Protein Domain : IPR003117

Type:  Domain Name:  cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring 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 [].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. All R subunits have a conserved domain structure consisting of the N-terminal dimerization 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.Two types of regulatory (R) subunits exist - types I and I - which differ in molecular weight, sequence, autophosphorylation cabaility, cellular location and tissue distribution. Types I and II were further sub-divided into alpha and beta subtypes, based mainly on sequence similarity. This entry represents the dimerization-anchoring domain of types I-alpha, I-beta, II-alpha and II-beta regulatory subunits of PKA proteins. These subunits contain the dimerisation interface and binding site for A-kinase-anchoring proteins (AKAPs). Short Name:  cAMP_dep_PK_reg_su_I/II_a/b

0 Child Features

0 Contains

3 Cross Referencess

Identifier
PF02197
SM00394
SSF47391

2 Found Ins

DB identifier Type Name
IPR012198 Family cAMP-dependent protein kinase regulatory subunit
IPR012105 Family Sperm surface protein Sp17

0 GO Annotation

0 Parent Features

81 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
402537 D8QQZ6 PAC:15404987 Selaginella moellendorffii 197  
402629 D8QMJ0 PAC:15405776 Selaginella moellendorffii 100  
424131 D8SNX2 PAC:15422134 Selaginella moellendorffii 114  
evm.model.supercontig_112.86 PAC:16405991 Carica papaya 87  
35576 PAC:27390749 Coccomyxa subellipsoidea C-169 477  
40194 PAC:27390319 Coccomyxa subellipsoidea C-169 167  
38308 PAC:27388267 Coccomyxa subellipsoidea C-169 477  
53618 PAC:27388632 Coccomyxa subellipsoidea C-169 119  
63054 PAC:27340429 Micromonas pusilla CCMP1545 211  
123859 C1N186 PAC:27340242 Micromonas pusilla CCMP1545 164  
50851 C1MJ88 PAC:27345386 Micromonas pusilla CCMP1545 175  
122540 C1ML07 PAC:27342946 Micromonas pusilla CCMP1545 478  
122954 C1MLV2 PAC:27347475 Micromonas pusilla CCMP1545 353  
184763 C1MM48 PAC:27347300 Micromonas pusilla CCMP1545 150  
188348 C1MY51 PAC:27338680 Micromonas pusilla CCMP1545 288  
34566 PAC:27339121 Micromonas pusilla CCMP1545 497  
60706 PAC:27344358 Micromonas pusilla CCMP1545 123  
60816 PAC:27344573 Micromonas pusilla CCMP1545 289  
62265 PAC:27405349 Micromonas sp. RCC299 295  
86323 C1EEG1 PAC:27404879 Micromonas sp. RCC299 487  
63196 PAC:27399616 Micromonas sp. RCC299 150  
98177 PAC:27399973 Micromonas sp. RCC299 216  
109044 C1FH75 PAC:27397596 Micromonas sp. RCC299 325  
59235 C1E836 PAC:27401867 Micromonas sp. RCC299 150  
107587 C1FEB5 PAC:27398953 Micromonas sp. RCC299 477  
56497 C1DZL5 PAC:27396533 Micromonas sp. RCC299 96  
28765 A4RQS6 PAC:27417827 Ostreococcus lucimarinus 477  
32386 A4RZH3 PAC:27418590 Ostreococcus lucimarinus 200  
26947 A4S608 PAC:27417197 Ostreococcus lucimarinus 76  
Cre01.g034550.t1.2 PAC:30789260 Chlamydomonas reinhardtii 176  

6 Publications

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