Phosphorylates a large number of substrates in the cytoplasm and the nucleus.
Protein Kinase C Epsilon type is a member of the serine- and threonine-specific protein kinase family that can be activated by calcium and the second messenger diacylglycerol. Protein Kinase C Epsilon contains these domains: one AGC-kinase C-terminal domain; one C2 domain; one protein kinase domain and two phorbol-ester/DAG-type zinc fingers. Protein Kinase C Epsilon phosphorylate a variety of protein targets and has been identified to participate in diverse cellular signaling pathways. It has many different cellular functions; such as neuron channel activation; apoptosis; cardioprotection from ischemia; heat shock response; as well as insulin exocytosis. Protein Kinase C Epsilon also serves as the receptor for phorbol esters; a class of tumor promoters.
Protein kinase C iota type, also known as Atypical protein kinase C-lambda/iota, aPKC-lambda/iota and PRKCI, is a cytoplasm, membrane and nucleus protein which belongs to theprotein kinase superfamily, AGC Ser/Thr protein kinase family and PKC subfamily. PRKCI contains oneAGC-kinase C-terminal domain, oneOPR domain, onephorbol-ester/DAG-type zinc finger and oneprotein kinase domain. PRKCI is predominantly expressed in lung and brain, but also expressed at lower levels in many tissues including pancreatic islets. It is highly expressed in non-small cell lung cancers. PRKCI is a calcium-independent, phospholipid-dependent, serine- and threonine-specific kinase. It may play a role in the secretory response to nutrients. PRKCI is involved in cell polarization processes and the formation of epithelial tight junctions. It is implicated in the activation of several signaling pathways including Ras, c-Src and NF-kappa-B pathways. PRKCI functions in both pro- and anti-apoptotic pathways. It functions in the RAC1/ERK signaling required for transformed growth. PRKCI plays a role in microtubule dynamics through interaction with RAB2A and GAPDH and recruitment to vesicular tubular clusters (VTCs). PRKCI might be a target for novel lipid activators that are elevated during nutrient-stimulated insulin secretion.
Serine/threonine-protein kinase D3, also known as Protein kinase C nu type, Protein kinase EPK2, PRKD3, EPK2 and PRKCN, is a cytoplasm and membrane protein which belongs to theprotein kinase superfamily, CAMK Ser/Thr protein kinase family and PKD subfamily. PRKD3 / PRKCN contains onePH domain, twophorbol-ester/DAG-type zinc fingers and oneprotein kinase domain. 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. They 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. PRKD3 / PRKCN converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. It is involved in resistance to oxidative stress. PRKD3 / PRKCN is activated by DAG and phorbol esters. Phorbol-ester/DAG-type domains 1 and 2 bind both DAG and phorbol ester with high affinity and mediate translocation to the cell membrane. Autophosphorylation of Ser-735 and phosphorylation of Ser-731 by PKC relieves auto-inhibition by the PH domain. PRKD3 / PRKCN can be activated rapidly by the agonists of G protein-coupled receptors. It resides in both cytoplasm and nucleus, and its nuclear accumulation is found to be dramatically enhanced in response to its activation. PRKD3 / PRKCN can also be activated after B-cell antigen receptor (BCR) engagement, which requires intact phospholipase C gamma and the involvement of other PKC family members.
Polycystin-1 (also PKD1) is a 500-550 kDa member of the polycystin family of proteins. It is expressed in renal tubule primary cilia, and the membrane region that forms adherens junctions. Polycystin-1 binds to polycystin-2, promoting its insertion into the cell membrane, and regulating its calcium channel activity. In conjunction with polycystin-2, it detects fluid flow and converts this information into calcium signals. It also exists in the ER, where it negatively modulates polycystin-2 mediated calcium release. Mature human polycystin-1 is a 4280 amino acid (aa), 11 transmembrane glycoprotein.
cAMP-Dependent Protein Kinase Inhibitor β (PKI-β) is a member of the PKI family. As a member of the cAMP-dependent protein kinase inhibitor family,It has been shown that PKI-β is an extremely potent competitive inhibitor of cAMP-dependent protein kinase activity; this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains. It may play a role in the protein kinase A (PKA) pathway by interacting with the catalytic subunit of PKA, and overexpression of this gene may play a role in prostate cancer.
Pyruvate Kinase Isozymes R/L (PKLR) belongs to the pyruvate kinase family, There are 4 isozymes of pyruvate kinase in mammals: L, R, M1 and M2. L type is major isozyme in the liver; R is found in red cells; M1 is the main form in muscle, heart and brain; M2 is found in early fetal tissues. PKLR exists as a homotetramer and catalyzes the production of phosphoenolpyruvate from pyruvate and ATP. Defects in PKLR are also the cause of pyruvate kinase deficiency of red cells, which is a frequent cause of hereditary non-spherocytic hemolytic anemia.
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