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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.

Akt1, also known as "Akt" or protein kinaseB (PKB) is an important molecule in mammaliancellular signaling.
In humans, there are three genes in the "Akt family": Akt1, Akt2, and Akt3. These enzymesare members of the serine/threonine-specific protein kinasefamily (EC2.7.11.1).
Akt1 is involved in cellular survival pathways, by inhibiting apoptoticprocesses. Akt1 is also able to induce protein synthesispathways, and is therefore a key signaling protein in the cellular pathways that 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 major factor in many types of cancer. Akt (now also called Akt1) was originally identified as the oncogenein the transforming retrovirus, AKT8.

Tachykinin-1 (TAC1) belongs to the tachykinin peptide hormone family. TAC1 are a family of peptides which have similar biologic activities and share a common C-terminal sequence, phe-X-gly-leu-met-NH2, however they have distinct N-terminal sequences that convey receptor specificities. TAC1 is assumed to act as neurotransmitters which interact with nerve receptors and smooth muscle cells. TAC1 induces behavioral responses and serves as vasodilators and secretagogues.

Glucokinase or GLK, is a protein, part of the bacterial glucokinase superfamily. In the bacteria E. coli, glucose can be transported to the inner cell through a system called PTS as glucose 6-phosphate, therefore, GLK is less crucial to the bacteria.

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.
Mice that lack casein kinase 2 alpha prime have a defect in the morphology of developing sperm.

FANK1 was localized in the nuclei of identical cells in the seminiferous epithelium. Depending on its nuclear localization, a gene ontology analysis proposes that FANK1 has a DNA binding activity therefor operates as a transcription factor. The extremely controlled expression of FANK1, suggests that it takes part in regulating gene expression in the transition from the meiotic phase to the haploid phase throughout spermatogenesis.

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).

Adenosine Kinase is an abundant enzyme in mammalian tissues which catalyzes the transfer of the gamma-phosphate from ATP to adenosine, thus is as a regulator of concentrations of both extracellular adenosine and intracellular adenine nucleotides. Adenosine has extensive effects on the cardiovascular, nervous, respiratory, and immune systems and inhibitors of the enzyme take a crucial pharmacological part in growing intravascular adenosine concentrations and acting as anti-inflammatory agents.

Hexokinases phosphorylate glucose to produce glucose-6-phosphate, thus committing glucose to the glycolytic pathway. Hexokinase1 encodes a ubiquitous form of hexokinase which localizes to the outer membrane of mitochondria. Mutations in this gene have been associated with hemolytic anemia due to hexokinase deficiency. Alternative splicing of HXK1 results in five transcript variants which encode different isoforms, some of which are tissue-specific. Each isoform has a distinct N-terminus; the remainder of the protein is identical among all the isoforms. A sixth transcript variant has been described, but due to the presence of several stop codons, it is not thought to encode a protein.

NEK7, protein kinase, has a vital role in mitotic cell cycle progression. It is essential for microtubule nucleation activity of the centrosome, robust mitotic spindle formation and cytokinesis. NEK7 is greatly expressed in lung, muscle, testis, brain, heart, liver, leukocyte and spleen.

PKLR is a pyruvate kinase which catalyzes the transphosphorylation of phohsphoenolpyruvate into pyruvate and ATP. That is the rate-limiting step of glycolysis. PKLR gene encodes the L- and R-type isoenzymes through alternate splicing events controlled by different promoters. L-type isoform can also appear as a tetramer and is upregulated by glucose with implications in maturity-onset diabetes of the young.

Akt1, also known as "Akt" or protein kinaseB (PKB) is an important molecule in mammaliancellular signaling.
In humans, there are three genes in the "Akt family": Akt1, Akt2, and Akt3. These enzymesare members of the serine/threonine-specific protein kinasefamily (EC2.7.11.1).
Akt1 is involved in cellular survival pathways, by inhibiting apoptoticprocesses. Akt1 is also able to induce protein synthesispathways, and is therefore a key signaling protein in the cellular pathways that 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 major factor in many types of cancer. Akt (now also called Akt1) was originally identified as the oncogenein the transforming retrovirus, AKT8.

GCK is an enzyme that expedite the formation of glucose-6-phosphate for glucose by phosphorylation. Humans and other vertebrates have GCK in the cells of the pancreas and liver. In both organs, the enzyme has an important role in carbohydrate metabolism regulation by sensing sugar levels and acting according to the change in glucose levels, that can rise after a meal or fall during fasting. Mutations in the gene that codes for this enzyme can cause hypoglycemia or diabetes.

