Protein Domain : IPR017441

Type:  Binding_site Name:  Protein kinase, ATP binding 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 enzymes that 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.This entry represents a conserved site, which is located in the N-terminal extremity of the catalytic domain, where there is a glycine-rich stretch of residues in the vicinity of a lysine residue. It is this lysine residue that has been shown to be involved in ATP binding. Short Name:  Protein_kinase_ATP_BS
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0 Child Features

0 Contains

1 Cross References

Identifier
PS00107

64 Found Ins

DB identifier Type Name
IPR000719 Domain Protein kinase domain
IPR020635 Domain Tyrosine-protein kinase, catalytic domain
IPR011009 Domain Protein kinase-like domain
IPR002290 Domain Serine/threonine/dual specificity protein kinase, catalytic domain
IPR001245 Domain Serine-threonine/tyrosine-protein kinase catalytic domain
IPR017348 Family Serine/threonine-protein kinase pim-1/2/3
IPR008352 Family Mitogen-activated protein (MAP) kinase, p38
IPR016243 Family Tyrosine-protein kinase, CSF-1/PDGF receptor family
IPR008350 Family Mitogen-activated protein (MAP) kinase, ERK3/4
IPR002374 Family cGMP-dependent kinase
IPR016255 Family Serine/threonine-protein kinase, GCN2
IPR016251 Family Tyrosine-protein kinase, non-receptor Jak/Tyk2
IPR016248 Family Fibroblast growth factor receptor family
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
IPR016236 Family Serine/threonine-protein kinase PknK, predicted
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
IPR016249 Family Tyrosine-protein kinase, Ret receptor
IPR016244 Family Tyrosine-protein kinase, HGF/MSP receptor
IPR016246 Family Tyrosine-protein kinase, insulin-like receptor
IPR016252 Family Serine/threonine-protein kinase SpkB
IPR020693 Family Tyrosine-protein kinase, non-receptor Jak2
IPR020775 Family Tyrosine-protein kinase, non-receptor Jak3
IPR020776 Family Tyrosine-protein kinase, non-receptor Jak1

1 GO Annotation

GO Term Gene Name
GO:0005524 IPR017441

1 Ontology Annotations

GO Term Gene Name
GO:0005524 IPR017441

0 Parent Features

0 Proteins

9 Publications

First Author Title Year Journal Volume Pages PubMed ID
            3291115
            12368087
            12471243
            15078142
            15320712
            7768349
            1835513
            1956325
            12734000