, overview, the enzyme is involved in the insulin signaling pathway
-
-
?
ATP + microtubule associated protein 1B
ADP + phosphorylated microtubule associated protein 1B
-
DYRK1A phosphorylates the S1392 site on microtubule associated protein 1B
-
-
?
ATP + neurodegeneration-related septin 4
ADP + phosphorylated neurodegeneration-related septin 4
SEPT4, also known as Pnutl2/CDCrel-2
-
-
?
ATP + NFAT
ADP + phosphorylated NFAT
-
-
-
-
?
ATP + Notch protein
ADP + phosphorylated Notch protein
-
-
-
-
?
ATP + p27
ADP + phospho-p27
-
p27 phosphorylation at Ser10 and Thr198
-
-
?
ATP + PRAS40
ADP + phospho-PRAS40
phosphorylation at Thr246
-
-
?
ATP + RNA binding family protein
ADP + phospho-RNA binding family protein
ATP + S6K1
ADP + phospho-S6K1
phosphorylation at Thr389
-
-
?
ATP + serine/arginine-rich protein 55
ADP + phospho-serine/arginine-rich protein 55
i.e. splicing factor SRp55, DYRK1a mainly phosphorylates the proline-rich domain of SRp55
-
-
?
ATP + SF3B1 protein-L-Thr434
ADP + [SF3B1 protein]-L-Thr434 phosphate
-
-
-
-
?
ATP + splicing factor 2
ADP + phosphorylated splicing factor 2
-
-
-
-
?
ATP + splicing factor 3
ADP + phosphorylated splicing factor 3
-
-
-
-
?
ATP + splicing factor 3B1
ADP + phosphorylated splicing factor 3B1
-
splicing factor 3B1 is poshorylated at Thr434
-
-
?
ATP + STAT3
ADP + phosphorylated STAT3
-
-
-
-
?
ATP + synaptojanin I
ADP + phosphorylated synaptojanin I
-
-
-
-
?
ATP + tau protein-L-Thr434
ADP + [tau protein]-L-Thr434 phosphate
-
-
-
-
?
ATP + transcription factor FKHR
ADP + phosphorylated transcription factor FKHR
-
-
-
-
?
biliverdin + ?
bilirubin + ?
-
-
-
-
?
additional information
?
-
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + annexin 1
ADP + phospho-annexin 1
phosphorylation at tyrosine and serine/threonine residues
-
-
?
ATP + annexin 1
ADP + phospho-annexin 1
phosphorylation at tyrosine and serine/threonine residues
-
-
?
ATP + annexin 2
ADP + phospho-annexin 2
phosphorylation at tyrosine and serine/threonine residues
-
-
?
ATP + annexin 2
ADP + phospho-annexin 2
phosphorylation at tyrosine and serine/threonine residues
-
-
?
ATP + annexin 4
ADP + phospho-annexin 4
phosphorylation at tyrosine residues
-
-
?
ATP + annexin 4
ADP + phospho-annexin 4
phosphorylation at tyrosine residues
-
-
?
ATP + RNA binding family protein
ADP + phospho-RNA binding family protein
phosphorylation at serine/threonine residues
-
-
?
ATP + RNA binding family protein
ADP + phospho-RNA binding family protein
phosphorylation at serine/threonine residues
-
-
?
ATP + SR protein
ADP + ?
the enzyme is required in distinct neuroblast proliferation centers during postembryonic neurogenesis
-
-
?
ATP + SR protein
ADP + ?
-
-
-
?
ATP + SR protein
ADP + ?
enzyme is involved in the regulation of nuclear functions
-
-
?
ATP + SR protein
ADP + ?
DYRK may be involved in the abnormal neurogenesis found in Down syndrome
-
-
?
ATP + SR protein
ADP + ?
MNB protein may play a significant role in a signaling pathway regulating nuclear functions of neuronal cell proliferation, contributing to certain features of Down syndrome
-
-
?
ATP + SR protein
ADP + ?
-
-
-
?
ATP + SR protein
ADP + ?
enzyme may be involved in cell cycle control
-
-
?
ATP + SR protein
ADP + ?
enzyme is a good candidate to mediate some of the pleiotropic effects of Down syndrome
-
-
?
ATP + SR protein
ADP + ?
enzyme may be constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing
-
-
?
ATP + SR protein
ADP + ?
the enzyme phosphorylates SR splicing factors and regulates their intranuclear distribution
-
-
?
ATP + SR protein
ADP + ?
might be a component of a signaling pathway regulating nuclear functions
-
-
?
ATP + SR protein
ADP + ?
enzyme regulates a predominately testicular function
-
-
?
ATP + SR protein
ADP + ?
functions as a negative regulator of the cell cycle in Saccharomyces cerevisiae, acting downstream of the cAMP-dependent protein kinase
-
-
?
ATP + SR protein
ADP + ?
Yak1 acts downstream from, or on a parallel pathway to, the kinase step in the Ras/cAMP pathway
-
-
?
ATP + SR protein
ADP + ?
Yak1p and Pop2p are part of a novel glucose-sensing system in yeast that is involved in growth control in response to glucose availability
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of Mg-chelatase and chlorophyll biosynthesis
-
-
?
additional information
?
-
-
the enzyme is developmentally regulated
-
-
?
additional information
?
-
-
the enzyme is developmentally regulated
-
-
?
additional information
?
-
-
PrkG is a unique dual specificity protein kinase that mediates autophosphorylation and substrate phosphorylation on Ser, Thr, and Tyr residues
-
-
?
additional information
?
-
-
the enzyme is associated with nitrate dissimilation involving the NirV domain
-
-
?
additional information
?
-
a role for tyrosine phosphorylation in controlling Dictyostelium development
-
-
?
additional information
?
-
regulates the differentiation of spore cells
-
-
?
additional information
?
-
-
the enzyme is associated to ubiquinone biosynthesis
-
-
?
additional information
?
-
the enzyme is associated with cell proliferation
-
-
?
additional information
?
-
autophosphorylation of the tyrosine 246 residue within the activation loop is necessary for full DYRK4 kinase activity, no differences in tyrosine phosphorylation are evident for the long and the short human DYRK4 isoforms
-
-
?
additional information
?
-
-
the enzyme is associated to ubiquinone biosynthesis
-
-
?
additional information
?
-
-
the enzyme is associated to ubiquinone biosynthesis
-
-
?
additional information
?
-
Esk kinase may play some role in the control of cell proliferation or differentiation
-
-
?
additional information
?
-
-
Esk kinase may play some role in the control of cell proliferation or differentiation
-
-
?
additional information
?
-
-
Dyrk1A undergoes self-activation through autophosphorylation at Tyr 321
-
-
?
additional information
?
-
autophosphorylation of a tyrosine residue within the activation loop is necessary for full DYRK4 kinase activity
-
-
?
additional information
?
-
-
the enzyme is associated to ubiquinone biosynthesis
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of Mg-chelatase and chlorophyll biosynthesis
-
-
?
additional information
?
-
the enzyme is involved in response to plant abiotic and biotic stresses
-
-
?
additional information
?
-
the enzyme is involved in response to plant abiotic and biotic stresses
-
-
?
additional information
?
-
the enzyme is involved in response to plant abiotic and biotic stresses
-
-
?
additional information
?
-
the enzyme is involved in response to plant abiotic and biotic stresses
-
-
?
additional information
?
-
-
neither clathrin heavy chain nor endophilin 1 is phosphorylated by the Dyrk1A
-
-
?
additional information
?
-
-
the enzyme is associated to ubiquinone biosynthesis
-
-
?
additional information
?
-
required for the execution of checkpoint arrest at multiple stages of the cell cycle. Rad53 modulates the lagging strand replication apparatus by controlling phosphorylation of the DNA polymerase alpha-primase complex in response to intra-S DNA damage
-
-
?
additional information
?
-
-
required for the execution of checkpoint arrest at multiple stages of the cell cycle. Rad53 modulates the lagging strand replication apparatus by controlling phosphorylation of the DNA polymerase alpha-primase complex in response to intra-S DNA damage
-
-
?
additional information
?
-
Rad53 exerts its role in checkpoint control through regulation of the Polo kinase Cdc5
-
-
?
additional information
?
-
the SAD1/RAD53 protein kinase controls multiple checkpoints and DNA damage-induced transcription in yeast
-
-
?
additional information
?
-
the enzyme is not essential for cell growth and a variety of other cellular processes in yeast
-
-
?
additional information
?
-
negative regulation of filamentous growth and flocculation
-
-
?
additional information
?
-
-
negative regulation of filamentous growth and flocculation
-
-
?
additional information
?
-
may function in a checkpoint control which couples DNA replication to mitosis. The level of the RPK1 transcript is extremely low and constant throughout the mitotic cycle. However it is regulated during cellular differentiation, being decreased in alpha-factor-treated cells and increased late in meiosis in alpha diploids. Rpk1 is involved in a pathway that coordinates cell proliferation and differentiation
-
-
?
additional information
?
-
-
may function in a checkpoint control which couples DNA replication to mitosis. The level of the RPK1 transcript is extremely low and constant throughout the mitotic cycle. However it is regulated during cellular differentiation, being decreased in alpha-factor-treated cells and increased late in meiosis in alpha diploids. Rpk1 is involved in a pathway that coordinates cell proliferation and differentiation
-
-
?
additional information
?
-
-
the enzyme is associated to ubiquinone biosynthesis
-
-
?
additional information
?
-
-
the enzyme is associated to ubiquinone biosynthesis
-
-
?
additional information
?
-
-
the enzyme is associated to ubiquinone biosynthesis
-
-
?
