A casein kinase I isoenzyme that plays a role in intracellular signaling pathways including the WNT SIGNALING PATHWAY, the CELL CYCLE, membrane trafficking, and RNA processing. Multiple isoforms of casein kinase I alpha exist and are due to ALTERNATIVE SPLICING.
A cyclic GMP-dependent protein kinase subtype that is expressed in SMOOTH MUSCLE tissues and plays a role in regulation of smooth muscle contraction. Two isoforms, PKGIalpha and PKGIbeta, of the type I protein kinase exist due to alternative splicing of its mRNA.
A group of cyclic GMP-dependent enzymes that catalyze the phosphorylation of SERINE or THREONINE residues of proteins.
A group of protein-serine-threonine kinases that was originally identified as being responsible for the PHOSPHORYLATION of CASEINS. They are ubiquitous enzymes that have a preference for acidic proteins. Casein kinases play a role in SIGNAL TRANSDUCTION by phosphorylating a variety of regulatory cytoplasmic and regulatory nuclear proteins.
A ubiquitous casein kinase that is comprised of two distinct catalytic subunits and dimeric regulatory subunit. Casein kinase II has been shown to phosphorylate a large number of substrates, many of which are proteins involved in the regulation of gene expression.
A mixture of related phosphoproteins occurring in milk and cheese. The group is characterized as one of the most nutritive milk proteins, containing all of the common amino acids and rich in the essential ones.
A casein kinase that was originally described as a monomeric enzyme with a molecular weight of 30-40 kDa. Several ISOENZYMES of casein kinase I have been found which are encoded by separate genes. Many of the casein kinase I isoenzymes have been shown to play distinctive roles in intracellular SIGNAL TRANSDUCTION.
A casein kinase I isoenzyme with specificity for proteins involved the regulation of the CIRCADIAN RHYTHM.
A casein kinase I isoenzyme that plays a regulatory role in a variety of cellular functions including vesicular transport, CHROMOSOME SEGREGATION; CYTOKINESIS, developmental processes, and the CIRCADIAN RHYTHM.

Protein kinase CK1alpha regulates mRNA binding by heterogeneous nuclear ribonucleoprotein C in response to physiologic levels of hydrogen peroxide. (1/41)

At low concentrations, hydrogen peroxide (H(2)O(2)) is a positive endogenous regulator of mammalian cell proliferation and survival; however, the signal transduction pathways involved in these processes are poorly understood. In primary human endothelial cells, low concentrations of H(2)O(2) stimulated the rapid phosphorylation of the acidic C-terminal domain (ACD) of heterogeneous nuclear ribonucleoprotein C (hnRNP-C), a nuclear restricted pre-mRNA-binding protein, at Ser(240) and at Ser(225)-Ser(228). A kinase activity was identified in mouse liver that phosphorylates the ACD of hnRNP-C at Ser(240) and at two sites at Ser(225)-Ser(228). The kinase was purified and identified by tandem mass spectrometry as protein kinase CK1alpha (formerly casein kinase 1alpha). Protein kinase CK1alpha immunoprecipitated from primary human endothelial cell nuclei also phosphorylated the ACD of hnRNP-C at these positions. Pretreatment of endothelial cells with the protein kinase CK1-specific inhibitor IC261 prevented the H(2)O(2)-stimulated phosphorylation of hnRNP-C. Utilizing phosphoserine-mimicking Ser-to-Glu point mutations, the effects of phosphorylation on hnRNP-C function were investigated by quantitative equilibrium fluorescence RNA binding analyses. Wild-type hnRNP-C1 and hnRNP-C1 modified at the basal sites of phosphorylation (S247E and S286E) both avidly bound RNA with similar binding constants. In contrast, hnRNP-C1 that was also modified at the CK1alpha phosphorylation sites exhibited a 14-500-fold decrease in binding affinity, demonstrating that CK1alpha-mediated phosphorylation modulates the mRNA binding ability of hnRNP-C.  (+info)

Physiological role for casein kinase 1 in glutamatergic synaptic transmission. (2/41)

