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protein kinase D2

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Target not currently curated in GtoImmuPdb

Target id: 2173

Nomenclature: protein kinase D2

Abbreviated Name: PKD2

Family: Protein kinase D (PKD) family

Contents:

Gene and Protein Information Click here for help
Species TM AA Chromosomal Location Gene Symbol Gene Name Reference
Human - 878 19q13.32 PRKD2 protein kinase D2
Mouse - 875 7 A2 Prkd2 protein kinase D2
Rat - 875 1q21 Prkd2 protein kinase D2
Database Links Click here for help
Alphafold Q9BZL6 (Hs), Q8BZ03 (Mm), Q5XIS9 (Rn)
BRENDA 2.7.11.13
CATH/Gene3D 2.30.29.30
ChEMBL Target CHEMBL4900 (Hs)
Ensembl Gene ENSG00000105287 (Hs), ENSMUSG00000041187 (Mm), ENSRNOG00000016434 (Rn)
Entrez Gene 25865 (Hs), 101540 (Mm), 292658 (Rn)
Human Protein Atlas ENSG00000105287 (Hs)
KEGG Enzyme 2.7.11.13
KEGG Gene hsa:25865 (Hs), mmu:101540 (Mm), rno:292658 (Rn)
OMIM 607074 (Hs)
Pharos Q9BZL6 (Hs)
RefSeq Nucleotide NM_001079880 (Hs), NM_178900 (Mm), NM_001013895 (Rn)
RefSeq Protein NP_001073349 (Hs), NP_849231 (Mm), NP_001013917 (Rn)
UniProtKB Q9BZL6 (Hs), Q8BZ03 (Mm), Q5XIS9 (Rn)
Wikipedia PRKD2 (Hs)
Selected 3D Structures Click here for help
Image of receptor 3D structure from RCSB PDB
Description:  Solution structure of the PH domain of protein kinase C, D2 type from human
PDB Id:  2COA
Resolution:  0.0Å
Species:  Human
References: 
Image of receptor 3D structure from RCSB PDB
Description:  Crystal Structure of PKD2 Phosphopeptide Bound to Human Class I MHC HLA-A2
PDB Id:  3BGM
Resolution:  1.6Å
Species:  Human
References:  5
Enzyme Reaction Click here for help
EC Number: 2.7.11.13

Download all structure-activity data for this target as a CSV file go icon to follow link

