dual specificity tyrosine phosphorylation regulated kinase 2 | Dyrk2 subfamily | IUPHAR/BPS Guide to PHARMACOLOGY

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dual specificity tyrosine phosphorylation regulated kinase 2

Target not currently curated in GtoImmuPdb

Target id: 2011

Nomenclature: dual specificity tyrosine phosphorylation regulated kinase 2

Abbreviated Name: DYRK2

Family: Dyrk2 subfamily

Annotation status:  image of an orange circle Annotated and awaiting review. Please contact us if you can help with reviewing.  » Email us

Gene and Protein Information
Species TM AA Chromosomal Location Gene Symbol Gene Name Reference
Human - 528 12q15 DYRK2 dual specificity tyrosine phosphorylation regulated kinase 2
Mouse - 599 10 D2 Dyrk2 dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 2
Rat - 527 7 q22 Dyrk2 dual specificity tyrosine phosphorylation regulated kinase 2
Previous and Unofficial Names
dual specificity tyrosine-(Y)-phosphorylation regulated kinase 2
Database Links
BRENDA
ChEMBL Target
Ensembl Gene
Entrez Gene
Human Protein Atlas
KEGG Enzyme
KEGG Gene
OMIM
RefSeq Nucleotide
RefSeq Protein
UniProtKB
Wikipedia
Selected 3D Structures
Image of receptor 3D structure from RCSB PDB
Description:  Crystal Structure of dual-specificity tyrosine phosphorylation regulated kinase 2 (DYRK2) in complex with an indirubin ligand
PDB Id:  3KVW
Resolution:  2.28Å
Species:  Human
References: 
Image of receptor 3D structure from RCSB PDB
Description:  Crystal Structure of dual-specificity tyrosine phosphorylation regulated kinase 2 (DYRK2)
PDB Id:  3K2L
Resolution:  2.36Å
Species:  Human
References:  7
Enzyme Reaction
EC Number: 2.7.12.1

Download all structure-activity data for this target as a CSV file

Inhibitors
Key to terms and symbols View all chemical structures Click column headers to sort
Ligand Sp. Action Value Parameter Reference
leucettine L41 Hs Inhibition 9.5 pIC50 4
pIC50 9.5 (IC50 3.5x10-10 M) [4]
compound 5b [PMID: 24900464] Hs Inhibition 7.2 pIC50 5
pIC50 7.2 (IC50 6x10-8 M) [5]
compound 3b [PMID: 23454515] Hs Inhibition 6.9 pIC50 2
pIC50 6.9 (IC50 1.3x10-7 M) [2]
DiscoveRx KINOMEscan® screen
A screen of 72 inhibitors against 456 human kinases. Quantitative data were derived using DiscoveRx KINOMEscan® platform.
http://www.discoverx.com/services/drug-discovery-development-services/kinase-profiling/kinomescan
Reference: 3,8

Key to terms and symbols Click column headers to sort
Target used in screen: DYRK2
Ligand Sp. Type Action Value Parameter
lestaurtinib Hs Inhibitor Inhibition 7.7 pKd
PP-242 Hs Inhibitor Inhibition 7.2 pKd
A-674563 Hs Inhibitor Inhibition 7.2 pKd
AST-487 Hs Inhibitor Inhibition 6.7 pKd
staurosporine Hs Inhibitor Inhibition 6.6 pKd
KW-2449 Hs Inhibitor Inhibition 6.4 pKd
tamatinib Hs Inhibitor Inhibition 6.3 pKd
sunitinib Hs Inhibitor Inhibition 6.2 pKd
erlotinib Hs Inhibitor Inhibition 5.9 pKd
SU-14813 Hs Inhibitor Inhibition 5.9 pKd
Displaying the top 10 most potent ligands  View all ligands in screen »
EMD Millipore KinaseProfilerTM screen/Reaction Biology Kinase HotspotSM screen
A screen profiling 158 kinase inhibitors (Calbiochem Protein Kinase Inhibitor Library I and II, catalogue numbers 539744 and 539745) for their inhibitory activity at 1µM and 10µM against 234 human recombinant kinases using the EMD Millipore KinaseProfilerTM service.

