Complex: TOM40 mitochondrial outer membrane translocase holocomplex
Macromolecular complex annotations are imported from the Complex Portal. These annotations have been derived from physical molecular interaction evidence extracted from the literature and cross-referenced in the entry, or by curator inference from information on homologs in closely related species or by inference from scientific background.
Complex Diagram
This diagram displays the protein subunits (blue) of the complex and how they interact with each other. Interactions with other relevant participants such as small molecules (purple), sub-complexes (yellow), and other subunits (red) are also shown. If a participant appears in the diagram with no lines connected to it, then its specific interactions with other participants are currently unknown.
Subunits
This table lists all participants of the complex (proteins, small molecules, nucleic acids, etc.) and their respective stoichiometry. A brief description is also provided for each participant in the table.
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| Subunit | Description | Stoichiometry |
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Gene Ontology
Gene Ontology (GO) terms that describe the function of a complex, the biological process in which it participates, or its cellular location. Click on a term for its definition and other objects annotated to that term.
- Biological Process
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- protein insertion into mitochondrial outer membrane
- Cellular Component
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- mitochondrial outer membrane
- mitochondrial outer membrane translocase complex
Shared Annotations
This diagram displays Gene Ontology terms (green) and subunits (blue) that are shared between the given macromolecular complex (black) and other yeast complexes (yellow). The shared GO terms or subunits can be visualized separately using the radio button at the bottom of the graph. Note: No diagram is shown ("No shared annotations") if there are less than 2 shared annotations (either GO terms or subunits of other complexes) between this complex and any other complexes.
References
List of references used specifically to curate the information on this page.
- Araiso Y, et al. (2019) Structure of the mitochondrial import gate reveals distinct preprotein paths. Nature 575(7782):395-401 PMID: 31600774
- Tucker K and Park E (2019) Cryo-EM structure of the mitochondrial protein-import channel TOM complex at near-atomic resolution. Nat Struct Mol Biol 26(12):1158-1166 PMID: 31740857
- Endo T, et al. (2003) Functional cooperation and separation of translocators in protein import into mitochondria, the double-membrane bounded organelles. J Cell Sci 116(Pt 16): 3259-67. PMID: 12857785