Protein Domain : IPR012198

Type:  Family Name:  cAMP-dependent protein kinase regulatory subunit
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 [].In the absence of cAMP, protein kinase A (PKA) exists as an equimolar tetramer of regulatory (R) and catalytic (C) subunits. In addition to its role as an inhibitor of the C subunit, the R subunit anchors the holoenzyme to specific intracellular locations and prevents the C subunit from entering the nucleus. Typical R subunits have a conserved domain structure, consisting of the N-terminal dimerisation domain, inhibitory region, cAMP-binding domain A and cAMP-binding domain B. R subunits interact with C subunits primarily through the inhibitory site. The cAMP-binding domains show extensive sequence similarity and bind cAMP cooperatively.On the basis of phylogenetic trees generated from multiple sequence alignment of complete sequences, this family was divided into four sub-families, types I to IV []. Types I and II, found in animals, differ in molecular weight, sequence, autophosphorylation capability, cellular location and tissue distribution. Types I and II are further sub-divided into alpha and beta subtypes, based mainly on sequence similarity. Type III are from fungi and type IV are from alveolates. Short Name:  cAMP_dep_PK_reg_su

0 Child Features

5 Contains

DB identifier Type Name
IPR018490 Domain Cyclic nucleotide-binding-like
IPR000595 Domain Cyclic nucleotide-binding domain
IPR014710 Domain RmlC-like jelly roll fold
IPR003117 Domain cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain
IPR018488 Conserved_site Cyclic nucleotide-binding, conserved site

1 Cross References

Identifier
PIRSF000548

0 Found In

3 GO Annotations

GO Term Gene Name Organism
GO:0008603 IPR012198
GO:0001932 IPR012198
GO:0005952 IPR012198

0 Parent Features

6 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
105805 D8S0D3 PAC:15417860 Selaginella moellendorffii 293  
21119 PAC:27339325 Micromonas pusilla CCMP1545 314  
155958 PAC:27341485 Micromonas pusilla CCMP1545 308  
Sphfalx0136s0042.1.p PAC:32622002 Sphagnum fallax 311  
Pp3c22_7030V3.2.p PAC:32904450 Physcomitrella patens 305  
Mapoly0030s0069.1.p PAC:33006916 Marchantia polymorpha 348  

6 Publications

First Author Title Year Journal Volume Pages PubMed ID
            3291115
            12368087
            12471243
            15078142
            15320712
            11734894