Casein kinase 1 (CK1) is a highly conserved serine/threonine kinase, present in virtually all cell types, in which it phosphorylates a wide variety of substrates. So far, no role has been found for this ubiquitous protein kinase in the physiology of nerve cells. In the present study, we show that CK1 regulates fast synaptic transmission mediated by glutamate, the major excitatory neurotransmitter in the brain. Through the use of CK1 inhibitors, we present evidence that activation of CK1 decreases NMDA receptor activity in the striatum via a mechanism that involves activation by this kinase of protein phosphatase 1 and/or 2A and resultant increased dephosphorylation of NMDA receptors. Indeed, inhibition of CK1 increases NMDA-mediated EPSCs in medium spiny striatal neurons. This effect is associated with an increased phosphorylation of the NR1 and NR2B subunits of the NMDA receptor and is occluded by the phosphatase inhibitor okadaic acid. The mGluR1, but not mGluR5, subclass of metabotropic glutamate receptors uses CK1 to inhibit NMDA-mediated synaptic currents. These results provide the first evidence for a role of CK1 in the regulation of synaptic transmission in the brain.  (+info)

Regulation of p53-MDMX interaction by casein kinase 1 alpha. (3/41)

MDMX is a homolog of MDM2 that is critical for regulating p53 function during mouse development. MDMX degradation is regulated by MDM2-mediated ubiquitination. Whether there are other mechanisms of MDMX regulation is largely unknown. We found that MDMX binds to the casein kinase 1 alpha isoform (CK1alpha) and is phosphorylated by CK1alpha. Expression of CK1alpha stimulates the ability of MDMX to bind to p53 and inhibit p53 transcriptional function. Regulation of MDMX-p53 interaction requires CK1alpha binding to the central region of MDMX and phosphorylation of MDMX on serine 289. Inhibition of CK1alpha expression by isoform-specific small interfering RNA (siRNA) activates p53 and further enhances p53 activity after ionizing irradiation. CK1alpha siRNA also cooperates with DNA damage to induce apoptosis. These results suggest that CK1alpha is a functionally relevant MDMX-binding protein and plays an important role in regulating p53 activity in the absence or presence of stress.  (+info)

Phosphorylation of FADD at serine 194 by CKIalpha regulates its nonapoptotic activities. (4/41)

FADD is essential for death receptor (DR)-induced apoptosis. However, it is also critical for cell cycle progression and proliferation, activities that are regulated by phosphorylation of its C-terminal Ser194, which has also been implicated in sensitizing cancer cells to chemotherapeutic drugs and in regulating FADD's intracellular localization. We now demonstrate that casein kinase Ialpha (CKIalpha) phosphorylates FADD at Ser194 both in vitro and in vivo. FADD-CKIalpha association regulates the subcellular localization of FADD, and phosphorylated FADD was found to colocalize with CKIalpha on the spindle poles in metaphase. Inhibition of CKIalpha diminished FADD phosphorylation, prevented the ability of Taxol to arrest cells in mitosis, and blocked mitogen-induced proliferation of mouse splenocytes. In contrast, a low level of cycling splenocytes from mice expressing FADD with a mutated phosphorylation site was insensitive to CKI inhibition. These data suggest that phosphorylation of FADD by CKI is a crucial event during mitosis.  (+info)

Phosphorylation by double-time/CKIepsilon and CKIalpha targets cubitus interruptus for Slimb/beta-TRCP-mediated proteolytic processing. (5/41)

Hedgehog (Hh) proteins govern animal development by regulating the Gli/Ci family of transcription factors. In Drosophila, Hh signaling blocks proteolytic processing of full-length Ci to generate a truncated repressor form. Ci processing requires sequential phosphorylation by PKA, GSK3, and a casein kinase I (CKI) family member(s). Here we show that Double-time (DBT)/CKIepsilon and CKIalpha act in conjunction to promote Ci processing. CKI phosphorylates Ci at three clusters of serine residues primed by PKA and GSK3 phosphorylation. CKI phosphorylation of Ci confers binding to the F-box protein Slimb/beta-TRCP, the substrate recognition component of the SCF(Slimb/beta-TRCP) ubiquitin ligase required for Ci processing. CKI phosphorylation sites act cooperatively to promote Ci processing in vivo. Substitution of Ci phosphorylation clusters with a canonical Slimb/beta-TRCP recognition motif in beta-catenin renders Slimb/beta-TRCP binding and Ci processing independent of CKI. We propose that phosphorylation of Ci by CKI creates multiple Slimb/beta-TRCP binding sites that act cooperatively to recruit SCF(Slimb/beta-TRCP).  (+info)

