Proteins > Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform
Page last updated: 2024-08-07 18:43:08
Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform
A phosphorylase b kinase gamma catalytic chain, skeletal muscle isoform that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q16816]
Synonyms
PHK-gamma-M;
EC 2.7.11.19;
Phosphorylase kinase subunit gamma-1;
Serine/threonine-protein kinase PHKG1;
2.7.11.1;
2.7.11.26
Research
Bioassay Publications (9)
Timeframe | Studies on this Protein(%) | All Drugs % |
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 1 (11.11) | 18.2507 |
2000's | 4 (44.44) | 29.6817 |
2010's | 4 (44.44) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Compounds (76)
Drugs with Inhibition Measurements
Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
staurosporine | Homo sapiens (human) | IC50 | 0.0017 | 3 | 3 |
sf 2370 | Homo sapiens (human) | IC50 | 0.0017 | 2 | 2 |
Drugs with Activation Measurements
ASR352, A potent anticancer agent: Synthesis, preliminary SAR, and biological activities against colorectal cancer bulk, 5-fluorouracil/oxaliplatin resistant and stem cells.European journal of medicinal chemistry, , Jan-01, Volume: 161, 2019
Novel quinazoline derivatives bearing various 6-benzamide moieties as highly selective and potent EGFR inhibitors.Bioorganic & medicinal chemistry, , 05-01, Volume: 26, Issue:8, 2018
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
A small molecule-kinase interaction map for clinical kinase inhibitors.Nature biotechnology, , Volume: 23, Issue:3, 2005
Inhibitors of protein kinase C. 1. 2,3-Bisarylmaleimides.Journal of medicinal chemistry, , Volume: 35, Issue:1, 1992
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
A small molecule-kinase interaction map for clinical kinase inhibitors.Nature biotechnology, , Volume: 23, Issue:3, 2005
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
Fibrogenic Disorders in Human Diseases: From Inflammation to Organ Dysfunction.Journal of medicinal chemistry, , 11-21, Volume: 61, Issue:22, 2018
Inhibitors of protein kinase C. 1. 2,3-Bisarylmaleimides.Journal of medicinal chemistry, , Volume: 35, Issue:1, 1992
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
A small molecule-kinase interaction map for clinical kinase inhibitors.Nature biotechnology, , Volume: 23, Issue:3, 2005
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
Identification of genotype-correlated sensitivity to selective kinase inhibitors by using high-throughput tumor cell line profiling.Proceedings of the National Academy of Sciences of the United States of America, , Dec-11, Volume: 104, Issue:50, 2007
A small molecule-kinase interaction map for clinical kinase inhibitors.Nature biotechnology, , Volume: 23, Issue:3, 2005
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
Enables
This protein enables 6 target(s):
Target | Category | Definition |
phosphorylase kinase activity | molecular function | Catalysis of the reaction: 4 ATP + 2 phosphorylase b = 4 ADP + phosphorylase a. [EC:2.7.11.19] |
calmodulin binding | molecular function | Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states. [GOC:krc] |
ATP binding | molecular function | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. [ISBN:0198506732] |
enzyme binding | molecular function | Binding to an enzyme, a protein with catalytic activity. [GOC:jl] |
tau-protein kinase activity | molecular function | Catalysis of the reaction: ATP + tau-protein = ADP + O-phospho-tau-protein. [EC:2.7.11.26, MetaCyc:TAU-PROTEIN-KINASE-RXN] |
protein serine kinase activity | molecular function | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate. [RHEA:17989] |
Located In
This protein is located in 1 target(s):
Target | Category | Definition |
cytosol | cellular component | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl] |
Part Of
This protein is part of 1 target(s):
Target | Category | Definition |
phosphorylase kinase complex | cellular component | An enzyme complex that catalyzes the phosphorylation of phosphorylase b to form phosphorylase a. [PMID:1370475] |
Involved In
This protein is involved in 2 target(s):
Target | Category | Definition |
carbohydrate metabolic process | biological process | The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. [GOC:mah, ISBN:0198506732] |
glycogen biosynthetic process | biological process | The chemical reactions and pathways resulting in the formation of glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues. [ISBN:0198506732] |