YRC Logo
PROTEIN SEARCH:
Descriptions Names[Advanced Search]

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. Protease complex of the mitochondrial inner membrane that is involved in mitochondrial protein turnover and in processing of proteins imported into mitochondria. Either of the lipid bilayers that surround the mitochondrion and form the mitochondrial envelope. A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which the constituent parts function together. The inner, i.e. lumen-facing, lipid bilayer of an organelle envelope; usually highly selective to most ions and metabolites. Any constituent part of a mitochondrion, a semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. Any constituent part of a mitochondrial membrane, either of the lipid bilayers that surround the mitochondrion and form the mitochondrial envelope. The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae. Any constituent part of a membrane, a double layer of lipid molecules that encloses all cells, and, in eukaryotes, many organelles; may be a single or double lipid bilayer; also includes associated proteins.

View Gene Ontology (GO) Term

GO TERM SUMMARY
Name: m-AAA complex
Acc: GO:0005745
Aspect: Cellular Component
Desc: Protease complex of the mitochondrial inner membrane that is involved in mitochondrial protein turnover and in processing of proteins imported into mitochondria.
Proteins in PDR annotated with:
   This term: 5 [Search]
   Term or descendants: 5 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0005745 - m-AAA complex (interactive image map)
YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle