GO:0005829
|
cytosol
|
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
GO:0032991
|
protein-containing complex
|
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. |
GO:0005737
|
cytoplasm
|
The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
GO:0005575
|
cellular_component
|
A location, relative to cellular compartments and structures, occupied by a macromolecular machine. There are three types of cellular components described in the gene ontology: (1) the cellular anatomical entity where a gene product carries out a molecular function (e.g., plasma membrane, cytoskeleton) or membrane-enclosed compartments (e.g., mitochondrion); (2) virion components, where viral proteins act, and (3) the stable macromolecular complexes of which gene product are parts (e.g., the clathrin complex). |
GO:0005622
|
intracellular anatomical structure
|
A component of a cell contained within (but not including) the plasma membrane. In eukaryotes it includes the nucleus and cytoplasm. |
GO:0110165
|
cellular anatomical structure
|
A part of a cellular organism consisting of a material entity with granularity above the level of a protein complex but below that of an anatomical system. Note that cellular organisms exclude viruses. |
GO:0140535
|
intracellular protein-containing complex
|
A protein-containing complex located intracellularly. |
GO:0005832
|
chaperonin-containing T-complex
|
A multisubunit ring-shaped complex that mediates protein folding in the cytosol without a cofactor. |
GO:0101031
|
protein folding chaperone complex
|
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. |