Information on EC 2.7.11.1 - non-specific serine/threonine protein kinase and Organism(s) Caenorhabditis elegans

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Caenorhabditis elegans


The taxonomic range for the selected organisms is: Caenorhabditis elegans

The enzyme appears in selected viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.11.1
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RECOMMENDED NAME
GeneOntology No.
non-specific serine/threonine protein kinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + a protein = ADP + a phosphoprotein
show the reaction diagram
catalytic mechanism and regulation of PKN
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP:protein phosphotransferase (non-specific)
This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analysed to date.
CAS REGISTRY NUMBER
COMMENTARY hide
191808-15-8
phosphoinositide dependent protein kinase 1
340830-03-7
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37278-10-7
-
377752-08-4
ribosomal protein S6 kinase 2
389133-24-8
ribosomal S6 kinase 3
52660-18-1
casein kinase, protein kinase CK2
9026-43-1
this CAS Reg. No. encompasses a great variety of protein kinases including the serine/threonine specific kinases
90698-26-3
ribosomal protein S6 kinase 1
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
casein + ATP
phosphorylated casein + ADP
show the reaction diagram
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-
-
?
casein + GTP
phosphorylated casein + GDP
show the reaction diagram
-
-
-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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PKN possesses an autoinhibitory site at the C-terminal C2 domain, which also binds activating arachidonic acid
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
arachidonic acid
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activates in vitro, binds at the autoinhibitory site at the C-terminal C2-domain
Rho
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small GTPase, binds and activates PKN
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additional information
-
phosphorylation of PKN is required for full activation
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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isozymes show different tissue distribution
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
x * 29000 + x * 42000
42000
x * 29000 + x * 42000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 29000 + x * 42000
additional information
-
isozyme structure analysis, PKN kinase contains a catalytic domain homologous to that of protein kinase C, as well as a unique regulatory region containing antiparallel coiled-coil domain, the ACC domain, and an autoinhibitory C2 domain binding activators
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
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phosphorylation is required for full activation