Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.11.1 extracted from

  • Mukai, H.
    The structure and function of PKN, a protein kinase having a catalytic domain homologous to that of PKC (2003), J. Biochem., 133, 17-27.
    View publication on PubMed
Search for more literature for 2.7.11.1

Activating Compound

Activating Compound Comment Organism Structure
arachidonic acid activates in vitro, binds at the autoinhibitory site at the C-terminal C2-domain Drosophila melanogaster
arachidonic acid activates in vitro, binds at the autoinhibitory site at the C-terminal C2-domain Homo sapiens
arachidonic acid activates in vitro, binds at the autoinhibitory site at the C-terminal C2-domain Xenopus laevis
arachidonic acid activates in vitro, binds at the autoinhibitory site at the C-terminal C2-domain Caenorhabditis elegans
arachidonic acid activates in vitro, binds at the autoinhibitory site at the C-terminal C2-domain Asteroidea
arachidonic acid activates in vitro, binds at the autoinhibitory site at the C-terminus Mus musculus
arachidonic acid activates in vitro, binds at the autoinhibitory site at the C-terminus Rattus norvegicus
arachidonic acid activates in vitro, binds at the autoinhibitory site at the C-terminus Bos taurus
cardiolipin activates isozyme PKNalpha Homo sapiens
cardiolipin activates isozyme PKNalpha Rattus norvegicus
linoleic acid
-
 Homo sapiens
lysophosphatidic acid activates isozyme PKNalpha Mus musculus
lysophosphatidic acid activates isozyme PKNalpha Homo sapiens
lysophosphatidic acid activates isozyme PKNalpha Rattus norvegicus
lysophosphatidylinositol activates isozyme PKNalpha Homo sapiens
lysophosphatidylinositol activates isozyme PKNalpha Rattus norvegicus
additional information no activation by calcium/phosphatidylserine/diolein, phosphorylation of PKN is required for full activation Homo sapiens
additional information no activation by calcium/phosphatidylserine/diolein, phosphorylation of PKN is required for full activation Rattus norvegicus
additional information phosphorylation of PKN is required for full activation Drosophila melanogaster
additional information phosphorylation of PKN is required for full activation Mus musculus
additional information phosphorylation of PKN is required for full activation Bos taurus
additional information phosphorylation of PKN is required for full activation Xenopus laevis
additional information phosphorylation of PKN is required for full activation Caenorhabditis elegans
additional information phosphorylation of PKN is required for full activation Asteroidea
phosphatidylinositol 3,4,5-trisphosphate activates isozyme PKNalpha Homo sapiens
phosphatidylinositol 3,4,5-trisphosphate activates isozyme PKNalpha Rattus norvegicus
phosphatidylinositol 4,5-bisphosphate activates isozyme PKNalpha Homo sapiens
phosphatidylinositol 4,5-bisphosphate activates isozyme PKNalpha Rattus norvegicus
Rac1 GTPase, binds and activates PKN Drosophila melanogaster
Rac2 GTPase, binds and activates PKN Drosophila melanogaster
Rho small GTPase, binds and activates PKN Caenorhabditis elegans
Rho small GTPase, binds and activates PKN Asteroidea
Rho1 small GTPase, binds GTP-dependently and activates PKN Drosophila melanogaster
RhoA small GTPase, binds to the ACC domain and activates isozymes PKNalpha and PRK2/PKNgamma/PAK-2 Mus musculus
RhoA small GTPase, binds to the ACC domain and activates isozymes PKNalpha and PRK2/PKNgamma/PAK-2 Homo sapiens
RhoA small GTPase, binds to the ACC domain and activates isozymes PKNalpha and PRK2/PKNgamma/PAK-2 Rattus norvegicus
RhoA small GTPase, binds to the ACC domain and activates isozymes PKNalpha and PRK2/PKNgamma/PAK-2 Bos taurus
RhoA small GTPase, binds to the ACC domain of PKNalpha forming a catalytic active site Drosophila melanogaster
small GTPase Rho small GTPase, binds and activates PKN Xenopus laevis

Cloned(Commentary)