Inhibitors
Key to terms and symbols View all chemical structures Click column headers to sort
Ligand Sp. Action Value Parameter Reference
CRT 0066101 Small molecule or natural product Primary target of this compound Click here for species-specific activity table Hs Inhibition 8.6 pIC50 4
⤷ pIC50 8.6 (IC50 2.5x10-9 M) [4]
BPKDi Small molecule or natural product Click here for species-specific activity table Hs Inhibition 8.1 pIC50 6
⤷ pIC50 8.1 (IC50 9x10-9 M) [6]
Description: In a biochemical enzyme assay.
DiscoveRx KINOMEscan® screen Click here for help
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: 2,7
Key to terms and symbols Click column headers to sort
Target used in screen: PRKD2
Ligand Sp. Type Action Value Parameter
lestaurtinib Small molecule or natural product Ligand has a PDB structure Immunopharmacology Ligand Hs Inhibitor Inhibition 8.1 pKd
staurosporine Small molecule or natural product Ligand has a PDB structure Hs Inhibitor Inhibition 7.1 pKd
NVP-TAE684 Small molecule or natural product Ligand has a PDB structure Hs Inhibitor Inhibition 6.8 pKd
JNJ-28312141 Small molecule or natural product Hs Inhibitor Inhibition 6.5 pKd
sunitinib Small molecule or natural product Approved drug Ligand has a PDB structure Hs Inhibitor Inhibition 6.4 pKd
BI-2536 Small molecule or natural product Ligand has a PDB structure Hs Inhibitor Inhibition 6.3 pKd
ruboxistaurin Small molecule or natural product Ligand has a PDB structure Hs Inhibitor Inhibition 6.1 pKd
AST-487 Small molecule or natural product Hs Inhibitor Inhibition 6.0 pKd
alvocidib Small molecule or natural product Ligand has a PDB structure Hs Inhibitor Inhibition 6.0 pKd
neratinib Small molecule or natural product Approved drug Hs Inhibitor Inhibition 6.0 pKd
Displaying the top 10 most potent ligands  View all ligands in screen »
EMD Millipore KinaseProfilerTM screen/Reaction Biology Kinase HotspotSM screen Click here for help
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: 1,3
Key to terms and symbols Click column headers to sort
Target used in screen: PKD2/PKD2(PRKD2)
Ligand Sp. Type Action % Activity remaining at 0.5µM % Activity remaining at 1µM % Activity remaining at 10µM
staurosporine Small molecule or natural product Ligand has a PDB structure Hs Inhibitor Inhibition 1.0 5.0 0.5
K-252a Small molecule or natural product Hs Inhibitor Inhibition 1.4 2.0 0.0
SB 218078 Small molecule or natural product Hs Inhibitor Inhibition 2.0 92.0 90.0
JAK3 inhibitor VI Small molecule or natural product Hs Inhibitor Inhibition 2.2 25.0 4.0
PKR inhibitor Small molecule or natural product Ligand has a PDB structure Hs Inhibitor Inhibition 4.2 30.0 3.0
JAK inhibitor I Small molecule or natural product Ligand has a PDB structure Hs Inhibitor Inhibition 6.1 40.0 22.0
Cdk1/2 inhibitor III Small molecule or natural product Ligand has a PDB structure Hs Inhibitor Inhibition 9.1 45.0 6.0
SU11652 Small molecule or natural product Ligand has a PDB structure Hs Inhibitor Inhibition 11.9 73.0 16.0
Gö 6976 Small molecule or natural product Ligand has a PDB structure Hs Inhibitor Inhibition 18.7 29.0 32.0
sunitinib Small molecule or natural product Approved drug Ligand has a PDB structure Hs Inhibitor Inhibition 21.1
Displaying the top 10 most potent ligands  View all ligands in screen »
Immuno Process Associations
Immuno Process:  Immune regulation
Immuno Process:  Cytokine production & signalling
Immuno Process:  Cellular signalling
Immuno Process:  T cell (activation)
Immuno Process:  B cell (activation)

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. 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]

3. 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]

4. Harikumar KB, Kunnumakkara AB, Ochi N, Tong Z, Deorukhkar A, Sung B, Kelland L, Jamieson S, Sutherland R, Raynham T et al.. (2010) A novel small-molecule inhibitor of protein kinase D blocks pancreatic cancer growth in vitro and in vivo. Mol Cancer Ther, 9 (5): 1136-46. [PMID:20442301]

5. Mohammed F, Cobbold M, Zarling AL, Salim M, Barrett-Wilt GA, Shabanowitz J, Hunt DF, Engelhard VH, Willcox BE. (2008) Phosphorylation-dependent interaction between antigenic peptides and MHC class I: a molecular basis for the presentation of transformed self. Nat Immunol, 9 (11): 1236-43. [PMID:18836451]

6. Monovich L, Vega RB, Meredith E, Miranda K, Rao C, Capparelli M, Lemon DD, Phan D, Koch KA, Chapo JA et al.. (2010) A novel kinase inhibitor establishes a predominant role for protein kinase D as a cardiac class IIa histone deacetylase kinase. FEBS Lett, 584 (3): 631-7. [PMID:20018189]

7. 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

Protein kinase D (PKD) family: protein kinase D2. Last modified on 08/11/2016. Accessed on 19/04/2024. IUPHAR/BPS Guide to PHARMACOLOGY, https://www.guidetoimmunopharmacology.org/GRAC/ObjectDisplayForward?objectId=2173.