Coordination of NF-kappaB and NFAT antagonism by the forkhead transcription factor Foxd1. (6/41)

Forkhead transcription factors play critical roles in the maintenance of immune homeostasis. In this study, we demonstrate that this regulation most likely involves intricate interactions between the forkhead family members and inflammatory transcription factors: the forkhead member Foxd1 coordinates the regulation of the activity of two key inflammatory transcription factors, NF-AT and NF-kappaB, with Foxd1 deficiency resulting in multiorgan, systemic inflammation, exaggerated Th cell-derived cytokine production, and T cell proliferation in autologous MLRs. Foxd1-deficient T cells possess increased activity of both NF-AT and NF-kappaB: the former correlates with the ability of Foxd1 to regulate casein kinase 1, an NF-AT inhibitory kinase; the latter with the ability of Foxd1 to regulate Foxj1, which regulates the NF-kappaB inhibitory subunit IkappaB beta. Thus, Foxd1 modulates inflammatory reactions and prevents autoimmunity by directly regulating anti-inflammatory regulators of the NF-AT pathway, and by coordinating the suppression of the NF-kappaB pathway via Foxj1. These findings indicate the presence of a general network of forkhead proteins that enforce T cell quiescence.  (+info)

Planar polarity is positively regulated by casein kinase Iepsilon in Drosophila. (7/41)

Members of the casein kinase I (CKI) family have been implicated in regulating canonical Wnt/Wingless (Wg) signaling by phosphorylating multiple pathway components. Overexpression of CKI in vertebrate embryos activates Wg signaling, and one target is thought to be the cytoplasmic effector Dishevelled (Dsh), which is an in vitro target of CKI phosphorylation. Phosphorylation of Dsh by CKI has also been suggested to switch its activity from noncanonical to canonical Wingless signaling. However, in vivo loss-of-function experiments have failed to identify a clear role for CKI in positive regulation of Wg signaling. By examining hypomorphic mutations of the Drosophila CKIepsilon homolog discs overgrown (dco)/double-time, we now show that it is an essential component of the noncanonical/planar cell polarity pathway. Genetic interactions indicate that dco acts positively in planar polarity signaling, demonstrating that it does not act as a switch between canonical and noncanonical pathways. Mutations in dco result in a reduced level of Dishevelled phosphorylation in vivo. Furthermore, in these mutants, Dishevelled fails to adopt its characteristic asymmetric subcellular localisation at the distal end of pupal wing cells, and the site of hair outgrowth is disrupted. Finally, we also find that dco function in polarity is partially redundant with CKIalpha.  (+info)

Wnt-5a/Ca2+-induced NFAT activity is counteracted by Wnt-5a/Yes-Cdc42-casein kinase 1alpha signaling in human mammary epithelial cells. (8/41)

Wnt-5a has been shown to influence the metastatic behavior of human breast cancer cells, and the loss of Wnt-5a expression is associated with metastatic disease. We show here that NFAT1, a transcription factor connected with breast cancer metastasis, is activated by Wnt-5a through a Ca2+ signaling pathway in human breast epithelial cells. This activation was simultaneously counteracted by a Wnt-5a-induced Yes/Cdc42 signaling pathway. The observation that inhibition of the Wnt-5a/Yes/Cdc42 signal prolonged the duration of ionomycin-induced NFAT1 activation revealed the general importance of this pathway. The Wnt-5a-induced inhibition of NFAT1 did not require glycogen synthase kinase 3beta, JNK, or Pak1 activity or modulation of the cytoskeleton. Instead, we observed that Wnt-5a induced a complex formation of NFAT1/casein kinase 1alpha, even upon treatment with ionomycin, which was blocked upon inhibition of the Wnt-5a/Yes/Cdc42 signaling pathway. Our results explain why Wnt-5a/Ca2+-induced NFAT activity is hard to detect and suggest a novel mechanism by which Wnt-5a can suppress tumor-specific, agonist-induced NFAT activity and thus the metastatic behavior of breast cancer cells.  (+info)

Casein Kinase 1 Alpha (CK1α) is a serine/threonine protein kinase that plays a crucial role in various cellular processes, including the regulation of circadian rhythms, DNA damage response, and Wnt signaling pathway. It phosphorylates specific serine and threonine residues on its target proteins, thereby modulating their activity, stability, or localization. CK1α is widely expressed in different tissues and has been implicated in several diseases, such as cancer and neurodegenerative disorders. Inhibition of CK1α has emerged as a potential therapeutic strategy for treating these conditions.

