FAS1
Gene Ontology Biological Process
Gene Ontology Molecular Function- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase activity [IDA, IMP]
- [acyl-carrier-protein] S-acetyltransferase activity [IDA, IMP]
- [acyl-carrier-protein] S-malonyltransferase activity [IDA, IMP]
- enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) activity [IDA, IMP]
- fatty acid synthase activity [IMP]
- palmitoyltransferase activity [IDA, IMP]
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase activity [IDA, IMP]
- [acyl-carrier-protein] S-acetyltransferase activity [IDA, IMP]
- [acyl-carrier-protein] S-malonyltransferase activity [IDA, IMP]
- enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) activity [IDA, IMP]
- fatty acid synthase activity [IMP]
- palmitoyltransferase activity [IDA, IMP]
Gene Ontology Cellular Component
FAS2
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Co-crystal Structure
Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.
Publication
Direct structural insight into the substrate-shuttling mechanism of yeast fatty acid synthase by electron cryomicroscopy.
Yeast fatty acid synthase (FAS) is a 2.6-MDa barrel-shaped multienzyme complex, which carries out cyclic synthesis of fatty acids. By electron cryomicroscopy of single particles we obtained a three-dimensional map of yeast FAS at 5.9-A resolution. Compared to the crystal structures of fungal FAS, the EM map reveals major differences and new features that indicate a considerably different arrangement of ... [more]
Throughput
- Low Throughput
Additional Notes
- Electron microscopy (EM) structure
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| FAS2 FAS1 | Affinity Capture-MS Affinity Capture-MS An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods. | High | - | BioGRID | - | |
| FAS1 FAS2 | Affinity Capture-MS Affinity Capture-MS An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods. | High | 10 | BioGRID | 3607487 | |
| FAS1 FAS2 | Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex. | Low | - | BioGRID | - | |
| FAS1 FAS2 | Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex. | Low | - | BioGRID | - | |
| FAS1 FAS2 | Co-purification Co-purification An interaction is inferred from the identification of two or more protein subunits in a purified protein complex, as obtained by classical biochemical fractionation or affinity purification and one or more additional fractionation steps. | Low | - | BioGRID | - | |
| FAS1 FAS2 | Co-purification Co-purification An interaction is inferred from the identification of two or more protein subunits in a purified protein complex, as obtained by classical biochemical fractionation or affinity purification and one or more additional fractionation steps. | Low | - | BioGRID | - | |
| FAS1 FAS2 | Phenotypic Enhancement Phenotypic Enhancement A genetic interaction is inferred when mutation or overexpression of one gene results in enhancement of any phenotype (other than lethality/growth defect) associated with mutation or over expression of another gene. | Low | - | BioGRID | 202175 | |
| FAS1 FAS2 | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | - |
Curated By
- BioGRID