Cloned (Comment) Organism
DNA sequence determination of isozyme PKNbeta Homo sapiens
gene mapping, DNA sequence determination and analysis of multiple isozymes Rattus norvegicus
PKNalpha gene mapps to 19p12-p13.1 of chromosome 8 situated at the prostanoid receptor gene locus Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
additional information PKN possesses an autoinhibitory site at the C-terminal C2 domain, which also binds activating arachidonic acid Asteroidea
additional information PKN possesses an autoinhibitory site at the C-terminal C2 domain, which also binds activating arachidonic acid Bos taurus
additional information PKN possesses an autoinhibitory site at the C-terminal C2 domain, which also binds activating arachidonic acid Caenorhabditis elegans
additional information PKN possesses an autoinhibitory site at the C-terminal C2 domain, which also binds activating arachidonic acid Drosophila melanogaster
additional information PKN possesses an autoinhibitory site at the C-terminal C2 domain, which also binds activating arachidonic acid Homo sapiens
additional information PKN possesses an autoinhibitory site at the C-terminal C2 domain, which also binds activating arachidonic acid Mus musculus
additional information PKN possesses an autoinhibitory site at the C-terminal C2 domain, which also binds activating arachidonic acid Rattus norvegicus
additional information PKN possesses an autoinhibitory site at the C-terminal C2 domain, which also binds activating arachidonic acid Xenopus laevis

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Rattus norvegicus 5829
-
cytosol
-
 Asteroidea 5829
-
cytosol juxtanuclear, isozyme PKNalpha, no isozyme PKNbeta Homo sapiens 5829
-
endoplasmic reticulum isozyme PKNalpha Homo sapiens 5783
-
endosome isozyme PKNalpha Homo sapiens 5768
-
membrane
-
 Bos taurus 16020
-
membrane isozyme PKNalpha Homo sapiens 16020
-
membrane postnuclear fraction Rattus norvegicus 16020
-
additional information PKNalpha translocates from the cytosol to the nucleus in response to various stresses, PRK2/PKNgamma/PAK-2 translocates from the cytosol to germinal vesicles during meiotic maturation in oocytes Asteroidea
-
-
nucleus
-
 Asteroidea 5634
-
nucleus isozyme PKNbeta Homo sapiens 5634
-
perinuclear space isozyme PKNbeta Homo sapiens
-
-
vesicle isozyme PKNalpha Homo sapiens 31982
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Drosophila melanogaster regulation mechanism and biological function of PKN ?
-
 ?
additional information Bos taurus regulation mechanism and biological function of PKN ?
-
 ?
additional information Caenorhabditis elegans regulation mechanism and biological function of PKN ?
-
 ?
additional information Asteroidea regulation mechanism and biological function of PKN ?
-
 ?
additional information Mus musculus regulation mechanism and biological function of PKN, PKNalpha is involved in insulin-induced actin cytoskeleton reorganization and cell adhesion, overview, isozyme PKNalpha is involved in glucose transport in 3T3/L1 cells ?
-
 ?
additional information Homo sapiens regulation mechanism and biological function of PKN, PKNalpha is involved in insulin-induced actin cytoskeleton reorganization and cell adhesion, overview, PKNalpha is involved in vesicle transport in the endoplasmic reticulum, PKNalpha is cleaved by caspase-3 or related proteases in apoptotic Jurkat and U-937 cells contributing to signal transduction, PKN interacts with papillomaviral oncoproteins being involved in tumorigenesis, overview ?
-
 ?
additional information Rattus norvegicus regulation mechanism and biological function of PKN, PKNalpha is involved in insulin-induced actin cytoskeleton reorganization, overview ?
-
 ?
additional information Xenopus laevis regulation mechanism and biological function of PKN, the enzyme is involved in cell cycle control ?
-
 ?

Organism

Organism UniProt Comment Textmining
Asteroidea
-
 at least 3 different isozymes PKNalpha/PKN-1/PAK-1, PKNbeta, and PRK2/PKNgamma/PAK-2
-
Bos taurus
-
 at least 3 different isozymes PKNalpha/PKN-1/PAK-1, PKNbeta, and PRK2/PKNgamma/PAK-2
-
Caenorhabditis elegans
-
 at least 3 different isozymes PKNalpha/PKN-1/PAK-1, PKNbeta, and PRK2/PKNgamma/PAK-2
-
Drosophila melanogaster
-
 at least 3 different isozymes PKNalpha/PKN-1/PAK-1, PKNbeta, and PRK2/PKNgamma/PAK-2
-
Homo sapiens
-
 at least 3 different isozymes PKNalpha/PKN-1/PAK-1, PKNbeta, and PRK2/PKNgamma/PAK-2
-
Mus musculus
-
 at least 3 different isozymes PKNalpha/PKN-1/PAK-1, PKNbeta, and PRK2/PKNgamma/PAK-2
-
Rattus norvegicus
-
 at least 3 different isozymes PKNalpha/PKN-1/PAK-1, PKNbeta, and PRK2/PKNgamma/PAK-2
-
Xenopus laevis
-
 at least 3 different isozymes PKNalpha/PKN-1/PAK-1, PKNbeta, and PRK2/PKNgamma/PAK-2
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein e.g. phosphorylation of isozyme PRK2/PKNgamma/PAK-2 at Ser473 and Thr308, phosphorylation is required for full activation Homo sapiens
phosphoprotein phosphorylation is required for full activation Drosophila melanogaster
phosphoprotein phosphorylation is required for full activation Mus musculus
phosphoprotein phosphorylation is required for full activation Rattus norvegicus
phosphoprotein phosphorylation is required for full activation Bos taurus
phosphoprotein phosphorylation is required for full activation Xenopus laevis
phosphoprotein phosphorylation is required for full activation Caenorhabditis elegans
phosphoprotein phosphorylation is required for full activation Asteroidea
proteolytic modification PKNalpha is cleaved by caspase-3 or related proteases in apoptotic Jurkat and U-937 cells contributing to signal transduction Homo sapiens

