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An enzyme complex that catalyzes the removal of serine- or threonine-bound phosphate groups from a wide range of phosphoproteins, including a number of enzymes that have been phosphorylated under the action of a kinase. A complex, normally consisting of a catalytic and a regulatory subunit, which catalyzes the removal of a phosphate group from a serine or threonine residue of a protein. The basic structural and functional unit of all organisms. Includes the plasma membrane and any external encapsulating structures such as the cell wall and cell envelope. A protein complex that has protein serine/threonine phosphatase activity that is polycation-stimulated (PCS), being directly stimulated by protamine, polylysine, or histone H1; it constitutes a subclass of several enzymes activated by different histones and polylysine, and consists of catalytic, scaffolding, and regulatory subunits. The catalytic and scaffolding subunits form the core enzyme, and the holoenzyme also includes the regulatory subunit. A protein serine/threonine phosphatase complex that is involved in nuclear envelope organization, and contains proteins known in budding yeast as Nem1p and Spo7p. The part of a cell or its extracellular environment in which a gene product is located. A gene product may be located in one or more parts of a cell and its location may be as specific as a particular macromolecular complex, that is, a stable, persistent association of macromolecules that function together. Any macromolecular complex composed of two or more polypeptide subunits, which may or may not be identical. Protein complexes may have other associated non-protein prosthetic groups, such as nucleotides, metal ions or other small molecules. The complex formed by the catalytic subunit of protein phosphatase 4 plus a regulatory subunit. A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which the constituent parts function together. A protein complex that possesses magnesium-dependent protein serine/threonine phosphatase (AMD phosphatase) activity, and consists of a catalytic subunit and one or more regulatory subunits that dictates the phosphatase's substrate specificity, function, and activity. Any constituent part of a cell, the basic structural and functional unit of all organisms. An enzyme complex that catalyzes the removal of the phosphate group from phosphomyosin. A heterodimeric calcium ion and calmodulin dependent protein phosphatase composed of catalytic and regulatory subunits; the regulatory subunit is very similar in sequence to calmodulin.

View Gene Ontology (GO) Term

GO TERM SUMMARY
Name: protein serine/threonine phosphatase complex
Acc: GO:0008287
Aspect: Cellular Component
Desc: A complex, normally consisting of a catalytic and a regulatory subunit, which catalyzes the removal of a phosphate group from a serine or threonine residue of a protein.
Proteins in PDR annotated with:
   This term: 103 [Search]
   Term or descendants: 255 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0008287 - protein serine/threonine phosphatase complex (interactive image map)
YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle