BAIT
SYNGAP1
Gm1963, Syngap
synaptic Ras GTPase activating protein 1 homolog (rat)
GO Process (14)
GO Function (4)
GO Component (7)
Gene Ontology Biological Process
- Ras protein signal transduction [IDA]
- dendrite development [IMP]
- negative regulation of Ras protein signal transduction [IBA, ISO]
- negative regulation of axonogenesis [IDA]
- negative regulation of neuron apoptotic process [IMP]
- pattern specification process [IMP]
- positive regulation of Rab GTPase activity [IDA]
- positive regulation of Ras GTPase activity [IBA, ISO]
- receptor clustering [IMP]
- regulation of MAPK cascade [IMP]
- regulation of long-term neuronal synaptic plasticity [IGI, IMP]
- regulation of synapse structure or activity [IMP]
- regulation of synaptic plasticity [ISO]
- visual learning [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Mus musculus
PREY
RAB1
Gtbp, Rab-1, Rab1A, Ypt1, mKIAA3012, RP23-19L22.4
RAB1, member RAS oncogene family
GO Process (18)
GO Function (4)
GO Component (10)
Gene Ontology Biological Process
- ER to Golgi vesicle-mediated transport [IBA, ISA, ISO]
- GTP catabolic process [IBA, ISO]
- Golgi organization [ISO]
- Rab protein signal transduction [IBA]
- autophagic vacuole assembly [IBA, ISO]
- autophagy [ISO]
- cargo loading into COPII-coated vesicle [ISO]
- cell migration [IMP, ISO]
- defense response to bacterium [ISO]
- endocytosis [ISO]
- growth hormone secretion [ISO]
- interleukin-8 secretion [ISO]
- intracellular protein transport [TAS]
- melanosome transport [IMP]
- positive regulation of glycoprotein metabolic process [ISO]
- substrate adhesion-dependent cell spreading [IMP]
- vesicle transport along microtubule [ISO]
- virion assembly [ISO]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Mus musculus
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
Long-term potentiation modulates synaptic phosphorylation networks and reshapes the structure of the postsynaptic interactome.
The postsynaptic site of neurons is composed of more than 1500 proteins arranged in protein-protein interaction complexes, the composition of which is modulated by protein phosphorylation through the actions of complex signaling networks. Components of these networks function as key regulators of synaptic plasticity, in particular hippocampal long-term potentiation (LTP). The postsynaptic density (PSD) is a complex multicomponent structure that ... [more]
Sci Signal Aug. 11, 2016; 9(440);rs8 [Pubmed: 27507650]
Throughput
- High Throughput
Curated By
- BioGRID