Aliases for PRKCQ Gene
External Ids for PRKCQ Gene
Previous GeneCards Identifiers for PRKCQ Gene
Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and the second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role. The protein encoded by this gene is one of the PKC family members. It is a calcium-independent and phospholipid-dependent protein kinase. This kinase is important for T-cell activation. It is required for the activation of the transcription factors NF-kappaB and AP-1, and may link the T cell receptor (TCR) signaling complex to the activation of the transcription factors. [provided by RefSeq, Jul 2008]
GeneCards Summary for PRKCQ Gene
PRKCQ (Protein Kinase C, Theta) is a Protein Coding gene. Diseases associated with PRKCQ include gastrointestinal stromal tumor. Among its related pathways are PI-3K cascade and Signaling by GPCR. GO annotations related to this gene include identical protein binding and ubiquitin-protein transferase activity. An important paralog of this gene is PRKCB.
UniProtKB/Swiss-Prot for PRKCQ Gene
Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that mediates non-redundant functions in T-cell receptor (TCR) signaling, including T-cells activation, proliferation, differentiation and survival, by mediating activation of multiple transcription factors such as NF-kappa-B, JUN, NFATC1 and NFATC2. In TCR-CD3/CD28-co-stimulated T-cells, is required for the activation of NF-kappa-B and JUN, which in turn are essential for IL2 production, and participates to the calcium-dependent NFATC1 and NFATC2 transactivation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11 on several serine residues, inducing CARD11 association with lipid rafts and recruitment of the BCL10-MALT1 complex, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. May also play an indirect role in activation of the non-canonical NF-kappa-B (NFKB2) pathway. In the signaling pathway leading to JUN activation, acts by phosphorylating the mediator STK39/SPAK and may not act through MAP kinases signaling. Plays a critical role in TCR/CD28-induced NFATC1 and NFATC2 transactivation by participating in the regulation of reduced inositol 1,4,5-trisphosphate generation and intracellular calcium mobilization. After costimulation of T-cells through CD28 can phosphorylate CBLB and is required for the ubiquitination and subsequent degradation of CBLB, which is a prerequisite for the activation of TCR. During T-cells differentiation, plays an important role in the development of T-helper 2 (Th2) cells following immune and inflammatory responses, and, in the development of inflammatory autoimmune diseases, is necessary for the activation of IL17-producing Th17 cells. May play a minor role in Th1 response. Upon TCR stimulation, mediates T-cell protective survival signal by phosphorylating BAD, thus protecting T-cells from BAD-induced apoptosis, and by up-regulating BCL-X(L)/BCL2L1 levels through NF-kappa-B and JUN pathways. In platelets, regulates signal transduction downstream of the ITGA2B, CD36/GP4, F2R/PAR1 and F2RL3/PAR4 receptors, playing a positive role in outside-in signaling and granule secretion signal transduction. May relay signals from the activated ITGA2B receptor by regulating the uncoupling of WASP and WIPF1, thereby permitting the regulation of actin filament nucleation and branching activity of the Arp2/3 complex. May mediate inhibitory effects of free fatty acids on insulin signaling by phosphorylating IRS1, which in turn blocks IRS1 tyrosine phosphorylation and downstream activation of the PI3K/AKT pathway. Phosphorylates MSN (moesin) in the presence of phosphatidylglycerol or phosphatidylinositol. Phosphorylates PDPK1 at Ser-504 and Ser-532 and negatively regulates its ability to phosphorylate PKB/AKT1.
Protein kinase C (PKC) refers to a family of serine/threonine protein kinases grouped by their activation mechanism. Classical or conventional PKCs (cPKC alpha-, betaI- , betaII- and gamma-) are activated by phosphatidylserine in a calcium dependent manner and can bind diacylglycerol (DAG). The Ca2+ insensitive novel PKCs (nPKCs epsilon-, delta-, theta- and eta- isotypes) are also activated by DAG and phosphatidylserine. The atypical PKCs (aPKCs iota- and zeta-) are insensitive to Ca2+, DAG and phorbol esters. All PKCs isoforms consist of a highly conserved catalytic domain connected to a regulatory domain via a hinge region. The physiological roles of PKCs are vast. This due to PKC phosphorylation and activation of multiple target proteins, which are involved in signal transduction pathways including, but not limited to, receptor desensitization, modulation of membrane structure events, regulation of transcription, regulation of cell growth, immune responses, and in learning and memory.