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Thymidine Kinase 1 (TK1) is a phosphotransferase (a kinase): 2'-deoxythymidine kinase, ATP-thymidine 5'-phosphotransferase. TK1 is present in 2 forms in mammalian cells, TK1 and TK2. Thymidine kinases hold a main function in the synthesis of DNA and thus in cell division, as they are part of the distinctive reaction chain to introduce deoxythymidine (present in the body fluids as a result of degradation of DNA from food and from dead cells) into the DNA. Thymidine kinase is necessary for the action of many antiviral drugs. Thymidine kinase is used to select hybridoma cell lines in production of monoclonal antibodies.

Mitogen-activated protein kinase 9 (MAPK9) belongs to the MAP kinase family. MAP kinases function as an integration point for numerous biochemical signals, and are involved in a broad variety of cellular processes such as proliferation, differentiation, transcription regulation and development. MAPK9 targets specific transcription factors, and consequently mediates immediate-early gene expression in response to diverse cell stimuli. As an active dimer, MAPK9 can translocate to the nucleus and control transcription through its effects on c-Jun, ATF-2, and other transcription factors. MAPK9 blocks the ubiquitination of tumor suppressor p53, and so it increases the stability of p53 in nonstressed cells.

Flavokinase is a transferases family member, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. Flavokinase is an enzyme that catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin-mononucleotide (FMN), which is an obligatory step in vitamin B2 utilization and flavin cofactor synthesis. It has been proposed that TNF, through the activation of the RFK gene, enhances the incorporation of FAD in NADPH oxidase enzymes, which is a critical step for the assembly and activation of NADPH oxidase.

KIT, also known as KIT Proto-Oncogene Receptor Tyrosine, is a cytokine receptor which is expressed not only in hematopoietic stem cells but likewise in other cell types. KIT binds to receptor tyrosine kinase type III, which is a stem cell factor, also named a "rigid factor" or "c-kit ligand". Once this receptor binds to stem cell factor (SCF), it forms a dimer which activates intrinsic tyrosine kinase activity, which sequentially phosphorylates & activates signaling molecules which breed signals in cells. This receptor protects vascular smooth muscle cells from apoptosis in addition to restoring cardiac function after myocardial infarction.

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.

Akt1, also known as Akt or else protein kinase B (PKB) is an important molecule in mammaliancellular signaling. In humans, there are three genes in the "Akt family": Akt1, Akt2, and Akt3. Moreover, these enzymes are members of the serine/threonine-specific protein kinase family (EC2.7.11.1). Akt1 is involved in cellular survival pathways, by inhibiting apoptoticprocesses. Akt1 is also able to induce protein synthesis pathways, and is therefore a key signaling protein in the cellular pathways which lead to skeletal muscle hypertrophy, and general tissue growth. Since it can block apoptosis, and thereby promote cell survival, Akt1 has been implicated as a most important factor in numerous types of cancer. Akt (now also called Akt1) was at first identified as the oncogenein the transforming retrovirus, AKT8.

Testis-specific serine/threonine-protein kinase 6 (TSSK6) is an intronless gene, which belongs to the CAMK Ser/Thr protein kinase family. The TSSK6 protein contains one protein kinase domain. TSSK6 is highly expressed in the testis and lowly expressed in the colon, prostate, thymus, small intestine, and peripheral blood leukocytes. TSSK6 interacts with the heatshock proteins HSPA8, HSPCB, and HAPA1A; these interactions seem to be essential for TSSK6 kinase activity. TSSK6 plays a role in DNA condensation during postmeiotic chromatin remodeling. In addition, TSSK6 is required for sperm production and function.

Phosphoglycerate kinase 1, also referred to PGK1, is an X-linked enzyme whichfunctions in the glycolytic pathway.The gene encoding the erythrocyte enzyme PGK1 & it seems that PGK-1 plays a role as a polymerase alpha cofactor protein (primer recognition protein) as a glyxolytic enzyme role. The PGK1 catalyzes the reversible conversion of 1, 3-diphosphoglycerate to 3-phosphoglycerate during glycolysis, generating one molecule of ATP.

Proto-oncogene tyrosine-protein kinase MER is a protein, this enzyme is coded from the MERTK gene. This gene is a part of the TYRO3/AXL/MER receptor kinase group and encodes a transmembrane protein with two fibronectin type-III domains, two Ig-like C2-type (immunoglobulin-like) sites, and one tyrosine kinase site. Mutations in this gene have been correlated with interruption of the retinal pigment epithelium phagocytosis process and commencement of autosomal recessive retinitis pigmentosa.

PFKM is a regulatory glycolytic enzyme that converts fructose 6-phosphate and ATP into fructose 1,6-bisphosphate (through PFK-1), fructose 2,6-bisphosphate (through PFK-2) and ADP. Three phosphofructokinase isozymes exist in humans: muscle, liver and platelet. Mutations in PFKM gene have been related with glycogen storage disease type VII, also identified as Tarui disease.

