A serine/threonine-protein phosphatase 5 that is encoded in the genome of human. [PRO:DNx, UniProtKB:P53041]
PP5;
EC 3.1.3.16;
Protein phosphatase T;
PP-T;
PPT
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 (100.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
---|---|---|---|---|---|
cefsulodin | Homo sapiens (human) | IC50 | 200.0000 | 1 | 1 |
This protein enables 13 target(s):
Target | Category | Definition |
---|---|---|
RNA binding | molecular function | Binding to an RNA molecule or a portion thereof. [GOC:jl, GOC:mah] |
phosphoprotein phosphatase activity | molecular function | Catalysis 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 activity | molecular function | Catalysis of the reaction: protein serine phosphate + H2O = protein serine + phosphate, and protein threonine phosphate + H2O = protein threonine + phosphate. [GOC:bf] |
protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
ATP binding | molecular function | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. [ISBN:0198506732] |
lipid binding | molecular function | Binding to a lipid. [GOC:ai] |
phosphatase activity | molecular function | Catalysis of the hydrolysis of phosphoric monoesters, releasing phosphate ions. [GOC:curators, GOC:pg] |
myosin phosphatase activity | molecular function | Catalysis of the reaction: phosphomyosin + H2O = myosin + phosphate. [EC:3.1.3.16] |
identical protein binding | molecular function | Binding to an identical protein or proteins. [GOC:jl] |
ADP binding | molecular function | Binding to ADP, adenosine 5'-diphosphate. [GOC:jl] |
metal ion binding | molecular function | Binding to a metal ion. [GOC:ai] |
tau protein binding | molecular function | Binding to tau protein. tau is a microtubule-associated protein, implicated in Alzheimer's disease, Down Syndrome and ALS. [GOC:jid] |
Hsp90 protein binding | molecular function | Binding to Hsp90 proteins, any of a group of heat shock proteins around 90kDa in size. [GOC:ai] |
This protein is located in 4 target(s):
Target | Category | Definition |
---|---|---|
nucleoplasm | cellular component | That part of the nuclear content other than the chromosomes or the nucleolus. [GOC:ma, ISBN:0124325653] |
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] |
plasma membrane | cellular component | The 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 organelle | cellular component | Organized 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] |
This protein is active in 2 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] |
nucleus | cellular component | A 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] |
This protein is part of 2 target(s):
Target | Category | Definition |
---|---|---|
protein-containing complex | cellular component | A 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 complex | cellular component | A 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] |
This protein is involved in 11 target(s):
Target | Category | Definition |
---|---|---|
MAPK cascade | biological process | An 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 cycle | biological process | Progression 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 repair | biological process | The repair of double-strand breaks in DNA via homologous and nonhomologous mechanisms to reform a continuous DNA helix. [GOC:elh] |
DNA-templated transcription | biological process | The synthesis of an RNA transcript from a DNA template. [GOC:jl, GOC:txnOH] |
protein dephosphorylation | biological process | The process of removing one or more phosphoric residues from a protein. [GOC:hb] |
response to lead ion | biological process | Any 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 dephosphorylation | biological process | The removal of phosphoric residues from peptidyl-O-phospho-L-threonine to form peptidyl-threonine. [GOC:bf] |
positive regulation of canonical NF-kappaB signal transduction | biological process | Any process that activates or increases the frequency, rate or extent of a canonical NF-kappaB signaling cascade. [GOC:jl] |
response to morphine | biological process | Any 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 dephosphorylation | biological process | The removal of phosphoric residues from peptidyl-O-phospho-L-serine to form peptidyl-serine. [GOC:bf] |
response to arachidonic acid | biological process | Any 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] |