Cyclic guanosine monophosphate (cGMP)-dependent protein kinase type I (PKG I) is a major enzyme responsible for mediating the effects of cGMP, which is a second messenger molecule involved in various cellular signaling pathways. PKG I is a serine/threonine protein kinase that is activated by binding to cGMP.

PKG I exists in two isoforms, alpha and beta, which are encoded by separate genes but share a similar structure and function. The enzyme consists of a regulatory domain, which contains the cGMP-binding sites, and a catalytic domain, which carries out the phosphorylation of target proteins.

PKG I plays a critical role in regulating various physiological processes, including smooth muscle relaxation, cardiac contractility, platelet aggregation, and neuronal signaling. It does so by phosphorylating specific protein targets that control these processes, such as ion channels, enzymes, and cytoskeletal proteins.

Defects in PKG I function have been implicated in several human diseases, including pulmonary hypertension, heart failure, and erectile dysfunction. Therefore, PKG I is an important therapeutic target for the development of drugs to treat these conditions.

Cyclic guanosine monophosphate (cGMP)-dependent protein kinases (PKGs) are a type of enzyme that add phosphate groups to other proteins, thereby modifying their function. These kinases are activated by cGMP, which is a second messenger molecule that helps transmit signals within cells. PKGs play important roles in various cellular processes, including smooth muscle relaxation, platelet aggregation, and cardiac contractility. They have been implicated in the regulation of a number of physiological functions, such as blood flow, inflammation, and learning and memory. There are two main isoforms of cGMP-dependent protein kinases, PKG I and PKG II, which differ in their tissue distribution, regulatory properties, and substrate specificity.

Casein kinases are a family of protein kinases that play important roles in various cellular processes, including signal transduction, cell cycle regulation, and DNA damage repair. These enzymes phosphorylate serine and threonine residues on their target proteins by transferring a phosphate group from ATP to the hydroxyl side chain of these amino acids.

There are several isoforms of casein kinases, including Casein Kinase 1 (CK1) and Casein Kinase 2 (CK2), which differ in their structure, substrate specificity, and cellular functions. CK1 is involved in various signaling pathways, such as the Wnt signaling pathway, and regulates processes such as gene transcription, DNA repair, and circadian rhythm. CK2, on the other hand, is a highly conserved serine/threonine protein kinase that plays a role in many cellular processes, including cell division, apoptosis, and transcriptional regulation.

Dysregulation of casein kinases has been implicated in various diseases, including cancer, neurodegenerative disorders, and cardiovascular disease. Therefore, these enzymes are considered important targets for the development of new therapeutic strategies.

Casein Kinase II (CK2) is a serine/threonine protein kinase that is widely expressed in eukaryotic cells and is involved in the regulation of various cellular processes. It is a heterotetrameric enzyme, consisting of two catalytic subunits (alpha and alpha') and two regulatory subunits (beta).

CK2 phosphorylates a wide range of substrates, including transcription factors, signaling proteins, and other kinases. It is known to play roles in cell cycle regulation, apoptosis, DNA damage response, and protein stability, among others. CK2 activity is often found to be elevated in various types of cancer, making it a potential target for cancer therapy.

Caseins are a group of phosphoproteins found in the milk of mammals, including cows and humans. They are the major proteins in milk, making up about 80% of the total protein content. Caseins are characterized by their ability to form micelles, or tiny particles, in milk when it is mixed with calcium. This property allows caseins to help transport calcium and other minerals throughout the body.

Caseins are also known for their nutritional value, as they provide essential amino acids and are easily digestible. They are often used as ingredients in infant formula and other food products. Additionally, caseins have been studied for their potential health benefits, such as reducing the risk of cardiovascular disease and improving bone health. However, more research is needed to confirm these potential benefits.

Casein Kinase 1 (CK1) is a type of serine/threonine protein kinase that plays a crucial role in various cellular processes, including the regulation of circadian rhythms, signal transduction, and DNA damage response. CK1 phosphorylates specific serine or threonine residues on its target proteins, thereby modulating their activity, localization, or stability.

