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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.

STK17A belongs to the DAP kinase-associated apoptosis-inducing protein kinase family and encodes an autophosphorylated nuclear protein with a protein kinase domain. STK17A acts as a positive regulator of apoptosis. STK17A is greatly expressed in the placenta with lower levels in the heart, lung, skeletal muscle, kidney and pancreas.

Protein Kinase, AMP-Activated, Alpha 1 (PRKAA1) is a protein coding gene which is the catalytic subunit of AMPK. AMPK is an energy sensor protein kinase which regulates cellular energy metabolism. AMPK adjusts the activity of various important metabolic enzymes by direct phosphorylation. Among its other features, AMPK protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways.

AK4 belongs to the adenylate kinase family of enzymes. AK4 protein is restricted to the mitochondrial matrix. Adenylate kinases regulate the adenine and guanine nucleotide structures in a cell by catalyzing the reversible transfer of phosphate group among these nucleotides. Hereditary mutations which cause AK4 deficiencies in erythrocytes have been associated to hemolytic anemia.

Cell division protein kinase 5 (CDK5) belongs to the cyclin-dependent kinase family. CDK5 is essential for appropriate development of the brain and in order to be activated CDK5 must link to CDK5R1 or CDK5R2. CDK5 doesn't need phosphorylation on the T loop so that binding with the activator is enough to activate the kinase. CDK5 is engaged in the processes of neuronal maturation and migration, phosphorylating the central intracellular adaptor of the reeling signaling chain.

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.

Fructosamine 3 Kinase (FN3K) catalyzes the phosphorylation of fructosamines which may result in deglycation, the non-enzymatic reaction of glucose with primary amines followed by Amadori re-arrangement. Phosphorylation of fructosamines instigates metabolism of the modified amine and brings about the de-glycation of fructoselysine and of glycated proteins. A high concentration of glucose may affect non-enzymatic oxidation of proteins by reaction of glucose and lysine residues (glycation). Fructosamines, the proteins altered in this way, are less active or functional.

CKS2 protein binds to the catalytic subunit of the cyclin dependent kinases and is necessary for their biological function. The CKS2 mRNA is expressed in various patterns through the cell cycle in HeLa cells, which shows spcific role for the encoded protein. CKS2 (CDC28) Protein kinase 2 binds to the catalytic subunit of cyclin-dependent kinases and has thus in involved in cell cycle regulation. CKS2 is required for the first metaphase/anaphase transition during the meiosis. An increase in expression of CKS2 protects the cells from apoptosis. CKS2 is essential during early embryogenesis and cell cycle progression in somatic cells.

MAP2K1 is a member of the dual specificity protein kinase family, which plays a role as a mitogen-activated protein (MAP) kinase kinase. MAP kinases, are recognized as extracellular signal-regulated kinases (ERKs), that act as an integration position for multiple biochemical signals. MEK1 is located upstream of MAP kinases and stimulates the enzymatic activity of MAP kinases upon wide variety of extra- and intracellular signals. As a key player of MAP kinase signal transduction pathway, MEK1 is involved in many cellular processes such as proliferation, differentiation, transcription regulation and development. MAP2K1 catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in a thr-glu-tyr sequence located in map kinases. MEK1 activates erk1 and erk2 map kinases.

AK1 is a small ubiquitous enzyme which is essential for maintenance and cell growth. It is involved in the regulation of adenine nucleotide composition within a cell by catalyzing the reversible transfer of the terminal phosphate group between ATP and AMP. The AK1 protein is found in the cytosol of skeletal muscle, brain and erythrocytes. Defects in the AK1 gene are the cause of a form of hemolytic anemia.

Serum-and glucocorticoid-regulated kinase (SGK1) is a serine/threonine protein kinase and a member of the “AGC” subfamily, which includes protein kinases A, G, and C. The SGK1 protein has an imperative role in activating specific potassium, sodium and chloride channels, suggesting a participation in the regulation of processes such as cell survival, neuronal excitability, and renal sodium excretion. SGK1 is activated in vitro by PDK-1 (3-phosphoinositide-dependent protein kinase-1) and in vivo in reaction to signals which activate phosphatidylinositol (PI) 3-kinase.

SKP1 is a F-box enzyme which functions as a substrate recognition component of the SCF ubiquitin ligase complex which controls the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. SKP1 binds to proteins containing an F-box motif, such as cyclin F, S-phase kinase-associated protein 2, and other regulatory proteins involved in ubiquitin dependent proteolysis. SKP1 takes part in the control of beta-catenin levels and the activity of beta-catenin dependent TCF transcription factors. SKP1 serves as an adapter that links the F-box protein to CUL1 in the SCF complex.

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.

