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

0 Child Features

0 Contains

1 Cross References

Identifier
PS00107

64 Found Ins

DB identifier Type Name
IPR000719 Domain Protein kinase domain
IPR011009 Domain Protein kinase-like domain
IPR020635 Domain Tyrosine-protein kinase, catalytic domain
IPR001245 Domain Serine-threonine/tyrosine-protein kinase catalytic domain
IPR002290 Domain Serine/threonine/dual specificity 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
IPR009136 Family Vascular endothelial growth factor receptor 2 (VEGFR2)
IPR020691 Family Ephrin type-A receptor 8
IPR016246 Family Tyrosine-protein kinase, insulin-like receptor
IPR016251 Family Tyrosine-protein kinase, non-receptor Jak/Tyk2
IPR020775 Family Tyrosine-protein kinase, non-receptor Jak3
IPR020693 Family Tyrosine-protein kinase, non-receptor Jak2
IPR020776 Family Tyrosine-protein kinase, non-receptor Jak1
IPR020777 Family Tyrosine-protein kinase, neurotrophic receptor
IPR020446 Family Tyrosine-protein kinase, neurotrophic receptor, type 3
IPR020455 Family Tyrosine-protein kinase, neurotrophic receptor, type 2
IPR020461 Family Tyrosine-protein kinase, neurotrophic receptor, type 1
IPR020679 Family Serine/threonine-protein kinase Tda1
IPR020675 Family Myosin light chain kinase-related
IPR015725 Family Telokin/Myosin light chain kinase
IPR015726 Family Serine/threonine protein kinase, striated muscle-specific
IPR020676 Family Death-associated protein kinase 1
IPR016257 Family Ephrin receptor type-A /type-B
IPR020684 Family Rho-associated protein kinase 1/2
IPR020682 Family Obscurin-myosin light chain kinase
IPR012234 Family Tyrosine-protein kinase, non-receptor SYK/ZAP-70
IPR015785 Family Mitogen-activated protein (MAP) kinase kinase kinase 10
IPR021160 Family Mitogen-activated protein (MAP) kinase kinase kinase kinase

1 GO Annotation

GO Term Gene Name Organism
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