There are several isoforms of CK1, including CK1α, CK1δ, CK1ε, and CK1γ, which exhibit distinct subcellular distributions and functions. Dysregulation of CK1 has been implicated in several human diseases, such as cancer, neurodegenerative disorders, and metabolic syndromes. Therefore, understanding the molecular mechanisms underlying CK1 function is essential for developing novel therapeutic strategies to treat these conditions.

Casein Kinase 1 Epsilon (CSNK1E or CK1ε) is a serine/threonine protein kinase that plays a role in various cellular processes, including the regulation of circadian rhythms, DNA damage response, and Wnt signaling pathway. It phosphorylates specific serine and threonine residues on its target proteins, thereby modulating their activity, localization, or stability. Mutations in the CSNK1E gene have been associated with certain human diseases, such as Familiial Advanced Sleep Phase Disorder (FASPD).

Casein Kinase 1 Delta (CK1δ) is a serine/threonine protein kinase that plays a crucial role in various cellular processes, including the regulation of circadian rhythms, DNA damage response, and Wnt signaling pathway. It phosphorylates specific target proteins on serine or threonine residues, thereby modulating their activity, stability, or localization. CK1δ is widely expressed in various tissues and has been implicated in several diseases, such as cancer, neurodegenerative disorders, and inflammatory conditions. Inhibitors of CK1δ are being investigated as potential therapeutic agents for these diseases.

