Protein kinase

protein kinasestransmembranekinaseskinasetrans-autophosphorylationPKNprotein-kinase5'-AMP-activated protein kinaseAGC kinase familyautophosphorylation
A protein kinase is a kinase enzyme that modifies other molecules, mostly proteins, by chemically adding phosphate groups to them (phosphorylation).wikipedia
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Signal transduction

signaling pathwayssignaling cascadesignal transduction pathways
Up to 30% of all human proteins may be modified by kinase activity, and kinases are known to regulate the majority of cellular pathways, especially those involved in signal transduction.
Signal transduction is the process by which a chemical or physical signal is transmitted through a cell as a series of molecular events, most commonly protein phosphorylation catalyzed by protein kinases, which ultimately results in a cellular response.

Pseudokinase

Protein kinases are also found in bacteria and plants, and include the pseudokinase sub-family, which exhibit unusual features including atypical nucleotide binding and weak, or no, catalytic activity and are part of a much larger pseudoenzyme group of 'degraded' enzyme relatives that are found throughout life, where they take an active participation in mechanistic cellular signaling.
Pseudokinases are catalytically-deficient pseudoenzyme variants of protein kinases that are represented in all kinomes across the kingdoms of life.

Tyrosine kinase

tyrosine kinasesprotein-tyrosine kinaseprotein tyrosine kinase
Most kinases act on both serine and threonine (serine/threonine kinases), others act on tyrosine (tyrosine kinases), and a number act on all three (dual-specificity kinases).
Tyrosine kinases are a subclass of protein kinase.

Tyrosine

Tyrtyrosine metabolismL-tyrosine
Most kinases act on both serine and threonine (serine/threonine kinases), others act on tyrosine (tyrosine kinases), and a number act on all three (dual-specificity kinases).
It occurs in proteins that are part of signal transduction processes and functions as a receiver of phosphate groups that are transferred by way of protein kinases.

Histidine kinase

Histidine '''K'''inaseprotein histidine kinasehistidine protein kinase
There are also protein kinases that phosphorylate other amino acids, including histidine kinases that phosphorylate histidine residues to create acid and heat-labile phosphoramidate bonds.
Distinct from other classes of protein kinases, HKs are usually parts of a two-component signal transduction mechanisms in which HK transfers a phosphate group from ATP to a histidine residue within the kinase, and then to an aspartate residue on the receiver domain of a response regulator protein (or sometimes on the kinase itself).

Protein kinase C

PKCprotein kinase C (PKC)C
Protein kinase C, commonly abbreviated to PKC (EC 2.7.11.13), is a family of protein kinase enzymes that are involved in controlling the function of other proteins through the phosphorylation of hydroxyl groups of serine and threonine amino acid residues on these proteins, or a member of this family.

Casein kinase 1

CK1casein kinase icasein kinase 1 family
The Casein kinase 1 family of protein kinases are serine/threonine-selective enzymes that function as regulators of signal transduction pathways in most eukaryotic cell types.

Protein kinase A

PKAcAMP-dependent protein kinasecyclic AMP-dependent protein kinase
The catalytic subunit contains the active site, a series of canonical residues found in protein kinases that bind and hydrolyse ATP and a domain to bind the regulatory subunit.

Cyclin-dependent kinase

CDKcyclin-dependent kinasescyclin dependent kinase
Cyclin-dependent kinases (CDKs) are the families of protein kinases first discovered for their role in regulating the cell cycle.

Enzyme inhibitor

inhibitorinhibitioninhibitors
Kinases are turned on or off by phosphorylation (sometimes by the kinase itself - cis-phosphorylation/autophosphorylation), by binding of activator proteins or inhibitor proteins, or small molecules, or by controlling their location in the cell relative to their substrates.
For example, some protein kinase inhibitors have chemical structures that are similar to adenosine triphosphate, one of the substrates of these enzymes.

Mitogen-activated protein kinase

MAPKMAP kinasemitogen-activated protein kinases
One very important group of protein kinases are the MAP kinases (acronym from: "mitogen-activated protein kinases").
A mitogen-activated protein kinase (MAPK or MAP kinase) is a type of protein kinase that is specific to the amino acids serine and threonine (i.e., a serine/threonine-specific protein kinase).

