Description

IPR000961 is a AGC-kinase, C-terminal.

<p>The AGC (cAMP-dependent, cGMP-dependent and protein kinase C) protein kinase family embraces a collection of protein kinases that display a high degree of sequence similarity within their respective kinase domains. AGC kinase proteins are characterised by three conserved phosphorylation sites that critically regulate their function. The first one is located in an activation loop in the centre of the kinase domain. The two other phosphorylation sites are located outside the kinase domain in a conserved region on its C-terminal side, the AGC-kinase C-terminal domain. These sites serves as phosphorylation-regulated switches to control both intra- and inter-molecular interactions. Without these priming phosphorylations, the kinases are catalytically inactive [[cite:PUB00043770], [cite:PUB00043771], [cite:PUB00043772]].</p> <p>Several structures of the AGC-kinase C-terminal domain have been solved. The first phosphorylation site is located in a turn motif, the second one at the end of the domain in an hydrophobic pocket. In PKB the phosphorylated hydrophobic motif engages a hydrophobic groove within the N-lobe of the kinase domain which orders α helices close to the active site [[cite:PUB00022308]].</p> <p>Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity [[cite:PUB00005115]]:</p> <ul> <li>Serine/threonine-protein kinases</li> <li>Tyrosine-protein kinases</li> <li>Dual specificity protein kinases (e.g. MEK -phosphorylates both Thr and Tyr on target proteins)</li> </ul> <p>Protein kinase function is evolutionarily conserved from Escherichia coli to human [[cite:PUB00020114]]. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation [[cite:PUB00015362]]. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [[cite:PUB00034898]], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [[cite:PUB00034899]].</p>

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on April 27, 2020, while the GO metadata was last updated on April 27, 2020.

Associated Lotus transcripts 36

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: