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Casein kinase 2 subunit alpha (CSNK2A2) controls numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. CSNK2A2 protein functions as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response.

PI3Ka plays a specific role in apoptosis in human colon cancer cells. Injection of neutralizing antibodies specific to PI3Ka into adenocarcinoma cells induced apoptosis, a response that was reverted by treating cells with caspase inhibitor. It was also shown that PI3Ka mediated phosphorylation of the p85a adapter reduces the lipid kinase activity of the heterodimer and this gives hints for PI3K-dependent signaling events not requiring production of 3’-phosphorylated phosphoinositides.
PI3Ka is a key regulator of the initiation of keratinocyte differentiation. A decrease in PI3Ka activity results in a loss of keratinocyte adhesion to the extracellular membrane and the initiation of early phase differentiation.

pykF (pyruvate kinase I) is a member of the pyruvate kinase family. pykF is an enzyme involved in glycolysis. pykF catalyzes the transfer of a phosphate group from phosphoenolpyruvate (PEP) to ADP, yielding one molecule of pyruvate and one molecule of ATP, a process which also requires a Magnesium ion. This is the final step in the glycolytic pathway, which produces pyruvate molecules, the ultimate product of aerobic glycolysis.

Extracellular signal-regulated kinases (ERKs) or classical MAP kinases are widely expressed protein kinaseintracellular signalingmolecules which are involved in functions including the regulation of meiosis, mitosis, and postmitotic functions in differentiated cells. Many different stimuli, including growth factors, cytokines, virusinfection, ligands for heterotrimeric G protein-coupled receptors, transforming agents, and carcinogens, activate the ERK pathway.
The term, "extracellular signal-regulated kinases", is sometimes used as a synonym for mitogen-activated protein kinase(MAPK), but has more recently been adopted for a specific subset of the mammalianMAPK family. In the MAPK/ERK pathway, Rasactivates c-Raf, followed by MEKand then MAPK1/2 (below). Ras is typically activated by growth hormones through receptor tyrosine kinasesand GRB2/SOS, but may also receive other signals. ERKs are known to activate many transcription factors and some downstream protein kinases. Disruption of the ERK pathway is common in cancers, especially Ras, c-Raf and receptors such as HER2.
Mitogen-activated protein kinase 3 (MAPK3) is also known as "extracellular signal-regulated kinase 1" (ERK1). Transgenic gene knockoutmice lacking MAPK3 are viable and it is thought that MAPK1 can fulfill most MAPK3 functions in most cells. The main exception is in T cells. Mice lacking MAPK3 have reduced T cell development past the CD4+CD8+ stage.

Protein Tyrosine Phosphatase Non Receptor Type-11 or PTPN11 has 2 Src homology 2 domains and part of the tyrosine phosphatase group of proteins. PTPN11 is responsible for the catalyzation of tyrosine residues dephosphorylation in proteins and takes part in the stimulation and activation of Erk/MAP kinase transduction via signals from tyrosine kinase. Noonan syndrome and acute myeloid leukemia can be caused from mutations in PTPN11.

Staphylokinase (SAK) is a 136-amino acidenzymefrom Staphylococcus aureus. It is positively regulated by the "agr" gene regulator. It activates plasminogen, which in turn can degrade various host proteins during infection.

Casein Kinase 2 beta (CSNK2B) is a ubiquitous Ser/Thr kinase expressed in all eukaryotes. CSNK2Bis atetramer comprised of 2 catalytic kinase domains, alpha subunits and 2 identical regulatory beta subunits.CSNK2Btakes part incell cycle control, DNA repair,regulation of the circadian rhythm and other cellularprocesses. The beta subunit itself confers stability to the CK2 alpha subunitand is involved in activity and substrate specificity but does not have kinase activity.

Ephrin A5 (EFNA5) is a part of the ephrin ligand family which binds the members of ephrin receptor subfamily of tyrosine kinases and stimulates contact-dependent bidirectional signaling into neighboring cells. EFNA5 is mainly expressed in human adult brain, heart, spleen, and ovary and human fetal brain, lung, and kidney.

AURKA (Aurora Kinase A) belongs to the mitotic serine/threonine kinases family. AURKA is a cell cycle-regulated kinase which may be involved in microtubule formation and/or stabilization at the spindle pole during chromosome segregation. AURKA is found at the centrosome in interphase cells and at the spindle poles in mitosis. Since the AURKA expression is cell-cycle regulated, it is low in G1/S, it accumulates during G2/M, and it decreases rapidly after. AURKA is involved in important processes during mitosis and meiosis whose proper function is essential for healthy cell proliferation. In addition, AURKA plays an essential role in tumourigenesis and is overexpressed in various types of cancers. AURKA is strongly expressed in the testis, colon, ovarian, prostate, neuroblastoma, breast and cervical cancer cell lines and weakly in skeletal muscle, thymus and spleen. AURKA interacts with its substrates BORA and ARHGEF2, as well as with TACC1 and CPEB1.
Defects in the AURKA gene cause numerical centrosome aberrations including aneuploidy. AURKA overexpression has been linked to chromosomal instability in colorectal cancer. AURKA expression may have a prognostic significance in ovarian carcinoma.

Tyrosylprotein Sulfotransferase 1, also known as TPST1 is the enzyme which catalyzes the sulfation reaction of protein tyrosines, a post-translational modification of proteins. TPST1 belongs to the protein sulfotransferase family. In addition, TPST1 utilizes 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) as the sulfonate donor and also binds proteins with target tyrosineresidues to eventually form the tyrosine O-sulfate ester group in addition to the desulfonated 3’-phosphoadenosine-5’-phosphate.