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(1Z)-1-(3-ethyl-5-methoxy-1,3-benzothiazol-2(3H)-ylidene)propan-2-one
-
(4Z)-1-(3,4-dichlorophenyl)-4-(4-hydroxy-3-methoxybenzylidene)pyrazolidine-3,5-dione
-
82.6% inhibition at 0.01 mM
(4Z)-1-(3,4-dichlorophenyl)-4-(4-hydroxy-3-nitrobenzylidene)pyrazolidine-3,5-dione
-
76% inhibition at 0.01 mM
(4Z)-1-(3,4-dichlorophenyl)-4-(4-hydroxybenzylidene)pyrazolidine-3,5-dione
-
73% inhibition at 0.01 mM
(4Z)-1-(4-fluorophenyl)-4-(4-hydroxy-3-methoxybenzylidene)pyrazolidine-3,5-dione
-
44% inhibition at 0.01 mM
(4Z)-4-(4-hydroxy-3-methoxybenzylidene)-1-(4-methoxyphenyl)pyrazolidine-3,5-dione
-
55% inhibition at 0.01 mM
(5-[4-[ethyl(thiophen-2-ylmethyl)amino]quinazolin-6-yl]furan-2-yl)methanol
-
(5-{4-[(5-methylfuran-2-yl)amino]quinazolin-6-yl}furan-2-yl)methanol
-
(5-{4-[methyl(3-methylthiophen-2-yl)amino]quinazolin-6-yl}furan-2-yl)methanol
-
(5Z)-2-(2,6-dichloroanilino)-5-(quinoxalin-6-ylmethylidene)-1,3-thiazol-4-one
i.e. GSK-626616, the DYRK kinase inhibitor GSK-626616 affects, among others, the phosphorylation of mRNA-associated proteins and proteins downstream of mTORC1 signaling
2-(1,3-benzodioxol-5-yl)-N-(3,4-dichlorobenzyl)pyrimidin-4-amine
-
2-(1,3-benzodioxol-5-yl)-N-(4-chlorobenzyl)pyrimidin-4-amine
-
2-(1,3-benzodioxol-5-yl)-N-(pyridin-3-ylmethyl)pyrimidin-4-amine
-
2-(1H-indazol-5-yl)-N-(pyridin-3-ylmethyl)pyrimidin-4-amine
-
2-(1H-indazol-6-yl)-N-(pyridin-3-ylmethyl)pyrimidin-4-amine
-
2-methyl-5-[(4-methylphenyl)amino]benzothiazole-4,7-dione
i.e. CDK4 inhibitor III
3-(N-benzyl-N-isopropyl)amino-1-(naphthalen-2-yl)propan-1-one hydrochloride
i.e. Jak3 inhibitor IV
3-[4-(2-phenylethyl)quinazolin-6-yl]benzonitrile
-
3-[4-[2-(4-methoxyphenyl)ethyl]quinazolin-6-yl]benzonitrile
-
3-[4-[2-(4-methylphenyl)ethyl]quinazolin-6-yl]benzonitrile
-
4-(1,3-benzodioxol-5-yl)-N-(3,4-dibromobenzyl)pyrimidin-2-amine
-
4-(1,3-benzodioxol-5-yl)-N-(3,4-dichlorobenzyl)pyrimidin-2-amine
-
4-(1,3-benzodioxol-5-yl)-N-(3,5-dibromobenzyl)pyrimidin-2-amine
-
4-(1,3-benzodioxol-5-yl)-N-(3,5-dichlorobenzyl)pyrimidin-2-amine
-
4-(1,3-benzodioxol-5-yl)-N-(4-chlorobenzyl)pyrimidin-2-amine
-
4-(1,3-benzodioxol-5-yl)-N-(4-chlorophenyl)pyrimidin-2-amine
-
4-(1,3-benzodioxol-5-yl)-N-(pyridin-3-ylmethyl)pyrimidin-2-amine
-
4-(1,3-benzodioxol-5-yl)-N-[2-bromo-4-(trifluoromethyl)phenyl]pyrimidin-2-amine
-
4-(1,3-benzodioxol-5-yl)-N-[4-(trifluoromethyl)phenyl]pyrimidin-2-amine
-
4-(1H-indazol-5-yl)-N-(pyridin-3-ylmethyl)pyrimidin-2-amine
-
4-(1H-indazol-6-yl)-N-(pyridin-3-ylmethyl)pyrimidin-2-amine
-
4-(2-phenyl)-9-hydroxypyrrolo[3,4-c]carbazole-1,3-(2H,6H)-dione
i.e. Wee1/Chk1 inhibitor
4-(6-cyclohexylmethoxy-9H-purin-2-ylamino)-N,N-diethylbenzamide
i.e. CDK2 inhibitor IV
4-[(4Z)-4-(4-hydroxy-3-methoxybenzylidene)-3,5-dioxopyrazolidin-1-yl]benzonitrile
-
78% inhibition at 0.01 mM
5-chloro-3-(3,5-dichloro-4-hydroxybenzylidene)-1,3-dihydro-indol-2-one
i.e. HMS3229I17, a CDK2 inhibitor IV
5-[4-(thiophen-2-ylamino)quinazolin-6-yl]furan-2-carboxylic acid
-
5-{4-[(5-methylfuran-2-yl)amino]quinazolin-6-yl}furan-2-carboxylic acid
-
6-(1,3-benzodioxol-5-yl)-N-(1,3-thiazol-2-yl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-(1,3-thiazol-2-ylmethyl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-(1H-imidazol-2-yl)-N-methylquinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-(1H-imidazol-2-yl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-(1H-imidazol-2-ylmethyl)-N-methylquinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-(1H-imidazol-2-ylmethyl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-(1H-imidazol-4-ylmethyl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-(2,2-dimethylpropyl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-(2-methyl-1,3-thiazol-4-yl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-(2-methylfuran-3-yl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-(3,4-dichlorobenzyl)pyrimidin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-(3,5-dichlorobenzyl)pyrimidin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-(3,5-dichlorobenzyl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-(3-methylthiophen-2-yl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-(4-chlorobenzyl)pyrimidin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-(4-methoxybenzyl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-(5-methylfuran-2-yl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-(5-methylthiophen-2-yl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-(cyclopentylmethyl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-(furan-2-yl)-N-methylquinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-(furan-2-yl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-(furan-2-ylmethyl)-N-methylquinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-(furan-2-ylmethyl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-(furan-3-yl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-(furan-3-ylmethyl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-(pyridin-3-ylmethyl)pyrimidin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-(tetrahydro-2H-pyran-2-ylmethyl)quinazolin-4-amine
-
-
6-(1,3-benzodioxol-5-yl)-N-(tetrahydro-2H-pyran-3-yl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-(tetrahydrofuran-2-yl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-(tetrahydrofuran-2-ylmethyl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-(tetrahydrofuran-3-yl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-(tetrahydrofuran-3-ylmethyl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-(thiophen-2-yl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-(thiophen-2-ylmethyl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-benzylquinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-cyclopentylquinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-ethyl-N-(thiophen-2-yl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-ethyl-N-(thiophen-2-ylmethyl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-methyl-N-(1,3-thiazol-2-yl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-methyl-N-(1,3-thiazol-2-ylmethyl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-methyl-N-(2-methyl-1,3-thiazol-4-yl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-methyl-N-(3-methylthiophen-2-yl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-methyl-N-(4-methyl-1,3-thiazol-2-yl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-methyl-N-(5-methyl-1,3,4-oxadiazol-2-yl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-methyl-N-(thiophen-2-yl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-methyl-N-(thiophen-2-ylmethyl)quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-methyl-N-[(3-methylthiophen-2-yl)methyl]quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-methyl-N-[(4-methyl-1,3-thiazol-2-yl)methyl]quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-methyl-N-[(5-methyl-1,3,4-oxadiazol-2-yl)methyl]quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-[(2-methylfuran-3-yl)methyl]quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-[(3-methylthiophen-2-yl)methyl]quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-[(4-methyl-1,3-thiazol-2-yl)methyl]quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-[(5-methylfuran-2-yl)methyl]quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-[(5-methylthiophen-2-yl)methyl]quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-[2-(1H-imidazol-4-yl)ethyl]quinazolin-4-amine
-
6-(1,3-benzodioxol-5-yl)-N-[2-(furan-2-yl)ethyl]quinazolin-4-amine
-
6-(1-methyl-1H-indazol-6-yl)-N-(thiophen-2-yl)quinazolin-4-amine
-
6-(1-methyl-1H-indol-5-yl)-N-(thiophen-2-yl)quinazolin-4-amine
-
6-(1-methyl-1H-indol-5-yl)-N-(thiophen-2-ylmethyl)quinazolin-4-amine
-
6-(2,3-dihydro-1,4-benzodioxin-6-yl)-N-(thiophen-2-ylmethyl)quinazolin-4-amine
-
6-(2-chlorophenyl)-N-(thiophen-2-yl)quinazolin-4-amine
-
6-(2-chlorophenyl)-N-(thiophen-2-ylmethyl)quinazolin-4-amine
-
6-(2-methylfuran-3-yl)-N-(5-methylfuran-2-yl)quinazolin-4-amine
-
6-(2-methylfuran-3-yl)-N-[(5-methylfuran-2-yl)methyl]quinazolin-4-amine
-
6-(3,4-dimethoxyphenyl)-N-(thiophen-2-yl)quinazolin-4-amine
-
6-(3-chlorophenyl)-N-(thiophen-2-yl)quinazolin-4-amine
-
6-(3-methoxyphenyl)-N-(4-methylbenzyl)quinazolin-4-amine
-
6-(3-methoxyphenyl)-N-(thiophen-2-yl)quinazolin-4-amine
-
6-(3-methoxyphenyl)-N-(thiophen-2-ylmethyl)quinazolin-4-amine
-
6-(3-methoxyphenyl)quinazoline
-
6-(3-methylphenyl)-N-(thiophen-2-yl)quinazolin-4-amine
-
6-(4-fluoro-1,3-benzodioxol-5-yl)-N-(thiophen-2-yl)quinazolin-4-amine
-
6-(4-fluoro-1,3-benzodioxol-5-yl)-N-(thiophen-2-ylmethyl)quinazolin-4-amine
-
6-(4-methoxyphenyl)-N-(thiophen-2-yl)quinazolin-4-amine
-
6-(4-methoxyphenyl)-N-(thiophen-2-ylmethyl)quinazolin-4-amine
-
6-(furan-2-yl)-N-(thiophen-2-yl)quinazolin-4-amine
-
6-(furan-2-yl)-N-(thiophen-2-ylmethyl)quinazolin-4-amine
-
6-(furan-3-yl)-N-(2-methyl-1,3-thiazol-4-yl)quinazolin-4-amine
-
6-(furan-3-yl)-N-(thiophen-2-yl)quinazolin-4-amine
-
6-(furan-3-yl)-N-(thiophen-2-ylmethyl)quinazolin-4-amine
-
6-(furan-3-yl)-N-methyl-N-(3-methylthiophen-2-yl)quinazolin-4-amine
-
6-(furan-3-yl)-N-methyl-N-[(3-methylthiophen-2-yl)methyl]quinazolin-4-amine
-
6-(furan-3-yl)-N-[(2-methyl-1,3-thiazol-4-yl)methyl]quinazolin-4-amine
-
6-(pyridin-3-yl)-N-(thiophen-2-yl)quinazolin-4-amine
-
7-(1,3-benzodioxol-5-yl)-N-(thiophen-2-yl)quinazolin-4-amine
-
7-methoxy-1-methyl-9H-pyrido[3,4-b]indole
i.e. harmine
ethyl 5-(4-[[(2-methyl-1,3-thiazol-4-yl)methyl]amino]quinazolin-6-yl)furan-2-carboxylate
-
ethyl 5-(4-[[(3-methylthiophen-2-yl)methyl]amino]quinazolin-6-yl)furan-2-carboxylate
-
ethyl 5-(4-[[(5-methylfuran-2-yl)methyl]amino]quinazolin-6-yl)furan-2-carboxylate
-
ethyl 5-(4-[[2-(1H-imidazol-4-yl)ethyl]amino]quinazolin-6-yl)furan-2-carboxylate
-
ethyl 5-[4-(1H-imidazol-2-ylamino)quinazolin-6-yl]furan-2-carboxylate
-
ethyl 5-[4-(thiophen-2-ylamino)quinazolin-6-yl]furan-2-carboxylate
-
ethyl 5-[4-[(1H-imidazol-2-ylmethyl)amino]quinazolin-6-yl]furan-2-carboxylate
-
ethyl 5-[4-[ethyl(thiophen-2-ylmethyl)amino]quinazolin-6-yl]furan-2-carboxylate
-
ethyl 5-{4-[(1H-imidazol-4-ylmethyl)amino]quinazolin-6-yl}furan-2-carboxylate
-
ethyl 5-{4-[(2-methyl-1,3-thiazol-4-yl)amino]quinazolin-6-yl}furan-2-carboxylate
-
ethyl 5-{4-[(5-methylfuran-2-yl)amino]quinazolin-6-yl}furan-2-carboxylate
-
ethyl 5-{4-[methyl(3-methylthiophen-2-yl)amino]quinazolin-6-yl}furan-2-carboxylate
-
GSK-626616
i.e. (5Z)-2-(2,6-dichloroanilino)-5-[(quinoxalin-6-yl)methylidene]-1,3-thiazol-4(5H)-one, ATP competitive inhibitor
