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Target not currently curated in GtoImmuPdb
Target id: 1542
Nomenclature: protein kinase AMP-activated catalytic subunit alpha 2
Abbreviated Name: AMPKA2
Family: AMPK subfamily
Gene and Protein Information | ||||||
Species | TM | AA | Chromosomal Location | Gene Symbol | Gene Name | Reference |
Human | - | 552 | 1p32.2 | PRKAA2 | protein kinase AMP-activated catalytic subunit alpha 2 | |
Mouse | - | 552 | 4 C6 | Prkaa2 | protein kinase, AMP-activated, alpha 2 catalytic subunit | |
Rat | - | 552 | 5q34 | Prkaa2 | protein kinase AMP-activated catalytic subunit alpha 2 |
Database Links | |
Alphafold | P54646 (Hs), Q8BRK8 (Mm), Q09137 (Rn) |
BRENDA | 2.7.11.1 |
ChEMBL Target | CHEMBL2116 (Hs), CHEMBL1255154 (Mm), CHEMBL4637 (Rn) |
Ensembl Gene | ENSG00000162409 (Hs), ENSMUSG00000028518 (Mm), ENSRNOG00000007706 (Rn) |
Entrez Gene | 5563 (Hs), 108079 (Mm), 78975 (Rn) |
Human Protein Atlas | ENSG00000162409 (Hs) |
KEGG Enzyme | 2.7.11.1 |
KEGG Gene | hsa:5563 (Hs), mmu:108079 (Mm), rno:78975 (Rn) |
OMIM | 600497 (Hs) |
Pharos | P54646 (Hs) |
RefSeq Nucleotide | NM_006252 (Hs), NM_178143 (Mm), NM_023991 (Rn) |
RefSeq Protein | NP_006243 (Hs), NP_835279 (Mm), NP_076481 (Rn) |
UniProtKB | P54646 (Hs), Q8BRK8 (Mm), Q09137 (Rn) |
Wikipedia | PRKAA2 (Hs) |
Selected 3D Structures | |||||||||||
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Enzyme Reaction | ||||
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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: 1,4 |
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Key to terms and symbols | Click column headers to sort | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Target used in screen: AMPK-alpha2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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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: 2... |
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Key to terms and symbols | Click column headers to sort | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Target used in screen: AMPKα2/nd | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Displaying the top 10 most potent ligands View all ligands in screen » |
1. 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]
2. 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]
3. Littler DR, Walker JR, Davis T, Wybenga-Groot LE, Finerty PJ, Newman E, Mackenzie F, Dhe-Paganon S. (2010) A conserved mechanism of autoinhibition for the AMPK kinase domain: ATP-binding site and catalytic loop refolding as a means of regulation. Acta Crystallogr Sect F Struct Biol Cryst Commun, 66 (Pt 2): 143-51. [PMID:20124709]
4. 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]
AMPK subfamily: protein kinase AMP-activated catalytic subunit alpha 2. Last modified on 30/03/2016. Accessed on 03/12/2024. IUPHAR/BPS Guide to PHARMACOLOGY, https://www.guidetoimmunopharmacology.org/GRAC/ObjectDisplayForward?objectId=1542.