A phosphoglycerate mutase 1 that is encoded in the genome of human. [PRO:DNx, UniProtKB:P18669]
EC 5.4.2.11;
EC 5.4.2.4;
BPG-dependent PGAM 1;
Phosphoglycerate mutase isozyme B;
PGAM-B
Timeframe | Studies on this Protein(%) | All Drugs % |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 0 (0.00) | 29.6817 |
2010's | 1 (50.00) | 24.3611 |
2020's | 1 (50.00) | 2.80 |
Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
---|---|---|---|---|---|
xanthone | Homo sapiens (human) | IC50 | 0.5000 | 1 | 1 |
epigallocatechin gallate | Homo sapiens (human) | IC50 | 0.4900 | 2 | 2 |
alizarin red s | Homo sapiens (human) | IC50 | 2.3000 | 1 | 1 |
mangostin | Homo sapiens (human) | IC50 | 7.2000 | 1 | 1 |
gamma-mangostin | Homo sapiens (human) | IC50 | 1.9000 | 1 | 1 |
This protein enables 6 target(s):
Target | Category | Definition |
---|---|---|
bisphosphoglycerate mutase activity | molecular function | Catalysis of the reaction: 3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate. [EC:5.4.2.4] |
phosphoglycerate mutase activity | molecular function | Catalysis of the reaction: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate. [RHEA:15901] |
protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
hydrolase activity | molecular function | Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. [ISBN:0198506732] |
protein kinase binding | molecular function | Binding to a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate. [GOC:jl] |
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity | molecular function | Catalysis of the reaction: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate; this reaction mechanism uses 2,3-bisphosphoglycerate as a phosphate donor. [EC:5.4.2.11] |
This protein is located in 7 target(s):
Target | Category | Definition |
---|---|---|
extracellular region | cellular component | The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. [GOC:go_curators] |
cytoplasm | cellular component | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684] |
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] |
membrane | cellular component | A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. [GOC:dos, GOC:mah, ISBN:0815316194] |
secretory granule lumen | cellular component | The volume enclosed by the membrane of a secretory granule. [GOC:rph] |
extracellular exosome | cellular component | A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm. [GOC:BHF, GOC:mah, GOC:vesicles, PMID:15908444, PMID:17641064, PMID:19442504, PMID:19498381, PMID:22418571, PMID:24009894] |
ficolin-1-rich granule lumen | cellular component | Any membrane-enclosed lumen that is part of a ficolin-1-rich granule. [GO_REF:0000064, GOC:TermGenie, PMID:23650620] |
This protein is involved in 2 target(s):
Target | Category | Definition |
---|---|---|
gluconeogenesis | biological process | The formation of glucose from noncarbohydrate precursors, such as pyruvate, amino acids and glycerol. [MetaCyc:GLUCONEO-PWY] |
canonical glycolysis | biological process | The glycolytic process that begins with the conversion of glucose to glucose-6-phosphate by glucokinase activity. Glycolytic processes are the chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP. [GOC:dph, ISBN:0201090910, ISBN:0879010479] |