Purification (Commentary)

Purification (Comment) Organism
isozyme PKNalpha from brain membrane Bos taurus
PKN from testis to homogeneity by immuno affinity Rattus norvegicus

Reaction

Reaction Comment Organism Reaction ID
ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate catalytic mechanism and regulation of PKN Drosophila melanogaster
a
ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate catalytic mechanism and regulation of PKN Mus musculus
a
ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate catalytic mechanism and regulation of PKN Homo sapiens
a
ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate catalytic mechanism and regulation of PKN Rattus norvegicus
a
ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate catalytic mechanism and regulation of PKN Bos taurus
a
ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate catalytic mechanism and regulation of PKN Xenopus laevis
a
ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate catalytic mechanism and regulation of PKN Caenorhabditis elegans
a
ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate catalytic mechanism and regulation of PKN Asteroidea
a

Source Tissue

Source Tissue Comment Organism Textmining
3T3-L1 cell isozyme PKNalpha Mus musculus
-
A2780-DX3 cell lymphoid cell line, specific expression of isozyme PRK2/PKNgamma/PAK-2 Homo sapiens
-
brain isozyme PKNalpha Homo sapiens
-
brain isozyme PKNalpha Rattus norvegicus
-
brain isozyme PKNalpha Bos taurus
-
embryo
-
 Xenopus laevis
-
epithelium
-
 Homo sapiens
-
fibroblast IR fibroblasts Rattus norvegicus
-
HeLa cell isozymes PRK2/PKNgamma/PAK-2, and PKNbeta Homo sapiens
-
hippocampus
-
 Homo sapiens
-
JURKAT cell isozyme PRK2/PKNgamma/PAK-2 Homo sapiens
-
K-562 cell chromic myelogenous leukemia cell line, isozyme PKNbeta Homo sapiens
-
keratinocyte
-
 Homo sapiens
-
keratinocyte isozyme PRK2/PKNgamma/PAK-2 Mus musculus
-
liver isozyme PRK2/PKNgamma/PAK-2 Rattus norvegicus
-
additional information isozymes show different tissue distribution Drosophila melanogaster
-
additional information isozymes show different tissue distribution Mus musculus
-
additional information isozymes show different tissue distribution Bos taurus
-
additional information isozymes show different tissue distribution Xenopus laevis
-
additional information isozymes show different tissue distribution Caenorhabditis elegans
-
additional information isozymes show different tissue distribution Asteroidea
-
additional information ubiquitous expression of isozyme PKNalpha, isozymes show different tissue distribution Rattus norvegicus
-
additional information ubiquitous expression of isozyme PKNalpha, isozymes show different tissue distribution, PKNbeta is mainly expressed in cancer cells in adults Homo sapiens
-
neuron isozyme PKNalpha Homo sapiens
-
NIH-3T3 cell isozyme PKNalpha Mus musculus
-
oocyte isozyme PRK2/PKNgamma/PAK-2 Asteroidea
-
spleen
-
 Homo sapiens
-
spleen
-
 Rattus norvegicus
-
SW-480 cell colorectal adenocarcinoma cell line, isozyme PKNbeta Homo sapiens
-
testis
-
 Homo sapiens
-
testis
-
 Rattus norvegicus
-
thymus
-
 Homo sapiens
-
thymus
-
 Rattus norvegicus
-
U-937 cell isozyme PKNalpha Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + MARCKS protein isozyme PKNalpha Homo sapiens ADP + MARCKS phosphoprotein
-
 ?
ATP + MB protein
-
 Homo sapiens ADP + MB phosphoprotein
-
 ?
ATP + protein kinase C isozyme PKNalpha Homo sapiens ADP + phosphorylated protein kinase C
-
 ?
ATP + vimentin isozyme PKNalpha Homo sapiens ADP + phosphorylated vimentin
-
 ?
additional information regulation mechanism and biological function of PKN Drosophila melanogaster ?
-
 ?
additional information regulation mechanism and biological function of PKN Bos taurus ?
-
 ?
additional information regulation mechanism and biological function of PKN Caenorhabditis elegans ?
-
 ?
additional information regulation mechanism and biological function of PKN Asteroidea ?
-
 ?
additional information regulation mechanism and biological function of PKN, PKNalpha is involved in insulin-induced actin cytoskeleton reorganization and cell adhesion, overview, isozyme PKNalpha is involved in glucose transport in 3T3/L1 cells Mus musculus ?
-
 ?
