EC Number |
General Information |
Reference |
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2.7.11.13 | malfunction |
depletion of PKCepsilon in human endothelial cells reduces expression of the cytoprotective genes A1, A20 and Bcl-2. Constitutively active PKCepsilon expressed in human endothelial cells increases mRNA and protein levels of these cytoprotective genes, with up-regulation dependent upon ERK1/2 (extracellular-signal regulated kinase 1/2) activation |
724237 |
2.7.11.13 | malfunction |
knockdown of PKCalpha almost completely reduces myristoylated alanine-rich C kinase substrate phosphorylation, indicating that PKCalpha is responsible for the majority of phosphorylated myristoylated alanine-rich C kinase substrate in the cells |
704702 |
2.7.11.13 | malfunction |
knockdown of PKCdelta accelerates T-cell receptor-induced NF-kappaB activation and IL-2 secretion, suggesting an inhibitory role of PKCdelta in T-cell receptor-mediated NF-kappaB activation. PKCdelta inhibits T-cell receptor-induced NF-kappaB activation by steric hindrance of recruiting TRAF6 to CARMA1 signalosome |
725477 |
2.7.11.13 | malfunction |
overexpression of PKCdelta inhibits CARMA1-mediated NF-kappaB activation |
725477 |
2.7.11.13 | malfunction |
PKC-beta1 and PKC-gamma are important for the development of retinal, as their absence completely inhibits rod differentiation |
725770 |
2.7.11.13 | metabolism |
overexpression of the enzyme isoforms: PKCalpha, PKCbeta, and PKCtheta, but not PKCgamma, stimulates protein kinase CK2 activity |
737786 |
2.7.11.13 | metabolism |
PKC activity controls serine racemase phosphorylation and D-serine levels both in vitro and in vivo |
725768 |
2.7.11.13 | metabolism |
site-specific phosphorylation of casein kinase 1delta by the enzyme contributes to fine-tuning of casein kinase 1delta activity |
760634 |
2.7.11.13 | physiological function |
a significant decline of STAT3 tyrosine phosphorylation is observed by activation of PKC, while inhibition of PKC results in an increase of phosphorylated STAT3 along with a delayed cell cycle exit of progenitors with prolonged PCNA expression |
725770 |
2.7.11.13 | physiological function |
activation of protein kinase C significantly attenuates starvation- or rapamycin-induced LC3 processing. The formation of autophagosomes in response to starvation or rapamycin is blocked by PKC activators. PKC inhibitors dramatically induce LC3 processing and autophagosome formation |
724170 |