HCD160
-
82.6% inhibition at 0.01 mM
leucettamine B
marine alkaloid, strong inhibitor
midostaurin
i.e. PKC412, a derivative of the broad-spectrum kinase inhibitor staurosporine, an alkaloid isolated from Streptomyces staurosoreus; i.e. PKC412, a derivative of the broad-spectrum kinase inhibitor staurosporine, an alkaloid isolated from Streptomyces staurosoreus. Enzyme binding structure analysis, overview
N,4-bis(1,3-benzodioxol-5-yl)pyrimidin-2-amine
-
N-(2,2-dimethylpropyl)-6-[5-[(ethylamino)methyl]furan-2-yl]quinazolin-4-amine
-
N-(3,4-dichlorobenzyl)-2-(1H-indazol-5-yl)pyrimidin-4-amine
-
N-(3,4-dichlorobenzyl)-4-(1H-indazol-5-yl)pyrimidin-2-amine
-
N-(3,4-dichlorobenzyl)-4-(1H-indazol-6-yl)pyrimidin-2-amine
-
N-(3,4-dichlorobenzyl)-4-(2,3-dihydro-1,4-benzodioxin-6-yl)pyrimidin-2-amine
-
N-(3,4-dichlorobenzyl)-4-(3,4-dimethoxyphenyl)pyrimidin-2-amine
-
N-(3,4-dichlorobenzyl)-4-(3-methoxyphenyl)pyrimidin-2-amine
-
N-(3,4-dichlorobenzyl)-4-(4-methoxyphenyl)pyrimidin-2-amine
-
N-(3,4-dichlorobenzyl)-6-(pyridin-3-yl)quinazolin-4-amine
-
N-(4-chlorobenzyl)-4-(3-methoxyphenyl)pyrimidin-2-amine
-
N-(4-chlorobenzyl)-4-(4-methoxyphenyl)pyrimidin-2-amine
-
N-(4-chlorobenzyl)-6-(3-methoxyphenyl)quinazolin-4-amine
-
N-(4-chlorobenzyl)-6-(pyridin-3-yl)quinazolin-4-amine
-
N-(4-methoxybenzyl)-6-(3-methoxyphenyl)quinazolin-4-amine
-
N-(4-methoxybenzyl)-6-(pyridin-3-yl)quinazolin-4-amine
-
N-(thiophen-2-yl)-6-(3,4,5-trimethoxyphenyl)quinazolin-4-amine
-
N-tert-butyl-6-{5-[(ethylamino)methyl]furan-2-yl}quinazolin-4-amine
-
N6-Dimethylaminopurine
-
unspecific inhibitor of protein kinases
RAD-001
a rapamycin derivative
-
roscovitine
-
63% inhibition at 0.01 mM
tyrphostin
-
competitive versus ATP, mixed inhibition versus histone H1
Zn2+
-
inhibits the autophosphoylation, which cannot be reversed by Mn2+ addition
[5-(4-[methyl[(3-methylthiophen-2-yl)methyl]amino]quinazolin-6-yl)furan-2-yl]methanol
-
{5-[4-(thiophen-2-ylamino)quinazolin-6-yl]furan-2-yl}methanol
-
genistein
-
competitive inhibition versus ATP, uncompetitive inhibition versus histone H1
genistein
-
inhibits the enzyme and affects Bacillus anthracis cell growth
genistein
-
protein tyrosine kinase inhibitor
harmine
-
-
harmine
-
potent and specific inhibitor of DYRK1A both in vitro and in cultured cells, harmine inhibits DYRK1A substrate phosphorylation more potently than it inhibits tyrosine autophosphorylation; potent and specific inhibitor of DYRK1A, inhibits DYRK1A substrate phosphorylation more potently than it inhibits tyrosine autophosphorylation
harmine
a plant-derived beta-carboline alkaloid, ATP-competitive; a plant-derived beta-carboline alkaloid, ATP-competitive
harmine
ATP competitive inhibitor
harmine
specific inhibitor of DYRK1A
staurosporine
-
competitive versus ATP, mixed inhibition versus histone H1
staurosporine
-
unspecific inhibitor of protein kinases
additional information
-
molecular docking with tyrosine kinase inhibitors, recombinant His-tagged wild-type and mutant enzymes
-
additional information
drought stress decreased the expression level
-
additional information
-
drought stress decreased the expression level
-
additional information
analysis of highly selective substituted pyrimidine inhibitors of the Dyrk kinase Dyrk1A, structure-activity relationships, overview. No inhibition by 6-(1,3-benzodioxol-5-yl)-N-(3,4-dichlorobenzyl)quinazolin-4-amine6-(1,3-benzodioxol-5-yl)-N-(3,4-dichlorobenzyl)quinazolin-4-amine, 6-(1,3-benzodioxol-5-yl)-N-(4-methylbenzyl)quinazolin-4-amine, 6-(1,3-benzodioxol-5-yl)-N-(4-chlorobenzyl)quinazolin-4-amine, 6-(1,3-benzodioxol-5-yl)quinazoline, 3-(quinazolin-6-yl)benzonitrile, N-(3,4-dichlorobenzyl)-6-(3-methoxyphenyl)quinazolin-4-amine, N-benzyl-6-(3,5-dimethyl-1,2-oxazol-4-yl)quinazolin-4-amine, N-(3,4-dichlorobenzyl)-6-(3,5-dimethyl-1,2-oxazol-4-yl)quinazolin-4-amine, 6-(3,5-dimethyl-1,2-oxazol-4-yl)-N-(4-methylbenzyl)quinazolin-4-amine, N-(4-chlorobenzyl)-6-(3,5-dimethyl-1,2-oxazol-4-yl)quinazolin-4-amine, 6-(3,5-dimethyl-1,2-oxazol-4-yl)-N-(4-methoxybenzyl)quinazolin-4-amine, 6-(3,5-dimethyl-1,2-oxazol-4-yl)quinazoline, N-benzyl-6-[4-(dimethylamino)phenyl]quinazolin-4-amine, N-(3,4-dichlorobenzyl)-6-[4-(dimethylamino)phenyl]quinazolin-4-amine, 6-[4-(dimethylamino)phenyl]-N-(4-methylbenzyl)quinazolin-4-amine, N-(4-chlorobenzyl)-6-[4-(dimethylamino)phenyl]quinazolin-4-amine, 6-[4-(dimethylamino)phenyl]-N-(4-methoxybenzyl)quinazolin-4-amine, N,N-dimethyl-4-(quinazolin-6-yl)aniline, N-(4-methylbenzyl)-6-(pyridin-3-yl)quinazolin-4-amine, and N-benzyl-6-(4-methoxyphenyl)quinazolin-4-amine, N-(3,4-dichlorobenzyl)-6-(4-methoxyphenyl)quinazolin-4-amine, 6-(4-methoxyphenyl)-N-(4-methylbenzyl)quinazolin-4-amine, N-(4-chlorobenzyl)-6-(4-methoxyphenyl)quinazolin-4-amine, N-(4-methoxybenzyl)-6-(4-methoxyphenyl)quinazolin-4-amine, and 6-(4-methoxyphenyl)quinazoline; analysis of highly selective substituted pyrimidine inhibitors of the Dyrk kinase Dyrk1B, structure-activity relationships, overview. No inhibition by N-(3,4-dichlorobenzyl)-4-(3,4-dimethoxyphenyl)pyrimidin-2-amine
-
additional information
analysis of highly selective substituted pyrimidine inhibitors of the Dyrk kinase Dyrk1A, structure-activity relationships, overview. No inhibition by 6-(1,3-benzodioxol-5-yl)-N-(3,4-dichlorobenzyl)quinazolin-4-amine6-(1,3-benzodioxol-5-yl)-N-(3,4-dichlorobenzyl)quinazolin-4-amine, 6-(1,3-benzodioxol-5-yl)-N-(4-methylbenzyl)quinazolin-4-amine, 6-(1,3-benzodioxol-5-yl)-N-(4-chlorobenzyl)quinazolin-4-amine, 6-(1,3-benzodioxol-5-yl)quinazoline, 3-(quinazolin-6-yl)benzonitrile, N-(3,4-dichlorobenzyl)-6-(3-methoxyphenyl)quinazolin-4-amine, N-benzyl-6-(3,5-dimethyl-1,2-oxazol-4-yl)quinazolin-4-amine, N-(3,4-dichlorobenzyl)-6-(3,5-dimethyl-1,2-oxazol-4-yl)quinazolin-4-amine, 6-(3,5-dimethyl-1,2-oxazol-4-yl)-N-(4-methylbenzyl)quinazolin-4-amine, N-(4-chlorobenzyl)-6-(3,5-dimethyl-1,2-oxazol-4-yl)quinazolin-4-amine, 6-(3,5-dimethyl-1,2-oxazol-4-yl)-N-(4-methoxybenzyl)quinazolin-4-amine, 6-(3,5-dimethyl-1,2-oxazol-4-yl)quinazoline, N-benzyl-6-[4-(dimethylamino)phenyl]quinazolin-4-amine, N-(3,4-dichlorobenzyl)-6-[4-(dimethylamino)phenyl]quinazolin-4-amine, 6-[4-(dimethylamino)phenyl]-N-(4-methylbenzyl)quinazolin-4-amine, N-(4-chlorobenzyl)-6-[4-(dimethylamino)phenyl]quinazolin-4-amine, 6-[4-(dimethylamino)phenyl]-N-(4-methoxybenzyl)quinazolin-4-amine, N,N-dimethyl-4-(quinazolin-6-yl)aniline, N-(4-methylbenzyl)-6-(pyridin-3-yl)quinazolin-4-amine, and N-benzyl-6-(4-methoxyphenyl)quinazolin-4-amine, N-(3,4-dichlorobenzyl)-6-(4-methoxyphenyl)quinazolin-4-amine, 6-(4-methoxyphenyl)-N-(4-methylbenzyl)quinazolin-4-amine, N-(4-chlorobenzyl)-6-(4-methoxyphenyl)quinazolin-4-amine, N-(4-methoxybenzyl)-6-(4-methoxyphenyl)quinazolin-4-amine, and 6-(4-methoxyphenyl)quinazoline; analysis of highly selective substituted pyrimidine inhibitors of the Dyrk kinase Dyrk1B, structure-activity relationships, overview. No inhibition by N-(3,4-dichlorobenzyl)-4-(3,4-dimethoxyphenyl)pyrimidin-2-amine
-
additional information
synthesis and evaluation of a series of 6-arylquinazolin-4-amine inhibitors as potential enzyme inhibitors, hologram quantitative structure-activity relationship (QSAR) studies, molecular modeling, overview
-
additional information
synthesis and evaluation of a series of 6-arylquinazolin-4-amine inhibitors as enzyme inhibitors, three-dimensional quantitative structure-activity relationship (3D-QSAR) studies, binding mode from docking studies, molecular homology modeling, overview. A hydrogen bond between ligand and the counterpart Lys 188 in Dyrk1A is present in part of the crystal structures of Dyrk1A (PDB IDs 3ANQ and 3ANR). By contrast, the involvement of the residue at the same position as Leu242 in the hydrogen bond interaction is available in all identified Dyrk1A structures (PDB IDs: 3ANQ, 3ANR, 2WO6, and 2VX3)
-
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0.0025
(4Z)-1-(3,4-dichlorophenyl)-4-(4-hydroxy-3-methoxybenzylidene)pyrazolidine-3,5-dione
Homo sapiens
-
for autophosphorylation
0.0006
(4Z)-1-(3,4-dichlorophenyl)-4-(4-hydroxy-3-nitrobenzylidene)pyrazolidine-3,5-dione
Homo sapiens
-
for autophosphorylation
0.0025
(4Z)-1-(3,4-dichlorophenyl)-4-(4-hydroxybenzylidene)pyrazolidine-3,5-dione
Homo sapiens
-
for autophosphorylation
0.0025
(4Z)-1-(4-fluorophenyl)-4-(4-hydroxy-3-methoxybenzylidene)pyrazolidine-3,5-dione
Homo sapiens
-
for autophosphorylation
0.0012
(4Z)-4-(4-hydroxy-3-methoxybenzylidene)-1-(4-methoxyphenyl)pyrazolidine-3,5-dione
Homo sapiens
-
for autophosphorylation
3.454 - 10
2-(1,3-benzodioxol-5-yl)-N-(3,4-dichlorobenzyl)pyrimidin-4-amine
4.579 - 8.862
2-(1,3-benzodioxol-5-yl)-N-(4-chlorobenzyl)pyrimidin-4-amine
10
2-(1,3-benzodioxol-5-yl)-N-(pyridin-3-ylmethyl)pyrimidin-4-amine
Homo sapiens
above, pH and temperature not specified in the publication
0.179 - 0.349
2-(1H-indazol-5-yl)-N-(pyridin-3-ylmethyl)pyrimidin-4-amine
0.829 - 1.434
2-(1H-indazol-6-yl)-N-(pyridin-3-ylmethyl)pyrimidin-4-amine
0.0164
3-[4-[2-(4-methoxyphenyl)ethyl]quinazolin-6-yl]benzonitrile
Homo sapiens
pH and temperature not specified in the publication
0.0412
3-[4-[2-(4-methylphenyl)ethyl]quinazolin-6-yl]benzonitrile
Homo sapiens
pH and temperature not specified in the publication
0.018 - 0.112
4-(1,3-benzodioxol-5-yl)-N-(3,4-dibromobenzyl)pyrimidin-2-amine
0.014 - 0.038
4-(1,3-benzodioxol-5-yl)-N-(3,4-dichlorobenzyl)pyrimidin-2-amine
0.009 - 0.018
4-(1,3-benzodioxol-5-yl)-N-(3,5-dibromobenzyl)pyrimidin-2-amine
0.004 - 0.007
4-(1,3-benzodioxol-5-yl)-N-(3,5-dichlorobenzyl)pyrimidin-2-amine
0.273 - 0.884
4-(1,3-benzodioxol-5-yl)-N-(4-chlorophenyl)pyrimidin-2-amine
0.012 - 0.016
4-(1,3-benzodioxol-5-yl)-N-(pyridin-3-ylmethyl)pyrimidin-2-amine
0.107 - 0.137
4-(1,3-benzodioxol-5-yl)-N-[2-bromo-4-(trifluoromethyl)phenyl]pyrimidin-2-amine
0.01 - 0.018
4-(1,3-benzodioxol-5-yl)-N-[4-(trifluoromethyl)phenyl]pyrimidin-2-amine
0.061 - 0.093
4-(1H-indazol-5-yl)-N-(pyridin-3-ylmethyl)pyrimidin-2-amine
0.0006
4-[(4Z)-4-(4-hydroxy-3-methoxybenzylidene)-3,5-dioxopyrazolidin-1-yl]benzonitrile
Homo sapiens
-
for autophosphorylation
0.282 - 1.156
6-(1,3-benzodioxol-5-yl)-N-(3,5-dichlorobenzyl)quinazolin-4-amine
0.0463
6-(1,3-benzodioxol-5-yl)-N-(4-methoxybenzyl)quinazolin-4-amine
Homo sapiens
pH and temperature not specified in the publication
0.026
6-(1,3-benzodioxol-5-yl)-N-benzylquinazolin-4-amine
Homo sapiens
pH and temperature not specified in the publication
0.0654
6-(3-methoxyphenyl)-N-(4-methylbenzyl)quinazolin-4-amine
