InterPro : IPR017441

Name  Protein kinase, ATP binding site Short Name  Protein_kinase_ATP_BS
Type  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.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

0 Contains

65 Found In

Id Name Short Name Type
IPR011009 Protein kinase-like domain Kinase-like_dom Domain
IPR000719 Protein kinase domain Prot_kinase_dom Domain
IPR001245 Serine-threonine/tyrosine-protein kinase catalytic domain Ser-Thr/Tyr_kinase_cat_dom Domain
IPR015725 Telokin/Myosin light chain kinase Telokin/Myosin_light_ch_kin Family
IPR002290 Serine/threonine/dual specificity protein kinase, catalytic domain Ser/Thr_dual-sp_kinase Domain
IPR000239 GPCR kinase GPCR_kinase Family
IPR020635 Tyrosine-protein kinase, catalytic domain Tyr_kinase_cat_dom Domain
IPR002374 cGMP-dependent kinase cGMP_dep_kinase Family
IPR008352 Mitogen-activated protein (MAP) kinase, p38 MAPK_p38 Family
IPR008349 Mitogen-activated protein (MAP) kinase, ERK1/2 MAPK_ERK1/2 Family
IPR020675 Myosin light chain kinase-related Myosin_light_ch_kinase-rel Family
IPR008350 Mitogen-activated protein (MAP) kinase, ERK3/4 MAPK_ERK3/4 Family
IPR020676 Death-associated protein kinase 1 DAPK1 Family
IPR015727 Protein kinase C mu-related Protein_Kinase_C_mu-related Family
IPR017184 Serine/threonine-protein kinase Unc-51 Ser/Thr_kinase_Unc51 Family
IPR016250 Tyrosine-protein kinase, Fes/Fps type Tyr-prot_kinase_Fes/Fps Family
IPR017421 Mitogen-activated protein (MAP) kinase kinase kinase 7 MAPKKK7 Family
IPR020691 Ephrin type-A receptor 8 EphrinA_rcpt8 Family
IPR016232 cGMP-dependent protein kinase cGMP-dependent_protein_kinase Family
IPR016255 Serine/threonine-protein kinase, GCN2 Ser/Thr_kinase_GCN2 Family
IPR016251 Tyrosine-protein kinase, non-receptor Jak/Tyk2 Tyr_kinase_non-rcpt_Jak/Tyk2 Family
IPR016248 Fibroblast growth factor receptor family FGF_rcpt_fam Family
IPR016231 Mitogen-activated protein (MAP) kinase kinase kinase, 9/10/11 MAPKKK9/10/11 Family
IPR015785 Mitogen-activated protein (MAP) kinase kinase kinase 10 MAP3K10 Family
IPR016238 Ribosomal protein S6 kinase Ribosomal_S6_kinase Family
IPR016237 Serine/threonine-protein kinase, Ulk1/Ulk2 Ser/Thr_kin_STPK_Ulk-1/2 Family
IPR016239 Ribosomal protein S6 kinase II Ribosomal_S6_kinase_II Family
IPR016236 Serine/threonine-protein kinase PknK, predicted Ser/Thr_kinase_PknK_prd Family
IPR016235 Tyrosine/threonine-protein kinase, Cdc2 inhibitor Tyr/Thr_kinase_Cdc2_inhib Family
IPR016241 Serine/threonine-protein kinase YKL171W, predicted Ser/Thr_kin_YKL171w_prd Family

0 Parent Features

9 Publications

First Author Title Year Journal Volume Pages
Hanks SK The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. 1988 Science 241 42-52
Manning G Evolution of protein kinase signaling from yeast to man. 2002 Trends Biochem Sci 27 514-20
Manning G The protein kinase complement of the human genome. 2002 Science 298 1912-34
Stout TJ High-throughput structural biology in drug discovery: protein kinases. 2004 Curr Pharm Des 10 1069-82
Li B Creating chemical diversity to target protein kinases. 2004 Comb Chem High Throughput Screen 7 453-72
Hanks SK Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. 1995 FASEB J 9 576-96
Hunter T Protein kinase classification. 1991 Methods Enzymol 200 3-37
Hanks SK Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. 1991 Methods Enzymol 200 38-62
Hanks SK Genomic analysis of the eukaryotic protein kinase superfamily: a perspective. 2003 Genome Biol 4 111

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)