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 (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 | 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 | 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 | 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 | 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 | 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 (Comment) | Organism |
---|---|
isozyme PKNalpha from brain membrane | Bos taurus |
PKN from testis to homogeneity by immuno affinity | Rattus norvegicus |
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 | |
ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate | catalytic mechanism and regulation of PKN | Mus musculus | |
ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate | catalytic mechanism and regulation of PKN | Homo sapiens | |
ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate | catalytic mechanism and regulation of PKN | Rattus norvegicus | |
ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate | catalytic mechanism and regulation of PKN | Bos taurus | |
ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate | catalytic mechanism and regulation of PKN | Xenopus laevis | |
ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate | catalytic mechanism and regulation of PKN | Caenorhabditis elegans | |
ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate | catalytic mechanism and regulation of PKN | Asteroidea |
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 | 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 | 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 | 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 | 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 |