Aliases for PRKCI Gene
External Ids for PRKCI Gene
Previous HGNC Symbols for PRKCI Gene
Previous GeneCards Identifiers for PRKCI Gene
This gene encodes a member of the protein kinase C (PKC) family of serine/threonine protein kinases. The PKC family comprises at least eight members, which are differentially expressed and are involved in a wide variety of cellular processes. This protein kinase is calcium-independent and phospholipid-dependent. It is not activated by phorbolesters or diacylglycerol. This kinase can be recruited to vesicle tubular clusters (VTCs) by direct interaction with the small GTPase RAB2, where this kinase phosphorylates glyceraldehyde-3-phosphate dehydrogenase (GAPD/GAPDH) and plays a role in microtubule dynamics in the early secretory pathway. This kinase is found to be necessary for BCL-ABL-mediated resistance to drug-induced apoptosis and therefore protects leukemia cells against drug-induced apoptosis. There is a single exon pseudogene mapped on chromosome X. [provided by RefSeq, Jul 2008]
GeneCards Summary for PRKCI Gene
PRKCI (Protein Kinase C, Iota) is a Protein Coding gene. Among its related pathways are Signaling by FGFR and GPCR Pathway. GO annotations related to this gene include protein serine/threonine kinase activity and protein kinase activity. An important paralog of this gene is PRKCB.
UniProtKB/Swiss-Prot for PRKCI Gene
Calcium- and diacylglycerol-independent serine/ threonine-protein kinase that plays a general protective role against apoptotic stimuli, is involved in NF-kappa-B activation, cell survival, differentiation and polarity, and contributes to the regulation of microtubule dynamics in the early secretory pathway. Is necessary for BCR-ABL oncogene-mediated resistance to apoptotic drug in leukemia cells, protecting leukemia cells against drug-induced apoptosis. In cultured neurons, prevents amyloid beta protein-induced apoptosis by interrupting cell death process at a very early step. In glioblastoma cells, may function downstream of phosphatidylinositol 3-kinase (PI(3)K) and PDPK1 in the promotion of cell survival by phosphorylating and inhibiting the pro-apoptotic factor BAD. Can form a protein complex in non-small cell lung cancer (NSCLC) cells with PARD6A and ECT2 and regulate ECT2 oncogenic activity by phosphorylation, which in turn promotes transformed growth and invasion. In response to nerve growth factor (NGF), acts downstream of SRC to phosphorylate and activate IRAK1, allowing the subsequent activation of NF-kappa-B and neuronal cell survival. Functions in the organization of the apical domain in epithelial cells by phosphorylating EZR. This step is crucial for activation and normal distribution of EZR at the early stages of intestinal epithelial cell differentiation. Forms a protein complex with LLGL1 and PARD6B independently of PARD3 to regulate epithelial cell polarity. Plays a role in microtubule dynamics in the early secretory pathway through interaction with RAB2A and GAPDH and recruitment to vesicular tubular clusters (VTCs). In human coronary artery endothelial cells (HCAEC), is activated by saturated fatty acids and mediates lipid-induced apoptosis.
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.