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  • 11.0 [archived version]
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CACNA1B CACNA1B GRIN2B GRIN2B GRIN1 GRIN1 DLG4 DLG4 PDLIM5 PDLIM5 GRIN2D GRIN2D SIPA1L1 SIPA1L1 GRIN2A GRIN2A DLG3 DLG3 GRIN2C GRIN2C DLG2 DLG2
"PDLIM5" - PDZ and LIM domain protein 5 in Homo sapiens
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
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gene co-occurrence
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textmining
co-expression
protein homology
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[Homology]
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PDLIM5PDZ and LIM domain protein 5; May play an important role in the heart development by scaffolding PKC to the Z-disk region. May play a role in the regulation of cardiomyocyte expansion. Overexpression promotes the development of heart hypertrophy. Contributes to the regulation of dendritic spine morphogenesis in neurons. May restrain postsynaptic growth of excitatory synapses (By similarity); LIM domain containing (625 aa)    
Predicted Functional Partners:
DLG4
Disks large homolog 4; Interacts with the cytoplasmic tail of NMDA receptor subunits and shaker-type potassium channels. Required for synaptic plasticity associated with NMDA receptor signaling. Overexpression or depletion of DLG4 changes the ratio of excitatory to inhibitory synapses in hippocampal neurons. May reduce the amplitude of ASIC3 acid-evoked currents by retaining the channel intracellularly. May regulate the intracellular trafficking of ADR1B (By similarity); Belongs to the MAGUK family (767 aa)
       
  0.917
SIPA1L1
Signal-induced proliferation-associated 1-like protein 1; Stimulates the GTPase activity of RAP2A. Promotes reorganization of the actin cytoskeleton and recruits DLG4 to F- actin. Contributes to the regulation of dendritic spine morphogenesis (By similarity); PDZ domain containing (1804 aa)
         
  0.912
DLG2
Disks large homolog 2; Required for perception of chronic pain through NMDA receptor signaling. Regulates surface expression of NMDA receptors in dorsal horn neurons of the spinal cord. Interacts with the cytoplasmic tail of NMDA receptor subunits as well as inward rectifying potassium channels. Involved in regulation of synaptic stability at cholinergic synapses. Part of the postsynaptic protein scaffold of excitatory synapses (By similarity); Membrane associated guanylate kinases (975 aa)
       
    0.909
DLG3
Disks large homolog 3; Required for learning most likely through its role in synaptic plasticity following NMDA receptor signaling; Membrane associated guanylate kinases (817 aa)
       
    0.909
GRIN2B
Glutamate receptor ionotropic, NMDA 2B; Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+). Sensitivity to glutamate and channel kinetics depend on the subunit composition. In concert with DAPK1 at extrasynaptic sites, acts as a central mediator for stroke damage. [...] (1484 aa)
         
  0.903
GRIN2A
Glutamate receptor ionotropic, NMDA 2A; Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+). Sensitivity to glutamate and channel kinetics depend on the subunit composition; channels containing GRIN1 and GRIN2A have higher sensitivity to glutamate and faster kineti [...] (1464 aa)
         
  0.902
GRIN1
Glutamate receptor ionotropic, NMDA 1; Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+). Sensitivity to glutamate and channel kinetics depend on the subunit composition; Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. NR1/GRIN1 subfamily (943 aa)
         
    0.900
GRIN2C
Glutamate receptor ionotropic, NMDA 2C; Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+). Sensitivity to glutamate and channel kinetics depend on the subunit composition (Probable). Plays a role in regulating the balance between excitatory and inhibitory activit [...] (1233 aa)
         
    0.900
GRIN2D
Glutamate receptor ionotropic, NMDA 2D; Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+). Sensitivity to glutamate and channel kinetics depend on the subunit composition; Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. NR2D/GRIN2D subfamily (1336 aa)
         
    0.900
CACNA1B
Voltage-dependent N-type calcium channel subunit alpha-1B; Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1B gives rise to N-type calcium currents. N-type calcium channels belong to the ’high-voltage activated’ (HVA) group and are blocked by omega-conotoxin-GVIA (omega-CTx-GVIA) and by omega-agatoxin- IIIA (omega-Aga-IIIA). Th [...] (2339 aa)
     
 
  0.848
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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