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Phosphorylation is a key post translational modification (PTM) of proteins and lipids. Protein kinases are responsible for PTMs and this type of modification represents one of the most efficient ways to regulate protein and lipid function in cells.

Protein Kinases are one of the largest classes of enzymes (there are 516 family members and they constitute ~2% of all human genes) that catalyse the transfer of the γ-phosphate from ATP to acceptor hydroxyl groups on amino acids (such as serine, threonine and tyrosine) in proteins or glycosyl moieties in lipids.

Protein kinases are found in almost all living organisms and in humans approimately 30% of all proteins are subject to phosphorylation. Phosphorylation can lead to functional modifications to substrate or target proteins and this can cause changes to enzyme activity, cellular localization or association with other proteins.

Defective signalling by protein kinases accounts for more than 400 human diseases and these targets are being actively pursued for therapeutic intervention. Targeting protein kinases by small molecule inhibitors or neutralizing antibodies has been extremely beneficial in the treatment of various human diseases such as cancer and more than 10 drugs targeting protein kinases have been approved while another 60 candidates are in clinical trials.

All Active Kinases
All Active Kinase Mutants
Unactive Kinases
Protein Kinases
Fructose Kinases
Lipid Kinases
Ser/Thr Kinases
Receptor Tyrosine Kinases
Cytoplasmic Tyrosine Kinases
Biochemical Compounds
Kinase Activators
Kinase Inhibitors
Signaling Reagents
Assay Reagents
Oligo Substrates
Peptide Substrates
Protein Substrates
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