"Identification of casein kinase Ialpha interacting protein partners". FEBS Letters. 517 (1-3): 167-71. doi:10.1016/s0014-5793( ... Casein kinase 1, alpha 1 Nucleolin, P110α, PRKCI, Protein kinase D1, and Protein kinase Mζ. Model organisms have been used in ... "Casein kinase I associates with members of the centaurin-alpha family of phosphatidylinositol 3,4,5-trisphosphate-binding ... "Casein kinase I associates with members of the centaurin-alpha family of phosphatidylinositol 3,4,5-trisphosphate-binding ...
Dubois T, Howell S, Zemlickova E, Aitken A (Apr 2002). "Identification of casein kinase Ialpha interacting protein partners". ... Casein kinase I isoform alpha is an enzyme that in humans is encoded by the CSNK1A1 gene. Casein kinase 1, alpha 1 has been ... Zhang Y, Qiu WJ, Chan SC, Han J, He X, Lin SC (May 2002). "Casein kinase I and casein kinase II differentially regulate axin ... Casein kinase 1 GRCh38: Ensembl release 89: ENSG00000113712 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000024576 ...
Dubois T, Howell S, Zemlickova E, Aitken A (April 2002). "Identification of casein kinase Ialpha interacting protein partners ... "Transcriptional repressor ERF is a Ras/mitogen-activated protein kinase target that regulates cellular proliferation". ...
Dubois T, Howell S, Zemlickova E, Aitken A (April 2002). "Identification of casein kinase Ialpha interacting protein partners ... Zemlickova E, Johannes FJ, Aitken A, Dubois T (March 2004). "Association of CPI-17 with protein kinase C and casein kinase I". ... Multiple kinases are identified to phosphorylate CPI-17, such as PKC, ROCK, PKN, ZIPK, ILK, and PAK. Agonist stimulation of ... Protein phosphatase 1 regulatory subunit 14A also known as CPI-17 (C-kinase potentiated Protein phosphatase-1 Inhibitor Mr = 17 ...
Dubois T, Howell S, Zemlickova E, Aitken A (Apr 2002). "Identification of casein kinase Ialpha interacting protein partners". ... "Regulated exocytosis contributes to protein kinase C potentiation of vanilloid receptor activity". The Journal of Biological ... "Regulated exocytosis contributes to protein kinase C potentiation of vanilloid receptor activity". The Journal of Biological ...
Dubois T, Howell S, Zemlickova E, Aitken A (Apr 2002). "Identification of casein kinase Ialpha interacting protein partners". ... Kim YM, Barak LS, Caron MG, Benovic JL (May 2002). "Regulation of arrestin-3 phosphorylation by casein kinase II". The Journal ...
Dubois T, Howell S, Zemlickova E, Aitken A (Apr 2002). "Identification of casein kinase Ialpha interacting protein partners". ... "High mobility group proteins 1 and 2 can function as DNA-binding regulatory components for DNA-dependent protein kinase in ...
Dubois T, Howell S, Zemlickova E, Aitken A (2002). "Identification of casein kinase Ialpha interacting protein partners". FEBS ... Spanner S, Ansell GB (1979). "Choline kinase and ethanolamine kinase activity in the cytosol of nerve endings from rat ... Choline kinase alpha is an enzyme that in humans is encoded by the CHKA gene. The major pathway for the biosynthesis of ... 1999). "Increased choline kinase activity and elevated phosphocholine levels in human colon cancer". Jpn. J. Cancer Res. 90 (4 ...
"The AP-3 complex required for endosomal synaptic vesicle biogenesis is associated with a casein kinase Ialpha-like isoform". ...
... casein kinase i MeSH D08.811.913.696.620.682.700.140.300.100 - casein kinase ialpha MeSH D08.811.913.696.620.682.700.140. ... map kinase kinase kinase 1 MeSH D08.811.913.696.620.682.700.559.200 - map kinase kinase kinase 2 MeSH D08.811.913.696.620.682. ... map kinase kinase kinase 3 MeSH D08.811.913.696.620.682.700.559.400 - map kinase kinase kinase 4 MeSH D08.811.913.696.620.682. ... casein kinase idelta MeSH D08.811.913.696.620.682.700.140.300.300 - casein kinase iepsilon MeSH D08.811.913.696.620.682.700.140 ...
