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Protein Domain : IPR000961

Name  AGC-kinase, C-terminal Short Name  AGC-kinase_C
Type  Domain Description  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 []:Serine/threonine-protein kinasesTyrosine-protein kinasesDual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)Protein kinase function is evolutionarily conserved from Escherichia coli to human []. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation []. 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 [], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [].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 [, , ].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 alpha helices close to the active site [].

Publication Counts Displayer

1 Child Features

DB identifier Name Short Name Type
IPR017892 Protein kinase, C-terminal Pkinase_C Domain

0 Contains

2 Cross References

Identifier
Source . Name

Subject . Primary Identifier
PS51285 PROFILE IPR000961
SM00133 SMART IPR000961

3 Data Sets

Name URL
Swiss-Prot data set http://ca.expasy.org/sprot
InterPro data set  
InterPro GO Annotation data set  

4 Found In

DB identifier Name Short Name Type
IPR016232 cGMP-dependent protein kinase cGMP-dependent_protein_kinase Family
IPR002374 cGMP-dependent kinase cGMP_dep_kinase Family
IPR000239 GPCR kinase GPCR_kinase Family
IPR020684 Rho-associated protein kinase Rho-assoc_coiled-coil_kin Family

3 GO Annotation


Subject . Secondary Identifier

Subject . Name

Subject . Symbol

Ontology Term . Identifier

Ontology Term . Name
AGC-kinase, C-terminal   GO:0004674 protein serine/threonine kinase activity
AGC-kinase, C-terminal   GO:0005524 ATP binding
AGC-kinase, C-terminal   GO:0006468 protein phosphorylation

3 Ontology Annotations


Subject . Secondary Identifier

Subject . Name

Subject . Symbol

Ontology Term . Identifier

Ontology Term . Name
AGC-kinase, C-terminal   GO:0004674 protein serine/threonine kinase activity
AGC-kinase, C-terminal   GO:0005524 ATP binding
AGC-kinase, C-terminal   GO:0006468 protein phosphorylation

0 Parent Features

358 Proteins

DB identifier Primary Accession
Organism . Name
FBpp0076820 Q94533 Drosophila melanogaster
FBpp0072194 Q9W1B0 Drosophila melanogaster
FBpp0099769 P32023 Drosophila melanogaster
FBpp0075283 P16912 Drosophila melanogaster
FBpp0290731 Q4QQA3 Drosophila melanogaster
FBpp0075702 Q9VTY8 Drosophila melanogaster
FBpp0087682 A1Z7T0 Drosophila melanogaster
FBpp0087683 A1Z7T1 Drosophila melanogaster
FBpp0087686 A1Z7T4 Drosophila melanogaster
FBpp0087684 A1Z7T2 Drosophila melanogaster
FBpp0082682 Q8INB9 Drosophila melanogaster
FBpp0086196 P13677 Drosophila melanogaster
FBpp0111731 A8DYG9 Drosophila melanogaster
FBpp0293606 D3DMK5 Drosophila melanogaster
FBpp0086197 P05130 Drosophila melanogaster
FBpp0085082 Q9VA38 Drosophila melanogaster
FBpp0110413 P32865 Drosophila melanogaster
FBpp0085149 P32866 Drosophila melanogaster
FBpp0085089 Q53XD8 Drosophila melanogaster
FBpp0083089 Q95TN8 Drosophila melanogaster
FBpp0079448 P12370 Drosophila melanogaster
FBpp0077052 Q9VR61 Drosophila melanogaster
FBpp0074061 Q9VXE3 Drosophila melanogaster
FBpp0292487 A1Z9X0 Drosophila melanogaster
FBpp0075315 Q9VUQ9 Drosophila melanogaster
FBpp0088354 E1JHR9 Drosophila melanogaster
FBpp0088350 Q03043 Drosophila melanogaster
FBpp0085090 Q9VA47 Drosophila melanogaster
FBpp0079534 Q9VL34 Drosophila melanogaster
FBpp0075965 Q9V3I5 Drosophila melanogaster