PGK1 is an X-linked enzyme that has a major role in the glycolytic pathway. PGK1 is a glycolytic enzyme which catalyzes the conversion of 1,3-diphosphoglycerate to 3-phosphoglycerate, generating an ATP molecule. PGK1 may also act as a cofactor for polymerase alpha. Defects in the PGK1 gene are usually associated with chronic hemolytic anemia, though it can be accompanied by either mental retardation or muscular disease (rhabdomyolysis). Overexpression of PGK1 and its signalling targets are possibly an expression-pathway in diffuse primary gastric carcinomas promoting peritoneal dissemination. It was shown that PGK1 is differentially expressed in the dorsolateral prefrontal cortex from patients with schizophrenia.

Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVE supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

ETNK2 belongs to theethanolaminekinase family which catalyzes the 1st step of PtdEtn biosynthesis via the cytidine diphosphate.

Mitogen-activated protein kinase 1 (MAPK1) is also known as "extracellular signal-regulated kinase 2" (ERK2). Two similar (85% sequence identity) protein kinases were originally called ERK1 and ERK2. They were found during a search for protein kinases that are rapidly phosphorylated after activation of cell surface tyrosine kinases such as the epidermal growth factor receptor. Phosphorylation of ERKs leads to the activation of their kinase activity.The molecular events linking cell surface receptors to activation of ERKs are complex. It was found that Ras GTP-binding proteins are involved in the activation of ERKs. Another protein kinase, Raf-1, was shown to phosphorylate a "MAPK kinase", thus qualifying as a "MAPK kinase kinase". The MAPK kinase was named "MAPK/ERK kinase" (MEK). Receptor-linked tyrosine kinases, Ras, Raf, MEK and MAPK could be fitted into a signaling cascade linking an extracellular signal to MAPK activation Transgenic gene knockout mice lacking MAPK1 have major defe

Cyclin-dependent kinase inhibitor 3 (CDKN3) is a member of the dual specificity protein phosphatase family. CDKN3 was identified as a cyclin-dependent kinase inhibitor, and was shown to interact with, and dephosphorylate CDK2 kinase, consequently prevent the activation of CDK2 kinase. In addition CDKN3 is important in cell cycle regulation. The CDKN3 gene was reported to be deleted, mutated, or overexpressed in several kinds of cancers.

JUN N-terminal Kinase 2is a member of the MAP kinase family. MAP kinases act as an integration point for multiple biochemical signals, and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation and development. This kinase targets specific transcription factors, and thus mediates immediate-early gene expression in response to various cell stimuli. It is most closely related to MAPK8, both of which are involved in UV radiation induced apoptosis, thought to be related to the cytochrome c-mediated cell death pathway. This gene and MAPK8 are also known as c-Jun N-terminal kinases. This kinase blocks the ubiquitination of tumor suppressor p53, and thus it increases the stability of p53 in nonstressed cells. Studies of this gene's mouse counterpart suggest a key role in T-cell differentiation. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.

Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVE supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Creatine Kinase MM is a cytoplasmic enzyme involved in energy homeostasis and is an important serum marker for myocardial infarction. The encoded protein reversibly catalyzes the transfer of phosphate between ATP and various phosphogens such as creatine phosphate. It acts as a homodimer in striated muscle as well as in other tissues, and as a heterodimer with a similar brain isozyme in heart. The encoded protein is a member of the ATP:guanido phosphotransferase protein family.

Caseine Kinase 1 alpha belongs is a member of the protein kinase superfamily, CK1 Ser/Thr protein kinase family, Casein kinase I subfamily. The CK1 isoforms - alpha, beta, gamma, delta, epsilon and their splice variants are involved in diverse cellular processes including membrane trafficking, circadian rhythm, cell cycle progression, chromosome segregation, apoptosis and cellular differentiation. Possibly CSNK1A1 can phosphorylate a large number of proteins and is involved in Wnt signaling where it phosphorylates CTNNB1 on Ser45. CSNK1A1 also interacts with the Axin complex.

The Casein kinase 2 (EC2.7.11.1) is a serine/threonine-selective protein kinasethat is a tetramer of two alpha subunits and two beta subunits. The alpha subunits have the catalytic kinase domain. Casein kinase 2 has been implicated in cell cyclecontrol, DNA repair, regulation of the circadian rhythmand other cellular processes.
Casein kinase 2 activity has been reported to be activated following Wnt signaling pathwayactivation. A Pertussis toxin-sensitive G proteinand Disheveled appear to be an intermediary between Wnt-mediated activation of the Frizzled receptor and activation of casein kinase 2.

Calcium/Calmodulin-Dependent Protein Kinase II Inhibitor 2 (CAMK2N2) is a protein coding gene which regulates cell growth when overexpressed in colon adenocarcinoma LoVo cells. CAMK2N2 plays a role as a cellular inhibitor of CaM-kinase II (CAMK2).

Adenylate kinase isoenzyme 5 (AK5) belongs to the adenylate kinase family, which is involved in regulating the adenine nucleotide composition within a cell by catalyzing the reversible transfer of phosphate groups among adenine nucleotides. AK5 is related to the UMP/CMP kinase of several species. AK5 is located in the cytosol and expressed exclusively in the brain.

HGF, also known as scatter factor (SF) and Hepatocyte growth factor, is secreted from mesenchymal cells, targets and acts mainly on epithelial and endothelial cells. The protein is a paracrine cellular growth, motility and morphogenic factor. HGF can also be part of haemopoietic progenitor cells and T cells. HGF has a crucial role in embryonic organ development, mainly in myogenesis. In adults HGF takes part in organ regeneration and wound healing.