... casein kinase ialpha MeSH D12.776.476.150.300.200 - casein kinase idelta MeSH D12.776.476.150.300.300 - casein kinase iepsilon ... cdc2 protein kinase MeSH D12.776.476.250.067.500 - cdc28 protein kinase, s cerevisiae MeSH D12.776.476.250.067.875 - cyclin- ... dependent kinase 5 MeSH D12.776.476.250.067.900 - cyclin-dependent kinase 9 MeSH D12.776.476.250.580.500 - cdc2 protein kinase ... mitogen-activated protein kinase 1 MeSH D12.776.476.450.169.750 - mitogen-activated protein kinase 3 MeSH D12.776.476.450. ...
... casein kinase i MeSH D12.644.360.150.300.100 - casein kinase ialpha MeSH D12.644.360.150.300.200 - casein kinase idelta MeSH ... map kinase kinase kinase 1 MeSH D12.644.360.400.200 - map kinase kinase kinase 2 MeSH D12.644.360.400.300 - map kinase kinase ... kinase 3 MeSH D12.644.360.400.400 - map kinase kinase kinase 4 MeSH D12.644.360.400.500 - map kinase kinase kinase 5 MeSH ... map kinase kinase 1 MeSH D12.644.360.440.200 - map kinase kinase 2 MeSH D12.644.360.440.300 - map kinase kinase 3 MeSH D12.644. ...
"Identification of casein kinase Ialpha interacting protein partners". FEBS Letters. 517 (1-3): 167-71. doi:10.1016/s0014-5793( ... Casein kinase 1, alpha 1 Nucleolin, P110α, PRKCI, Protein kinase D1, and Protein kinase Mζ. Model organisms have been used in ... "Casein kinase I associates with members of the centaurin-alpha family of phosphatidylinositol 3,4,5-trisphosphate-binding ... "Casein kinase I associates with members of the centaurin-alpha family of phosphatidylinositol 3,4,5-trisphosphate-binding ...
D12.776.476.150.299 Casein Kinase Ialpha D12.644.360.150.300.100 D5.500.117.750.100 D12.776.476.150.300.100 D12.776.476.81. ... D12.776.476.150.299.300 Casein Kinase II D12.644.360.150.600 Casein Kinases D12.644.360.150 CD4 Lymphocyte Count E1.450.375.107 ... D2.33.755.624.698.207 Casein Kinase I D12.644.360.150.300 D5.500.117.750 D12.776.476.150.300 D12.776.476.81.750 ... D12.776.476.150.299.200 Casein Kinase Iepsilon D12.644.360.150.300.300 D5.500.117.750.300 D12.776.476.150.300.300 D12.776. ...
D12.776.476.150.299 Casein Kinase Ialpha D12.644.360.150.300.100 D5.500.117.750.100 D12.776.476.150.300.100 D12.776.476.81. ... D12.776.476.150.299.300 Casein Kinase II D12.644.360.150.600 Casein Kinases D12.644.360.150 CD4 Lymphocyte Count E1.450.375.107 ... D2.33.755.624.698.207 Casein Kinase I D12.644.360.150.300 D5.500.117.750 D12.776.476.150.300 D12.776.476.81.750 ... D12.776.476.150.299.200 Casein Kinase Iepsilon D12.644.360.150.300.300 D5.500.117.750.300 D12.776.476.150.300.300 D12.776. ...
Casein Kinase II Caseína Quinase II Quinasa de la Caseína II Casein Kinase Ialpha Caseína Quinase Ialfa Quinasa Ialpha de la ... Casein Kinase Iepsilon Caseína Quinase Iépsilon Quinasa Iépsilon de la Caseína Casein Kinases Caseína Quinases Quinasas de la ... MAP Kinase Kinase Kinase 1 MAP Quinase Quinase Quinase 1 Quinasa 1 de Qinasa de Quinasa MAP ... MAP Kinase Kinase Kinase 2 MAP Quinase Quinase Quinase 2 Quinasa 2 de Qinasa de Quinasa MAP ...
Casein Kinase I Quinasa de la Caseína I Caseína Quinase Ialfa Casein Kinase Ialpha Quinasa Ialpha de la Caseína ... Kinase Kinase Kinase 1 Quinasa 1 de Qinasa de Quinasa MAP MAP Quinase Quinase Quinase 2 MAP Kinase Kinase Kinase 2 Quinasa 2 de ... Kinase Kinase Kinase 3 Quinasa 3 de Qinasa de Quinasa MAP MAP Quinase Quinase Quinase 4 MAP Kinase Kinase Kinase 4 Quinasa 4 de ... Casein Kinase Idelta Quinasa Idelta de la Caseína Caseína Quinase Iépsilon Casein Kinase Iepsilon Quinasa Iépsilon de la ...
Casein Kinase Ialpha / physiology* Actions. * Search in PubMed * Search in MeSH * Add to Search ...
... functional interactions with casein kinase Ialpha, Galpha(i) proteins, and ERK1/2 signaling.. García-Fuster MJ; Ramos-Miguel A ... MDMX inhibits casein kinase 1α activity and stimulates Wnt signaling.. Huang Q; Chen L; Schonbrunn E; Chen J. EMBO J; 2020 Jul ... 7. Casein kinase 1α-dependent feedback loop controls autophagy in RAS-driven cancers.. Cheong JK; Zhang F; Chua PJ; Bay BH; ... Suppression of casein kinase 1alpha in melanoma cells induces a switch in beta-catenin signaling to promote metastasis. ...
