Page last updated: 2024-08-07 10:18:48

Serine/threonine-protein phosphatase 5

A serine/threonine-protein phosphatase 5 that is encoded in the genome of human. [PRO:DNx, UniProtKB:P53041]

Synonyms

PP5;
EC 3.1.3.16;
Protein phosphatase T;
PP-T;
PPT

Research

Bioassay Publications (1)

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 (100.00)24.3611
2020's0 (0.00)2.80

Compounds (1)

Drugs with Inhibition Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
cefsulodinHomo sapiens (human)IC50200.000011

Enables

This protein enables 13 target(s):

TargetCategoryDefinition
RNA bindingmolecular functionBinding to an RNA molecule or a portion thereof. [GOC:jl, GOC:mah]
phosphoprotein phosphatase activitymolecular functionCatalysis of the reaction: a phosphoprotein + H2O = a protein + phosphate. Together with protein kinases, these enzymes control the state of phosphorylation of cellular proteins and thereby provide an important mechanism for regulating cellular activity. [ISBN:0198547684]
protein serine/threonine phosphatase activitymolecular functionCatalysis of the reaction: protein serine phosphate + H2O = protein serine + phosphate, and protein threonine phosphate + H2O = protein threonine + phosphate. [GOC:bf]
protein bindingmolecular functionBinding to a protein. [GOC:go_curators]
ATP bindingmolecular functionBinding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. [ISBN:0198506732]
lipid bindingmolecular functionBinding to a lipid. [GOC:ai]
phosphatase activitymolecular functionCatalysis of the hydrolysis of phosphoric monoesters, releasing phosphate ions. [GOC:curators, GOC:pg]
myosin phosphatase activitymolecular functionCatalysis of the reaction: phosphomyosin + H2O = myosin + phosphate. [EC:3.1.3.16]
identical protein bindingmolecular functionBinding to an identical protein or proteins. [GOC:jl]
ADP bindingmolecular functionBinding to ADP, adenosine 5'-diphosphate. [GOC:jl]
metal ion bindingmolecular functionBinding to a metal ion. [GOC:ai]
tau protein bindingmolecular functionBinding to tau protein. tau is a microtubule-associated protein, implicated in Alzheimer's disease, Down Syndrome and ALS. [GOC:jid]
Hsp90 protein bindingmolecular functionBinding to Hsp90 proteins, any of a group of heat shock proteins around 90kDa in size. [GOC:ai]

Located In

This protein is located in 4 target(s):

TargetCategoryDefinition
nucleoplasmcellular componentThat part of the nuclear content other than the chromosomes or the nucleolus. [GOC:ma, ISBN:0124325653]
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]
plasma membranecellular componentThe membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. [ISBN:0716731363]
intracellular membrane-bounded organellecellular componentOrganized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane. [GOC:go_curators]

Active In

This protein is active in 2 target(s):

TargetCategoryDefinition
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]
nucleuscellular componentA membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. [GOC:go_curators]

Part Of

This protein is part of 2 target(s):

TargetCategoryDefinition
protein-containing complexcellular componentA stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together. [GOC:dos, GOC:mah]
protein folding chaperone complexcellular componentA protein complex required for the non-covalent folding or unfolding, maturation, stabilization or assembly or disassembly of macromolecular structures. Usually active during or immediately after completion of translation. Many chaperone complexes contain heat shock proteins. [GOC:bhm, PMID:21855797]

Involved In

This protein is involved in 11 target(s):

TargetCategoryDefinition
MAPK cascadebiological processAn intracellular protein kinase cascade containing at least a MAP kinase (MAPK). It starts with the activation of a MAP3K, and the consecutive activation of a MPK2K and a MAPK. The cascade can also contain an additional tier: the upstream MAP4K. The kinases in each tier phosphorylate and activate the kinase in the downstream tier to transmit a signal within a cell. [PMID:20811974, PMID:9561267]
mitotic cell cyclebiological processProgression through the phases of the mitotic cell cycle, the most common eukaryotic cell cycle, which canonically comprises four successive phases called G1, S, G2, and M and includes replication of the genome and the subsequent segregation of chromosomes into daughter cells. In some variant cell cycles nuclear replication or nuclear division may not be followed by cell division, or G1 and G2 phases may be absent. [GOC:mah, ISBN:0815316194, Reactome:69278]
double-strand break repairbiological processThe repair of double-strand breaks in DNA via homologous and nonhomologous mechanisms to reform a continuous DNA helix. [GOC:elh]
DNA-templated transcriptionbiological processThe synthesis of an RNA transcript from a DNA template. [GOC:jl, GOC:txnOH]
protein dephosphorylationbiological processThe process of removing one or more phosphoric residues from a protein. [GOC:hb]
response to lead ionbiological processAny process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a lead ion stimulus. [GOC:tair_curators, PMID:16461380]
peptidyl-threonine dephosphorylationbiological processThe removal of phosphoric residues from peptidyl-O-phospho-L-threonine to form peptidyl-threonine. [GOC:bf]
positive regulation of canonical NF-kappaB signal transductionbiological processAny process that activates or increases the frequency, rate or extent of a canonical NF-kappaB signaling cascade. [GOC:jl]
response to morphinebiological processAny process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a morphine stimulus. Morphine is an opioid alkaloid, isolated from opium, with a complex ring structure. [GOC:ef, GOC:jl]
peptidyl-serine dephosphorylationbiological processThe removal of phosphoric residues from peptidyl-O-phospho-L-serine to form peptidyl-serine. [GOC:bf]
response to arachidonic acidbiological processAny process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an arachidonic acid stimulus. [GO_REF:0000071, GOC:TermGenie, PMID:16382163]