DLGAP1
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
CAMK2D
Gene Ontology Biological Process
- G1/S transition of mitotic cell cycle [IMP]
- calcium ion transport [IDA, IMP]
- cardiac muscle cell contraction [ISO, ISS]
- cardiac muscle contraction [IDA]
- cell growth involved in cardiac muscle cell development [ISO]
- cellular potassium ion homeostasis [ISO]
- endoplasmic reticulum calcium ion homeostasis [ISO]
- negative regulation of sodium ion transmembrane transport [ISO]
- negative regulation of sodium ion transmembrane transporter activity [ISO]
- peptidyl-serine phosphorylation [IDA, ISO]
- peptidyl-threonine phosphorylation [ISO, ISS]
- positive regulation of ERK1 and ERK2 cascade [ISO]
- positive regulation of Rac protein signal transduction [ISO]
- positive regulation of cardiac muscle hypertrophy [ISO]
- positive regulation of smooth muscle cell migration [ISO]
- positive regulation of smooth muscle cell proliferation [ISO]
- protein autophosphorylation [IMP, ISO]
- protein oligomerization [ISO]
- protein phosphorylation [ISO]
- regulation of G2/M transition of mitotic cell cycle [ISO]
- regulation of cardiac muscle cell action potential [ISO]
- regulation of cell communication by electrical coupling [ISO]
- regulation of cellular localization [ISO]
- regulation of generation of L-type calcium current [ISO]
- regulation of membrane depolarization [ISO]
- regulation of relaxation of cardiac muscle [IGI, ISO]
- regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum [ISO]
- regulation of sodium ion transport [IDA]
- relaxation of cardiac muscle [ISO, ISS]
- response to hypoxia [ISO]
Gene Ontology Molecular Function- calmodulin binding [ISO]
- calmodulin-dependent protein kinase activity [ISO, ISS]
- ion channel binding [IPI, ISO]
- nitric-oxide synthase binding [ISO]
- protein binding [IPI]
- protein homodimerization activity [ISO]
- protein serine/threonine kinase activity [IDA, IMP, ISO]
- sodium channel inhibitor activity [ISO]
- titin binding [ISO]
- calmodulin binding [ISO]
- calmodulin-dependent protein kinase activity [ISO, ISS]
- ion channel binding [IPI, ISO]
- nitric-oxide synthase binding [ISO]
- protein binding [IPI]
- protein homodimerization activity [ISO]
- protein serine/threonine kinase activity [IDA, IMP, ISO]
- sodium channel inhibitor activity [ISO]
- titin binding [ISO]
Gene Ontology Cellular Component
- T-tubule [IDA]
- axon initial segment [IDA]
- calcium channel complex [IDA, ISO]
- cytoplasm [IDA, ISO]
- cytosol [ISO]
- endoplasmic reticulum [ISO]
- intercalated disc [IDA]
- membrane [ISO]
- neuromuscular junction [IDA]
- neuronal cell body [IDA]
- nucleus [IDA, ISO]
- perinuclear region of cytoplasm [ISO]
- protein complex [ISO]
- sarcoplasmic reticulum [IDA]
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]
Throughput
- High Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| DLGAP1 CAMK2D | Affinity Capture-MS 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. | High | - | BioGRID | 2333857 |
Curated By
- BioGRID