D12.776.476.150.299 Casein Kinase Ialpha D12.644.360.150.300.100 D5.500.117.750.100 D12.776.476.150.300.100 D12.776.476.81. ... D12.776.476.150.299.300 Casein Kinase II D12.644.360.150.600 Casein Kinases D12.644.360.150 CD4 Lymphocyte Count E1.450.375.107 ... D2.33.755.624.698.207 Casein Kinase I D12.644.360.150.300 D5.500.117.750 D12.776.476.150.300 D12.776.476.81.750 ... D12.776.476.150.299.200 Casein Kinase Iepsilon D12.644.360.150.300.300 D5.500.117.750.300 D12.776.476.150.300.300 D12.776. ...
Casein Kinases [D08.811.913.696.620.682.700.140] * Casein Kinase I [D08.811.913.696.620.682.700.140.300] * Casein Kinase Ialpha ... Casein Kinase I alpha Casein Kinase IalphaL Casein Kinase IalphaLS Casein Kinase IalphaS Registry Number. EC 2.7.11.1. Related ... Casein Kinases [D12.776.476.563.140] * Casein Kinase I [D12.776.476.563.140.300] * Casein Kinase Ialpha [D12.776.476.563. ... Multiple isoforms of casein kinase I alpha exist and are due to ALTERNATIVE SPLICING.. Terms. Casein Kinase Ialpha Preferred ...
Casein Kinases [D08.811.913.696.620.682.700.140] * Casein Kinase I [D08.811.913.696.620.682.700.140.300] * Casein Kinase Ialpha ... Casein Kinase I alpha Casein Kinase IalphaL Casein Kinase IalphaLS Casein Kinase IalphaS Registry Number. EC 2.7.11.1. Related ... Casein Kinases [D12.776.476.563.140] * Casein Kinase I [D12.776.476.563.140.300] * Casein Kinase Ialpha [D12.776.476.563. ... Multiple isoforms of casein kinase I alpha exist and are due to ALTERNATIVE SPLICING.. Terms. Casein Kinase Ialpha Preferred ...
Cascara N0000170587 Casein Kinase I N0000170588 Casein Kinase Ialpha N0000170589 Casein Kinase Idelta N0000170590 Casein Kinase ... MAP Kinase Kinase 6 N0000170606 MAP Kinase Kinase 7 N0000170480 MAP Kinase Kinase Kinase 1 N0000170477 MAP Kinase Kinase Kinase ... MAP Kinase Kinase Kinase 3 N0000170479 MAP Kinase Kinase Kinase 4 N0000170481 MAP Kinase Kinase Kinase 5 N0000170472 MAP Kinase ... N0000170603 MAP Kinase Kinase 1 N0000170602 MAP Kinase Kinase 2 N0000170601 MAP Kinase Kinase 3 N0000170607 MAP Kinase Kinase 4 ...
Multiple isoforms of casein kinase Ialpha exist and are due ALTERNATIVE MRNA SPLICING. HN - 2005(2000) MH - Casein Kinase ... The B-raf Kinases are MAP kinase kinase kinases that have specificity for MAP KINASE KINASE 1 and MAP KINASE KINASE 2. HN - ... A 180-kDa MAP kinase kinase kinase with specificity for MAP KINASE KINASE 4 and MAP KINASE KINASE 6. HN - 2005(1997) MH - MAP ... A 70-kDa MAPK kinase kinase with specificity for MAP KINASE KINASE 5. HN - 2005(1999) MH - MAP Kinase Kinase Kinase 4 UI - ...
D12.776.476.150.299 Casein Kinase Ialpha D12.644.360.150.300.100 D5.500.117.750.100 D12.776.476.150.300.100 D12.776.476.81. ... D12.776.476.150.299.300 Casein Kinase II D12.644.360.150.600 Casein Kinases D12.644.360.150 CD4 Lymphocyte Count E1.450.375.107 ... D2.33.755.624.698.207 Casein Kinase I D12.644.360.150.300 D5.500.117.750 D12.776.476.150.300 D12.776.476.81.750 ... D12.776.476.150.299.200 Casein Kinase Iepsilon D12.644.360.150.300.300 D5.500.117.750.300 D12.776.476.150.300.300 D12.776. ...
Casein Kinase I Quinasa de la Caseína I Caseína Quinase Ialfa Casein Kinase Ialpha Quinasa Ialpha de la Caseína ... Kinase Kinase Kinase 1 Quinasa 1 de Qinasa de Quinasa MAP MAP Quinase Quinase Quinase 2 MAP Kinase Kinase Kinase 2 Quinasa 2 de ... Kinase Kinase Kinase 3 Quinasa 3 de Qinasa de Quinasa MAP MAP Quinase Quinase Quinase 4 MAP Kinase Kinase Kinase 4 Quinasa 4 de ... Casein Kinase Idelta Quinasa Idelta de la Caseína Caseína Quinase Iépsilon Casein Kinase Iepsilon Quinasa Iépsilon de la ...
Casein Kinase I Quinasa de la Caseína I Caseína Quinase Ialfa Casein Kinase Ialpha Quinasa Ialpha de la Caseína ... Kinase Kinase Kinase 1 Quinasa 1 de Qinasa de Quinasa MAP MAP Quinase Quinase Quinase 2 MAP Kinase Kinase Kinase 2 Quinasa 2 de ... Kinase Kinase Kinase 3 Quinasa 3 de Qinasa de Quinasa MAP MAP Quinase Quinase Quinase 4 MAP Kinase Kinase Kinase 4 Quinasa 4 de ... Casein Kinase Idelta Quinasa Idelta de la Caseína Caseína Quinase Iépsilon Casein Kinase Iepsilon Quinasa Iépsilon de la ...

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