Homo sapiens
pH and temperature not specified in the publication
0.026
6-(3-methoxyphenyl)quinazoline
Homo sapiens
pH and temperature not specified in the publication
0.00004
leucettine L-41
Homo sapiens
pH and temperature not specified in the publication
0.000059 - 0.000066
midostaurin
0.025 - 0.042
N,4-bis(1,3-benzodioxol-5-yl)pyrimidin-2-amine
0.514 - 2.352
N-(3,4-dichlorobenzyl)-2-(1H-indazol-5-yl)pyrimidin-4-amine
0.0129 - 0.125
N-(3,4-dichlorobenzyl)-4-(1H-indazol-5-yl)pyrimidin-2-amine
0.0169 - 0.599
N-(3,4-dichlorobenzyl)-4-(1H-indazol-6-yl)pyrimidin-2-amine
0.013 - 0.055
N-(3,4-dichlorobenzyl)-4-(2,3-dihydro-1,4-benzodioxin-6-yl)pyrimidin-2-amine
10
N-(3,4-dichlorobenzyl)-4-(3,4-dimethoxyphenyl)pyrimidin-2-amine
Homo sapiens
above, pH and temperature not specified in the publication
4.654 - 10
N-(3,4-dichlorobenzyl)-4-(3-methoxyphenyl)pyrimidin-2-amine
0.203 - 0.411
N-(3,4-dichlorobenzyl)-4-(4-methoxyphenyl)pyrimidin-2-amine
0.0412
N-(3,4-dichlorobenzyl)-6-(pyridin-3-yl)quinazolin-4-amine
Homo sapiens
pH and temperature not specified in the publication
6.361 - 6.782
N-(4-chlorobenzyl)-4-(3-methoxyphenyl)pyrimidin-2-amine
0.558 - 0.871
N-(4-chlorobenzyl)-4-(4-methoxyphenyl)pyrimidin-2-amine
0.0207
N-(4-chlorobenzyl)-6-(3-methoxyphenyl)quinazolin-4-amine
Homo sapiens
pH and temperature not specified in the publication
0.0292
N-(4-chlorobenzyl)-6-(pyridin-3-yl)quinazolin-4-amine
Homo sapiens
pH and temperature not specified in the publication
0.026
N-(4-methoxybenzyl)-6-(3-methoxyphenyl)quinazolin-4-amine
Homo sapiens
pH and temperature not specified in the publication
0.0328
N-(4-methoxybenzyl)-6-(pyridin-3-yl)quinazolin-4-amine
Homo sapiens
pH and temperature not specified in the publication
additional information
additional information
-
3.454
2-(1,3-benzodioxol-5-yl)-N-(3,4-dichlorobenzyl)pyrimidin-4-amine
Homo sapiens
pH and temperature not specified in the publication
10
2-(1,3-benzodioxol-5-yl)-N-(3,4-dichlorobenzyl)pyrimidin-4-amine
Homo sapiens
above, pH and temperature not specified in the publication
4.579
2-(1,3-benzodioxol-5-yl)-N-(4-chlorobenzyl)pyrimidin-4-amine
Homo sapiens
pH and temperature not specified in the publication
8.862
2-(1,3-benzodioxol-5-yl)-N-(4-chlorobenzyl)pyrimidin-4-amine
Homo sapiens
pH and temperature not specified in the publication
0.179
2-(1H-indazol-5-yl)-N-(pyridin-3-ylmethyl)pyrimidin-4-amine
Homo sapiens
pH and temperature not specified in the publication
0.349
2-(1H-indazol-5-yl)-N-(pyridin-3-ylmethyl)pyrimidin-4-amine
Homo sapiens
pH and temperature not specified in the publication
0.829
2-(1H-indazol-6-yl)-N-(pyridin-3-ylmethyl)pyrimidin-4-amine
Homo sapiens
pH and temperature not specified in the publication
1.434
2-(1H-indazol-6-yl)-N-(pyridin-3-ylmethyl)pyrimidin-4-amine
Homo sapiens
pH and temperature not specified in the publication
0.018
4-(1,3-benzodioxol-5-yl)-N-(3,4-dibromobenzyl)pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
0.112
4-(1,3-benzodioxol-5-yl)-N-(3,4-dibromobenzyl)pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
0.014
4-(1,3-benzodioxol-5-yl)-N-(3,4-dichlorobenzyl)pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
0.038
4-(1,3-benzodioxol-5-yl)-N-(3,4-dichlorobenzyl)pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
0.009
4-(1,3-benzodioxol-5-yl)-N-(3,5-dibromobenzyl)pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
0.018
4-(1,3-benzodioxol-5-yl)-N-(3,5-dibromobenzyl)pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
0.004
4-(1,3-benzodioxol-5-yl)-N-(3,5-dichlorobenzyl)pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
0.007
4-(1,3-benzodioxol-5-yl)-N-(3,5-dichlorobenzyl)pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
0.273
4-(1,3-benzodioxol-5-yl)-N-(4-chlorophenyl)pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
0.884
4-(1,3-benzodioxol-5-yl)-N-(4-chlorophenyl)pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
0.012
4-(1,3-benzodioxol-5-yl)-N-(pyridin-3-ylmethyl)pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
0.016
4-(1,3-benzodioxol-5-yl)-N-(pyridin-3-ylmethyl)pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
0.107
4-(1,3-benzodioxol-5-yl)-N-[2-bromo-4-(trifluoromethyl)phenyl]pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
0.137
4-(1,3-benzodioxol-5-yl)-N-[2-bromo-4-(trifluoromethyl)phenyl]pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
0.01
4-(1,3-benzodioxol-5-yl)-N-[4-(trifluoromethyl)phenyl]pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
0.018
4-(1,3-benzodioxol-5-yl)-N-[4-(trifluoromethyl)phenyl]pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
0.061
4-(1H-indazol-5-yl)-N-(pyridin-3-ylmethyl)pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
0.093
4-(1H-indazol-5-yl)-N-(pyridin-3-ylmethyl)pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
0.282
6-(1,3-benzodioxol-5-yl)-N-(3,5-dichlorobenzyl)quinazolin-4-amine
Homo sapiens
pH and temperature not specified in the publication
1.156
6-(1,3-benzodioxol-5-yl)-N-(3,5-dichlorobenzyl)quinazolin-4-amine
Homo sapiens
pH and temperature not specified in the publication
0.000033
harmine
Homo sapiens
-
in 25 mM HEPES, pH 7.0, 5 mM MgCl2, 0.5 mmM dithiothreitol, at 30°C
0.000033
harmine
Homo sapiens
-
isoform DYRK1A
0.000033 - 0.00008
harmine
Homo sapiens
pH and temperature not specified in the publication
0.000166
harmine
Homo sapiens
-
isoform DYRK1B
0.000166
harmine
Homo sapiens
pH and temperature not specified in the publication
0.001
harmine
Homo sapiens
-
-
0.000059
midostaurin
Homo sapiens
pH 6.8, 22°C
0.000066
midostaurin
Homo sapiens
pH 6.8, 22°C
0.025
N,4-bis(1,3-benzodioxol-5-yl)pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
0.042
N,4-bis(1,3-benzodioxol-5-yl)pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
0.514
N-(3,4-dichlorobenzyl)-2-(1H-indazol-5-yl)pyrimidin-4-amine
Homo sapiens
pH and temperature not specified in the publication
2.352
N-(3,4-dichlorobenzyl)-2-(1H-indazol-5-yl)pyrimidin-4-amine
Homo sapiens
pH and temperature not specified in the publication
0.0129
N-(3,4-dichlorobenzyl)-4-(1H-indazol-5-yl)pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
0.125
N-(3,4-dichlorobenzyl)-4-(1H-indazol-5-yl)pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
0.0169
N-(3,4-dichlorobenzyl)-4-(1H-indazol-6-yl)pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
0.599
N-(3,4-dichlorobenzyl)-4-(1H-indazol-6-yl)pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
0.013
N-(3,4-dichlorobenzyl)-4-(2,3-dihydro-1,4-benzodioxin-6-yl)pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
0.055
N-(3,4-dichlorobenzyl)-4-(2,3-dihydro-1,4-benzodioxin-6-yl)pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
4.654
N-(3,4-dichlorobenzyl)-4-(3-methoxyphenyl)pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
10
N-(3,4-dichlorobenzyl)-4-(3-methoxyphenyl)pyrimidin-2-amine
Homo sapiens
above, pH and temperature not specified in the publication
0.203
N-(3,4-dichlorobenzyl)-4-(4-methoxyphenyl)pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
0.411
N-(3,4-dichlorobenzyl)-4-(4-methoxyphenyl)pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
6.361
N-(4-chlorobenzyl)-4-(3-methoxyphenyl)pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
6.782
N-(4-chlorobenzyl)-4-(3-methoxyphenyl)pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
0.558
N-(4-chlorobenzyl)-4-(4-methoxyphenyl)pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
0.871
N-(4-chlorobenzyl)-4-(4-methoxyphenyl)pyrimidin-2-amine
Homo sapiens
pH and temperature not specified in the publication
0.000012
TG003
Homo sapiens
pH and temperature not specified in the publication
0.00013
TG003
Homo sapiens
pH and temperature not specified in the publication
additional information
additional information
Homo sapiens
pIC50 values of 6-arylquinazolin-4-amine inhibitors, overview
-
additional information
additional information
Homo sapiens
pIC50 values of 6-arylquinazolin-4-amine inhibitors, overview
-
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metabolism
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the SARK-mediated pathway may be a widespread mechanism in regulating leaf senescence
evolution
enzme Yak1 is a member of dual-specificity Tyr phosphorylation-regulated kinases (DYRKs) that are evolutionarily conserved
evolution
enzyme DYRK2 is a member of the dual specificity kinase family, which can phosphorylate both Ser/Thr and Tyr substrates. At least seven DYRK family members have been identified (DYRK1A, DYRK1B, DYRK1C, DYRK2, DYRK3, DYRK4A and DYRK4B)
evolution
enzyme DYRK4 belongs to the dual specificity tyrosine phosphorylation-regulated kinases, DYRKs, a family of conserved protein kinases that play key roles in the regulation of cell differentiation, proliferation, and survival. DYRKs contain a conserved Tyr-Xaa-Tyr motif in the activation loop. Autophosphorylation of a second tyrosine residue within the activation loop is necessary for full DYRK4 kinase activity and is a defining feature of the DYRK family. Family members DYRK1A, DYRK2, and DYRK4 differ in their target recognition sequence, and preference for an arginine residue at position P -3 is a feature of DYRK1A but not of DYRK2 and DYRK4
evolution
enzyme DYRK4 belongs to the dual specificity tyrosine phosphorylation-regulated kinases, DYRKs, a family of conserved protein kinases that play key roles in the regulation of cell differentiation, proliferation, and survival. DYRKs contain a conserved Tyr-Xaa-Tyr motif in the activation loop. Autophosphorylation of a second tyrosine residue within the activation loop is necessary for full DYRK4 kinase activity and is a defining feature of the DYRK family. Family members DYRK1A, DYRK2, and DYRK4 differ in their target recognition sequence, and preference for an arginine residue at position P -3 is a feature of DYRK1A but not of DYRK2 and DYRK4
evolution
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Ser/Thr protein kinases present in Bacillus anthracis genome: Bacillus anthracis has lost key tyrosine kinases and gained novel dual specificity kinases. Dual specificity protein kinases are identified, of which one is similar to the eukaryotic DYRK superfamily. PhrkD and PrkG DSPKs belong to different classes and have different modes of regulation. The mechanism of autophosphorylation and the substrate phosphorylation in PrkG is distinct from that of PrkD and involves Thr residues in addition to Tyr residues
evolution
