BAIT
PREX1
P-REX1
phosphatidylinositol-3,4,5-trisphosphate-dependent Rac exchange factor 1
GO Process (3)
GO Function (5)
GO Component (4)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
STXBP1
MUNC18-1, NSEC1, P67, RBSEC1, UNC18, RP11-56D16.3
syntaxin binding protein 1
GO Process (15)
GO Function (5)
GO Component (8)
Gene Ontology Biological Process
- axon target recognition [ISS]
- energy reserve metabolic process [TAS]
- glutamate secretion [TAS]
- negative regulation of synaptic transmission, GABAergic [ISS]
- neurotransmitter secretion [TAS]
- platelet aggregation [IMP]
- platelet degranulation [IMP]
- protein localization to plasma membrane [IDA]
- regulation of SNARE complex assembly [TAS]
- regulation of insulin secretion [TAS]
- regulation of synaptic vesicle fusion to presynaptic membrane [TAS]
- regulation of synaptic vesicle priming [ISS]
- small molecule metabolic process [TAS]
- synaptic transmission [TAS]
- synaptic vesicle maturation [ISS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
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.
Publication
Norbin Stimulates the Catalytic Activity and Plasma Membrane Localization of the Guanine-Nucleotide Exchange Factor P-Rex1.
P-Rex1 is a guanine-nucleotide exchange factor (GEF) that activates the small G protein (GTPase) Rac1 to control Rac1-dependent cytoskeletal dynamics, and thus cell morphology. Three mechanisms of P-Rex1 regulation are currently known: (i) binding of the phosphoinositide second messenger PIP3, (ii) binding of the G?? subunits of heterotrimeric G proteins, and (iii) phosphorylation of various serine residues. Using recombinant P-Rex1 ... [more]
J. Biol. Chem. Mar. 18, 2016; 291(12);6359-75 [Pubmed: 26792863]
Throughput
- Low Throughput
Curated By
- BioGRID