Active site

catalytic domaincatalytic siteactive sites
There are a number of conserved regions in the catalytic domain of protein kinases.
Many enzymes including serine protease, cysteine protease, protein kinase and phosphatase evolved to form transient covalent bonds between them and their substrates to lower the activation energy and allow the reaction to occur.

Cyclic guanosine monophosphate

cGMPcyclic GMP3',5'-cyclic GMP
Activity of these protein kinases can be regulated by specific events (e.g., DNA damage), as well as numerous chemical signals, including cAMP/cGMP, diacylglycerol, and Ca 2+ /calmodulin.
Its most likely mechanism of action is activation of intracellular protein kinases in response to the binding of membrane-impermeable peptide hormones to the external cell surface.

Pseudoenzyme

pseudoenzymeslack the active site residuespseudoenzyme analysis
Protein kinases are also found in bacteria and plants, and include the pseudokinase sub-family, which exhibit unusual features including atypical nucleotide binding and weak, or no, catalytic activity and are part of a much larger pseudoenzyme group of 'degraded' enzyme relatives that are found throughout life, where they take an active participation in mechanistic cellular signaling.
The best studied pseudoenzymes reside amongst various key signalling superfamilies of enzymes, such as the proteases, the protein kinases, protein phosphatases and ubiquitin modifying enzymes.

Phosphatase

phosphatasesprotein phosphatasesalkaline and acid phosphatases
Activity of MAP kinases is restricted by a number of protein phosphatases, which remove the phosphate groups that are added to specific serine or threonine residues of the kinase and are required to maintain the kinase in an active conformation.
Phosphatase enzymes are essential to many biological functions, because phosphorylation (e.g. by protein kinases) and dephosphorylation (by phosphatases) serve diverse roles in cellular regulation and signaling.

Cyclic adenosine monophosphate

cAMPcyclic AMP3',5'-cyclic AMP
Activity of these protein kinases can be regulated by specific events (e.g., DNA damage), as well as numerous chemical signals, including cAMP/cGMP, diacylglycerol, and Ca 2+ /calmodulin.
It is also involved in the activation of protein kinases.

Epidermal growth factor receptor

EGFREGF receptorEGFR inhibitor
As a result, autophosphorylation of several tyrosine (Y) residues in the C-terminal domain of EGFR occurs.

Staurosporine

Staurosporin
The main biological activity of staurosporine is the inhibition of protein kinases through the prevention of ATP binding to the kinase.

Calmodulin

CaMcalcium/calmodulincalcium/calmodulin (Ca2+/CaM)
Activity of these protein kinases can be regulated by specific events (e.g., DNA damage), as well as numerous chemical signals, including cAMP/cGMP, diacylglycerol, and Ca 2+ /calmodulin.

Kinase

kinaseskinase domainprotein kinase C
A protein kinase is a kinase enzyme that modifies other molecules, mostly proteins, by chemically adding phosphate groups to them (phosphorylation).

Enzyme

enzymologyenzymesenzymatic
A protein kinase is a kinase enzyme that modifies other molecules, mostly proteins, by chemically adding phosphate groups to them (phosphorylation).

Phosphate

phosphatesphosphate groupinorganic phosphate
A protein kinase is a kinase enzyme that modifies other molecules, mostly proteins, by chemically adding phosphate groups to them (phosphorylation).

Phosphorylation

phosphorylatedphosphorylatephosphorylates
A protein kinase is a kinase enzyme that modifies other molecules, mostly proteins, by chemically adding phosphate groups to them (phosphorylation).

Substrate (chemistry)

substratessubstratesubstrate specificity
Kinases are turned on or off by phosphorylation (sometimes by the kinase itself - cis-phosphorylation/autophosphorylation), by binding of activator proteins or inhibitor proteins, or small molecules, or by controlling their location in the cell relative to their substrates. Phosphorylation usually results in a functional change of the target protein (substrate) by changing enzyme activity, cellular location, or association with other proteins.

Catalysis

catalyzescatalysescatalyst
Phosphorylation usually results in a functional change of the target protein (substrate) by changing enzyme activity, cellular location, or association with other proteins.