the enzyme is a member of kinase1 (Yak1) subfamily in the dual-specificity tyrosine phosphorylation-regulated kinase family. The kinase domain of TAR1 also has conserved functional features of the DYRK family, such as an ATP anchor, a phosphate anchor, a catalytic loop, a cation-binding site, and an activation loop
evolution
-
enzme Yak1 is a member of dual-specificity Tyr phosphorylation-regulated kinases (DYRKs) that are evolutionarily conserved
-
evolution
-
the enzyme is a member of kinase1 (Yak1) subfamily in the dual-specificity tyrosine phosphorylation-regulated kinase family. The kinase domain of TAR1 also has conserved functional features of the DYRK family, such as an ATP anchor, a phosphate anchor, a catalytic loop, a cation-binding site, and an activation loop
-
malfunction
-
Dyrk1A participates in the pathogenic mechanisms underlying the mental and other physical symptoms of Down syndrome, alterations in Dyrk1A expression are frequently associated with Down syndrome phenotypes. Knock-out mice are embryonic lethal and heterozygous Dyrk1A mice exhibit decreased neonatal viability, developmental delay, and altered neocortical pyramidal cells
malfunction
-
dyrk1b antisense morpholino knockdown animals reveal modestly expanded expression of the dorsal axial mesoderm marker gsc while the pan-mesodermal marker bik is largely unaffected, show moderately reduced endodermal markers cas and sox17, and reduced expression of the pharyngeal pouch marker edn1
malfunction
-
heterozygous mice for Dyrk1A show marked alterations in traction ability, prehensile reflex and balance, but only present a slight impairment of visuo-spatial memory even though they show a robust decrease of CA1, CA2, CA3 and dentate gyrus cells
malfunction
-
knockdown of DYRK1A in cortical neurons disrupts neuritogenesis and alters microtubule stability
malfunction
-
overexpressed DYRK1A contributes to neurofibrillary degeneration in Down syndrome more significantly than in subjects with two copies of the DYRK1A gene and sporadic Alzheimers disease
malfunction
-
a T-DNA insertion mutant of AtSARK shows significantly delayed senescence, while inducible overexpression of AtSARK in Arabidopsis thaliana causes precocious senescence and abnormal floral organ development. phenotypes of transgenic lines, overview
malfunction
Dyrk1A expression is increased in the brain of cystathionine-beta-synthase (CBS)-deficient mice. The murine model of hyperhomocysteinemia shows an activation of extracellular signal-regulated kinase (ERK) pathway. Significant increase of phosphorylated ERK, phosphorylated MAP kinase kinases, and phosphorylated Akt in the brain of CBS-deficient and Dyrk1A-overexpressing mice. Interaction between Dyrk1A and Grb2 is increased in the brain of Dyrk1A transgenic mice, but Dyrk1A overexpression results in decreased interaction of sprouty 2 and Grb2, and in increased receptor tyrosine kinases phosphorylation and activation, overview
malfunction
increased expression of this enzyme leads to hyper-phosphorylation of Tau protein and amyloid precursor protein, which results in high levels of beta-amyloid peptide (leading to beta-amyloidosis) and aggregation of Tau protein, and subsequent formation of neurofibrillary tangles
malfunction
-
inducible GmSARK overexpression in Arabidopsis thaliana leads to early leaf senescence, chloroplast destruction, and abnormal flower morphology. GmSARK-overexpressing seedlings reveal a multitude of changes in phytohormone synthesis and signaling, specifically the repression of cytokinin functions and the induction of auxin and ethylene pathways. Inhibition of either auxin action or ethylene biosynthesis alleviates the senescence induced by GmSARK. Mutation of either auxin resistant1 or ethylene insensitive2 genes completely reverses the GmSARK-induced senescence. Phenotype, detailed overview
malfunction
kinase-inactive DYRK3 inhibits mTORC1 by preventing dissociation from stress granules
malfunction
-
knockdown of Dyrk1B by siRNA leads to a modest but statistically significant reduction of BrdU incorporation in RPE1-E7 cells, and reduction of Dyrk1B or mutation T198A significantly reduce S10P in E7 expressing cells
malfunction
-
loss of Ser162 and Tyr182 in PrkD results in a significant loss in substrate phosphorylation
malfunction
overexpression of Dyrk1A does not affect Tau exon 10 inclusion, whereas the expression of dominant negative Dyrk1A, Dyrk1AK188R, which results in the loss of its kinase activity, significantly promotes Tau exon10 inclusion
malfunction
some splicing events affect the catalytic domain, including a three-amino acid deletion within subdomain XI that markedly reduces the enzymatic activity of DYRK4
malfunction
some splicing events affect the catalytic domain, including a three-amino acid deletion within subdomain XI that markedly reduces the enzymatic activity of DYRK4
malfunction
the dyrk1a gene is located in the Down syndrome critical region (DSCR) on chromosome 21 and full or partial trisomy of DSCR in Down syndrome (DS) leads to overexpression of DYRK1A
malfunction
the endocytic process of invasion of human brain microvascular endothelial cells. Cryptococcus neoformans is abolished by cytochalasin D, nocodazole, or anti-DYRK3 siRNA
malfunction
the TAR1-defective mutant, tar1-1, accumulates TAG to levels 0.5 and 0.1fold of those of a wild-type strain in sulfur- and nitrogen-deficient conditions, respectively. In N-deficient conditions, tar1-1 shows more pronounced arrest of cell division than the wild-type, has increased cell size and cell dry weight, and maintains chlorophyll and photosynthetic activity, which are not observed in S-deficient conditions. In N-deficient conditions, global changes in expression levels of nitrogen deficiency-responsive genes in nitrogen assimilation and tetrapyrrole metabolism are noted between tar1-1 and wild-type cells. Mutant tar1-1 cells retain their photosynthetic activity in N-deficient conditions. The wild-type TAR1 gene restores the low-TAG accumulation phenotype. Phenotype, overview
malfunction
TTK knockdown inhibits growth, migration and invasiveness of human liver cancer cells in vitro, TTK deficiency induces cell death of liver cancer cells in vitro. In HepG2 cell line, TTK knockdown also results in increased numbers of enlarged viable cells and to significantly increaed levels of LC3-II protein, a sensitive indicator of autophagy. No no difference in overall levels of apoptotic cells, but relative TTK deficiency leads to enhanced senescent and autophagic cell death
malfunction
upon TTK knockdown in pancreatic ductal adenocarcinoma cells, cell proliferation is significantly attenuated, whereas apoptosis and necrosis rates are significantly increased. Anchorage-independent growth, a hallmark of malignant transformation and metastatic potential, is strongly impaired in the absence of TTK gene function. Immortalised normal pancreatic hTERT-HPNE cells are not affected by loss of TTK function. Phenotype, overview. The effects in cancer cells are associated with increased formation of micronuclei, suggesting that loss of TTK function in pancreatic cancer cells results in chromosomal instability and mitotic catastrophe
malfunction
-
the TAR1-defective mutant, tar1-1, accumulates TAG to levels 0.5 and 0.1fold of those of a wild-type strain in sulfur- and nitrogen-deficient conditions, respectively. In N-deficient conditions, tar1-1 shows more pronounced arrest of cell division than the wild-type, has increased cell size and cell dry weight, and maintains chlorophyll and photosynthetic activity, which are not observed in S-deficient conditions. In N-deficient conditions, global changes in expression levels of nitrogen deficiency-responsive genes in nitrogen assimilation and tetrapyrrole metabolism are noted between tar1-1 and wild-type cells. Mutant tar1-1 cells retain their photosynthetic activity in N-deficient conditions. The wild-type TAR1 gene restores the low-TAG accumulation phenotype. Phenotype, overview
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physiological function
-
DYRK1A primes S1388, a glycogen synthase kinase 3beta phosphorylation sites on microtubule associated protein 1B
physiological function
-
human biliverdin reductase is an upstream activator of the insulin/insulin growth factor-1 and mitogen-activated protein kinase signaling pathways, and also a basic-leucine-zipper DNA/chromatin-binding transcription factor, an activator and anchor protein for translocation of protein kinase C betaII and zeta isozymes within cell compartments, and a kinase kinase for their activation. Biliverdin reductase is essential for mitogen-activated protein kinase-extracellular signal-regulated kinase 1/2-eukaryotic-like protein kinase signaling and has been identified as the cytoplasm-nuclear heme transporter of extracellular signal-regulated kinase 1/2 and hematin
physiological function
-
the zebrafish dyrk1b gene is important for endoderm formation, craniofacial patterning, and ndr2 expression
physiological function
AtYak1 is a dual specificity protein kinase in Arabidopsis that may regulate the phosphorylation status of the annexin family proteins
physiological function
Cryptococcus neoformans invasion is mediated through the endocytic pathway via lipid rafts.Human CD44 molecules from lipid rafts can directly interact with hyaluronic acid, the Cryptococcus neoformans ligand. Bikunin, which perturbs CD44 function in the lipid raft, can block Cryptococcus neoformans adhesion and invasion of human brain microvascular endothelial cells. Cryptococcus neoformans internalization into human brain microvascular endothelial cells involves the CD44 protein of the hosts, cytoskeleton, and intracellular kinase-DYRK3, overview. Cryptococcus neoformans-induced endocytic dynamics require actin filaments, microtubules, and DYRK3. Effect of DYRK3 on Cryptococcus neoformans transversal across the blood-brain barrier in vitro
physiological function
dual-specificity tyrosine phosphorylation-regulated kinase 1A (DYRK1A) is a protein kinase associated with neuronal development and brain physiology. Activity of DYRK1A to prime the tau protein for further phosphorylation by GSK-3beta. This leads to the hyperphosphorylation of tau, followed by selfaggregation into neurofibrillary tangles, which are the primary biomarker of Alzheimer's disease
physiological function