The MAP2K1 protein is encoded by the MAP2K1 gene. This enzyme serves as a MAP (mitogen activated protein) kinase, it is a part of the dual specificity protein kinase family. Extracellular signal-regulated kinases such as MAP kinases has an important role in assimilation of various biochemical signals. MAP2K1 is located upstream to the MAP kinases and activates them by multiple intra and extracellular signals. The enzyme serves as a key factor in the signal transduction pathway of MAP kinase, therefore it takes part in the cell development (transcription regulation, proliferation, differentiation etc.).

Dual specificity mitogen-activated protein kinase kinase 3 (MAP2K3) is a dual specificity protein kinase which is a member of the MAP kinase kinase family. MAP2K3 is activated by mitogenic and environmental stress, and participates in the MAP kinase-mediated signaling cascade. MAP2K3 phosphorylates and consequently activates MAPK14/p38-MAPK.

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).

MAPK3 is a part of the MAP kinase family which is recognized as extracellular signal-regulated kinases (ERKs), that function in a signaling cascade that controls various cellular procedures such as proliferation, differentiation, and cell cycle progression in reaction to a variety of extracellular signals. MAPK3 is activated by upstream kinases, resulting in its translocation to the nucleus where it phosphorylates nuclear targets.

Mitogen-Activated Protein Kinase 6 (MAP2K6) is a part of the dual specificity protein kinase family. MAP2K6 phosphorylates and activates p38 MAP kinase in response to inflammatory cytokines or environmental stress. MAP2K6 is a vital component of the MAP kinase signal transduction pathway. MAP2K6 takes part in various cellular processes such as stress induced cell cycle arrest and apoptosis.

MAPK12 is a member of the MAP kinase family. MAPK12 acts as a signal transducer during differentiation of myoblasts to myotubes. p38 proteins utilizes magnesium as a cofactor to catalyze the ATP-dependent phosphorylation of target proteins and is produced in several regions all over the body with common expression patterns in heart.

Creatine Kinase BB is a cytoplasmic enzyme involved in energy homeostasis. The encoded protein reversibly catalyzes the transfer of phosphate between ATP and various phosphogens such as creatine phosphate. It acts as a homodimer in brain as well as in other tissues, and as a heterodimer with a similar muscle isozyme in heart. The encoded protein is a member of the ATP:guanido phosphotransferase protein family. A pseudogene of this gene has been characterized.

Calcium/Calmodulin Dependent Protein Kinase II Inhibitor 1 (CAMK2N1), which interacts with CAMK2B, is a part of the CAMK2N family. CAMK2N1 is also interacts with CAMK2A in a way which requires CAMK2A activation by Ca2+. CAMK2N1 is potent and specific inhibitor of CaM-kinase II (CAMK2).

Calcium/Calmodulin Dependent Protein Kinase II Inhibitor 1 (CAMK2N1), which interacts with CAMK2B, is a part of the CAMK2N family. CAMK2N1 is also interacts with CAMK2A in a way which requires CAMK2A activation by Ca2+. CAMK2N1 is potent and specific inhibitor of CaM-kinase II (CAMK2).

Thiamin pyrophosphokinase 1 (TPK1) is a homodimer which catalyzes the phosphorylation of thiamine to thiamine pyrophosphate. TPK1 is found in the heart, kidney, testis, small intestine and peripheral blood leukocytes, and at very low levels in a variety of tissues. TPK1 gene defects cause the thiamine metabolism dysfunction syndrome type 5, episodic encephalopathy type (THMD5), which is an autosomal recessive metabolic disorder due to an inborn error of thiamine metabolism.

CDKN1A holds a key part in the cellular response to DNA mutation. CDKN1A overexpression causes cell cycle to stop. When collaborating with CDK2 complexes, CDKN1A aids to prevent kinase activity and inhibits progression through G1/S. Nevertheless, CDKN1A can additionally increase assembly and activity in complexes of CDK4 or CDK6 and cyclin D. CDKN1A is a vital intermediary by which p53/TP53 facilitates its part as an inhibitor of cellular proliferation as a reaction to DNA impairment.

DCK (Deoxycytidine kinase) is a key enzyme in the salvage of deoxyribonucleosides and in the activation of clinically relevant nucleoside analogues. DCK is responsible for the 5`-phosphorylation of purine and pyrimidine deoxynucleosides to the corresponding monophosphates using ATP or UTP as phosphate donors. Deficiency of the DCK enzyme activity is linked to resistance to antiviral and anticancer chemotherapeutic agents, whereas increased DCK enzyme activity is linked to increased activation of these compounds to cytotoxic nucleoside triphosphate derivatives.

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.

Cyclin-dependent kinase inhibitors (CDKIs) are proteins that bind to and inhibit the activity of CDKs. Two major classes of CDK inhibitors have been identified. The p16 family (p15, p16, p18 and p19) binds to and inhibits the activities of CDK4 and CDK6. The p21 family (p21, p27, p28 and p57) can bind to broad range of CDK-cyclin complexes and inhibit their activities. CDKIs are capable of suppressing growth, and several lines of evidence strongly suggest that at least some CDKIs may be tumor suppressor proteins.