Protein Domain : IPR008271

Type:  Active_site Name:  Serine/threonine-protein kinase, active site
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 [].Eukaryotic protein kinases [, , , ] are enzymesthat belong to a very extensive family of proteins which share a conserved catalytic core common with both serine/threonine and tyrosine protein kinases. There are a number of conserved regions in the catalytic domain of protein kinases. In the N-terminal extremity of the catalytic domain there is a glycine-rich stretch of residues in the vicinity of a lysine residue, which has been shown to be involved in ATP binding. In the central part of the catalytic domain there is a conserved aspartic acid residue, which is important for the catalytic activity of the enzyme []. This signature contains the active site aspartate residue. Short Name:  Ser/Thr_kinase_AS
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0 Child Features

0 Contains

1 Cross References

Identifier
PS00108

51 Found Ins

DB identifier Type Name
IPR000719 Domain Protein kinase domain
IPR011009 Domain Protein kinase-like domain
IPR002290 Domain Serine/threonine/dual specificity protein kinase, catalytic domain
IPR020636 Family Calcium/calmodulin-dependent/calcium-dependent protein kinase
IPR015783 Family Serine/threonine-protein kinase HT1, plant
IPR008351 Family Mitogen-activated protein (MAP) kinase, JNK
IPR017348 Family Serine/threonine-protein kinase pim-1/2/3
IPR008350 Family Mitogen-activated protein (MAP) kinase, ERK3/4
IPR002374 Family cGMP-dependent kinase
IPR016255 Family Serine/threonine-protein kinase, GCN2
IPR016231 Family Mitogen-activated protein (MAP) kinase kinase kinase, MLK1/MLK2/MLK4
IPR015785 Family Mitogen-activated protein (MAP) kinase kinase kinase 10
IPR016238 Family Ribosomal protein S6 kinase
IPR016237 Family Serine/threonine-protein kinase, Ulk1/Ulk2
IPR016239 Family Ribosomal protein S6 kinase II
IPR016234 Family Serine/threonine-protein kinase, Sbk1
IPR016235 Family Tyrosine/threonine-protein kinase, Cdc2 inhibitor
IPR016241 Family Nitrogen network kinase 1
IPR016240 Family Serine/threonine-protein kinase YKL116C, predicted
IPR016242 Family Serine/threonine-protein kinase Mps1
IPR016254 Family Serine/threonine-protein kinase, asfivirus
IPR016256 Family Serine/threonine-protein kinase Rad53
IPR020676 Family Death-associated protein kinase 1
IPR014375 Family Protein kinase C, alpha/beta/gamma types
IPR014376 Family Protein kinase C, delta/epsilon/eta/theta types
IPR020684 Family Rho-associated protein kinase 1/2
IPR015727 Family Protein kinase C mu-related
IPR012233 Family Protein kinase C
IPR017405 Family Citron Rho-interacting kinase
IPR002291 Family Phosphorylase kinase, gamma catalytic subunit

2 GO Annotations

GO Term Gene Name
GO:0004672 IPR008271
GO:0006468 IPR008271

2 Ontology Annotations

GO Term Gene Name
GO:0004672 IPR008271
GO:0006468 IPR008271

0 Parent Features

0 Proteins

9 Publications

First Author Title Year Journal Volume Pages PubMed ID
            3291115
            12368087
            12471243
            15078142
            15320712
            7768349
            1835513
            1956325
            1862342