during cellular stress the dual specificity kinase DYRK3 regulates the stability of P-granule-like structures and mTORC1 signaling. DYRK3 displays a cyclic partitioning mechanism between stress granules and the cytosol via a low-complexity domain in its N-terminus and its kinase activity. When DYRK3 is inactive, it prevents stress granule dissolution and the release of sequestered mTORC1. When DYRK3 is active, it allows stress granule dissolution, releasing mTORC1 for signaling and promoting its activity by directly phosphorylating the mTORC1 inhibitor PRAS40. This mechanism links cytoplasmic compartmentalization via liquid phase transitions with cellular signaling. DYRK3 has the potential to condense granules in the cytosol of human cells to which the mRNA-binding protein GW182 can be recruited, and DYRK3 localizes to stress granules during oxidative and osmotic stress. Activity-dependent dynamic cycling of DYRK3 on stress granules and mechanism of mTORC1 reactivation by DYRK3, overview
physiological function
Dyrk1A is involved in diverse functions ranging from development and growth to apoptosis
physiological function
enzyme Dyrk1A interacts with and phosphorylates diverse cellular proteins including transcription and splicing factors. Dyrk1A enhances tau expression and regulates expression of endogenous tau in neuronal cells, mechanism, overview. Dyrk1A does not enhance tau gene transcription, but increases tau mRNA stability. The enhancement does not require the kinase activity of Dyrk1A, the inactive enzyme mutant K188R also increases tau expression. Dyrk1A increases the expression of tau isoforms containing exon 10 to a larger extent than isoforms lacking exon 10. Dyrk1A is overexpressed in Down syndrome and may play a critical role in the early onset of tau pathology in this disease
physiological function
enzyme Dyrk1A regulates the pre-mRNA alternative splicing of Tau through splicing factors. Dyrk1A interacts with SRp55 through its RRM domain, phosphorylates its proline-rich domain and inhibits its ability to promote Tau exon 10 inclusion. Upregulation of Dyrk1A disrupts the alternative splicing of Tau exon 10, which encodes the second microtubule-binding repeat. Tau 10 alternative splicing generates Tau isoforms with three- or four-microtubule-binding repeats, named 3R-tau and 4R-tau Dysregulation of the alternative splicing of Tau exon 10 causes several types of neurodegenerative diseases, e.g. neurofibrillary degeneration
physiological function
-
enzyme Dyrk1B is a dual-specificity kinase and negative regulator of cell proliferation in quiescent cells. Dyrk1B plays a positive role in S-phase entry of quiescent high-risk human papillomavirus E7 oncogene, HPV E7, expressing cells, and Dyrk1B upregulates HPV E7. Dyrk1B contributes to p27 phosphorylation (at Ser10 and Thr198), which is important for the proliferation of HPV E7 expressing cells. DYRK1B overexpression does not increase S-phase entry in control RPE1 cells
physiological function
-
enzyme GmSARK mediates leaf senescence, it has specific roles in senescence-inducing hormonal pathways, molecular mechanism, overview
physiological function
enzyme TTK function is critical for growth and proliferation of pancreatic cancer cells
physiological function
-
possible role of the kinase in cell growth and development
physiological function
role of DYRK2 in human cancer and as a potential oncogene. Overexpression of DYRK2 predicts a better survival in human non-small cell lung cancer, low expression level of DYRK2 correlates with poor prognosis in colorectal cancer. DYRK2 expression is significantly downregulated in colorectal cancer tissues compared with adjacent non-tumorous tissues. Enzyme DYRK2 inhibits cell invasion and migration in both HCT-116 and SW-480 cells and functions as a tumor suppressor in colorectal cancer cells. DYRK2 behaves as a proapoptotic kinase through phosphorylation of p53 at S46 which promotes its apoptotic activity. Downregulation of DYRK2 also induces a G2/M arrest. DYRK2 inhibits the proliferation, cell migration and invasion of colorectal cancer cells in vitro
physiological function
several splice variants of DYRK4 have distinct functional capacities
physiological function
several splice variants of DYRK4 have distinct functional capacities
physiological function
Syk is a dual-specificity kinase, phosphorylating serine and tyrosine residues, that self-regulates the signal output from the B-cell antigen receptor. The B-cell antigen receptor (BCR) comprises the membrane-bound Ig molecule and the Ig-alpha/Ig-beta heterodimer, which function as the ligand-binding and signaling subunits, respectively. The cytoplasmic tails of Ig-alpha and Ig-beta contain an immunoreceptor tyrosine-based activation motif. The ITAM tyrosines of Ig-alpha and Ig-beta are phosphorylated by Syk. And enzyme Syk (spleen tyrosine kinase) phosphorylates S197 on Ig-alpha, not only activating but also inhibiting signaling from the B-cell antigen receptor. Phosphorylation of S197 in the Ig-alpha cytoplasmic tail plays a negative role in B-cell antigen receptor (BCR) activation
physiological function
TAR1 is a regulator of TAG accumulation in S- and N-deficient conditions, and it functions in cell growth and repression of photosynthesis in conditions of nitrogen deficiency. The kinase domain of TAR1 also has conserved functional features of the DYRK family, such as an ATP anchor, a phosphate anchor, a catalytic loop, a cation-binding site, and an activation loop. TAR1 enhances the degradation of chlorophyll and photosynthesis-related proteins, which leads to a decrease of photosynthetic activity in wild-type cells in N-deficient conditions. TAR1 also might enhance acetate assimilation and rate of cell division and prevent increase of cell biomass
physiological function
TTK is a dual-specificity protein kinase that is thought to be involved in mitotic spindle assembly checkpoint and control of cell cycle program. Increased intratumoral expression of TTK correlates with aggressive clinical course and low survival in liver cancer8. TTK has pro-carcinogenic roles in hepatocellular carcinoma development and progression
physiological function
cyclin L2promotes HIV-1 replication through interactions with DYRK1A. Knockdown or inhibition of DYRK1A increases HIV-1 replication in macrophages, while depletion of cyclin L2 decreases HIV-1 replication. Depletion of DYRK1A increases expression levels of cyclin L2. Mutations of cyclin L2 at serine residues preceding proline abolishes phosphorylation by DYRK1A, significantly stabilizes cyclin L2 and increases HIV-1 replication in macrophages
physiological function
-
DYRK1 overexpressing parasites display a decrease in proliferation and in cell cycle re-entry of arrested cells. Parasites lacking DYRK1 display distinct fitness phenotypes in logarithmic and stationary growth phases. In logarithmic growth phase, DYRK1-/- parasites proliferate better than control lines, while in stationary growth phase, DYRK1-/- parasites round up, accumulate vacuoles and lipid bodies and display subtle but consistent differences in lipid composition. They express less metacyclic-enriched transcripts, display increased sensitivity to complement lysis and a significant reduction in survival within peritoneal macrophages
physiological function
Dyrk2 down regulation promotes osteoclast fusion, whereas its overexpression inhibits fusion. Dyrk2 knockdown increases the number of nuclei in osteoclasts. Dyrk2 also promotes the fusion of foreign-body giant cells. Dyrk2 limits the expansion of multinucleated founder cells through the suppression of the fusion competency of follower cells
physiological function
DYRK2 phosphorylates Notch1-IC in response to chemotherapeutic agents and facilitates its proteasomal degradation by FBXW7 ubiquitin ligase through a Thr-2512 phosphorylation-dependent mechanism. DYRK2 regulation by chemotherapeutic agents has a relevant effect on the viability, motility and invasion capacity of cancer cells expressing NOTCH1
physiological function
kinase YAK1 interacts with LIGHT-REGULATED WD1 (LWD1). YAK1 is an important regulator for various light responses, including the circadian clock, photomorphogenesis and reproductive development. AtYAK1 can antagonize the function of LIGHT-REGULATED WDs in regulating the circadian clock and photoperiodic flowering. YAK1 regulates light-induced period-length shortening and photomorphogenic development. YAK1 mediates plant fertility especially under inferior light conditions including low light and short-day length
physiological function
-
MPKL promotes photoperiodic diapause induction of Locusta migratoria. MPKL significantly inhibits Akt and FOXO (i.e. forkhead box protein O) phosphorylation levels in ovaries, and also enhances reactive oxygen species, superoxide dismutase and catalase activities, whereas peroxidase activity is decreased under both photoperiodic regimes
physiological function
-
AtYak1 is a dual specificity protein kinase in Arabidopsis that may regulate the phosphorylation status of the annexin family proteins
-
physiological function
-
TAR1 is a regulator of TAG accumulation in S- and N-deficient conditions, and it functions in cell growth and repression of photosynthesis in conditions of nitrogen deficiency. The kinase domain of TAR1 also has conserved functional features of the DYRK family, such as an ATP anchor, a phosphate anchor, a catalytic loop, a cation-binding site, and an activation loop. TAR1 enhances the degradation of chlorophyll and photosynthesis-related proteins, which leads to a decrease of photosynthetic activity in wild-type cells in N-deficient conditions. TAR1 also might enhance acetate assimilation and rate of cell division and prevent increase of cell biomass
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additional information
-
absence of characteristic DYRK motifs, such as the DYRK homology box, N-terminal autophosphorylation accessory region, and motif rich in Pro, Glu, Ser, and Thr residues (PEST) in PrkD
additional information
both human and murine DYRK4 genes express several transcripts as a result of alternative splicing, with the two main protein products differing in their N-terminal domain
additional information
both human and murine DYRK4 genes express several transcripts as a result of alternative splicing, with the two main protein products differing in their N-terminal domain
additional information
rebuilding of the BCR receptor complex in S2 Drodophila melanogster system and phosphorylation and analysis with Syk overview
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?
