BAIT
ASAP1
AV239055, DEF-1, Ddef1, PAP, mKIAA1249, s19
ArfGAP with SH3 domain, ankyrin repeat and PH domain1
GO Process (2)
GO Function (4)
GO Component (0)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Mus musculus
PREY
SESTD1
1500031J16Rik, A930010O20, Solo/Trio8, RP23-15E4.1
SEC14 and spectrin domains 1
GO Process (0)
GO Function (7)
GO Component (1)
Gene Ontology Molecular Function- phosphatidic acid binding [ISO]
- phosphatidylinositol-3,4-bisphosphate binding [ISO]
- phosphatidylinositol-3,5-bisphosphate binding [ISO]
- phosphatidylinositol-3-phosphate binding [ISO]
- phosphatidylinositol-4,5-bisphosphate binding [ISO]
- phosphatidylinositol-4-phosphate binding [ISO]
- phosphatidylinositol-5-phosphate binding [ISO]
- phosphatidic acid binding [ISO]
- phosphatidylinositol-3,4-bisphosphate binding [ISO]
- phosphatidylinositol-3,5-bisphosphate binding [ISO]
- phosphatidylinositol-3-phosphate binding [ISO]
- phosphatidylinositol-4,5-bisphosphate binding [ISO]
- phosphatidylinositol-4-phosphate binding [ISO]
- phosphatidylinositol-5-phosphate binding [ISO]
Gene Ontology Cellular Component
Mus musculus
Two-hybrid
Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.
Publication
Arf GTPase-activating protein ASAP1 interacts with Rab11 effector FIP3 and regulates pericentrosomal localization of transferrin receptor-positive recycling endosome.
ADP-ribosylation factors (Arfs) and Arf GTPase-activating proteins (GAPs) are key regulators of membrane trafficking and the actin cytoskeleton. The Arf GAP ASAP1 contains an N-terminal BAR domain, which can induce membrane tubulation. Here, we report that the BAR domain of ASAP1 can also function as a protein binding site. Two-hybrid screening identified FIP3, which is a putative Arf6- and Rab11-effector, ... [more]
Mol. Biol. Cell Oct. 01, 2008; 19(10);4224-37 [Pubmed: 18685082]
Throughput
- Low Throughput
Curated By
- BioGRID