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The Proteinase K enzyme is a member of the Peptidase family S8. Proteinase K is a broad-spectrum serine protease. Proteinase K is capable of digesting hair (keratin), henceforth, the name "Proteinase K". Proteinase K is activated by calcium, the enzyme digests proteins especially after hydrophobic amino acids (aliphatic, aromatic and other hydrophobic amino acids). Proteinase K is frequently utilized in molecular biology to digest protein and remove contamination from preparations of nucleic acid. Addition of Proteinase K to nucleic acid preparations rapidly inactivates nucleases which may otherwise degrade the DNA or RNA during purification. Proteinase K is greatly fitting to this application as the enzyme is active in the presence of chemicals which denature proteins, such as SDS and urea, chelating agents such as EDTA, sulfhydryl reagents, as well as trypsin or chymotrypsin inhibitors. Proteinase K is utilized for the destruction of proteins in cell lysates (tissue, cell culture cells) and for the release of nucleic acids, given that it quite effectively inactivates DNases and RNases.

Hydroxylysine Kinase, also known as HYKK, is a Protein Coding gene. HYKK which is a part of the aminoglycoside phosphotransferase family catalyzes the GTPdependent phosphorylation of 5-hydroxy-L-lysine.

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.

cAMP-dependent protein kinase inhibitor beta (PKIB) belongs to the cAMP-dependent protein kinase inhibitor family. PKIB may interact with the catalytic subunit of cAMP-dependent protein kinase and function as a competitive inhibitor.

GALK1 enzyme is needed in the first step of the galactose metabolism pathway.
(ATP + D-galactose = ADP + alpha-D-galactose 1-phosphate). GALK1 deficinecy lead galactosemia II which is an autosomal recessive deficiency known by congenital cataracts during infancy and presenile cataracts in the adult population. The cataracts are secondary to accumulation of galactitol in the lenses.

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.

MAPK10 is part of the MAP kinase protein family. MAP Kinases perform as assimilation point for many biochemical pathways. The enzyme also takes part in wide range of cellular pathways: differentiation, proliferation, development and transcription regulation.

Serine/threonine kinase 17b (STK17B) is a member of the protein kinase superfamily. STK17B functions as a positive regulator of apoptosis. STK17B interacts with CHP1; this interaction stimulates CHP1 to translocate from the Golgi to the nucleus. STK17B is highly expressed in the placenta, lung, pancreas, however it has lower levels in the heart, brain, liver, skeletal muscle and kidney.

CK-MB Type II possesses the naturally occurring carboxy-terminal amino acid lysine.
This occurs during a myocardial infarct (MI or heart attack) when CK-MB Type II is released from damaged heart muscle, and the C-terminal lysine is cleaved in the blood stream, thus creating CK-MB Type I. This difference can be exploited in diagnosis of an MI.

PMSG Hormone is a well know used hormone together with progestogen to increase ovulation just before to artificial insemination. PMSG hormone is a placental glycoprotein produced from the serum of pregnant mares. PMSG comprises of an alfa subunit and a beta subunit. PMSG hormone is secreted from endometrial cups within the pregnant mare uterus aging from 40 to 130 days into their maturation, and once extracted, it can been used to promote artificially estrus in female animals. These assemblies produce PMSG hormone to induce mare's ovarian and repsouctive structures. PMSG can induce the growth of follicles by ovaries and results in ovulatation. PMSG hormone has an about a 4 day half-life of bioactivity in species other than horses. The extended biological activity can cause ovarian stimulation and ovulation. However, PMSG use alone often causes cystic ovarian disease because of the unrestrained ovarian stimulation and due to the sugar molecules which decrease clearance of the hormone. PMSG is more likely to be used than other pituitary hormones due to the extended circulatory half-life. PMSG solely exhibits luteinizing hormone like activity, however in other animal classes it has FSH & LH like activity.

MVK is a member of the GHMP kinase family. Mevalonate is a vital mediator, and MVK an important early enzyme, in isoprenoid and sterol synthesis. MVK deficiency can result in gene mutation associated with Mevalonic aciduria, an illness which causes psychomotor retardation, failure to thrive hepatosplenomegaly, anemia and frequent febrile crises. Mutations in this gene also cause hyperimmunoglobulinaemia D and sporadic fever syndrome, in which the person suffers from recurrent episodes of fever related with lymphadenopathy, skin rash, gastrointestinal dismay and arthralgia.