additional information regulation mechanism and biological function of PKN, PKNalpha is involved in insulin-induced actin cytoskeleton reorganization and cell adhesion, overview, PKNalpha is involved in vesicle transport in the endoplasmic reticulum, PKNalpha is cleaved by caspase-3 or related proteases in apoptotic Jurkat and U-937 cells contributing to signal transduction, PKN interacts with papillomaviral oncoproteins being involved in tumorigenesis, overview Homo sapiens ?
-
 ?
additional information regulation mechanism and biological function of PKN, PKNalpha is involved in insulin-induced actin cytoskeleton reorganization, overview Rattus norvegicus ?
-
 ?
additional information regulation mechanism and biological function of PKN, the enzyme is involved in cell cycle control Xenopus laevis ?
-
 ?
additional information enzyme performs autophosphorylation, PKN binds several associated proteins via its ACC domain Xenopus laevis ?
-
 ?
additional information enzyme performs autophosphorylation, PKN binds several associated proteins via its ACC domain Caenorhabditis elegans ?
-
 ?
additional information enzyme performs autophosphorylation, PKN binds several associated proteins via its ACC domain Asteroidea ?
-
 ?
additional information enzyme performs autophosphorylation, PKN binds several associated proteins via its ACC domain, i.e. RhoA, a small GTPase, which binds to the ACC domain of PKNalpha forming a catalytic active site Mus musculus ?
-
 ?
additional information enzyme performs autophosphorylation, PKN binds several associated proteins via its ACC domain, i.e. RhoA, a small GTPase, which binds to the ACC domain of PKNalpha forming a catalytic active site Homo sapiens ?
-
 ?
additional information enzyme performs autophosphorylation, PKN binds several associated proteins via its ACC domain, i.e. RhoA, a small GTPase, which binds to the ACC domain of PKNalpha forming a catalytic active site Rattus norvegicus ?
-
 ?
additional information enzyme performs autophosphorylation, PKN binds several associated proteins via its ACC domain, i.e. RhoA, a small GTPase, which binds to the ACC domain of PKNalpha forming a catalytic active site Bos taurus ?
-
 ?
additional information enzyme performs autophosphorylation, PKN binds several associated proteins via its ACC domain, i.e. RhoA, a small GTPase, which binds to the ACC domain of PKNalpha forming a catalytic active site, isozyme PRK2/PKNgamma/PAK-2 binds to the large non-transmembrane protein Tyr phosphatase PTP-BL involved in the modulation of cytoskeleton, mediated by PSD-95 Drosophila melanogaster ?
-
 ?

Subunits

Subunits Comment Organism
More 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 Drosophila melanogaster
More 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 Mus musculus
More 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 Homo sapiens
More 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 Rattus norvegicus
More 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 Bos taurus
More 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 Xenopus laevis
More 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 Caenorhabditis elegans
More 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 Asteroidea

Synonyms

Synonyms Comment Organism
More PKN belongs to the AGC subfamily of protein kinases Drosophila melanogaster
More PKN belongs to the AGC subfamily of protein kinases Mus musculus
More PKN belongs to the AGC subfamily of protein kinases Homo sapiens
More PKN belongs to the AGC subfamily of protein kinases Rattus norvegicus
More PKN belongs to the AGC subfamily of protein kinases Bos taurus
More PKN belongs to the AGC subfamily of protein kinases Xenopus laevis
More PKN belongs to the AGC subfamily of protein kinases Caenorhabditis elegans
More PKN belongs to the AGC subfamily of protein kinases Asteroidea
PKN
-
 Drosophila melanogaster
PKN
-
 Mus musculus
PKN
-
 Homo sapiens
PKN
-
 Rattus norvegicus
PKN
-
 Bos taurus
PKN
-
 Xenopus laevis
PKN
-
 Caenorhabditis elegans
PKN
-
 Asteroidea

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Drosophila melanogaster
ATP
-
 Mus musculus
ATP
-
 Homo sapiens
ATP
-
 Rattus norvegicus
ATP
-
 Bos taurus
ATP
-
 Xenopus laevis
ATP
-
 Caenorhabditis elegans
ATP
-
 Asteroidea