protein kinase, cAMP-dependent, catalytic, alpha subunit

Nomenclature: protein kinase, cAMP-dependent, catalytic, alpha subunit

Abbreviated Name: PKACa

Family: Protein kinase A

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 - 351 19p13.1 PRKACA protein kinase, cAMP-dependent, catalytic, alpha
Mouse - 351 8 C3 Prkaca protein kinase, cAMP dependent, catalytic, alpha
Rat - 351 19q11 Prkaca protein kinase, cAMP-dependent, catalytic, alpha
Previous and Unofficial Names
Cs-PKA
PKCA1
PKA C-alpha
Protein kinase, cAMP-dependent, catalytic, alpha
cAMP-dependent protein kinase catalytic subunit C alpha
protein kinase A
PKA
C alpha
Cs
cAMP-dependent protein kinase catalytic subunit alpha
Pkaca
PRKACA
Database Links
BRENDA
Ensembl Gene
Entrez Gene
ExplorEnz
GeneCards
GenitoUrinary Development Molecular Anatomy Project
HomoloGene
Human Protein Reference Database
InterPro
KEGG BRITE Hierarchy
KEGG Gene
OMIM
PhosphoSitePlus
RefSeq Nucleotide
RefSeq Protein
TreeFam
UniGene
UniProtKB
Wikipedia
Selected 3D Structures
Image of receptor 3D structure from RCSB PDB
Description:  Complex of PKA with the bisubstrate protein kinase inhibitor ARC-1039
PDB Id:  3AGL
Resolution:  2.1Å
Species:  Human
References:  4
Enzyme Reaction
EC Number: 2.7.11.11
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: 2,5

Key to terms and symbols Click column headers to sort
Target used in screen: PKAC-alpha
Ligand Sp. Type Action Affinity Units
GSK690693 Hs Inhibitor Inhibition 7.72 pKd
staurosporine Hs Inhibitor Inhibition 7.72 pKd
A-674563 Hs Inhibitor Inhibition 7.25 pKd
lestaurtinib Hs Inhibitor Inhibition 6.66 pKd
enzastaurin Hs Inhibitor Inhibition 6.48 pKd
R406 Hs Inhibitor Inhibition 6.22 pKd
midostaurin Hs Inhibitor Inhibition 6.14 pKd
SB203580 Hs Inhibitor Inhibition <5.52 pKd
erlotinib Hs Inhibitor Inhibition <5.52 pKd
crizotinib Hs Inhibitor Inhibition <5.52 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: 1,3

Key to terms and symbols Click column headers to sort
Target used in screen: PKA/PKA
Ligand Sp. Type Action % Activity remaining at 0.5µM % Activity remaining at 1µM % Activity remaining at 10µM
staurosporine Hs Inhibitor Inhibition 1.9 0.5 2.5
H-89 Hs Inhibitor Inhibition 10.5 2.0 6.0
K-252a Hs Inhibitor Inhibition 18.0 7.0 3.0
midostaurin Hs Inhibitor Inhibition 34.0 13.0 10.0
PKR inhibitor Hs Inhibitor Inhibition 40.1 25.0 5.0
SB 218078 Hs Inhibitor Inhibition 44.7 70.0 68.0
PP1 Analog II Hs Inhibitor Inhibition 54.3 34.0 8.0
GF109203X Hs Inhibitor Inhibition 72.0 60.0 20.0
bosutinib Hs Inhibitor Inhibition 73.8
PDK1/Akt/Flt dual pathway inhibitor Hs Inhibitor Inhibition 76.6 95.0 82.0
Displaying the top 10 most potent ligands  View all ligands in screen »

References

Show »

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. Pflug A, Rogozina J, Lavogina D, Enkvist E, Uri A, Engh RA, Bossemeyer D. (2010) Diversity of bisubstrate binding modes of adenosine analogue-oligoarginine conjugates in protein kinase a and implications for protein substrate interactions. J. Mol. Biol.403 (1): 66-77. [PMID:20732331]

5. 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 A: protein kinase, cAMP-dependent, catalytic, alpha subunit. Last modified on 22/03/2013. Accessed on 23/10/2014. IUPHAR/BPS Guide to PHARMACOLOGY, http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=1476.