Protein Kinase IFN Double Stranded RNA Activator, also known as PRKRA, mediates the effects of interferon when a viral infection takes place. PRKRA activates EIF2AK2/PKR in the absence of double-stranded RNA (dsRNA) and leads to phosphorylation of EIF2S1/EFI2-alpha and inhibition of translation and induction of apoptosis. Mutations in PRKRA are associated with dystonia.

PDK1 takes part in the regulation of enzymatic activity of mammalian pyruvate dehydrogenase which is part of a mitochondrial multienzyme complex to catalyze the oxidative decarboxylation of pyruvate and is one of the major enzymes responsible for the regulation of homeostasis of carbohydrate fuels in mammals. PDK1 inhibits glioblastoma growth. PDK1 inhibits the mitochondrial pyruvate dehydrogenase complex by phosphorylation of the e1 alpha subunit, therefore contributing to the regulation of glucose metabolism. PDK1 kinase activity is negatively regulated by binding to 14-3-3.

GUK1 is part of the guanylate kinase family. GUK1 occurs as a monomer that catalyzes the ATP-dependent conversion of GMP to GDP, thus takes an important part in the recycling of GMP. Through its catalytic activity, GUK1 functions in regulation of the supply of guanine nucleotides to signal transduction pathways. GUK1 overexpression is related with pituitary adenocarcinomas, implicating that GUK1 is has a role in tumorigenesis.

MAPK14 belongs to the MAP kinase family and is most associated with p38 MAP kinases(MAPKs). MAPKs are activated mainly as a reaction to cellular stress and inflammatory cytokines, and inhibitors that target the MAPK14 and MAPK11 have demonstrated ability to cure inflammatory disease. The substrates of this kinase contain transcription regulator ATF2, MEF2C, and MAX, cell cycle regulator CDC25B, and tumor suppressor p53, which demonstrate the parts of MAPK14 in stress-related transcription, cell cycle regulation and genotoxic stress response.

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.

5'-AMP-activated protein kinase subunit beta-1 (PRKAB1) hinders protein, carbohydrate and lipid biosynthesis, in addition to cell growth and proliferation. AMPK is a heterotrimer comprised of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK acts via direct phosphorylation of metabolic enzymes, and longer-term effects by phosphorylation of transcription regulators. PRKAB1 is a regulator of cellular polarity by remodeling the actin cytoskeleton; most likely by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex compiles, through its C-terminus that joins alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3).

PGK2 is a testis-specific form of phosphoglycerate kinase. Originally presumed to be a pseudogene, the PGK2 protein is actually a functional phosphoglycerate kinase which catalyzes the reversible conversion of 1,3-bisphosphoglycerate to 3-phosphoglycerate, during the Embden-Meyerhof-Parnas pathway of glycolysis, in the later stages of spermatogenesis. The PGK2 gene is intronless, results from retrotransposition of the phosphoglycerate kinase 1 gene, and is expressed specifically in the testis.

Cyclin-dependent kinase inhibitor 1B (CDKN1B) is a member of the Cip/Kip family of cyclin dependent kinase (Cdk) inhibitor proteins. The CDKN1B protein binds to and prevents the activation of cyclin E-CDK2 or cyclin D-CDK4 complexes, and so controls the cell cycle progression at G1. CDKN1B is often referred to as a cell cycle inhibitor protein since its major function is to stop or slow down the cell division cycle. The degradation of the CDKN1B protein, which is triggered by its CDK dependent phosphorylation and ensuing ubiquitination by SCF complexes, is compulsory for the cellular transition from inactive to the proliferative state.

B lymphoid kinase (BLK) is a 55kDa tyrosine kinase with SH3, SH2, and catalytic domains which contain consensus sequences of the Src protein tyrosine kinase family. BLK is a nonreceptor tyrosine-kinase belonging to the src family of proto-oncogenes which are typically involved in cell proliferation and differentiation. The BLK protein is expressed specifically in the B cell lineage and has a role in the signal-transduction pathway which is restricted to B lymphoid cells. In addition, BLK stimulates ins. synthesis and secretion in response to glucose and increases the expression of several pancreatic beta-cell transcription factors.

UCK1 is a uridine-cytidine kinase which catalyzes the phosphorylation of uridine and cytidine to uridine monophosphate and cytidine monophosphate. UCK1 does not phosphorylate deoxyribonucleosides or purine ribonucleosides. UCK1 is also phosphorylates uridine and cytidine analogs and uses ATP and GTP as a phosphate donor.

Thymidylate kinase (DTYMK) is involved in pyrimidine metabolism. Specifically, DTYMK catalyzes the ATP-dependent conversion of dTMP (deoxythymidine monophosphate) to dTDP (deoxythymidine diphosphate), which then acts as one of the 4 nucleotides in DNA. Through its role in the catalytic creation of dTDP, DTYMK has an imperative role in the pathway of DNA synthesis and is assumed to be involved in cell cycle progression and cell growth.