InterPro : IPR020635

Name  Tyrosine-protein kinase, catalytic domain Short Name  Tyr_kinase_cat_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 [].Tyrosine-protein kinases can transfer a phosphate group from ATP to a tyrosine residue in a protein. These enzymes can be divided into two main groups []:Receptor tyrosine kinases (RTK), which are transmembrane proteins involved in signal transduction; they play key roles in growth, differentiation, metabolism, adhesion, motility, death and oncogenesis []. RTKs are composed of 3 domains: an extracellular domain (binds ligand), a transmembrane (TM) domain, and an intracellular catalytic domain (phosphorylates substrate). The TM domain plays an important role in the dimerisation process necessary for signal transduction []. Cytoplasmic / non-receptor tyrosine kinases, which act as regulatory proteins, playing key roles in cell differentiation, motility, proliferation, and survival. For example, the Src-family of protein-tyrosine kinases [].
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Sequence Features

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Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

4 Contains

Id Name Short Name Type
IPR017441 Protein kinase, ATP binding site Protein_kinase_ATP_BS Binding_site
IPR008266 Tyrosine-protein kinase, active site Tyr_kinase_AS Active_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

23 Found In

Id Name Short Name Type
IPR016250 Tyrosine-protein kinase, Fes/Fps type Tyr-prot_kinase_Fes/Fps Family
IPR020691 Ephrin type-A receptor 8 EphrinA_rcpt8 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
IPR016243 Tyrosine-protein kinase, CSF-1/PDGF receptor family Tyr_kinase_CSF1/PDGF_rcpt Family
IPR016249 Tyrosine-protein kinase, Ret receptor Tyr_kinase_Ret_rcpt Family
IPR016245 Tyrosine protein kinase, EGF/ERB/XmrK receptor Tyr_kinase_EGF/ERB/XmrK_rcpt Family
IPR016244 Tyrosine-protein kinase, HGF/MSP receptor Tyr_kinase_HGF/MSP_rcpt 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
IPR016257 Ephrin receptor type-A /type-B Tyr_kinase_ephrin_rcpt Family
IPR020461 Tyrosine-protein kinase, neurotrophic receptor, type 1 Tyr_kinase_neurotrophic_rcpt_1 Family
IPR020446 Tyrosine-protein kinase, neurotrophic receptor, type 3 Tyr_kin_neurotrophic_rcpt_3 Family
IPR020455 Tyrosine-protein kinase, neurotrophic receptor, type 2 Tyr_kin_neurotrophic_rcpt_2 Family
IPR020777 Tyrosine-protein kinase, neurotrophic receptor Tyr_kinase_NGF_rcpt Family
IPR012234 Tyrosine-protein kinase, non-receptor SYK/ZAP-70 Tyr_kinase_non-rcpt_SYK/ZAP70 Family
IPR020766 Receptor-like tyrosine-protein kinase kin-15/kin-16 kin-15/kin-16 Family
IPR009136 Vascular endothelial growth factor receptor 2 (VEGFR2) VEGFR2_rcpt Family

1 Parent Features

Id Name Short Name Type
IPR001245 Serine-threonine/tyrosine-protein kinase catalytic domain Ser-Thr/Tyr_kinase_cat_dom Domain

8 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
Sharma PS Receptor tyrosine kinase inhibitors as potent weapons in war against cancers. 2009 Curr Pharm Des 15 758-76
Li E Role of receptor tyrosine kinase transmembrane domains in cell signaling and human pathologies. 2006 Biochemistry 45 6241-51
Roskoski R Jr Src kinase regulation by phosphorylation and dephosphorylation. 2005 Biochem Biophys Res Commun 331 1-14



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)