BAIT

MTOR

2610315D21Rik, AI327068, FRAP, FRAP2, Frap1, RAFT1, RAPT1, flat, RP23-423L9.1
mechanistic target of rapamycin (serine/threonine kinase)
GO Process (41)
GO Function (11)
GO Component (13)

Gene Ontology Biological Process

Mus musculus
PREY

FKBP1A

FKBP-12, FKBP-1A, FKBP1, FKBP12, PKC12, PKCI2, PPIASE, RP11-314N13.2
FK506 binding protein 1A, 12kDa
GO Process (26)
GO Function (11)
GO Component (7)
Homo sapiens

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.

Publication

Regulation of eIF-4E BP1 phosphorylation by mTOR.

Hara K, Yonezawa K, Kozlowski MT, Sugimoto T, Andrabi K, Weng QP, Kasuga M, Nishimoto I, Avruch J

The proteins eIF-4E BP1 and p70 S6 kinase each undergo an insulin/mitogen-stimulated phosphorylation in situ that is partially inhibited by rapamycin. Previous work has established that the protein known as mTOR/RAFT-1/FRAP is the target through which the rapamycin.FKBP12 complex acts to dephosphorylate/deactivate the p70 S6 kinase; thus, some mTOR mutants that have lost the ability to bind to the rapamycin.FKBP12 ... [more]

J. Biol. Chem. Oct. 17, 1997; 272(42);26457-63 [Pubmed: 9334222]

Throughput

  • Low Throughput

Curated By

  • BioGRID