InterPro : IPR000719

Name  Protein kinase domain Short Name  Prot_kinase_dom
Type  Domain 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 withboth serine/threonine and tyrosine protein kinases. There are a number of conserved regions in thecatalytic domain of protein kinases. In the N-terminal extremity of the catalytic domain there is aglycine-rich stretch of residues in the vicinity of a lysine residue, which has been shown to be involvedin ATP binding. In the central part of the catalytic domain there is a conserved aspartic acid residuewhich is important for the catalytic activity of the enzyme []. This entry represents the protein kinase domain containing the catalytic function of protein kinases []. This domain is found in serine/threonine-protein kinases, tyrosine-protein kinases and dual specificity protein kinases.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



3 Child Features

Id Name Short Name Type
IPR001245 Serine-threonine/tyrosine-protein kinase catalytic domain Ser-Thr/Tyr_kinase_cat_dom Domain
IPR002290 Serine/threonine/dual specificity protein kinase, catalytic domain Ser/Thr_dual-sp_kinase Domain
IPR027916 Protein kinase-like domain, Apicomplexa Kinase-like_dom_Apicomplexa Domain

6 Contains

Id Name Short Name Type
IPR008271 Serine/threonine-protein kinase, active site Ser/Thr_kinase_AS Active_site
IPR017441 Protein kinase, ATP binding site Protein_kinase_ATP_BS Binding_site
IPR008266 Tyrosine-protein kinase, active site Tyr_kinase_AS Active_site
IPR003527 Mitogen-activated protein (MAP) kinase, conserved site MAP_kinase_CS Conserved_site
IPR002011 Tyrosine-protein kinase, receptor class II, conserved site Tyr_kinase_rcpt_2_CS Conserved_site
IPR001824 Tyrosine-protein kinase, receptor class III, conserved site Tyr_kinase_rcpt_3_CS Conserved_site

56 Found In

Id Name Short Name Type
IPR020636 Calcium/calmodulin-dependent/calcium-dependent protein kinase Ca/CaM-dep_Ca-dep_prot_Kinase Family
IPR015725 Telokin/Myosin light chain kinase Telokin/Myosin_light_ch_kin Family
IPR002291 Phosphorylase kinase, gamma catalytic subunit Phosph_kin_gamma Family
IPR000239 GPCR kinase GPCR_kinase Family
IPR002374 cGMP-dependent kinase cGMP_dep_kinase 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
IPR015782 Dual specificity testis-specific protein kinase 1 TESK1 Family
IPR020676 Death-associated protein kinase 1 DAPK1 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
IPR020691 Ephrin type-A receptor 8 EphrinA_rcpt8 Family
IPR016232 cGMP-dependent protein kinase cGMP-dependent_protein_kinase Family
IPR016251 Tyrosine-protein kinase, non-receptor Jak/Tyk2 Tyr_kinase_non-rcpt_Jak/Tyk2 Family
IPR009220 Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein tRNA_threonyl_synthase/kinase 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
IPR016237 Serine/threonine-protein kinase, Ulk1/Ulk2 Ser/Thr_kin_STPK_Ulk-1/2 Family
IPR016234 Serine/threonine-protein kinase, Sbk1 Ser/Thr_kinase_Sbk1 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
IPR016240 Serine/threonine-protein kinase YKL116C, predicted Ser/Thr_kin_YKL116c_prd Family
IPR016243 Tyrosine-protein kinase, CSF-1/PDGF receptor family Tyr_kinase_CSF1/PDGF_rcpt Family
IPR016242 Serine/threonine-protein kinase Mps1-like, Saccharomycetes Ser/Thr_kinase_Mps1_Saccharo Family
IPR016247 Tyrosine-protein kinase, receptor ROR Tyr_kinase_rcpt_ROR Family
IPR016246 Tyrosine-protein kinase, insulin-like receptor Tyr_kinase_insulin-like_rcpt Family
IPR020693 Tyrosine-protein kinase, non-receptor Jak2 Tyr_kinase_non-rcpt_Jak2 Family
IPR020775 Tyrosine-protein kinase, non-receptor Jak3 Tyr_kinase_non-rcpt_Jak3 Family
IPR020776 Tyrosine-protein kinase, non-receptor Jak1 Tyr_kinase_non-rcpt_Jak1 Family

1 Parent Features

Id Name Short Name Type
IPR011009 Protein kinase-like domain Kinase-like_dom Domain

10 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
Knighton DR Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. 1991 Science 253 407-14
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)