x * 65000, splicing variant 1, SDS-PAGE, x * 70000, splicing variant 2, SDS-PAGE, x * 75000, splicing variant 3 from skeletal muscle, SDS-PAGE
additional information
-
enzyme domain determination and analysis, modular organization, the enzyme contains N-terminal TPR repeats, followed by a GGDEF domain at the C-terminus, overview
additional information
-
enzyme domain determination and analysis, modular organization, the enzyme contains an universal stress induced protein associated domain, USPA, and a C-terminal GUN4 domain, the latter binds magnesium-protoporphyrin IX
additional information
-
analysis of sequence motifs
additional information
-
structure modeling of wild-type and mutant enzymes based on the X-ray structure of homologous sequences, computational docking and molecular dynamics simulations, overview
additional information
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enzyme domain determination and analysis, modular organization, the enzyme contains an universal stress induced protein associated domain, USPA
additional information
-
enzyme domain determination and analysis, modular organization, the enzyme contains a C-terminal NirV domain and a TPR domain, an N-terminal protein kinase domain, overview
additional information
-
enzyme domain determination and analysis, modular organization, the enzyme contains WD repeats
additional information
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enzyme domain determination and analysis, modular organization, the enzyme contains several tetratrico peptide repeats
additional information
-
enzyme domain determination and analysis, modular organization, the enzyme contains PQQ family repeats, which form beta-propeller-like structures and can serve as sites for the interaction with target proteins, the enzyme also contains three to six NHL repeats, following the kinase domain, which are known to serve as protein interaction surfaces and might possess enzymic activity
additional information
-
enzyme domain determination and analysis, modular organization, the enzyme contains several tetratrico peptide repeats
additional information
-
enzyme domain determination and analysis, modular organization, the enzyme contains a O-sialoglycoprotein endopeptidase, OSGP, domain at the N-terminus, the enzyme contains an N-terminal ABC1 kinase domain and a putative transmembrane spanning segment at the C-terminus
additional information
Dyrk1A contains a nuclear targeting signal sequence, a protein kinase domain, a PEST domain (protein domain that is enriched in proline (P), glutamic acid (E), serine (S), and threonine (T) residues), 13 consecutive histidine residues (His repeats) and a serine/threonine rich segment (S/T). The PEST region is located in the C terminus of the catalytic domain. A stretch of 13 histidines located between 607 and 619 amino acid residues follows subsequently a segment of 14 serine/threonine residues
additional information
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enzyme domain determination and analysis, modular organization, the enzyme contains several tetratrico peptide repeats
additional information
-
enzyme domain determination and analysis, modular organization, the enzyme contains an universal stress induced protein associated domain, USPA
additional information
-
enzyme domain determination and analysis, modular organization, the enzyme contains a O-sialoglycoprotein endopeptidase, OSGP, domain at the N-terminus
additional information
-
enzyme domain determination and analysis, modular organization, the enzyme contains an N-terminal ABC1 kinase domain and a putative transmembrane spanning segment at the C-terminus
additional information
-
enzyme domain determination and analysis, modular organization, the enzyme contains an N-terminal ABC1 kinase domain and a putative transmembrane spanning segment at the C-terminus
additional information
-
enzyme domain determination and analysis, modular organization, the enzyme contains a O-sialoglycoprotein endopeptidase, OSGP, domain at the N-terminus
additional information
-
enzyme domain determination and analysis, unique modular organization, the enzyme contains an N-terminal protein kinase domain, a central transmembrane domain, and a C-terminal peptidyl-prolyl cis-trans isomerase domain
additional information
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enzyme domain determination and analysis, modular organization, the enzyme contains several tetratrico peptide repeats, and three to six NHL repeats, following the kinase domain, which are known to serve as protein interaction surfaces and might possess enzymic activity, the enzyme also contains an N-terminal protein kinase domain and a hydrophobin-like region at the C-terminus, the latter plays a role in the recognition of D-alanyl D-alanine dipeptides
additional information
-
enzyme domain determination and analysis, modular organization, the enzyme contains several tetratrico peptide repeats, and three to six NHL repeats, following the kinase domain, which are known to serve as protein interaction surfaces and might possess enzymic activity, the enzyme also contains an N-terminal protein kinase domain and a hydrophobin-like region at the C-terminus, the latter plays a role in the recognition of D-alanyl D-alanine dipeptides
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additional information
-
enzyme domain determination and analysis, modular organization, the enzyme contains an N-terminal protein kinase domain and a hydrophobin-like region at the C-terminus, the latter plays a role in the recognition of D-alanyl-D-alanine dipeptides
additional information
-
enzyme domain determination and analysis, modular organization, the enzyme contains an N-terminal protein kinase domain and a hydrophobin-like region at the C-terminus, the latter plays a role in the recognition of D-alanyl-D-alanine dipeptides
-
additional information
-
enzyme domain determination and analysis, modular organization, the enzyme contains an universal stress induced protein associated domain, USPA, the enzyme contains an N-terminal ABC1 kinase domain and a putative transmembrane spanning segment at the C-terminus
additional information
-
enzyme domain determination and analysis, modular organization, the enzyme contains WD repeats
additional information
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enzyme domain determination and analysis, modular organization, the enzyme contains several tetratrico peptide repeats and a C-terminal GUN4 domain, the latter binds magnesium-protoporphyrin IX, the enzyme of strain PCC 7120 contains a pectinesterase domain catalyzing the hydrolysis of pectin, and WD repeats
additional information
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enzyme domain determination and analysis, modular organization, the enzyme contains several tetratrico peptide repeats
additional information
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enzyme domain determination and analysis, modular organization, the enzyme contains a PP2C-like domain at the N-terminus, and 11 STYK-like sequences, overview
additional information
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enzyme domain determination and analysis, modular organization, the enzyme contains a PP2C-like domain at the N-terminus
additional information
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enzyme domain determination and analysis, modular organization, the enzyme contains a PP2C-like domain at the N-terminus
additional information
-
enzyme domain determination and analysis, modular organization, the enzyme contains several tetratrico peptide repeats, the enzyme contains an N-terminal ABC1 kinase domain and a putative transmembrane spanning segment at the C-terminus
additional information
-
enzyme domain determination and analysis, modular organization, the enzyme contains several tetratrico peptide repeats, the enzyme contains PQQ family repeats, which form beta-propeller-like structures and can serve as sites for the interaction with target proteins
additional information
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enzyme domain determination and analysis, modular organization, the enzyme contains PQQ family repeats, which form beta-propeller-like structures and can serve as sites for the interaction with target proteins
additional information
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enzyme domain determination and analysis, modular organization, the enzyme contains several tetratrico peptide repeats, the enzyme contains an N-terminal ABC1 kinase domain and a putative transmembrane spanning segment at the C-terminus
additional information
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enzyme domain determination and analysis, modular organization, the enzyme contains WD repeats
additional information
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enzyme domain determination and analysis, modular organization, the enzyme contains a O-sialoglycoprotein endopeptidase, OSGP, domain at the N-terminus, the enzyme contains an N-terminal ABC1 kinase domain and a putative transmembrane spanning segment at the C-terminus
additional information
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enzyme domain determination and analysis, modular organization, the enzyme contains an N-terminal ABC1 kinase domain and a putative transmembrane spanning segment at the C-terminus
additional information
Thermospora curvatum
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enzyme domain determination and analysis, modular organization, the enzyme contains WD repeats
additional information
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enzyme domain determination and analysis, modular organization, the enzyme contains WD repeats
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K160R
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site-directed mutagenesis, inactive mutant enzyme
K53M
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site-directed mutagenesis, inactive mutant
T180A
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site-directed mutagenesis, the mutant enzyme shows loss in activity
T181A
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site-directed mutagenesis, the mutant enzyme shows loss in activity and in phosphorylation
T181A/Y182F
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site-directed mutagenesis, the mutant enzyme shows high loss in activity and in phosphorylation
T245A/Y349F
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site-directed mutagenesis, the mutant enzyme shows high loss in activity and in phosphorylation
Y182F
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site-directed mutagenesis, the mutant enzyme shows loss in activity
K218M
site-directed mutagenesis, a kinase-deficient mutant
K238M
loss of kinase activity
S350A
50% of wild-type activity, melting temperature decreases by almost 5 degrees compared to wild-type
S350D
80% of wild-type activity, melting temperature is similar to wild-type
S350E
90% of wild-type activity, melting temperature decreases by 2 degrees compared to wild-type
T198A
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site-directed mutagenesis, the mutation reduces the enzyme activity compared to the wild-type enzyme
Y246F
site-directed mutagenesis, mutation of the autophosphorylation site. The DYRK4 mutant is neither autophosphorylated nor does it display kinase activity on a synthetic substrate, the exogenous peptide substrate DYRKtide
K188R
a dominant negative, inactive Dyrk1A mutant
Y148F
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site-directed mutagenesis, ATP binding site residue, the mutant is unable to phosphorylate histone and is not phosphorylated itself
Y148F
