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

CDC42

CDC42Hs, G25K, RP1-224A6.5
cell division cycle 42
GO Process (25)
GO Function (7)
GO Component (14)
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

GTP-binding protein-like domain of AGAP1 is protein binding site that allosterically regulates ArfGAP protein catalytic activity.

Luo R, Akpan IO, Hayashi R, Sramko M, Barr V, Shiba Y, Randazzo PA

AGAPs are a subtype of Arf GTPase-activating proteins (GAPs) with 11 members in humans. In addition to the Arf GAP domain, the proteins contain a G-protein-like domain (GLD) with homology to Ras superfamily proteins and a PH domain. AGAPs bind to clathrin adaptors, function in post Golgi membrane traffic, and have been implicated in glioblastoma. The regulation of AGAPs is ... [more]

J. Biol. Chem. May. 18, 2012; 287(21);17176-85 [Pubmed: 22453919]

Throughput

  • Low Throughput

Curated By

  • BioGRID