Page last updated: 2024-08-07 22:37:34

Phosphoglycerate mutase 1

A phosphoglycerate mutase 1 that is encoded in the genome of human. [PRO:DNx, UniProtKB:P18669]

Synonyms

EC 5.4.2.11;
EC 5.4.2.4;
BPG-dependent PGAM 1;
Phosphoglycerate mutase isozyme B;
PGAM-B

Research

Bioassay Publications (2)

TimeframeStudies on this Protein(%)All Drugs %
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's0 (0.00)29.6817
2010's1 (50.00)24.3611
2020's1 (50.00)2.80

Compounds (5)

Drugs with Inhibition Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
xanthoneHomo sapiens (human)IC500.500011
epigallocatechin gallateHomo sapiens (human)IC500.490022
alizarin red sHomo sapiens (human)IC502.300011
mangostinHomo sapiens (human)IC507.200011
gamma-mangostinHomo sapiens (human)IC501.900011

Enables

This protein enables 6 target(s):

TargetCategoryDefinition
bisphosphoglycerate mutase activitymolecular functionCatalysis of the reaction: 3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate. [EC:5.4.2.4]
phosphoglycerate mutase activitymolecular functionCatalysis of the reaction: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate. [RHEA:15901]
protein bindingmolecular functionBinding to a protein. [GOC:go_curators]
hydrolase activitymolecular functionCatalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. [ISBN:0198506732]
protein kinase bindingmolecular functionBinding 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 activitymolecular functionCatalysis 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]

Located In

This protein is located in 7 target(s):

TargetCategoryDefinition
extracellular regioncellular componentThe 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]
cytoplasmcellular componentThe contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684]
cytosolcellular componentThe part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl]
membranecellular componentA 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 lumencellular componentThe volume enclosed by the membrane of a secretory granule. [GOC:rph]
extracellular exosomecellular componentA 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 lumencellular componentAny membrane-enclosed lumen that is part of a ficolin-1-rich granule. [GO_REF:0000064, GOC:TermGenie, PMID:23650620]

Involved In

This protein is involved in 2 target(s):

TargetCategoryDefinition
gluconeogenesisbiological processThe formation of glucose from noncarbohydrate precursors, such as pyruvate, amino acids and glycerol. [MetaCyc:GLUCONEO-PWY]
canonical glycolysisbiological processThe 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]