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Information on EC 2.7.4.8 - guanylate kinase and Organism(s) Mus musculus and UniProt Accession Q64520
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2.7.4.8 guanylate kinaseIUBMB Comments
dGMP can also act as acceptor, and dATP can act as donor.
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Word Map
- 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
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
maguk, guanylate kinase, membrane-associated guanylate kinase, maguks, membrane-associated guanylate kinases, guanylate kinase (gk), gmp kinase, membrane associated guanylate kinase, gmpk, cavbeta2a, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5'-GMP kinase
-
-
-
-
ATP:GMP phosphotransferase
-
-
-
-
deoxyguanylate kinase
-
-
-
-
GMP kinase
-
-
-
-
guanosine monophosphate kinase
-
-
-
-
kinase, guanylate (phosphorylating)
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:(d)GMP phosphotransferase
dGMP can also act as acceptor, and dATP can act as donor.
CAS REGISTRY NUMBER
COMMENTARY
9026-59-9
-
SUBSTRATE
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
additional information
?
-
-
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
-
-
?
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
additional information
?
-
-
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
Mn2+
K+
-
activity of dGMP kinase progressively enhanced as the concentration of KCl is increased to 250 mM, GMP phosphorylation unaffected
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). KGUA_MOUSE
198
0
21918
Swiss-Prot
Mitochondrion (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
-
PSD-MAGUK's major phosphorylation sites, regulation by phosphorylation, through Ser/Thr protein kinases and also Tyr-dependent kinases, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
-
incubation for 2 min, 5 min, 10 min or 20 min leads to 43%, 67%, 89% or 97% loss of activity, respectively, 30 min: inactivation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Griffith, T.J.; Helleiner, C.W.
The partial purification of deoxynucleoside monophosphate kinases from L cells
Biochim. Biophys. Acta
108
114-124
1965
Mus musculus
Brady, W.A.; Kokoris, M.S.; Fitzgibbon, M.; Black, M.E.
Cloning, characterization, and modeling of mouse and human guanylate kinases
J. Biol. Chem.
271
16734-16740
1996
Homo sapiens, Mus musculus (Q64520), Mus musculus
Stolworthy, T.S.; Black, M.E.
The mouse guanylate kinase double mutant E72Q/D103N is a functional adenylate kinase
Protein Eng.
14
903-909
2001
Mus musculus
Sekulic, N.; Shuvalova, L.; Spangenberg, O.; Konrad, M.; Lavie, A.
Structural characterization of the closed conformation of mouse guanylate kinase
J. Biol. Chem.
277
30236-30243
2002
Mus musculus
Willmon, C.L.; Krabbenhoft, E.; Black, M.E.
A guanylate kinase/HSV-1 thymidine kinase fusion protein enhances prodrug-mediated cell killing
Gene Ther.
13
1309-1312
2006
Homo sapiens, Mus musculus
EXTERNAL LINKS (specific for EC-Number 2.7.4.8)
Transporter Classification Database (TCDB): 8.A.24.1.8
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