EC Number   |
Natural Substrates |
|---|
    2.7.4.8 | dGMP + ATP |
GMPKs catalyze the reversible phosphorylation of GMP and dGMP to their diphosphate form in the cell using ATP as a preferred phosphate donor. |
| 2.7.4.8 | GMP + ATP |
- |
| 2.7.4.8 | GMP + ATP |
GMPKs catalyze the reversible phosphorylation of GMP and dGMP to their diphosphate form in the cell using ATP as a preferred phosphate donor. |
| 2.7.4.8 | more |
MAGUKs contain three PSD-95/Discs large/Zona occludens 1, i.e. PDZ, domains, an src-homology 3, i.e. SH3, domain and a C-terminal guanylate kinase domain and play a key role in the regulation of the intracellular trafficking and synaptic localization of ionotropic glutamate receptors. In particular, the postsynaptic density-95-like subfamily of MAGUKs, PSD-MAGUKs, organizes ionotropic glutamate receptors and their associated signaling proteins in the postsynaptic density of the excitatory synapse regulating the strength of synaptic activity. Alterations of PSD-MAGUK protein interaction with N-methyl-D-aspartate, NMDA, receptors regulatory subunits are common events in several CNS disorders, overview, NMDA receptors' synaptic localization and binding to PSD-MAGUK protein family play a key role in the control of downstream signals resulting from receptor activation, physiological function, overview |
| 2.7.4.8 | more |
MAGUKs contain three PSD-95/Discs large/Zona occludens 1, i.e. PDZ, domains, an src-homology 3, i.e. SH3, domain and a C-terminal guanylate kinase domain and play a key role in the regulation of the intracellular trafficking and synaptic localization of ionotropic glutamate receptors. In particular, the postsynaptic density-95-like subfamily of MAGUKs, PSD-MAGUKs, organizes ionotropic glutamate receptors and their associated signaling proteins in the postsynaptic density of the excitatory synapse regulating the strength of synaptic activity. Alterations of PSD-MAGUK protein interaction with N-methyl-D-aspartate, NMDA, receptors regulatory subunits are common events in several CNS disorders, overview. NMDA receptors' synaptic localization and binding to PSD-MAGUK protein family play a key role in the control of downstream signals resulting from receptor activation, physiological function, overview. The enzyme plays a role in excitotoxicity and neurodegenerative disorders, e.g. in Parkinson disease and Alzheimer disease. Physiological functions, detailed overview |
| 2.7.4.8 | more |
synaptic scaffolding molecule, S-SCAM, is a synaptic protein, which harbors five or six PSD-95/Discs large/ZO-1, a guanylate kinase, and two WW domains. S-SCAM is associated with beta-DG and neuroligin 2 at inhibitory synapses, and functions as a linker between the dystrophin glycoprotein complex and the neurexin-neuroligin complex, complex formation analysis, overview |
| 2.7.4.8 | more |
the cytosolic isozyme is indispensable for the growth and development of plants, but not for chloroplast development, while the plastid/mitochondrial isozyme is is essential for chloroplast differentiation, overview |
| 2.7.4.8 | more |
the post-synaptic density-95 membrane associated guanylate kinase family of scaffolding proteins, MAGUK, associate with N-methyl-D-aspartate receptor NR2 subunits via their C-terminal glutamate serine, or aspartate/glutamate, valine motifs. N-methyl-D-aspartate receptors are a subclass of ionotropic glutamate receptors that are trafficked and/or clustered at synapses by MAGUK. Receptor binding of PSD variants differin the impact on the stabilisation, turnover and compartmentalisation of N-methyl-D-aspartate receptor subtypes in neurones during development and in the mature brain |
| 2.7.4.8 | more |
the voltage-gated calcium channel beta1b contains a conserved guanylate kinase domain, which is alone recapitulating calcium channel beta-subunit CaVbeta-mediated modulation of channel activation facilitating inactivation of the voltage-gated channel. CaVbeta can switch the inactivation phenotype conferred to CaV2.3 from slow to fast after posttranslational modifications during channel biogenesis, modulation mechanism, overview |
| 2.7.4.8 | more |
the voltage-gated calcium channel beta2a contains a conserved guanylate kinase domain, which is alone recapitulating calcium channel beta-subunit CaVbeta-mediated modulation of channel activation inhibiting inactivation of the voltage-gated channel. CaVbeta can switch the inactivation phenotype conferred to CaV2.3 from slow to fast after posttranslational modifications during channel biogenesis, modulation mechanism, overview |