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site-directed mutagenesis, the mutant enzyme shows altered inhibition kinetics with tyrosine kinase inhibitors compared to the wild-type enzyme
Y213F
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site-directed mutagenesis, TEY motif residue, the mutant shows 4fold increased autophosphorylation and 2.8fold increased activity with ATP and histone compared to the wild-type enzyme
Y213F
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site-directed mutagenesis, the mutant enzyme shows altered inhibition kinetics with tyrosine kinase inhibitors compared to the wild-type enzyme
Y297F
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site-directed mutagenesis, inactive mutant enzyme
Y297F
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site-directed mutagenesis, the mutant enzyme shows altered inhibition kinetics with tyrosine kinase inhibitors compared to the wild-type enzyme
Y317F
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site-directed mutagenesis, ATP binding site residue, the mutant is unable to phosphorylate histone and is not phosphorylated itself
Y317F
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site-directed mutagenesis, the mutant enzyme shows altered inhibition kinetics with tyrosine kinase inhibitors compared to the wild-type enzyme
K523R
site.directed mutagenesis, substitution of the putative phosphate anchor Lys, mutant pTAR1KD is catalytically inactive
K523R
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site.directed mutagenesis, substitution of the putative phosphate anchor Lys, mutant pTAR1KD is catalytically inactive
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K188R
site-directed mutagenesis, catalytically inactive mutant
K188R
kinase-dead DYRK1 mutant
K188R
kinase-dead Dyrk1A construct
additional information
atyak1-1 (SAIL_31_C10) and atyak1-2 (SALK_0746) T-DNA insertion mutants
additional information
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atyak1-1 (SAIL_31_C10) and atyak1-2 (SALK_0746) T-DNA insertion mutants
additional information
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construction of a a T-DNA insertion mutant of AtSARK that shows significantly delayed senescence
additional information
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atyak1-1 (SAIL_31_C10) and atyak1-2 (SALK_0746) T-DNA insertion mutants
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additional information
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loss of Ser162 and Tyr182 in PrkD results in a significant loss in substrate phosphorylation
additional information
AdipoRed fluorescence-activated cell sorting-based screening of low triacylglycerol-accumulating mutants in nutrient (nitrogen and sulfur)-deficient conditions, identification of the TAR1-defective mutant tar1-1 with a DNA tag insertion in the TAR1 locus. the phenotypes of tar1-1 related to triacylglycerol are caused by disruption of the TAR1 gene. The wild-type TAR1 gene restores the low-TAG accumulation phenotype
additional information
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AdipoRed fluorescence-activated cell sorting-based screening of low triacylglycerol-accumulating mutants in nutrient (nitrogen and sulfur)-deficient conditions, identification of the TAR1-defective mutant tar1-1 with a DNA tag insertion in the TAR1 locus. the phenotypes of tar1-1 related to triacylglycerol are caused by disruption of the TAR1 gene. The wild-type TAR1 gene restores the low-TAG accumulation phenotype
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additional information
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enzyme knock-out leads to increased D-glucose uptake in response to insulin
additional information
construction of three deletion mutations of Dyrk1A from C-terminus, including Dyrk1A1-616 without S/T region, Dyrk1A1-588 without His repeats and S/T region, and Dyrk1A1-474 without PEST, His repeats, and S/T region for investigation whether C-terminus of Dyrk1A is responsible for the regulation of tau expression. All three C-terminal deletion mutations of Dyrk1A enhance the expression of tau to a much less extent as compared with the full length Dyrk1A
additional information
enzyme knockout by anti-DYRK3 siRNA expression in brain microvascular endothelial cells and HeLa cells causing similar phenotypes, overview
additional information
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enzyme knockout by anti-DYRK3 siRNA expression in brain microvascular endothelial cells and HeLa cells causing similar phenotypes, overview
additional information
enzyme TTK knockout by siRNA transfection of cell lines PaTu-8988T, Panc1 and S2-028
additional information
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enzyme TTK knockout by siRNA transfection of cell lines PaTu-8988T, Panc1 and S2-028
additional information
generation of stable TTK-deficient hepatoccellular carcinoma cells using lentiviral shRNA methods. The cell lines display differential sensitivity to TTK inhibition. Production of TTK deficiency is only possible in Hep-G2 and Huh-7 cell lines, whereas knockdown of TTK is lethal for Hep-3B and PLC/PRL/5 cells. TTK deficiency induces cell death of liver cancer cells in vitro
additional information
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generation of stable TTK-deficient hepatoccellular carcinoma cells using lentiviral shRNA methods. The cell lines display differential sensitivity to TTK inhibition. Production of TTK deficiency is only possible in Hep-G2 and Huh-7 cell lines, whereas knockdown of TTK is lethal for Hep-3B and PLC/PRL/5 cells. TTK deficiency induces cell death of liver cancer cells in vitro
additional information
exchange of two Tyr residues in the activation loop between subdomains VII and VIII for Phe almost completely suppresses the activity and Tyr autophosphorylation of Dyrk. Tyr autophosphorylation is also reduced by exchange of Tyr219 in a tyrosine phosphorylation consensus motif
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AtSARK, the gene gene consists of 11 exons, quantitative RT-PCR analysis, inducible overexpression of AtSARK in Arabidopsis thaliana causes precocious senescence and abnormal floral organ development
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DNA and amino acid sequence determination and analysis, the enzyme occurs in several splicing variants, analysis overview, expression in murine hypothalamic GT1-7 cell line, expression of splicing variants in COS_7 cells and in Escherichia coli
DNA and amino acid sequence determination and analysis, the enzyme occurs in several splicing variants, expression in human fibroblast 3T3-L1 cell line
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EGFP-tagged DYRK1A is expressed in HEK-293 cell
enzyme PrkD expression analysis, recombinant expression of His- or GST-tagged enzyme in Escherichia coli strain BL21(DE3)
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) codon plus RIL, plasmid pcDNA3.1
expressed in Mus musculus
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expression in Escherichia coli strain DH5alpha as GST-fusion protein, expression in 293A cells
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expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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fusion protein of DYRK1A accumulates in the nucleus of transfected COS-7 and HEK293 cells, expression in Escherichia coli
gene dyrk1A, Dyrk1A and HA-tagged SRp55 are cotransfected into HEK-293FT cells for 48 h, and SRp55 is immunoprecipitated with anti-HA antibodies. Dyrk1A is coimmunoprecipitated by SRp55. SRp55 interacts with Dyrk1A through its RRM domain. DYRK1A and SRp55 coexpression and colocalization in HeLA cell nuclei
gene DYRK1A, quantitative expression analysis
gene DYRK3, recombinant expression of GST-tagged wild-type and mutant enzymes
gene DYRK4, DNA and amino acid sequence determination and analysis, splicing variants analysis and comparison to the human splicing variants, expression analysis, overview. Recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS and of the GFP-tagged DYRK4 N-terminus in HEK-293T cells
gene DYRK4, DNA and amino acid sequence determination and analysis, splicing variants analysis and comparison to the murine splicing variants, expression analysis, overview. Recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS and in insect cells
gene TAR1, DNA and amino acid sequence determination and analysis, genetic organization
gene TTK, quantitative real time reverse transcription PCR enzyme expression analysis
genomic clones of DYRK3 isolated from a 129svJ Lambda phage library, transgenic mice generated, DYRK3 gene deletion in E14 ES cells using a floxed PGKneo targeting vector, targeted cells injected into C57BL/6J blastocysts, transgenic pA2gata1-DYRK3 mice prepared using an Myc epitope-tagged mDYRK3 cDNA within a pA2gata1 vector
GmSARK, quantitative RT-PCR analysis, inducible overexpression in Arabidopsis thaliana leads to early leaf senescence, chloroplast destruction, and abnormal flower morphology. GmSARK-overexpressing seedlings reveal a multitude of changes in phytohormone synthesis and signaling, specifically the repression of cytokinin functions and the induction of auxin and ethylene pathways. Overexpressing GmSARK induces the expression of critical senescence-related transcription factors, including NAC1, NAC2, WRKY6, and AtNAP, in Arabidopsis seedlings
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green fluorescent protein fusion protein of DYRK1B is found mainly in the nucleus of transfected COS-7 cells
isozyme DPK1, DNA and amino acid sequence determination and analysis, gene mapping, expression analysis under stress conditions
isozyme DPK2, DNA and amino acid sequence determination and analysis, gene mapping, expression analysis under stress conditions
isozyme DPK3, DNA and amino acid sequence determination and analysis, gene mapping, expression analysis under stress conditions
isozyme DPK4, DNA and amino acid sequence determination and analysis, gene mapping, expression analysis under stress conditions
overexpression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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phylogenetic tree of kinases derived from the kinase core sequence, overview, overexpression as GST-fusion protein under control of the galactose-inducible GAL1 promotor in Escherichia coli, determination of 5'-end sequences
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PrkG expression analysis, recombinant expression of His- or GST-tagged enzyme in Escherichia coli strain BL21(DE3)
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quantitative real-time PCR expression analysis of DYRK2 expression in colorectal carcinoma samples
recombinant Dyrk1A-protein expressed in mammalian expression vector pcDNA3, wild-type and mutant
recombinant expression of His6-tagged Dyrk1b kinase domain, residues 78-451
sequence analysis for enzyme domain determination
single-copy gene, DNA and amino acid sequence determination and analysis, comparison of subdomain sequences with those of Arabidopsis thaliana
the catalytic domain of DYRK1A is expressed in Escherichia coli BL21(DE3) cells
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the dyrk1a gene is located in the Down syndrome critical region (DSCR) on chromosome 21 and full or partial trisomy of DSCR in Down syndrome (DS) leads to overexpression of DYRK1A, recombinant expression of His6-tagged Dyrk1a kinase domain, residues 126-490
transfected into NIH-3T3 cells
wild-type and mutant DNA fragments of DYRK1A, vectors pCMV-Tag2B, pRK5, pCITE4, pGEX-5X-1, pCDNA3-HA
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
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sequence analysis for enzyme domain determination
Thermospora curvatum
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