A screen profiling the inhibitory activity of 178 commercially available kinase inhibitors at 0.5µM against a panel of 300 recombinant protein kinases using the Reaction Biology Corporation Kinase HotspotSM platform.

http://www.millipore.com/techpublications/tech1/pf3036
http://www.reactionbiology.com/webapps/main/pages/kinase.aspx


Reference: 1,6

Key to terms and symbols Click column headers to sort
Target used in screen: DYRK2/DYRK2
Ligand Sp. Type Action % Activity remaining at 0.5µM % Activity remaining at 1µM % Activity remaining at 10µM
JAK3 inhibitor VI Hs Inhibitor Inhibition 3.1 -5.0 -6.0
SB 218078 Hs Inhibitor Inhibition 5.9 91.0 58.0
K-252a Hs Inhibitor Inhibition 9.9 2.0 -4.0
PKR inhibitor Hs Inhibitor Inhibition 12.1 1.0 -5.0
SP600125 Hs Inhibitor Inhibition 14.2 4.0 -5.0
Cdc2-like kinase inhibitor Hs Inhibitor Inhibition 19.5 5.0 -5.0
JNK inhibitor V Hs Inhibitor Inhibition 22.2 19.0 2.0
PI 3-Kg inhibitor Hs Inhibitor Inhibition 39.8 7.0 -4.0
alsterpaullone 2-cyanoethyl Hs Inhibitor Inhibition 46.8 28.0 12.0
dorsomorphin Hs Inhibitor Inhibition 47.0 52.0 7.0
Displaying the top 10 most potent ligands  View all ligands in screen »

References

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1. Anastassiadis T, Deacon SW, Devarajan K, Ma H, Peterson JR. (2011) Comprehensive assay of kinase catalytic activity reveals features of kinase inhibitor selectivity. Nat. Biotechnol., 29 (11): 1039-45. [PMID:22037377]

2. Burgy G, Tahtouh T, Durieu E, Foll-Josselin B, Limanton E, Meijer L, Carreaux F, Bazureau JP. (2013) Chemical synthesis and biological validation of immobilized protein kinase inhibitory Leucettines. Eur J Med Chem, 62: 728-37. [PMID:23454515]

3. Davis MI, Hunt JP, Herrgard S, Ciceri P, Wodicka LM, Pallares G, Hocker M, Treiber DK, Zarrinkar PP. (2011) Comprehensive analysis of kinase inhibitor selectivity. Nat. Biotechnol., 29 (11): 1046-51. [PMID:22037378]

4. Debdab M, Carreaux F, Renault S, Soundararajan M, Fedorov O, Filippakopoulos P, Lozach O, Babault L, Tahtouh T, Baratte B et al.. (2011) Leucettines, a class of potent inhibitors of cdc2-like kinases and dual specificity, tyrosine phosphorylation regulated kinases derived from the marine sponge leucettamine B: modulation of alternative pre-RNA splicing. J. Med. Chem., 54 (12): 4172-86. [PMID:21615147]

5. Dowling JE, Chuaqui C, Pontz TW, Lyne PD, Larsen NA, Block MH, Chen H, Su N, Wu A, Russell D et al.. (2012) Potent and Selective Inhibitors of CK2 Kinase Identified through Structure-Guided Hybridization. ACS Med Chem Lett, 3 (4): 278-83. [PMID:24900464]

6. Gao Y, Davies SP, Augustin M, Woodward A, Patel UA, Kovelman R, Harvey KJ. (2013) A broad activity screen in support of a chemogenomic map for kinase signalling research and drug discovery. Biochem. J., 451 (2): 313-28. [PMID:23398362]

7. Soundararajan M, Roos AK, Savitsky P, Filippakopoulos P, Kettenbach AN, Olsen JV, Gerber SA, Eswaran J, Knapp S, Elkins JM. (2013) Structures of Down syndrome kinases, DYRKs, reveal mechanisms of kinase activation and substrate recognition. Structure, 21 (6): 986-96. [PMID:23665168]

8. Wodicka LM, Ciceri P, Davis MI, Hunt JP, Floyd M, Salerno S, Hua XH, Ford JM, Armstrong RC, Zarrinkar PP et al.. (2010) Activation state-dependent binding of small molecule kinase inhibitors: structural insights from biochemistry. Chem. Biol., 17 (11): 1241-9. [PMID:21095574]

How to cite this page

Dyrk2 subfamily: dual specificity tyrosine phosphorylation regulated kinase 2. Last modified on 30/03/2016. Accessed on 24/02/2020. IUPHAR/BPS Guide to PHARMACOLOGY, http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=2011.