PCM-1 is required for centrosome assembly and function. This protein is essential for the correct localization of several centrosomal proteins including CEP250, CETN3, PCNT and NEK2. The protein is required to anchor microtubules to the

DPT is an extracellular matrix protein with possible functions in cell-matrix interactions and matrix assembly. This protein is found in various tissues and many of its tyrosine residues are sulphated. The protein is postulated to

ERK1, a member of the MAP kinase subfamily of Ser/Thr protein kinases, is involved in both the initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription

CYP3A5 is a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This protein

Protein kinases are enzymes that transfer a phosphate group from a phosphate donor, generally the g phosphate of ATP, onto an acceptor amino acid in a substrate protein. By this basic mechanism, protein kinases mediate

PTK2 is a cytoplasmic protein tyrosine kinase which is found concentrated in the focal adhesions that form between cells growing in the presence of extracellular matrix constituents. This protein is a member of the FAK

Cyclin-dependent kinase 14, a member of the CDC2/CDKX subfamily of Ser/Thr protein kinases, may play a role in meiosis as well as in neuron differentiation and/or function It is highly expressed in brain, pancreas, kidney,

HSPCB are highly conserved molecular chaperones that have key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. This protein normally associate with other cochaperones and play important roles in folding newly synthesized

Protein kinases are enzymes that transfer a phosphate group from a phosphate donor, generally the g phosphate of ATP, onto an acceptor amino acid in a substrate protein. By this basic mechanism, protein kinases mediate

The degradation of L-threonine to glycine consists of a two-step biochemical pathway involving the enzymes L-threonine dehydrogenase and 2-amino-3-ketobutyrate coenzyme A ligase. L-Threonine is first converted into 2-amino-3-ketobutyrate by L-threonine dehydrogenase. GCAT is the second

Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active

FKBP1B is a member of the immunophilin protein family, which play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. This protein is a cis-trans prolyl isomerase that binds the immunosuppressants