2.7.4.8: guanylate kinase
This is an abbreviated version!
For detailed information about guanylate kinase, go to the full flat file.
Word Map on EC 2.7.4.8
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2.7.4.8
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junction
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synapses
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drosophila
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nmda
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cell-cell
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src
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excitatory
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synapse-associated
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hippocampal
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domain-containing
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magi-1
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adaptor
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spine
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palmitoylated
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n-methyl-d-aspartate
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presynaptic
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glutamatergic
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kinase-like
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adherens
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pdz-binding
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zonula
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carma1
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crumbs
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bcl10
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neurexins
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discs-large
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dgmp
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septate
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occludens
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kinase-associated
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junction-associated
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tcr-induced
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ampars
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shank
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mucosa-associated
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card-containing
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neuroligins
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drug development
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medicine
- 2.7.4.8
- junction
- synapses
- drosophila
- nmda
-
cell-cell
- src
-
excitatory
-
synapse-associated
- hippocampal
-
domain-containing
-
magi-1
- adaptor
-
spine
-
palmitoylated
- n-methyl-d-aspartate
-
presynaptic
-
glutamatergic
-
kinase-like
-
adherens
-
pdz-binding
-
zonula
- carma1
-
crumbs
- bcl10
-
neurexins
-
discs-large
- dgmp
-
septate
-
occludens
-
kinase-associated
-
junction-associated
-
tcr-induced
-
ampars
-
shank
-
mucosa-associated
-
card-containing
-
neuroligins
- drug development
- medicine
Reaction
Synonyms
5'-GMP kinase, apo-EcGMPK, ATP: GMP phosphotransferase, ATP:GMP phosphotransferase, BmGK, CASK polypeptide, Cavbeta1b, Cavbeta2a, deoxyguanylate kinase, DLG1/SAP97, ecGMPK, GK, GK3, GKc, GKpm, GMK, GMK3, GMP kinase, GMPK, guanosine monophosphate kinase, guanosine monophosphate kinase (EcGMPK), guanylate kinase, guanylate kinase (GK), guanylate monophosphate kinase, GUK, kinase, guanylate (phosphorylating), MAGUK, MAGUK PSD-95, MAGUKs, membrane associated guanylate kinase, membrane associated guanylate kinase protein, membrane-associated guanylate kinase, membrane-associated guanylate kinases, MoGuk1, MoGuk2, More, organellar GK, post-synaptic density-95 membrane associated guanylate kinase, postsynaptic density protein-95 SH3 GK, PSD-95 GK, PSD-95 MAGUK, PSD-95alpha, PSD-95beta, Staphylococcus aureus guanylate monophosphate kinase, voltage-gated calcium channel beta1b, voltage-gated calcium channel beta2a, YGK
ECTree
2.7.4.8 guanylate kinaseAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 2.7.4.8 - guanylate kinase
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + GMP
ADP + GDP
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first step in 'cGMP-cycle' toward re-synthesis of cGMP
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?
ATP + GMP
ADP + GDP
guanylate kinase is an essential enzyme
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?
ATP + GMP
ADP + GDP
guanylate kinase is an essential enzyme
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?
ATP + GMP
ADP + GDP
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regulation of cellular adhesion and signal transduction at sites of cell-cell contact
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?
ATP + GMP
ADP + GDP
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regulation of cellular adhesion and signal transduction at sites of cell-cell contact
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?
ATP + GMP
ADP + GDP
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key enzyme of biosynthetic pathway of GTP or dGTP
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r
dGMP + ATP
dGDP + ADP
GMPKs catalyze the reversible phosphorylation of GMP and dGMP to their diphosphate form in the cell using ATP as a preferred phosphate donor.
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r
GMP + ATP
GDP + ADP
GMPKs catalyze the reversible phosphorylation of GMP and dGMP to their diphosphate form in the cell using ATP as a preferred phosphate donor.
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r
additional information
?
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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
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?
additional information
?
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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
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?
additional information
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
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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
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?
additional information
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
