Protein Domain : IPR016149

Type:  Domain Name:  Casein kinase II, regulatory subunit, alpha-helical
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 [].Casein kinase, a ubiquitous, well-conserved protein kinase involved in cell metabolism and differentiation, is characterised by its preference for Ser or Thr in acidic stretches of amino acids. The enzyme is a tetramer of 2 alpha- and 2 beta-subunits [, ]. However, some species (e.g., mammals) possess 2 related forms of the alpha-subunit (alpha and alpha'), while others (e.g., fungi) possess 2 related beta-subunits (beta and beta') []. The alpha-subunit is the catalytic unit and contains regions characteristic of serine/threonine protein kinases. The beta-subunit is believed to be regulatory, possessing an N-terminal auto-phosphorylation site, an internal acidic domain, and a potential metal-binding motif []. The beta subunit is a highly conserved protein of about 25kDa that contains, in its central section, a cysteine-rich motif, CX(n)C, that could be involved in binding a metal such as zinc []. The mammalian beta-subunit gene promoter shares common features with those of other mammalian protein kinases and is closely related to the promoter of the regulatory subunit of cAMP-dependent protein kinase [].This entry represents the N-terminal alpha-helical domain, which has an orthogonal bundle topology. Short Name:  Casein_kin_II_reg-sub_a-hlx

0 Child Features

0 Contains

1 Cross References


1 Found In

DB identifier Type Name
IPR000704 Family Casein kinase II, regulatory subunit

2 GO Annotations

GO Term Gene Name Organism
GO:0019887 IPR016149
GO:0005956 IPR016149

0 Parent Features

315 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
evm.model.supercontig_249.10 PAC:16414672 Carica papaya 710  
30009.m000828 B9S0R4 PAC:16815609 Ricinus communis 713  
orange1.1g029318m A0A067HC58 PAC:18136931 Citrus sinensis 195  
orange1.1g029292m A0A067HC58 PAC:18136930 Citrus sinensis 195  
Thhalv10024456m V4MD13 PAC:20195400 Eutrema salsugineum 789  
Thhalv10018205m V4MA83 PAC:20192418 Eutrema salsugineum 704  
MDP0000561057 PAC:22648197 Malus domestica 169  
MDP0000249450 PAC:22648516 Malus domestica 214  
MDP0000203215 PAC:22632956 Malus domestica 214  
MDP0000842796 PAC:22637528 Malus domestica 184  
Potri.001G149600.3 PAC:27041657 Populus trichocarpa 254  
Gorai.009G230900.1 A0A0D2USJ5 PAC:26761977 Gossypium raimondii 68  
Gorai.008G110700.3 A0A0D2U137 PAC:26816957 Gossypium raimondii 178  
Gorai.008G110700.5 A0A0D2RDG8 PAC:26816958 Gossypium raimondii 154  
Gorai.008G110700.2 A0A0D2T477 PAC:26816956 Gossypium raimondii 205  
mrna35160.1-v1.0-hybrid PAC:27265837 Fragaria vesca 132  
Thecc1EG027050t1 A0A061G976 PAC:27438180 Theobroma cacao 534  
Pavir.J00519.2.p PAC:30246049 Panicum virgatum 205  
Pavir.J00519.1.p PAC:30246048 Panicum virgatum 206  
Glyma.17G081200.2.p A0A0R0FA62 PAC:30478683 Glycine max 225  
Bostr.25542s0007.3.p PAC:30672206 Boechera stricta 669  
Bostr.25542s0007.4.p PAC:30672207 Boechera stricta 669  
Bostr.25542s0007.5.p PAC:30672208 Boechera stricta 669  
GRMZM2G098208_P02 B4FN07 PAC:31006163 Zea mays 166  
GRMZM2G098208_P05 A0A096RIZ3 PAC:31006164 Zea mays 132  
GRMZM2G098208_P04 B4FN07 PAC:31006162 Zea mays 166  
GRMZM2G148216_P02 K7VCB7 PAC:31037336 Zea mays 159  
GRMZM2G148216_P04 K7VCB7 PAC:31037335 Zea mays 159  
Medtr1g041545.1 A0A072VI10 PAC:31097042 Medicago truncatula 84  
SapurV1A.0241s0220.5.p PAC:31446374 Salix purpurea 191  

9 Publications

First Author Title Year Journal Volume Pages PubMed ID