BAIT

AGAP1

AGAP-1, CENTG2, GGAP1, cnt-g2
ArfGAP with GTPase domain, ankyrin repeat and PH domain 1
GO Process (0)
GO Function (1)
GO Component (0)

Gene Ontology Molecular Function

Homo sapiens
PREY

AGAP1

AGAP-1, CENTG2, GGAP1, cnt-g2
ArfGAP with GTPase domain, ankyrin repeat and PH domain 1
GO Process (0)
GO Function (1)
GO Component (0)

Gene Ontology Molecular Function

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

AGAP1, a novel binding partner of nitric oxide-sensitive guanylyl cyclase.

Meurer S, Pioch S, Wagner K, Mueller-Esterl W, Gross S

Nitric oxide (NO)-sensitive soluble guanylyl cyclase (sGC) is the major cytosolic receptor for NO, catalyzing the conversion of GTP to cGMP. In a search for proteins specifically interacting with human sGC, we have identified the multidomain protein AGAP1, the prototype of an ArfGAP protein with a GTPase-like domain, Ankyrin repeats, and a pleckstrin homology domain. AGAP1 binds through its carboxyl ... [more]

J. Biol. Chem. Nov. 19, 2004; 279(47);49346-54 [Pubmed: 15381706]

Throughput

  • Low Throughput

Curated By

  • BioGRID